wanglab/gogpt-training-data huggingface dataset:
Protein: Ephrin type-B receptor 4 (EC 2.7.10.1) (Hepatoma transmembrane kinase) (Tyrosine-protein kinase TYRO11) (P54760)
Organism: Homo sapiens (Human)
Function: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 it is involved in the regulation of cell adhesion and migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28687708, ECO:0000269|PubMed:8188704}; Single-pass type I membrane protein {ECO:0000269|PubMed:8188704}.
Interaction partners:
- Ephrin-B1
- Ephrin-B2
- Ephrin-B3
- Ras GTPase-activating protein 1
- Tyrosine-protein kinase ABL1
- Ephexin-1
- Ephrin-A5
- Ephrin-A2
- Ephrin-A1
- Ephrin-A4
Sequence:
MELRVLLCWASLAAALEETLLNTKLETADLKWVTFPQVDGQWEELSGLDEEQHSVRTYEVCDVQRAPGQAHWLRTGWVPRRGAVHVYATLRFTMLECLSLPRAGRSCKETFTVFYYESDADTATALTPAWMENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYLAFQDQGACMALLSLHLFYKKCAQLTVNLTRFPETVPRELVVPVAGSCVVDAVPAPGPSPSLYCREDGQWAEQPVTGCSCAPGFEAAEGNTKCRACAQGTFKPLSGEGSCQPCPANSHSNTIGSAVCQCRVGYFRARTDPRGAPCTTPPSAPRSVVSRLNGSSLHLEWSAPLESGGREDLTYALRCRECRPGGSCAPCGGDLTFDPGPRDLVEPWVVVRGLRPDFTYTFEVTALNGVSSLATGPVPFEPVNVTTDREVPPAVSDIRVTRSSPSSLSLAWAVPRAPSGAVLDYEVKYHEKGAEGPSSVRFLKTSENRAELRGLKRGASYLVQVRARSEAGYGPFGQEHHSQTQLDESEGWREQLALIAGTAVVGVVLVLVVIVVAVLCLRKQSNGREAEYSDKHGQYLIGHGTKVYIDPFTYEDPNEAVREFAKEIDVSYVKIEEVIGAGEFGEVCRGRLKAPGKKESCVAIKTLKGGYTERQRREFLSEASIMGQFEHPNIIRLEGVVTNSMPVMILTEFMENGALDSFLRLNDGQFTVIQLVGMLRGIASGMRYLAEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLEENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDAWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTSLHQLMLDCWQKDRNARPRFPQVVSALDKMIRNPASLKIVARENGGASHPLLDQRQPHYSAFGSVGEWLRAIKMGRYEESFAAAGFGSFELVSQISAEDLLRIGVTLAGHQKKILASVQHMKSQAKPGTPGGTGGPAPQY
Protein: Fatty-acid amide hydrolase 1 (EC 3.5.1.99) (Anandamide amidohydrolase 1) (Fatty acid ester hydrolase) (EC 3.1.1.-) (Oleamide hydrolase 1) (O08914)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of endogenous amidated lipids like the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides such as the taurine-conjugated fatty acids (a structural class of central nervous system (CNS) metabolites), to their corresponding fatty acids, thereby regulating the signaling functions of these molecules. FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids. It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:32271712}; Single-pass membrane protein {ECO:0000250|UniProtKB:P97612}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P97612}; Single-pass membrane protein {ECO:0000250|UniProtKB:P97612}. Note=Seems to be associated with the endoplasmic reticulum and/or Golgi apparatus. {ECO:0000250|UniProtKB:P97612}.
Interaction partners:
- Glutamyl-tRNA
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Monoglyceride lipase
- Monoacylglycerol lipase ABHD6
- Bifunctional glutamate/proline--tRNA ligase
- Cannabinoid receptor 1
- Lysophosphatidylserine lipase ABHD12
- N-acylethanolamine-hydrolyzing acid amidase
- Cannabinoid receptor 2
- G-protein coupled receptor 55
Sequence:
MVLSEVWTALSGLSGVCLACSLLSAAVVLRWTRSQTARGAVTRARQKQRAGLETMDKAVQRFRLQNPDLDSEALLALPLLQLVQKLQSGELSPEAVLFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHASTLGLSLNEGVTSESDCVVVQVLKLQGAVPFVHTNVPQSMLSYDCSNPLFGQTMNPWKPSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKSCVYGQTAVQLSVGPMARDVDSLALCMKALLCEDLFRLDSTIPPLPFREEIYRSSRPLRVGYYETDNYTMPTPAMRRAVMETKQSLEAAGHTLVPFLPNNIPYALEVLSAGGLFSDGGCSFLQNFKGDFVDPCLGDLVLVLKLPRWFKKLLSFLLKPLFPRLAAFLNSMCPRSAEKLWELQHEIEMYRQSVIAQWKAMNLDVVLTPMLGPALDLNTPGRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMEHYKGYFGDMWDNILKKGMKKGIGLPVAVQCVALPWQEELCLRFMREVERLMTPEKRPS
Protein: Jouberin (Abelson helper integration site 1 protein) (AHI-1) (Q8K3E5)
Organism: Mus musculus (Mouse)
Function: Involved in vesicle trafficking and required for ciliogenesis, formation of primary non-motile cilium, and recruitment of RAB8A to the basal body of primary cilium. Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Involved in neuronal differentiation. As a positive modulator of classical Wnt signaling, may play a crucial role in ciliary signaling during cerebellum embryonic development.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:18633336, ECO:0000269|PubMed:19625297, ECO:0000269|PubMed:21623382}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:19625297}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q8N157}. Note=In the retinal photoreceptor cell layer, localizes at the connecting cilium. {ECO:0000269|PubMed:29899041}.
Interaction partners:
- Coiled-coil and C2 domain-containing protein 2A
- B9 domain-containing protein 1
- Centrosomal protein of 290 kDa
- Meckelin
- Tectonic-1
- B9 domain-containing protein 2
- Transmembrane protein 231
- Transmembrane protein 216
- Tectonic-2
- Nephrocystin-1
Sequence:
MEPETPEKVDSAQEKVRGKTPTADDSDDSREKTGIEEKGELTDAYQLQVAEEMAKEIKKKIRKKLKEQLTYFPPDTLLHDDKLASEKRKKKKKKVPVPTKPESSPSDVCDSAVEGEQKKEGTPEDSQHMEGICSREQDVDATVPENAKPKPKKTKKKTKAVSNDNEDTNGDGVHEITSRDSPVHPKCLLDDDLVMGVYIHRTDRLKSDFMISHPMVKIHVVDEHTGQYVKKDDSERPVSSYYEKDNVDYILPIMTQPYDFKKLKSRLPEWEEQVIFNENFPYLLREFEECPKVILFFEILDFLSMDEIKNNSEVQNQECGFRKIAWAFLKLLGANGNANINSKLRLQLYYPPTKPRSQLNVVEVFEWWSKCPRNRYPSTLYVTVRGLKVPDCIKPSYRSMMALQEERGTPVYCERHRETSSVDTEPGLEDSKEEVKWKRLPGQACRIPNKHLFSLNAGERGCFCLDFSHNGRILAAACASRDGYPIILYEIPSGRFMRELCGHLNIIYDLDWSKDDRYLVTSSSDGTARVWKNEINSTSTFRVLPHPSFVYTAKFHPATRELVVTGCYDSMIRIWKIDAREDAAILVRQLDVHKSFVNSICFDDEGHHMYSGDCIGVIVVWDTYVKVNDVQTSVRHWTINKEIKETEFRGVPISYLEVHPNGKRLLIHTKDSTLRIMDLRILAARKFVGAANYREKIHSTLTPCGTLLFSGSEDGIVYVWNPETGEQVAMYSDLPFKSTIRDISYHPLENMVAFCAFGQSEPILLYIYDFQVAQQEAEMLKRYSGTLPLPGIHQSEDALCTCPKLPQQGSFQIDEFVNTENSSSRKIQLVKQRLETVTEVIRSCAAKVNKNLSMTSPPPGPAKKPRVKQSFVLTTDEIIHQFGLPQTAFISIERGPFVRHVDPPPMVVALYDYTASRSDELTIHRGDIIRVYFKDNEDWWYGSVRKGQEGFFPANHVASETLYRDSPPKVKERSPPLTPKEKTKPEKPLASQKQSLSKGRPLDPRLGPQPVGHSEKGKDQNVEDRGHKVDMETKKSEPVVRKVTLIE
Protein: Neuronal pentraxin receptor (O95502)
Organism: Homo sapiens (Human)
Function: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Reticulocalbin-2
- Chromobox protein homolog 6
- Atrial natriuretic peptide receptor 1
- Neuronal pentraxin-2
- Atrial natriuretic peptide receptor 3
- Atrial natriuretic peptide receptor 2
- Natriuretic peptides A
Sequence:
MKFLAVLLAAGMLAFLGAVICIIASVPLAASPARALPGGADNASVASGAAASPGPQRSLSALHGAGGSAGPPALPGAPAASAHPLPPGPLFSRFLCTPLAAACPSGAQQGDAAGAAPGEREELLLLQSTAEQLRQTALQQEARIRADQDTIRELTGKLGRCESGLPRGLQGAGPRRDTMADGPWDSPALILELEDAVRALRDRIDRLEQELPARVNLSAAPAPVSAVPTGLHSKMDQLEGQLLAQVLALEKERVALSHSSRRQRQEVEKELDVLQGRVAELEHGSSAYSPPDAFKISIPIRNNYMYARVRKALPELYAFTACMWLRSRSSGTGQGTPFSYSVPGQANEIVLLEAGHEPMELLINDKVAQLPLSLKDNGWHHICIAWTTRDGLWSAYQDGELQGSGENLAAWHPIKPHGILILGQEQDTLGGRFDATQAFVGDIAQFNLWDHALTPAQVLGIANCTAPLLGNVLPWEDKLVEAFGGATKAAFDVCKGRAKA
Protein: Snake venom vascular endothelial growth factor toxin vammin (svVEGF) (VEGF-F) (P67863)
Organism: Vipera ammodytes ammodytes (Western sand viper)
Function: Snake venom VEGFs may contribute to venom dispersion and prey subjugation by inducing vascular permeability and hypotension. The hypotension is mediated by nitric oxide (NO), which is produced by VEGF-activated endothelium NO synthase. Also induces angiogenesis in vitro, probably through VEGF receptor (KDR/VEGFR-2) signaling. May also induce capillary permeability through VEGF receptor (KDR/VEGFR-2) signaling.
Subcellular location: Secreted {ECO:0000269|PubMed:14600159, ECO:0000269|PubMed:15542594}.
Interaction partners:
Sequence:
MAAYLLAVAILFCIQGWPSGTVQGQVRPFLEVHERSACQARETLVPILQEYPDEISDIFRPSCVAVLRCSGCCTDESLKCTPVGKHTVDLQIMRVNPRTQSSKMEVMKFTEHTACECRPRRKQGEPDGPKEKPRRGGVRARFPFV
Protein: Serine protease inhibitor A3M (Serpin A3M) (Q03734)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Transcription factor PU.1
- Haptoglobin
- Intraflagellar transport protein 122 homolog
Sequence:
MAFIAALGILMAGICPTVLCFSDDTWGIDILLHKNQESGTPDDSLTLASINTDFAFSLYKKMALKNPDKNIVFSPLSISAALALVSLGAKGNTLEEILEGLKFNLTETSEADIHQGFGHLLQRLSQPEDQDQINIGNAMFIEKDLQILAEFHEKTRALYQTEAFTADFQQPTEATKLINDYVSNQTQGMIKKLISELDDRTLMVLVNYIYFKGKWKISFDPQDTFESEFYLDEKRSVKVPMMKMKFLTTRHFRDEELSCSVLELKYTGNASALFILPDQGRMQQVEASLQPETLRKWWKSLKTRKIGELYLPKFSISTDYNLKDILPELGIKEIFSKQADLSGITGTKDLSVSQVVHKAVLDVAETGTEAAAATGFIFGFRSRRLQTMTVQFNRPFLMVISHTGVQTTLFMAKVTNPK
Protein: Translation initiation factor eIF2B subunit beta (eIF2B GDP-GTP exchange factor subunit beta) (Q57VZ6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
- Translation initiation factor, putative
- Elongation initiation factor 2 alpha subunit, putative
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF-2B alpha subunit, putative
- Translation initiation factor eIF2B subunit delta
- Glucose-1-phosphate adenylyltransferase/Bifunctional protein GlmU-like C-terminal hexapeptide domain-containing protein
- protein-synthesizing GTPase
- Selenocysteine-specific elongation factor
- VPS9 domain-containing protein
- mannose-1-phosphate guanylyltransferase
Sequence:
MGKRSIRIQEEASPLMEIIGDLIEKFVGNVRRGKLGPRDGKSFSMTAASGSVQLMHEIITEFKNHLEKKGTTGTHSHSCEIITSRDVHRLIWLISFTGDAMLRAQFGTLLLTNVTRRVLSFIRTAAVECKVSSNEVDSFEKGDAGGSDNEKSASLDMQRLATTNRQSSGVCSVAGGTGRGTGTTNDSNESYEEEEQEISTVGIPGRQTLRRAPSRREVDSVVREEAAVLVHAHDFFNCVLQHIVELRAEIEGMCDALCERAVKQLHPTDTVITTGSSHTTRRYLLHALSAGTSFKVIILEGAPLLCEASHKLAAELRSKHAEVQVLPDSSAFAVMGTCTKVLIGAENVLANGGILAPIGTHPLCIAAKHFAVPVLVVTATIKMTPFYPSDAYCTSLVKISRSSAQEIPWNTYGSPGDVLPAPYGADVDTFGSFVVHSPVTEYVPPELITLYATNESEYTPSQIHRIVRENYSPED
Protein: Large ribosomal subunit protein uL1 (60S ribosomal protein L10a) (P53028)
Organism: Trypanosoma brucei rhodesiense
Interaction partners:
Sequence:
MSKIPPALLSEAIQNVLKDRKERKFKESIDLQVNLKNYDPQKDKRFSGSVRLPHVCRPRMTVCLLCDLVHEDIAKKNDVPTMNQEELKKLNKNKKLVKKMCNQYDAFLCSESIIKTVPRLVGPHMHRVGKFPTVCAQNESLPDKVLELQSTVKFQLKKVLCLGTCVGHVDMTEDQVRQNVVMAINFLVSLLKKNWQNLKSAYIKSTMGKSQRIY
Protein: Multiple C2 domain and transmembrane region protein 8 (Q9M2D4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vesicle {ECO:0000269|PubMed:29259105}. Note=Localized in small structures within cells. {ECO:0000269|PubMed:29259105}.
Interaction partners:
- 16 kDa phloem protein 2
Sequence:
MMSNLKLGVEVISARLKPREDYGGVNAYVELRFDDQKVITMTKIDDSSPVWNEKFFFNISDTEDLSNQFLDAYVYNKTSSITKSCLGKIRILGTAFLPYSEAVGLPYPLEKEKWSMFSSAAANGGELALKVFLTDNPSPKVPNLISTKKIPSKSRHKFHNIPTNESNHSPRGNQQSFQPQPPPPQSQTALPPPMMESSLYQAPRFGTPIPTTMGFNPNPPDYSIKETKPILGGGKRARSSDHDLVEPMEFLFIKIVKARNLPSMDLTGSLDPYIEVKLGNYTGKTKHFEKNQNPVWNEVFAFSKSNQQSNVLEVIVMDKDMVKDDFVGLIRFDLNQIPTRVAPDSPLAPEWYRVNNEKGGEIMLAVWFGTQADEAFSDATYSDALNAVNKSSLRSKVYHSPRLWYLRVNVIEAQDLVIVPDRTRLPNPYVKIRLNNQVVRTKPSHSLNPRWNEEFTLVAAEPFEDLIISIEDRVAPNREETLGEVHIPIGTIDKRIDDNRTVPNRWFSLKTENQRRVRFATTRLHLNVCLEGGYHVLDESTYYSSDFRPSMKELLSHKQPSFGVLELGILRIEGLNLSQEGKKETVDAYCVAKYGTKWVRTRTVTNCLNPRFNEQYTWEVYEPATVITIGVFDNNQINSGNGNKGDGKIGKIRVRISTLEAGRIYSHSYPLLVLRPSGLKKMGELHLAIRFSCSSMFQMLMQYWKPLLPKMHYARPLKVVQQEILRQHAVNLVAARLSRAEPPLRKEVVEYISDSNSHLWSMRKSRANLFRLSSVFSGLLGTGEWFQDICRWKKPVETTAIHIIFLVLVCSPEMILPVMSLCLFMLGVWNYRLRPRQPPHMDTRLSFADNIHPEELNEEFDTFPFSSQDPGIVKMRYERLRSIASRAQTVVGDIAGQGERVQALLSWRDPRATSIFMVLCLVSTVVLYVVPFKVFVLLAGLYIMRPPRFRGKTPPGPINFFRRLPAKTDCML
Protein: Putative aminopeptidase-2 (EC 3.4.11.-) (Q22531)
Organism: Caenorhabditis elegans
Function: Putative aminopeptidase which plays a role in oocyte maturation.
Interaction partners:
- Protein-S-isoprenylcysteine O-methyltransferase
Sequence:
MRRKLLLLLCFIGLFSLISTAPAPNNVGLESEFTEGHAETINLEEVEFNHPSILPEHPDNFRQDKLAARKRQSLYVTKTRLPPNLYAIDYSLWFQPYFPSPGVQYAPEKNFTFDGRASIQVEALVASDRFILNAYNFKIQSYKVVDIDGTVVPINSISQDDTTQQLSLITNANGVVAGQIYNIEFVYTGIINPYTDGGVYYTSYNDPQGNTHYMIATHMEPFSARKVFPSLDEPSYKAKFTITVQYPASQVALSNMMETEPTKIDNIWSTITFPQTPKMSSYLIAFAVGPYVNSQYVNKHNTLTRAWGWPGTEQYLQFAAQNAGECLYQLGEYTGIKFPLSKADQLGMPEFLAGAMENWGLIIYKYQYIAYNPTTMTTRNMEAAAKVMCHELAHQWFGDLVTTAWWDDLFLNEGFADYFMTFIQKSVYPQQATYLDTLQVLDELQVGLTADVRYDAHPLVYPDGPAFDDITYNKGASMLRMLSDVLGADVFKQGIRAYLQKMQYSNANDFDLFSTLTDTAKSNNILDWCGLPLNVTDFMQPYIHQTNHPLIRYNNNQKIGGSTFSQEPFLDISDLTATPWNYTWSIPLTSANLRHADPYKQWLPRQQGCANMNENIQEERIKEPNKRAVQWELTSITSATYGRIIYDDIGFDRILKLIKQDDINDNLKLTLLADEYNYMLREKKANRPFGYNRFLDLAKVIFNTQSFTNYPSYGVFAQAQPVLEQIAQLYRDGIDAEFVPRLYKLFFQNSYNQLKWQDTSIWDTDTFSEVFLPFAVRYDIGDVQNRTLNMFANVKSACINSLNGTAWCNPYSTNLRKAIYCGAAKYAPATSDYFFQMLHSYNKEVITNPYFYQEYMALLEGMSCTQSPATLKVLIRLFTTSTLNPSTIFGFLKYNPAASDVLYNYFMANPQLVNSTMLDAYLDAMTYNWNSYFREGQLSTLMNTLTLTNDQFDIFDFYINRVSLMFEYKSTYALPTYNWLYDNLVVIGKTPWEKTPNIDAVFPYYKLDLQVNIPGSGPYQWYENMTFSATSTVTFQLVSPTSSITINAHRLMFDPVSIRLYNENDENAHTPIPIDFSKVMKDYDKGTVTIPTMNNTVLYPNQYSLFIEYTGFIFQNPDEGDASNTYLGGLNNRKGWIFTTDFEGGPGARSLLPCWDEPSYKGQFEVSVFHPTDMIALSNEVDIQRTIYDNGWTTTKFATTNQMSTYLLALCVGHFSNLATVTRTGVLTRVWTWSGMEQYGEFALNVTAGTIDFMENYFSYDFPLKKLDVMALPEYTMNAGAMENWGLIIGEYSLFMFDPDYATTRDITEVAETTAHEVVHQWFGDIVTLDWWNDIFLNEGFAQYWFANGIDNTFPEQHAYSIDYNRFYMNHIALKYDCIPGVAKPVISDTPPVFGIEPYYKGSALLNLLNNVLTPAVFQEGLSSYLTQYGYVNASPRNLWTSLTVAAQRHNITDWNGQPLDVSSFMDPYTLQTSYPIITLTLRGTSTVQANQQSCMSDETLWNVPLFTQTPGALDFNWFVNFTGGNDATWLRPLPTGYRVDNAGSTSFARINYDDKSWYSIQAQLLSNMNTMSSTTRAMLLDDANFFYQSGRWEMTKFLDLTLYLVNEDSLAPWEQAIEFFTEMLNRFQYQPEIDTVRNYVIQITKNAVSKFQWNTNGLWANDRIVQLLVNVNNLAVNRQSRQVALTLFNNFVLKCKYSLSGTGKCSGIHPNLRQPTYCYGLRQSNNIDDFTTVNNLYSWFVQNAGYLQTDGSNLLNALGCVQNLDLQKTMLRSILSGDYPPSLLNSIAVHDDSSDVLYNFLLDNTQDILNAPFDFSLYVKAMFQNWSTSNQLELAKDFQNSSNYNLLNAAQKNIYKQGILTVNSNANWMLIYKTPFLEWIQKNFGAPNL
Protein: POC1 centriolar protein homolog A (Pix2) (Proteome of centriole protein 1A) (WD repeat-containing protein 51A) (Q8NBT0)
Organism: Homo sapiens (Human)
Function: Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control. Acts in concert with POC1B to ensure centriole integrity and proper mitotic spindle formation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, spindle pole. Note=Component of both mother and daughter centrioles.
Interaction partners:
- POC1 centriolar protein homolog B
- Sororin
- Centromere protein W
Sequence:
MAAPCAEDPSLERHFKGHRDAVTCVDFSINTKQLASGSMDSCLMVWHMKPQSRAYRFTGHKDAVTCVNFSPSGHLLASGSRDKTVRIWVPNVKGESTVFRAHTATVRSVHFCSDGQSFVTASDDKTVKVWATHRQKFLFSLSQHINWVRCAKFSPDGRLIVSASDDKTVKLWDKSSRECVHSYCEHGGFVTYVDFHPSGTCIAAAGMDNTVKVWDVRTHRLLQHYQLHSAAVNGLSFHPSGNYLITASSDSTLKILDLMEGRLLYTLHGHQGPATTVAFSRTGEYFASGGSDEQVMVWKSNFDIVDHGEVTKVPRPPATLASSMGNLPEVDFPVPPGRGRSVESVQSQPQEPVSVPQTLTSTLEHIVGQLDVLTQTVSILEQRLTLTEDKLKQCLENQQLIMQRATP
Protein: 2-oxoglutarate dehydrogenase E1 component (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase) (P0AFG3)
Organism: Escherichia coli (strain K12)
Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Interaction partners:
- Succinate--CoA ligase subunit beta
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- Succinate--CoA ligase subunit alpha
- Dihydrolipoyl dehydrogenase
- Succinate dehydrogenase flavoprotein subunit
- Isocitrate dehydrogenase
- Succinate dehydrogenase iron-sulfur subunit
- Succinate dehydrogenase cytochrome b556 subunit
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Citrate synthase
Sequence:
MQNSALKAWLDSSYLSGANQSWIEQLYEDFLTDPDSVDANWRSTFQQLPGTGVKPDQFHSQTREYFRRLAKDASRYSSTISDPDTNVKQVKVLQLINAYRFRGHQHANLDPLGLWQQDKVADLDPSFHDLTEADFQETFNVGSFASGKETMKLGELLEALKQTYCGPIGAEYMHITSTEEKRWIQQRIESGRATFNSEEKKRFLSELTAAEGLERYLGAKFPGAKRFSLEGGDALIPMLKEMIRHAGNSGTREVVLGMAHRGRLNVLVNVLGKKPQDLFDEFAGKHKEHLGTGDVKYHMGFSSDFQTDGGLVHLALAFNPSHLEIVSPVVIGSVRARLDRLDEPSSNKVLPITIHGDAAVTGQGVVQETLNMSKARGYEVGGTVRIVINNQVGFTTSNPLDARSTPYCTDIGKMVQAPIFHVNADDPEAVAFVTRLALDFRNTFKRDVFIDLVCYRRHGHNEADEPSATQPLMYQKIKKHPTPRKIYADKLEQEKVATLEDATEMVNLYRDALDAGDCVVAEWRPMNMHSFTWSPYLNHEWDEEYPNKVEMKRLQELAKRISTVPEAVEMQSRVAKIYGDRQAMAAGEKLFDWGGAENLAYATLVDEGIPVRLSGEDSGRGTFFHRHAVIHNQSNGSTYTPLQHIHNGQGAFRVWDSVLSEEAVLAFEYGYATAEPRTLTIWEAQFGDFANGAQVVIDQFISSGEQKWGRMCGLVMLLPHGYEGQGPEHSSARLERYLQLCAEQNMQVCVPSTPAQVYHMLRRQALRGMRRPLVVMSPKSLLRHPLAVSSLEELANGTFLPAIGEIDELDPKGVKRVVMCSGKVYYDLLEQRRKNNQHDVAIVRIEQLYPFPHKAMQEVLQQFAHVKDFVWCQEEPLNQGAWYCSQHHFREVIPFGASLRYAGRPASASPAVGYMSVHQKQQQDLVNDALNVE
Protein: Neurexin-3-beta (Neurexin III-beta) [Cleaved into: Neurexin-3-beta, soluble form; Neurexin-3-beta, C-terminal fragment (NRXN3-CTF)] (Q28143)
Organism: Bos taurus (Bovine)
Function: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May play a role in angiogenesis (By similarity).
Subcellular location: [Isoform 1]: Presynaptic cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Presynaptic cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.
Interaction partners:
- Neuroligin 1
- Neuroligin 3
- Carboxylesterase type B domain-containing protein
- Neuroligin 2
- Neurexin-1
- Dystroglycan 1
- Neurexin 3
- Neurexin 2.
- Neurexin 3
- LRRTM2 protein
Sequence:
MHLRIHARRNPPRRPAWTLGIWSLFWGCIVSSVWSSSNVASSSSSPGSHSQHEHHFHGSKHHSVPISIYRSPVSLRGGHAGATYIFGKSGGLILYTWPANDRPSTRSDRLAVGFSTTVKDGILVRIDSAPGLGDFLQLHIEQGKIGVVFNIGTVDISIKEERTPVNDGKYHVVRFTRNGGNATLQVDNWPVNEHYPTGNTDNERFQMVKQKIPFKYNRPVEEWLQEKGRQLTIFNTQAQIAIGGKDKGRLFQGQLSGLYYDGLKVLNMAAENNPNIKINGSVRLVGEVPSILGTTQTTSMPPEMSTTVMETTTTMATTTTRKNRSTASIQPTSDDLVSSAECSSDDEDFVECEPSTANPTEPGVRRVPGASEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDETRNYISNSAQSNGTLLKEKPPSSKGGHKKQKNKDKEYYV
Protein: Outer spore wall protein LDS1 (Lipid droplets in sporulation protein 1) (P31379)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in spore wall assembly.
Subcellular location: Prospore membrane {ECO:0000269|PubMed:23966878}; Multi-pass membrane protein {ECO:0000255}. Lipid droplet {ECO:0000269|PubMed:24390141}. Spore wall {ECO:0000269|PubMed:23966878}. Note=Localizes to the ascal side of growing prospore membranes in mid-meiosis II and to the spore wall in post-meiotic cells. Localizes to a specific subset of lipid droplets associated with the exterior surface of the spore throughout spore wall formation. {ECO:0000269|PubMed:23966878, ECO:0000269|PubMed:24390141}.
Interaction partners:
- Clathrin adapter accessory protein LAA2
- Protein ECM13
- Peroxisomal membrane protein PEX32
- Probable transporter SEO1
- Fructose-2,6-bisphosphatase
Sequence:
MSFTGSLALAGIGGLVYKFGGGQSYEKLPYVNIPFNQYLDKVYKKHFSKVMSRTRYVLMNFFKDAFTGGAFMYPFKGFLEFNTNKSSYSTTMLGILSSYLIMFALVSFVYWATITPMYTAFLIVLGPIGLFIAIFHSFLQANVFTLLFMRLSHFNNHLVEVCLEKNGLEENLSEVKPIKYYAPINSIYFWAYYFPFKLVKYMLGLSVLFVLLVISFFPLIGPILFHILISPFITQIYFTKVLRLQNFDNIQRRENIYLHAGQYASFGFLAGLIESVPILAGFAISTNTIGSVLFNLDHPMVPENLVETQAEIEAAPQDINQQPNQ
Protein: DNA repair protein Rad1 (IP03973p2) (Radiation insensitive 1) (Q9VQD4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cell cycle checkpoint control protein Rad9
- Checkpoint protein Hus1-like
- Rad17
- Replication factor C subunit 2
- Activator 1 subunit 5
- Replication factor C subunit 2
- Replication factor C subunit 3
- Flap endonuclease 1
- DNA repair endonuclease XPF
- Serine/threonine-protein kinase ATM
Sequence:
MTDVEPSPYGDCKFVARVEHIKTFIQAIKSICFNDYGMVQVSEDGLRITVEQGKSIQATLFMPPGAFMEFRVQDFQCFGVKMNVLSECLSLFGSADCSLRMMYRDKGDPLKIILYPHDDDDVSTECAIKTMDCDEPIDYDQNLKDPDLNVIFVRGPNLSKVFNELEKSAEEFEFVTSPNRPHFKITTVGIMQAVFSVEVAKTSPMMMMFNCKQTVVARYKSQQIRMTNKAMQSATKVAIKTNSVGLLELHLVMQGDSQEEIFIQFFIIPLLNTD
Protein: Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (Protein EF-10) (O35718)
Organism: Mus musculus (Mouse)
Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
Interaction partners:
- Tyrosine-protein kinase JAK2
- Non-receptor tyrosine-protein kinase TYK2
- Tyrosine-protein kinase JAK1
- Interleukin-6 receptor subunit beta
- Leptin receptor
- Signal transducer and activator of transcription 3
- Elongin-B
- Insulin receptor substrate 1
- Signal transducer and activator of transcription 1
- Insulin receptor substrate 2
Sequence:
MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGTPSFSLPPTEPSSEVPEQPPAQALPGSTPKRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL
Protein: C-fos induced growth factor (Vascular endothelial growth factor D) (Vascular endothelial growth factor D precursor) (Vascular enthelial growth factor D) (Q208T6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Vascular endothelial growth factor receptor 3
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor kdr-like
- receptor protein-tyrosine kinase
- Vascular endothelial growth factor C
- Angiopoietin-1 receptor
- Collagen and calcium-binding EGF domain-containing protein 1
- Lymphatic vessel endothelial hyaluronic receptor 1b
- Neuropilin-1a
- Macrophage colony-stimulating factor 1 receptor
Sequence:
MKKQKCAGLHMLLLLYVRLMLAVDAYRPQRDTNQEKWEQELREAGSLDELLMLTEYPDWKLWRCRLKLKHFDDVTPPENRRSTRYAAASFSPEMLKDIDDEWQKTQCMPRETCVDVAKELGTNTAVFFKPPCVSVFRCGGCCNKEGVTCRNTSMTYVNKTILSVSLAPYISGPEPVLVKIANHTECKCQEHSLIRRHARERHRKNSCSPTRKPEDKRLCNKGLIWDWMAERCVTYPSSKQEPPSAITEEDCEMDVERCECIPKEWTHRLHYT
Protein: MADS-box transcription factor 13 (OsMADS13) (RMADS206) (Q2QW53)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- MADS-box transcription factor 7
Sequence:
MGRGRIEIKRIENTTSRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSSRGRLYEYSNNNNVKATIDRYKKAHACGSTSGAPLIEVNAQQYYQQESAKLRHQIQMLQNTNKHLVGDNVSNLSLKELKQLESRLEKGISKIRARKNELLASEINYMAKREIELQNDNMDLRTKIAEEEQQLQQVTVARSAAMELQAAAAAQQQQQNPFAVAAAQLDMKCFFPLNLFEAAAQVQAVAAQRQQIIPTELNLGYHHHLAIPGAAAADAPPPHF