###################################################### ##### Sequences and other information for the FYVE 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. ###################################################### ANFY1_HUMAN Human 1 SUBCELLULAR LOCATION: Cytoplasm. Endosome; endosomal membrane; peripheral membrane protein. Also associated with endosomal membranes. WCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVLT ANFY1_MOUSE Mouse 1 SUBCELLULAR LOCATION: Cytoplasm. Endosome; endosomal membrane; peripheral membrane protein. Also associated with endosomal membranes. WCDGSNCYECTAKFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVLT EEA1_HUMAN Human 1 FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking. SUBCELLULAR LOCATION: Cytoplasm. Endosome; early endosome; early endosomal membrane; peripheral membrane protein. DNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDACFNDLQ EEA1_MOUSE Mouse 1 FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Endosome; early endosome; early endosomal membrane; peripheral membrane protein (By similarity). DNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACFNDLQ HGS_HUMAN Human 1 " FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down- regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM. This complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex." SUBCELLULAR LOCATION: Cytoplasm. Endosome; early endosome; early endosomal membrane; peripheral membrane protein. WVDAEECHRCRVQFGVMTRKHHCRACGQIFCGKCSSKYSTIPKFGIEKEVRVCEPCYEQLN HGS_MOUSE Mouse 1 " FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down- regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM. This complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex." SUBCELLULAR LOCATION: Cytoplasm. Endosome; early endosome; early endosomal membrane; peripheral membrane protein. Endosome; multivesicular body; multivesicular body membrane; peripheral membrane protein. WVDAEECHRCRVQFGVVTRKHHCRACGQIFCGKCSSKYSTIPKFGIEKEVRVCEPCYEQLN HGS_RAT Others 1 " FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down- regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM. This complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity). May contribute to the efficient recruitment of SMADs to the activin receptor complex." SUBCELLULAR LOCATION: Cytoplasm. Endosome; early endosome; early endosomal membrane; peripheral membrane protein. Endosome; multivesicular body; multivesicular body membrane; peripheral membrane protein. WVDAEECHRCRVQFGVVTRKHHCRACGQIFCGKCSSKYSTIPKFGIEKEVRVCEPCYEQLN MTMR3_HUMAN Human 1 " FUNCTION: Dephosphorylates proteins phosphorylated on Ser, Thr, and Tyr residues and low molecular weight phosphatase substrate para-nitrophenylphosphate." SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. DHLAAHCYACDSAFWLASRKHHCRNCGNVFCSSCCNQKVPVPSQQLFEPSRVCKSCYSSLH RIMS1_RAT Others 1 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short- term synaptic plasticity (By similarity). SUBCELLULAR LOCATION: Cell membrane; peripheral membrane protein. Associated with plasma membranes from synaptic junctions. Not detected in synaptic vesicles. Detected in presynaptic nerve terminals close to the active zone. Detected in synaptic ribbons of ribbon synapses of retinal photoreceptor cells. KDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQE RFFL_HUMAN Human 1 FUNCTION: Has E3 ubiquitin protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Has anti-apoptotic activity. May bind phosphatidylinositol phosphates. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. TGLEPSCKSCGAHFANTARKQTCLDCKKNFCMTCSSQVGNGPRLCLLCQRFRATAF RFFL_MOUSE Mouse 1 FUNCTION: Has E3 ubiquitin protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Has anti-apoptotic activity. May bind phosphatidylinositol phosphates (By similarity). Overexpression slows protein traffic through recycling endosomes. SUBCELLULAR LOCATION: Cytoplasm; perinuclear region. Membrane; peripheral membrane protein. Associated with perinuclear vesicles. TGSEPSCKACGVHFASTTRKQTCLDCKKNFCMTCSSQEGNGPRLCLLCLRFRA RFFL_RAT Others 1 FUNCTION: Has E3 ubiquitin protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Has anti-apoptotic activity. May bind phosphatidylinositol phosphates (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. TGSEPSCKACGVHFASTTRKQTCLDCKKNFCMTCSSQEGNGPRLCLLCLRFRA RNF34_BOVIN Others 1 FUNCTION: Has E3 ubiquitin protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Protects cells against apoptosis induced by TNF. Binds phosphatidylinositol-5-phosphate and phosphatidylinositol-3- phosphate (By similarity). SUBCELLULAR LOCATION: Nucleus; nucleoplasm; nuclear speckle (By similarity). Intracellular membrane; peripheral membrane protein (By similarity). EGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLLQE RNF34_HUMAN Human 1 FUNCTION: Has E3 ubiquitin protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Protects cells against apoptosis induced by TNF. Binds phosphatidylinositol-5-phosphate and phosphatidylinositol-3- phosphate. SUBCELLULAR LOCATION: Nucleus; nucleoplasm; nuclear speckle. Intracellular membrane; peripheral membrane protein. EGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLLQE RNF34_MOUSE Mouse 1 FUNCTION: Has E3 ubiquitin protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Protects cells against apoptosis induced by TNF. Binds phosphatidylinositol-5-phosphate and phosphatidylinositol-3- phosphate (By similarity). SUBCELLULAR LOCATION: Nucleus; nucleoplasm; nuclear speckle (By similarity). Intracellular membrane; peripheral membrane protein (By similarity). EGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSLCSVSQENLRRCSTCHLLQE RNF34_PONPY Others 1 FUNCTION: Has E3 ubiquitin protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Protects cells against apoptosis induced by TNF. Binds phosphatidylinositol-5-phosphate and phosphatidylinositol-3- phosphate (By similarity). SUBCELLULAR LOCATION: Nucleus; nucleoplasm; nuclear speckle (By similarity). Intracellular membrane; peripheral membrane protein (By similarity). EGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLLQE RNF34_RAT Others 1 FUNCTION: Has E3 ubiquitin protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Protects cells against apoptosis induced by TNF. Binds phosphatidylinositol-5-phosphate and phosphatidylinositol-3- phosphate (By similarity). SUBCELLULAR LOCATION: Nucleus; nucleoplasm; nuclear speckle (By similarity). Intracellular membrane; peripheral membrane protein. EGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSLCSVSQENLRRCSTCHLLQE SYTL5_HUMAN Human 1 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). CVHCHRNLGLIFDRGDPCQACSLRVCRECRVAGPNGSWKCTVC SYTL5_MOUSE Mouse 1 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). CVHCHKTLGLIFDRGDPCQACSLRVCSECRVTGLDGSWKCTVC SYTL5_RAT Others 1 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). CVHCQKSLGLIFDRGAPCQACSLRVCSECRVTGLDGSWKCTVC FAB1_SCHPO Yeast 1 " FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol-4- phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol-4,5-biphosphate. Required for survival under conditions of nitrogen starvation. May have a role in the secretion of pheromone peptides." " SUBCELLULAR LOCATION: Cytoplasm. During cell fusion of opposite mating types, migrates to the isthmus." DERTNNCSLCETEFTLFRRKHHCRICGKIICKYCLKEAPGFIFRLQGSIKVCRPCASILV FAB1_YEAST Yeast 1 " FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol-3- phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol-3,5-bisphosphate. Required for endocytic- vacuolar pathway and nuclear migration. The product of the reaction it catalyzes functions as an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole." SUBCELLULAR LOCATION: Vacuole; vacuolar membrane; peripheral membrane protein. Endosome; endosomal membrane; peripheral membrane protein. DESSKECFSCGKTFNTFRRKHHCRICGQIFCSSCTLLIDGDRFGCHAKMRVCYNCYEHAD FYV1_DROME Others 1 " FUNCTION: Supports the intracellular PIP pool and to a lesser extent, the PI 4,5-P(2) pool. It generates PIP from PI and, to a lesser extent, PI 4,5-P(2) from PI 4-P. There are indications that it phosphorylates the D-5 rather than the D-4 position. Has a role in endosome-related membrane trafficking (By similarity)." DSKAKECYDCSQKFSTFRRKHHCRLCGQIFCSKCCNQVVPGMIIRCDGDLKVCNYCSKIVL FYV1_HUMAN Human 1 " FUNCTION: Supports the intracellular PIP pool and to a lesser extent, the PI 4,5-P(2) pool. It generates PIP from PI and, to a lesser extent, PI 4,5-P(2) from PI 4-P. There are indications that it phosphorylates the D-5 rather than the D-4 position. Has a role in endosome-related membrane trafficking (By similarity)." SUBCELLULAR LOCATION: Endosome; endosomal membrane. Mainly associated with membranes of the late endocytic pathway. DSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRKIAL FYV1_MOUSE Mouse 1 " FUNCTION: Supports the intracellular PIP pool and to a lesser extent, the PI 4,5-P(2) pool. It generates PIP from PI and, to a lesser extent, PI 4,5-P(2) from PI 4-P. There are indications that it phosphorylates the D-5 rather than the D-4 position. Has a role in endosome-related membrane trafficking." SUBCELLULAR LOCATION: Associated with vesicle structures. Displays a peripheral vesicular punctate pattern. DSQCKECYDCSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRKIAL HRS_DROME Others 1 " FUNCTION: Essential role in endosome membrane invagination and formation of multivesicular bodies, MVBs. Required during gastrulation and appears to regulate early embryonic signaling pathways. Inhibits tyrosine kinase receptor signaling by promoting degradation of the tyrosine-phosphorylated, active receptor, potentially by sorting activated receptors into MVBs. The MVBs are then trafficked to the lysosome where their contents are degraded." SUBCELLULAR LOCATION: Locates to vesicles present in the perinuclear regions of muscle cells and in the periphery of Garland cells of third-instar larvae. WADGRVCHRCRVEFTFTNRKHHCRNCGQVFCGQCTAKQCPLPKYGIEKEVRVCDGCFAALQ RBNS5_HUMAN Human 1 FUNCTION: Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3). SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; cytoplasmic side. Endosome; early endosome; early endosome membrane; lipid- anchor. DQDVPFCPDCGNKFSIRNRRHHCRLCGSIMCKKCMELISLPLANKLTSASKESLSTHTSPSQSPNSVHGSRRGSISSMSSVSSVLDEKDDDRIRCCTHCKDTLL RBNS5_MOUSE Mouse 1 FUNCTION: Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3) (By similarity). SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; cytoplasmic side (By similarity). Endosome; early endosome; early endosome membrane; lipid-anchor (By similarity). DQDVPFCPDCGNKFSIRNRRHHCRLCGSIMCKKCMELIGLPLAHKLTSASKDSLSTHTSPSQSPNSVHGSRRGSISSMSSVSSVLDEKDDDRIRCCTHCKDKLL VPS27_YEAST Yeast 1 FUNCTION: Required for membrane traffic to the vacuole. WIDSDACMICSKKFSLLNRKHHCRSCGGVFCQEHSSNSIPLPDLGIYEPVRVCDSCFEDYD DSVVQICPECNNSFTLTRRRRHCRLCGRVICRFCVLEISLPQHPQPLLICMSCNQNYF ZFY16_HUMAN Human 1 FUNCTION: May be involved in regulating membrane trafficking in the endosomal pathway. Overexpression induces endosome aggregation. Required to target TOM1 to endosomes. " SUBCELLULAR LOCATION: Cytoplasmic; localized to early endosomes. Membrane-associated, probably via its association with phosphatidylinositol 3-phosphate (PI3P)." DSEAPNCMNCQVKFTFTKRRHHCRACGKVFCGVCCNRKCKLQYLEKEARVCVVCYETIS DRSVLFCNICSEPFGLLLRKHHCRLCGMVVCDDANRNCSNEISIGYLMSAASDLPFEYNIQKDDLLHIPISIRLCSHCIDMLF ZFY16_MOUSE Mouse 1 FUNCTION: May be involved in regulating membrane trafficking in the endosomal pathway. Overexpression induces endosome aggregation. Required to target TOM1 to endosomes (By similarity). " SUBCELLULAR LOCATION: Cytoplasmic; localized to early endosomes. Membrane-associated, probably via its association with phosphatidylinositol 3-phosphate (PI3P) (By similarity)." DSEAPNCMNCQVKFTFTKRRHHCRACGKVFCGVCCNRKCKLQYLEKEARVCVICYETIN SYTL4_HUMAN Human 1 FUNCTION: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity). " SUBCELLULAR LOCATION: Peripheral membrane protein. Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles (By similarity)." CARCQESLGRLSPKTNTCRGCNHLVCRDCRIQESNGTWRCKVC SYTL4_MOUSE Mouse 1 FUNCTION: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner. " SUBCELLULAR LOCATION: Peripheral membrane protein. Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles." CARCQEGLGRLIPKSSTCVGCNHLVCRECRVLESNGSWRCKVC SYTL4_RAT Others 1 FUNCTION: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity). " SUBCELLULAR LOCATION: Peripheral membrane protein. Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles." CARCQEGLGRLISKSNTCVGCNHLVCRECRVLESNGSWRCKVC 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). EKEVTMCMRCQEPFNSITKRRHHCKACGHVVCGKCSEFRARLVYDNNRSNRVCTDCYVALH 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. EKEVTMCMRCQEPFNSITKRRHHCKACGHVVCGKCSEFRARLIYDNNRSNRVCTDCYVALH 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). DNEVTMCMKCKESFNALTRRRHHCRACGHVVCWKCSDYKAQLEYDGGRLNKVCKDCYQIIS 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. DNEVTMCMKCKESFNALTRRRHHCRACGHVVCWKCSDYKAQLEYDGGRLNKVCKDCYQIMS FGD5_HUMAN Human 1 " FUNCTION: May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a role in regulating the actin cytoskeleton and cell shape (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). VTHVMMCMNCGCDFSLTLRRHHCHACGKIVCRNCSRNKYPLKYLKDRMAKVCDGCFGELK FGD5_MOUSE Mouse 1 " FUNCTION: May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a role in regulating the actin cytoskeleton and cell shape (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). VTHAMMCMNCGCDFSLTVRRHHCHACGKIVCRNCSRNKYPLKCLKNRMAKVCDGCFRELK FGD6_HUMAN Human 1 " FUNCTION: May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a role in regulating the actin cytoskeleton and cell shape (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). DTRATMCMICTSEFTLTWRRHHCRACGKIVCQACSSNKYGLDYLKNQPARVCEHCFQELQ FGD6_MOUSE Mouse 1 " FUNCTION: May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a role in regulating the actin cytoskeleton and cell shape (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). DTRATMCMICTSEFTLTWRRHHCRACGKIVCQACSSNKYGLDYLKGQLARVCEHCFQELQ FGD2_HUMAN Human 1 " FUNCTION: May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a role in regulating the actin cytoskeleton and cell shape (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). DKMVTMCMRCQEPFNALTRRRHHCRACGYVVCARCSDYRAELKYDDNRPNRVCLHCYAFLT FGD2_MOUSE Mouse 1 " FUNCTION: May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a role in regulating the actin cytoskeleton and cell shape (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (Probable). DKMVTMCMRCQEPFNALTRRRHHCRACGYVVCAKCSDYRAELKYDSNRPNRVCLTCYTFLT PEP7_SCHPO Yeast 1 " FUNCTION: Required for vacuole segregation and vacuole protein sorting. Possibly part of a complex which tethers the vacuole membrane to microtubules, either directly or via kinesin or dynein-like motor proteins. Probably functions in several interorganelle traffic pathways (By similarity)." PDMVCHDPMCDKLLNFINGHIHCRKCGYIFCNFHSMYQIKLSIHATYDSENGFWCRVCRECYEGRP PEP7_YEAST Yeast 1 " FUNCTION: Required for vacuole segregation and vacuole protein sorting. Possibly part of a complex which tethers the vacuole membrane to microtubules, either directly or via kinesin or dynein-like motor proteins. Probably functions in several interorganelle traffic pathways." SUBCELLULAR LOCATION: Vacuole; vacuolar membrane; peripheral membrane protein; cytoplasmic side. KKGKSCCHTCGRTLNNNIGAINCRKCGKLYCRRHLPNMIKLNLSAQYDPRNGKWYNCCHDCFVTKP MYRIP_HUMAN Human 1 FUNCTION: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments (By similarity). SUBCELLULAR LOCATION: Cytoplasmic; in pre- and post-synaptic areas in photoreceptor cells and in the basal microvilli of retinal pigment epithelium cells. Associated with melanosomes. Colocalizes with actin filaments (By similarity). CCMRCCSPFTFLVNTKRQCGDCKFNVCKSCCSYQKHEKAWVCC MYRIP_MOUSE Mouse 1 FUNCTION: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments. SUBCELLULAR LOCATION: Cytoplasmic; in pre- and post-synaptic areas in photoreceptor cells and in the basal microvilli of retinal pigment epithelium cells. Associated with melanosomes. Colocalizes with actin filaments. CCMRCCSPFTFLVNARRRCGECKFSVCKSCCSYQKHEKLWVCC FGD3_HUMAN Human 0 " 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). DKEKQSCKSCGETFNSITKRRHHCKLCGAVICGKCSEFKAENSRQSRVCRDCFLTQP FGD3_MOUSE Mouse 0 " 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). DKEKPGCKSCGETFNSITKRRYRCKLCGEVICRKCSEFKAENSKQSRVCRECFLEEP FGD3_PONPY Others 0 " 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). DKEKQSCKSCGETFNSITKRRHHCKLCGVVICGKCSEFKAENSRQSRVCRECFLTQP FGD4_HUMAN Human 0 " 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). DNEVTMCMKCKEPFNALTRRRHHCRACGYVVCWKCSDYKAQLEYDGGKLSKVCKDCYQIIS PIB2_YEAST Yeast 0 DSKRNSCRYCHKPFTLWERKHHCRHCGDIFCQDHLRHWLYLDSQANFIMINELNNGGINGGGTLCKICDDCLVEYE RBF1_CAEEL Others 0 FUNCTION: Rab-3 effector. GNGVTHCLLCHTEFGLLASKSYAAMCVDCRKYVCQRNCGVETTDVNQTTGKVETVFLCKICSEARE RIMS1_HUMAN Human 0 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short- term synaptic plasticity (By similarity). KDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQE RIMS1_MOUSE Mouse 0 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short- term synaptic plasticity. KDDAPTCGICHKTKFADGCGHLCSYCRTKFCARCGGRVSLRSNNEDKVVMWVCNLCRKQQE RIMS2_HUMAN Human 0 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein. KGDAPTCGICHKTKFADGCGHNCSYCQTKFCARCGGRVSLRSNKVMWVCNLCRKQQE RIMS2_MOUSE Mouse 0 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein. KGDAPTCGICHKTKFADGCGHNCSYCQTKFCARCGGRVSLRSNKVMWVCNLCRKQQE RIMS2_RAT Others 0 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein. KGDAPTCGICHKTKFADGCGHNCSYCQTKFCARCGGRVSLRSNKVMWVCNLCRKQQE RIM_CAEEL Others 0 FUNCTION: Regulates the efficiency of a post-docking step of the release pathway. Acts after vesicle docking likely via regulating priming. May regulate the conformational changes in syntaxin. Binding of vesicles via rab-3[GTP] to Rim may signal the presence of a docked synaptic vesicle. Rim may then signal to unc-13 to change the conformation of syntaxin from the closed to the open state. Syntaxin could then engage synaptobrevin on the docked vesicle to form SNARE complexes and to prime the vesicle for release. Not required for the development or the structural organization of synapses. TQDDAICQICQKTKFADGIGHKCFYCQLRSCARCGGRAQSKNKAIWACSLCQKRQQ RP3A_BOVIN Others 0 FUNCTION: Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. GDGVNRCILCGEQLGMLGSACVVCEDCKKNVCTKCGVETSNNRPHPVWLCKICIEQRE RP3A_HUMAN Human 0 FUNCTION: Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal (By similarity). GDGVNRCILCGEQLGMLGSACVVCEDCKKNVCTKCGVETNNRLHSVWLCKICIEQRE RP3A_MOUSE Mouse 0 FUNCTION: Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. GDGVNRCILCGEQLGMLGSACVVCEDCKKNVCTKCGVETSNNRPHPVWLCKICLEQRE DHEILHCHNCRKEFSIKLSKHHCRACGQGFCDECSHDRRAVPSRGWDHPVRVCFNCNKKPG RP3A_RAT Others 0 FUNCTION: Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. GDGVNRCILCGEQLGMLGSACVVCEDCKKNVCTKCGVETSNNRPHPVWLCKICLEQRE DHEILHCHNCRKEFSVKLSKHHCRACGQGFCDECSHDCRAVPSRGWDHPVRVCFNCNKKPG RUFY1_HUMAN Human 0 DDEATHCRQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLL WDFY1_HUMAN Human 0 SUBCELLULAR LOCATION: Endosome; early endosome. WLESDSCQKCEQPFFWNIKQMWDTKTLGLRQHHCRKCGQAVCGKCSSKRSSYPVMGFEFQVRVCDSCYDSIK WDFY2_HUMAN Human 0 WLDSDSCQKCDQPFFWNFKQMWDSKKIGLRQHHCRKCGKAVCGKCSSKRSSIPLMGFEFEVRVCDSCHEAIT WDFY2_MOUSE Mouse 0 WLDSDSCQKCDQPFFWNVKQMWDSKKIGLRQHHCRKCGKAVCGKCSSKRSSIPLMGFEFEVRVCDSCHEAIT YLN2_CAEEL Others 0 WKTSDCCQKCNQPFFWNLQAMWQRKVVGLRQHHCRTCGSAVCGSCCDNWTTYPPMGYETKIRICNDCNARMK YOTB_CAEEL Others 0 DGEAVKCMVCGKTQFNLVQRRHHCRNCGRVVCGACSSRTFRIDNVHKKPVRVCDHCFDSLS YW91_CAEEL Others 0 " FUNCTION: Not known, could be a tyrosine-phosphatase." EGESGHCAYCKKEFNKLSVYVEDRQHHCRNCGRVVCEDCSKNRFSVIEEGKSVQKRACDSCYDSMH ZFY19_HUMAN Human 0 ATMESRCYGCAVKFTLFKKEYGCKNCGRAFCSGCLSFSAAVPRTGNTQQKVCKQCHEVLT ZFY19_MOUSE Mouse 0 MESRCYGCAVKFTLFKKEYGCKNCGRAFCNGCLSFSALVPRAGNTQQKVCKQCHTILT ZFY21_HUMAN Human 0 DKECRRCMQCDAKFDFLTRKHHCRRCGKCFCDRCCSQKVPLRRMCFVDPVRQCAECALVSL ZFY21_MOUSE Mouse 0 DKECPRCMQCDAKFDFITRKHHCRRCGKCFCDRCCSQKVPLRRMCFVDPVRQCADCALVSH ZFY28_HUMAN Human 0 DEACGFCTACKAPFTVIRRKHHCRSCGKIFCSRCSSHSAPLPRYGQVKPVRVCTHCYMFHVTP ZFYV1_HUMAN Human 0 SUBCELLULAR LOCATION: Golgi apparatus; Golgi stack. Resides predominantly in the cisternal stacks of the Golgi. NSQILSCNKCATSFKDNDTKHHCRACGEGFCDSCSSKTRPVPERGWGPAPVRVCDNCYEARN ZFYV1_MOUSE Mouse 0 SUBCELLULAR LOCATION: Golgi apparatus; Golgi stack (By similarity). Resides predominantly in the cisternal stacks of the Golgi (By similarity). NSQILSCNQCATSFKDNDTKHHCRACGEGFCDSCSSKTRPVPERGWGPAPVRVCDSCYDARN ZFYV9_HUMAN Human 0 FUNCTION: Involved in recruiting unphosphorylated forms of SMAD2/SMAD3 to the TGF-beta receptor by controlling their subcellular localization and by interacting and colocalizing with the TGF-beta receptor. Phosphorylation of SMAD2/SMAD3 induces dissociation from ZFYVE9 and formation of SMAD2/SMAD4 complexes and nuclear translocation. SUBCELLULAR LOCATION: Cytoplasm. DSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCVICHSVLM MELPH_HUMAN Human 0 FUNCTION: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A. SUBCELLULAR LOCATION: Cytoplasm. CARCLQPYQLLVNSKRQCLECGLFTCKSCGRVHPEEQGWICDPC MELPH_MOUSE Mouse 0 FUNCTION: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A. SUBCELLULAR LOCATION: Melanosome. CARCLQPYRLLLNSRRQCLECSLFVCKSCSHAHPEEQGWLCDPC