###################################################### ##### Sequences and other information for the FERM 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. ###################################################### E41L3_MOUSE Mouse 1 FUNCTION: Isoform 2 (heart-specific) has the complete spectrin-- actin-binding (SAB) domain and fully interacts with spectrin and actin. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. MQCKVTLLDGSEYGCDVDKRSRGQVLFDKVCEHLNLLEKDYFGLTYRDAENQKNWLDPAKEIKKQIRSGAWHFSFNVKFYPPDPAQLSEDITRYYLCLQLRDDIVSGRLPCSFVTLALLGSYTVQSELGDYDPDECGNDYISEFRFAPNHTKELEDKVIELHKSHRGMTPAEAEMHFLENAKKLSMYGVDLHHAKDSEGVEIMLGVCASGLLIYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQFESTIGFKLPNHRAAKRLWKVCVEHHTFFRLLL EZRI_BOVIN Others 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Membrane-associated. Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Localizes to cell extensions and peripheral processes of astrocytes (By similarity). Microvillar peripheral membrane protein (cytoplasmic side). PKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKESPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKELHKAGYLGSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDSAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRR EZRI_HUMAN Human 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Membrane-associated. Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Localizes to cell extensions and peripheral processes of astrocytes (By similarity). Microvillar peripheral membrane protein (cytoplasmic side). PKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRR EZRI_MOUSE Mouse 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Membrane-associated. Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Microvillar peripheral membrane protein (cytoplasmic side). Localizes to cell extensions and peripheral processes of astrocytes (By similarity). PKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPVQFKFRAKFYPEDVAEELIQDITQKLFFLQVKDGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEMHKSGYLSSERLIPQRVMDQHKLSRDQWEDRIQVWHAEHRGMLKDSAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRR EZRI_RABIT Others 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane (By similarity). SUBCELLULAR LOCATION: Cell membrane; peripheral membrane protein. Localizes to cell extensions and peripheral processes of astrocytes (By similarity). Microvillar peripheral membrane protein (cytoplasmic side). Localization to the apical membrane of parietal cells depends on the interaction with MPP5. PKPINVRVTTMDAELEFAVQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPVQFKFRAKFYPEDVSEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYSKEAHKAGYLSSERLIPQRVMDQHKLSRDQWEDRIQVWHAEHRGMLKDSAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKNDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRR EZRI_RAT Others 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Membrane-associated. Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Microvillar peripheral membrane protein (cytoplasmic side) (By similarity). Localizes to cell extensions and peripheral processes of astrocytes. PKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPVQFKFRAKFYPEDVADELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEMHKSGYLSSERLIPQRVMDQHKLSRDQWEDRIQVWHAEHRGMLKDSAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRR JAK1_BRARE Others 1 " FUNCTION: Tyrosine kinase of the non-receptor type. Appears to be required in early development for specific cell migrations (epiboly), expression of homeobox protein goosecoid and formation of anterior structures." " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated (By similarity)." KGLEIHFYLADTHQLEFFKACYTAEDLCVEAAKRCRISPLCHNLFALYEESQDLWYAPNHVFKVTDETSIKLHYRMRFYFTNWHGTSEIESPVWRHTLSKQKSVLNSQKTTEGTPLLDAASLDYLFAQGQYDFLRGLSPVRPTQTDEEHHEIENECLGMAVLAITHHAKSNNLPLSGAGAETSYKRFIPDSLNRTIKQRNFLTRIRISNVFKNFLNEFNSKTIQDSNIGLYDLKVKYLSTLETLTQGVGREIFKPKNLKVTGESEGSPAQMLPLGDNGMGYEVQVYGTTGISWRRKPAPNQLILKDKPKSKKIKGDKQWNDKKKDSGWTLFSDFHEITHIVIKDCCVTIYRQDNKTMELDLFYRDAALSFAALVDGYFRLTVDAH JAK1_CYPCA Others 1 FUNCTION: Tyrosine kinase of the non-receptor type (By similarity). " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated (By similarity)." KGLEIHFYLPDTHQLEYFKDCHTAEDLCVEGCQEDATSHLCADNLFALSEESQDLWYAPNHAFKITEETSIKLHYRMRFYFTNWHAPVRTESPVWRHSLFKHKGVSVSPKGPEGTPLLDAASLEYLFAQGQYDFLRGLAPVRAPQNEAEKHEIENECLGMAVLAITHHAKSNDLPLSGVGAETSYKRFIPDSLNRTIKQRNFSHVYVYNNVFKNFLNEFNSKTIQDSNITLYDLKVKYLSTLETLTQGLGRETIEPKILKVSGESDGSPALTLPSGDDGLGYEVQVSGTTGISWRRKPVPNILIVKDKTKSKKNKADKQSKKEMTKRKTVMTIFSDFFEITHIVIKESCATIYSQDNKTMELDLFYRDAALSFAALVDGYFRLTVDAH JAK1_HUMAN Human 1 " FUNCTION: Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor." " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated." PGVEVIFYLSDREPLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKKIPDATPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLENKDKKDEEKNKIREEWNNFSFFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAH JAK1_MOUSE Mouse 1 " FUNCTION: Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor." " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated." PGVEVTFYLLDREPLRLGSGEYTAEELCIRAAQECSISPLCHNLFALYDESTKLWYAPNRIITVDDKTSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKRVPEATPLLDASSLEYLFAQGQYDLIKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVHDLKVKYLATLETSTLTKHYGAEIFETSMLLISSENELSRCHSNDSGNVLYEVMVTGNLGIQWRQKPNVVPVEKEKNKLKRKKLEYNKHKKDDERNKLREEWNNFSYFPEITHIVIKESVVSINKQDNKNMELKLSSREEALSFVSLVDGYFRLTADAH JAK2_HUMAN Human 1 " FUNCTION: Tyrosine kinase of the non-receptor type, involved in interleukin 3 signal transduction." " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated (By similarity)." PVLQVYLYHSLGKSEADYLTFPSGEYVAEEICIAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHNVLYRIRFYFPRWYCSGSNRAYRHGISRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKENDQTPLAIYNSISYKTFLPKCIRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEKFEVKEPGSGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPNIIDVSIKQANQEGSNESRVVTIHKQDGKNLEIELSSLREALSFVSLIDGYYRLTADAH JAK2_MOUSE Mouse 1 " FUNCTION: Tyrosine kinase of the non-receptor type, involved in interleukin 3 signal transduction." " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated (By similarity)." PVLQVYLYHSLGQAEGEYLKFPSGEYVAEEICVAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHDILYRIRFYFPHWYCSGSSRTYRYGVSRGAEAPLLDDFVMSYLFVQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKEKDQTPLAVYNSVSYKTFLPKCVRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEQFEVKESARGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDVQLYCDFPDIIDVSIKQANQECSNESRIVTVHKQDGKVLEIELSSLKEALSFVSLIDGYYRLTADAH JAK2_RAT Others 1 " FUNCTION: Tyrosine kinase of the non-receptor type, involved in interleukin 3 signal transduction." " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated (By similarity)." PVLQVYLYHSLGQAEGDYLKFPNGEYVAEEICVAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHNILYRIRFYFPHWYCSGSNRTYRYGVSRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKEKDQTPLAVYNSISYKTFLPKCVRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEQFEVKESARGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPDIIDVSIKQANQECSTESRVVTVHKQDGKVLEIELSSLKEALSFVSLIDGYYRLTADAH JAK3_HUMAN Human 1 " FUNCTION: Tyrosine kinase of the non-receptor type, involved in the interleukin-2 and interleukin-4 signaling pathway. Phosphorylates STAT6, IRS1, IRS2 and PI3K." " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated (By similarity)." GALHVLLPARGPGPPQRLSFSFGDHLAEDLCVQAAKASGILPVYHSLFALATEDLSCWFPPSHIFSVEDASTQVLLYRIRFYFPNWFGLEKCHRFGLRKDLASAILDLPVLEHLFAQHRSDLVSGRLPVGLSLKEQGECLSLAVLDLARMAREQAQRPGELLKTVSYKACLPPSLRDLIQGLSFVTRRRIRRTVRRALRRVAACQADRHSLMAKYIMDLERLDPAGAAETFHVGLPGALGGHDGLGLLRVAGDGGIAWTQGEQEVLQPFCDFPEIVDISIKQAPRVGPAGEHRLVTVTRTDNQILEAEFPGLPEALSFVALVDGYFRLTTDSQ JAK3_MOUSE Mouse 1 " FUNCTION: Tyrosine kinase of the non-receptor type, involved in the interleukin-2 and interleukin-4 signaling pathway. Phosphorylates STAT6, IRS1, IRS2 and PI3K." " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated (By similarity)." GALHVLLPPRGPGPPQRLSFSFGDYLAEDLCVRAAKACAILPVYHSLFALATEDFSCWFPPSHIFCIEDVDTQVLVYRLRFYFPDWFGLETCHRFGLRKDLTSAILDLHVLEHLFAQHRSDLVSGRLPVGLSMKEQGEFLSLAVLDLAQMAREQAQRPGELLKTVSYKACLPPSLRDVIQGQNFVTRRRIRRTVVLALRVWSPARPTATAHGQVYLDLERLHPAATTETFRVGLPGAQEEPGLLRVAGDNGISWSSGDQEVLGLGLRSGVRGEAWRLVKKPVRTIRKVASPGRADCTTGQGGGVNLKVGPGMELPQGLTWGVTRRVRLDRGRGRTEGDSMDWISGHDPTRPVFSPLTSSPPPHKWRWEGGRRGGCAGSRSVIPWLLSLFLFFFFNGFARQGFSYSSGCPGTHFVRPGWPRTQKSACLCLSSAVIKGRVPLRRYCLSFLPQLFQTFCDFPEIVDVSIKQPTCGSGREHRLVTVTRMDGHILEAEFPGLPEALSFVALVDGYFRLICDSR JAK3_RAT Others 1 " FUNCTION: Tyrosine kinase of the non-receptor type, involved in the interleukin-2 and interleukin-4 signaling pathway. Phosphorylates STAT6, IRS1, IRS2 and PI3K." " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated (By similarity)." GALHVLLPPRGPGPPQRLSFSFGDYLAEDLCVRAAKACGILPVYHSLFALATEDLSCWFPPSHIFSIEDVDTQVLVYRLRFYFPGWFGLETCHRFGLHKDLTSAILDVHVLEHLFAQHRSDLVSGRLPVGLSLKDQGEFLSLAVLDLAQMARKQAQRPGELLKSVSYKACLPPSLRDLIQGQSFVTRRRIRRTVVQALAPCSSLPSRPYALMAKYILDLERLHPAATTESFLVGLPGAQEEPGCLRVTGDNGIAWSSKDQELFQTFCDFPEIVDVSIKQAPRVGPAGEHRLVTITRMDGHILEAEFPGLPEALSFVALVDGYFRLICDSR JAK_DROME Others 1 " FUNCTION: Tyrosine kinase of the non-receptor type, phosphorylates the marelle protein. Required maternally for the establishment of the normal array of embryonic segments: involved in the control of pair-rule gene transcription in a stripe-specific manner." " SUBCELLULAR LOCATION: Intracellular membrane; peripheral membrane protein. Wholly intracellular, possibly membrane associated (By similarity)." GTIRVFNFTTGEFERFHPNMLCEEICNTMCRQLGIAPIAQLLYGIREHSTSRRPSPLVRLDLTWCLPGERLNCQLVYCFRMRFRVPELDSQLELIDGRSHKFLYRQMRYDMRTEQIPEIRYPEHKDKSTGLAVMDMLIDDQEQSEDQQAMRSIEKLYKLYLPPSLWRAHSFFVGSKIREVFRSLKANSLSVERLKWHYVHQVSHLAPTYMTEQFTCTVQYLPNEEVARGSGPIGTSLAHSTSTLASSGSTNTLSTLTTNTNSVALGGSGKKAKRRSTSGGIDVYVRVFPHDSLEPGLKVARVTSEATLKWILVGAVEGIFMISKINDTSVRLEIVGLPKGYEMQFQTEKEMKSFISYLGIYIRLSSKWM KRIT1_BOVIN Others 1 SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (Probable). EKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKKIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPITKLKSKAPHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDADSCFQIHSMENKMSFIVHTKQAGLVVKLLVKLNGQLMPMER KRIT1_HUMAN Human 1 SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (Probable). EKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKAPHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLMPTER KRIT1_MOUSE Mouse 1 SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (Probable). EKVRIYRMDGSYRSVELKHGNNTTAQQIMEGMRLSQETQRYFTIWICSENLSLQFKPYHKPLQQVHDWPEILAELTNLDPQRETPQLFLRRDVGLPLEVEKKIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEETLKSIVPITKLKSKAPHWINRILHEYKNLSLSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYCCFTWQLGDAGTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLMPSERNS MERH_DROME Others 1 " FUNCTION: May have a role in regulation of cellular growth and signaling, possibly by having a role in endocytic processes." " SUBCELLULAR LOCATION: Cell membrane; cell-cell junction; adherens junction; peripheral membrane protein. Intracellular membrane; peripheral membrane protein. Membrane-associated, adherens junctions and endocytic compartments. Cytoplasmic, punctate." LSVRVSTFDSELEFKLEPRASGQDLFDLVCRTIGLRESWYFGLQYVDTRSNVSWLKMEKRVRDQRVELHASNNVYVFSFYAKFFPENVSEELIQEITQHLFFLQVKQSILSMDIYCRPEASVLLASYAVHVQYGPYDYETYKDGMLAGGELLPKGVTDQYQMTPEMWEERIKTWYMDHEPMTRDEVEMEYLKIAQDLDMYGVNYFPITNKNKTKLWLGVTSVGLNIYDERDKLTPKTTFQWNEIRHVSFDDKKFTIRLVDAKVSNFIFYSQDLHINKMILDLCKGNHDLYMRRR MOEH_DROME Others 1 FUNCTION: Involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; cell-cell junction; adherens junction; peripheral membrane protein. MSPKALNVRVTTMDAELEFAIQSTTTGKQLFDQVVKTIGLREVWFFGLQYTDSKGDSTWIKLYKKVMNQDVKKENPLQFRFRAKFYPEDVAEELIQDITLRLFYLQVKNAILTDEIYCPPETSVLLASYAVQARHGDHNKTTHTAGFLANDRLLPQRVIDQHKMSKDEWEQSIMTWWQEHRSMLREDAMMEYLKIAQDLEMYGVNYFEIRNKKGTDLWLGVDALGLNIYEQDDRLTPKIGFPWSEIRNISFSEKKFIIKPIDKKAPDFMFFAPRVRINKRILALCMGNHELYMRRR 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. WLDSSRSLMEQGIFEGDIILLRFKFMNFFDLNPKYDPVRINQLYEQAKWSILLDEFDHTEEEATLFAALQLQATLQRDSPEPEENNKDDVDILLDELEQNLDAAALNRRSDLTQVPELADYLKYMKPKKLAAFKGFKRAFFSFRDLYLSYHQSSSDVNSAPLGHFSLKGCEVSQDVSVGQQKYHIKLLLPTAEGMIDFILKCDSEHQYARWMAACRLASRGKSMADSSYQQEVESIKNLLKMQSGNGNENGNSNTASRKAAAVKLPNDFNVDEYISSKYVRRARSKQQIQQRVSDAHGNVRQLTATEAKLQYIRAWQALPEHGIHYF 41_BOVIN Others 1 FUNCTION: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. MHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVSGRLPCSFATLALLGSYTIQSELGDYDPELHGADYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKEKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTS 41_CANFA Others 1 FUNCTION: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. MHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNGASKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVSGRLPCSFATLALLGSYTIQSELGDYDPELHGAEYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTS 41_CHICK Others 1 FUNCTION: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By similarity). EFLENAKKLSMYGVDLHHAKDLEGVDITLGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAK 41_HUMAN Human 1 FUNCTION: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. MHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTS 41_MOUSE Mouse 1 FUNCTION: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By similarity). MHCKVSLLDDTVYECVVEKHANLQDLLKRVCEHLNLLEEDYFGLALWDSATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGMDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISSKRSSFFIKIRPGEQEHYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTS 41_XENLA Others 1 FUNCTION: Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By similarity). MRCKVTLLDDTVYECDLEKHAKGQDIFKKVCSHLNIVEEDYFGLAIWESPTCKVWLDPLKDIRKQVHGGPCEFTSNVKFYPPDPAQLSEDITRYYLCLQLRKDIFSGRLPCSFATLALLGSYTVQSEVGDYEEDLHGVDYVSEFKLSPNQTKDLEEKVGELHKSYRSMTPAQADLEFLENAKKLTMYGVDIHQAKDLEGVDIKLGVCSGGLMVFKDNLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYKAAKKLWKVCVEHHTFFRLTS FAK1_CHICK Others 1 " FUNCTION: Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity." SUBCELLULAR LOCATION: Cell membrane; cell-matrix junction; focal adhesion; cytoplasmic side. Constituent of focal adhesions. RVLKVFHYFENSSEPTTWASIIRHGDATDVRGIIQKIVDCHKVKNVACYGLRLSHLQSEEVHWLHLDMGVSNVREKFELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKNDYMLEIADQVDQEIALKLGCLEIRRSYGEMRGNALEKKSNYEVLEKDVGLRRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGANPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGAT FAK1_HUMAN Human 1 " FUNCTION: Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity." SUBCELLULAR LOCATION: Cell membrane; cell-matrix junction; focal adhesion; cytoplasmic side. Constituent of focal adhesions. RVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTS FAK1_MOUSE Mouse 1 " FUNCTION: Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity." SUBCELLULAR LOCATION: Cell membrane; cell-matrix junction; focal adhesion; cytoplasmic side. Constituent of focal adhesions. RVLKVFHHFESSSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMQEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGAT FAK1_RAT Others 1 " FUNCTION: Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity." SUBCELLULAR LOCATION: Cell membrane; cell-matrix junction; focal adhesion; cytoplasmic side. Constituent of focal adhesions. RVLKVFHYFESSNEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQDIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGAT FAK1_XENLA Others 1 " FUNCTION: Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy (By similarity)." SUBCELLULAR LOCATION: Cell membrane; cell-matrix junction; focal adhesion; cytoplasmic side. Constituent of focal adhesions. RVLRVFHYFESNNEPATWSSNIRHGDATDVRGIIQKIVDSHKVKNVASYGLRLSHLHSEEVHWLHPDIGVSHIREKYEQSHPPEEWKYELRIRYLPKGFVNQFTEDKPTLNFFYQQVKNDYMSEIADQVDQEIALKLGCLEIRRSYGEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRYDKECFKCALGSSWIISVELAIGPEEGISYLTDKGSNPTHLADFTQVQTIQYSSSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVSGAS FAK2_HUMAN Human 1 FUNCTION: Involved in calcium induced regulation of ion channel and activation of the map kinase signaling pathway. May represent an important signaling intermediate between neuropeptide activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity. Interacts with the SH2 domain of Grb2. May phosphorylate the voltage-gated potassium channel protein Kv1.2. Its activation is highly correlated with the stimulation of c-Jun N-terminal kinase activity. SUBCELLULAR LOCATION: Cytoplasmic. Interaction with Nephrocystin induces the membrane-association of the kinase. RILKVCFYSNSFNPGKNFKLVKCTVQTEIREIITSILLSGRIGPNIRLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDAKPTCLAEFKQIRSIRCLPLEEGQAVLQLGIEGAPQALSIKTSSLAEAENMADLIDGYCRLQGEHQ FAK2_MOUSE Mouse 1 FUNCTION: Involved in calcium induced regulation of ion channel and activation of the map kinase signaling pathway. May represent an important signaling intermediate between neuropeptide activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity. Interacts with the SH2 domain of Grb2. May phosphorylate the voltage-gated potassium channel protein Kv1.2. Its activation is highly correlated with the stimulation of c-Jun N-terminal kinase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasmic. Interaction with Nephrocystin induces the membrane-association of the kinase. RILKVCFYSNSFNPGKNFKLVKCTVQTEIQEIITSILLSGRIGPNIQLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDTKPTCLAEFKQIRSIRCLPLEETQAVLQLGIEGAPQSLSIKTSSLAEAENMADLIDGYCRLQGEHK FAK2_RAT Others 1 FUNCTION: Involved in calcium induced regulation of ion channel and activation of the map kinase signaling pathway. May represent an important signaling intermediate between neuropeptide activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity. Interacts with the SH2 domain of Grb2. May phosphorylate the voltage-gated potassium channel protein Kv1.2. Its activation is highly correlated with the stimulation of c-Jun N-terminal kinase activity. " SUBCELLULAR LOCATION: Cytoplasmic. Interaction with Nephrocystin induces the membrane-association of the kinase (By similarity). Isoform 2 localizes to focal adhesions, but not isoforms 1 and 3." RILKVCFYSNSFNPGKNFKLVKCTVQTEIQEIITSILLSGRIGPNIQLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDTKPTCLAEFKQIRSIRCLPLEETQAVLQLGIEGAPQSLSIKTSSLAEAENMADLIDGYCRLQGEHK FRM4B_HUMAN Human 1 FUNCTION: Member of GRP1 signaling complexes that are acutely recruited to plasma membrane ruffles in response to insulin receptor signaling. May function as a scaffolding protein (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). RHCQVHLLDDRRLELLVQPKLLARELLDLVASHFNLKEKEYFGITFIDDTGQQNWLQLDHRVLDHDLPKKPGPTILHFAVRFYIESISFLKDKTTVELFFLNAKACVHKGQIEVESETIFKLAAFILQEAKGDYTSDENARKDLKTLPAFPTKTLQEHPSLAYCEDRVIEHYLKIKGLTRGQAVVQYMKIVEALPTYGVHYYAVKDKQGLPWWLGISYKGIGQYDIQDKVKPRKLFQWKQLENLYFREKKFAVEVHDPRRISVSRRTFGQSGLFVQTWYANSSLIKSIWVMAISQHQFYLDRK FRM4B_MOUSE Mouse 1 FUNCTION: Member of GRP1 signaling complexes that are acutely recruited to plasma membrane ruffles in response to insulin receptor signaling. May function as a scaffolding protein. SUBCELLULAR LOCATION: Cytoplasm. RHCQVHLLDDRRLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQENWLQLDHRVLEHDLPKKPGPTLLHFAVRFYIESISFLKDKNTVELFFLNAKACVHKGQIEVDSETIFKLAALVLQESKGDYTSDENARKDLKTLPVFPTKTLQEHPSLAYCEDRVIEHYLKIKGLTRGQAVVQYMKIVEALPTYGVHYYAVKDKQGLPWWLGISYKGIGQYDLQDKVKPRKLFQWKQLENLYFREKKFAVEVHDPRRISVSRRTFGQSGLFVQTWYANSSLIKSIWVMAISQHQFYLDRK MOES_HUMAN Human 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Cytoplasmic. Phosphorylated form is enriched in microvilli-like structures at apical membrane (By similarity). PKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRR MOES_LYTVA Others 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. MPRGVAVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYIDSKGLVTWLKLNKKVVAQDLRKDNPLQFKFRVKFYPEEVTEELIQEITQRLFFLQIKEGILSDEVYCPPETSVLLASYAAQAKYGPHSASTKARLTEDTNILPKRVIEQHKMTKEQWYERVSNWHQEHLSLSKEDAITEYMKIAQDLEMYGVNYFEIRNKKGTDLWLGVDALGLNVYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIEKKAPDFVFYASRLRINKRILALCMGNHELYMRRR MOES_MOUSE Mouse 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Cytoplasmic. Phosphorylated form is enriched in microvilli-like structures at apical membrane. PKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKAFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRR MOES_PIG Others 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Cytoplasmic. Phosphorylated form is enriched in microvilli-like structures at apical membrane (By similarity). PKTINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSSKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRR MOES_RAT Others 1 FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Cytoplasmic. Phosphorylated form is enriched in microvilli-like structures at apical membrane (By similarity). PKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKAFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRR 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." MTSTVHCHGGGSCKITVNSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTIVADVLAKFEKLAATSEVGEQPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHYPAPEENLQVLAALRLQYLQGDYAPHAPVPPLEEVYSLQRLKARISQSTKSFTPGERLEKRRTSFLEGTLRRSFRTGSAIRQKAEEEQMVDMWVKEEVCSARASILDKWKKFQGMSQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQDLWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKR 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." MTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTVVADVLAKFEKLAATSEVGDLPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHHPAPEENLQVLAALRLQYLQGDYTLHAAIPPLEEVYSLQRLKARISQSTKTFTPCERLEKRRTSFLEGTLRRSFRTGSVVRQKVEEEQMLDMWIKEEVSSARASIIDKWRKFQGMNQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKR MYO15_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). May play a role in the formation or maintenance of the actin-rich structures of the inner ear sensory hair cells." SUBCELLULAR LOCATION: Cytoplasm. SKRQLFLLPGGLERHLKIKTCTVALDVVEEICAEMALTRPEAFNEYVIFVVTNRGQHVCPLSRRAYILDVASEMEQVDGGYMLWFRRVLWDQPLKFENELYVTMHYNQVLPDYLKGLFSSVPASRPSEQLLQQVSKLASLQHRAKDHFYLPSVREVQEYIPAQLYRTTAGSTWLNLVSQHRQQTQALSPHQARAQFLGLLSALPMFGSSFFFIQSCSNIAVPAPCILAINHNGLNFLSTETHELMVKFPLKEIQSTRTQRPTANSSYPYVEIALGDVAAQRTLQLQLEQGLELCRVVAVHVENLLSAHEKRLTLPPSEITLL MYO15_MOUSE Mouse 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). May play a role in the formation or maintenance of the actin-rich structures of the inner ear sensory hair cells." SUBCELLULAR LOCATION: Cytoplasm (By similarity). SKRQLSLLPGGLERHLKIKTCTVALDVIEGLCTEMALTRPEAFDEYVIFVVTNRGQHVCPLSCRAYILDVASEMEQVDGGYTLWFRRVLWDQPLKFENELYVTMHYNQVLPDYLKGLFSSVPARQPTEQQLQQVSKLASLQHRAKDHFYLPSVREVQEYIPAQLYHTTAGDTWLNLVSQHRQQTQALSPHQARAQFLGLLSAFPLFGSSFFFIQSCSNVLVPAPCILAVNHNGLNFLSTKTHELIVKIPLKEIQSTWTQKPTANSSYPYVEISLGDVAAQRTMQLQLEQGLELCRVVAVHVESMLSAREERLTLPPSEITLL MYO7A_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. In retina, myosin VIIa might play a role in trafficking of ribbon- synaptic vesicle complexes and renewal of the outer photoreceptors disks. In inner ear, it might maintain the rigidity of stereocilia during the dynamic movements of the bundle. Involved in hair-cell vesicle trafficking of aminoglycosides, which are known to induce ototoxicity (By similarity)." " SUBCELLULAR LOCATION: Cytoplasm (Probable). In the photoreceptor cells, mainly localized in the inner and base of outer segments as well as in the synaptic ending region." IMLPVTFMDGTTKTLLTDSATTAKELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQERNAPWRLFFRKEVFTPWHSPSEDNVATNLIYQQVVRGVKFGEYRCEKEDDLAELASQQYFVDYGSEMILERLLNLVPTYIPDREITPLKTLEKWAQLAIAAHKKGIYAQRRTDAQKVKEDVVSYARFKWPLLFSRFYEAYKFSGPSLPKNDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSRECRVWLSLGCSDLGCAAPHSGWAGLTPAGPCSPCWSCRGAKTTAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLR MYO7A_MOUSE Mouse 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. In retina, myosin VIIa might play a role in trafficking of ribbon- synaptic vesicle complexes and renewal of the outer photoreceptors disks. In inner ear, it might maintain the rigidity of stereocilia during the dynamic movements of the bundle. Involved in hair-cell vesicle trafficking of aminoglycosides, which are known to induce ototoxicity." SUBCELLULAR LOCATION: Cytoplasm (Probable). IMLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQERNAPWRLFFRKEVFTPWHNPSEDNVATNLIYQQVVRGVKFGEYRCEKEDDLAELASQQYFVDYGSEMILERLLSLVPTYIPDREITPLKNLEKWAQLAIAAHKKGIYAQRRTDSQKVKEDVVNYARFKWPLLFSRFYEAYKFSGPPLPKSDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSRECRVLLSLGCSDLGCATCQSGRAGLTPAGPCSPCWSCRGTKMMAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLR PTN3_HUMAN Human 1 FUNCTION: May act at junctions between the membrane and the cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm. VICSIHFLDGVVQTFKVTKQDTGQVLLDMVHNHLGVTEKEYFGLQHDDDSVDSPRWLEASKPIRKQLKGGFPCTLHFRVRFFIPDPNTLQQEQTRHLYFLQLKMDICEGRLTCPLNSAVVLASYAVQSHFGDYNSSIHHPGYLSDSHFIPDQNEDFLTKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELHSGRDLHNLDLMIGIASAGVAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCKNLWKSCVEHHTFFQAKK PTN4_HUMAN Human 1 FUNCTION: May act at junctions between the membrane and the cytoskeleton. VVCNILLLDNTVQAFKVNKHDQGQVLLDVVFKHLDLTEQDYFGLQLADDSTDNPRWLDPNKPIRKQLKRGSPYSLNFRVKFFVSDPNKLQEEYTRYQYFLQIKQDILTGRLPCPSNTAALLASFAVQSELGDYDQSENLSGYLSDYSFIPNQPQDFEKEIAKLHQQHIGLSPAEAEFNYLNTARTLELYGVEFHYARDQSNNEIMIGVMSGGILIYKNRVRMNTFPWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKNLWKACVEHHTFFRLDR RADI_CHICK Others 1 FUNCTION: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane (By similarity). INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVRKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQSKYGDYNKEIHKLGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRR RADI_HUMAN Human 1 FUNCTION: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. " SUBCELLULAR LOCATION: Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively." INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRR RADI_MOUSE Mouse 1 FUNCTION: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. " SUBCELLULAR LOCATION: Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively." INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRR RADI_PIG Others 1 FUNCTION: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. " SUBCELLULAR LOCATION: Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively." INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSIMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRR TLN1_CHICK Others 1 " FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. Talin is a high molecular weight cytoskeletal protein concentrated at regions of cell- substratum contact and, in lymphocytes, at cell-cell contacts." RPLKIRMLDGTVKTVMVDDSKTVTDMLTTICARIGITNYDEYSLVREIMEEKKEEVTGTLKKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTLREQGIDDNETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGYQCQIQFGPHNEQKHKPGFLELKDFLPKEYIKQKGERKIFMAHKNCGNMSEIEAKVRYVKLARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWSLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDIILKKK TLN1_HUMAN Human 1 " FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts (By similarity)." RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKEEITGTLRKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTLREQGVEEHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWNLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDIILKKK TLN1_MOUSE Mouse 1 " FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts." RPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKDEGTGTLRKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTLREQGVEEHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWSLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDIILKKK TYK2_HUMAN Human 1 FUNCTION: Probably involved in intracellular signal transduction by being involved in the initiation of type I IFN signaling. Phosphorylates the interferon-alpha/beta receptor alpha chain. GGLKVLLHWAGPGGGEPWVTFSESSLTAEEVCIHIAHKVGITPPCFNLFALFDAQAQVWLPPNHILEIPRDASLMLYFRIRFYFRNWHGMNPREPAVYRCGPPGTEASSDQTAQGMQLLDPASFEYLFEQGKHEFVNDVASLWELSTEEEIHHFKNESLGMAFLHLCHLALRHGIPLEEVAKKTSFKDCIPRSFRRHIRQHSALTRLRLRNVFRRFLRDFQPGRLSQQMVMVKYLATLERLAPRFGTERVPVCHLRLLAQAEGEPCYIRDSGVAPTDPGPESAAGPPTHEVLVTGTGGIQWWPVEEEVNKEEGSSGSSGRNPQASLFGKKAKAHKAVGQPADRPREPLWAYFCDFRDITHVVLKEHCVSIHRQDNKCLELSLPSRAAALSFVSLVDGYFRLTADSS 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. MTPTYDAHDGSPLSPTSAWFGDSALSEGNPGILAVSQPITSPEILAKMFKPQALLDKAKINQGWLDSSRSLMEQDVKENEALLLRFKYYSFFDLNPKYDAIRINQLYEQAKWAILLEEIECTEEEMMMFAALQYHINKLSIMTSENHLNNSDKEVDEVDAALSDLEITLEGGKTSTILGDITSIPELADYIKVFKPKKLTLKGYKQYWCTFKDTSISCYKSKEESSGTPAHQMNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHLNPDPQLIPEQITTDITPECLVSPRYLKKYKNKQITARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFIARFQGGKKEELIGIAYNRLIRMDASTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEVRLSFICTEVDCKVVHEFIGGYIFLSTRAK 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). MTPTYDAHDGSPLSPTSAWFGDSALSEGNPGILAVSQPVTSPEILAKMFKPQALLDKAKTNQGWLDSSRSLMEQDVKENEALLLRFKYYSFFDLNPKYDAIRINQLYEQAKWALLLEEIECTEEEMMMFAALQYHINKLSIMTSENHLNNSDKEVDEVDAALSDLEITLEGGKTSTILGDITSIPELADYIKVFKPKKLTLKGYKQYWCTFKDTSISCYKSREESSGTPAHQLNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHLNPDPQLIPDQITTDVNPECLVSPRYLKKYKSKQITARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFIARFQGGKREELIGIAYNRLIRMDASTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEVRLSFICTEVDCKVVHEFIGGYIFLSTRAK 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." WLDSSRSLMEQGIQEDEQLLLRFKYYSFFDLNPKYDAVRINQLYEQARWAILLEEIDCTEEEMLIFAALQYHISKLSLSAETQDFAGESEVDEIEAALSNLEVTLEGGKADSLLEDITDIPKLADNLKLFRPKKLLPKAFKQYWFIFKDTSIAYFKNKELEQGEPLEKLNLRGCEVVPDVNVAGRKFGIKLLIPVADGMNEMYLRCDHENQYAQWMAACMLASKGKTMADSSYQPEVLNILSFLRMKNRNSASQVASSLENMDMNPECFVSPRCAKRHKSKQLAARILEAHQNVAQMPLVEAKLRFIQAWQSLPEFGLTYY 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)." WLDSSRSLMEQSIQEDEQLQLRFKYYTFFDLNPKYDAVRINQLYEQARWAVLLEEIDCTEEEMLIFAALQYHISKLSQCAEIQDFATKSEVDEVEAALSSLEVTLEGGKADNTLEDITDIPKLADYLKLFRPKKLMLKACKQYWFVFKDTSIAYFKNKELEQGEPIEKLNLRGCEIVPDVNVSGRKFGIKLLIPVADGMNEVYLRCDHEDQYARWMAACILASKGKTMADSSYQPEVISILSFLKMKNRNSSPLVASSLENMDMNPECLVSPRCAKKHKSKQLAARILEAHHNVAQMPLVEAKLQFIQAWQSLPEFGLTYY URP2_HUMAN Human 1 FUNCTION: Probably involved in cell adhesion (By similarity). SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane-associated in chronic lymphocytic leukemia (CLL) cells. WLDSSRCLMQQGIKAGDALWLRFKYYSFFDLDPKTDPVRLTQLYEQARWDLLLEEIDCTEEEMMVFAALQYHINKLSQSGEVGEPAGTDPGLDDLDVALSNLEVKLEGSAPTDVLDSLTTIPELKDHLRIFRIPRRPRKLTLKGYRQHWVVFKETTLSYYKSQDEAPGDPIQQLNLKGCEVVPDVNVSGQKFCIKLLVPSPEGMSEIYLRCQDEQQYARWMAGCRLASKGRTMADSSYTSEVQAILAFLSLQRTGSGGPGNHPHGPDASAEGLNPYGLVAPRFQRKFKAKQLTPRILEAHQNVAQLSLAEAQLRFIQAWQSLPDFGISYV URP2_MOUSE Mouse 1 FUNCTION: Probably involved in cell adhesion (By similarity). SUBCELLULAR LOCATION: Cytoplasm (Probable). WLDSSRCLMQQGIKAGDVLWLRFKYYSFFDLDPKTDPVRLTQLYEQARWDLLTEEIDCTEEEMMVFAALQYHINKLTLSGDVGELASGDLGLDDLDAALNNLEVKLKGSAPSDMLDSLTTIPELKDHLRIFRPRKLTLKGYRQYWVVFKDTTLSYYKSQDEAPGDPTQQLNLKGCEVVPDVNVSGQKFCIKLLVPSPEGMSEIYLRCQDEQQYAQWMAACRLASKGRTMADSSYASEVQAILAFLSLQRAGGSNGGSGNKPQGPEAPAEGLNPYGLVAPRFQRKFKAKQLTPRILEAHQNVAQLSLTEAQLRFIQAWQSLPDFGISYV E41L1_HUMAN Human 1 " FUNCTION: May function to confer stability and plasticity to neuronal membrane via multiple interactions, including the spectrin-actin-based cytoskeleton, integral membrane channels and membrane-associated guanylate kinases." AICRVTLLDASEYECEVEKHGRGQVLFDLVCEHLNLLEKDYFGLTFCDADSQKNWLDPSKEIKKQIRSSPWNFAFTVKFYPPDPAQLTEDITRYYLCLQLRADIITGRLPCSFVTHALLGSYAVQAELGDYDAEEHVGNYVSELRFAPNQTRELEERIMELHKTYRGMTPGEAEIHFLENAKKLSMYGVDLHHAKDSEGIDIMLGVCANGLLIYRDRLRINRFAWPKILKISYKRSNFYIKIRPGEYEQFESTIGFKLPNHRSAKRLWKVCIEHHTFFRLVS E41L1_MOUSE Mouse 1 " FUNCTION: May function to confer stability and plasticity to neuronal membrane via multiple interactions, including the spectrin-actin-based cytoskeleton, integral membrane channels and membrane-associated guanylate kinases." AICRVTLLDASEYECEVEKHGRGQVLFDLVCEHLNLLEKDYFGLTYCDADSQKNWLDPSKEIKKQIRSSPWNFAFTVKFYPPDPAQLTEDITRYYLCLQLRADIITGRLPCSFVTHALLGSYAVQAELGDYDAEEHVGNYVSELRFAPNQTRELEERIMELHKTYRGMTPGEAEIHFLENAKKLSMYGVDLHHAKDSEGIDIMLGVCANGLLIYRDRLRINRFAWPKILKISYKRSNFYIKIRPGEYEQFESTIGFKLPNHRSAKRLWKVCIEHHTFFRLVS TALA_DICDI Others 1 FUNCTION: Actin-binding protein that may be involved in the control of cell motility and chemotaxis. SUBCELLULAR LOCATION: Cytoplasmic; rapidly assembles at the leading edge of cells in response to chemoattractant. RPQKFKLLDGTIKTQLVDESQNVSEIVNSICKKMGIKNPEEYSLMNSAGAWLNNTQILSEQGISENDITVLMKKFFFNDANIDRNDPVQLHLLFVQCRDGIIEGKYPTQREESLALSALQCQVQLGDYNPTKHEPGFLTLKDYLPLQWLKSKGVEKDIFKEHKKLVSMTEVNAKYRYVQLCRSLKTYGMTSFDVKIREYGKKKMVDHILGITREQMLLMLTETKEVIMTHPLKHIKRWAATDKSFTLDFGDHETEYLILQTPNPEQISQLIGGYIEIIMKAR TYK2_MOUSE Mouse 1 " FUNCTION: Involved in intracellular signal transduction by amplifying type I and type II IFN signaling. Phosphorylates the interferon-alpha/beta receptor alpha chain. Plays an essential role in promoting selective immune responses, including innate host defense mechanisms and specific antiviral activities." LMVLLHWPGPEGGEPWVTFSQTSLTAEEVCIHIAHKVGITPPCLNLFALYNAQAKVWLPPNHILDTSQDMNLYFRMRFYFRNWHGMNPQEPAVYRCGFPGAETSSDRAEQGVQLLDSASFEYLFEQGKHEFMNDVVSLRDLSSEEEIHHFKNESLGMAFLHLCHLALSRGVPLEEMAREISFKNCIPHSFRQHIRQHNVLTRLRLHRVFRRFLRAFRPGHLSQQVVMVKYLATLERLAPRFGSERIPVCHLEVLAQPERDPCYIQNSGQTAGDPGPELPSGPPTHEVLVTGTGGIQWHPLQTQESERGNSRGNPHGSRSGKKPKAPKAGEHLTESPQEPPWTYFCDFQDISHVVLKERRVHIHLQDNKCLLLCLCSQAEALSFVALVDGYFRLTADSS 41_DROME Others 0 FUNCTION: An integral component of the septate junction. May play a role in cell-cell interactions that are necessary for proper development. Vital for embryonic development. SUBCELLULAR LOCATION: Septate junction in the apical-lateral domain of epithelial cells during embryonic and imaginal disk development. ALARVTLLDGSLLDVSIDRKAIGRDVINSICAGLNLIEKDYFGLTYETPTDPRTWLDLEKPVSKFFRTDTWPLTFAVKFYPPEPSQLKEDITRYHLCLQVRNDILEGRLPCTFVTHALLGSYLVQSEMGDYDAEEMPTRAYLKDFKIAPNQTAELEDKVMDLHKTHKGQSPAEAELHYLENAKKLAMYGVDLHPAKDSEGVDIMLGVCASGLLVYRDKLRINRFAWPKILKISYKRHHFYIKIRPGEFEQYESTIGFKLANHRAAKKLWKSCVEHHTFFRLMT E41L2_HUMAN Human 0 VQCKVTLLDGTEYSCDLEKHAKGQVLFDKVCEHLNLLEKDYFGLLFQESPEQKNWLDPAKEIKRQLRNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQDIASGRLPCSFVTHALLGSYTLQAELGDYDPEEHGSIDLSEFQFAPTQTKELEEKVAELHKTHRGLSPAQADSQFLENAKRLSMYGVDLHHAKDSEGVDIKLGVCANGLLIYKDRLRINRFAWPKILKISYKRSNFYIKVRPAELEQFESTIGFKLPNHRAAKRLWKVCVEHHTFYRLVS E41L2_MOUSE Mouse 0 VLAKVTLLDGTEYSCDLEKRAKGQVLFDRVCEHLNLLEKDYFGLLFQDHPEQKNWLDPAKEIKRQLKNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQDIASGRLPCSFVTHALLGSYTLQAEHGDYDPEEYDSIDLGDFQFAPAHTKELEEKVSELHKTHRGLSPAQADSQFLENAKRLSMYGVDLHHAKDSEGVDIKLGVCANGLLIYKDRLRINRFAWPKILKISYKRSNFYIKVRPAELEQFESTIGFKLPNHRAAKRLWKVCVEHHTFYRLVS E41L3_HUMAN Human 0 FUNCTION: Critical growth regulator in the pathogenesis of meningiomas. MQCKVILLDGSEYTCDVEKRSRGQVLFDKVCEHLNLLEKDYFGLTYRDAENQKNWLDPAKEIKKQVRSGAWHFSFNVKFYPPDPAQLSEDITRYYLCLQLRDDIVSGRLPCSFVTLALLGSYTVQSELGDYDPDECGSDYISEFRFAPNHTKELEDKVIELHKSHRGMTPAEAEMHFLENAKKLSMYGVDLHHAKDSEGVEIMLGVCASGLLIYRDRLRINRFAWPKVLKISYKRNNFYIKIRPGEFEQFESTIGFKLPNHRAAKRLWKVCVEHHTFFRLLL E41L4_BRARE Others 0 " FUNCTION: Not known, binds calmodulin." FYCEVLLLDESKLILTTQQQGIKKSTRGSVVLDYVFSHVNLAETEYFGVRYCDRSHQTFWLDPSKTLAEHKDLIATGPPYTLYFGVKFYAEDPGKLKEEITRYQFFLQVKQDVLQGRLPCAFNISAQLAALAIQSELGDYDPYKHTAGYVSEYRFVPDQKEDLEDSIEQIHKTLLGQVPAEAENNYLAIAKTLEMYGVDLHPVFGEKQAEYFLGLTPVGVVVYKNKTQVGKYFWPRITKVYFKETQFELRVLGRDCNETSFFFDAASKTACKNLWKCCVEHHTFFRMPE E41L5_HUMAN Human 0 ITCRVSLLDGTDVSVDLPKKAKGQELFDQIMYHLDLIESDYFGLRFMDSAQVAHWLDGTKSIKKQVKIGSPYCLHLRVKFYSSEPNNLREELTRYLFVLQLKQDILSGKLDCPFDTAVQLAAYNLQAELGDYDLAEHSPELVSEFRFVPIQTEEMELAIFEKWKEYRGQTPAQAETNYLNKAKWLEMYGVDMHVVKARDGNDYSLGLTPTGVLVFEGDTKIGLFFWPKITRLDFKKNKLTLVVVEDDDQGKEQEHTFVFRLDHPKACKHLWKCAVEHHAFFRLRG E41LA_HUMAN Human 0 FYCEVLLLDESKLTLTTQQQGIKKSTKGSVVLDHVFHHVNLVEIDYFGLRYCDRSHQTYWLDPAKTLAEHKELINTGPPYTLYFGIKFYAEDPCKLKEEITRYQFFLQVKQDVLQGRLPCPVNTAAQLGAYAIQSELGDYDPYKHTAGYVSEYRFVPDQKEELEEAIERIHKTLMGQIPSEAELNYLRTAKSLEMYGVDLHPVYGENKSEYFLGLTPVGVVVYKNKKQVGKYFWPRITKVHFKETQFELRVLGKDCNETSFFFEARSKTACKHLWKCSVEHHTFFRMPE E41LA_MOUSE Mouse 0 FYCEVLLLDESKLTLTTQQQGIKKSTKGSVVLDHVFRHINLVEIDYFGLRYCDRSHQTYWLDPAKTLAEHKELINTGPPYTLYFGIKFYAEDPCKLKEEITRYQFFLQVKQDALQGRLPCPVNIAAQMGAYAIQAELGDHDPYKHTAGYVSEYRFVPDQKEELEEAIERIHKTLMGQAPSEAELNYLRTAKSLEMYGVDLHPVYGENKSEYFLGLTPSGVVVYKNKKQVGKYFWPRITKVHFKETQFELRVLGKDCNETSFFFEARSKTACKHLWKCSVEHHTFFRMPD E41LB_HUMAN Human 0 LYCRVFLLDGTEVSVDLPKHAKGQDLFDQIVYHLDLVETDYFGLQFLDSAQVAHWLDHAKPIKKQMKIGPAYALHFRVKYYSSEPNNLREEFTRYLFVLQLRHDILSGKLKCPYETAVELAALCLQAELGECELPEHTPELVSEFRFIPNQTEAMEFDIFQRWKECRGKSPAQAELSYLNKAKWLEMYGVDMHVVRGRDGCEYSLGLTPTGILIFEGANKIGLFFWPKITKMDFKKSKLTLVVVEDDDQGREQEHTFVFRLDSARTCKHLWKCAVEHHAFFRLRT IFHKVYFPDDTDEAFEVESSTKAKDFCQNIATRLLLKSSEGFSLFVKIADKVISVPENDFFFDFVRHLTDWIKKARPIKDGIVPSLTYQVFFMKKLWTTTVPGKDPMADSIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPKLLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPKTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKMDDLLTSYISQMLTAM E41LB_MOUSE Mouse 0 LYCRVFLLDGTEVSVDLPKHAKGQDLFDQIVYHLDLVETDYFGLQFLDSAQVTHWLDHAKPIKKQMKVGPAYALHFRVKYYSSEPNNLREEFTRYLFVLQLRHDILSGKLKCPYETAVELAALCLQAELGECELPEHTPELVSEFRFIPNQTEAMEFDIFQRWKEYRGKSPAQAELSYLNKAKWLEMYGVDMHVVRGRDGCEYSLGLTPTGILIFEGANKIGLFFWPKITKMDFKKSKLTLVVVEDDDQGREQEHTFVFRLDSARTCKHLWKCAVEHHAFFRLRT IFHKVYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKVISVPENDFFFDFVRHLTDWIKKARPIKDGIVPSLTYQVFFMKKLWTTTVPGKDPMADSIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPKLLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPRTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKMDDLLTSYISQMLTAM EXPA_DROME Others 0 FUNCTION: Involved in the control of cell proliferation in imaginal disks. May bind to certain proteins of signal transduction pathways by interaction with their SH3 domains. SUBCELLULAR LOCATION: Apical surface of disk cells. RFLALRLLGQQQPKTLYFLVDAKSRVREVYTQTCLHFATQGMLDTELFGLAVLIDGEYMFADPESKLSKYGPKSWRSSHTHGLDANGRPLLELHFRVQFYIESPFMLKDETSRHNYYLQLRHNILQRDLPREQAEQALVFLAGLALQADLGDAPPGTSNSKDDSGEETSASPSNGGRGLSATTTLPKISKRANERMLRLSTYVASTSKRETIPLPPSLPPNGADYYRIEDYLPSGLHTPWARSAMRACHREHLGMATAEAELLYIQQACSLHETINAHTYRMRLAKSEQGSGSAWFVVYAKGIKILGGESTNSSSNPETTTFLWPNITKLSFERKKFEIRSGESRITLYAASDEKNKLLLTLCKDTHQWSMKLA FARP1_HUMAN Human 0 FUNCTION: May function as Rho-guanine nucleotide exchange factor (By similarity). VSIKIQMLDDTQEAFEVPQRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYIPQQDALEDKIVEFHHNHIGQTPAESDFQLLEIARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDANSAYQDTLEFLMASRDFCKSFWKICVEHHAFFRLFE FARP1_PONPY Others 0 FUNCTION: May function as Rho-guanine nucleotide exchange factor (By similarity). VSIKIQMLDDTQEAFEVPQRAPGKVLLDAVCNHLNLVEGDYFGLECPDHKKITVWLDLLKPLVKQIRRPKHVVVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYIPQQDALEDKIVEFHHNHIGQTPAESDFQLLEIARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDANSAYQDTLEFLMASRDFCKSFWKICVEHHAFFRLFE FARP2_HUMAN Human 0 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). LHLRVKLLDNTMEIFDIEPKCDGQVLLTQVWKRLNLVECDYFGMEFQNTQSYWIWLEPMKPIIRQIRRPKNVVLRLAVKFFPPDPGQLQEEYTRYLFALQLKRDLLEERLTCADTTAALLTSHLLQSEIGDYDETLDREHLKVNEYLPGQQHCLEKILEFHQKHVGQTPAESDFQVLEIARKLEMYGIRFHMASDREGTKIQLAVSHMGVLVFQGTTKINTFNWSKVRKLSFKRKRFLIKLHPEVHGPYQDTLEFLLGSRDECKNFWKICVEYHTFFRLLD FARP2_MOUSE Mouse 0 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. MRIRVKLLDSTVELFDIEPKCDGQVLLTQVWKHLNLIECDYFGLEFKNVQSYWIWLEPMKPIIRQVRKPKNAVLRLAVKFFPPDPGQLQEEYTRYLFALQLKRDLLEERLTCTANTAALLISHLLQSEIGDYDETLDREHLKANEYLPNQEKSLEKILDFHQRHTGQTPAESDFQVLEIARKLEMYGIRFHMASDREGTKINLAVSHMGVLVFQGTTKINTFNWSKVRKLSFKRKRFLIKLHPEVHGPYQDTLEFLLGSRDECKNFWKICVEYHTFFRLSD FRM4A_HUMAN Human 0 RRCQVHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHDFPKKSGPVVLYFCVRFYIESISYLKDNATIELFFLNAKSCIYKELIDVDSEVVFELASYILQEAKGDFSSNEVVRSDLKKLPALPTQALKEHPSLAYCEDRVIEHYKKLNGQTRGQAIVNYMSIVESLPTYGVHYYAVKDKQGIPWWLGLSYKGIFQYDYHDKVKPRKIFQWRQLENLYFREKKFSVEVHDPRRASVTRRTFGHSGIAVHTWYACPALIKSIWAMAISQHQFYLDRK FRM4A_MOUSE Mouse 0 RRCQVHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHDFPKKSGPVVLYFCVRFYIESISYLKDNATIELFFLNAKSCIYKELIDVDSEVVFELASYILQEAKGDFSSNEVVRSDLKKLPALPTQALKEHPSLAYCEDRVIEYYKKLNGQTRGQAIVNYMSIVESLPTYGVHYYAVKDKQGIPWWLGLSYKGIFQYDYHDKVKPRKIFQWRQLENLYFREKKFSVEVHDPRRASVTRRTFGHSGIAVHTWYACPALIKSIWAMAISQHQFYLDRK FRMD6_HUMAN Human 0 RSVCIFLPNDESLNIIINVKILCHQLLVQVCDLLRLKDCHLFGLSVIQNNEHVYMELSQKLYKYCPKEWKKEASKVRQYEVTWGIDQFGPPMIIHFRVQYYVENGRLISDRAARYYYYWHLRKQVLHSQCVLREEAYFLLAAFALQADLGNFKRNKHYGKYFEPEAYFPSWVVSKRGKDYILKHIPNMHKDQFALTASEAHLKYIKEAVRLDDVAVHYYRLYKDKREIEASLTLGLTMRGIQIFQNLDEEKQLLYDFPWTNVGKLVFVGKKFEILPDGLPSARKLIYYTGCPMRSRHLLQLLSNSHRLYMNLQ FRMD6_MOUSE Mouse 0 RRVCIFLPNDKSVSIIINVKILCHQLLVQVCDLLRLKDSHLFGLSVIQNNEHVYMELSQKLYKYCPKEWKKEASKVRQYEVTWGIDQFGPPMIIHFRVQYYVENGKLISDRIARYYYYWHLRKQVLHSQCVLREEAYFLLAAFALQADLGNFKRKLHHGDYFEPEAYFPAWVVSKRGKDYILKHIPNMHKDQFALTASEAYLKYIKEAVRLDDVAIHYYRLYKDKREAEGSLTLGLTMRGIQIFQNLEEEKQLLYDFPWTNVGKLVFVGKKFEILPDGLPSARKLVYYTGCPTRSRHLLQLLSNSHRLYMNLQ FRMD6_RAT Others 0 RRVCIFLPNDKSVSIIINVKILCHQLLVQVCDLLRLKDSHLFGLSVIQNNEHVYMELSQKLYKYCPKEWKKEASKGIDQFGPPMIIHFRVQYYVENGKLISDRIARYYYYWHLRKQVLHSQCVLREEAYFLLAAFALQADLGNFKRKVHHGDYFEPEAYFPAWVVSKRGKDYILKHIPNMHRDQFALTASEAYLKYIKEAVRLDDVAIHYYRLYKDKREVEGSLTLGLTMRGIQIFQNLEEEKQLLYDFPWTNVGKLVFVGKKFEILPDGLPSARKLVYYTGCPTRSRHLLQLLSNSHRLYMNLQ MERL_HUMAN Human 0 FUNCTION: Probably acts as a membrane stabilizing protein. May inhibit PI3 kinase by binding to CENTG1 and impairing its stimulating activity. " SUBCELLULAR LOCATION: In a fibroblastic cell line, isoforms 1 and 10 are found homogenously distributed over the entire cell, with a particularly strong staining in ruffling membranes and filopodia. Isoform 10 is also found in the nucleus. Isoforms 7, 9 and 10 are observed in cytoplasmic granules concentrated in a perinuclear location. Isoforms 7 and 9 are absent from ruffling membranes and filopodia." FTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRR MERL_MOUSE Mouse 0 FUNCTION: Probably acts as a membrane stabilizing protein. May inhibit PI3 kinase by binding to CENTG1 and impairing its stimulating activity. FTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRR MERL_PAPAN Others 0 FUNCTION: Probably acts as a membrane stabilizing protein. May inhibit PI3 kinase by binding to CENTG1 and impairing its stimulating activity. FTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRR MERL_RAT Others 0 FUNCTION: Probably acts as a membrane stabilizing protein. May inhibit PI3 kinase by binding to CENTG1 and impairing its stimulating activity. FTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRR MYLIP_BRARE Others 0 FUNCTION: E3 ubiquitin ligase protein that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC) (By similarity). Required during embryogenesis. SUBCELLULAR LOCATION: Cytoplasm (Probable). MLCHVTRPDAVVMEIEVDAKANGEDCLNKVCRKLGIIEVDYFGLQFSGSKGENLWLNLRNRISQQMDNLTPCRLRLRVKFFVEPHLILQEQTRHLFFMHVKEDLHRGHLRMCSEQAQELSALLAQAEFGDYNQNTAKYWYTELCGSEPNQTTINSIIAKHKALEGLSQASVEYQALQLVSSLEHYGVEWHWARDAEAQRLAIGVGPEGIAICRDDFSLVNRISYPIIQIATQSGKSVYLTVTKESSDSVVLLFKLISNRAASGLYRAITETHAFYRCDT MYLIP_HUMAN Human 0 FUNCTION: E3 ubiquitin ligase protein that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC). Stable or transient overexpression of MIR induces proteasomal degradation of MRLC inhibiting neurite outgrowth in presence of NGF. MIR counteracts the stabilization of MRLC by MIR- interacting saposin-like protein (MSAP/TMEM4) and reduces MSAP- stimulated neurite outgrowth. SUBCELLULAR LOCATION: Cytoplasm (Probable). MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKEALLAGHLLCSPEQAVELSALLAQTKFGDYNQNTAKYNYEELCAKELSSATLNSIVAKHKELEGTSQASAEYQVLQIVSAMENYGIEWHSVRDSEGQKLLIGVGPEGISICKDDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDT MYLIP_MOUSE Mouse 0 FUNCTION: E3 ubiquitin ligase protein that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC). Stable or transient overexpression of MIR induces proteasomal degradation of MRLC inhibiting neurite outgrowth in presence of NGF. MIR counteracts the stabilization of MRLC by MIR- interacting saposin-like protein (MSAP/TMEM4) and reduces MSAP- stimulated neurite outgrowth (By similarity). SUBCELLULAR LOCATION: Cytoplasm (Probable). MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKESLLAGHLQCSPEQAVELSALLAQTKFGDYNQNTAQYSYEDLCEKELSSSTLNSIVAKHKELEGISQASAEYQVLQIVSAMENYGIEWHAVRDSEGQKLLIGVGPEGISICKEDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDT PTN13_HUMAN Human 0 FUNCTION: Regulates negatively FAS-induced apoptosis and NGFR- mediated pro-apoptotic signaling. SUBCELLULAR LOCATION: Cytoplasm (By similarity). RKVNIMLLNGQRLELTCDTKTICKDVFDMVVAHIGLVEHHLFALATLKDNEYFFVDPDLKLTKVAPEGWKEEPKKKTKATVNFTLFFRIKFFMDDVSLIQHTLTCHQYYLQLRKDILEERMHCDDETSLLLASLALQAEYGDYQPEVHGVSYFRMEHYLPARVMEKLDLSYIKEELPKLHNTYVGASEKETELEFLKVCQRLTEYGVHFHRVHPEKKSQTGILLGVCSKGVLVFEVHNGVRTLVLRFPWRETKKISFSKKKITLQNTSDGIKHGFQTDNSKICQYLLHLCSYQHKFQLQMR PTN13_MOUSE Mouse 0 FUNCTION: Regulates negatively FAS-induced apoptosis and NGFR- mediated pro-apoptotic signaling. SUBCELLULAR LOCATION: Cytoplasm (By similarity). RKVNIRLLSGQRLELTCDTKTICKDVFDMVVAHIGLVEHHLFALATRKENEYFFVDPDLKLTKVAPEGWKEEPKRKGKAAVDFTLFFRIKFFMDDVSLIQHDLTCHQYYLQLRKDLLDERVHCDDEAALLLASLALQAEYGDYQPEVHGVSYFRLEHYLPARVMEKLDVSYIKEELPKLHNTYAGASEKETELEFLKVCQRLTEYGVHFHRVHPEKKSQTGILLGVCSKGVLVFEVHNGVRALVLRFPWRETKKISFSKKKITLQNTSDGIKHAFQTDSSKACQYLLHLCSSQHKFQLQMR PTN14_HUMAN Human 0 FVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFFGVMFYVPNVSWLQQEATRYQYYLQVKKDVLEGRLRCTLDQVIRLAGLAVQADFGDYNQFDSQDFLREYVLFPMDLALEEAVLEELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIFPVKDNHGNCVHLGIFFMGIFVRNRIGRQAVIYRWNDMGNITHNKSTILVELINKEETALFHTDDIENAKYISRLFATRHKFYKQNK PTN14_MOUSE Mouse 0 FUNCTION: May be involved in the regulation of T-cell development. FVARIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFFGVMFYVPNVSRLQQEATRYQYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDSQEFLREYVLFPMDLAMEEAALEELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIFPVKDSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDKEETALFHTDDIENAKYISRLFTTRHKFYKQNK PTN21_HUMAN Human 0 LVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKYALEPTVYFGVVFYVPSVSQLQQEITRYQYYLQLKKDILEGSIPCTLEQAIQLAGLAVQADFGDFDQYESQDFLQKFALFPVGWLQDEKVLEEATQKVALLHQKYRGLTAPDAEMLYMQEVERMDGYGEESYPAKDSQGSDISIGACLEGIFVKHKNGRHPVVFRWHDIANMSHNKSFFALELANKEETIQFQTEDMETAKYIWRLCVARHKFYRLNQ PTN21_MOUSE Mouse 0 FUNCTION: May be involved in the regulation of growth and differentiation of liver cells. LVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREVTYFSLWYYNKQNQRRWVDLEKPLKKQLDKHALEPTVYFGVLFYVPSVSQLQQEITRYQYYLQLKKDILEGNLPCTLEHAIQLAGLAVQADFGDFDQYESQDFLQKFALLPVAWLQDEKVLEEAAQKVALLHQKYRGLTAPEAELLYMQEVERMDGYGEESYPAKDSQGSDISIGACLDGIFVKHKNGRPPVVFRWHDIANMSHNKSFFALELANKEETIQFQTEDMETAKYVWRLCVARHKFYRLNQ PTN21_RAT Others 0 LVARIQLLNNEFVEFTLSVESTGQESLEAVAQRLELREITYFSLWYYNKQNQRRWVDLEKPLKKQLDKHALEPTVYFGVVFYVPSVSQLQQEITRYQYYLQLKKDVLEGNLPCTLEQAIQLAGLAVQADFGDFDQYESQDFLQKFALLPVGWLQDEKLLEEAAQKVALLHQKYRGLTAPEAEMLYMQEVERMDGYGEESYPAKDSQGSDISIGACLDGIFVKHKNGRPPVVFRWHDIANMSHNKSFFALELANKEETIQFQTEDMETAKYVWRLCVARHKFYRLNQ PTP1_CAEEL Others 0 IRCTVTFLDSTSYHFEIEKNSLGIVLLEKVFNYLEIIEKDYFGLVFIAVDNSSAQQKKWLDPSKNLRKQMICPPYHLFFRVKFYVRDPNRLRDEFTRFQFYQQVRQNLEEGRLPCNEGSLALLASYVVQAEVGDFEEKTHGMSRTCLCYKIQFATLPDDFSDRVAELHQLHIGQTPDVAEQNFLDHARRLEMYGMDVYDGVDANHLPIEIGVGAVGIKVFHEGIKMNEYAWVRIRKLSFKKKQFQVLVANEDGVSETIMIFNIMSAKICKLLWKCCIEQHTFFRLKT TLN2_HUMAN Human 0 " FUNCTION: As a major component of focal adhesion plaques that links integrin to the actin cytoskeleton, may play an important role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques and strongly activates its kinase activity (By similarity)." SUBCELLULAR LOCATION: Focal adhesion plaques and synapses. RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKLHTDDDLNWLDHSRTFREQGVDENETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGAEKRIFQAHKNCGEMSEIEAKVKYVKLARSLRTYGVSFFLVKEKMKGKNKLVPRLLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAASPKSFTLDFGEYQESYYSVQTTEGEQISQLIAGYIDIILKKK TLN2_MOUSE Mouse 0 " FUNCTION: As a major component of focal adhesion plaques that links integrin to the actin cytoskeleton, may play an important role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques and strongly activates its kinase activity (By similarity)." SUBCELLULAR LOCATION: Focal adhesion plaques and synapses (By similarity). RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKLHTDDDLNWLDHSRTFREQGVDENETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGAEKRIFQEHKNCGEMSEIEAKVKYVKLARSLRTYGVSFFLVKEKMKGKNKLVPRLLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAASPKSFTLDFGEYQESYYSVQTTEGEQISQLIAGYIDIILKKK Y34F_DROME Others 0 HAIPVHMMNSTYQVVSFDGSTTIEEFQATLAHELGTRDATNGFCLFSDDPIEKDLEHYLEPLAKLCDVISKWETALREKGSGKFENSRVIQLSYKNRLYWKHTIKCETDKERLLLCYQTNSQIVQGRFPLSRELALELASLMSQIDMGDYSLEKSRDVGVGLKGLDKFYPYRYRDALGAEQLKDVQELLVSKWMLLKGRSTLDCVRIYLTCCRKWPYFGACLFQAKPRQSPESNTASGATPVAWLAVAEDALNVLELSTMAPVARYPYSSVMTFGGCQDDFMLVVSHDDGGGGEQKLLFAMSKPKILEITLLIADYMNALGHTV UN112_DROME Others 0 FUNCTION: Probably involved in cell adhesion (By similarity). SUBCELLULAR LOCATION: Cytoplasm (Probable). WLDSSLSIMEQGVREYDTLCLRFKYFTFFDLNPKYDQVRINQLYEQAKWSILNEELEPTEEETLMFAALQFQVNHQTDLHPPGIDSGIDTSSQETGGEDDIDSALNELQITLEGPGGGKDQGNITRIPELSDYLKFLKPQRFTLKGYKRYFFTYRDLHLHLYKSQDESRRGAPTISINLKGCEVTPDVNLAQGKFAIRLEVPSEIRNGPNSEVWVRCDNEEQYAKWMAACRLAAKGRSLADSSYDSEVSSIRSLLQMQKPAQGAPLTVNPRSVEPMDYLSPKMMRKLSSKAVQRILEAHANVRQLSLMDAKMKYIQAWQSLPDFGVTLF