###################################################### ##### Sequences and other information for the PH Domain ##### Prepared as a part of MeTaDoR (http://proteomics.bioengr.uic.edu/metador) ##### By Nitin Bhardwaj (Dr Hui Lu's Lab at the Univ of Illinois at Chicago) ##### As of May 2007 ###################################################### ###################################################### ##### README ##### First column contains the name of the host-protein ##### Second column contains the species name. 'Human', 'Yeast' and ##### 'Mouse' Have been indicated and others have been indicated by 'Others' ##### Third column indicates membrane-binding (indicated by 1) or ##### non-membrane-binding (indicated by 0) behavior of the protein. ##### Fourth and fifth columns state the function and subcellular location ##### of the protein as given in the Swiss-Prot/Uniprot database, respectively (wherever available). ##### Sixth and subsequent columns provide the sequences of all occurrence of ##### the domain in the host protein. ###################################################### DDEF2_MOUSE Mouse 1 " FUNCTION: Activates the small GTPases ARF1, ARF5 and ARF6. Regulates the formation of post-Golgi vesicles and modulates constitutive secretion. Modulates phagocytosis mediated by Fc gamma receptor and ARF6. Modulates PXN recruitment to focal contacts and cell migration (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus; Golgi stack; Golgi membrane; peripheral membrane protein. Cell membrane; peripheral membrane protein. Colocalizes with F-actin and ARF6 in phagocytic cups. GTERNGNLYKKSDGIRKVWQKRKCSVKNGFLTISHGTANRPPAKLNLLTCQVKTNPEEKKCFDLISHDRTYHFQAEDEQECQIWMSVLQNSKE DDEF2_HUMAN Human 1 " FUNCTION: Activates the small GTPases ARF1, ARF5 and ARF6. Regulates the formation of post-Golgi vesicles and modulates constitutive secretion. Modulates phagocytosis mediated by Fc gamma receptor and ARF6. Modulates PXN recruitment to focal contacts and cell migration." SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus; Golgi stack; Golgi membrane; peripheral membrane protein. Cell membrane; peripheral membrane protein. Colocalizes with F-actin and ARF6 in phagocytic cups. GTERNGSLYKKSDGIRKVWQKRKCSVKNGFLTISHGTANRPPAKLNLLTCQVKTNPEEKKCFDLISHDRTYHFQAEDEQECQIWMSVLQNSKE APS_RAT Others 1 " FUNCTION: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis (By similarity). Involved in stimulation of glucose uptake by insulin. Involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Induces cytoskeletal reorganization and neurite outgrowth in cultured neurons." SUBCELLULAR LOCATION: Cytoplasmic. Recruited to the membrane by binding to an autophosphorylated receptor after receptor stimulation by its extracellular ligand. DIQREGALRFMVADDAASGPGGTAQWQKCRLLLRRAVAGERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVD APS_MOUSE Mouse 1 " FUNCTION: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. May be involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis. May induce cytoskeletal reorganization via interaction with VAV3 (By similarity)." " SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Cytoplasmic before PDGF stimulation. After PDGF stimulation, localized at the cell membrane and peripheral region (By similarity)." DIQREGALRFMVADDAASGPGGTAQWQKCRLLLRRAVAGERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVD APS_HUMAN Human 1 " FUNCTION: Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. May be involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis. May induce cytoskeletal reorganization via interaction with VAV3." " SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Cytoplasmic before PDGF stimulation. After PDGF stimulation, localized at the cell membrane and peripheral region." DIQREGALRFMVADDAAAGSGGSAQWQKCRLLLRRAVAEERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVD SNT1_CAEEL Others 1 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex (DGC). May also act by slowing calcium channel activity via a direct or indirect mechanism potentially involving other second messengers. Plays an early role in the formation of the neuromuscular junction and is necessary for muscle maintenance. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). AAVRSGLVDIFVQGQWHRVLATLDPTAITLQTMEQNEAEAEKRTVRVVKYDGNGLGISIKGGRDNNMPIVISKIFKGMAADQAGELFLDDVIISVNGENLLDASHEEAVRALKRAGRVVDLQVQYRREDMMHRENIVENVEWDDDIRERVRTIGLKLAYVARAGIDADAEGRILEMRSPSGRYSLAMRCSSSEEADGWFEALHACTT SNTB1_HUMAN Human 1 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. " SUBCELLULAR LOCATION: Sarcolemma; sarcolemmal membrane; peripheral membrane protein; cytoplasmic side (By similarity). In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions (By similarity)." RAQRSGLLEVLVRDRWHKVLVNLSEDALVLSSEEGAAAYNGIGTATNGSFCRGAGAGHPGAGGAQPPDSPAGVRTAFTDLPEQVPESISNQKRGVKVLKQELGGLGISIKGGKENKMPILISKIFKGLAADQTQALYVGDAILSVNGADLRDATHDEAVQALKRAGKEVLLEVKYMREATPYVKKGSPVSEIGWETPPPESPRLGGSTSDPPSSQSFSFHRDRKSIPLKMCYVTRSMALADPENRQLEIHSPDAKHTVILRSKDSATAQAWFSAIHSNVN SNTB1_MOUSE Mouse 1 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. " SUBCELLULAR LOCATION: Sarcolemma; sarcolemmal membrane; peripheral membrane protein; cytoplasmic side. In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions." RAQRSGLLEVLVRDRWHKVLVNLSEDALVLSCEEGAAAYNGIGAATNGSFCRGSGTGHPVPGVAQAPDSPAGVRTAFTDLPEQVPESISNQKRGVKVLKQELGGLGISIKGGKENKMPILISKIFKGLAADQTQALYVGDAILSVNGADLRDATHDEAVQALKRAGKEVLLEVKYMREATPYVKKGSPVSEIGWETPPPESPRLGGGSAEPLSSQSFSFHRDRKSIPLKMCYVTRNMTLADPENRQLEIHSPDAKHTVILRSKDSATAQAWFSAIHSNAG SNTB2_MOUSE Mouse 1 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN (By similarity). " SUBCELLULAR LOCATION: Membrane-associated. In insulinoma cell line, it is enriched in secretory granules (By similarity). In muscle, it is exclusively localized at the neuromuscular junction." ILSVNGTDLRQATHDQAVQALKRAGKEVLLEVKFIREVTPYIKKPSLVSDLPWEGASPQSPSFSGSEDSGSPKHQNTTKDRKVIPLKMCFAARNLSMPDLENRLIELHSPDSRNTLILRCKDTATAHSWFVAIHTNIM SNTB2_HUMAN Human 1 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN. " SUBCELLULAR LOCATION: Membrane-associated. In muscle, it is exclusively localized at the neuromuscular junction (By similarity). In insulinoma cell line, it is enriched in secretory granules." ILSVNGTDLRQATHDQAVQALKRAGKEVLLEVKFIREVTPYIKKPSLVSDLPWEGAAPQSPSFSGSEDSGSPKHQNSTKDRKIIPLKMCFAARNLSMPDLENRLIELHSPDSRNTLILRCKDTATAHSWFVAIHTNIM SNTA1_HUMAN Human 1 " FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-biphosphate (By similarity)." " SUBCELLULAR LOCATION: Sarcolemma; sarcolemmal membrane; peripheral membrane protein; cytoplasmic side (By similarity). In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions (By similarity)." RAPRTGLLELRAGAGSGAGGERWQRVLLSLAEDVLTVSPADGDPGPEPGAPREQEPAQLNGAAEPGAGPPQLPEALLLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKGLAADQTEALFVGDAILSVNGEDLSSATHDEAVQVLKKTGKEVVLEVKYMKDVSPYFKNSTGGTSVGWDSPPASPLQRQPSSPGPTPRNFSEAKHMSLKMAYVSKRCTPNDPEPRYLEICSADGQDTLFLRAKDEASARSWATAIQAQVN SNTA1_MOUSE Mouse 1 " FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-biphosphate." " SUBCELLULAR LOCATION: Sarcolemma; sarcolemmal membrane; peripheral membrane protein; cytoplasmic side. In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions." RAPRTGLLELRCGAGSGAGGERWQRVLLSLAEDALTVSPADGEPGPEPEPAQLNGAAEPGAAPPQLPEALLLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKGLAADQTEALFVGDAILSVNGEDLSSATHDEAVQALKKTGKEVVLEVKYMKEVSPYFKNSAGGTSVGWDSPPASPLQRQPSSPGPQPRNLSEAKHVSLKMAYVSRRCTPTDPEPRYLEICAADGQDAVFLRAKDEASARSWAGAIQAQIG SNTA1_RABIT Others 1 " FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-biphosphate (By similarity)." " SUBCELLULAR LOCATION: Sarcolemma; sarcolemmal membrane; peripheral membrane protein; cytoplasmic side (By similarity). In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions (By similarity)." RAPRTGLLELRAGTGAGAGGERWQRVLVSLAEDALTVSPADGEPGPEPGAVREPEPAQINGAAEPGAAPPQLPEALLLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKGLAADQTEALFVGDAILSVNGEDLSSATHDEAVQALKKTGKEVVLEVKYMKEVSPYFKNSAGGTSVGWDSPPASPLQRQPSSPGPQTRNLSEAKHVPLKMAYVSRRCTPSDPEHRYLEICSADGQDTIFLRAKDEASARSWAGAIQAQIN SNTG2_MOUSE Mouse 1 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex (By similarity). " SUBCELLULAR LOCATION: Sarcolemma; sarcolemmal membrane; peripheral membrane protein; cytoplasmic side. In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane." QVVHMGWVNERLQGADNSQNFRPKFLALRGSSFYIFGAPPVSTLDWGRAERAYNLCEVLFKVHKFWLSDNYWLQANLYLGLQDFDCEDPRSYCFSVLANHGKSHIFSVELGSELAVWEKAFQRATF SNTG2_HUMAN Human 1 FUNCTION: Adapter protein that binds to and probably organizes the subcellular localization of a variety of proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex (By similarity). " SUBCELLULAR LOCATION: Sarcolemma; sarcolemmal membrane; peripheral membrane protein; cytoplasmic side. In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane." QVVHMGWVNEKLQGADSSQTFRPKFLALKGPSFYVFSTPPVSTFDWVRAERTYHLCEVLFKVHKFWLTEDCWLQANLYLGLQDFDFEDQRPYCFSIVAGHGKSHVFNVELGSELAMWEKSFQRATF ITSN1_MOUSE Mouse 1 FUNCTION: Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. SUBCELLULAR LOCATION: Cytoplasmic; membrane-associated protein. Enriched in synaptosomes (By similarity). KFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYKMYKTPIFLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASE ITSN1_HUMAN Human 1 FUNCTION: Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. Isoform 1 could be involved in brain-specific synaptic vesicle recycling. SUBCELLULAR LOCATION: Cytoplasmic; membrane-associated protein. Enriched in synaptosomes (By similarity). KFLHSGKLYKAKNNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYKMYKTPIFLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASE AB1IP_BRARE Others 1 FUNCTION: Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodelling. SUBCELLULAR LOCATION: Cell membrane; peripheral membrane (By similarity). VPDLEGVLYLKEDGKKSWKQRYFLLRASGLYYSPKGKTKASRDLVCLVQFDNVNVYYCKEYRIKYKAPTDHCFMLKHPQIQKESQYIKFMCCDDEWSMNLWVTGIRVAKY AB1IP_CHICK Others 1 FUNCTION: Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodelling. SUBCELLULAR LOCATION: Cell membrane; peripheral membrane (By similarity). VPELEGALYLKEDGKKSWKRRYFLLRASGIYYVPKGKTKTSRDLMCFIQFENMNVYYGSQHKVKYKAPTDHCFVLKHPQIQKESQYIKYLCCDDRATLHQWVTGIRIAKY AB1IP_XENLA Others 1 FUNCTION: Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodelling. SUBCELLULAR LOCATION: Cell membrane; peripheral membrane (By similarity). VPELEAALYLKEDGKKSWKKRYFLLRASGIYYVPKGKTKTSRDLACFVQFDNVNVYYGTQYRMKYKAPTDHCFVLKHPQIQKESQYIKYLCCEDPWLLHQWVTGIRIAKY AB1IP_MOUSE Mouse 1 FUNCTION: Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodelling. Suppresses insulin- induced promoter activities through AP1 and SRE. Mediates Rap1- induced adhesion (By similarity). " SUBCELLULAR LOCATION: Cell membrane; peripheral membrane. Colocalizes with ENA/VASP proteins at lamellipodia tips and focal adhesions, and F-actin at the leading edge. At the membrane surface, associates, via the PH domain, preferentially with the inositol phosphates, PtdIns(5)P and PtdIns(3)P. This binding appears to be necessary for the efficient interaction of the RA domain to Ras-GTPases." VPELEGALYLKEDGKKSWKRRYFLLRASGIYYVPKGKTKTSRDLACFIQFENVNIYYGIQCKMKYKAPTDHCFVLKHPQIQKESQYIKYLCCDDARTLSQWVMGIRIAKY AB1IP_HUMAN Human 1 FUNCTION: Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodelling. Suppresses insulin- induced promoter activities through AP1 and SRE. Mediates Rap1- induced adhesion. " SUBCELLULAR LOCATION: Cell membrane; peripheral membrane (By similarity). Colocalizes with ENA/VASP proteins at lamellipodia tips and focal adhesions, and F-actin at the leading edge. At the membrane surface, associates, via the PH domain, preferentially with the inositol phosphates, PtdIns(5)P and PtdIns(3)P. This binding appears to be necessary for the efficient interaction of the RA domain to Ras-GTPases (By similarity)." VPELEGALYLKEDGKKSWKRRYFLLRASGIYYVPKGKTKTSRDLACFIQFENVNIYYGTQHKMKYKAPTDYCFVLKHPQIQKESQYIKYLCCDDTRTLNQWVMGIRIAKY OSBP2_MOUSE Mouse 1 FUNCTION: Binds 7-ketocholesterol (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). LDSYKGWLLKWTNYLKGYQRRWFVLGNGLLSYYRNQGEMAHTCRATINLASTHFETEDSCGILLCNGARTYHLKASSEVDRQHWITALELAKA OSBP2_HUMAN Human 1 FUNCTION: Binds 7-ketocholesterol. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. LDSFEGWLLKWTNYLKGYQRRWFVLGNGLLSYYRNQGEMAHTCRGTINLSTAHIDTEDSCGILLTSGARSYHLKASSEVDRQQWITALELAKA 3BP2_MOUSE Mouse 1 FUNCTION: Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. Binds to phosphatidylinositols; linking the hemopoietic tyrosine kinase fes to the cytoplasmic membrane in a phosphorylation dependent mechanism (By similarity). GVAKAGYLHKKGGTQLQLLKWPLRFVIIHKRCIYYFKSSTSASPQGAFSLSGYNRVMRAAEETTSNNVFPFKIIHISKKHRTWFFSASSEDERKSWMAFVRREIG 3BP2_HUMAN Human 1 FUNCTION: Binds differentially to the SH3 domains of certain proteins of signal transduction pathways. Binds to phosphatidylinositols; linking the hemopoietic tyrosine kinase fes to the cytoplasmic membrane in a phosphorylation dependent mechanism. GVAKAGYLHKKGGTQLQLLKWPLRFVIIHKRCVYYFKSSTSASPQGAFSLSGYNRVMRAAEETTSNNVFPFKIIHISKKHRTWFFSASSEEERKSWMALLRREIG OSBL1_HUMAN Human 1 FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3- phosphate (By similarity). LKRYEGPLWKSSRFFGWRLFWVVLEHGVLSWYRKQPDAVHNIYRQGCKHLTQAVCTVKSTDSCLFFIKCFDDTIHGFRVPKNSLQQSREDWLEAIEEHSA OSBL1_RAT Others 1 FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3- phosphate (By similarity). LKRFEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDGCLFSVRCFDDTVHGFRVPKNSLQQSREKWLEAIEEHSA OSBL1_MOUSE Mouse 1 FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3- phosphate. LKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTVHCFRVPKNSVQQSREKWLEAIEEHSA PKHA1_MOUSE Mouse 1 " FUNCTION: Binds specifically to phosphatidylinositol-3,4- diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane (By similarity)." " SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane; peripheral membrane protein (By similarity). Nucleus (By similarity). Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2 (By similarity)." QNRICGFLDIEENENSGKFLRRYFILDTREDSFVWYMDNPQNLPSGSSRVGAIKLTYISKVSDATKLRPKAEFCFVMNAGMRKYFLQANDQQDLVEWVNVLNKAIK PKHA2_BOVIN Others 1 " FUNCTION: Binds specifically to phosphatidylinositol-3,4- diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane (By similarity)." " SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane; peripheral membrane protein (By similarity). Nucleus (By similarity). Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2 (By similarity)." QNRICGFLDIEENENSGKFLRRYFILDTQANCLLWYMDNPQNLAIGAGAVGSLQLTYISKVSIATPKQKPKTPFCFVINALSQRYFLQANDQKDLKDWVEALNQASK PKHA2_HUMAN Human 1 " FUNCTION: Binds specifically to phosphatidylinositol-3,4- diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane (By similarity)." " SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane; peripheral membrane protein (By similarity). Nucleus (By similarity). Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2 (By similarity)." QNRICGFLDIEEHENSGKFLRRYFILDTQANCLLWYMDNPQNLAMGAGAVGALQLTYISKVSIATPKQKPKTPFCFVINALSQRYFLQANDQKDMKDWVEALNQASK PKHA1_HUMAN Human 1 " FUNCTION: Binds specifically to phosphatidylinositol-3,4- diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane." " SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; peripheral membrane protein. Nucleus. Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2." QNRICGFLDIEENENSGKFLRRYFILDTREDSFVWYMDNPQNLPSGSSRVGAIKLTYISKVSDATKLRPKAEFCFVMNAGMRKYFLQANDQQDLVEWVNVLNKAIK PKHA2_MOUSE Mouse 1 " FUNCTION: Binds specifically to phosphatidylinositol-3,4- diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane." " SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; peripheral membrane protein. Nucleus. Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2." QNRICGFLDIEDNENSGKFLRRYFILDTQANCLLWYMDNPQNLAVGAGAVGSLQLTYISKVSIATPKQKPKTPFCFVINALSQRYFLQANDQKDLKDWVEALNQASK PKHA4_MOUSE Mouse 1 " FUNCTION: Binds specifically to phosphatidylinositol-3-phosphate (PtdIns3P), but not to other phosphoinositides (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (Probable). PVHIRGWLHKQDSSGLRLWKRRWFVLSGHCLFYYKDSREESVLGSVLLPSYSVRPDGPGAPRGRRFTFTAEHPGMRTYVLAADTLEDLRGWLRALGRASR PKHA4_RAT Others 1 " FUNCTION: Binds specifically to phosphatidylinositol-3-phosphate (PtdIns3P), but not to other phosphoinositides (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (Probable). PVHIRGWLHKQDSSGLRLWKRRWFVLSGHCLFYYKDSREESVLGSVLLPSYSVRPDGPGAPRGRRFTFTAEHPGMRTYVLAADTLEDLRGWLRALGKASR PH1_ARATH Mouse 1 " FUNCTION: Binds specifically to phosphatidylinositol-3-phosphate (PtdIns3P), but not to other phosphoinositides." SUBCELLULAR LOCATION: Cytoplasm (Probable). NPERSGWLTKQGDYIKTWRRRWFVLKRGKLLWFKDQAAAGIRGSTPRGVISVGDCLTVKGAEDVVNKPFAFELSSGSYTMFFIADNEKEKEEWINSIGRSIV PKHA4_HUMAN Human 1 " FUNCTION: Binds specifically to phosphatidylinositol-3-phosphate (PtdIns3P), but not to other phosphoinositides." SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (Probable). PVHIRGWLHKQDSSGLRLWKRRWFVLSGHCLFYYKDSREESVLGSVLLPSYNIRPDGPGAPRGRRFTFTAEHPGMRTYVLAADTLEDLRGWLRALGRASR PKHA3_MOUSE Mouse 1 " FUNCTION: Binds specifically to phosphatidylinositol-4-phosphate (PtdIns4P), but not to other phosphoinositides (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (Probable). MEGVLYKWTNYLTGWQPRWFVLDNGILSYYDSQDDVCKGSKGSIKMAVCEIKVHPADNTRMELIIPGEQHFYMKAVNAAERQRWLVALGSSKA PKHA3_HUMAN Human 1 " FUNCTION: Binds specifically to phosphatidylinositol-4-phosphate (PtdIns4P), but not to other phosphoinositides." SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (Probable). MEGVLYKWTNYLTGWQPRWFVLDNGILSYYDSQDDVCKGSKGSIKMAVCEIKVHSADNTRMELIIPGEQHFYMKAVNAAERQRWLVALGSSKA RASL2_HUMAN Human 1 " FUNCTION: Ca(2+)-dependent Ras GTPase-activating protein, that switches off the Ras-MAPK pathway following a stimulus that elevates intracellular calcium." " SUBCELLULAR LOCATION: Localized to the cytosol as a result of its lack of phosphoinositide binding activity. Upon agonist-stimulated calcium mobilization, utilizes the C2A and C2B domains to associate with the plasma membrane." PPVKEGPLFIHRTKGKGPLMSSSFKKLYFSLTTEALSFAKTPSSKKSALIKLANIRAAEKVEEKSFGGSHVMQVIYTDDAGRPQTAYLQCKCVNELNQWLSALRKVSI CAPS_DROME Others 1 " FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles. However, it probably also participate to small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering." " SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Restricted to all classes of presynaptic termini independent of the ratio of vesicular content (DCVs versus SVs). Found in all identified classes of peripheral and central synapses. In the CNS, it is highly enriched in the synapse-dense neuropil, which lacks cell bodies. Present in all synapses in the neuropil where it precisely colocalizes with other pansynaptic markers. Similarly abundant in all classes of neuromuscular junction (NMJ) termini, including type I, II, and III NMJs, where it localizes to all 3 bouton types. Expressed at similar levels in boutons which contain primarily small clear glutamatergic vesicles, as well as boutons very highly enriched in large DCVs. It appears that neither bouton class contains a pure population of either SVs or DCVs, but only differs dramatically in the relative abundance of the vesicular classes. Thus, the level of expression does not correlate with the abundance of DCVs. Clearly present presynaptically and colocalizes exclusively with presynaptic markers." NMKHCGYLYAIGKSVWKKWKRRYFVLVQVSQYTFAMCSYKEKKSEPSEMMQLDGYTVDYIEAASANLMFGIDLNGGRYFFNAVREGDSISFACDDENECSLWVMAMYRATG CAPS_CAEBR Others 1 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense- core vesicles (By similarity). SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles (By similarity). Strongly enriched in synaptic fractions (By similarity). NLKYSGHCWCIGRNSWKKWKKRFFCLVQVSQYAFAVCSFREKKADPTEFIQLDGFTIDYMPESDPELSAQGGKHFFTAIKEGDELKFATDDENERHLWVQALYRATG CAPS_CAEEL Others 1 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense- core vesicles (By similarity). Specifically required to activate the neuronal G-alpha pathway. Functions with G-alpha proteins from the same motor neurons to regulate locomotion. SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles (By similarity). Strongly enriched in synaptic fractions. Often concentrated at or near active zones of motor neuron synapses. NLKYCGYCYCIGRNAWKKWKKRFFCLVQVSQYAFAVCSFRQKKADPTEFIQLDGFTIDYMPESDPELSAQGGKHFFTAIKEGDELKFATDDENERHLWVQALYRATG CAPS1_XENLA Others 1 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) (By similarity). SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Preferentially binds to DCVs but not to SVs. Binds phosphoinosides (By similarity). NMKHCGYLWVIGKNVWKRWKKRFFVLVQVSQYTFAMCSYREKKAEPQELLQLDGYTVDYTDPQPGLEGGRSFFNAVKEGDTVIFASDDEQDRILWVQAMYRATG CAPS1_MOUSE Mouse 1 " FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates to DCVs-membrane fusion. However, it may also participate to small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering (By similarity)." " SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. May preferentially binds to DCVs but not to SVs. Probably localizes to different vesicles compared to CADPS2. Binds phosphoinosides, with a strong selectivity for PtdIns(4,5)P2 over PtdIns(3,4,5)P3." NMKHSGYLWTIGKNVWKRWKKRFFVLVQVSQYTFAMCSYREKKAEPQELLQLDGYTVDYTDPQPGLEGGRAFFNAVKEGDTVIFASDDEQDRILWVQAMYRATG CAPS1_HUMAN Human 1 " FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates to DCVs-membrane fusion. However, it may also participate to small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering (By similarity)." " SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Preferentially binds to DCVs but not to SVs. Binds phosphoinosides, with a strong selectivity for PtdIns(4,5)P2 over PtdIns(3,4,5)P3. Probably localizes to different vesicles compared to CADPS2 (By similarity)." NMKHSGYLWAIGKNVWKRWKKRFFVLVQVSQYTFAMCSYREKKAEPQELLQLDGYTVDYTDPQPGLEGGRAFFNAVKEGDTVIFASDDEQDRILWVQAMYRATG CAPS1_RAT Others 1 " FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates to DCVs-membrane fusion. However, it may also participate to small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering." " SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Preferentially binds to DCVs but not to SVs. Binds phosphoinosides, with a strong selectivity for PtdIns(4,5)P2 over PtdIns(3,4,5)P3. Probably localizes to different vesicles compared to CADPS2." NMKHSGYLWTIGKNVWKRWKKRFFVLVQVSQYTFAMCSYREKKAEPQELLQLDGYTVDYTDPQPGLEGGRAFFNAVKEGDTVIFASDDEQDRILWVQAMYRATG CAPS2_HUMAN Human 1 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates neurotrophin release from granule cells leading to regulate cell differentiation and survival during cerebellar development. May specifically mediate the Ca(2+)- dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles (By similarity). SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Probably localizes to different vesicles compared to CADPS. Enriched on vesicular structures in the parallel fiber terminal of granule cells that are distinct from synaptic vesicles. HMKHSGYLYALGQKVWKRWKKRYFVLVQVSQYTFAMCSYREKKSEPQELMQLEGYTVDYTDPHPGLQGGCMFFNAVKEGDTVIFASDDEQDRILWVQAMYRATG CAPS2_MOUSE Mouse 1 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates neurotrophin release from granule cells leading to regulate cell differentiation and survival during cerebellar development. May specifically mediate the Ca(2+)- dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles. SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Probably localizes to different vesicles compared to CADPS. Enriched on vesicular structures in the parallel fiber terminal of granule cells that are distinct from synaptic vesicles. HMKHSGYLYALGQKVWKRWKKRYFVLVQVSQYTFAMCSYREKKSEPQELMQLEGYTVDYTDPHPGLQGGQVFFNAVKEGDTVIFASDDEQDRILWVQAMYRATG KPCD2_HUMAN Human 1 " FUNCTION: Calcium-independent, phospholipid-dependent, serine- and threonine-specific protein kinase." TTLREGWVVHYSNKDTLRKRHYWRLDCKCITLFQNNTTNRYYKEIPLSEILTVESAQNFSLVPPGTNPHCFEIVTANATYFVGEMPGGTPGGPSGQGAEAARGWETAIRQALM EXOC8_CHICK Others 1 FUNCTION: Component of the exocyst complex involved in the docking of exocystic vesicles with fusion sites on the plasma membrane (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). YLVYNGDLLEYDADHMAQIQRVHAFLMNDCLLVATALPNRRGAYRYDALYPLEGLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKKEWLEVLEETKR EXOC8_XENLA Others 1 FUNCTION: Component of the exocyst complex involved in the docking of exocystic vesicles with fusion sites on the plasma membrane (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). YLVYNGDLTEFDVDNMALIQKVHAFLMNDCLLIATSVPNRRGIYKYNALHNLDDLAVVNVKENPPMKDMFKILMFPESRIFQAENAKIKKEWLEILEQTKK EXOC8_MOUSE Mouse 1 FUNCTION: Component of the exocyst complex involved in the docking of exocystic vesicles with fusion sites on the plasma membrane (By similarity). " SUBCELLULAR LOCATION: Cytoplasm. Redistributes to growing neurites and growth cones during cell differentiation. Binds lipids with phosphatidylinositol-3,4,5-trisphosphate groups (By similarity)." YLVYNGDLVEYDADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKR EXOC8_RAT Others 1 FUNCTION: Component of the exocyst complex involved in the docking of exocystic vesicles with fusion sites on the plasma membrane. " SUBCELLULAR LOCATION: Cytoplasm. Binds lipids with phosphatidylinositol-3,4,5-trisphosphate groups (By similarity). Perinuclear in undifferentiated PC12 cells. Redistributes to growing neurites and growth cones during cell differentiation." YLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKR EXOC8_HUMAN Human 1 FUNCTION: Component of the exocyst complex involved in the docking of exocystic vesicles with fusion sites on the plasma membrane. " SUBCELLULAR LOCATION: Cytoplasm. Redistributes to growing neurites and growth cones during cell differentiation (By similarity). Binds lipids with phosphatidylinositol-3,4,5-trisphosphate groups." YLVYNGDLVEYDADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYSLDGLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEDTKR PREX1_HUMAN Human 1 " FUNCTION: Functions as a RAC1 guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol-3,4,5-triphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils." SUBCELLULAR LOCATION: Cytoplasm; cytosol. Mainly. Cell membrane. Some amount is apparently associated to the plasma membrane. QLLLQGTLLKISAGNIQERAFFLFDNLLVYCKRKSRVTGSKKSTKRTKSINGSLYIFRGRINTEVMEVENVEDGTADYHSNGYTVTNGWKIHNTAKNKWFVCMAKTAEEKQKWLDAIIRERE APEKCGYLELRGYKAKIFTVLRGNSVWLCKNEQDFKSGLGITIIPMNVANVKQVDRAVKQSFEIITPYRSFSFTADSEREKQEWIEAVQQSIA CENA2_MOUSE Mouse 1 " FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Potential). Binds phosphatidylinositol 3,4,5- trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). Possesses a stoichiometry of two binding sites for InsP4 with identical affinity (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Constitutively associated with the plasma membrane. Excluded from the nucleus (By similarity). PGNREGFLWKRGRDNAQFLRRRFVLLSREGLLKYYTKEEGKAPKAVISIKDLNATFQTEKIGHPHGLQITYRKEGHTRNLFVYHDSGKEIVDWFNALRAARL CENA2_HUMAN Human 1 " FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Potential). Binds phosphatidylinositol 3,4,5- trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). Possesses a stoichiometry of two binding sites for InsP4 with identical affinity." SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Constitutively associated with the plasma membrane. Excluded from the nucleus. PGNREGFLWKRGRDNSQFLRRKFVLLAREGLLKYFTKEQGKSPKAVISIKDLNATFQTEKIGHPHGLQITYRRDGHTRNLFVYHESGKEIVDWFNALRAARL CENA2_RAT Others 1 " FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Potential). Binds phosphatidylinositol 4,5- bisphosphate, phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). Binding of phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4-bisphosphate occurs at a much lower affinity. Possesses a stoichiometry of two binding sites for InsP4 with identical affinity (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Constitutively associated with the plasma membrane. Excluded from the nucleus (By similarity). PGDREGFLWKRGRDNSQFLRRRFVLLSREGLLKYYTKEEGKTPKAIINIKDLNATFQTEKIGHPHGLQITYRKEGQTRNLFVYHDSGKEIVDWFNALRAARL CENA1_HUMAN Human 1 " FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Probable). Binds phosphatidylinositol 3,4,5- trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4)." " SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Recruited to the plasma membrane upon epidermal growth factor-dependent activation of phosphatidylinositol 4,5-diphosphate (PtdInsP2) 3-kinase." AGYREGFLWKRGRDNGQFLSRKFVLTEREGALKYFNRNDAKEPKAVMKIEHLNATFQPAKIGHPHGLQVTYLKDNSTRNIFIYHEDGKEIVDWFNALRAARF POB1_SCHPO Yeast 1 FUNCTION: Has a role in cell elongation and separation. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Membrane-associated at the cell tips during interphase. TADCHGWMRKRSDRYGVWKSRYFVLKGTRLSYYHSLNDASEKGLIDMTSHRVTKTDDIVLSGGKTAIKLIPPAPGAAKAAVMFTPPKVHYFTCENNEELHRWSSAFLKATV AKT3_RAT Others 1 " FUNCTION: IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins (By similarity)." TIVKEDWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVAD AKT3_MOUSE Mouse 1 " FUNCTION: IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins. Truncated isoform 2/PKB gamma 1 without the second serine phosphorylation site could still be stimulated but to a lesser extent (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Membrane-associated after cell stimulation leading to its translocation. TIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVAD AKT3_HUMAN Human 1 " FUNCTION: IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins. Truncated isoform 2/PKB gamma 1 without the second serine phosphorylation site could still be stimulated but to a lesser extent." SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Membrane-associated after cell stimulation leading to its translocation. TIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVAD PLD1_RAT Others 1 " FUNCTION: Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity)." " SUBCELLULAR LOCATION: Perinuclear regions: endoplasmic reticulum, Golgi apparatus and late endosomes (By similarity)." PKGLEGMIMKRSGGHRIPGVNCCGHGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRIKVGKKETETKYGLRIDNLSRTLILKCNSYRHARWWGGAIEEFIQ PLD1_CRIGR Others 1 " FUNCTION: Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity)." " SUBCELLULAR LOCATION: Perinuclear regions: endoplasmic reticulum, Golgi apparatus and late endosomes (By similarity)." PKGLEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRIKVGRKETETKYGLRIDNLSRTLILKCNSYRHARWWGGAIEEFIQ PLD1_HUMAN Human 1 " FUNCTION: Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity)." " SUBCELLULAR LOCATION: Perinuclear regions: endoplasmic reticulum, Golgi apparatus and late endosomes (By similarity)." PKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQ PLD1_MOUSE Mouse 1 " FUNCTION: Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic." " SUBCELLULAR LOCATION: Perinuclear regions: endoplasmic reticulum, Golgi apparatus and late endosomes." PKGLEGMIMKRSGGHRIPGVNCCGHGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRVKVGRKETETKYGLRIDNLSRTLILKCNSYRHARWWGGAIEEFIR SYGP1_RAT Others 1 FUNCTION: Inhibitory regulator of the Ras-cAMP pathway. Member of the NMDAR signaling complex in excitatory synapses it may play a role in NMDAR-dependent control of AMPAR potentiation and synaptic plasticity. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. Mostly in excitatory glutamatergic synapses. LDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVK RASA2_MOUSE Mouse 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) and phospholipids. SUBCELLULAR LOCATION: Cell membrane (Potential). VHLKEGEMYKRAQGRTRIGKKNFKKRWFCLTSRELTYHRQQGKDAIYTIPVKNILAVEKLEEGSFNKKNMFQVIHTEKTLYIQANNCVEANEWIDVLCRVSR RASA3_HUMAN Human 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) with high affinity. Might be a specific IP4 receptor. SUBCELLULAR LOCATION: Cell membrane. IVLKEGFMIKRAQGRKRFGMKNFKKRWFRLTNHEFTYHKSKGDQPLYSIPIENILAVEKLEEESFKMKNMFQVIQPERALYIQANNCVEAKDWIDILTKVSQ RASA2_HUMAN Human 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4). SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm; perinuclear region. VHLKEGEMYKRAQGRTRIGKKNFKKRWFCLTSRELTYHKQPGKDAIYTIPVKNILAVEKLEESSFNKKNMFQVIHTEKPLYVQANNCVEANEWIDVLCRVSR RASA2_RAT Others 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4) and phospholipids. SUBCELLULAR LOCATION: Cell membrane (Potential). VHLKEGEMYKRAQGRTRIGKKNFKKRWFCLTSKELTYHKQQGKDAIYTIPVKNILAVEKLEESSFNKKNMFQVIHTEKTLYIQANNCVEANEWIDMLCRVSR RASA3_BOVIN Others 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4). ILLKEGFMIKRAQGRKRFGMKNFKKRWFRLTNHEFTYQKSKGDPPLYSIPIENILAVEPLEEESFKMKNMFQVIQPERALYIQANNCVEAKAWIDILTKVSQ RASA3_MOUSE Mouse 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4). ILLKEGFMIKRAQGRKRFGMKNFKKRWFRLTNHEFTYQKSKGDQPLCNIPIENILAVERLEEESFRMKNMFQVIQPERALYIQANNCVEAKDWIDILTKVSQ ENQLSGNLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDNHPLASLPLLGYSLTIPSESENIQKDYVFKLHFKSHVYYFRAESEYTFERWMEVIRSATS GRB14_MOUSE Mouse 1 FUNCTION: Interacts with the cytoplasmic domain of the autophosphorylated insulin receptor which is then inhibited. The interaction is mediated by the SH2 domain (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus; Golgi membrane; peripheral membrane protein (By similarity). Endosome; endosomal membrane; peripheral membrane protein (By similarity). YPEIHGFLHAKEQGKKSWKKAYFFLRRSGLYFSTKGTSKEPRHLQLFSEFSTSHVYMSLAGKKKHGAPTPYGFCLKPNKAGGPRDLKMLCAEEEQSRTCWVTAIRLLKD NSVICSFLHYMEKGGKGWHKAWFVVPENEPLVLYIYGAPQDVKAQRSLPLIGFEVGPPEAGERPDRRHVFKITQSHLSWYFSPETEELQRRWMAVLGRAGR GRB14_HUMAN Human 1 FUNCTION: Interacts with the cytoplasmic domain of the autophosphorylated insulin receptor which is then inhibited. The interaction is mediated by the SH2 domain (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus; Golgi membrane; peripheral membrane protein. Endosome; endosomal membrane; peripheral membrane protein. YPEIHGFLHAKEQGKKSWKKIYFFLRRSGLYFSTKGTSKEPRHLQFFSEFGNSDIYVSLAGKKKHGAPTNYGFCFKPNKAGGPRDLKMLCAEEEQSRTCWVTAIRLLKY QSLMCSFLQLIGDKWGKSGPRGWCVIPRDDPLVLYVYAAPQDMRAHTSIPLLGYQVTVGPQGDPRVFQLQQSGQLYTFKAETEELKGRWVKAMERAAS GRB14_RAT Others 1 FUNCTION: Interacts with the cytoplasmic domain of the autophosphorylated insulin receptor which is then inhibited. The interaction is mediated by the SH2 domain. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus; Golgi membrane; peripheral membrane protein (By similarity). Endosome; endosomal membrane; peripheral membrane protein (By similarity). YPEIHGFLHAKEQGKKSWKKAYFFLRRSGLYFSTKGTSKEPRHLQFFSEFSTSNVYMSLAGKKKHGAPTPYGFCFKPTKAGGPRDLKMLCAEEDQSRMCWVTAIRLLKY QSLVCSFLQLIGDKCSRSLPRSWCVIPRDDPLVLYVYAAPQDTKAHTSIPLLGYQVISGPQGDPRVFQLQQSGQQYTFKAESVELQGRWVTAIKRAAS URP1_MOUSE Mouse 1 " FUNCTION: Involved in cell adhesion, possibly via its interaction with integrins (By similarity)." " SUBCELLULAR LOCATION: Cytoplasm (By similarity). Colocalizes with filamentous actin. Cell membrane; cell-matrix junction; focal adhesion. Constituent of focal adhesions (By similarity). Upon TGFB1 treatment, it localizes to membrane ruffles (By similarity)." KLFRPKKLMLKACKQYWFVFKDTSIAYFKNKELEQGEPIEKLNLRGCEIVPDVNVSGRKFGIKLLIPVADGMNEVYLRCDHEDQYARWMAACILASK NSEVCSFLQYMEKSKPWQKIWCVIPKQDPLVLYMYGAPQDVRAQATIPLLGYVVDDMPKSADLPHSFKLTQSKSVHSFAADNEELKQKWLKIILLAVT URP1_HUMAN Human 1 " FUNCTION: Involved in cell adhesion, possibly via its interaction with integrins. May mediate TGF-beta 1 signaling in tumor progression." " SUBCELLULAR LOCATION: Cytoplasm. Colocalizes with filamentous actin. Cell membrane; cell-matrix junction; focal adhesion. Constituent of focal adhesions. Upon TGFB1 treatment, it localizes to membrane ruffles." KLFRPKKLLPKAFKQYWFIFKDTSIAYFKNKELEQGEPLEKLNLRGCEVVPDVNVAGRKFGIKLLIPVADGMNEMYLRCDHENQYAQWMAACMLASK NSEVCSFLQYMEKSKPWQKIWCVIPKQDPLVLYMYGAPQDVRAQATIPLLGYIVDDMPKSADLPHSFKLTQSKSVHSFAADSEELKQKWLKIILLAVT ELMO2_MOUSE Mouse 1 FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). SSFRKIGNRRRQERFWHCRLALNHKVLHYGDLDDNPQGEVTFESLQEKIPVADIKAIVTGKDCPHMKEKSALKQNKEVLELAFSILYDPDETLNFIAPNKYEYCIWIDGLSALLGKDMSSEL GSAISGYLSRCKRGKRHWKKLWFVIKGKVLYTYMASEDKVALESMPLLGFTIAPEKEEGSSEVGPIFHLYHKKTLFYSFKAEDTNSAQRWIEAMEDASV ELMO3_HUMAN Human 1 FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). RLCEGTLFRKISSRRRQDKLWFCCLSPNHKLLQYGDMEEGASPPTLESLPEQLPVADMRALLTGKDCPHVREKGSGKQNKDLYELAFSISYDRGEEEAYLNFIAPSKREFYLWTDGLSALLGS GSAISGYLSRCKSGKRRWKKLWLVIKGKVLYTYLASEDKVAMESIPLLGFTIAPEKEEGSSEVGPVFHLYHKKTLFYSFKAEDSNSAQRWMEAMEDASV ELMO3_MOUSE Mouse 1 FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). RLCEGMLFRKISSRRRQDKLWFCCLSPNHKVLQYGDVEEGAKPPTLESLPEQLPVADIRALLMGKDCPHVREKGSGKQNKDLYELAFSISYDHGEEEAYLNFIAPSKRDFYLWTDGLSALLGS DSSMSGYLYRSKGNKKPWKHFWFVIKNKVLYTYAASEDVAALESQPLLGFTVIQVKDENSESKVFQLLHKNMLFYVFKAEDAHSAQKWIEAFQEGTI ELMO1_MOUSE Mouse 1 FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Translocation to plasma membrane seems to be mediated by DOCK1 and CRK (By similarity). RLVEGTCFRKLNARRRQDKFWYCRLSPNHKVLHYGDLEESPQGEVPHDSLQDKLPVADIKAVVTGKDCPHMKEKGALKQNKEVLELAFSILYDSNCQLNFIAPDKHEYCIWTDGLNALLGKD DSTMSGYLYRSKGSKKPWKHLWFVIKNKVLYTYAASEDVAALESQPLLGFTVTLVKDENSESKVFQLLHKGMVFYVFKADDAHSTQRWIDAFQEGTV ELMO2_HUMAN Human 1 FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1. SUBCELLULAR LOCATION: Cytoplasm. SSFRKIGNRRRQERFWYCRLALNHKVLHYGDLDDNPQGEVTFESLQEKIPVADIKAIVTGKDCPHMKEKSALKQNKEVLELAFSILYDPDETLNFIAPNKYEYCIWIDGLSALLGKDMSSEL ELMO1_HUMAN Human 1 FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Translocation to plasma membrane seems to be mediated by DOCK1 and CRK. RLVEGTCFRKLNARRRQDKFWYCRLSPNHKVLHYGDLEESPQGEVPHDSLQDKLPVADIKAVVTGKDCPHMKEKGALKQNKEVLELAFSILYDSNCQLNFIAPDKHEYCIWTDGLNALLGKD ATG26_PICPA Yeast 1 FUNCTION: Involved in the biosynthesis of sterol glucoside. Involved in the invagination of peroxisomes into the vacuole for their degradation in both glucose-induced micropexophagy and ethanol-induced macropexophagy. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Found in perivacuolar punctate structures and micropexophagic apparatus (MIPA). VTMSGALSIRSSTTMRFSVRRWAVLKGNYFRLYANSTERYFPSLNIDLRFLLKVELSNPNLEENKPTVFKLITEARTHYFQADSLDNARSWVTDLRKHIF DAPP1_MOUSE Mouse 1 FUNCTION: May act as a B-cell-associated adapter that regulates B- cell antigen receptor (BCR)-signaling downstream of PI3K. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). Membrane-associated after cell stimulation leading to its translocation (By similarity). LGTKEGYLTKQGGLVKTWKTRWFTLQRNELKYFKDQMSPEPIRILDLTECSAVQFDYSQERVNCFCLVFPFRTFYLCAKTGVEADEWIKILRWKLS DAPP1_HUMAN Human 1 FUNCTION: May act as a B-cell-associated adapter that regulates B- cell antigen receptor (BCR)-signaling downstream of PI3K. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Membrane-associated after cell stimulation leading to its translocation. LGTKEGYLTKQGGLVKTWKTRWFTLHRNELKYFKDQMSPEPIRILDLTECSAVQFDYSQERVNCFCLVFPFRTFYLCAKTGVEADEWIKILRWKLS MRCKG_MOUSE Mouse 1 " FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Concentrates at the leading edge of cells (By similarity). GTAYEGFLSVPRPSGVRRGWQRVYAALSDSRLLLFDAPDPRGSLASGVLLQALDLRDPQFSATPVLAPDVIHAQSKDLPRIFRVTASQLTVPPTTCTVLLLAENEGERERWLQVLGELQR MRCKG_HUMAN Human 1 " FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Concentrates at the leading edge of cells. GTAYEGFLSVPRPSGVRRGWQRVFAALSDSRLLLFDAPDLRLSPPSGALLQVLDLRDPQFSATPVLASDVIHAQSRDLPRIFRVTTSQLAVPPTTCTVLLLAESEGERERWLQVLGELQR MRCKB_HUMAN Human 1 " FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation (By similarity)." " SUBCELLULAR LOCATION: Cytoplasmic. Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (By similarity)." GTAYKGHVKVPKPTGVKKGWQRAYAVVCDCKLFLYDLPEGKSTQPGVIASQVLDLRDDEFSVSSVLASDVIHATRRDIPCIFRVTASLLGAPSKTSSLLILTENENEKRKWVGILEGLQS MRCKB_MOUSE Mouse 1 " FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation (By similarity)." " SUBCELLULAR LOCATION: Cytoplasmic. Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (By similarity)." GTAYKGYVKVPKPTGVKKGWQRAYAVVCDCKLFLYDLPEGKSTQPGVVASQVLDLRDEEFAVSSVLASDVIHATRRDIPCIFRVTASLLGSPSKTSSLLILTENENEKRKWVGILEGLQA MRCKB_RAT Others 1 " FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation (By similarity)." " SUBCELLULAR LOCATION: Cytoplasmic. Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (By similarity)." GTAYKGYVKVPKPTGVKKGWQRAYAVVCDCKLFLYDLPEGKSTQPGVIASQVLDLRDDEFAVSSVLASDVIHATRRDIPCIFRVTASLLGSPSKTSSLLILTENENEKRKWVGILEGLQA MRCKA_HUMAN Human 1 " FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation." " SUBCELLULAR LOCATION: Cytoplasmic. Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (By similarity)." GTAYEGHVRIPKPAGVKKGWQRALAIVCDFKLFLYDIAEGKASQPSVVISQVIDMRDEEFSVSSVLASDVIHASRKDIPCIFRVTASQLSASNNKCSILMLADTENEKNKWVGVLSELHK MRCKA_RAT Others 1 " FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation." " SUBCELLULAR LOCATION: Cytoplasmic. Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent." GTAYEGHVRIPKPAGVKKGWQRALAVVCDFKLFLYDIAEGKASQPSSVISQVIDMRDEEFSVSSVLASDVIHASRKDIPCIFRVTASQLSAPSDKCSILMLADSETERSKWVGVLSELHK ATG26_CANAL Yeast 1 FUNCTION: May be involved in decane metabolism and autophagy (By similarity). Involved in the biosynthesis of sterol glucoside. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). SIVYSGNLGLKSAKYGEVVLNTVLQHRYWAVLRAETLSIYSSSTNLYFPVLVIDIKKCLYTEIIDKEKLNREAISPVNRGTYSPNGGLSGTATPRASTLENTASELNSMLSGDSYSPTEDNVETTASTVWFKLVTKKKTYKFSCDSSFSARQWCNNITKLIF ATG26_YEAST Yeast 1 FUNCTION: May be involved in decane metabolism and autophagy (By similarity). Involved in the biosynthesis of sterol glucoside. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. SVKMSGNLNIRTKLIRSTRYWCVLKNHLFSMYTSSTELYFPVLTIDLREVQKIETQKHTLNGSATKTFKLYTDESTFKFNADSEFSAKSWVNALKKEQF ATG26_ASHGO Yeast 1 FUNCTION: May be involved in decane metabolism and autophagy. Involved in the biosynthesis of sterol glucoside (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). SARLTGNLSICNNGLSISGISGKPTRYWTVLKDHTLSLYSSSTDLYFPVLTIDLRYVTKVQHCKNNGKDTRQFHITTESKTYTFYSDNEHSARSWSSALKKQVF ATG26_CRYNE Others 1 FUNCTION: May be involved in decane metabolism and autophagy. Involved in the biosynthesis of sterol glucoside (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). LLVKSGPLHKKASRSKLNTKFWVVLKNDVLSWYESTSDPYFPKGNISLQYCHSCDAVSGTRFKVRTSERNYTFTADTESSRDEWVKAIQKVMF ATG26_YARLI Others 1 FUNCTION: May be involved in decane metabolism and autophagy. Involved in the biosynthesis of sterol glucoside (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). RYAYTPTIEDLFLLTQPSRTQSELARRIKTENILNSFHDSLEAAYEKCHGGANPEEHQSNKTEYFQQKLKGFAALDVDEQLIADYPVWLLKNVLIQGHLYI ATG26_LEPMC Others 1 FUNCTION: May be involved in decane metabolism and autophagy. Involved in the biosynthesis of sterol glucoside (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). DVSKTGYLSKRGRSKHNRYWFILRGDVLAYYTNPAELYFPRNRINLQYAISAEVLEPKRKGDEETSFVVTTDERTYQFKADSVASAREWVKSIQKVIF ATG26_NEUCR Others 1 FUNCTION: May be involved in decane metabolism and autophagy. Involved in the biosynthesis of sterol glucoside (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). EIAKSGYLSKSGKRNPKYNRYWFRLKGDVLSYYQDPKDHYFPAGQIDLRYGISASVNDKEKEGNYFSVSTHHRTYHFKADSARSAKEWVKSLQRVIF ATG26_DEBHA Yeast 1 FUNCTION: May be involved in decane metabolism and autophagy. Involved in the biosynthesis of sterol glucoside (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (Potential). DVIQSGSLGMKTALYGDTVFSTPLTHRFWVILRNETITVYHSPTDLYFPITLIDLKSCVRAEVIEKGRNDNASPRPDLHRNDSQEVSSGDEEVEFSNMLNSNYQLEDNSENVSGGYWFKVVTKKKTHKFHSDSLYSARQWVNNIVKVVF ATG26_EMENI Others 1 FUNCTION: May be involved in decane metabolism and autophagy. Involved in the biosynthesis of sterol glucoside (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (Potential). RVIKSGYIYKRGRKNPKYNRYWFSLKEDVLSYYADPSNLYFPSGQIDLRYGISASLTEPKDKSRESRDFQVTTDHRTYYFRADSSVNAKEWVRALQKVIF ATG26_KLULA Yeast 1 FUNCTION: May be involved in decane metabolism and autophagy. Involved in the biosynthesis of sterol glucoside (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (Potential). DFNVTGSLRLISGHVLSKSHRYWVVLKGHTLSFHNSSTDLYFPLLTIDLRDISSVQMTSSENNPTKFELSIKDQSLVLKADSFHSARHWVSSIKKQMF SLETSSYLNVLVNSQWKSRWCSVRDNHLHFYQDRNRSKVAQQPLSLVGCEVVPDPSPDHLYSFRILHKGEELAKLEAKSSEEMGHWLGLLLSESG DDEF1_MOUSE Mouse 1 " FUNCTION: May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types (By similarity). Posseses phosphatidylinositol 4,5-biphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2." SUBCELLULAR LOCATION: Cytoplasmic; predominantly. Membrane- associated; partially. GSEKKGFLLKKSDGIRKVWQRRKCAVKNGILTISHATSNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYIAWISVLTNSKE SLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRSKVAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSSEEMGHWLGLLLSESG STAP1_MOUSE Mouse 1 FUNCTION: May function as an adapter molecule downstream of KIT in the proliferation or differentiation of hematopoietic stem cells. SUBCELLULAR LOCATION: Cytoplasm (Potential). PLYFEGFLLVKRSDHQEYKHYWTELRGTTLFFYTDKKSTIYVGKLDIIDLVCLTGQHSTEKNCAKFTLVLPKEEVHVKTENTESGEEWRGFILTVTE CNKR2_RAT Others 1 " FUNCTION: May function as an adapter protein or regulator of Ras signaling pathways, in synaptic junctions." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). RGDCEGWLWKKKDAKSYFSQKWKKYWFVLKDASLYWYINEEDEKAEGFISLPEFKIDRASECRKKYAFKACHPKIKSFYFAAEHLDDMNRWLNRINMLTA CNKR1_HUMAN Human 1 FUNCTION: May function as an adapter protein or regulator of Ras signaling pathways. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). RPDCDGWLLLRKAPGGFMGPRWRRRWFVLKGHTLYWYRQPQDEKAEGLINVSNYSLESGHDQKKKYVFQLTHDVYKPFIFAADTLTDLSMWVRHLITCIS CNKR2_MOUSE Mouse 1 FUNCTION: May function as an adapter protein or regulator of Ras signaling pathways. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). RGDCEGWLWKKKDAKSYFSQKWKKYWFVLKDASLYWYINEEDEKAEGFISLPEFKIDRASECRKKYAFKACHPKIKSFYFAAEHLDDMNRWLNRINMLTA CNKR2_HUMAN Human 1 FUNCTION: May function as an adapter protein or regulator of Ras signaling pathways. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. RGDCEGWLWKKKDAKSYFSQKWKKYWFVLKDASLYWYINEEDEKAEGFISLPEFKIDRASECRKKYAFKACHPKIKSFYFAAEHLDDMNRWLNRINMLTA DGKD_HUMAN Human 1 FUNCTION: May function as signaling molecule. Isoform 2 may be involved in cell growth and tumorigenesis. SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Isoform 1: Membrane; peripheral membrane protein. TIIKEGMLTKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITPCRKLILCADNRKEMEDWIAALKTVQN PLD2_HUMAN Human 1 FUNCTION: May have a role in signal-induced cytoskeletal regulation and/or endocytosis (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). KGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVVKDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQARWWAQEITELAQ PLD2_RAT Others 1 FUNCTION: May have a role in signal-induced cytoskeletal regulation and/or endocytosis (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). KGLEGVIRKRSGGHRVPGFTCCGRDQVCYRWSKRWLVVKDSFLLYMRPETGAISFVQLFDPGFEVQVGKRSTEARYGVRIDTSHRSLILKCSSYRQARWWGQEITELAQ PLD2_MOUSE Mouse 1 FUNCTION: May have a role in signal-induced cytoskeletal regulation and/or endocytosis. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. KGLEGVIRKRSGGHRVPGFTFCGRDQVCYRWSKRWLVVKDSFLLYMRPETGAISFVQLFDPGFEVQVGKRSTETRYGVRIDTSHRSLILKCSSYRQARWWGQEITELAQ DIHSEGVLSQESSQSTFLCDFLYQAPSAASKLSSEKKLLEETNKKWCVLEGGFLSYYENDKSTTPNGTININEVICLAIHKEDFYLNTGPIFIFEIYLPSERVFLFGAETSQAQRKWTEAIAKHFV DYDLIGQLFYKDCHALDQWRKGWFAMDKSSLHFCLQMQEVQGDRMHLRRLQELTISTMVQNGEKLDVLLLVEKGRTLYIHGHTKLDFTVWHTAIEKAAGTD GSIKEGILKIKEEPSKILSGNKFQDRYFVLRDGFLFLYKDVKSSKHDKMFSLSSMKFYRGVKKKMKPPTSWGLTAYSEKHHWHLCCDSSQTQTEWMTSIFIAQH DUET_HUMAN Human 1 FUNCTION: May phosphorylate the cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm. Associated with the cytoskeleton. TLTAQGKLLQQDTFYVIELDAGMQSRTKERRVFLFEQIVIFSELLRKGSLTPGYMFKRSIKMNYLVLEENVDNDPCKFALMNRETSERVVLQAANADIQQAWVQDINQVLE QTAAAASRVSSEKKLLEDTNKKWCVLEGGFLSYYENDRCTTPNGTINISEVICLAVHKEDFYLNTGPIFVFEIYLPSERVFLFGAETSQIQRKWTETIAKRFV DYDLIGQLFYKDCHALDQWRKGWFAMDKSSLCFCLQTQEAQEERMNLRRLQELTISTMVQNGEKVDVLLLVEKGRTLYIHGHTKLDFTVWHTAIEKAAG KSIKEGILKLKEEPSKILSGNKFQDRCVVLRDGHLFIYKDPKSSKHDKMFPLRAMKFYLGVKKKMKPPTSWGLTVYSEKHHWHLCCDSLQAQMEWMASIFIAQH ITK_MOUSE Mouse 1 " FUNCTION: May play a role in T-cell development, potentially in thymic selection." " SUBCELLULAR LOCATION: Localizes to cell surface receptors in the plasma membrane after stimulation with respective receptors (TCR, CD28, CD2) in T-cells." FILLEEQLIKKSQQKRRTSPSNFKVRFFVLTKASLAYFEDRHGKKRTLKGSIELSRIKCVEIVKSDISIPCHYKYPFQTLVYLQVVHDNYLLYVFAPDCESRQRWVLTLKEETR TVSHSGFLYKTASAGKLLQDRRAREEFSRRWCVLGDGVLSYFENERAVTPNGEIRASEIVCLAVPPPDTHGFEHTFEVYTEGERLYLFGLESAEQAHEWVKCIAKAFV GDTKHGMMKFREDRSLLGLGLPSGGFHDRYFILNSSCLRLYKEVRSQRPWSGAPETSHRPEKEWPIKSLKVYLGVKKKLRPPTCWGFTVVHETEKHEKQQWYLCCDTQMELREWFATFLFVQH ARHGB_RAT Others 1 FUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13 (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By similarity). Translocated to the membrane upon stimulation (By similarity). KMIHEGPLTWRISKDKTLDLQVLLLEDLVVLLQRQEERLLLKCHSKTAVGSSDSKQTFSPVLKLNAVLIRSVATDKRAFFIICTSELGPPQIYELVALTSSDKNIWMELLEEAVQ ESPRVGLLRCREEPPRLLGSRFQERFFLLRGRCLLLLKEKKSSKPEREWPLEGAKVYLGIRKKLKPPTPWGFTLILEKMHLYLSCTDEDEMWDWTTSILKAQH ARHGC_MOUSE Mouse 1 FUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13 (By similarity). SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane (Probable). Translocated to the membrane upon stimulation (Probable). KMIHEGPLVWKVNRDKSIDLYTLLLEDILVLLQKQDDRLVLRCHSKILASTADSKHTFSPVIKLSTVLVRQVATDNKALFVISMSDNGAQIYELVAQTVSEKTVWQDLICRMAA LNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEIDLSACYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVH ATYRGFLYCGSISNKAGAPPLRRGRDAPPRLWCVLGAALEMFASESSPEPLSLLQPQDIVCLGVSPPPADPGDLDRFPFSFELILTGGRIQHFATDGADSLEAWISAVGKWFSPL LLRMGRLWLRSPSHAGLAPGLWLSGFGLLRGDHLFLCPAPGPGPPAPEDMVHLRRLQEISVVSAADTPDKKEHLVLVETGRTLYLQGEGRLDFAAWNTAIGGAAGGG ESPRVGLLRCREEPPRLLGNRFQERFFLVRGRCLLLLKEKKSSKPEREWSLEGAKVYLGIRKKLKPPTLWGFTLILEKMHLCLSCMDEEEMWDWTTSILKAQH ARHGC_HUMAN Human 1 FUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane (Probable). Translocated to the membrane upon stimulation (Probable). KMIHEGPLVWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLRCHSKILASTADSKHTFSPVIKLSTVLVRQVATDNKALFVISMSDNGAQIYELVAQTVSEKTVWQDLICRMAA LNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEINLSTCYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVL ARHGB_HUMAN Human 1 FUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. SUBCELLULAR LOCATION: Cytoplasm. Membrane. Translocated to the membrane upon stimulation. KMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLLLKCHSKTAVGSSDSKQTFSPVLKLNAVLIRSVATDKRAFFIICTSKLGPPQIYELVALTSSDKNTWMELLEEAVR LNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEINLSTCYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVL OSBP1_RABIT Others 1 FUNCTION: May play a role in the regulation of sterol metabolism. Binds a range of oxysterols. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus; Golgi membrane; peripheral membrane protein (By similarity). When bound to oxysterols it translocates to the periphery of Golgi membranes (By similarity). GSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQTYHLKASSEVERQRWVTALELAKA OSBP1_HUMAN Human 1 FUNCTION: May play a role in the regulation of sterol metabolism. Binds a range of oxysterols. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus; Golgi membrane; peripheral membrane protein. When bound to oxysterols it translocates to the periphery of Golgi membranes. GSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQTYHLKASSEVERQRWVTALELAKA TARA_MOUSE Mouse 1 " FUNCTION: May regulate actin cytoskeletal organization, cell spreading and cell contraction by directly binding and stabilizing filamentous F-actin. The localized formation of TARA and TRIO complexes coordinates the amount of F-actin present in stress fibers. May also serve as a linker protein to recruit proteins required for F-actin formation and turnover." SUBCELLULAR LOCATION: Nucleus. Cytoplasm; localized to F-actin in a periodic pattern (By similarity). LNFKKGWMSILDEPGEWKKHWFVLTDSSLKYYRDSTAEEADELDGEIDLRSCTDVTEYAVQRNYGFQIHTKDAVYTLSAMTSGIRRNWIEALRKTVR TARA_HUMAN Human 1 " FUNCTION: May regulate actin cytoskeletal organization, cell spreading and cell contraction by directly binding and stabilizing filamentous F-actin. The localized formation of TARA and TRIO complexes coordinates the amount of F-actin present in stress fibers. May also serve as a linker protein to recruit proteins required for F-actin formation and turnover." SUBCELLULAR LOCATION: Nucleus. Cytoplasm; localized to F-actin in a periodic pattern. LNFKKGWMSILDEPGEPPSPSLTTTSTSQWKKHWFVLTDSSLKYYRDSTAEEADELDGEIDLRSCTDVTEYAVQRNYGFQIHTKDAVYTLSAMTSGIRRNWIEALRKTVR EFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTD RAPH1_HUMAN Human 1 FUNCTION: Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion. " SUBCELLULAR LOCATION: Cell membrane; peripheral membrane. Recruited to the membrane, via the PH domain, by the phosphoinositide, PI(3,4)P2. Colocalizes with ENAH/VASP at the tips of lamellipodia and filopodia. Also colocalizes with the pathogens, Vaccinia and Enteropathogenic E.coli (EPEC) at the interface between the pathogen and their actin." VPEIEGVLWLKDDGKKSWKKRYFLLRASGIYYVPKGKAKVSRDLVCFLQLDHVNVYYGQDYRNKYKAPTDYCLVLKHPQIQKKSQYIKYLCCDDVRTLHQWVNGIRIAKY DRP2A_ARATH Mouse 1 FUNCTION: Microtubule-associated force-producing protein involved in clathrin-mediated vesicle trafficking from the trans-Golgi network to the central vacuole. Able to bind and hydrolyze GTP. Binds specifically to phosphatidylinositol-3-phosphate (PtdIns3P). SUBCELLULAR LOCATION: Cytoplasm; cytosol. Golgi apparatus; Golgi membrane; peripheral membrane protein. GEITAGYLMKKSAKTNGWSRRWFVLNEKTGKLGYTKKQEERNFRGTITLEECTIEEIPEDEVEKSKSSKDKKANGPDSKGPGLVFKITCKVPYKTVLKAHNALVLKAESVVDKNEWINKLQKVIQ DYN3_HUMAN Human 1 " FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Potential). Microtubule- associated (Potential). QVIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKDYRFLELACDSQEDVDSWKASLLRAGV DYN1_CAEEL Others 1 " FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis." SUBCELLULAR LOCATION: Cytoplasm. Microtubule-associated. QVIRKGWLSLSNVSFVRGSKDNWFVLMSDSLSWYKDDEEKEKKYMLPLDGVKLKDIEGGFMSRNHKFALFYPDGKNIYKDYKQLELGCTNLDEIDAWKASFLRAGV DYN1_HUMAN Human 1 " FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis." SUBCELLULAR LOCATION: Cytoplasm. Microtubule-associated. LVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGV DYN1_MOUSE Mouse 1 " FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis." SUBCELLULAR LOCATION: Cytoplasm. Microtubule-associated. QDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGV DYN1_RAT Others 1 " FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis." SUBCELLULAR LOCATION: Cytoplasm. Microtubule-associated. LVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGV DYN3_RAT Others 1 " FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis." SUBCELLULAR LOCATION: Cytoplasm. Microtubule-associated. QVIRKGWLTVSNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKGFMSSKHVFALFNTEQRNVYKDYRSLELACDSQEDVDSWKASLLRAGV DYN2_MOUSE Mouse 1 " FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis." SUBCELLULAR LOCATION: Cytoplasmic. Microtubule-associated. Also found in the postsynaptic density of neuronal cells (By similarity). LVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGV DYN2_RAT Others 1 " FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis." SUBCELLULAR LOCATION: Cytoplasmic. Microtubule-associated. Also found in the postsynaptic density of neuronal cells (By similarity). LVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGV DYN2_HUMAN Human 1 " FUNCTION: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis." SUBCELLULAR LOCATION: Cytoplasmic. Microtubule-associated. Also found in the postsynaptic density of neuronal cells. LVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGV DYN_DROME Others 1 FUNCTION: Microtubule-associated force-producing protein which is involved in the production of microtubule bundles and which is able to bind and hydrolyze GTP. Implicated in endocytic protein sorting. SUBCELLULAR LOCATION: Cytoplasm. Microtubule-associated. QVIRKGHMVIQNLGIMKGGSRPYWFVLTSESISWYKDEDEKEKKFMLPLDGLKLRDIEQGFMSMSRRVTFALFSPDGRNVYKDYKQLELSCETVEDVESWKASFLRAGV MTMRD_HUMAN Human 1 FUNCTION: Not known. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Associated with membranes. NRSFEGTLYKRGALLKGWKPRWFVLDVTKHQLRYYDSGEDTSCKGHIDLAEVEMVIPAGPSMGAPKHTSDKAFFDLKTSKRVYNFCAQDGQSAQQWMDKIQSCIS CEND1_HUMAN Human 1 " FUNCTION: Phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). KKVKSGWLDKLSPQGKRMFQKRWVKFDGLSISYYNNEKEMYSKGIIPLSAISTVRVQGDNKFEVVTTQRTFVFRVEKEEERNDWISILLNALK CEND1_MOUSE Mouse 1 " FUNCTION: Phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). AKEKCGWLDKLSPQGKRMFQKRWVKFDGLSISHYNNDREMYSKGIIPLTAISTVRAQGDNKFEIVTTQRTFVFRVEKEEERNDWISILLSALK CEND3_HUMAN Human 1 " FUNCTION: Phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Acts on ARF6, RAC1, RHOA and CDC42. Plays a role in the internalization of anthrax toxin." " SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane; peripheral membrane protein (By similarity). Cytoplasmic, and associated with F-actin-rich membrane ruffles and lamellipodia (By similarity)." TPLLSGWLDKLSPQGNYVFQRRFVQFNGRSLMYFGSDKDPFPKGVIPLTAIEMTRSSKDNKFQVITGQRVFVFRTESEAQRDMWCSTLQSCLK CEND3_MOUSE Mouse 1 " FUNCTION: Phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Acts preferentially on ARF5 and on RHOA." " SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; peripheral membrane protein. Cytoplasmic, and associated with F-actin-rich membrane ruffles and lamellipodia." VPLLSGWLDKLSPQGNYVFQRRFVQFNGRSLMYFGSDKDPFPKGVIPLTAIEMTRSSKDNKFQVITGQRVFVFRTESEAQRDLWCSTLQSCLK CEND2_HUMAN Human 1 " FUNCTION: Phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Has a preference for ARF1 and ARF5 (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus; Golgi stack; Golgi stack membrane; peripheral membrane protein. Associated with Golgi stacks in resting cells. Throughout the cytoplasm and in surface protrusion in cells that are in the process of attaching to a surface and spreading. PVIKAGWLDKNPPQGSYIYQKRWVRLDTDHLRYFDSNKDAYSKRFISVACISHVAAIGDQKFEVITNNRTFAFRAESDVERKEWMQALQQAMA PDPK1_RAT Others 1 " FUNCTION: Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, p70S6K and p90S6K/RSK. May play a general role in signaling processes and in development (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). Membrane-associated after cell stimulation leading to its translocation. Tyrosine phosphorylation seems to occur only at the plasma membrane. KMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQQYQSS PDPK1_HUMAN Human 1 " FUNCTION: Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, p70S6K and p90S6K/RSK. May play a general role in signaling processes and in development (By similarity). Isoform 3 is catalytically inactive." SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Membrane-associated after cell stimulation leading to its translocation. Tyrosine phosphorylation seems to occur only at the plasma membrane. KMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSH PDPK1_MOUSE Mouse 1 " FUNCTION: Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, p70S6K and p90S6K/RSK. May play a general role in signaling processes and in development. Could also play a role in sex differentiation processes." SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Membrane-associated after cell stimulation leading to its translocation. Tyrosine phosphorylation seems to occur only at the plasma membrane. KMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQQYQSN LNAKKGWLMKQDNRTCEWSKHWFTLSGAALFYYRDPLCEERGVLDGVLDVNSLTSVIPEPAASKQHAFQLTTWDKQRLVLASLSPSSRNSWLAVLRSAAG BTK_CHICK Others 1 FUNCTION: Plays a crucial role in B-cell ontogeny (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). SIILESIFLKRSQQKKKTSPLNFKKRLFLLTESKLSYYEYDFERGRRGSKKGSVDIEKITCVETVVPENNPPPERQVPKKGEDYNMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKSVIR BTK_MOUSE Mouse 1 FUNCTION: Plays a crucial role in B-cell ontogeny. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. AVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVIPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIR BTK_HUMAN Human 1 FUNCTION: Plays a crucial role in B-cell ontogeny. Transiently phosphorylates GTF2I on tyrosine residues in response to B-cell receptor crosslinking. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). AVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIR ITK_HUMAN Human 1 FUNCTION: Plays a role in T-cell proliferation and differentiation. " SUBCELLULAR LOCATION: Localizes to cell surface receptors in the plasma membrane after stimulation with respective receptors (TCR, CD28, CD2) in T-cells (By similarity)." FILLEEQLIKKSQQKRRTSPSNFKVRFFVLTKASLAYFEDRHGKKRTLKGSIELSRIKCVEIVKSDISIPCHYKYPFQVVHDNYLLYVFAPDRESRQRWVLALKEETR AVIKAGYCVKQGAVMKNWKRRYFQLDENTIGYFKSELEKEPLRVIPLKEVHKVQECKQSDIMMRDNLFEIVTTSRTFYVQADSPEEMHSWIKAVSGAIV DDEF1_BOVIN Others 1 " FUNCTION: Possesses phosphatidylinositol 4,5-biphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2 (By similarity). May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types." SUBCELLULAR LOCATION: Cytoplasmic; predominantly. Membrane- associated; partially (By similarity). GSEKKGYLLKKSDGIRKVWQRRKCSVKNGILTISHATSNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYVAWISVLTNSKE PLIKSGYCVKQGNVRKSWKRRFFALDDFTICYFKCEQDREPLRTIFLKDVLKTHECLVKSGDLLMRDNLFEIITSSRTFYVQADSPEDMHSWIKEIGAAVQ DDEF1_HUMAN Human 1 " FUNCTION: Possesses phosphatidylinositol 4,5-biphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types (By similarity)." SUBCELLULAR LOCATION: Cytoplasmic; predominantly. Membrane- associated; partially (By similarity). GSEKKGYLLKKSDGIRKVWQRRKCSVKNGILTISHATSNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYVAWISVLTNSKE PLIKSGYCVKQGNVRKSWKRRFFALDDFTICYFKCEQDREPLRTIFLKDVLKTHECLVKSGDLLMRDNLFEIITSSRTFYVQADSPEDMHSWIKEIGAAVQ PKHG4_HUMAN Human 1 FUNCTION: Possible role in intracellular signaling and cytoskeleton dynamics at the Golgi. NLKEQGQLVRQDEFVVRTGRHKSVRRIFLFEELLLFSKPRHGPTGVDTFAYKRSFKMADLGLTECCGNSNLRFEIWFRRRKARDTFVLQASSLAIKQAWTADISHLLW PLIKSGYCVKQGNVRKSWKRRFFALDDFTICYFKCEQDREPLRTIPLKDVLKTHECLVKSGDLLMRDNLFEIITTSRTFYVQADSPEDMHSWIEGIGAAVQ PHLPL_HUMAN Human 1 FUNCTION: Probable protein phosphatase (By similarity). SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (By similarity). May be membrane-associated (By similarity). RILLSGIYNVRKGKTQLHKWAERLVVLCGTCLIVSSVKDCQTGKMHILPLVGGKIEEVKRRQYSLAFSSAGAQAQTYHVSFETLAEYQRWQRQASKVVS PHLPL_MOUSE Mouse 1 FUNCTION: Probable protein phosphatase (By similarity). SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (By similarity). May be membrane-associated (By similarity). RILLSGIYNVRKGKTQLHKWAERLVVLCGTCLIVSSVKDCQTGKMHILPLVGGKIEEVKRRQHSLAFSSAGAQAQTYHVSFETLAEYQRWQRQASKVVS UN112_CAEEL Others 1 FUNCTION: Probable regulator of cell-extracellular matrix adhesion. Required during initial muscle assembly to form dense bodies and M-lines. SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Colocalizes with pat-3/beta-integrin in body wall muscles. Requires unc-52/perlecan and pat-3 to be localized to the muscle cell membrane. VPELADYLKYMKPKKLAAFKGFKRAFFSFRDLYLSYHQSSSDVNSAPLGHFSLKGCEVSQDVSVGQQKYHIKLLLPTAEGMIDFILKCDSEHQYARWMAACRLASR HAPIP_RAT Others 1 FUNCTION: Promotes the exchange of GDP by GTP. May act as part of a signal transduction system linking the catalytic domains of PAM in the lumen of the secretory pathway to cytosolic factors regulating the cytoskeleton and signal transduction pathways. SUBCELLULAR LOCATION: Cytoplasm. NLDVQGELILQDAFQVWDPKSLIRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHVEGDPCKFALWSGRTPSSDNKTVLKASNIETKQEWIKNIREVIQ VIIKQGCLLKQGHRRKNWKVRKFILREDPAYLHYYDPAGGEDPLGAVHLRGCVVTSVESSHDVKKSDEENLFEIITADEVHYYLQAATSKERTEWIKAIQVASR ROCK1_HUMAN Human 1 " FUNCTION: Protein kinase that phosphorylates a large number of important signaling proteins, and thereby regulates the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Necessary for apoptotic membrane blebbing. Plays a role in smooth muscle contraction. Required for centromere positioning and centromere- dependent exit from mitosis (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Associated with the mother centriole and an intercentriolar linker (By similarity). Golgi apparatus; Golgi membrane; peripheral membrane protein. A small proportion is associated with Golgi membranes. ESRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDVEMEPVQQAEKTNFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIP ROCK1_MOUSE Mouse 1 " FUNCTION: Protein kinase that phosphorylates a large number of important signaling proteins, and thereby regulates the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Necessary for apoptotic membrane blebbing. Plays a role in smooth muscle contraction. Required for centromere positioning and centromere- dependent exit from mitosis (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Associated with the mother centriole and an intercentriolar linker. Golgi apparatus; Golgi membrane; peripheral membrane protein (By similarity). A small proportion is associated with Golgi membranes (By similarity). ESRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSSPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDIEVEPVQQGEKTNFQNHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLISPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIP ROCK1_PANTR Others 1 " FUNCTION: Protein kinase that phosphorylates a large number of important signaling proteins, and thereby regulates the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Necessary for apoptotic membrane blebbing. Plays a role in smooth muscle contraction. Required for centromere positioning and centromere- dependent exit from mitosis (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Associated with the mother centriole and an intercentriolar linker. Golgi apparatus; Golgi membrane; peripheral membrane protein (By similarity). A small proportion is associated with Golgi membranes (By similarity). ESRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDVEMEPVQQAEKTNFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIP ROCK1_RABIT Others 1 " FUNCTION: Protein kinase that phosphorylates a large number of important signaling proteins, and thereby regulates the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Necessary for apoptotic membrane blebbing. Plays a role in smooth muscle contraction. Required for centromere positioning and centromere- dependent exit from mitosis (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Associated with the mother centriole and an intercentriolar linker. Golgi apparatus; Golgi membrane; peripheral membrane protein (By similarity). A small proportion is associated with Golgi membranes (By similarity). ESRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDVEVEPVQQAEKTNFQNHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLISPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIP ROCK1_RAT Others 1 " FUNCTION: Protein kinase that phosphorylates a large number of important signaling proteins, and thereby regulates the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Necessary for apoptotic membrane blebbing. Plays a role in smooth muscle contraction. Required for centromere positioning and centromere- dependent exit from mitosis (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Associated with the mother centriole and an intercentriolar linker. Golgi apparatus; Golgi membrane; peripheral membrane protein (By similarity). A small proportion is associated with Golgi membranes (By similarity). SSRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKMLFYNDEQDKEQSSPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDIEVEPVQQGEKTNFQNHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKSHRDHLDKKEDLIPPCKVSYDVTSARDMLLLACPQDEQKKWVTHLVKKIP ROCK2_HUMAN Human 1 " FUNCTION: Protein kinase that phosphorylates a large number of important signaling proteins, and thereby regulates the assembly of the actin cytoskeleton. Promotes formation of stress fibers and of focal adhesion complexes. Plays a role in smooth muscle contraction (By similarity)." " SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane; peripheral membrane protein (By similarity). Cytoplasmic, and associated with actin microfilaments and the plasma membrane (By similarity)." ESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISTAKNLLLLANSTEEQQKWVSRLVKKIP ROCK2_BOVIN Others 1 " FUNCTION: Protein kinase that phosphorylates a large number of important signaling proteins, and thereby regulates the assembly of the actin cytoskeleton. Promotes formation of stress fibers and of focal adhesion complexes. Plays a role in smooth muscle contraction (By similarity)." " SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; peripheral membrane protein. Cytoplasmic, and associated with actin microfilaments and the plasma membrane." ESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIP ROCK2_MOUSE Mouse 1 " FUNCTION: Protein kinase that phosphorylates a large number of important signaling proteins, and thereby regulates the assembly of the actin cytoskeleton. Promotes formation of stress fibers and of focal adhesion complexes. Plays a role in smooth muscle contraction." " SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane; peripheral membrane protein (By similarity). Cytoplasmic, and associated with actin microfilaments and the plasma membrane (By similarity)." ESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEPEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIP ROCK2_RAT Others 1 " FUNCTION: Protein kinase that phosphorylates a large number of important signaling proteins, and thereby regulates the assembly of the actin cytoskeleton. Promotes formation of stress fibers and of focal adhesion complexes. Plays a role in smooth muscle contraction." " SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; peripheral membrane protein. Cytoplasmic, and associated with actin microfilaments and the plasma membrane." ESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEPEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECSRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIP PHLPP_RAT Others 1 " FUNCTION: Protein phosphatase that specifically mediates dephosphorylation of Ser-473 of AKT1, a protein that regulate the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of Ser- 473 of AKT1 triggers apoptosis and suppression of tumor growth (By similarity). May act as a negative regulator of K-Ras signaling in the membrane rafts." SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (Potential). May be membrane-associated. RIQLSGMYNVRKGKMQLPVNRWTRRQVILCGTCLIVSSVKDSSSGKMHVLPLIGGKVEEVKKHQHCLAFSSSGPQSQTYYICFDTFTEYLRWLRQVSKVAS PHLPP_MOUSE Mouse 1 " FUNCTION: Protein phosphatase that specifically mediates dephosphorylation of Ser-473 of AKT1, a protein that regulate the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of Ser- 473 of AKT1 triggers apoptosis and suppression of tumor growth. May act as a negative regulator of K-Ras signaling in the membrane rafts (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (By similarity). May be membrane-associated (By similarity). RIQLSGMYNVRKGKMQLPVNRWTRRQVILCGTCLIVSSVKDSVSGKMHVLPLIGGKVEEVKKHQHCLAFSSSGPQSQTYYICFDTFTEYLRWLRQVSKVAS PHLPP_HUMAN Human 1 " FUNCTION: Protein phosphatase that specifically mediates dephosphorylation of Ser-473 of AKT1, a protein that regulate the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of Ser- 473 of AKT1 triggers apoptosis and suppression of tumor growth. May act as a negative regulator of K-Ras signaling in the membrane rafts." SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (By similarity). May be membrane-associated (By similarity). RIQLSGMYNVRKGKMQLPVNRWTRRQVILCGTCLIVSSVKDSLTGKMHVLPLIGGKVEEVKKHQHCLAFSSSGPQSQTYYICFDTFTEYLRWLRQVSKVAS APSA_EMENI Others 1 FUNCTION: Required for nuclear positioning and completion of asexual development. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. QTMIGEFLWKYTRRAVSGEISNTRHRRYFWVHPYTRTLYWSEHDPQSAGKSEGRTKSVSIEAVRVVADDNPYPPGLHCKSLEVVSPGRRIRFTATTSQRHETWFNALSYLLV DP13A_MOUSE Mouse 1 FUNCTION: Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction (By similarity). SUBCELLULAR LOCATION: Endosome; early endosome; early endosomal membrane; peripheral membrane protein (By similarity). Nucleus (By similarity). Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF (By similarity). LTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISK DP13A_HUMAN Human 1 FUNCTION: Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction. SUBCELLULAR LOCATION: Endosome; early endosome; early endosomal membrane; peripheral membrane protein. Nucleus. Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF. LTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISK DP13B_MOUSE Mouse 1 FUNCTION: Required for the regulation of cell proliferation in response to extracellular signals mediated by an early endosomal compartment. Links Rab5 to nuclear signal transduction (By similarity). SUBCELLULAR LOCATION: Endosome; early endosome; early endosomal membrane; peripheral membrane protein (By similarity). Nucleus (By similarity). Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF (By similarity). LIQKTGYLNLRNKTGLVTTTWERLYFFTQGGNLMCQPRGAVAGGLIQDLDNCSVMAVDCEDRRYCFQISTPSGKPGIILQAESRKEYEEWICAVNNISR DP13B_HUMAN Human 1 FUNCTION: Required for the regulation of cell proliferation in response to extracellular signals mediated by an early endosomal compartment. Links Rab5 to nuclear signal transduction. SUBCELLULAR LOCATION: Endosome; early endosome; early endosomal membrane; peripheral membrane protein. Nucleus. Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF. LIQKAGYLNLRNKTGLVTTTWERLYFFTQGGNLMCQPRGAVAGGLIQDLDNCSVMAVDCEDRRYCFQITTPNGKSGIILQAESRKENEEWICAINNISR PHLA1_RAT Others 1 FUNCTION: Seems to be involved in regulation of apoptosis. May be involved in detachment-mediated programmed cell death. May mediate apoptosis during neuronal development. May be involved in regulation of anti-apoptotic effects of IGF1. May be involved in translational regulation. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Colocalizes with intracellular vesicles. Nucleus; nucleolus (By similarity). SGCKALKEGVLEKRSDGLLQLWKKKCCILTEEGLLL DIKQIGWLTEQLPSGGTAPTLALLTEKELLLYGGLPQTREALSRPARTAPLIATRLVHSGPSKGSVPYDAELSFALRTGTRHGVDTHLFSVESPQELAAWTRQLVDGCH PHLA1_HUMAN Human 1 FUNCTION: Seems to be involved in regulation of apoptosis. May be involved in detachment-mediated programmed cell death. May mediate apoptosis during neuronal development. May be involved in regulation of anti-apoptotic effects of IGF1. May be involved in translational regulation. SUBCELLULAR LOCATION: Cytoplasm. Colocalizes with intracellular vesicles. Nucleus; nucleolus. ALKEGVLEKRSDGLLQLWKKKCCILTEEGLLLIPPKQLQHQQQQQQQQQQQQQQPGQGPAEPSQPSGPAVASLEPPVKLKELHFSNMKTVDCVERKGKYMYFTVVMAEGKEIDFRCPQDQGWNAEITLQMVQY EIRHLGWLAEKVPGESKKQWKPALVVLTEKDLLIYDSMPRRKEAWFSPVHTYPLLATRLVHSGPGKGSPQAGVDLSFATRTGTRQGIETHLFRAETSRDLSHWTRSIVQGCH PHLA1_MOUSE Mouse 1 FUNCTION: Seems to be involved in regulation of apoptosis. May be involved in detachment-mediated programmed cell death. May mediate apoptosis during neuronal development. May be involved in regulation of anti-apoptotic effects of IGF1. Required for TCR- induced apoptosis and expression of TNFRSF6/FAS in a T-cell hybridoma cell line. May be involved in translational regulation. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Colocalizes with intracellular vesicles. Nucleus; nucleolus (By similarity). ALKEGVLEKRSDGLLQLWKKKCCILTEEGLLLIPPKQLQQQQQQQQPGQGTAEPSQPSGPTVASLEPPVKLKELHFSNMKTVDCVERKGKYMYFTVVMTEGKEIDFRCPQDQGWNAEITLQMVQY EIRHLGWLAEKVPGESEKQWKPALVVLTEKDLLIYDSMPRRKEAWFSPVHSYPLLATRLVHSGPGKGSPQAGMDLSFATRTGTKQGIETHLFRAEISRDLSHWTRSIVQGCH PHLB2_HUMAN Human 1 FUNCTION: Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane (By similarity). " SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Translocates to the plasma membrane at high levels of PtdIns(3,4,5)P3. At low levels of PtdIns(3,4,5)P3 is translocated to vesicular compartments." EKTCRGFLIKMGGKIKTWKKRWFVFDRNKRTFSYYADKHETKLKGVIYFQAIEEVYYDHLKNANKSPNPLLTFSVKTHDRIYYMVAPSPEAMRIWMDVIVTGAE EVKHIAWLAEQAKLDGGRQQWRPVLMAVTEKDLLLYDCMPWTRDAWASPCHSYPLVATRLVHSGSGCRSPSLGSDLTFATRTGSRQGIEMHLFRVETHRDLSSWTRILVQGCH PHLB2_MOUSE Mouse 1 FUNCTION: Seems to be involved in the assembly of the postsynaptic apparatus. May play a role in acetyl-choline receptor (AChR) aggregation in the postsynaptic membrane. " SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). Translocates to the plasma membrane at high levels of PtdIns(3,4,5)P3. At low levels of PtdIns(3,4,5)P3 is translocated to vesicular compartments (By similarity)." EKTCRGYLIKMGGKIKTWKKRWFVFDRNKRTFSYYADKHEAKLKGVIYFQAIEEVYYDHLKNANKSPNPLLTFSVKTHDRIYYMVAPSPEAMRIWMDVIVTGAE EVKHIAWLAEQAKLDGGRQQWRPVLMAVTEKDLLLYDCMPWTRDAWASPCHSYPLVATRLVHSGSGCRSPSLGSDLTFATRTGSRQGIEMHLFRVETHRDLSTWTRILVQGCH ARHG1_RAT Others 1 " FUNCTION: Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12 (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By similarity). Translocated to the membrane by activated GNA13 or LPA stimulation (By similarity). KLVHEGPLTWRLTKDKAVEVHVLLLDDLLLLLQRQDEGCCSSHTSRTLTPTPDGKTMLRPVLRLTSAMTREVATDHKAFYVIFTWDQEAQIYELVAQTSSERKSWCALITETAG ARHG1_HUMAN Human 1 " FUNCTION: Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12." SUBCELLULAR LOCATION: Cytoplasm. Membrane. Translocated to the membrane by activated GNA13 or LPA stimulation. KLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDGKTMLRPVLRLTSAMTREVATDHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITETAG ARHG1_MOUSE Mouse 1 " FUNCTION: Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12. Isoform 3 and isoform 4 do not homooligomerize and show an enhanced RhoGEF activity." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By similarity). Translocated to the membrane by activated GNA13 or LPA stimulation (By similarity). KLVHEGPLTWRVTKDKAIEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDGKTMLRPVLRLTSAMTREVATDHKAFYVIFTWDQEAQIYELVAQTSSERKNWCNLITETAG AKT1_DROME Others 1 " FUNCTION: Serine/threonine kinase involved in various developmental processes. During early embryogenesis, acts as a survival protein. During mid-embryogenesis, phosphorylates and activates trh, a transcription factor required for tracheal cell fate determination. Also regulates tracheal cell migration. Later in development, acts downstream of PI3K and Pk61C/PDK1 in the insulin receptor transduction pathway which regulates cell growth and organ size, by phosphorylating and antagonizing FOXO transcription factor. Controls follicle cell size during oogenesis. May also stimulate cell growth by phosphorylating Gig/Tsc2 and inactivating the Tsc complex." SUBCELLULAR LOCATION: Cytoplasm; cytosol. Cell membrane. Recruited to plasma membrane upon activation. QVVKEGWLMKRGEHIKNWRQRYFVLHSDGRLMGYRSKPADSASTPSDFLLNNFTVRGCQIMTVDRPKPFTFIIRGLQWTTVIERTFAVESELERQQWTEAIRNVSS ARHG2_MOUSE Mouse 1 " FUNCTION: Stimulates guanine nucleotide exchange of Rac and Rho but is inactive toward CDC42, TC10, or Ras. Binds to Rac and Rho proteins in both the GDP- and guanosine 5'-3-O-(thio)triphosphate- bound states without detectable affinity for CDC42 or Ras. May have a direct role in activation of Rac and/or Rho and in bringing the activated GTPase to specific target sites such as microtubules (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Colocalizes with microtubules through the C-terminal coiled-coil domain (By similarity). GRFKDVLLLLMTDVLVFLQEKDQKYIFTSLDKPSVVSLQNLIVRDIANQAKGMFLISSGPPEMYEVHAASRDDRTTWIRVIQQSVRL ARHG2_HUMAN Human 1 " FUNCTION: Stimulates guanine nucleotide exchange of Rac and Rho but is inactive toward CDC42, TC10, or Ras. Binds to Rac and Rho proteins in both the GDP- and guanosine 5'-3-O-(thio)triphosphate- bound states without detectable affinity for CDC42 or Ras. May have a direct role in activation of Rac and/or Rho and in bringing the activated GTPase to specific target sites such as microtubules." SUBCELLULAR LOCATION: Cytoplasm. Colocalizes with microtubules through the C-terminal coiled-coil domain. GRFKDVLVLLMTDVLVFLQEKDQKYIFPTLDKPSVVSLQNLIVRDIANQEKGMFLISAAPPEMYEVHTASRDDRSTWIRVIQQSVRT STAP2_MOUSE Mouse 1 FUNCTION: Substrate of protein kinase PTK6 (By similarity). May play a regulatory role in the acute-phase response in systemic inflammation and may modulate STAT3 activity. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. The translocation to the membranes occurs in response to EGF when the protein is overexpressed in fibroblastic cells. HYYESFLEKKGPCDQDYRKFWAGLQGLAICFYNSNRDLQPLEKLDLRLFSKLRDEALLGSSRDTAYHFSLVLRDQEVKFKVESLESCEMWKGFILTVVELR KIVAQGKLLLQDTFLVTDQDAGLLPRCRERRIFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEENVENDPCKFALTSRTGDVVETFILHSSSPSVRQTWIHEINQILE STAP2_HUMAN Human 1 FUNCTION: Substrate of protein kinase PTK6. May play a regulatory role in the acute-phase response in systemic inflammation and may modulate STAT3 activity. SUBCELLULAR LOCATION: Cytoplasm. PSHYYESFLEKKGPCDRDYKKFWAGLQGLTIYFYNSNRDFQHVEKLNLGAFEKLTDEIPWGSSRDPGTHFSLILRNQEIKFKVETLECREMWKGFILTVVELRVPTDLTLLPG MRIP_RAT Others 1 FUNCTION: Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F- actin-binding region leads to disassembly of stress fibers in neuronal cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Colocalizes with F-actin (By similarity). KPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEMLMVYPR MRIP_HUMAN Human 1 FUNCTION: Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F- actin-binding region leads to disassembly of stress fibers in neuronal cells. SUBCELLULAR LOCATION: Cytoplasm. Colocalizes with F-actin. KPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEGRTGQKFSLCILTPEKEHFIRAETKEIVSGWLEMLMVYPR MRIP_MOUSE Mouse 1 FUNCTION: Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F- actin-binding region leads to disassembly of stress fibers in neuronal cells. SUBCELLULAR LOCATION: Cytoplasm. Colocalizes with F-actin. KPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEMLMVYPR PLCL4_HUMAN Human 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (By similarity)." GAMQEGMQMVKLRGGSKGLVRFYYLDEHRSCIRWRPSRKNEKAKISIDSIQEVSEGRQSEVFQRYPDGSFDPNCCFSIYHGSHRESLDLVSTSSEVARTWVTGLRYLMA PLCD1_BOVIN Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." PESQLFSIEDIQEVRMGHRTEGLEKFARDVPENRCFSIVFKDQRNTLDLIAPSPADAQHWVQGLGKIIH PLCD1_HUMAN Human 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." ALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMRTPESQLFSIEDIQEVRMGHRTEGLEKFARDVPEDRCFSIVFKDQRNTLDLIAPSPADAQHWVLGLHKIIH PLCD1_MOUSE Mouse 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." ALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMRSPESQLFSIEDIQEVRMGHRTEGLEKFARDIPEDRCFSIVFKDQRNTLDLIAPSPADVQHWVQGLRKIID PLCD1_RAT Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." ALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMRSPESQLFSIEDIQEVRMGHRTEGLEKFARDIPEDRCFSIVFKDQRNTLDLIAPSPADAQHWVQGLRKIIH PLCG1_BOVIN Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." RSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIRGLTWLME PLCG1_MOUSE Mouse 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." RSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGSIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLME PLCG1_RAT Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." RSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGSIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLME PLCG2_HUMAN Human 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling." RALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADKIEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAVNWLSGLKILHQ PLCG2_RAT Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling." RALELGTVMTVFSARKSTPERRTVQMIMETRQVAWSKTADKIEGFLDIMEIKEIRPGKNSKDFERAKAVRHKADCCFTIFYGTQFVLSTLSLATDSKEDAVKWLSGLKILHQ KPCD1_HUMAN Human 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme." TVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILSLEPVKTSALIPNGANPHCFEITTANVVYYVGENVVNPSSPSPNNSVLTSGVGADVARMWEIAIQHALM KPCD1_MOUSE Mouse 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme." TVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILCLEPAKPSALTPVGATPHCFEITTANVVYYVGENVVNPSSSPPNNSVLPSGIGPDVARMWEVAIQHALM KPCD3_MOUSE Mouse 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters (By similarity)." TVVKEGWMVHYTSRDNLRKRHYWRLDSKCLTLFQNESGSKYYKEIPLSEILRVSSPQDFTSISQGSNPHCFEIITDTVVYFVGENNGSSSHNPVLAATGVGLDVAQSWEKAIRQALM KPCD3_HUMAN Human 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." TMVKEGWMVHYTSRDNLRKRHYWRLDSKCLTLFQNESGSKYYKEIPLSEILRISSPRDFTNISQGSNPHCFEIITDTMVYFVGENNGDSSHNPVLAATGVGLDVAQSWEKAIRQALM OSH2_YEAST Yeast 1 " SUBCELLULAR LOCATION: Cell membrane; peripheral membrane protein. Cell periphery, enriched in small buds of G1 phase cells and near the bud-neck region of S phase cells." PPTYKGFLKKWTNFAHGYKLRWFILSGDGNLSYYKDQSHVDRPRGTLKVSTCRLHIDSSEKLNFELLGGITGTTRWRLKGNHPIETTRWVNAIQSAIR MTMRD_XENLA Others 1 SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane peripheral membrane protein (By similarity). Associated with membranes (By similarity). NRSYEGILYKRGALLKGWKPRWFVLDITKHQLRYYDSGEDTSCKGYIDLADVETVVPAAPTIGAPKHANEKAFFDVKTSKRVYNFCAQDAQSAQLWMDKIQNCIS PKHB2_HUMAN Human 1 SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (Potential). AFVKSGWLLRQSTILKRWKKNWFDLWSDGHLIYYDDQTRQNIEDKVHMPMDCINIRTGQECRDTQPPDGKSKDCMLQIVCRDGKTISLCAESTDDCLAWKFTLQDSRT PKHB2_MOUSE Mouse 1 SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (Potential). AFVKSGWLLRQSTILKRWKKNWFDLWSDGHLIYYDDQTRQSIEDKVHMPVDCINIRTGHECRDIQPPDGKPRDCLLQIVCRDGKTISLCAESTDDCLAWKFTLQDSRT VILD_DICDI Others 1 SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. Associated with membranes and the cytoskeleton. PFITEGIVKQEIEGWLFNSYENRYLKIVKDKIYCFLNEDSAPAIWDSPVLNIKYVDIYDEDENTSGEEWSLRFNIILLNRKELRMECSTVKQRDAWCQAIKAYRE PKHB1_HUMAN Human 1 " SUBCELLULAR LOCATION: Membrane-associated. Highly expressed in the outer segments of photoreceptor cells, both in rods and cones." ALVRGGWLWRQSSILRRWKRNWFALWLDGTLGYYHDETAQDEEDRVLIHFNVRDIKIGPECHDVQPPEGRSRDGLLTVNLREGGRLHLCAETKDDALAWKTALLEANS PKHB1_MOUSE Mouse 1 " SUBCELLULAR LOCATION: Membrane-associated. Highly expressed in the outer segments of photoreceptor cells, both in rods and cones." ALVRGGWLWRQSSILRRWKRNWFALWLDGTLGYYHDETAQDEEDRVVIHFNVRDIKVGQECQDVQPPEGRSRDGLLTVNLREGSRLHLCAETRDDAIAWKTALMEANS PKHB1_RAT Others 1 " SUBCELLULAR LOCATION: Membrane-associated. Highly expressed in the outer segments of photoreceptor cells, both in rods and cones. Associated with post-Golgi vesicles." ALVRGGWLWRQSSILRRWKRNWFALWLDGTLGYYHDETAQDEEDRVVIHFNVRDIKVGQECQDVQPPEGRSRDGLLTVNLREGSRLHLCAETRDDAIAWKTALMEANS FGD4_MOUSE Mouse 1 " FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Activates MAPK8 (By similarity). Plays a role in regulating the actin cytoskeleton and cell shape. Promotes the formation of lamellipodia." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Concentrated in filopodia and poorly detected at lamellipodia. Binds along the sides of actin fibers (By similarity). ELIKEGQILKLAARNTSAQERYLFLFNNMLLYCVPRFSLVGSKFTVRTRVGIDGMKIVETHNEEYPHTFQISGKERTLELQASSEQDKEEWIKALQESID FGD1_HUMAN Human 1 " FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Associated with membrane ruffles and lamellipodia (By similarity). ELIKEGHILKLSAKNGTTQDRYLILFNDRLLYCVPRLRLLGQKFSVRARIDVDGMELKESSNLNLPRTFLVSGKQRSLELQARTEEEKKDWVQAINSTLL FGD1_MOUSE Mouse 1 " FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape." SUBCELLULAR LOCATION: Cytoplasm. Associated with membrane ruffles and lamellipodia. ELIKEGHILKLSAKNGTTQDRYLILFNDRLLYCVPRLRLLGQKFTVRARIDVDGMELKESSNLNMPRTFLVSGKQRSLELQARTEEEKKDWVQAINSTLL FGD4_HUMAN Human 1 " FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. Activates MAPK8 (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Concentrated in filopodia and poorly detected at lamellipodia. Binds along the sides of actin fibers (By similarity). ELIKEGQILKLAARNTSAQERYLFLFNNMLLYCVPKFSLVGSKFTVRTRVGIDGMKIVETQNEEYPHTFQVSGKERTLELQASSAQDKEEWIKALQETID FGD4_RAT Others 1 " FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. Activates MAPK8." SUBCELLULAR LOCATION: Cytoplasm. Concentrated in filopodia and poorly detected at lamellipodia. Binds along the sides of actin fibers. ELIKEGQILKLAARNTSAQERYLFLFNNMLLYCVPRFSLVGSKFTVRTRVGIDGMKIVETHNEEYPHTFQVSGKERTLELQASSEQDKEEWIKALQESID SPTB2_HUMAN Human 1 " FUNCTION: Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane." SAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKTAASGIPYHSEVPVSLKEAVCEVALDYKKKKHVFKLRLNDGNEYLFQAKDDEEMNTWIQAISSAIS SPTB2_MOUSE Mouse 1 " FUNCTION: Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane." AAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGIPYHSEVPVSLKEAICEVALDYKKKKHVFKLRLSDGNEYLFQAKDDEEMNTWIQAISSAIS PLDP1_ARATH Mouse 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Phosphatidylcholine-selective. DDSNRCCGCCWFCCCNDNWQKVWGVLKPGFLALLEDPFDAKLLDIIVFDVLPVSNGNDGVDISLAVELKDHNPLRHAFKVTSGNRSIRIRAKNSAKVKDWVASINDAAL PLDP2_ARATH Mouse 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Phosphatidylcholine-selective. SKMKEGYVTVKHLRDVPGSDGVRCCLPTHCLGFFGTSWTKVWAVLKPGFLALLEDPFSGKLLDIMVFDTLGLQGTKESSEQPRLAEQVKEHNPLRFGFKVTSGDRTVRLRTTSSRKVKEWVKAVDEAGC LNK_HUMAN Human 1 " FUNCTION: Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB-2 and phosphatidylinositol 3-kinase (By similarity)." EALKEAVLRYSLADEASMDSGARWQRGRLALRRAPGPDGPDRVLELFDPPKSSRPKLQAACSSIQEVRWCTRLEMPDNLYTFVLKVKDRTDIIFEVGDEQQLNSWMAELSECTG LNK_MOUSE Mouse 1 " FUNCTION: Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB-2 and phosphatidylinositol 3-kinase (By similarity)." EALKEVVLRYSLADEAAMDSGARWQRGRLVLRSPGPGHSHFLQLFDPPKSSKPKLQEACSSIREVRPCTRLEMPDNLYTFVLKVQDQTDIIFEVGDEQQLNSWLAELRASTG KIF1B_RAT Others 1 FUNCTION: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility (By similarity). FUNCTION: Isoform 1 mediates the transport of synaptic vesicles in neuronal cells. SUBCELLULAR LOCATION: Predominantly found on the vesicle- and tubule-like structures within the cytoplasm (By similarity). Isoform 2 is involved in the translocation of lysosomes from perinuclear regions to the cell periphery. VVSKKGYLHFKEPLSSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMLKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLA KIF1B_HUMAN Human 1 FUNCTION: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility. SUBCELLULAR LOCATION: Predominantly found on the vesicle- and tubule-like structures within the cytoplasm (By similarity). VSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMVKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLA KIF1B_MOUSE Mouse 1 FUNCTION: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility. SUBCELLULAR LOCATION: Predominantly found on the vesicle- and tubule-like structures within the cytoplasm. VSKKGYLHFKEPLSSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMVKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLA MYO10_BOVIN Others 1 " FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Plays a role in regions of dynamic actin." EALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQAKLMYFENDSEEKLKGTVEVRAAKEIIDNTSKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHA MYO10_HUMAN Human 1 " FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Plays a role in regions of dynamic actin." EALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRTAKEIIDNTTKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHA PKHC1_MOUSE Mouse 1 FUNCTION: Participates in the connection between ECM adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits migfilin (FBLP1) protein to cell-ECM focal adhesion sites (By similarity). SUBCELLULAR LOCATION: Cytoplasmic; peripheral. Within actin stress fibers at cell-ECM focal adhesion sites (By similarity). KVFKPKKLTLKGYKQYWCTFKDTSISCYKSREESSGTPAHQLNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASK PKHC1_HUMAN Human 1 FUNCTION: Participates in the connection between ECM adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits migfilin (FBLP1) protein to cell-ECM focal adhesion sites. SUBCELLULAR LOCATION: Cytoplasmic; peripheral. Within actin stress fibers at cell-ECM focal adhesion sites. KVFKPKKLTLKGYKQYWCTFKDTSISCYKSKEESSGTPAHQMNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASK URP2_HUMAN Human 1 FUNCTION: Probably involved in cell adhesion (By similarity). SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane-associated in chronic lymphocytic leukemia (CLL) cells. DHLRIFRIPRRPRKLTLKGYRQHWVVFKETTLSYYKSQDEAPGDPIQQLNLKGCEVVPDVNVSGQKFCIKLLVPSPEGMSEIYLRCQDEQQYARWMAGCRLASK FGD3_HUMAN Human 1 " FUNCTION: Promotes the formation of filopodia. May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). ELIKEGQIQKLSAKNGTPQDRHLFLFNSMILYCVPKLRLMGQKFSVREKMDISGLQVQDIVKPNTAHTFIITGRKRSLELQTRTEEEKKEWIQIIQATIE FGD3_PONPY Others 1 " FUNCTION: Promotes the formation of filopodia. May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). ELIKEGQIQKLSAKNGTPQDRHLFLFNSMILYCVPKLRLMGQKFSVREKMDISGLQVQDIVKPNTAHTFIITGRKRSLELQTRTEEEKKEWIQIIQATIE FGD3_MOUSE Mouse 1 " FUNCTION: Promotes the formation of filopodia. May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape." SUBCELLULAR LOCATION: Cytoplasm (Probable). ELIKEGSIQKLSAKNGTTQDRHLFLFNNVMLYCVPKLRLMGQKLSVREKMDISDLQVQDIVKPNAACTFIITGRKRSLELQTRTEEEKKEWIQVIQATVE ANLN_MOUSE Mouse 1 FUNCTION: Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression (By similarity). " SUBCELLULAR LOCATION: Nucleus (By similarity). Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. This pattern persists until telophase, when the protein becomes concentrated in the midbody." AVEEKGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDERRKNPIGRINLANCISHQIEPANREFCARRNTLELITVRPQREDDRETLVSQCRDTLCVTKNWLSADTKEERDLWMQKLNQVIV ANLN_DROME Others 1 " FUNCTION: Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression and proper formation of the midbody. Required during cellularization of syncytial embryos for the proper formation and function of the furrow canals, the stable inward folds of the plasma membrane which separate the peripheral nuclei. Also required for the formation of the pole cells, the progenitors of the adult germline which are formed by cytokinesis of the cytoplasmic buds at the posterior pole of the syncytial embryo. Essential for embryonic viability." " SUBCELLULAR LOCATION: Nucleus. Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. This pattern persists until telophase, when the protein becomes concentrated in the midbody. Accumulates in the nucleus of newly divided cells in a diffuse staining pattern, thereby restarting the cycle." SVEYKGFLTMFEDISGFGAWHRRWCYLNGSVINYWKYPDDEKRKTPMGSIDLNSCTSQKVTTAPRDICARLNTMLLECERPALETDQESLIIVPNGRTTTVRHLLSADTKEEREEWCAYLNKALT ANLN_XENLA Others 1 FUNCTION: Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. SUBCELLULAR LOCATION: Nucleus. Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. SVEDKGFLTMFEDVSGFGAWHRRWCVLSGYCISYWTYPDDEKRKKPIGRINLANCTSRKIEPANREFCARPNTFELITVRPQREGDRETLVSQCRDTLCVTKNWLSADTKEERNLWMQKLNQFLV ANLN_HUMAN Human 1 FUNCTION: Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. " SUBCELLULAR LOCATION: Nucleus. Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. This pattern persists until telophase, when the protein becomes concentrated in the midbody." SVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVRPQREDDRETLVSQCRDTLCVTKNWLSADTKEERDLWMQKLNQVLV FARP2_HUMAN Human 1 FUNCTION: Rho-guanine nucleotide exchange factor that activates RAC1. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton (By similarity). EFIREGCLHKLTKKGLQQRMFFLFSDMLLYTSKGVAGTSHFRIRGLLPLQGMLVEESDNEWSVPHCFTIYAAQKTIVVAASTRLEKEKWMLDLNSAIQ DIKQIGWLTEQLPSGGTAPTLALLTEKELLLYLSLPETREALSRPARTAPLIATRLVHSGPSKGSVPYDAELSFALRTGTRHGVDTHLFSVESPQELAAWTRQLVDGCH SPTCB_DROME Others 1 FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Interacts with calmodulin in a calcium-dependent manner. GEGHEGYVTRKHEWDSTTKKASNRSWDKVYMAAKAGRISFYKDQKGYKSNPELTFRGEPSYDLQNAAIEIASDYTKKKHVLRVKLANGALFLLQAHDDTEMSQWVTSLKAQSD IRS1_DROME Others 0 " FUNCTION: Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity). May mediate the control of various cellular processes by insulin-like peptides. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains. Involved in control of cell proliferation, cell size, and body and organ growth throughout development. Also has a role in a signaling pathway controlling the physiological response required to endure periods of low nutrient conditions." GMALSGYLKKLKTMKKKFFVLYEETSTSAARLEYYDTEKKFLQRAEPKRVIYLKNCFNINRRLDTKHRFVIVLSSRDGGFGIVLENENDLRKWLDKLLVLQR BMX_MOUSE Mouse 0 FUNCTION: Activity is required for interleukin 6 (IL-6) induced differentiation. May play a role in the growth and differentiation of hematopoietic cells. May be involved in signal transduction in endocardial and arterial endothelial cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm (Probable). KSILEELLLKKSQQKKKMSPNNYKERLFVLTKTSLSYYEYDKMKRGSRKGSIEIKKIRCVEKVNLEEQTPVERQYPFQIVYKDGLLYVYASNEESRCQWLKALQKEIR BMX_HUMAN Human 0 FUNCTION: Activity is required for interleukin 6 (IL-6) induced differentiation. May play a role in the growth and differentiation of hematopoietic cells. May be involved in signal transduction in endocardial and arterial endothelial cells. SUBCELLULAR LOCATION: Cytoplasm (Probable). KSILEELLLKRSQQKKKMSPNNYKERLFVLTKTNLSYYEYDKMKRGSRKGSIEIKKIRCVEKVNLEEQTPVERQYPFQIVYKDGLLYVYASNEESRSQWLKALQKEIR ARHG6_CHICK Others 0 FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) (By similarity). DIKTMGNIIYMSQVMVQSGGSEEKEERYFLLFSNVLLMLSASPRMSGFIYQGRLPLTGMTLTKLEDAEGNEHMFEIAGNMMERITVSCSTSQDLHEWLEHLQRLTK ARHG6_MOUSE Mouse 0 FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) (By similarity). DIKTLGNVIFMSQVVMQHGACEEKEERYFLLFSSVLIMLSASPRMSGFMYQGKIPIAGMVVNRLDEIEGSDCMFEITGSTVERIVVHCNNNQDFQEWMEQLNRLTK ARHG6_RAT Others 0 FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) (By similarity). DIKTLGNVIFMSQVVMQHGACEEKEERYFLLFSSVLIMLSASPRMSGFMYQGKVPIAGMVVTRLDEIEGNDCTFEITGSTVERIVVHCNNNQDFQEWMEQLNRLTK ARHG7_HUMAN Human 0 FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling (By similarity). DIKTLGNVTYMSQVLIQCAGSEEKNERYLLLFPNVLLMLSASPRMSGFIYQGKLPTTGMTITKLEDSENHRNAFEISGSMIERILVSCNNQQDLQEWVEHLQKQTK ARHG7_MOUSE Mouse 0 FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling (By similarity). DIKTLGSVTYMSQVTIQCAGSEEKNERYLLLFPKPSVMLSPSPRMSGFIYQGKLPTTGMTITKLEDSENHRNAFEISGSMIERILVSCTSQQDLHEWVEHLQKQTK ARHG7_RAT Others 0 FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. DIKTLGSVTYMSQVTIQCAGSEEKNERYLLLFPNLLLMLSASPRMSGFIYQGKLPTTGMTITKLEDSENHRNAFEISGSMIERILVSCNNQQDLHEWVEHLQRQTK ARHG6_HUMAN Human 0 FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF). DIKNLGNVIFMSQVMVQYGACEEKEERYLMLFSNVLIMLSASPRMSGFIYQGKIPIAGTVVTRLDEIEGNDCTFEITGNTVERIVVHCNNNQDFQEWLEQLNRLIR VAV_CAEEL Others 0 " FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for Rho GTPase. Has a critical roles in the generation of rhythmic behaviors: feeding, defecation and ovulation by dynamically regulating the concentration of intracellular calcium." RVNLDGEVKMAESTLTQA