wanglab/gogpt-training-data huggingface dataset:
Protein: Inositol phosphosphingolipids phospholipase C (IPS phospholipase C) (IPS-PLC) (EC 3.1.4.-) (O74369)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Inositol phosphosphingolipids phospholipase essential for the coordination of cell wall formation. Responsible for the hydrolysis of the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol phosphorylceramide (M(IP)2C).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11514435}; Multi-pass membrane protein {ECO:0000269|PubMed:11514435}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11514435}; Multi-pass membrane protein {ECO:0000269|PubMed:11514435}.
Interaction partners:
- Sphingolipid delta
- Tubulin gamma chain
- Phosphoglucomutase
- Meiotic recombination protein rec14
Sequence:
MSVEKAPELRVLSFNCWGLRFVSKYRTERLKAVGEKLAKCDYDIVLLQEVWSIYDFQEIRNLVSCNLVYSRFFHSAAMGAGLAMFSKFPIIESSMNKYPLNGRPQAFWRGDWYVGKGVATASLQHPSGRIISLFNTHLHAPYGKGADTYLCHRLSQAWYISKLLRAAVQRGHIVIAAGDFNIQPLSVPHEIITSYGLVNDAWLSVYPDQVEHPPNRFSMNDKELVEIAGTTCDSRLNTWRENISSKDMDDFVAKRLDYVFHSPSTCEAKNAKVVFLERVPKLDCSYSDHFAIETVLSIKLQPIPVQETRVSYSIIDDTLGITYQYMARERLHMRLRIAHLLISIPLIIGVHVAIAWCDPAWLKVIILFFTVMLTIAAVVNGFCIGLLFGRWEFNGLLEFVAELKEQKLLCKQYLVDHPLPFAKS
Protein: Large ribosomal subunit protein bL12 (50S ribosomal protein L7/L12) (L8) (P0A7K2)
Organism: Escherichia coli (strain K12)
Function: The binding site for several of the GTPase factors involved in protein synthesis (IF-2, EF-Tu, EF-G and RF3). Is thus essential for accurate translation. Deletion of 1 of the L12 dimers from the ribosome (by deleting the binding site on L10) leads to decreased IF-2 association with the 70S ribosome and decreased stimulation of the GTPase activity of EF-G.
Interaction partners:
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein bL20
- Elongation factor G
- Small ribosomal subunit protein bS18
- Small ribosomal subunit protein bS16
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL18
Sequence:
MSITKDQIIEAVAAMSVMDVVELISAMEEKFGVSAAAAVAVAAGPVEAAEEKTEFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGVSKDDAEALKKALEEAGAEVEVK
Protein: 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component beta chain) (BCKDE1B) (BCKDH E1-beta) (Q6P3A8)
Organism: Mus musculus (Mouse)
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P21953}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Branched-chain-amino-acid aminotransferase, cytosolic
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Sequence:
MAAVAARAGGLLWLRAAGAERRRCGLRCAALVQGFLQPGGEDTAQKRRVAHFTFHPDPESLQYGQTQKMNLFQSITSALDNSLAKDPTAVIFGEDVAFGGVFRCTVGLRDKYGKDRVFNTPLCEQGIVGFGIGIAVTGATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSLTIRAPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQAKGLLLSCIEDKNPCIFFEPKILYRAAVEQVPVEPYKIPLSQAEVIQEGSDVTLVAWGTQVHVIREVASMAQEKLGVSCEVIDLRTIVPWDVDTVCKSVIKTGRLLISHEAPLTGGFASEISSTVQEECFLNLEAPISRVCGYDTPFPHIFEPFYIPDKWKCYDALRKMINY
Protein: Mitochondrial S-adenosylmethionine carrier protein (Solute carrier family 25 member 26) (H7C430)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKHMLAASAGEVVACLIRVPSEVVKQRAQVSASTRTFQIFSNILYEEGIQGLYRGYKSTVLREIPFSLVQFPLWESLKALWSWRQDHVVDSWQSAVCGAFAGGFAAAVTTPLDVAKTRITLAKAGSSTADGNVLSVLHGVWRSQGLAGDHIPGIFLQEQSSGLPLQRVGRQLPGLRASQLAVPPPHPDAELDHLCDCSFCVPLAVLISAI
Protein: Voltage-dependent T-type calcium channel subunit alpha (Q9WUT2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
Interaction partners:
Sequence:
MDEEEDGAGAEESGQPRSFTQLNDLSGAGGRQGPGSTEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERVSMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLEPYYQTENEDESPFICSQPRENGMRSCRSVPTLRGEGGGGPPCGLDYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAVGVRAGLLSSPVARGGQEPQPSGSCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRVPRASPEIQDRDANGSRWLMLPPPSTPTPSGGPPRGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPEMLKDKALVEVAPSPGPPTLTTFNIPPGPFSSMHKLLETQSTGACHSSCKISSPCSKADSGACGPDSCPYCARTGAGEPESADHEMPDSDSEAVYEFTQDAQHSDLRDPHRRRRPSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEEIGKREDTSGQLSCIQLPVNSQGGDATKSESEPDFFSPSVDGDGDRKKRLALVALGEHSELRKSLLPPLIIHTAATPMSLPKSSSTGVGEALGSGSRRTSSSGSAEPGTAHHEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEDRASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRSSASEHQDCNGKSASGRLARTLRADDPPLDGDDGDDEGNLSKGERLRAWVRARLPACCRERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLKRLEKKRRSKEKQMADLMLDDVIASGSSASAASEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGVNSPDSPKPGAPHTTAHIGAASSGFSLEHPTMVPHTEEGPVPLGPDLLTVRKSGVSRTHSLPNDSYMCRNGSTAERSLGHRGWGLPKAQSGSILSVHSQPADTSCILQLPKDAHYLLQPHGAPTWGAIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLSEVSGPSCPLTRSSSFWGGSSIQVQQRSGSQSKVSKHIRLPAPCPGLEPSWAKDPQETRSSLELDTELSWISGDLLPSSQEEPLSPRDLKKCYSVEAQSCRRRPGSWLDEQRRHSIAVSCLDSGSQPRLCPSPSSLGGQPLGGPGSRPKKKLSPPSISIDPPESQGPRPPCSPGVCLRRRAPASDSKDPSASSPLDSTAASPSPKKDALSLSGLSSDPTDLDP
Protein: Zinc finger protein 148 (Transcription factor ZBP-89) (Zinc finger DNA-binding protein 89) (Q9UQR1)
Organism: Homo sapiens (Human)
Function: Involved in transcriptional regulation. Represses the transcription of a number of genes including gastrin, stromelysin and enolase. Binds to the G-rich box in the enhancer region of these genes.
Subcellular location: Nucleus.
Interaction partners:
- Cellular tumor antigen p53
- Ornithine decarboxylase
- Histone acetyltransferase p300
- Histone deacetylase 1
Sequence:
MNIDDKLEGLFLKCGGIDEMQSSRTMVVMGGVSGQSTVSGELQDSVLQDRSMPHQEILAADEVLQESEMRQQDMISHDELMVHEETVKNDEEQMETHERLPQGLQYALNVPISVKQEITFTDVSEQLMRDKKQIREPVDLQKKKKRKQRSPAKILTINEDGSLGLKTPKSHVCEHCNAAFRTNYHLQRHVFIHTGEKPFQCSQCDMRFIQKYLLQRHEKIHTGEKPFRCDECGMRFIQKYHMERHKRTHSGEKPYQCEYCLQYFSRTDRVLKHKRMCHENHDKKLNRCAIKGGLLTSEEDSGFSTSPKDNSLPKKKRQKTEKKSSGMDKESALDKSDLKKDKNDYLPLYSSSTKVKDEYMVAEYAVEMPHSSVGGSHLEDASGEIHPPKLVLKKINSKRSLKQPLEQNQTISPLSTYEESKVSKYAFELVDKQALLDSEGNADIDQVDNLQEGPSKPVHSSTNYDDAMQFLKKKRYLQAASNNSREYALNVGTIASQPSVTQAAVASVIDESTTASILESQALNVEIKSNHDKNVIPDEVLQTLLDHYSHKANGQHEISFSVADTEVTSSISINSSEVPEVTPSENVGSSSQASSSDKANMLQEYSKFLQQALDRTSQNDAYLNSPSLNFVTDNQTLPNQPAFSSIDKQVYATMPINSFRSGMNSPLRTTPDKSHFGLIVGDSQHSFPFSGDETNHASATSTQDFLDQVTSQKKAEAQPVHQAYQMSSFEQPFRAPYHGSRAGIATQFSTANGQVNLRGPGTSAEFSEFPLVNVNDNRAGMTSSPDATTGQTFG
Protein: Latent-transforming growth factor beta-binding protein 4 (LTBP-4) (Q8N2S1)
Organism: Homo sapiens (Human)
Function: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:16157329, ECO:0000269|PubMed:9660815}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-2 proprotein
- Latent-transforming growth factor beta-binding protein 3
- Transforming growth factor beta-3 proprotein
Sequence:
MPRPGTSGRRPLLLVLLLPLFAAATSAASPSPSPSQVVEVPGVPSRPASVAVCRCCPGQTSRRSRCIRAFCRVRSCQPKKCAGPQRCLNPVPAVPSPSPSVRKRQVSLNWQPLTLQEARALLKRRRPRGPGGRGLLRRRPPQRAPAGKAPVLCPLICHNGGVCVKPDRCLCPPDFAGKFCQLHSSGARPPAPAVPGLTRSVYTMPLANHRDDEHGVASMVSVHVEHPQEASVVVHQVERVSGPWEEADAEAVARAEAAARAEAAAPYTVLAQSAPREDGYSDASGFGYCFRELRGGECASPLPGLRTQEVCCRGAGLAWGVHDCQLCSERLGNSERVSAPDGPCPTGFERVNGSCEDVDECATGGRCQHGECANTRGGYTCVCPDGFLLDSSRSSCISQHVISEAKGPCFRVLRDGGCSLPILRNITKQICCCSRVGKAWGRGCQLCPPFGSEGFREICPAGPGYHYSASDLRYNTRPLGQEPPRVSLSQPRTLPATSRPSAGFLPTHRLEPRPEPRPDPRPGPELPLPSIPAWTGPEIPESGPSSGMCQRNPQVCGPGRCISRPSGYTCACDSGFRLSPQGTRCIDVDECRRVPPPCAPGRCENSPGSFRCVCGPGFRAGPRAAECLDVDECHRVPPPCDLGRCENTPGSFLCVCPAGYQAAPHGASCQDVDECTQSPGLCGRGACKNLPGSFRCVCPAGFRGSACEEDVDECAQEPPPCGPGRCDNTAGSFHCACPAGFRSRGPGAPCQDVDECARSPPPCTYGRCENTEGSFQCVCPMGFQPNTAGSECEDVDECENHLACPGQECVNSPGSFQCRTCPSGHHLHRGRCTDVDECSSGAPPCGPHGHCTNTEGSFRCSCAPGYRAPSGRPGPCADVNECLEGDFCFPHGECLNTDGSFACTCAPGYRPGPRGASCLDVDECSEEDLCQSGICTNTDGSFECICPPGHRAGPDLASCLDVDECRERGPALCGSQRCENSPGSYRCVRDCDPGYHAGPEGTCDDVDECQEYGPEICGAQRCENTPGSYRCTPACDPGYQPTPGGGCQDVDECRNRSFCGAHAVCQNLPGSFQCLCDQGYEGARDGRHCVDVNECETLQGVCGAALCENVEGSFLCVCPNSPEEFDPMTGRCVPPRTSAGTFPGSQPQAPASPVLPARPPPPPLPRRPSTPRQGPVGSGRRECYFDTAAPDACDNILARNVTWQECCCTVGEGWGSGCRIQQCPGTETAEYQSLCPHGRGYLAPSGDLSLRRDVDECQLFRDQVCKSGVCVNTAPGYSCYCSNGYYYHTQRLECIDNDECADEEPACEGGRCVNTVGSYHCTCEPPLVLDGSQRRCVSNESQSLDDNLGVCWQEVGADLVCSHPRLDRQATYTECCCLYGEAWGMDCALCPAQDSDDFEALCNVLRPPAYSPPRPGGFGLPYEYGPDLGPPYQGLPYGPELYPPPALPYDPYPPPPGPFARREAPYGAPRFDMPDFEDDGGPYGESEAPAPPGPGTRWPYRSRDTRRSFPEPEEPPEGGSYAGSLAEPYEELEAEECGILDGCTNGRCVRVPEGFTCRCFDGYRLDMTRMACVDINECDEAEAASPLCVNARCLNTDGSFRCICRPGFAPTHQPHHCAPARPRA
Protein: PRKC apoptosis WT1 regulator protein (Prostate apoptosis response 4 protein) (Par-4) (Q925B0)
Organism: Mus musculus (Mouse)
Function: Pro-apoptotic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly cytoplasmic in absence of apoptosis signal and in normal cells. Nuclear in most cancer cell lines. Nuclear entry seems to be essential but not sufficient for apoptosis. Nuclear localization includes nucleoplasm and PML nuclear bodies (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MATGGYRSGGSTTTDFLEEWKAKREKMRAKQNPAGPGSSGGDPAAKSPAGSLTPTAVAGTSELNHGPAGAAAPAAPAPGALNCAHGSSTLPRAAPGSRRAEDECPSAAAASGAPGSRGDEEEPDSAREKGRSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAATLPDPGTSYLPQDPSRTVPGRYKSTTSAPEDEISNRYPRTDRSGFSRHNRDANAPASFSSSSTLEKRIEDLEKEVVRERQENLRLVRLMQDKEEMIGKLKEEIDLLNRDLDDMEDENEQLKQENKTLLKVVGQLTR
Protein: Chitin-binding type-2 domain-containing protein (Q9VSQ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI06432p
Sequence:
MLRLLIVLGFYILGCRAACNTCNANGVSCISETEFQFCSSASEPIGNLYTCPTGYYCTESTPICSSVASSAGCTGCNTCSSDNRFACTGRNTFALCLGTSTPSTSIGGSCGTNYVCNVGNANICGSPATYAVSCSTSSTSDCDTTAIKNATEYCQTIQTAGKYPYGGDTSTTCRQYVNCYTAAGIFYGNVYTCPGLTYFDSTSKLCTTQTQARCSDTVSCLTLNNRLLP
Protein: GEO08441p1 (Like Sm 7, isoform A) (Like Sm 7, isoform B) (Like Sm 7, isoform C) (RH73529p) (Q9VJI7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm6
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm4
- Protein associated with topo II related - 1, isoform A
- U6 snRNA-associated Sm-like protein LSm2
- ATP-dependent RNA helicase me31b
- Small nuclear ribonucleoprotein Sm D3
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm3
- U6 snRNA-associated Sm-like protein LSm1
Sequence:
MADKKVGGNNDGKEKRRKESILDLSKYLEKQIRVKFAGGREASGILKGYDALLNLVLDNTVEYLRDSDEPYKLTEEQTRSLGLVVCRGTALVLICPQDGVESIANPFITQ
Protein: Kinetochore protein NDC80 (80 kDa spindle component protein) (Nuclear division cycle protein 80) (Two-hybrid interaction with DMC1 protein 3) (P40460)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a component of the essential kinetochore-associated NDC80 complex, which is involved in chromosome segregation and spindle checkpoint activity.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores.
Interaction partners:
- Kinetochore protein SPC24
- Kinetochore protein NUF2
- Kinetochore protein SPC25
- Protein STU2
- Aurora kinase
- Serine/threonine-protein kinase MPS1
- Spindle assembly checkpoint serine/threonine-protein kinase BUB1
- Structural maintenance of chromosomes protein 2
- Outer kinetochore KNL1 complex subunit SPC105
- Structural maintenance of chromosomes protein 1
Sequence:
MQSSTSTDQHVLHHMDPHRFTSQIPTATSSQLRRRNSTNQGLTDMINKSIARNTISGTGIPTGGINKNKRTRSTVAGGTNGTALALNDKSNSRNSVSRLSINQLGSLQQHLSNRDPRPLRDKNFQSAIQEEIYDYLKKNKFDIETNHPISIKFLKQPTQKGFIIIFKWLYLRLDPGYGFTKSIENEIYQILKNLRYPFLESINKSQISAVGGSNWHKFLGMLHWMVRTNIKLDMCLNKVDRSLINQNTQEITILSQPLKTLDEQDQRQERYELMVEKLLIDYFTESYKSFLKLEDNYEPSMQELKLGFEKFVHIINTDIANLQTQNDNLYEKYQEVMKISQKIKTTREKWKALKSDSNKYENYVNAMKQKSQEWPGKLEKMKSECELKEEEIKALQSNISELHKILRKKGISTEQFELQNQEREKLTRELDKINIQSDKLTSSIKSRKLEAEGIFKSLLDTLRQYDSSIQNLTRSRSQLGHNVNDSSLKINISENLLDRDFHEGISYEQLFPKGSGINESIKKSILKLNDEIQERIKTIEKDNITLEKDIKNLKHDINEKTQINEKLELELSEANSKFELSKQENERLLVAQRIEIEKMEKKINDSNLLMKTKISDAEELVTSTELKLEELKVDLNRKRYKLHQQVIHVIDITSKFKINIQSSLENSENELGNVIEELRNLEFETEHNVTN
Protein: Trophinin-2 (Q99PW2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MDRRNDHGHRVPTFQGPLPPAGSLGLPFSPDVQSETTEKDPPIASRSKKNKNKKNSIKPMDKTTPAPPPVPSANDNASNKPKVTLQALNLPMFTQISQASATTEAPNIQASVTSQTQKAKTMRVTPKVSLTGSEDATTQLKPPLQALNLPVTTPTIQTPVANESANSLASTAVNKSKKASTANNAANKTVPSAAEISLASAATHTATTQGQAAKETGSIQTIAATARSKKNSKGKRTPAKTTNTDNEYVEASNAIEASSRQIGASGRQTEASNRQIEASSRQTEASNRQTEASSRQTEASSRQTETSNRQIGASNRQIMASNRQIGASNRQIEASNRQIGASNRQTEVSSRQIEASNRQIGASNRQTEASNRQIGASNRQTEASNRQIGASNRQTDASNRQTEASSRQTEASSRQTEASSRQTEASSRQIEASAAAVRPKKPRGKKGNNKGSNSASEPSEAPPAIQTVTNHALSVTVRIRRGSRARKAANKNRATESQAQIAEQGAQASEASISALETQVAAAVQALADDYLAQLSLEPTTRTRGKRNRKSKHPNGEERTGNNYRRIPWGRRLPPPRDVAILQERANKLVKYLLVKDQTKIPIKRSDMLKDVIQEYEDYFPEIIERASYALEKMFRVNLKEIDKQNNLYILISTQESSAGIMGTTKDTPKLGLLMVILSVIFMNGNKASEAVIWEVLRKLGLHPGVKHSLFGEVKKLITDEFVKQKYLEYKRVPNSRPPEYEFFWGLRSYHETSKMKVLKFACKVQKKDPKDWAAQYREAVEMDIQAAAVAVAEAKARAEARAQMGIGEEAVAGPWNWDDMDINCLTSGGPSTGAGFCSGPSTGGFGGGPSTGPGFGGPSTGPGFGGPSTGGGFGGPNTGGGFGGPSTGGGFGGPSTGGGFGGPSTGGGFGGPSTAAGFGSGLSTSTGFGGGLNTSAGFSGGPPSTGTGFGGGASSHGGCGFPYG
Protein: Early E1A protein (Early E1A 28 kDa protein) (P10407)
Organism: Human adenovirus E serotype 4 (HAdV-4) (Human adenovirus 4)
Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). Promotes the sumoylation of host ZBED1/hDREF with SUMO1 (By similarity).
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:P03255}.
Interaction partners:
Sequence:
MRHLRDLPDEEIIIASGSEILELVVNATMGDDHPEPPTPFGTPSLHDLYDLEVDVPEDDPNEKAVNDLFSDAALLAAEEASSPSSDSDSSLHTPRHDRGEKEIPGLKWEKMDLRCYEECLPPSDDEDEQAIQNAASHGVQAVSESFALDCPPLPGHGCKSCEFHRINTGDKAVLCALCYMRAYNHCVYSPVSDADDETPTTESTLSPPEIGTSPSDNIVRPVPVRATGRRAAVECLDDLLQGGDEPLDLCTRKRPRH
Protein: Transcriptional regulator MIT1 (P40002)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcriptional regulator of pseudohyphal growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Peptide methionine sulfoxide reductase
Sequence:
MDIEPTFKGYIEDEDDALLILQATLDGKLKHIPRRPYEIERPYLIVSGSIFVFIEEISGIKRWTDGVSWSPSRISGKFLIYKELDKENAGSNANATSSGSTDSAVITDGTSGARNNPSSSKIKLPPLKNHQFDLPPTMGHSSFESEQDTSISPSNRSNLPLKYTGLVKKTISVKLKRPPFNSIENLHIVSYYSVKDIKQNCLVTPKASPFLKDVRPSQELIVAMGNTTLGNVKNNSTTTGNGPNNINNKSNSSTPLNTVISTNNNSANINAAGSNQFTSANKNYYYKNDESSGYPITQFAPALPSTTLMYTANPPYITQSPDNTNATGMNTHVNNNNNNSNNSSNSNNSNNNNNNNNNNNNNNNNNINNINNVNTNAGNGNNPNRFHNASFAYNTTGDFINPQQQGQISYPFYYTTIPINNPNYYTTQPPNPVTNASTNENQGYSTSSTQHPYYGHPTESQSASAAAGATGTPGTAENVLPVSSMQPLLHQANNNSASSATSTAPYPVYSMNVNVPYYNSSASAYKRAQENTTSNTNAEPSGATSTNSGTMLSNPAYANSQYTPSQVYYQGFPQYAMASAQNPSMYQHQHQHPLPTVYPIATPQQNIMSSGHTLSTIGSDPQHHHYQQEPNDHKNFAMGHANNNILNITNNDTMNNLNTNTSTTTQ
Protein: Centrosomal protein of 85 kDa-like (Serologically defined breast cancer antigen NY-BR-15) (Q5SZL2)
Organism: Homo sapiens (Human)
Function: Plays an essential role in neuronal cell migration.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:21399614, ECO:0000269|PubMed:32097630}. Note=Localized specifically to the pericentriolar region. {ECO:0000269|PubMed:32097630}.
Interaction partners:
Sequence:
MWGRFLAPEASGRDSPGGARSFPAGPDYSSAWLPANESLWQATTVPSNHRNNHIRRHSIASDSGDTGIGTSCSDSVEDHSTSSGTLSFKPSQSLITLPTAHVMPSNSSASISKLRESLTPDGSKWSTSLMQTLGNHSRGEQDSSLDMKDFRPLRKWSSLSKLTAPDNCGQGGTVCREESRNGLEKIGKAKALTSQLRTIGPSCLHDSMEMLRLEDKEINKKRSSTLDCKYKFESCSKEDFRASSSTLRRQPVDMTYSALPESKPIMTSSEAFEPPKYLMLGQQAVGGVPIQPSVRTQMWLTEQLRTNPLEGRNTEDSYSLAPWQQQQIEDFRQGSETPMQVLTGSSRQSYSPGYQDFSKWESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDNELRAQHAMLGHYVNCEDSYVASLQPQYENTSLQTPFSEESVSHSQQGEFEQKLASTEKEVLQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQTVLSKRPLFDLTVIDQLFKEMSCCLFDLKALCSILNQRAQGKEPNLSLLLGIRSMNCSAEETENDHSTETLTKKLSDVCQLRRDIDELRTTISDRYAQDMGDNCITQ
Protein: Cyclin-dependent kinase-like 5 isoform 2 (EC 2.7.11.22) (Zgc:194395 protein) (B3DI12)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MKIPDIGNVMNKFEVLGIVGEGAYGVVLKCRHKETKELVAIKKFKDSEENEEVKETTLRELKMLRTLKQDNIVELKEAFRRRGKLYLVFEYVEKNMLELLEELPNGALPDKVRSYIFQLIKAIHWCHKNEIVHRDIKPENLLISANDILKLCDFGFARNLSEGSDANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPPEQMKLFYSNPRFAGLRFPSVSHPQTLDRRYLGIINGLMLDLMKNLLCLNPTERFLTEQCLNHPVFQGLRGPEQPAVPSPTPPRSSKRKPYHGDNTIPSRSHGSKSSSHRRANSKDCSSLPRHEDLHRSTDSFLNGTNMPTSSTLSPTLHPKSYQAQTLSRSASSNKDLANNNLPHLLSPKDAKGKTEFDFNLGPKVGVASVGMDTSTGKYLKSSKQGRHSSFLEGKTSTLQSGDKHSRHNYMESSHGSMPSTSSSKSSSSFLSLSKSHGALNDAKSVSNLAETRLHLDDPMAGSGSGSRYFPSSCLDLNAAPGSPRGERHAGTERQGHSPSGRGSNRLEGGTLDSRRSSGRKKTPDEPKPTDTLDPSRAAGGHAHNLPSPHESYPYGLGYTSPFSSQQRPHRHSMYVRRERHRPHGQENNLVVGQGVPTRASSLQLLSPQLQHRTLPRHNTSSSREELTPELSRNDQSPKEKPHSRPLIKDSTRDNTATFHTQRPKNEAGMYHDAHMEDGTSSKENRTIYSDSMPRRVGSFYRVPSPRPDNTFLETTGQSRVQAVAAENPTMTNHSKRQTNFDPWNNSEAMVMNPPEVPKQKEKQGFFRAIKKKKKKSQPVPSETQQDQLVLQRPVKSSSHHSSRHRNRDRERERDMERDRERERDRNRDRDRERDRDNTWPPEKQPEVQPQNQPLKSLRKLLHLSSPATSNQPPPPDRSAELRFQPLPNPPSKANLNEVRGHPAGSVTPNTKSRKPHNYPLPGQIESSWHVSALNRAEGAPYPDQLANKGGQNGIGFTRAARTRMPNLNDLKETAL
Protein: Contig An07c0260, genomic contig (EC 5.4.2.-) (A2QP68)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MPMVTAATSLRRALENPDSFIVAPGVYDGLSARVALSAGFDALYMTGAGTAASVHGQADLGICTLNDMRANAEMISNISPSTPVIADADTGYGGPIMVARTTEQYSRSGVAAFHIEDQVQTKRCGHLAGKILVDTDTYVTRIRAAVQARQRIGSDIVVIARTDSLQTHGYEESVARLRAARDAGADVGFLEGITSREMARQVIQDLAGWPLLLNMVEHGATPSISAAEAKEMGFRIIIFPFAALGPAVAAMREAMEKLKRDGIPGLDKEMTPQMLFRVCGLDESMKVDAQAGGAAFDGGVDLK
Protein: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (3-beta-HSD) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)] (P14893)
Organism: Bos taurus (Bovine)
Function: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
Interaction partners:
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Aromatase
- Cytochrome P450 11B1, mitochondrial
- Steroid 21-hydroxylase
- 17beta-estradiol 17-dehydrogenase
- Cytochrome P450 family 7 subfamily B member 1
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- 17-beta hydroxysteroid dehydrogenase 2
- 3-oxo-5-alpha-steroid 4-dehydrogenase
Sequence:
MAGWSCLVTGGGGFLGQRIICLLVEEKDLQEIRVLDKVFRPEVREEFSKLQSKIKLTLLEGDILDEQCLKGACQGTSVVIHTASVIDVRNAVPRETIMNVNVKGTQLLLEACVQASVPVFIHTSTIEVAGPNSYREIIQDGREEEHHESAWSSPYPYSKKLAEKAVLGANGWALKNGGTLYTCALRPMYIYGEGSPFLSAYMHGALNNNGILTNHCKFSRVNPVYVGNVAWAHILALRALRDPKKVPNIQGQFYYISDDTPHQSYDDLNYTLSKEWGFCLDSRMSLPISLQYWLAFLLEIVSFLLSPIYKYNPCFNRHLVTLSNSVFTFSYKKAQRDLGYEPLYTWEEAKQKTKEWIGSLVKQHKETLKTKIH