wanglab/gogpt-training-data huggingface dataset:
Protein: Importin subunit alpha-5 (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta) [Cleaved into: Importin subunit alpha-5, N-terminally processed] (P52294)
Organism: Homo sapiens (Human)
Function: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7604027, ECO:0000269|PubMed:7892216}. Nucleus {ECO:0000269|PubMed:7604027, ECO:0000269|PubMed:7892216}.
Interaction partners:
- Importin subunit beta-1
- Signal transducer and activator of transcription 1-alpha/beta
- Exportin-2
- Nuclear pore complex protein Nup50
- Importin subunit alpha-3
- Transcription factor p65
- Importin subunit alpha-4
- Nuclear factor NF-kappa-B p105 subunit
- Telomerase reverse transcriptase
- Transcription factor SOX-2
Sequence:
MTTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQISNMEMAPGGVITSDMIEMIFSKSPEQQLSATQKFRKLLSKEPNPPIDEVISTPGVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRIVIQAGAVPIFIELLSSEFEDVQEQAVWALGNIAGDSTMCRDYVLDCNILPPLLQLFSKQNRLTMTRNAVWALSNLCRGKSPPPEFAKVSPCLNVLSWLLFVSDTDVLADACWALSYLSDGPNDKIQAVIDAGVCRRLVELLMHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALQSLLHLLSSPKESIKKEACWTISNITAGNRAQIQTVIDANIFPALISILQTAEFRTRKEAAWAITNATSGGSAEQIKYLVELGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQEAKRNGTGINPYCALIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGTEDEDSSIAPQVDLNQQQYIFQQCEAPMEGFQL
Protein: E2F-associated phosphoprotein (EAPP) (Q56P03)
Organism: Homo sapiens (Human)
Function: May play an important role in the fine-tuning of both major E2F1 activities, the regulation of the cell-cycle and the induction of apoptosis. Promotes S-phase entry, and inhibits p14(ARP) expression.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Pre-mRNA-processing-splicing factor 8
- 116 kDa U5 small nuclear ribonucleoprotein component
- Protein AAR2 homolog
- U5 small nuclear ribonucleoprotein TSSC4
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- CD2 antigen cytoplasmic tail-binding protein 2
- Probable ATP-dependent RNA helicase DDX23
- G patch domain-containing protein 1
- Probable ATP-dependent RNA helicase DHX35
- Protein ecdysoneless homolog
Sequence:
MNRLPDDYDPYAVEEPSDEEPALSSSEDEVDVLLHGTPDQKRKLIRECLTGESESSSEDEFEKEMEAELNSTMKTMEDKLSSLGTGSSSGNGKVATAPTRYYDDIYFDSDSEDEDRAVQVTKKKKKKQHKIPTNDELLYDPEKDNRDQAWVDAQRRGYHGLGPQRSRQQQPVPNSDAVLNCPACMTTLCLDCQRHESYKTQYRAMFVMNCSINKEEVLRYKASENRKKRRVHKKMRSNREDAAEKAETDVEEIYHPVMCTECSTEVAVYDKDEVFHFFNVLASHS
Protein: Sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3bl (M9MM97)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Neuropilin
- Plexin D1.
- Neuropilin-1a
- Plexin-A4
Sequence:
MELPVLVLVALVLPLSSCTKVNVPRLRLTHKDLLDTNRTSVFNGLHGDLHLSAVFLDEYHDRLFLGGKDVLYSLRLDHTHDAKEIHWPSLPGNREDCILKGKDPEMECANFVRLLQPFNRTHLLACGTGAFQPVCAYVNVGHRGEHVFSLDQTTVQNGRGRCPHDPKLPFASTFTGGELYTGLTADFLGRDSVISRGFGTRSPMRTETDQRILHEPRFVAAHLIPDSADRDDDKIYFFFTERATETAERDDDGAIHTRIGRLCANDVGGQRVLVNKWSTFIKARLVCSVPGPHGIQTHFHQLEDVFLLRTKDETNPEIYAIFSTISNVFQGYAVCVYSMADIREAFNGPFAHKEGPDYQWGPYEGRVPYPRPGVCPSKITAQPGRAFRSTLEFPDTVLQFARTHPLMWRPVYPSHRQPLLLRTGAPYRLTHITVDRTQAEDGYYDVMFIGTDIGTVLKVIVLGKGNSLAGEEITLEEMQVFKVPTPITSMDISVKRQTLFVGSQTAVVQVPLHRCSMYGKACAECCLARDPYCAWDGQTCTRYLPNTKRRYRRQDIKHANPAVQCMDQNLSVEDVDLSEERVVYGTENNSTFLECVPRSPQATVTWHIQRDDYLGEVVFDERIIKTDDGLLFRRVLRQDEGIYVCRSREHGFTQTLSRFWLDVLNADTLSDLLSRDSKYKVWSPCPANSATMNRGPARAWFKDVLQLIGPSNLPQVEQYCERVWCNEKLRRKHKSMMDKYRQAQDSARRARVQKSTGESRHRSPRDVHTQQ
Protein: Guanine-nucleotide exchange factor YEL1 (EFA6-like protein 1) (P34225)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Guanine-nucleotide exchange factor for ARF3 required for localization of ARF3 to the bud neck and tip and involved in actin patch polarization.
Subcellular location: Cytoplasm. Cell membrane; Peripheral membrane protein. Bud neck. Bud tip. Note=Localizes at the cell membrane only at the bud neck and bud tip and this localization is ARF3-dependent.
Interaction partners:
- ADP-ribosylation factor 3
- Arf guanine nucleotide exchange factor SYT1
- ADP-ribosylation factor-like protein 1
- ARF3-interacting protein 1
- ARF guanine-nucleotide exchange factor 1
- ADP-ribosylation factor 2
- ARF guanine-nucleotide exchange factor 2
- ADP-ribosylation factor 1
Sequence:
MCASLNEVKKNDTYGVSQKGYNDNFSESEGVLHGSKSMPTSMKNMLQSPTMVNMCDILQNKEAANDEKPVIPTTDTATAGTGTEDISSTQSEETDQNSHLIASEILEGTFKDVSYKEYANFLGNDNNNQVLTEFVKLLSPLPSSLLETLFNLSKSIYFIAEAQNIDRILECLSIEWIACHPNTHWKSGYKSCHIVLFSLLILNSDLHNNFQVDHKKIKFSMVAFINNTLRALREENEYEELKIYSREHLIIEELSEYYKTLNETPLPLCTESRTSINISDNQSSLKRFSTLGSREFSTSNLRSVNSNSTTLYSRDGQVSVREMSAKSNKNFHNNHPMDALYLKESFDDGLITENGSSWFMDDLILISKKSLPRKYSKRDKDQVAAPKMTSKRNKSFFGWLKPSKTTTLIEHTSRRTSLSYLNKDSEWERVKIQVKEGRIFIFKIKPDVKDIIQSSETDSATIDYFKDISSSYFAYSLLEAEAHVVQDNIIIGSGAMKSNVCNKNTKRKSGNFTVSFPENINGPKLVLEFQTRSVEEAHKFMDCINFWAGRISPVPLTQFEAVSNAEYGWSDKILTEHASLNLKNIVVSEWKPLLGLELLYEDAKDVEMVELKERLKELMNFTRQLGIWIDKHNEIKDKLVEIWSFDDNYFEAVMNNWNSRYLYMNNQYKKRLSYLKALQKAMGSVQF
Protein: T-cell surface antigen CD2 (Q53F96)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MSFPCKFVASFLLIFNVSSKGAVSKEITNALETWGALGQDINLDIPSFQMSDDIDDIKWEKTSDKKKIAQFRKEKETFKEKDTYKLFKNGTLKIKHLKTDDQDIYKVSIYDTKGKNVLEKIFDLKIQERVSKPKISWTCINTTLTCEVMNGTDPELNLYQDGKHLKLSQRVITHKWTTSLSAKFKCTAGNKVSKESSVEPVSCPEKGLDIYLIIGICGGGSLLMVFVALLVFYITKRKKQRSRRNDEELETRAHRVATEERGRKPHQIPASTPQNPATSQHPPPPPGHRSQAPSHRPPPPGHRVQHQPQKRPPAPSGTQVHQQKGPPLPRPRVQPKPPHGAAENSLSPSSN
Protein: Potassium voltage-gated channel subfamily A member 4 (Voltage-gated potassium channel subunit Kv1.4) (Q61423)
Organism: Mus musculus (Mouse)
Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA4 forms a potassium channel that opens in response to membrane depolarization, followed by rapid spontaneous channel closure. Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:8020965}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P15385}.
Interaction partners:
- Disks large homolog 4
- Potassium voltage-gated channel subfamily A member 1
- Voltage-gated potassium channel subunit beta-2
- Voltage-gated potassium channel subunit beta-1
- Potassium voltage-gated channel subfamily A member 2
- A-type potassium channel modulatory protein KCNIP2
- Ubiquitin-like protein FUBI
- A-type potassium channel modulatory protein DPP6
- Voltage-gated potassium channel subunit beta-3
- Potassium voltage-gated channel subfamily A member 5
Sequence:
MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGTGGSGGGPHHHHQTRGAYSSHDPQGSRGSRRRRRQRTEKKKLHHRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEEDHGDGCSYTDLLPQDDGGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLIMALSAGGHSRLLNDTSAPHLENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFITLGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMRELGLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCGKEEKCQGKGDESETDKNNCSNAKAVETDV
Protein: Myosin-binding protein C, slow-type (Slow MyBP-C) (C-protein, skeletal muscle slow isoform) (Q00872)
Organism: Homo sapiens (Human)
Function: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. Slow skeletal protein that binds to both myosin and actin. In vitro, binds to native thin filaments and modifies the activity of actin-activated myosin ATPase. May modulate muscle contraction or may play a more structural role.
Interaction partners:
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Filamin-C
- Myosin-3
- Titin
- Myosin-8
- Kyphoscoliosis peptidase
- Myosin light chain 3
- Troponin I, fast skeletal muscle
- Troponin T, fast skeletal muscle
Sequence:
MPEPTKKEENEVPAPAPPPEEPSKEKEAGTTPAKDWTLVETPPGEEQAKQNANSQLSILFIEKPQGGTVKVGEDITFIAKVKAEDLLRKPTIKWFKGKWMDLASKAGKHLQLKETFERHSRVYTFEMQIIKAKDNFAGNYRCEVTYKDKFDSCSFDLEVHESTGTTPNIDIRSAFKRSGEGQEDAGELDFSGLLKRREVKQQEEEPQVDVWELLKNAKPSEYEKIAFQYGITDLRGMLKRLKRMRREEKKSAAFAKILDPAYQVDKGGRVRFVVELADPKLEVKWYKNGQEIRPSTKYIFEHKGCQRILFINNCQMTDDSEYYVTAGDEKCSTELFVREPPIMVTKQLEDTTAYCGERVELECEVSEDDANVKWFKNGEEIIPGPKSRYRIRVEGKKHILIIEGATKADAAEYSVMTTGGQSSAKLSVDLKPLKILTPLTDQTVNLGKEICLKCEISENIPGKWTKNGLPVQESDRLKVVHKGRIHKLVIANALTEDEGDYVFAPDAYNVTLPAKVHVIDPPKIILDGLDADNTVTVIAGNKLRLEIPISGEPPPKAMWSRGDKAIMEGSGRIRTESYPDSSTLVIDIAERDDSGVYHINLKNEAGEAHASIKVKVVDFPDPPVAPTVTEVGDDWCIMNWEPPAYDGGSPILGYFIERKKKQSSRWMRLNFDLCKETTFEPKKMIEGVAYEVRIFAVNAIGISKPSMPSRPFVPLAVTSPPTLLTVDSVTDTTVTMRWRPPDHIGAAGLDGYVLEYCFEGSTSAKQSDENGEAAYDLPAEDWIVANKDLIDKTKFTITGLPTDAKIFVRVKAVNAAGASEPKYYSQPILVKEIIEPPKIRIPRHLKQTYIRRVGEAVNLVIPFQGKPRPELTWKKDGAEIDKNQINIRNSETDTIIFIRKAERSHSGKYDLQVKVDKFVETASIDIQIIDRPGPPQIVKIEDVWGENVALTWTPPKDDGNAAITGYTIQKADKKSMEWFTVIEHYHRTSATITELVIGNEYYFRVFSENMCGLSEDATMTKESAVIARDGKIYKNPVYEDFDFSEAPMFTQPLVNTYAIAGYNATLNCSVRGNPKPKITWMKNKVAIVDDPRYRMFSNQGVCTLEIRKPSPYDGGTYCCKAVNDLGTVEIECKLEVKVIAQ
Protein: SHSP domain-containing protein (Q17849)
Organism: Caenorhabditis elegans
Interaction partners:
- MAP kinase-activated protein kinase mak-1
- MAP kinase-activated protein kinase mak-2
- BAG domain-containing protein
- J domain-containing protein
- Heat shock protein 90
- Heat shock protein 110
Sequence:
MPTYTRTYSYSKREMSERRIDVNRSNYSVIDNEFGNMRDRFEQEMRRVEEEMKRLRSEFEGYRPNGGPPAAISNQPYNAYSNTSSHHETSNRTGGFGSPLPPPSFHGPSDLMAHRPTYDPYLDNLKSPLIKDESDGKTLRLRFDVANYKPEEVTVKTIDNRLLVHAKHEEKTPQRTVFREYNQEFLLPRGTNPEQISSTLSTDGVLTVEAPLPQLAIQQ
Protein: FI06002p (Reduction in Cnn dots 7, isoform A) (Reduction in Cnn dots 7, isoform B) (Q9VW08)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Male sterile
- Male sterile
- GH07076p
- FI21919p1
- Male-specific sperm protein Mst84Dc
- AT14039p
- Sex-regulated protein janus-B
- FI13205p
- LP03867p
- GEO12122p1
Sequence:
MENPINFKDIPSEMPQPKRIQLEGETSVAEAINFLKTQCDTRKEHKPEEFQQDGPTVADELNARLAMVHVRETRAKRIRRLVKFSPNETQALYRFICVCPRYHPCYVPCQHTGQIIIDRDVLSREEHICFLATPKKDFSSPQLAKQARYYTKKIYVNQCTARVERLADPHPMRVSDTYNFFKDYLSPRHIAALENQMKPKPPVEAMSMEKALEYMEEEMRQRKAAKRVQKRRCKGLKKRIILRQRKQMQKIICVLFEEMKDFLLNDQFIVDENSPLCCVILERLREFTDQEFYTTSNLQEYQRILANNLTVWVNKFISNLNIYLTPQQIPVKRQMMAENDPEQFVPLSDFISVSDEADAEEMMNDVEHGAAEYDDYGYGEDYLPDVLNTDISEETII
Protein: Anion exchange protein (A0A494BBC3)
Organism: Mus musculus (Mouse)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
Sequence:
MKLPGQGDFESSDAHENAHSEEPDSGLGPGPGLNGPSGIDIGESQVSKDPLLFIQLNELLGWPQALEWRETGRWLLFEEKLDMGAGRWSAPHVPTLELPSLQKLRSLLAEGIVLLDCQAQSLLELVEQVVSGESLSPELRGQLQALLLQRPQHHIQTMGIRPCRESNAFRKASRDEDAPLKHQNPLRQKLPAGAEAAAVLAGELGFLEQPLGAFVRLRNPIVLEPLTEMILPSRFFCLLLGPPTLGRSYHEMGRAAAVLLSDPQFQWSVRRASHLPDLLAALDAFLQEVTALPPGRWDRTARIPPPKYLPSQHKRFPSKLQEVTSLSRQSAALAEDKHHHGPHTPIPELQRTGRLFGGLIQDVRRKACWYTSDFLDALHPQCFSAVFYIYLATVTNAITFGGLLGDATEGAQGVLESFLGTAVAGAAFCLMAGQPLTILSSTGPVLVFERLLFSFSRDYSLDYLPFRLWVGIWVTAFCLALVATEASLLVRYFTRFTEEGFCALISLIFIYDAMGKMLNLIRAYPIQRPGSSAYGCFCQYPGTGGNTSEWTSAKLKDTEDILSVPGLVNASFLPPPECIRQGGHPLGPSCHTVPDIAFFSLLLFFTSFLCAIALKHIKNSRFFPSVVRKVLGDFSSVLAILLGCGLDTFLGLATPKLLVPTEFKPTLSGRGWLVSPFGANPWWLSVAAALPALLLSILIFMDQQITAVILNRAEYRLQKGAGFHLDLFCVAVLMLFTSALGLPWEQRLTGLVVFVLTGVSIFLAPVLKFIPMPVLYGIFLYMGVAALSSIQFVKRVQLLLMPRKHQPDMLLLRHVPLSRVHLFTAIQLACLGLLWVVKSTPAAIVFPLMLLGLVAIRKALEWVFSPQELLWLDELMPEEEETIPENRSEPEHLFSGNDSEDSELMYQPKAPEINISVN
Protein: Putative antitoxin VapB44 (P9WJ17)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin is VapC44.
Interaction partners:
- Ribonuclease VapC44
- Putative antitoxin VapB19
Sequence:
MRTTLSIDDDVLLAVKERARREKRTAGEILSDLARQALTNQNPQPAASQEDAFHGFEPLPHRGGAVSNALIDRLRDEEAV
Protein: Probable lipid-A-disaccharide synthase, mitochondrial (EC 2.4.1.182) (Protein LIPID X B) (AtLpxB) (F4IF99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21709257}.
Interaction partners:
- Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial
- Probable UDP-3-O-acylglucosamine N-acyltransferase 2, mitochondrial
- Probable UDP-3-O-acylglucosamine N-acyltransferase 1, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 2, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 5, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 3, mitochondrial
- Probable tetraacyldisaccharide 4'-kinase, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 1, mitochondrial
- Probable 3-deoxy-D-manno-octulosonic acid transferase, mitochondrial
- Pentatricopeptide repeat-containing protein At1g80270
Sequence:
MMFQITKSKLRFPLSTFTKRYSSFQAAKSVIDKAAIDGELRVFIVSGEVSGDNIGSRLMSSLKKLSPLPIRFNGVGGSLMCKKGLNSLFPMEDLAVMGVWELLPHLYKFRVKLKETIDAAVKFKPHVVVTVDSKGFSFRLLKELRARYKQQRLENCSVHFHYVAPSFWAWKGGESRLGGLSEFVDHLFCILPNEERVCREHGVEATFVGHPVLEDASEFDLVRRCKPQELKLEGLSFSEHSIPSDSTVISVLPGSRLQEVERMLPIFSKAMKLLKDPFPKLVTLIHVASNNQVDHYIGESFSEWPVPAILVPSGSTQLKYDAFGASQAALCTSGTVAVELQLAHLPSLVAYRAHFLTELLIRYKAKIPYISLPNILLDSPIIPEALFQACNPSNLASILERLLLDEKMRERQVVGAEKLIQLLHPSESRMGNSIHCTGLESHRYTPSILAASTILSYARR
Protein: Kinesin associated protein 3, isoform M (A8JUR5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQFVLLLIFQIISGLVLLPIVIHYVYYIINAIAGDLCEQKRAQREQQLQRSPTPRHQNRHPPHPPPTEEEPVLSINNLTNSSRSPTAAATTTAMQTNDDAKFIKKRWKGGSIEPHPTDKALIVNYQLEATVFGEPNNPMIEEKKHCQKIIRLRSLNAKTDPAALAREVVEKCDLIHKSQLNDVEQIIFYLKNRKDNASNDIPDNNTHSRRSAALHTSHTRSSARSHSSVAAMTSSTGSGGGSTGASNGVSNALSAATPTADVSINNIDEYVELLYEELGERIRGSAMILQMARNPDNLEELEKNACLSALSRVLREDWRKSLDLSTNIIYIFFCFSTYTKFHPLIVQYKIGSLCMDVIDYELRRYETMRNELDVRKQPNGSSTPHSAKASKEKLNRSTDDFLDIMNEEKPKEMEPPRRRIPELKQRPKSGNWSSFHGSMSSSLIKSQILNSSYHESLCAGGSPGGDTPAVPAEQKAQSNESLDRNDPKVKKEEIDRLNKQLKIFAKKQEQLLRVAFYLLLNMAENVKLEEKMRRKHIVKMLVKALDRQNIDLLMLVSTFLKKLSIVGDNKDEMGALNIVAKLPRLFQSTHTDLVQVTLKLVFNLSFDGGLRRKMIAAGYLPMLVMFINDEKHHGIAVKILYHMSLDDKVKGMFTQTECVQMATDAIILNLNVKVDLDLIALCINLSLNRRNAQIMVEGQRLHSLMDRAFKYQDALLMKLLRNLSQHESLQLQFIDYVGDLARILTICDDEAFIVECLGILGNLALTDLDYSQILQNFQLIPWIRQILLPCARMDDLVLDTIVYLGTCACDELCALLFCRAKVVISLIELLKAKQEDDEIVLQIIFVFQQILRHESTREYMIKETESAAYLIDLMHDKNEEIRKVCDYCLDIIAISDSEWAKRIKLEKFRNHNSQWLCMVESQQDQDNEQDYADQEDECDNDLDTYLRSEYLDNCDLYNDNADNDSNSNSNHSNNNPASPAMSTYSRPLSTYRRSQDLDDLYNMTSSSKSQGSSDNNYIFKSNKSLDADGLHEELLMA
Protein: Maestro heat-like repeat family member 4 (A0A5F8MPT5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XKLLEFLNLDPRKATDKAFFFHLYGMILRECPSVEKVQCHLASLLDLSHQHSRQREGIALAVGLASTKHLEEVWALLEHLGRTKFLQSVAATEDSQPSDNLRWKWVSSTSLLCYGQIAKHTKEQILPWVDNIASRMVYYFSCGPCDEILKSSFLSATILLTRSLQAEYSSQRYKFTQTPELIQCLLGILQKEPNSLTNFLRQKIILVIIGLSNLRPRFKPLLKSQILKTCLQTVYMLPPAKDSRNDLFSVEQASDTTVLYKKTVRALDLLLQNFISENPSMDEVCFLLQHIEYWLMSDKIHERSRAVQSIYLLLQYVVDSLKLAKEAVPSLLGHQIGILILLWRDKDKITQQHSHFCVYLLMELVFQQKGKLVESAQWSKMKHFE
Protein: Parathyroid hormone-related protein (PTH-rP) (PTHrP) (Parathyroid hormone-like protein) (PLP) [Cleaved into: PTHrP[1-36]; PTHrP[38-94]; Osteostatin (PTHrP[107-139])] (P12272)
Organism: Homo sapiens (Human)
Function: Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport. Regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teeth. Required for skeletal homeostasis. Promotes mammary mesenchyme differentiation and bud outgrowth by modulating mesenchymal cell responsiveness to BMPs. Up-regulates BMPR1A expression in the mammary mesenchyme and this increases the sensitivity of these cells to BMPs and allows them to respond to BMP4 in a paracrine and/or autocrine fashion. BMP4 signaling in the mesenchyme, in turn, triggers epithelial outgrowth and augments MSX2 expression, which causes the mammary mesenchyme to inhibit hair follicle formation within the nipple sheath (By similarity). Promotes colon cancer cell migration and invasion in an integrin alpha-6/beta-1-dependent manner through activation of Rac1.
Subcellular location: Cytoplasm. Nucleus. Secreted.
Interaction partners:
- Parathyroid hormone/parathyroid hormone-related peptide receptor
- Parathyroid hormone
- Importin subunit beta-1
- Parathyroid hormone 2 receptor
- Indian hedgehog protein
- Guanine nucleotide-binding protein G
- Probable non-functional immunoglobulin heavy variable 3-16
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Fibroblast growth factor 2
Sequence:
MQRRLVQQWSVAVFLLSYAVPSCGRSVEGLSRRLKRAVSEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPSPNTKNHPVRFGSDDEGRYLTQETNKVETYKEQPLKTPGKKKKGKPGKRKEQEKKKRRTRSAWLDSGVTGSGLEGDHLSDTSTTSLELDSRRH
Protein: Growth hormone receptor b (Growth hormone receptor type 2b) (Q5MKL1)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MNSMATSHILFICLLLILTVVSQEPPTSEQALPQIRPQITGCVSHDMNTFRCRWNVGTFQNLTEPGDLRMFYYINNKNISPKEWSECPNYMADRIDECFFNESYTKVWITYSVQLRSGDQDNLYDEVIFTVEDIVEPDPPIALNWTLLNVGLTGSHFDIMVSWEPPHSADVSMGWMTLQYEVQYREVNSTLWRMVNLEKGRQRSLYGLRTNTDHEVRVRCKTLASRNFGEFSDPIVIHIPTKESRFPVTVLLVFAALGLAVILILVIYSQQQKLMMILLPPIPGPKIKGIDPELFKKGKLAELTSILGDHPDLRPELYCEDPWVEFIELDMEEPNDRLTELDTQCLMDRTPSSDCPPLTIGFGDDDSGRASCCDPDLPEPEAFPLSNTSPSLEPSGASTEASSPVQTPTTGMTLWAVPGREDLYTQVSEVRPTGEVLLMPEEQSKVEKDAEEKAKEGKEKEKPRKEFQLLVVNADGGGYTTELDAGKMSAKLPTGRGSQPAPTEDSRLVQGQPFGEYQSLYFEAEMPPIPPASPVSSLLPLSVYTMVEGVDRQNSLLLKPSPPPAPQPVLTKLPLPTPTPEGYLTPDLLGNVTP
Protein: Leucine-rich repeat-containing protein 4B (Netrin-G3 ligand) (NGL-3) (P0C192)
Organism: Mus musculus (Mouse)
Function: Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner (By similarity).
Subcellular location: Membrane; Single-pass membrane protein. Presynaptic cell membrane {ECO:0000250}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase S
- Receptor-type tyrosine-protein phosphatase F
- Netrin-G1
- Interleukin-1 receptor accessory protein-like 1
- Receptor-type tyrosine-protein phosphatase delta
- Neurexin-2
- Disks large homolog 4
Sequence:
MAQAHIRGSPCPLLPPGRMSWPHGALLLLWLFSPPLRAGGGGVAVTSAAGGGSPPATSCPAACSCSNQASRVICTRRELAEVPASIPVNTRYLNLQENSIQVIRTDTFKHLRHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRLTTVPTQAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLRRLDLGELKRLEYISEAAFEGLVNLRYLNLGMCNLKDIPNLTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLHRLERVHLNHNPWHCNCDVLWLSWWLKETVPSNTTCCARCHAPAGLKGRYIGELDQSHFTCYAPVIVEPPTDLNVTEGMAAELKCRTGTSMTSVNWLTPNGTLMTHGSYRVRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNVSAVDPVAAGGPGGGGPGGGGGAGGAGGYTYFTTVTVETLETQPGEEAQQPRGTEKEPPGPTTDGAWGGGRPDAAAPASASTTAPAPRSSRPTEKAFTVPITDVTENALKDLDDVMKTTKIIIGCFVAITFMAAVMLVAFYKLRKQHQLHKHHGPTRTVEIINVEDELPAASAVSVAAAAAVAGGAGVGGDSHLALPALERDHLNHHHYVAAAFKAHYGGNPGGGCGAKGPGLNSIHEPLLFKSGSKENVQETQI
Protein: Decay accelarating factor 1, isoform CRA_c (Decay accelerating factor soluble-form) (Q9Z0L9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MIRTRAPGTRAPPPPPLLLSLSLLLLLLSPTVSGDCGPPPDIPNATPNSGKHTKFAHQSQVTYSCNKGFKQIPDKPNTVVCLENDQWSNYETFCNKTCSAPLRLNYASLKKEYRNMNFFPIGTTVEFECRPGFQKVTSRTGKSTCLEELVWSPVVEFCKKRACPNPRELKNGHINIPTDILFGSEIIFSCDKGYKLVGVTSTFCSITGNAVDWDDVFPVCTTIFCPDPPKINNGRIREESDSYAYRQSVTYSCDQGFILVGNSSVHCTLNGEVGEWSSAPPKCIERHKVPTKTPPEVDIPSTMPHESTLINFPSTRAPLSHKPTTVKVPATQHVPVSKTTVRHPTRTSKDRGESNSGGDHFIYGKFDPQGVKRNCHHCGRHSPYFWKRIFSYNCLRKTIKMQCLWVPKGRWVKPFNRLVFWTPLGIQHGPSYPQQCSCSKAVLGQLRVIWPISQVALSARCVSVSF
Protein: Glutathione peroxidase-like peroxiredoxin 1 (EC 1.11.1.24) (EC 1.11.1.9) (Glutathione peroxidase homolog 1) (GPx 1) (P36014)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress. Has peroxidase activity using thioredoxin or glutathione as a reducing power. Involved in peroxisome formation.
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:22659048}. Mitochondrion outer membrane; Peripheral membrane protein {ECO:0000269|PubMed:22659048}.
Interaction partners:
- Glutathione reductase
- Peroxiredoxin TSA1
- Peroxiredoxin PRX1, mitochondrial
- Catalase T
- Peroxiredoxin AHP1
- Superoxide dismutase
- Peroxiredoxin TSA2
- Sulfiredoxin
- Thioredoxin-2
- Peroxisomal catalase A
Sequence:
MQEFYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQDKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGIKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPIIEELLNQPPEEQI