wanglab/gogpt-training-data huggingface dataset:
Protein: CENP-A multicopy suppressor protein 2 (Q9URT4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for proper chromosome segregation via regulation of CENP-A localization to the centromere.
Subcellular location: Nucleus {ECO:0000269|PubMed:12535531}. Chromosome, centromere {ECO:0000269|PubMed:12535531}.
Interaction partners:
- F-box/TPR repeat protein pof3
- Histone H3-like centromeric protein cnp1
Sequence:
MMEKSLNTVTSLPLRVIYCIDRASAIRCLAKSQHAVPIQVLKEVEPKKVICQVDIQHVIQTVCRCSPELSCKSQGDFSVYFLDHTEPDELFVGLGYWSSLLLSPTLNAGTSNSDTVWVNGFIVEFGIQRSIEIKLRFQSLQNSFEVGTPETHTSSKFLSSTLPPSLIFDPSSSEKSDSISGSLFDTNYTCPVNINGLSKQKSVRELKSPSRPSALAETNVEELELDSLFHASNDISCSATSFSEPYILDHQAALDHPATDPVCSASSTTVNSAVSTKKRRRESSTISPESAYVAAQLQNPSEREQVHEFIKEQVRIARGRIEKKFTNVRGKNRIEEQLTLSLQEGKIPPYCQNCGTIKTANWRNATYMNITLMLCNACGIYWTSRRSMRPRNLWSTYKAFETEKPLENDAFAQLELAVYKLSQQRKLSISIFRELENAGRHSPLNRLTSLDSTHSAPDPNHISKPSVVNQQKSRGGPRTAKLKNDLRRIQSSPIVAPTPDTSFREPLSEIGSNDSWLVLPNSLSANIQNDVLRKTDFMCTDKENVAFPLKTTTKPMPKVNKEETEPTLPVCDSEKENDDLECYFRTPPKPTTLQKQQQSPSPWRSELFLSDPDQNVLTPRHKPKFDLSKALSSVAKSNNIENSPQLPERYDFSLELGLNSQLDNEERRDIPLMTDLVMPSSPPMVPADRHLSVENTC
Protein: Transcription factor SKN7 (Q5A4X5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor that is part of a SLN1-YPD1-SKN7 two-component regulatory system, which controls gene expression in response to changes in the osmolarity of the extracellular environment. Under low osmotic conditions, phosphorylated and activated by the phosphorelay intermediate protein YPD1. Also activated in response to oxidative stress, independent on the two-component regulatory system. Regulates heat shock genes in response to oxidative stress and genes involved in cell wall integrity in response to osmotic changes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P38889}.
Interaction partners:
- Phosphorelay intermediate protein YPD1
- Heat shock protein 90 homolog
- 14-3-3 protein homolog
- Uncharacterized protein
- Flavin reductase like domain-containing protein
- Serine/threonine-protein kinase TOR
- Elongation factor 1-alpha 1
- Elongation factor 1-alpha 2
- Glycogen synthase kinase 1
- Ubiquitin-binding TORC1 subunit
Sequence:
MSSLQQPIPPNSTLATTASSNQSGSNDFVKKLFLMLQEDSYKEVVRWTVKGDSFVVINTNEFTKDILPKHFKHSNFASFVRQLNKYDFHKVKISNEAKASYPYGEDAWEFKHPEFRINDAEALENIKRKGPTAKKSASNVTIKTEANNNGTQPTCNHNYSQLVSATNHLKEQVESLKNDKHSLYQEISVLERKYKTVVENIVAINTFNERYYRSMNVLINSIVQNGMKLPPLDFPPPVQLGPDSGIGSNLGPISSDTALPSISHHLSSPLPHHQQLLNRTIRPISSPIDGIPLVKLQQQSLGQNLQAPIGTPSAVPFSEEASSSIQAATPAPLAQPVAQPINQPPPPPPPPATQQQPLPPPPPPATATSQIPSAPPPPTQQQVGTSSSSVPTISPKSQGIVVSNSASPTTSAQISTTSVPNPKFHVLLVEDDNVCIQLCRKFLVKYGCSVTVVTDGLNAISTVEHTKYDLVLMDIVMPNLDGATATSVIRSFDTKTPIIAMTGNIEDNDLVTYLQNGMSDILAKPFTKDDLYAILSKHLLDPKENKQDNEPTVKKQKLS
Protein: Antigen peptide transporter 1 (APT1) (EC 7.4.2.14) (ATP-binding cassette sub-family B member 2) (Peptide transporter TAP1) (P36370)
Organism: Rattus norvegicus (Rat)
Function: ABC transporter associated with antigen processing. In complex with TAP2 mediates unidirectional translocation of peptide antigens from cytosol to endoplasmic reticulum (ER) for loading onto MHC class I (MHCI) molecules (By similarity). Uses the chemical energy of ATP to export peptides against the concentration gradient (By similarity). During the transport cycle alternates between 'inward-facing' state with peptide binding site facing the cytosol to 'outward-facing' state with peptide binding site facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2 induces a switch to hydrolysis-competent 'outward-facing' conformation ready for peptide loading onto nascent MHCI molecules. Subsequently ATP hydrolysis resets the transporter to the 'inward facing' state for a new cycle (By similarity). As a component of the peptide loading complex (PLC), acts as a molecular scaffold essential for peptide-MHCI assembly and antigen presentation (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q03518}; Multi-pass membrane protein {ECO:0000255}. Note=The transmembrane segments seem to form a pore in the membrane.
Interaction partners:
- Antigen peptide transporter 2
- TAP binding protein
- Calreticulin
- Calreticulin
- Protein disulfide-isomerase A3
- Proteasome subunit beta type-9
- Beta-2-microglobulin
- Proteasome subunit beta type-8
- RT1 class Ib, locus S3
- Interferon regulatory factor 1
Sequence:
MAAHAWPTAALLLLLVDWLLLRPVLPGIFSLLVPEVPLLRVWAVGLSRWAILGLGVRGVLGVTAGARGWLAALQPLVAALGLALPGLASFRKLSAWGALREGDNAGLLHWNSRLDAFVLSYVAALPAAALWHKLGGFWAPSGHKGAGDMLCRMLGFLDSKKGRLHLVLVLLILSCLGEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEALAAPSD
Protein: AT03939p (Glutamate carrier 2, isoform B) (Q8INJ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- Mitochondrial glutamate carrier 2
- Protein encore
Sequence:
MLEQVEQKNQEQKKPQKFNVFPKIINGGVAGIIGVACVYPLDMVKTRLQNQTIGPNGERMYTSIADCFRKTIASEGYFGMYRGSAVNIVLITPEKAIKLTANDFFRYHLASDDGVIPLSRATLAGGLAGLFQIVVTTPMELLKIQMQDAGRVAAADRAAGREVKTITALGLTKTLLRERGIFGLYKGVGATGVRDITFSMVYFPLMAWINDQGPRKSDGSGEAVFYWSLIAGLLSGMTSAFMVTPFDVVKTRLQADGEKKFKGIMDCVNRTLKEEGISAFFKGGLCRIMVLAPLFGIAQMFYFLGVGEKILGIERTKSV
Protein: At3g16350 (Homeodomain-like superfamily protein) (Q84TG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Receptor-like protein 7
- MACPF domain-containing protein At4g24290
- Protein RADIALIS-like 4
Sequence:
MTRRCSHCSNNGHNSRTCPTRGGGTCGGSGGGGGGGGGGGSGSSSAVKLFGVRLTDGSIIKKSASMGNLSALAVAAAAATHHRLSPSSPLATSNLNDSPLSDHARYSNLHHNEGYLSDDPAHGSGSSHRRGERKRGVPWTEEEHRLFLVGLQKLGKGDWRGISRNYVTSRTPTQVASHAQKYFIRHTSSSRRKRRSSLFDMVTDEMVTDSSPTQEEQTLNGSSPSKEPEKKSYLPSLELSLNNTTEAEEVVATAPRQEKSQEAIEPSNGVSPMLVPGGFFPPCFPVTYTIWLPASLHGTEHALNAETSSQQHQVLKPKPGFAKERVNMDELVGMSQLSIGMATRHETETSPSPLSLRLEPSRPSAFHSNGSVNGADLSKGNSAIQAI
Protein: Muskelin (O89050)
Organism: Mus musculus (Mouse)
Function: Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Required for internalization of the GABA receptor GABRA1 from the cell membrane via endosomes and subsequent GABRA1 degradation. Acts as a mediator of cell spreading and cytoskeletal responses to the extracellular matrix component THBS1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9724633}. Cytoplasm, cytosol {ECO:0000269|PubMed:18710924}. Nucleus, nucleoplasm {ECO:0000269|PubMed:18710924}. Cell projection, ruffle {ECO:0000269|PubMed:9724633}. Cytoplasm, cell cortex {ECO:0000269|PubMed:9724633}. Synapse {ECO:0000269|PubMed:21482357}. Postsynapse {ECO:0000269|PubMed:21482357}. Note=Colocalizes with GABRA1 at synapses and in postsynaptic regions (PubMed:21482357). Colocalizes with actin fibers in the cell cortex. {ECO:0000269|PubMed:21482357, ECO:0000269|PubMed:9724633}.
Interaction partners:
- Glucose-induced degradation protein 8 homolog
- Ran-binding protein 9
- Ran-binding protein 10
- WD repeat-containing protein 26
- E3 ubiquitin-protein transferase RMND5B
- Armadillo repeat-containing protein 8
- E3 ubiquitin-protein transferase MAEA
- E3 ubiquitin-protein ligase RMND5A
- Glucose-induced degradation protein 4 homolog
- Protein yippee-like 5
Sequence:
MAAGGAVAVAPECRLLPYALHKWSSFSSTYLPENILVDKPNDQSSRWSSESNYPPQYLILKLERPAIVQNITFGKYEKTHVCNLKKFKVFGGMNEENMTELLSSGLKNDYNKETFTLKHKIDEQMFPCRFIKIVPLLSWGPSFNFSIWYVELSGIDDPDIVQPCLNWYSKYREQEAIRLCLKHFRQHNYTEAFESLQKKTKIALEHPMLTDMHDKLVLKGDFDACEELIEKAVNDGLFNQYISQQEYKPRWSQIIPKSTKGDGEDNRPGMRGGHQMVIDVQTETVYLFGGWDGTQDLADFWAYSVKENQWTCISRDTEKENGPSARSCHKMCIDIQRRQIYTLGRYLDSSVRNSKSLKSDFYRYDIDTNTWMLLSEDTAADGGPKLVFDHQMCMDSEKHMIYTFGGRILTCNGSVDDSRASEPQFSGLFAFNCQCQTWKLLREDSCNAGPEDIQSRIGHCMLFHSKNRCLYVFGGQRSKTYLNDFFSYDVDSDHVDIISDGTKKDSGMVPMTGFTQRATIDPELNEIHVLSGLSKDKEKREENVRNSFWIYDIVRNSWSCVYKNDQATKDNLSKSLQEEEPCPRFAHQLVYDELHKVHYLFGGNPGKSCSPKMRLDDFWSLKLCRPSKDYLLRHCKYLIRKHRFEEKAQMDPLSALKYLQNDLYITVDHSDPEETKEFQLLASALFKSGSDFTALGFSDVDHTYAQRTQLFDTLVNFFPDSMTPPKGNLVDLITL
Protein: Fibulin-1 (FIBL-1) (P23142)
Organism: Homo sapiens (Human)
Function: Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. Has been implicated in a role in cellular transformation and tumor invasion, it appears to be a tumor suppressor. May play a role in haemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots. Could play a significant role in modulating the neurotrophic activities of APP, particularly soluble APP.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Fibronectin
- Aggrecan core protein
- Fibulin-2
- Ras association domain-containing protein 8
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Elastin
- Microfibrillar-associated protein 2
- Nidogen-1
- Microfibril-associated glycoprotein 4
- Versican core protein
Sequence:
MERAAPSRRVPLPLLLLGGLALLAAGVDADVLLEACCADGHRMATHQKDCSLPYATESKECRMVQEQCCHSQLEELHCATGISLANEQDRCATPHGDNASLEATFVKRCCHCCLLGRAAQAQGQSCEYSLMVGYQCGQVFQACCVKSQETGDLDVGGLQETDKIIEVEEEQEDPYLNDRCRGGGPCKQQCRDTGDEVVCSCFVGYQLLSDGVSCEDVNECITGSHSCRLGESCINTVGSFRCQRDSSCGTGYELTEDNSCKDIDECESGIHNCLPDFICQNTLGSFRCRPKLQCKSGFIQDALGNCIDINECLSISAPCPIGHTCINTEGSYTCQKNVPNCGRGYHLNEEGTRCVDVDECAPPAEPCGKGHRCVNSPGSFRCECKTGYYFDGISRMCVDVNECQRYPGRLCGHKCENTLGSYLCSCSVGFRLSVDGRSCEDINECSSSPCSQECANVYGSYQCYCRRGYQLSDVDGVTCEDIDECALPTGGHICSYRCINIPGSFQCSCPSSGYRLAPNGRNCQDIDECVTGIHNCSINETCFNIQGGFRCLAFECPENYRRSAATLQQEKTDTVRCIKSCRPNDVTCVFDPVHTISHTVISLPTFREFTRPEEIIFLRAITPPHPASQANIIFDITEGNLRDSFDIIKRYMDGMTVGVVRQVRPIVGPFHAVLKLEMNYVVGGVVSHRNVVNVHIFVSEYWF
Protein: Exocyst complex component sec5 (O94598)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Localized at the cell tip and barrier septum.
Interaction partners:
- Exocyst complex component sec6
- Exocyst complex component sec10
- Uncharacterized protein C17G8.12
- Exocyst complex component sec15
- Exocyst complex component exo84
- Exocyst complex component sec8
- Exocyst complex component exo70
Sequence:
MSADEEILAHYGLTSLSQDYWTEKPDFAIANASVDVQSPTTGVHHERNRSEDILRTGGATSETTKDASAAGPVTPSFAMKRSQTSVQPSMSSQIAIGGMRNPMATRKIAGTYRDAPDNSMQQTSTGVHRSSSWLTTDGTHQLLSLMETNFNKFIAAKETIDNVYAQIISTLSHAGPAKTMDMCEESISGALQQLQLFNTESTNEVDISYGELLVMRECEALFTYPEKFRLYHKQEKYSLLMQEIENAKKLYEKDRERLAKVNPKLVYLVDHAWEIIQATIDGICASIWNQILQSQGDFAFVVRTLCDLLKLKPNPISGRDPVLYATVSQQKYLYNLMKERFSYFEKIIKSRQEDFSKLSCTRASPMLVWRAVARGCNLDYTLRGRPEVFAGMQLIEWANACVLKIVREIKEVELYAKEFISGIQQASYPEAAKHYGRDPKQMGVVVEKLNSQCLEMVYSFVGERGERLEMDGAFVLIQLHYFQRVADLLPKRIRTVFSMAATRCIVDTWMLQHAPQSKSANIEEMFIVDANENQVLEPELMVVDVLRELNKLYIPPHREEIVREIHHAFYKVLYANARFPSMSVSMANWESDVWSLASSTLIDFVQHRNQHDMKKLASKMTTSLPVFSTSITRSDVLHFVTRLLNLRSRLVPYQKFLLQTFPLNEVSPSLDPRISKSLRNLQDLYKLLAIRDTSFSNTTPSSISKLSIQPPTFQLFSTLETIYLELKDSMPPNEAADWMIATTSCMLAQFALHSPYAFFHDIPSISHFLNKCLPPTILDLLQQIQRKAEASSISPTTETATKTRLKFQFIEMIFS
Protein: RE10840p (Q8IGX2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MASVFMRIFNLICMMLLIGHWSGCLQFLVPMLQGFPSNSWVSINELQESYWLEQYSWALFKAMSHMLCIGYGRFPPQSLTDMWLTMLSMISGATCYALFLGHATNLIQSLDSSRRQYREKVKQVEEYMAYRKLPRDMRQRITEYFEHRYQGKFFDEELILGELSEKLREDVINYNCRSLVASVPFFANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIVMANGEVATSLSDGSYFGEICLLTNARRVASVRAETYCNLFSLSVDHFNCVLDQYPLMRKTMETVAAERLNKIGKNPNIMHQKDEQLSNPESNTITAVVNALAAEADDCKDDDMDLKENLLHGSESSIAEPVQTIREGLPRPRSGEFRALFEGNTP
Protein: Type 2A phosphatase-associated protein 42 (Q04372)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in negative regulation of the TOR signaling pathway in response to type of available nitrogen source. Inhibitor of PP2A phosphatase SIT4, which results in inhibition of nuclear export of MSN2, due to lack of dephosphorylation by SIT4. Also required for rapamycin induced activation of expression of many nitrogen discrimination pathway (NDP) genes. In complex with PPH21, required for organization of the actin cytoskeletom during the cell cycle via a Rho GTPase-dependent mechanism.
Interaction partners:
- Type 2A phosphatase activator TIP41
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase PP1-1
- Serine/threonine-protein kinase TOR1
- Serine/threonine-protein kinase TOR2
- Target of rapamycin complex 1 subunit KOG1
- Target of rapamycin complex subunit LST8
- Serine/threonine-protein phosphatase PP2A-like PPG1
Sequence:
MASVTEQFNDIISLYSTKLEHTSLRQDSPEYQGLLLSTIKKLLNLKTAIFDRLALFSTNETIDDVSTASIKFLAVDYYLGLLISRRQSNDSDVAQRQSMKLIYLKKSVESFINFLTLLQDYKLLDPLVGEKLGNFKDRYNPQLSELYAQPKNNKDLSGAQLKRKEKIELFQRNKEISTKLHCLELELKNNDEDHDHDELLRELYLMRLHHFSLDTINNIEQNLFECEMLSNFLKNSVHEVKSSGTQIRKESNDDDSTGFTDKLENINKPLIDKKGQVLRNFTLVDKRQQLQQKVRGYGQYGPTMSVEEFLDKEFEEGRVLQGGEEPEQAPDEENMDWQDRETYKAREWDEFKESHAKGSGNTMNRG
Protein: Malonyl-CoA decarboxylase (B9K0V9)
Organism: Allorhizobium ampelinum (strain ATCC BAA-846 / DSM 112012 / S4) (Agrobacterium vitis (strain S4))
Interaction partners:
- Biotin carboxylase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- methylmalonate-semialdehyde dehydrogenase
- Acyl-CoA thiolase
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
- biotin carboxylase
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
- biotin carboxylase
- Beta-ketothiolase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Sequence:
MAGTSFLSDLLSGVTERGRALLFSGSKARDRVVDTDIETLCEMLLSSRGEASGMAIAAEILDRWSRFNAAEAVQFLHMLSDRFGAEAAALDKAIDAYRTDKSPMAVIALHNAAEPRRQELLRRLNLAPNGTQKLVRMRERLLETKEDRADLGAVDTDFAHLFSSWFNRGFLTLQPIDWTTPAHILEKIIKYEAVHEIAGWEELRRRLAPADRRCFAFFHPRLRDDPLVFVEVALTRSIPSAIADVLDESRDHIGADTATTAVFYSISNCQDGLRGISFGNFLIKQVVEDLRRDLPGLKEFVTLSPVPGFARWISKIRDPKSGFPLSPEDRNTLVLLDDPTWPEDKARADAVERILLPLAARYFITERTPDNRPVDPVARFHLGNGARLERLNFLGDRSVKAMRQAHGLMVNYLYKLEDIETNHEALAQRGEVAASPAVKALQGKIEPILPEKPKDIKKAESLSGS
Protein: Heptahelical transmembrane protein 5 (PAQR family protein HHP5) (Q9SVF3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in abiotic stress response.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- AT3g59090/F17J16_140
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 8
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 6
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 7
- Tobamovirus multiplication protein 3
- At3g09570
- G-protein coupled receptor 1
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 2
Sequence:
MGDEAEIKEHLKPQASSETIDKKHNVKGKRLWQKVKYQLVEFHSLPAYLRDNEYIIGHYRSEWPIKQILLSIFTIHNETLNVWTHLIGFFLFLALTIYTATKVPSVVDLHSLQHRLPDLLRKTDLHKLHSELMSRLPSSPSSWHVMDLLYNCLPERFSHGNYTDMCVLHSVREDLANLIAPLIFRPITRWPFYAFLGGAIFCLLASSTCHLLSCHSERVSYIMLRLDYAGIAALIATSFYPPVYYSFMCDPFFCNLYLGFITILGIATVLVSLLPVFQSLEFRVVRASLFFGMGFSGLAPILHKLIIFWDQPEALHMTGYEILMGLLYGLGAVVYATRIPERWMPGKFDIAGHSHQLFHVLVVAGALTHYRAGL
Protein: Serine/arginine-rich splicing factor 5 (Delayed-early protein HRS) (Pre-mRNA-splicing factor SRP40) (Splicing factor, arginine/serine-rich 5) (O35326)
Organism: Mus musculus (Mouse)
Function: May be required for progression through G1 and entry into S phase of cell growth. May play a regulatory role in pre-mRNA splicing. Autoregulates its own expression. Plays a role in constitutive splicing and can modulate the selection of alternative splice sites (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SRSF protein kinase 1
- Serine and arginine-rich splicing factor 11
- Splicing factor U2AF 65 kDa subunit
- Serine/arginine-rich splicing factor 2
- Serine/arginine-rich splicing factor 7
- Serine/arginine-rich splicing factor 3
- Pre-mRNA-splicing factor SLU7
- Polyadenylate-binding protein 2
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 9
Sequence:
MSGCRVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCSERVTIEHARARSRGGRGRGRYSDRFSSRRPRNDRRNAPPVRTENRLIVENLSSRVSWQDLKDFMRQAGEVTFADAHRPKLNEGVVEFASYGDLKNAIEKLSGKEINGRKIKLIEGSKRHRSRSRSRSRTRSSSRSRSRSRSRRSKSYSRSRSRSRSRSKSRSGSRSPVPEKSQKRGSSSRSKSPASVDRQRSRSRSRSRSVDSGN
Protein: P-type Cu(+) transporter (EC 7.2.2.8) (Q9VYT4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}. Membrane {ECO:0000256|RuleBase:RU362081}.
Interaction partners:
- Copper transport protein ATOX1
- Superoxide dismutase
- Copper transport protein
- Copper transport protein
- Cytochrome c oxidase assembly protein COX11
- Copper transport protein
- AT19154p
- Protein Malvolio
- Metal response element-binding transcription Factor-1, isoform C
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
Sequence:
MPSDERVEATMSTVRLPIVGMTCQSCVRNITEHIGQKSGILGVRVILEENAGYFDYDPRQTDPARIASDIDDMGFECSYPGDAADPPETPASAWTNIRVVGMTCQSCVRNIEGNIGTKPGIHSIEVQLAAKNARVQYDPAQYDPAQIAELIDDMGFEASVQEPRSPSQSPSPAPASSPKKRATPTPPPPSYAQNGSAVAIPVEQELLTKCFLHIRGMTCASCVAAIEKHCKKIYGLDSILVALLAAKAEVKFNANVVTAENIAKSITELGFPTELIDEPDNGEAEVELEIMGMTCASCVNKIESHVLKIRGVTTASVTLLTKRGKFRYITEETGPRSICEAIEALGFEAKLMTGRDKMAHNYLEHKEEIRKWRNAFLVSLIFGGPCMVAMIYFMLEMSDKGHANMCCLVPGLSMENLVMFLLSTPVQFFGGFHFYVQSYRAIKHGTTNMDVLISMVTTISYVYSVAVVIAAVLLEQNSSPLTFFDTPPMLLIFISLGRWLEHIAKGKTSEALSKLLSLKAADALLVEISPDFDIISEKVISVDYVQRGDILKVIPGAKVPVDGKVLYGHSSCDESLITGESMPVAKRKGSVVIGGSINQNGVLLVEATHTGENTTLAQIVRLVEEAQTSKAPIQQLADRIAGYFVPFVVVVSSITLIAWIIIGFSNPNLVPVAMEHKMHMDQNTIIVSYAFKCALSVLAIACPCALGLATPTAVMVATGTGAINGVLVKGATALENAHKVKTVVFDKTGTITHGTPMTSKVTLFVTAQVCSLARALTIVGAAEQNSEHPIASAIVHFAKDMLNVGATPQAGSFGKSSHFQAVPGCGIRVTVSNYEQTLRQACNADRIINYENLHRTHPQGSVPVDNGASIEHLLPQRSVRKSMELNNQQLLSDLVLEPEEELLTDQKIIDSPEILVLIGNREWMERNAIEVPLEISDCMTHEERKGHTAVLCALNGQLVCMFAVSDMVKPEAHLAVYTLKRMGIDVVLLTGDNKNTAASIAREVGIRTVYAEVLPSHKVAKIQRIQANGIRVAMVGDGVNDSPALAQADVGITIAAGTDVAAEASDIVLMRNDLLDVVACLDLSRCTVRRIRYNFFFASMYNLLGIPLASGLFAPYGFTLLPWMASVAMAASSVSVVCSSLLLKMYRKPTAKTLRTAEYEAQLAAERASGSEDELDKLSLHRGLDDLPEKGRMPFKRSSTSLISRIFMHDYGNITSPDAKYGEGLLDPEEQYDGRTKIVRSRFHANDSTELQKL
Protein: ADAM metallopeptidase domain 28 (A0A8I6A4B8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQQWRLLVVWFLLSPVPASAIKELPKAKNYEVVYPIRLHLLHKRETKEPEPKETFETELRYKMTVNGKVVELYLKKNNKLLAPGYLETYYNSSGNKVTTSPQIMDSCYYQGHIINEKDSAASISMCQGLRGYFSQADERYFIEPLSSEILDEQAHALFKDDPKEDQENSNCGVDDALWLQGLHQDVVLPATRLIKLNDGMVQEPKKYIEYYVVLDNGEFKKYNKNLDEIRKRVHEMANYVNMLYNKLDAHVALVGMEIWTDEDKIKITPDANTTLENFSKWRGNDLLKRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHDYLSCKCPSEVCVMEQSLRFHMPTDFSSCSRDNYRRFLEEKLSHCLFNSPLPSDIISTPVCGNQLLEMNEDCDCGTPKECTNKCCDAETCKIKAGFQCALGECCEKCQLKKPGVVCRAAKDECDLPEMCDGKSSHCPVDRFRVNGFPCQNGHGYCLKGNCPTLQQQCMDMWGPETKVANKSCYKQNEGGSKYGYCHVENGTHMPCKAKDAMCGKLFCEGGSGDLPWKGLTIAFLTCKLFDPEDINQGVDMVANGTKCGNNKVCINAECVDMEKTYKSANCSSKCKGHAVCDHELQCQCKEGWAPPDCEDSATVFRYHPSRMPSYTSRSVDPKS
Protein: Histone H1 [Cleaved into: SAMP H1] (P84408)
Organism: Salmo salar (Atlantic salmon)
Function: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.
Subcellular location: Nucleus. Chromosome.; SUBCELLULAR LOCATION: [SAMP H1]: Secreted.
Interaction partners:
Sequence:
MAEVAPAPAAAAPAKAPKKKAAAKPKKAGPSVGELIVKAVSASKERSGVSLAALK
Protein: Gremlin-1 (Cysteine knot superfamily 1, BMP antagonist 1) (Down-regulated in Mos-transformed cells protein) (O35793)
Organism: Rattus norvegicus (Rat)
Function: Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as a BMP antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop. Down-regulates the BMP4 signaling in a dose-dependent manner (By similarity). Antagonist of BMP2; inhibits BMP2-mediated differentiation of osteoblasts (in vitro) (By similarity). Acts as inhibitor of monocyte chemotaxis. Can inhibit the growth or viability of normal cells but not transformed cells when is overexpressed.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Bone morphogenetic protein 2
- Gremlin
- Bone morphogenetic protein 4
- Bone morphogenetic protein 7
- Bone morphogenetic protein 6
- Bone morphogenetic protein 5
- Growth/differentiation factor 5
- Growth differentiation factor 7
Sequence:
MNRTAYTVGALLLLLGTLLPAAEGKKKGSQGAIPPPDKAQHNDSEQTQSPPQPGSRTRGRGQGRGTAMPGEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVKQCRCISIDLD
Protein: Protein Wnt-11 (Protein Wnt-11-related) (Wnt11-R) (Wnt11r) (Q670P5)
Organism: Xenopus laevis (African clawed frog)
Function: Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Shares much functionality with wnt11b. Signals through a non-canonical Wnt pathway to activate Jun-N-terminal kinase (JNK) to regulate gastrulation movements. Acts in a non-cell-autonomous manner to control neural crest migration, probably acting as an extracellular signal from surrounding tissue, but is not required for neural crest induction. Acts redundantly with wnt11b during pronephros induction. Regulates cardiac morphogenesis through the activation of JNK, but is not required for cardiac differentiation. Essential for dorsal fin development; required for an epithelial to mesenchymal transformation event prior to migration of cells into the fin, and ultimately for maintenance of fin structure. Mediates dorsal fin development through a non-canonical pathway mediated by Ca(2+).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18942153}.
Interaction partners:
Sequence:
MKIYFLLGTFLTFLLHTRICQGIKWLALSKTPLSLPLNQTQHCKQLEGLVSSQMQLCRSNLELMQTIIHAAKEVKKTCVKAFTDMRWNCSSIELAPTFHQDLERGTRESAFVHALSAAAISHTIARACTTGDIPGCSCAPIPGESPGPGYRWGGCADNLNYGILMGSKFSDAPMKMKKSGSQANKLMHLHNSEVGRQVLKASLEMKCKCHGVSGSCSIKTCWRGLQELREIALDLKTKYLSATKVVHRPMGTRKHLVPKDIDIRPVQETELIYLQSSPDYCLKNEKIGSHGTHERQCNKTSNGSDSCDLMCCGRGYNPYMDKVVERCLCKYHWCCYVTCKKCERTVERYVCK
Protein: Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (Phosphotyrosyl phosphatase activator) (F6WIT2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU361210}.
Interaction partners:
Sequence:
MGKWKRSQAYADYIGFILTLNEGVKGKKLTFEYRVSEAIEKLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLVATVVPTHLAAAVPEVAVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAIVFKVFNRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLECILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHPVTSG