wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger MIZ domain-containing protein 1 (PIAS-like protein Zimp10) (Retinoic acid-induced protein 17) (Q9ULJ6)
Organism: Homo sapiens (Human)
Function: Acts as transcriptional coactivator. Increases ligand-dependent transcriptional activity of AR and promotes AR sumoylation. The stimulation of AR activity is dependent upon sumoylation. Also functions as a transcriptional coactivator in the TGF-beta signaling pathway by increasing the activity of the SMAD3/SMAD4 transcriptional complex. Involved in transcriptional activation of a subset of NOTCH1 target genes including MYC. Involved in thymocyte and T cell development (By similarity). Involved in the regulation of postmitotic positioning of pyramidal neurons in the developing cerebral cortex.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:14609956, ECO:0000269|PubMed:16777850}. Cytoplasm {ECO:0000269|PubMed:14609956}. Nucleus {ECO:0000269|PubMed:30639322}. Note=Enriched at replication foci throughout S phase. {ECO:0000269|PubMed:14609956}.
Interaction partners:
- Androgen receptor
- Small ubiquitin-related modifier 1
- Neurogenic locus notch homolog protein 1
- Small ubiquitin-related modifier 2
Sequence:
MNSMDRHIQQTNDRLQCIKQHLQNPANFHNAATELLDWCGDPRAFQRPFEQSLMGCLTVVSRVAAQQGFDLDLGYRLLAVCAANRDKFTPKSAALLSSWCEELGRLLLLRHQKSRQSDPPGKLPMQPPLSSMSSMKPTLSHSDGSFPYDSVPWQQNTNQPPGSLSVVTTVWGVTNTSQSQVLGNPMANANNPMNPGGNPMASGMTTSNPGLNSPQFAGQQQQFSAKAGPAQPYIQQSMYGRPNYPGSGGFGASYPGGPNAPAGMGIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPMGPTQAYNSQFMNQPGPRGPASMGGSMNPASMAAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQRMPQQTYPGPRPQSLPIQNIKRPYPGEPNYGNQQYGPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRMPSQPSSGQYPPPTVNMGQYYKPEQFNGQNNTFSGSSYSNYSQGNVNRPPRPVPVANYPHSPVPGNPTPPMTPGSSIPPYLSPSQDVKPPFPPDIKPNMSALPPPPANHNDELRLTFPVRDGVVLEPFRLEHNLAVSNHVFHLRPTVHQTLMWRSDLELQFKCYHHEDRQMNTNWPASVQVSVNATPLTIERGDNKTSHKPLHLKHVCQPGRNTIQITVTACCCSHLFVLQLVHRPSVRSVLQGLLKKRLLPAEHCITKIKRNFSSVAASSGNTTLNGEDGVEQTAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMWGILNAIQHSEFEEVTIDPTCSWRPVPIKSDLHIKDDPDGIPSKRFKTMSPSQMIMPNVMEMIAALGPGPSPYPLPPPPGGTNSNDYSSQGNNYQGHGNFDFPHGNPGGTSMNDFMHGPPQLSHPPDMPNNMAALEKPLSHPMQETMPHAGSSDQPHPSIQQGLHVPHPSSQSGPPLHHSGAPPPPPSQPPRQPPQAAPSSHPHSDLTFNPSSALEGQAGAQGASDMPEPSLDLLPELTNPDELLSYLDPPDLPSNSNDDLLSLFENN
Protein: TSC complex subunit 1 (Tuberous sclerosis 1) (Q86WV8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAQQANVGELLAMLDSPMLGVRDDVTAVFKENLNSDRGPMLVNTLVDYYLETSSQPALHILTTLQEPHDKHLLDRINEYVGKAATRLSILSLLGHVIRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCLKKPGHVAEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENLETFEEVVKPMMEHVRIHPELVTGSKDHELDPRRWKRLETHDVVIECAKISLDPTEASYEDGYSVSHQISARFPHRSADVTTSPYADTQNSYGCATSTPYSTSRLMLLNMPGQLPQTLSSPSTRLITEPPQVWCQLVCLLSPLLSGEADPLGQI
Protein: Rac-like GTP-binding protein ARAC1 (GTPase protein ROP3) (Q38902)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with the membrane when activated.
Interaction partners:
- Guanine nucleotide exchange factor SPIKE 1
- Rho GTPase-activating protein 6
- Rop guanine nucleotide exchange factor 7
- KOW domain-containing protein
- Rho GTPase-activating protein 2
- Rho GTPase-activating protein 5
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Kinesin-like protein KIN-14E
- CRIB domain-containing protein RIC4
- CRIB domain-containing protein RIC3
Sequence:
MSASRFIKCVTVGDGAVGKTCLLISYTSNTFPTDYVPTVFDNFSANVVVNGATVNLGLWDTAGQEDYNRLRPLSYRGADVFILAFSLISKASYENVSKKWIPELKHYAPGVPIVLVGTKLDLRDDKQFFIDHPGAVPITTAQGEELKKLIGAPAYIECSSKTQENVKGVFDAAIRVVLQPPKQKKKKSKAQKACSIL
Protein: Uncharacterized protein YaiZ (P0AAQ0)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YnaJ
- Taurine transport system permease protein TauC
Sequence:
MNLPVKIRRDWHYYAFAIGLIFILNGVVGLLGFEAKGWQTYAVGLVTWVISFWLAGLIIRRRDEETENAQ
Protein: Polypeptide N-acetylgalactosaminyltransferase 3 (C9J2C3)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037847}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00037847}. Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MAHLKRLVKLHIKRHYHKKFWKLGAVIFFFIIVLVLMQREVSVQYSKEESRMERNMKNKNKMLDLMLEAVNNIKDAMPKMQIGAPVRQNIDAGERPCLQGYYTAAELKPVLDRPPQDSNAPGASGKAFKTTNLSVEEQKEKERGEAKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKRCPPLPTTSVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDEYLHDKLDEYVKQFSIVKIVRQRERKGLITARLLGATVATAETLTFLDAHCECFYGWLEPLLARIAENYTAVVSPDIASIDLNTFEFNKPSPYGSNHNRGNFDWSLSFGWESLPDHEKQRRKDETYPIKTPTFAGGLFSISKEYFEYIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSKSPHSFPKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIVKQ
Protein: Heptaprenylglyceryl phosphate synthase (HepGP synthase) (EC 2.5.1.n9) (Glycerol-1-phosphate heptaprenyltransferase) (O34790)
Organism: Bacillus subtilis (strain 168)
Function: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Cannot use glycerol-3-phosphate (G3P) or 3-phosphoglycerate (3PG) as an acceptor.
Interaction partners:
- Uncharacterized lipoprotein YerH
- Putative acetyltransferase YvoF
- ATP-dependent DNA helicase PcrA
- Uncharacterized protein YpjA
- Probable maltose O-acetyltransferase
- Uncharacterized protein YvkN
Sequence:
MYDVTEWKHVFKLDPNKDLPDEQLEILCESGTDAVIIGGSDGVTEDNVLRMMSKVRRFLVPCVLEVSAIEAIVPGFDLYFIPSVLNSKNADWIVGMHQKAMKEYGELMSMEEIVAEGYCIANPDCKAAALTEADADLNMDDIVAYARVSELLQLPIFYLEYSGVLGDIEAVKKTKAVLETSTLFYGGGIKDAETAKQYAEHADVIVVGNAVYEDFDRALKTVAAVKGE
Protein: Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 (Membrane-associated guanylate kinase inverted 3) (MAGI-3) (Q5TCQ9)
Organism: Homo sapiens (Human)
Function: Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2.
Subcellular location: Cell membrane; Peripheral membrane protein. Cell junction, tight junction. Nucleus {ECO:0000250}. Note=Concentrates in specific sites at the plasma membrane and in the nucleus. In epithelial cells, it localizes at tight junctions (By similarity). {ECO:0000250}.
Interaction partners:
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Catenin beta-1
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
- Rap guanine nucleotide exchange factor 2
- Lysophosphatidic acid receptor 2
- Rap guanine nucleotide exchange factor 6
- Frizzled-4
- Protein PHTF1
- Microtubule-associated serine/threonine-protein kinase 3
Sequence:
MSKTLKKKKHWLSKVQECAVSWAGPPGDFGAEIRGGAERGEFPYLGRLREEPGGGTCCVVSGKAPSPGDVLLEVNGTPVSGLTNRDTLAVIRHFREPIRLKTVKPGKVINKDLRHYLSLQFQKGSIDHKLQQVIRDNLYLRTIPCTTRAPRDGEVPGVDYNFISVEQFKALEESGALLESGTYDGNFYGTPKPPAEPSPFQPDPVDQVLFDNEFDAESQRKRTTSVSKMERMDSSLPEEEEDEDKEAINGSGNAENRERHSESSDWMKTVPSYNQTNSSMDFRNYMMRDETLEPLPKNWEMAYTDTGMIYFIDHNTKTTTWLDPRLCKKAKAPEDCEDGELPYGWEKIEDPQYGTYYVDHLNQKTQFENPVEEAKRKKQLGQVEIGSSKPDMEKSHFTRDPSQLKGVLVRASLKKSTMGFGFTIIGGDRPDEFLQVKNVLKDGPAAQDGKIAPGDVIVDINGNCVLGHTHADVVQMFQLVPVNQYVNLTLCRGYPLPDDSEDPVVDIVAATPVINGQSLTKGETCMNPQDFKPGAMVLEQNGKSGHTLTGDGLNGPSDASEQRVSMASSGSSQPELVTIPLIKGPKGFGFAIADSPTGQKVKMILDSQWCQGLQKGDIIKEIYHQNVQNLTHLQVVEVLKQFPVGADVPLLILRGGPPSPTKTAKMKTDKKENAGSLEAINEPIPQPMPFPPSIIRSGSPKLDPSEVYLKSKTLYEDKPPNTKDLDVFLRKQESGFGFRVLGGDGPDQSIYIGAIIPLGAAEKDGRLRAADELMCIDGIPVKGKSHKQVLDLMTTAARNGHVLLTVRRKIFYGEKQPEDDSSQAFISTQNGSPRLNRAEVPARPAPQEPYDVVLQRKENEGFGFVILTSKNKPPPGVIPHKIGRVIEGSPADRCGKLKVGDHISAVNGQSIVELSHDNIVQLIKDAGVTVTLTVIAEEEHHGPPSGTNSARQSPALQHRPMGQSQANHIPGDRSALEGEIGKDVSTSYRHSWSDHKHLAQPDTAVISVVGSRHNQNLGCYPVELERGPRGFGFSLRGGKEYNMGLFILRLAEDGPAIKDGRIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLRPGTGLIPDHGDWDINNPSSSNVIYDEQSPLPPSSHFASIFEESHVPVIEESLRVQICEKAEELKDIVPEKKSTLNENQPEIKHQSLLQKNVSKRDPPSSHGHSNKKNLLKVENGVTRRGRSVSPKKPASQHSEEHLDKIPSPLKNNPKRRPRDQSLSPSKGENKSCQVSTRAGSGQDQCRKSRGRSASPKKQQKIEGSKAPSNAEAKLLEGKSRRIAGYTGSNAEQIPDGKEKSDVIRKDAKQNQLEKSRTRSPEKKIKRMVEKSLPSKMTNKTTSKEVSENEKGKKVTTGETSSSNDKIGENVQLSEKRLKQEPEEKVVSNKTEDHKGKELEAADKNKETGRFKPESSSPVKKTLITPGPWKVPSGNKVTGTIGMAEKRQ
Protein: Toxin-like outer membrane protein (O25063)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
Sequence:
MKKFKKKPKSIKRSHQNQKTILKRPLWLMPLLISGFASGVYANNLWDLLNPKVGGEYVHWVKGSQYCAWWEFAGCLKNVWGANHKGYDAGNAANYLSSQNYQAISVGSGNETGTYSLSGFTNYVGGNLTINLGNSVVLDLSGSNSFTSYQGYNQGKDDVTFTVGAINLNGTLEVGNRVGSGAGTHTGTATLNLNANKVNINSNINAYKTSQVNIGNANSVITIGSVSLSGDVCSSLASVGIGANCSTSGPSYSFKGTTNATNTAFSNASGSFTFEENATFSGAKWNGGTYTFNKEFSATNNTAFSSGSFNFKGVSSFNGTSFSNASYTFDNQATFQNSSFNGGTFTFNNQTNPTNNAQHPQIQNSSFSGNATTLKGFVNFQQAFNNSNHQLTIQNASFNNATFNNTGKITIEKDASFNNTTFNTSVDTNNMSVTGGVTLSGKNDLKNGSTLDFGSSKITLAQGTTFNLTSLGSEKSVTILNSSGGITYSNLLNHAINGLTSALKTNESLSNPQSFAQGLWDIITYNGVTGQLLNENAATSKPTDSSPSKSSTNSTQVYQVGYKIGDTIYKLQETFSHNSIIIQALESGTYTPPPVINGSKFDLSASNYINADMPWYDHKYYIPKSQNFTESGTYYLPSVQIWGSYTNSFKQTFSANGSNLVIGYNSTWTDHNVSSSGTVSFGDTSGSALNGHCGPWPYYQCTGTTNGTYSAYHVYITANLRSGNRIGTGGAANLIFNGVDSINIANATITQHNAGIYSSSMTFSTQSMDNSQNLNGLNSNGKLSVYGTTFTNEAKDGKFIFNAGQAVFENTNFNGGSYQFSGDSLNFSNNNQFNSGSFEISAKNASFNNANFNNSASFNFNNSNATTSFVGDFTNANSNLQIAGNAVFGNSTNGSQNTANFNNTGSVNISGNATFDNVVFNGPTNTSVKGQVTLNNITLKNLNAPLSFGDGTITFNAHSVINIAESITNGNPITLVSSSKEIEYNNAFSKNLWQLINYQGHGASSEKLVSSAGNGVYDVVYSFNNQTYNFQEVFSQNSISIRRLGVNMVFDYVDMEKSDHLYYQNALGFMTYMPNSYNNNLGNANNTIYYYDKSIDFYASGKTLFTKAEFSQTFTGQNSAIVFGAKSIWTSLSDAPQSNTIIRFGDNKGAGSNDASGHCWNLQCIGFITGHYEAQKIYITGSIESGNRISSGGGASLNFNGLQGILLTNATLYNRAAGTQSSSMNFISNSANIQAQNSYFIDDTAQNGGNPNFSFNALNLDFSNSSFRGYVGKTQSVFKFNAKNAISFTNSTNLSSGLYQMQAKSVLFDNSNLSVSVGTSSIKANAINLSQNASINASNHSTLELQGDLNVNDTSSLNLNQSTINVSNNATINDYASLIASNGSHLNFNGAVNFNSANITTSLNNSSIVFKGAVSLGGQFNLSNNSSLDFQGSSAITSNTAFNFYDNAFSQSPITFHQALDIKAPLSLGGNLLNPNNSSVLDLKNSQLVFGDQGSLNIANIDLLSDLNDNKNRVYNIIQADMNSNWYERISFFGMHINDGIYDAKNQTYSFTNPLNNALKITESFKDNQLSVTLSQIPGIKNTLYNIGSEIFNYQKVYNNANGVYSYSDDAQGVFYLTSNVKGYYNPNQSYQASGSNNTTKNNNLTSESSIISQTYNAQGNPISALHIYNKGYNFNNIKALGQMALKLYPEIKKVLGNDFSPSSLNALNSNALNQLTKLITPNDWKNINELIDNANNSVVQNFNNGTLIVGATQIGQTDTNSAVVFGGLGYQTPCDYTDIVCQKFRGTYLGQLLESSSADLGYIDTTFNAKEIYLTGTLGSGNAWGTGGSASVTFNSQTSLILNQANIVSSQTDGIFSMLGQEGINKVFNQAGLANILGEVAVQSINKAGGLGNLIVNTLGSNSVIGGYLTPEQKNQTLSQLLGQNNFDNLMNDSGLNTAIKDLIRQKLGFWTGLVGGLAGLGGIDLQNPEKLIGSMSINDLLSKKGLFNQITGFISANDIGQVISVMLQDIVKPSNALKNDVAALGKQMIGEFLGQDTLNSLESLLQNQQIKSVLDKVLAAKGLGPIYEQGLGDLIPNLGKKGLFAPYGLSQVWQKGDFSFNAQGNVFVQNSTFSNANGGTLSFNAGNSLIFAGNNHIAFTNHAGTLQLLSDQVSNINITTLNASNGLKINAANNNVSVSQGNLFVSASCAQQSDPTTANIANPCALSAQSTNGASSNNASNNAPIALSNNDESLMVAANDFNFSGNIYANGVVDFSKIKGSANIKNLYLYNNAQFQANNLTISNQAVLEKNASFVTNNLNIQGAFNNNATQKIEVLQNLVIASNASLSTGIYGLEVGGALNNSGAIHFNLENTQTPTPLIQAEGIINLNTTQTPFMNVNNSMANNTTYTLLKSSRYIDYNINPNSLQSYLNLYTLININGNHIEEKNGALTYLGQRVLLQDKGLLLSVALPNSNNASQNNILSLSVLYNQVKMSCGDKAMDFTPPTLQDYIVGIQGQSALNQIEAVGGNAIKWLSTLMMETKENPFFAPIYLKNHSLNEILGVTKDLQNTASLISNPNFRDNATNLLELASYTQQTSRLTKLSDFRSREGESDFSLLELKNKRFSDPNPEVFVKYSQLSKHPNNLWVQGVGGASFISGGNGTLYGLNAGYDRLVKNVILGGYVAYGYSDFNGNIMHSLGNNVDVGMYARAFLKRNEFTLSANETYGGNATSINSSNSLLSVLNQRYNYNTWTTSVNGNYGYDFMFKQKSVVLKPQVGLSYHFIGLSGMKGNDAAYKQFLMHSNPSNESVLTLNMGLESRKYFGKNSYYFVTARLGRDLLIKSKGSNTVRFVGENTLLYRKGEVFNTFASVITGGEMHLWRLVYVNAGVGLKMGLQYQDINITGNVGMRVAF
Protein: Mediator of RNA polymerase II transcription subunit 18 (Mediator complex subunit 18) (A0A8I6ACJ8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364150}.
Interaction partners:
Sequence:
MTRNEMEAWTHCAFASSGSVLDHSLESLIHRLRGLCDNMEPETFLDHEMVFLLKGQQASPFVLRARRSMDRAGAPWHLRYLGQPEMGDKNRHALVRNCVDIATSENLTDFLMEMGFRMDHEFVAKGHLFRKGIMKIVVYKIFRILVPGNTDSTEALSLSYLVELSVVAPAGQDMVSDDMRNFAEQLKPLVHLEKIDPKRLM
Protein: Thymidylate synthase ThyA (TS) (TSase) (EC 2.1.1.45) (P9WFR9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00008}.
Interaction partners:
- Dihydrofolate reductase
- Flavin-dependent thymidylate synthase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Dihydrofolate synthase/folylpolyglutamate synthase
- Bifunctional protein FolD
- Serine hydroxymethyltransferase 2
- Serine hydroxymethyltransferase 1
- Thymidylate kinase
- Aminomethyltransferase
- Acid phosphatase
Sequence:
MSIVTPYEDLLRFVLETGTPKSDRTGTGTRSLFGQQMRYDLSAGFPLLTTKKVHFKSVAYELLWFLRGDSNIGWLHEHGVTIWDEWASDTGELGPIYGVQWRSWPAPSGEHIDQISAALDLLRTDPDSRRIIVSAWNVGEIERMALPPCHAFFQFYVADGRLSCQLYQRSADLFLGVPFNIASYALLTHMMAAQAGLSVGEFIWTGGDCHIYDNHVEQVRLQLSREPRPYPKLLLADRDSIFEYTYEDIVVKNYDPHPAIKAPVAV
Protein: Calvin cycle protein CP12-1, chloroplastic (CP12 domain-containing protein 1) (Chloroplast protein 12-1) (O22914)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20399532}.
Interaction partners:
- Phosphoribulokinase, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPCP1, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPCP2, chloroplastic
- Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic
- CHP-rich zinc finger protein-like
- CBBY-like protein
- Glyceraldehyde-3-phosphate dehydrogenase GAPB, chloroplastic
Sequence:
MTTIAAAGLNVATPRVVVRPVARVLGPVRLNYPWKFGSMKRMVVVKATSEGEISEKVEKSIQEAKETCADDPVSGECVAAWDEVEELSAAASHARDKKKAGGSDPLEEYCNDNPETDECRTYDN
Protein: Small ribosomal subunit protein uS2c (30S ribosomal protein S2, chloroplastic) (Q6ENI1)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Uncharacterized protein
- Small ribosomal subunit protein uS9c
- 30S ribosomal protein S9
- Small ribosomal subunit protein uS14c
- Uncharacterized protein
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS12c
- Small ribosomal subunit protein uS17c
- Small ribosomal subunit protein uS7cz/uS7cy
- S5 DRBM domain-containing protein
Sequence:
MTRRYWNINLKEMIEAGVHFGHGIKKWNPKMAPYISAKRKGTHITNLARTTRFLSEACDLVFDAASQGKSFLIVGTKKRAADLVASAAIRARCHYVNKKWFSGMLTNWSITKTRLSQFRDLRAEEKMEKFHHLPKRDVAILKRKLSTLLRYLGGIKYMTRLPDIVIVLDQQKEYIALRECAILGIPTISLADTNCDPDLANISIPANDDTMTSIRLILNKLVFAICEGRSLYIRNH
Protein: PAT complex subunit CCDC47 (Adipocyte-specific protein 4) (Calumin) (Coiled-coil domain-containing protein 47) (Q9D024)
Organism: Mus musculus (Mouse)
Function: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (By similarity). The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions (By similarity). Within the MPT complex, the PAT subcomplex sequesters any highly polar regions in the transmembrane domains away from the non-polar membrane environment until they can be buried in the interior of the fully assembled protein (By similarity). Within the PAT subcomplex, CCDC47 occludes the lateral gate of the SEC61 complex (By similarity). Involved in the regulation of calcium ion homeostasis in the ER (By similarity). Required for proper protein degradation via the ERAD (ER-associated degradation) pathway (By similarity). Has an essential role in the maintenance of ER organization during embryogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96A33}; Single-pass type I membrane protein {ECO:0000255}. Rough endoplasmic reticulum membrane {ECO:0000269|PubMed:25009997}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Calcium load-activated calcium channel
- PAT complex subunit Asterix
- BOS complex subunit TMEM147
- BOS complex subunit NCLN
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit beta
- DnaJ homolog subfamily B member 11
- Protein transport protein Sec61 subunit alpha isoform 2
- Sperm-associated antigen 1
- T-complex protein 1 subunit zeta
Sequence:
MKAFYAFCVVLLVFGSVSEAKFDDFEDEEDIVEYDDNDFAEFEDVMEDSVTESPQRVISTEDDEDEATVELEGQDESQEGDFEDADTQEGDTESEPYDDEEFEGYEDKPDTSSNKNKDPITIVDVPAHLQNSWESYYLEILMVTGLLAYIMNYIIGKNKNSRLAQAWFNSHRELLESNFTLVGDDGTNKEATSTGKLNQENEHIYNLWCSGRVCCEGMLIQLRFLKRQDLLNVLARMMRPVSDQVQIKVTMNDEDMDTYVFAVGTRKALLRLQKEMQDLSEFCSDKPKSGAKYGLPDSLAILSEMGEVTEGMMDTKMVHFLTHYADKIESVHFSDQFSGPKIMQEEGQPLKLPDTKRTLLFTFNVPGSGNTYPKDMESLLPLMNMVIYSIDKAKKFRLNREGKQKADKNRARVEENFLKLTHVQRQEAAQSRREEKKRAEKERIMNEEDPEKQRRLEEAALRREQKKLEKKQMKMKQIKVKAM
Protein: VIN3-like protein 1 (Protein VERNALIZATION 5) (Q9LHF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in both the vernalization and photoperiod pathways by regulating expression of the related floral repressors FLOWERING LOCUS C (FLC) and FLOWERING LOCUS M (FLM). Together with VIN3, required during vernalization for the modifications of FLC and FLM chromatin that are associated with an epigenetically silenced state (e.g. chromatin modifications, histone deacetylation, and trimethylated H3 'Lys-4' H3K4me3 and 'Lys-27' H3K27me3) and with acquisition of competence to flower. Promotes flowering in short days (SD=8 hours light/16 hours dark). Associates dynamically at FLC locus; during vernalization, binds to specific sites, but when in warm conditions, distributed along the whole locus.
Subcellular location: Nucleus {ECO:0000269|PubMed:17174094}. Nucleus speckle {ECO:0000269|PubMed:17174094}. Note=Probably DNA-associated. {ECO:0000250}.
Interaction partners:
- Polycomb group protein VERNALIZATION 2
- Protein VERNALIZATION INSENSITIVE 3
- Histone-binding protein MSI1
- Histone-lysine N-methyltransferase EZA1
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- VIN3-like protein 2
- Histone-lysine N-methyltransferase CLF
- Chromo domain-containing protein LHP1
- Ketose-bisphosphate aldolase class-II family protein
- B3 domain-containing transcription factor VRN1
Sequence:
MDSSSTKSKISHSRKTNKKSNKKHESNGKQQQQQDVDGGGGCLRSSWICKNASCRANVPKEDSFCKRCSCCVCHNFDENKDPSLWLVCEPEKSDDVEFCGLSCHIECAFREVKVGVIALGNLMKLDGCFCCYSCGKVSQILGCWKKQLVAAKEARRRDGLCYRIDLGYRLLNGTSRFSELHEIVRAAKSMLEDEVGPLDGPTARTDRGIVSRLPVAANVQELCTSAIKKAGELSANAGRDLVPAACRFHFEDIAPKQVTLRLIELPSAVEYDVKGYKLWYFKKGEMPEDDLFVDCSRTERRMVISDLEPCTEYTFRVVSYTEAGIFGHSNAMCFTKSVEILKPVDGKEKRTIDLVGNAQPSDREEKSSISSRFQIGQLGKYVQLAEAQEEGLLEAFYNVDTEKICEPPEEELPPRRPHGFDLNVVSVPDLNEEFTPPDSSGGEDNGVPLNSLAEADGGDHDDNCDDAVSNGRRKNNNDCLVISDGSGDDTGFDFLMTRKRKAISDSNDSENHECDSSSIDDTLEKCVKVIRWLEREGHIKTTFRVRFLTWFSMSSTAQEQSVVSTFVQTLEDDPGSLAGQLVDAFTDVVSTKRPNNGVMTSH
Protein: 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (EC 1.13.11.48) (O31266)
Organism: Paenarthrobacter nitroguajacolicus (Arthrobacter nitroguajacolicus)
Function: Ring-cleaving dioxygenase involved in quinaldine degradation and utilization.
Interaction partners:
Sequence:
MTDTYLHETLVFDNKLSYIDNQRDTDGPAILLLPGWCHDHRVYKYLIQELDADFRVIVPNWRGHGLSPCEVPDFGYQEQVKDALEILDQLGVETFLPVSHSHGGWVLVELLEQAGPERAPRGIIMDWLMWAPKPDFAKSLTLLKDPERWREGTHGLFDVWLDGHDEKRVRHHLLEEMADYGYDCWGRSGRVIEDAYGRNGSPMQMMANLTKTRPIRHIFSQPTEPEYEKINSDFAEQHPWFSYAKLGGPTHFPAIDVPDRAAVHIREFATAIRQGQ
Protein: Iron-sulfur cluster assembly 1 homolog, mitochondrial (HESB-like domain-containing protein 2) (Iron-sulfur assembly protein IscA) (Q9D924)
Organism: Mus musculus (Mouse)
Function: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. Probably involved in the binding of an intermediate of Fe/S cluster assembly.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BUE6}.
Interaction partners:
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Cysteine desulfurase
- Glutaredoxin-related protein 5, mitochondrial
- Ferredoxin-2, mitochondrial
- Lipoyl synthase, mitochondrial
- LYR motif-containing protein 4
- Ferrochelatase, mitochondrial
Sequence:
MSASLVRATVRAVSKRKLQPTRAALTLTPSAVNKIKQLLKDKPEHVGLKVGVRTRGCNGLSYSLEYTKTKGDSDEEVIQDGVRVFIEKKAQLTLLGTEMDYVEDKLSSEFVFNNPNIKGTCGCGESFHV
Protein: Probable transcription factor elt-4 (GATA-type domain-containing protein elt-4) (Q8MQA7)
Organism: Caenorhabditis elegans
Function: Probable transcription factor. Plays a role in regulating heme-dependent expression of heme transporter hrg-1. Modulates lifespan in a daf-16-dependent manner.
Subcellular location: Nucleus {ECO:0000305|PubMed:20938051, ECO:0000305|PubMed:24834345}.
Interaction partners:
- GATA transcription factor END-1
- GATA-type domain-containing protein
- GATA-type domain-containing protein
- GATA-type domain-containing protein
Sequence:
MDNNYLDASHRKRLVCSNCNGTNTTLWRRKAEGDPVCNACGLYFKLHHVTRPIPMKKNKKHAVLPAPGISKL
Protein: Probable histone H2A.7 (HTA6) (Q9FJE8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H4
- Histone H2B.10
- Histone H2B.6
- DNA-directed RNA polymerase II subunit 4
- Histone H3.1
- Lysine-specific demethylase ELF6
- Histone H2B.9
- Histone H2B.5
- Histone H2A variant 1
- Histone H2B.1
Sequence:
MESTGKVKKAFGGRKPPGAPKTKSVSKSMKAGLQFPVGRITRFLKKGRYAQRLGGGAPVYMAAVLEYLAAEVLELAGNAARDNKKSRIIPRHLLLAIRNDEELGKLLSGVTIAHGGVLPNINSVLLPKKSATKPAEEKATKSPVKSPKKA
Protein: Corepressor of pangolin, isoform A (Corepressor of pangolin, isoform B) (LD05592p) (Q7JUZ9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00371}.
Interaction partners:
Sequence:
MEMAYNASSSAASVGSASAAASATASFAFTNTAKLPIETVKRLIAAVSRRPMLWLRNNANGQKRSDITPVWFEVGQDVNLPADICRIKWGHLRDNFRKVYIRNNLSNETPSSWRFYNDMRFMEPAVHENIMRQTRSSSKKHPPGHWTENNNVLGPDKYDSMPIVATEPICELSHSYDSELHQPSFSDISSFFEDRDCQPPENKRFKSEPSQREEDEEDDDDFDEDAASENLEEERGNRADAASSGVFTIEVLDDDDEMEQAVTKTKANNTSHGGSSLKSEQEAKVFSNSQSPTADLPFKYISTDVATNTDPSGGDLQDEADRMFLLSLMPFLQRLDSRRRLRVRQKLQNVLIEELEFG