wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear pore glycoprotein p62 (62 kDa nucleoporin) (Q7JXF5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential component of the nuclear pore complex (By similarity). The N-terminal is probably involved in nucleocytoplasmic transport (By similarity). The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of Nup62 to the pore complex (By similarity). Binds to transcriptionally active genes. Negatively regulates chromatin attachment to the nuclear envelope, probably by preventing chromatin tethering by Nup154.
Subcellular location: Nucleus {ECO:0000269|PubMed:20144760, ECO:0000269|PubMed:26341556}. Chromosome {ECO:0000269|PubMed:20144760}. Nucleus envelope {ECO:0000269|PubMed:26341556}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:7641726}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P37198}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P37198}. Note=Central region of the nuclear pore, within the transporter (By similarity). Associates with chromatin (PubMed:20144760). {ECO:0000250|UniProtKB:P37198, ECO:0000269|PubMed:20144760}.
Interaction partners:
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup154
- Probable nucleoporin Nup54
- Nuclear pore complex protein Nup205
- Nuclear pore protein
- Nuclear pore complex protein Nup88
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup153
Sequence:
MVFQLPTTTAAPTGGATSSFSFGLSTGTPAAAPASGAATTAPATKTTFSFGTPAPTAGIGGGDADNSKAQAPPAFGFGLGSGTASAPLTLGTQAAANPASTTSATATGTSAAPPAFGGFTAQPAASVVPTIATSAPNTAATTTGLLGGSGLGAPKTTAAASTTLTAAPSAIASTQGAAPAPTLSTGGAFANLTTETKTTDSSAVSTASQLSYHQLEEHINKWTLEFEEQEKVFTEQATQINAWDKLLISNNGKIVELNDAVKKVKTDQQVLDQELEFIATQQKELEDSLGPLEKEFVNLPRVDMERSQTYLMVENLDTQLKQMSEDLKEIIDNLNEANKGQDTTDPIIQIGKILNAHMNSLQWIESQSTNISKKLEDIGKIQDSQKRDIFRAPF
Protein: UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2 (Beta-1,3-GalNAc-T2) (EC 2.4.1.313) (Beta-1,3-N-acetylgalactosaminyltransferase II) (Q502B3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-glycans. Has no galactose nor galactosaminyl transferase activity toward any acceptor substrate. Involved in alpha-dystroglycan (dag1) glycosylation.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Protein O-mannose kinase
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Protein O-mannosyl-transferase 1
- Ribitol-5-phosphate xylosyltransferase 1
- Beta-1,4-glucuronyltransferase 1
- Fukutin.
- Protein O-mannosyl-transferase 2
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase
- Dolichol-phosphate mannosyltransferase subunit 1
- Ribitol-5-phosphate transferase
Sequence:
MRSAAAALSVCVLAVLLHWICWTDRSAELLGFRAADRPKADVREVLVGVLSARHNHELRQAIRDTWLGYLKQHPHFQNRVLVKFIIGAQGCSVPLEDLEDQYSCSQLELSEAAVSGQEMAILSVPDSSALLQSDVPVLSLDFKVLHSVVITQLGVFPNKPPHYLKGNITVRLLQVDQEEAVISARFSSVSPGTAADGMFYKPVEQFILPKGFEGTLLWEAEDSTALMSVNTSALRLNNGGGVLHFRSIEEGTLPHRNALGFPGLAGGFTFTVYDVEVLSEMLRGRSGRQKIREAQLKGEDEALQEESLRHGDMVFVDVVGTYRNVPSKLLQFYKWSVENADFSLLLKTDDDCFIDVDAVLMKMQRRRLTHTSLWWGNFRQNWAVDRVGKWQELEYASPAYPAFACGSGYVVSRDLVQWLASNAQHLKAYQGEDVSMGIWMAAVGPRKYQDSGWLCEKECYVDMLSSPQHSAEELRLLWSRKNKCGDPCGCS
Protein: Paxillin, isoform F (Paxillin, isoform G) (Q2PDT4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Rhea, isoform B
- Vinculin
- GH23568p
- Integrin linked kinase, isoform A
- Focal adhesion kinase, isoform D
- Breast cancer anti-estrogen resistance protein 1
- Tyrosine-protein kinase
- Adapter molecule Crk
- Cortactin, isoform A
- LIM domain-containing protein
Sequence:
MDRTMYGKIDPGARQPYRTARSKGILPGYALLADLQNSVPGQPQQPQPQYGTVQPKHQALQQQQFVDNTPGYGSLRGKAQPQVYQEHYSVETRSPTAGHDFNGSSTTPGYANQGSLPRQAAGASTGLSELDSLLQDLQKIDVPVNYSTPVSKYNTMNSYATVEERPSVDSLLKELDNAHIYAVPNGSAHKSPTPGRHVTITVRETKTEKLTGPDGPVGTVEEQIVQQKDSYTPNHAVPGQQVHQAYTSQATKELDDLMASLSDFKVSNGTNGIGNGSHPQQHSSTVQHQTVTDYARPNKGSQQAHLTQTIEETTIVEDSREDQLDSMLGNLQANMSRQGVNTVQKGCCNACEKPIVGQVITALGKTWHPEHFTCNHCSQELGTRNFFERDGFPYCEPDYHNLFSPRCAYCNGAILDKCVTALDKTWHTEHFFCAQCGQQFGEEGFHERDGKPYCRNDYFEMFAPKCNGCNRAIMENYISALNSQWHPDCFVCRDCRQPFQGGSFFDHEGLPYCETHYHAKRGSLCAGCSKPITGRCITAMFKKFHPEHFVCAFCLKQLNKGTFKEQKDKPYCHTCFDKIFG
Protein: UDP-glucuronic acid decarboxylase 1 (EC 4.1.1.35) (UDP-XYL synthase 1) (UDP-glucuronate decarboxylase 1) (UGD) (UXS-1) (Q8VZC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q5PQX0}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- UDP-glucose 6-dehydrogenase 1
- UDP-sugar pyrophosphorylase
- UDP-glucose 6-dehydrogenase 3
- UDP-D-apiose/UDP-D-xylose synthase 1
- UDP-D-apiose/UDP-D-xylose synthase 2
- Cellulose synthase-like protein D5
- UDP-glucose 6-dehydrogenase 4
- UDP-glucose 6-dehydrogenase 2
- Putative UDP-glucose 6-dehydrogenase
- UDP-glucuronate 4-epimerase 6
Sequence:
MKQLHKQMSSKRDEETIPMSQSSPYSPKTLKHPRSLPRSLHYLFREQRLLFILVGILIGSTFFILQPSLSRLGAAESTSLITRSVSYAVTDSPPSRSTFNSGGGGGRTGRVPVGIGRKRLRIVVTGGAGFVGSHLVDKLIGRGDEVIVIDNFFTGRKENLVHLFSNPRFELIRHDVVEPILLEVDQIYHLACPASPVHYKYNPVKTIKTNVMGTLNMLGLAKRVGARFLLTSTSEVYGDPLEHPQKETYWGNVNPIGERSCYDEGKRTAETLAMDYHRGAGVEVRIARIFNTYGPRMCLDDGRVVSNFVAQTIRKHPMTVYGDGKQTRSFQYVSDLVEGLVALMENDHVGPFNLGNPGEFTMLELAEVVKEVIDPSATIEFKPNTADDPHKRKPDISKAKEQLNWEPKISLREGLPRMVSDFRNRILNEDEGKGL
Protein: Receptor protein-tyrosine kinase (EC 2.7.10.1) (B8LFF6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MWPVRFLLLFCLVFTFAVLQRSSGQSVCPGTDNKLSTLSDLDQQYKTLRKFYENCEVVMGNLEITSIERNRNLSFLKSIREVTGYVLVALNQFDYLPLENLRIIRGTKLYEGRYSLAIFLNYRRDGYFGLRQLGLRNLTEILNGGVYVDQNKFLCHADTIHWQDIIKNPRSELLVVPSNNSGNTCRRCHRSCNGRCWGPQEDQCQSLTXTVCAEQCDGRCFGPYVSNCCHRECAGGCFGPKDTDCFACTNFNDSGACVTQCPQPFVYNPTTFQLEHNPNAKYTYGAFCVKKCPHNFVVDHSSCVRACPSNKMEVEENQTKMCIPCTDICPKVCDGIGTGSLQMAQTVDSSNIEKFVNCTKINGNLIFLITGIKGDMFHGIRALDPDRLNVFRTVREITGFLNVQSWPENMTDLGVFSNLATIGGRSLYSGISLLILKQRWITSLQFQSLREISAGNVYMTNNSQLCFYSTVNWTSLFRTSTQRALIKNNREPRECSKEQKICDPLCSEAGCWGPGPDQCLSCKYFSRGKTCVKSCNLYYGDVREFANGSVCVECDSQCEKAGEKGLTCHGPGPDHCVKCLHLKDGPNCVEKCPDGLQGANSFIFKYAETNNECHPCHPNCTQGCTGPRIQDCVGMLDRTPLIAAGLIGGLFVIVIIALSVAVYIRRKSIKKKRALRRFLETELVEPLTPSGAAPNQAQLRILKETELKRVKILGAGAFGMVYXGIWVPEGETVKIPVAIKILNESTGPKANVEFMDEALIMASMEHPHLVRLLGVCLSPTIQLVTQLMPHGCLLDYVHEHQDNIGSQLLLNWCVQIAKGMMXLEERRLVHRXLAARNVLVKSPNHIKITDFGLARLLDTDEKEYNSDGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGXPYDGIPTRDIPDILEKGERLPQPPICTIDVYMVMVKCWMIDADSRPRFKELAAEFSRMARDPQRYLVIQGDDRMKLPSPNHSTFFQSLLDEEELDDLMDADEYLVPQTCNISTSTYTSRTTMDASWTLRCRDRVFSPEDGMGACSRDVPASASAVFVPVSTQAAGLNVLEEQHCNGSLKKQQPMSGSGDDCDGQRYSADPTVFLGERSLKNTDEDGYMSPMNKSTSDHLSPVEENPFVNHRKNGNITALDNPGYHSTPDRKSKAEEDEYINEPLYLNAYNTTGGTNLEIMRRNGSSIPLQMTTATSAASSHIILSTQPGKAHHHGQGTHVHFAIPPVQPPQTRAMSQNGQHSQSSHAVESNSSSMSANPSLLSQISLVSQQIQPCLASQSQVPKSTVPNKSISGLPGHLVYPVNMLQTGHTGTVMADRKSKKNFDNPDYWQHSLPPKVTQANPQDPTQTCKSKHLYRHSIRSRLAVADNPEFVSEFNKRPGPVLPPPPYRHRNTVV
Protein: Small ribosomal subunit protein uS14c (30S ribosomal protein S14, chloroplastic) (Q6ENH6)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: Binds 16S rRNA, required for the assembly of 30S particles.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Small ribosomal subunit protein uS12c
- Small ribosomal subunit protein mS35 mitochondrial conserved domain-containing protein
- S5 DRBM domain-containing protein
- Uncharacterized protein
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS9c
- Small ribosomal subunit protein uS17c
- Small ribosomal subunit protein uS7cz/uS7cy
- Uncharacterized protein
- 30S ribosomal protein S9
Sequence:
MAKKSLIQRERKRQKLEQKYHLIRRSSKKKIRSKVYPLSLSEKTKMREKLQSLPRNSAPTRLHRRCFLTGRPRANYRDFGLSGHILREMVYACLLPGATRSSW
Protein: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (F4JAF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDITVRISGLKSSNLIRITPRFSSSSRFRCSNNEPPRKGNESNAGGGGDKASTDWDKAWKNFKKQSKKSLFSQFNVDKYVTWNPPRSEFDLSEEVDPIKRTERSNLMLWTSPRFTLVGAIVIVSFLLLYTILAPVK
Protein: Adenylate cyclase type 2 (EC 4.6.1.1) (ATP pyrophosphate-lyase 2) (Adenylyl cyclase 76E) (Q9VW60)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P26769}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26769}. Cell membrane {ECO:0000250|UniProtKB:P26769}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P26769}.
Interaction partners:
- RAC serine/threonine-protein kinase
- Bis
- IP06402p
- LD28489p
- Inosine triphosphate pyrophosphatase
- Molybdenum cofactor biosynthesis protein 1
- GTP cyclohydrolase 1
- 3',5'-cyclic-AMP phosphodiesterase, isoform I
- cGMP-specific 3',5'-cyclic phosphodiesterase
Sequence:
MVNHNAETAKTGNGTNATANLIVKADGNATQPKAMTSSAARMNDALSASLADLSEQENGTTAEDIHLNDLYTRYRQRLRKSLFRSGLLTSLLACVVSIIIGIVYGQHLVQTMLLVLAALISGSILTALQFPAVLSSPAAALAFAIVTTFSLGTIAAITGDELAPLPMYALFLCIHSMLPISWPVSVVLALFMTAIHIVYRIGTSPDYAPNLPMLFGEIVMLASASVSGLYYRIMSDAAHNRTVDGTRTGIEQRVKLECEREQQEQLLLSVIPAYIAAEVKRSIMLKMADACQRAGGQASTSATRFHELHVQRHTNVTILFADIVNFTPLSSSLTASDLVKTLNDLFGRFDQIAQENQCLRIKILGDCYYCVSGLPISRPQHATNCVNMGLQMIDAIRHVREATGINVDMRIGIHTGNVLCGVLGLRKWQFDVWSDDVTLANHMESGGVAGRVHITKQTLDFLGDKFEVEQGEGGNRDAYLADHKVESYLIVPPKPAYTYSVPRVVECIEQNDPSPTTEETKEIKETDQSHEATDVADVLLPVTVAPPPAIVDEKMSPTSINSQEAPLHAPLASAASMSIKELSEEEDEADEATAVTEPLMHRDQDGKNDKEPKANGGHRGSGDSAASESVAKSAALSLPADDLLSMSGSESGISNSGAQAQSSNPASVTPTAAAPAGGAASNSLTVAEAPERSRRKLSVQGLMSFADRRRSSGAFIEGRKLSIHSGESFRSHAGHVTRNRPSSKMTKYVECWGADRPFANIAESKLVKNIGLASIAMIESNLLPPERKCFNFNFFGPPTELKPFTMWYRNTPREAMYRAQPDTHFRFDLICAFVLFLSLAVVQLIVIELNLALLGSLLASFVSLALFLYLSNMSVPDVHASTTERNGPGQVVASSRYLRLAMFVVVNILISSCAVFSVINYTVPDGVSKEPSSNQTILESNFSSVFVNSTLEDVQLWEIDYAIPIAPVFLYCCAISLAAISAFLRSGFILKLIAMLVAVIAQVTVLGYSDLFEMYNDANITHGLPLEIKGFLLLLVIILVLHTLDRQGEYVARTDFLWKAKLKVEQEEVETMRGINKILLENILPAHVATHFLHLERSTELYHESYSCVAVMFASIPNYKEFYDETDVNKQGLECLRLLNEIICDFDKLLLKPKFSGIEKIKTIASTYMCASGLRPGKEDGATDEKRTEEHNVVILVEFAIALMSILDSINRESFQRFRLRIGLNHGPVIAGVIGAQKPQYDIWSNTVNVASRMDSCGVMGRLQTTENTAKILMTAGYECECRGLTYVKGKGNLVTYFVKTPFDGKL
Protein: Major facilitator superfamily domain-containing protein 12 (F1PZV2)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Transporter that mediates the import of cysteine into melanosomes, thereby regulating skin/hair pigmentation. In melanosomes, cysteine import is required both for normal levels of cystine, the oxidized dimer of cysteine, and provide cysteine for the production of the cysteinyldopas used in pheomelanin synthesis, thereby regulating skin/hair pigmentation. Also catalyzes import of cysteine into lysosomes in non-pigmented cells.
Subcellular location: Melanosome membrane {ECO:0000250|UniProtKB:Q6NUT3}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q6NUT3}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hermansky-Pudlak syndrome 3 protein homolog
- TLC domain containing 3A.
- Transmembrane protein 132E.
Sequence:
MGPGPPAAGAAAPPRPLSLSARLSYAVGHFLNDLCASMWFTYLLLYLHSVRAYSSRGAGLLLLLGHVADGLCTPLVGYEADRAAGRCVRCGPRKAWHLVGTVCVLLSFPFIFSPCLGCGPATPEWAALLYYGPFIVIFQFGWAATQIAHLSLIPELATNDHEKVELTALRYAFTVVANITVYAAAWFLLHLQGSPNVEMARDASDQLGIQDVQVFQNLSLLVIGVGAVFSLLFHLGTREGRRPQVEEPDENRPLLAPTTARPLLLWRHWLREPAFYQVGLLYMSTRLIVNLSQTYIAMYLTYSLSLPKKFIATIPLVMYLSGFCSSFLMKPVNKCIGRNLTYFTGLLVILAFAAWVALADRLGMAVYAAAVLLGSGCATILVTSLAMTADLIGPHTHSGAFVYGAMSFSDKVANGLAVMAIQSLYPCSLEICCRACMGFYRWVMVAATGGVGVAATLCLCSLLIWPIRLRSWDPGAQP
Protein: Nuclear factor of activated T-cells 3 (D3ZU59)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTANCGAHDELDFKLVFGEDGAPTPVSQVSRPADLEPDDCASIYIFNVDPPPSTLNSSLGLPHHGLLQSHSSVLSPSFQLQGFKNYEGTDDISESKYSSLSGPKPFECPSIQITSISPNCHQETDAHEDDLHVNDPEREYLERPSRDHLYLPLEPSYRESSLSPSPASSVSSRSWFSDASSCESLSHIYDDVDSELNEAAARFTLGSPLTSPGGSPGGCPGEESWHQQYGPGHSLSPRQSPCHSPRSSITDENWLSPRPASGPSSRPTSPCGKRRHSSAEVCYAGSLSPHHSPVPSPGHSPRGSVTEDTWLTAPVHTGSGLSPAPFPFQYCVETDIPLKTRKTSDDQAAILPGKLEVCSDDQGSLSPSRETSVDDGLGSQYPLKKDSSGDQFLSVPSPFTWSKPKPGHTPIFRTSSLPPLDWPLPTHFGQCELKIEVQPKTHHRAHYETEGSRGAVKASTGGHPVVKLLGYSEKPINLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIIASTKVLEIPLLPENNMSASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGKVLSLQIASIPVECSQRSAQELPHIEKYSINSCSVNGGHEMIVTGSNFLPESKIIFLEKGQDGRPHWEAEGKIIREKCQGGHIVLEVPPYHNPAVTSAVQVHFYLCNGKRKKSQSQRFTYTPVLMKQEQREDTDLSSVPSLPVPHSAQTQRPSSDTGHPHDSALSAPRSLICPVQPAYASMITSTHLPQLQCRDEGAGKEQHIIPSSVMHQPFQVTPTSPMGSSYQSIQTNMYNGPTCLPMNPASSQEFDPVLFQQDAALSNLVNLGCQPLSPIPFHSSNSDATGHLLAHSPHSVQTPPHLQSMGYHCSSAGQRSLSSPVAAQVTGQPSSHLQPITYCPSHPGSATAASPAASHALSSSPISGPPSPQLQSMPYQSPSSGTASSPSPVTRMHSGQHSTQAQSTGQGGLSVPSSLVCHSLCDPASFPPGGAAVSIKPEPEDQEPNFATIGLQDITLDDDQFMSDLEHQPSGSTEKWPNHSEFSCPVPFWRI
Protein: Probable nucleolar GTP-binding protein 1 (O94659)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the biogenesis of the 60S ribosomal subunit.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Pescadillo homolog
- GTPase grn1
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein nsa2
- Nucleolar GTP-binding protein 2
- Ribosome biogenesis protein rlp24
- 25S rRNA
- Uncharacterized RNA-binding protein C1827.05c
- Ribosome biogenesis protein erb1
- Nucleolar complex-associated protein 3
Sequence:
MATAVFKNITPIPDVNTFLDVVLSRTQRKTPTVIRSGFKISRIRGFYGRKVKFTQDTITEKLDSILQEFPKLNDIHPFHADLLNILYDRDHLKIALSQLSTAKHLVENVARDYIRLLKYGDSLYRCKQLKRAALGRMATIIKRQKSSLEFLEQVRQHLSRLPAIDPNTRTLLVCGYPNVGKSSFMNKVTRAQVDVQPYAFTTKSLFVGHFDYKYLRWQVIDTPGILDHPLEQMNTIEMQSITAMAHLRSAVLYFMDLSEMCGYSVAAQVKLYHSIKPLFANKVTILVLNKIDAMRPEDLDQKNQELLQTIIDDGNVKVVQTSCVQDIGVMDVRTTACEALLAARVEQKLKGSRVNNVLNRIHLAEPAARDEVARPACIPDSVKTRRAYDANDPNRRILARDIEAANGGAGVYNVELRDKYILQDPSWKYDRMPELLDGKNVADFVDPEIEAKLLALDEEEERLEREGYYDSDQEIEDADEEEVLEKASRIREKNKLTMLAARQKKIKNRPVLPRTAGIRTLDELQSSLQSAGLPSDSIEERARSRARTAAANEMADGSGVDLLMNEGEEIRSKSIAPRSQSNRRESGVHAEGARSYADRLARVKQIHRNRMARASESDRHVIAAKPKHLLSGKRGNGKTQRR
Protein: Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2] (P01025)
Organism: Sus scrofa (Pig)
Function: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Complement factor B
- Complement C2
- Complement factor H
- Complement factor I
- Integrin beta-2
- Plasminogen
- Complement C4A
- Complement factor D
- Complement C5a anaphylatoxin
- Haptoglobin
Sequence:
MGSTSGPRLLLLLLTSLPLALGDPIYTIITPNVLRLESEEMVVLEAHEGQGDIRVSVTVHDFPAKRQVLSSETTTLNNANNYLSTVNIKIPASKEFKSEKGHKFVTVQALFGNVQVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVDHKLLPVGQTIVVTIETPEGIDIKRDSLSSHNQFGILALSWNIPELVNMGQWKIRAHYEDAPQQVFSAEFEVKEYVLPSFEVQVEPSEKFYYIDDPNGLTVNIIARFLYGESVDGTAFVIFGVQDGDQRISLSQSLTRVPIIDGTGEATLSQGVLLNGVHYSSVNDLVGKSIYVSVTVILNSGSDMVEAERTGIPIVTSPYQIHFTKTPKFFKPAMPFDLMVYVTNPDGSPARHIPVVTEDFKVRSLTQEDGVAKLSINTPDNRNSLPITVRTEKDGIPAARQASKTMHVLPYNTQGNSKNYLHLSLPRVELKPGENLNVNFHLRTDPGYQDKIRYFTYLIMNKGKLLKVGRQPRESGQVVVVLPLTITTDFIPSFRLVAYYTLIAANGQREVVADSVWVDVKDSCVGTLVVKGGGKQDKQHRPGQQMTLEIQGERGARVGLVAVDKGVFVLNKKNKLTQRRIWDVVEKADIGCTPGSGKDFAGVFTDAGLAFKSSKGLQTPQRADLECPKPAARKRRSVQLMEKRMDKLGQYSKDVRRCCEHGMRDNPMKFSCQRRAQFIQHGDACVKAFLDCCEYIAKLRQQHSRNKPLGLARSDLDEEIIPEEDIISRSQFPESWLWTIEEFKEPDKNGISTKTMNVFLKDSITTWEILAVSLSDKKGICVADPYEVVVKQDFFIDLRLPYSVVRNEQVEIRAILYNYREAEDLKVRVELLYNPAFCSLATAKKRHQQTLTVPAKSSVPVPYIIVPLKTGLQEVEVKAAVYNHFISDGVKKTLKVVPEGMRVNKTVVTRTLDPEHKGQQGVQREEIPPADLSDQVPDTESETKILLQGTPVAQMVEDAIDGDRLKHLIQTPSGCGEQNMIGMTPTVIAVHYLDSTEQWEKFGLEKRQEALELIKKGYTQQLAFRQKNSAFAAFQDRLSSTLLTAYVVKVFAMAANLIAIDSQVLCGAVKWLILEKQKPDGVFEENGPVIHQEMIGGFKNTEEKDVSLTAFVLIALQEAKDICEPQVNSLLRSINKARDFLADYYLELKRPYTVAIAGYALALSDKLDEPFLNKLLSTAKERNRWEEPGQKLHNVEATSYALLALLVVKDFDSVPPIVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDVPDHKDLNLDVSIHLPSRSAPVRHRILWESASLLRSEETKENEGFTLIAEGKGQGTLSVVTMYHGKAKGKTTCKKFDLKVSIHPAPEPVKKPQEAKSSMVLDICTRYLGNQDATMSILDISMMTGFSPDTEDLKLLSTGVDRYISKYELNKALSNKNTLIIYLDKISHTLEDCISFKVHQYFNVGLIQPGSVKVYSYYNLDESCTRFYHPEKEDGMLNKLCHKEMCRCAEENCFMHHDEEEVTLDDRLERACEPGVDYVYKTRLLKKELSDDFDDYIMVIEQIIKSGSDEVQVGQERRFISHIKCREALKLKEGGHYLVWGVSSDLWGEKPNISYIIGKDTWVELWPDGDVCQDEENQKQCQDLANFSENMVVFGCPN
Protein: Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95) (Q63199)
Organism: Rattus norvegicus (Rat)
Function: Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P51867}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P51867}. Membrane raft {ECO:0000250|UniProtKB:P25445}.
Interaction partners:
- FAS-associated death domain protein
- Tumor necrosis factor ligand superfamily member 6
- Caspase-8
- CASP8 and FADD-like apoptosis regulator
- Death domain-associated protein 6
- Tumor necrosis factor receptor superfamily member 1A
- Caspase-3
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Tumor necrosis factor
- FAS-associated factor 1
Sequence:
MLWIMAVLPLVLAGPELNVRMQGTDSIFEGLELKRSVRETDNNCSEGLYQVGPFCCQPCQPGERKVKDCTTSGGAPTCHPCTEGEEYTDRKHYSDKCRRCAFCDEGHGLEVETNCTRTQNTKCRCKENFYCNASLCDHCYHCTSCGLEDILEPCTRTSNTKCKKQSSNYKLLWLLILPGLAILFVFIYKRYRKRQPGDPESGIPSPESVPMNVSDVNLNKYIWRTAEKMKICDAKKFARQHKIPESKIDEIEHNSPQDAAEQKIQLLQCWYQSHGKTGACQALIQGLRKANRCDIAEEIQAMVWEDHENSISNSRNENEGQSLE
Protein: EF-hand domain-containing protein (Q17744)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQAMSAPRNLRVWRLLRNRTNVSAASATQIQADVTPTKSAHPAELNVVSPPKRTASVPASRLNLNGTLDSNGNYGRKSASQSDLNYSAELSVAAPTRHAIPELDLTFDSYNDEQYRPTPKPTQVISRPLPPKPQAPKEPIYYPQGKPVPQLQNDTALRRVCEVFRSVPNQKCTLENMPAVCEAAGLPMYWKMPVFLAITNDEDRLATQVDFTSWWKAMTSVAHDEAARFVYTLTMGSRSYLQPEDFYEMLMDVIHTHPGLAFYRDATEFHDKYCQVVMTRIFWNDAHSWSGRLTTERLRKGGVLQAIRNLQFDDDINKSLRYFSYEHFYVVYCKFWEIDSDHDLKISSTDLAQHAGGALVPMVVDRIFSGAVCTNPNRGQPVEDIGLAEFTQFLLAEEDKTHPTSIEYWFRILDLDGDGLVTLYDMELFHTQVQRKLAAEGIDSMGFADVACQLIDMLNVPGGVSAFRLSDLKKSSLRGRFINTFVNWRKFFAQETNEGSESPRIEDEGGQELTEWDRYCIEEYEAMMEDDQADAETISLNLEEDDGRSSLAYHDVL
Protein: YY1-associated factor 2 (Q99LW6)
Organism: Mus musculus (Mouse)
Function: Binds to MYC and inhibits MYC-mediated transactivation. Also binds to MYCN and enhances MYCN-dependent transcriptional activation. Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of histone H3, suggesting that it is involved in chromatin-remodeling.
Subcellular location: Nucleus {ECO:0000269|PubMed:14557078}.
Interaction partners:
- E3 ubiquitin-protein ligase RING1
- E3 ubiquitin-protein ligase RING2
- Polycomb group RING finger protein 1
- Polycomb group RING finger protein 6
- Lysine-specific demethylase 2B
- RING1 and YY1-binding protein
- Polycomb group RING finger protein 5
- Lethal
- Polycomb group RING finger protein 3
- Polycomb group RING finger protein 2
Sequence:
MGDKKSPTRPKRQPKPASDEGYWDCSVCTFRNSAEAFKCMMCDVRKGTSTRKPRPVSQLVAQQVTQQFVPPTQSKKEKKDRVEKDKSEKEAASKKNCHKKTRPRLKNVDRSSAQHLEVTVGDLTVIITDFKEKAKSAPASSAAGDQHSQGSCSSDSTERGVSRSSSPRGEASSLNGESH
Protein: Homeobox protein HMX2 (Homeobox protein H6 family member 2) (A2RU54)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in specification of neuronal cell types and which is required for inner ear and hypothalamus development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MGSKEDAGKGCPAAGGVSSFTIQSILGGGPSEAPREPVGWPARKRSLSVSSEEEEPDDGWKAPACFCPDQHGPKEQGPKHHPPIPFPCLGTPKGSGGSGPGGLERTPFLSPSHSDFKEEKERLLPAGSPSPGSERPRDGGAERQAGAAKKKTRTVFSRSQVYQLESTFDMKRYLSSSERACLASSLQLTETQVKTWFQNRRNKWKRQLSAELEAANMAHASAQTLVSMPLVFRDSSLLRVPVPRSLAFPAPLYYPGSNLSALPLYNLYNKLDY
Protein: Liprin-alpha-2 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-2) (PTPRF-interacting protein alpha-2) (O75334)
Organism: Homo sapiens (Human)
Function: Alters PTPRF cellular localization and induces PTPRF clustering. May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. In neuronal cells, is a scaffolding protein in the dendritic spines which acts as immobile postsynaptic post able to recruit KIF1A-driven dense core vesicles to dendritic spines.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9624153}. Cell surface {ECO:0000269|PubMed:9624153}. Cell projection, dendritic spine {ECO:0000269|PubMed:30021165}. Note=Colocalizes with PTPRF at the cell surface.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Peripheral plasma membrane protein CASK
- Regulating synaptic membrane exocytosis protein 1
- ARF GTPase-activating protein GIT1
- Liprin-beta-1
- Liprin-beta-2
- Protein lin-7 homolog A
- Receptor-type tyrosine-protein phosphatase S
- Receptor-type tyrosine-protein phosphatase F
Sequence:
MMCEVMPTINEDTPMSQRGSQSSGSDSDSHFEQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGGLAGSKGADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNLARVHPGTSITASVTASSLASSSPPSGHSTPKLTPRSPAREMDRMGVMTLPSDLRKHRRKIAVVEEDGREDKATIKCETSPPPTPRALRMTHTLPSSYHNDARSSLSVSLEPESLGLGSANSSQDSLHKAPKKKGIKSSIGRLFGKKEKARLGQLRGFMETEAAAQESLGLGKLGTQAEKDRRLKKKHELLEEARRKGLPFAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPPTSRTPSGNVWVTHEEMENLAAPAKTKESEEGSWAQCPVFLQTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRLNYDRKELERRREASQHEIKDVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLLALGTERRLDESDDKNFRRGSTWRRQFPPREVHGISMMPGSSETLPAGFRLTTTSGQSRKMTTDVASSRLQRLDNSTVRTYSC