wanglab/gogpt-training-data huggingface dataset:
Protein: Basic leucine zipper transcriptional factor ATF-like (B-cell-activating transcription factor) (B-ATF) (SF-HT-activated gene 2 protein) (SFA-2) (Q16520)
Organism: Homo sapiens (Human)
Function: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Cytoplasm {ECO:0000250}. Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells. {ECO:0000250}.
Interaction partners:
- Transcription factor JunB
- Transcription factor Jun
- Interferon regulatory factor 4
- Basic leucine zipper transcriptional factor ATF-like 3
- Transcription factor JunD
- Basic leucine zipper transcriptional factor ATF-like 2
- Protein c-Fos
- Nuclear receptor ROR-gamma
- Signal transducer and activator of transcription 3
- B-cell lymphoma 6 protein
Sequence:
MPHSSDSSDSSFSRSPPPGKQDSSDDVRRVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLNSHEPLCSVLAASTPSPPEVVYSAHAFHQPHVSSPRFQP
Protein: Large ribosomal subunit protein mL59 (54S ribosomal protein L25, mitochondrial) (YmL25) (P23369)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein mS45
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein mL38
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein bL28m
- Small ribosomal subunit protein uS8m
- Large ribosomal subunit protein bL21m
Sequence:
MSYKQYFDSLPLKLKSFFQRYPPSIKYSPVSTSTKAINANPFLPNKHPVTQRFHDPKYSLRRMSDVYKLALRYGVEEFLPPIENTKKLFFEEKYNKKTLMKGVLLPKGHKHELKLNEKLKKREEALKKVDELIASKKGSKYAKRVEKMKKNQSIGWF
Protein: Broad-specificity phosphatase YOR283W (EC 3.1.3.-) (Q12040)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Metal-independent phosphatase active against a broad range of phosphorylated substrates including nucleoside tri- and diphosphates, phosphorylated organic acids, and amino acids. Shows no activity against phytic acid, phosphorylated carbohydrates, and nucleoside monophosphates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Phosphoglycerate mutase 3
- Phosphoglycerate mutase 2
- Triosephosphate isomerase
- Phosphoglycerate kinase
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Enolase 2
- Enolase 1
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Pyruvate kinase 1
Sequence:
MTKEVPYYCDNDDNNIIRLFIIRHGQTEHNVKKILQGHKDTSINPTGEEQATKLGHYLRSRGIHFDKVVSSDLKRCRQTTALVLKHSKQENVPTSYTSGLRERYMGVIEGMQITEAEKYADKHGEGSFRNFGEKSDDFVARLTGCVEEEVAEASNEGVKNLALVSHGGAIRMILQWLKYENHQAHKIIVFNTSVTIVDYVKDSKQFIVRRVGNTQHLGDGEFVVSDLRLR
Protein: Zona pellucida sperm-binding protein 3 (O73670)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}. Zona pellucida {ECO:0000256|RuleBase:RU367066}. Cell membrane {ECO:0000256|RuleBase:RU367066}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU367066}.
Interaction partners:
Sequence:
MQGSCVVLGLLCCLVARVGSYTPWDLSWSARGDPSAWSWGAEVHSRAVSSSHPVAVQCQEAQLVVTVHRDLFGTGRLINAADLTLGPAACKHSSLNAAHNTLTFAAGLHECGSVVQVTPDTLIYRTLINYDPSPASNPVIIRTNPAVIPIECHYPRRENVSSNAIRPTWSPFKLCPVSRGEAVFSLRLMSDDWSTERPFTGFQLGDILNIQAEVSTESHVPLRLFVDSCVAALSPDGDSSPHYAIIDFNGCLVDGRVDDTSSAFITPRPREDVLRFRIDVFRFAGDTRNLIYITCHLKVTPADQGPDPQNKACSFNKARNTWVPVEGSRDVCSCCETGNCDAARALRRLNPWSDGTAARFRRDAGKEVAADVVIGPVLLSADPGAVGQQQEGGDGAAVTEPSVGTGLVCVAVVVALAAVGVAVGIARKGCTRTSVAA
Protein: Tetrahydromethanopterin S-methyltransferase subunit G (EC 7.2.1.4) (N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit G) (Q50774)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Tetrahydromethanopterin S-methyltransferase subunit H
- Tetrahydromethanopterin S-methyltransferase subunit E
- Tetrahydromethanopterin S-methyltransferase subunit B
- Tetrahydromethanopterin S-methyltransferase subunit A 1
- Tetrahydromethanopterin S-methyltransferase subunit C
- Tetrahydromethanopterin S-methyltransferase subunit D
- Tetrahydromethanopterin S-methyltransferase subunit A 2
- Tetrahydromethanopterin S-methyltransferase subunit F
- Methyl-coenzyme M reductase I operon protein D
- Methyl-coenzyme M reductase I operon protein C
Sequence:
MSEEEKTTIPRVLVSADEFNKANEKLDEIEEKVEFTVGEYSQRIGQQIGRDIGILYGIVIGLIILAVTNILFAGLLKGLLKSLFGL
Protein: Homeobox protein goosecoid-2 (GSC-2) (Homeobox protein goosecoid-like) (GSC-L) (O15499)
Organism: Homo sapiens (Human)
Function: May have a role in development. May regulate its own transcription. May bind the bicoid consensus sequence TAATCC.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- G protein subunit beta 1 like.
- Tricarboxylate transport protein, mitochondrial
- T-box transcription factor TBX1
- Proline dehydrogenase 1, mitochondrial
Sequence:
MAAAAGGAASRRGAGRPCPFSIEHILSSLPERSLPARAACPPQPAGRQSPAKPEEPGAPEAAPCACCCCCGPRAAPCGPPEAAAGLGARLAWPLRLGPAVPLSLGAPAGGSGALPGAVGPGSQRRTRRHRTIFSEEQLQALEALFVQNQYPDVSTRERLAGRIRLREERVEVWFKNRRAKWRHQKRASASARLLPGVKKSPKGSC
Protein: Mitochondrial import receptor subunit TOM40B (Protein TOMM40-like) (A4F267)
Organism: Rattus norvegicus (Rat)
Function: Potential channel-forming protein implicated in import of protein precursors into mitochondria.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:17437969}; Multi-pass membrane protein {ECO:0000269|PubMed:17437969}.
Interaction partners:
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import receptor subunit TOM70
- Sorting and assembly machinery component 50 homolog
- Mitochondrial import receptor subunit TOM7 homolog
- Metaxin-1
- Translocase of outer mitochondrial membrane 5
- Mitochondrial import receptor subunit TOM40 homolog
- Superoxide dismutase
- Metaxin
- Mitochondrial import receptor subunit TOM20 homolog
Sequence:
MGNTLGLAPMGTLPRWSHRREEPLPNPGSFDELHRLCKDVFPAQMEGVKLVVNKVLSSHFQVAHTVHMSALGLPGYHLHTAYAGDWQLSPTEVFPTVVGDMDSSGSLNAQVLLLLAERLRAKAVFQTQQAKFLTWQFDGEYRGDDYTATLTLGNPDLIGESVIMVAHFLQSITHRLVLGGELVYHRRPGEEGAILTLAGKYSALHWVATLNVGSGGAHASYYHKANEQVQVGVEFEANTRLQDTTFSFGYHLTLPQADMVFRGLVDSNWCVGAVLEKKMRPLPVTLALGAFLNHWRNRFHCGFSITVG
Protein: Transcriptional regulator Myc-A (c-Myc-A) (zc-Myc) (P52160)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes.
Subcellular location: Nucleus.
Interaction partners:
- Kruppel-like factor 4.
- Biklf
- Cellular tumor antigen p53
- Mitogen-activated protein kinase
- G1/S-specific cyclin-D1
- Catenin beta-1
- Transcription factor Sox-2
- POU domain, class 5, transcription factor 1
- Ubiquitin-specific peptidase 28
- Mitogen-activated protein kinase
Sequence:
MERHSLNTSVKMPVSASLACKNYDYDYDSIQPYFYFDNDDEDFYHHQQGQTQPSAPSEDIWKKFELLPTPPLSPSRRQSLSTAEQLEMVSEFLGDDVVSQSFICDDADYSQSFIKSIIIQDCMWSGFSAAAKLEKVVSERLASLHAERKELMSDSNSNRLNASYLQDLSTSASECIDPSVVFPYPLTECGKAGKVASPQPMLVLDTPPNSSSSSGSDSEDEEEEDEEEEEEEEEEEEEEEEEEIDVVTVEKRQKRHETDASESRYPSPLVLKRCHVSTHQHNYAAHPSTRHDQPAVKRLRLEASNNHSINSSSSNRHVKQRKCASPRTSDSEDNDKRRTHNVLERQRRNELKLSFFALRDEIPEVANNEKAAKVVILKKATECIHSMQLDEQRLLSIKEQLRRKSEQLKHRLQQLRSSH
Protein: Methyl-coenzyme M reductase I subunit gamma (MCR I gamma) (EC 2.8.4.1) (Coenzyme-B sulfoethylthiotransferase gamma) (P11562)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis. Neither N-6-mercaptohexanoylthreonine phosphate (H-S-HxoTP) nor N-8-mercaptooctanoylthreonine phosphate (H-SOcoTP) nor any other thiol compound such as CoA or CoM can substitute for CoB as the electron donor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23533332}. Note=Under growth limiting conditions on nickel-depleted media, a fraction of 70% of the enzyme is localized close to the cytoplasmic membrane, which implies 'facultative' membrane association of the enzyme. {ECO:0000269|PubMed:23533332}.
Interaction partners:
- Methyl-coenzyme M reductase I subunit alpha
- Methyl-coenzyme M reductase I operon protein D
- Methyl-coenzyme M reductase I operon protein C
- Methyl-coenzyme M reductase I subunit beta
- Methyl-coenzyme M reductase II subunit alpha
- Methyl-coenzyme M reductase II subunit beta
- CCG domain-containing protein
- Tetrahydromethanopterin S-methyltransferase subunit D
- Tetrahydromethanopterin S-methyltransferase subunit E
- Tetrahydromethanopterin S-methyltransferase subunit G
Sequence:
MAQYYPGTTKVAQNRRNFCNPEYELEKLREISDEDVVKILGHRAPGEEYPSVHPPLEEMDEPEDAIREMVEPIDGAKAGDRVRYIQFTDSMYFAPAQPYVRSRAYLCRYRGADAGTLSGRQIIETRERDLEKISKELLETEFFDPARSGVRGKSVHGHSLRLDEDGMMFDMLRRQIYNKDTGRVEMVKNQIGDELDEPVDLGEPLDEETLMEKTTIYRVDGEAYRDDVEAVEIMQRIHVLRSQGGFNLE
Protein: Calcium/calmodulin-dependent protein kinase type II subunit gamma (CaM kinase II subunit gamma) (CaMK-II subunit gamma) (EC 2.7.11.17) (Q923T9)
Organism: Mus musculus (Mouse)
Function: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplasmic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity (By similarity). In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of the ryanodine receptor-coupling factor triadin (By similarity). In the central nervous system, it is involved in the regulation of neurite formation and arborization. It may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway.
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Calmodulin-1
- Calmodulin 5
- Calmodulin-4
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Ryanodine receptor 2
- Glutamate receptor 1
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Sequence:
MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHPWVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKKRKSSSSVHLMPQSNNKNSLVSPAQEPAPLQTAMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKVRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWLNVHYHCSGAPAAPLQ
Protein: Quinate/shikimate dehydrogenase (NAD(+)) (QSDH) (EC 1.1.1.-) (EC 1.1.1.24) (A4QB65)
Organism: Corynebacterium glutamicum (strain R)
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids, and plays a key role in the quinate degradation pathway. Catalyzes the NAD(+)-dependent oxidation of both quinate and shikimate to 3-dehydroquinate and 3-dehydroshikimate, respectively.
Interaction partners:
Sequence:
MNDSILLGLIGQGLDLSRTPAMHEAEGLAQGRATVYRRIDTLGSRASGQDLKTLLDAALYLGFNGLNITHPYKQAVLPLLDEVSEQATQLGAVNTVVIDANGHTTGHNTDVSGFGRGMEEGLPNAKLDSVVQVGAGGVGNAVAYALVTHGVQKLQVADLDTSRAQALADVINNAVGREAVVGVDARGIEDVIAAADGVVNATPMGMPAHPGTAFDVSCLTKDHWVGDVVYMPIETELLKAARALGCETLDGTRMAIHQAVDAFRLFTGLEPDVSRMRETFLSL
Protein: Spore germination lipase LipC (EC 3.-.-.-) (P42969)
Organism: Bacillus subtilis (strain 168)
Function: Lipase involved in spore germination.
Subcellular location: Spore coat {ECO:0000269|PubMed:17220230}.
Interaction partners:
- Uncharacterized protein YpmS
- 5-oxoprolinase subunit C
- Uncharacterized membrane protein YcsG
- HTH-type transcriptional regulator KipR
- 5-oxoprolinase subunit B
- 5-oxoprolinase subunit A
- Putative hydro-lyase YcsI
Sequence:
MVLRYTALGDSLTTGRGSGLFSPGFVQRFGDMMEADLKTRTAINIFARSGLNTEEILGLLSYPYVQKCIRDADMITITGCGNDLIDSVLAYQTSKDETIFSRVSAHCHENFEKMIAKVAEIKGENPSPYAIRVFNLYNPFPEIDIAGKWITSFNSHLETLASAPHVKIADAYSIFKGKEQEYLSFDGVHPNSKGYQAMAEAVHKLGYKELSVS
Protein: Cholesterol 16,22-dihydroxylase CYP90G4 (EC 1.14.14.-) (Cytochrome P450 CYP90G4) (PpCYP90G4) (Protein DWARF 4 homolog) (PpDWF4) (Steroid 22-alpha-hydroxylase CYP90G4) (EC 1.14.14.-) (A0A517FNC5)
Organism: Paris polyphylla (Daiswa polyphylla)
Function: Involved in the biosynthesis of spiroketal steroid and saponin natural products from cholesterol such as diosgenin and analogs (e.g. furostanol and spirostanol), plant defense compounds used as main precursors for the industrial production of steroid hormones. During the 5,6-spiroketalization of cholesterol, catalyzes the hydroxylation of cholesterol to form 16S,22S-dihydroxycholesterol and, possibly, the subsequent conversion of 16S,22S-dihydroxycholesterol into 16-oxo-22-hydroxy-cholesterol and 16-hydroxy-22-oxo-cholesterol. 16-hydroxy-22-oxo-cholesterol submit a spontaneous reaction leading to the production of furostanol-type steroid diastereomers, precursors of diosgenin.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAPVVILFFLFPTLLVLVVAVLGLRGGDDSWKKRGLKVPPGSMGWPLLGETIAFRRLHPCTSLGEYMEEHVNKYGKIYRSNLFGAPTIVSADAELNRFVLMNDERLFEPCFPKSVADILGHTSMLVLTGEMHRYMKSLSVNFMGIARLRNNFLGDSELYITQNFNRWKENIPFPAKEEACKVTFNLMVKNILSLNPGEPESEHLRKLYMSFMKGVVAIPLNLPGTAYKKAIQSRATILKMIEKLMEERIRNKKAGTDKIGEADLLGFILEQSNLDAEQFGDLLLGLLFGGHETSATAITLVIYFLYDCPKAVDHLREEHLGIVRAKKARGEPPALTWDDYKQMEFSQCVVSETLRLGNIIKFVHRKAKTDVQFKGYDIPKGWSVIPVFAAAHLDPSVYENPQKFDPWRWQTISTGTARIDNYMPFGQGLRNCAGLELAKMEIVVFLHHLTLNFDWEMAEPDHPLAYAFPDFPKGLPIKVRRLALK
Protein: Copine 3 (A0A087WXR6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAQCVTKVALNVSCANLLDKDIGSKSDPLCVLFLNTSGQQWYEVERTERIKNCLNPQFSKTFIIDYYFEVVQKLKFGVYDIDNKTIELSDDDFLGECECTLGQIVSSKKLTRPLVMKTGRPAGKGSITISAEEIKDNR
Protein: Negative elongation factor D (NELF-D) (TH1-like protein) (Q922L6)
Organism: Mus musculus (Mouse)
Function: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (By similarity). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8IXH7}.
Interaction partners:
- Negative elongation factor B
- Negative elongation factor A
- Negative elongation factor E
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4-A
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
Sequence:
MAGPAPGTIMGEDYFGNASEWGEEADGGQHQEDDSGEGEDDAEVQQECLHKFSTRDYIMEPSIFNTLKRYFQAGGSPENVIQLLSENYTAVAQTVNLLAEWLIQTGVEPVQVQETVENHLKSLLIKHFDPRKADSIFTEEGETPAWLEQMIAHTTWRDLFYKLAEAHPDCLMLNFTVKLISDAGYQGEITSVSTACQQLEVFSRVLRTSLATILDGGEENLEKNLPEFAKMVCHGEHTYLFAQAMMSVLAQEEQGGSAVRRVAQEVQRFAQEKGHDASQITLALGTAASYPRACQALGAMLSRGALNPADITVLFKMFTSMDPPPVELIRVPAFLDLFMQSLFKPGAKINQDHKHKYIHILAYAASVVETWKKNKRVSIGKDELKSTSKAIETVHNLCCNENKGASELVAELSTLYQCIRFPVVAMGVLKWVDWTVSEPRYFQLQTDHTPVHLALLDEISTCHQLLHPQVLQLLVKLFETEHSQLDVMEQLELKKTLLDRMVHLLSRGYVLPVVSYIRKCLEKLDTDISLIRYFVTEVLDVIAPPYTSDFVQLFLPILENDSIAGTIKAEGEHDPVTEFIAHCKSNFIVVN
Protein: V5-1 protein (Q5NV61)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
LPVLTQPPSASALLGASIKLTCTLSSEHSTYTIEWYQQRPGRSPQYIMKVKSDGSHSKGDGIPDRFMGSSSGADRYLTFSNLQSDDEAEYHCGESHTIDGQVG
Protein: Carbohydrate sulfotransferase 5 (EC 2.8.2.-) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 4) (GST4) (Intestinal N-acetylglucosamine-6-O-sulfotransferase) (I-GlcNAc6ST) (Intestinal GlcNAc-6-sulfotransferase) (mIGn6ST) (N-acetylglucosamine 6-O-sulfotransferase 3) (GlcNAc6ST-3) (Gn6st-3) (Q9QUP4)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues of keratan. Mediates sulfation of keratan in cornea. Keratan sulfate plays a central role in maintaining corneal transparency. Acts on the non-reducing terminal GlcNAc of short and long carbohydrate substrates that have poly-N-acetyllactosamine structures. May also have activity toward O-linked sugars of mucin-type acceptors.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Golgi membrane, early secretory pathway. {ECO:0000250}.
Interaction partners:
Sequence:
MRLPRFSSTVMLSLLMVQTGILVFLVSRQVPSSPAGLGERVHVLVLSSWRSGSSFVGQLFSQHPDVFYLMEPAWHVWDTLSQGSAPALHMAVRDLIRSVFLCDMDVFDAYLPWRRNISDLFQWAVSRALCSPPVCEAFARGNISSEEVCKPLCATRPFGLAQEACSSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREQTAKALARDNGIVLGTNGTWVEADPRLRVVNEVCRSHVRIAEAALHKPPPFLQDRYRLVRYEDLARDPLTVIRELYAFTGLGLTPQLQTWIHNITHGSGPGARREAFKTTSRDALSVSQAWRHTLPFAKIRRVQELCGGALQLLGYRSVHSELEQRDLSLDLLLPRGMDSFKWASSTEKQPES
Protein: SUMO-conjugating enzyme UBC9 (EC 2.3.2.-) (RING-type E3 SUMO transferase UBC9) (SUMO-protein ligase) (Ubiquitin carrier protein 9) (Ubiquitin carrier protein I) (Ubiquitin-conjugating enzyme E2 I) (Ubiquitin-protein ligase I) (P63282)
Organism: Xenopus laevis (African clawed frog)
Function: Accepts the ubiquitin-like proteins sumo1, sumo2 and sumo3 from the uble1a-uble1b E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as ranbp2 or cbx4. Essential for nuclear architecture and chromosome segregation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS
Protein: Heat shock transcription factor 1 (E9PMQ6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEEPPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGRPPSPPPTSTPEKCLSVACLDNLARTPQMSRVARLFPCPSSSPHGQVQPGNELSDHLDAMDSNLDNLQTMLSSHGFSVDTSALLDIQELLSPQEPPRPPEAENSSPDSAGALHSAAAVPAGPRLRGHREQRPAGAV
Protein: RNA-binding protein 33 (Proline-rich protein 8) (RNA-binding motif protein 33) (Q96EV2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:35589130}. Cytoplasm {ECO:0000269|PubMed:35589130}. Note=Localizes predominantly to the nucleus. {ECO:0000269|PubMed:35589130}.
Interaction partners:
Sequence:
MAAALGASGGAGAGDDDFDQFDKPGAERSWRRRAADEDWDSELEDDLLGEDLLSGKKNQSDLSDEELNDDLLQSDNEDEENFSSQGVTISLNATSGMVTSFELSDNTNDQSGEQESEYEQEQGEDELVYHKSDGSELYTQEYPEEGQYEGHEAELTEDQIEYVEEPEEEQLYTDEVLDIEINEPLDEFTGGMETLELQKDIKEESDEEEEDDEESGRLRFKTERKEGTIIRLSDVTRERRNIPETLELSAEAKAALLEFEERERQHKQGRYSSRRGGRRGGPLMCRGVGDQRRESTERGRMKDHRPALLPTQPPVVPQAPPPPPPPPQQQPIRSLFQPQPLQPLLPVQHPHHPSPPQGMHMPPQLETPRMMMTPPPVTPQQPKNIHINPHFKGTVVTPVQVPLLPVPSQPRPAVGPQRFPGPPEFPQHTPGPVPNSFSQPPRLPLQDQWRAPPPPQDRDPFFLGVSGEPRFPSHLFLEQRSPPPPPPPPTLLNSSHPVPTQSPLPFTQPGPAFNQQGQQPVFPRERPVRPALQPPGPVGILHFSQPGSATTRPFIPPRQPFLPGPGQPFLPTHTQPNLQGPLHPPLPPPHQPQPQQPQQQPPPQHQPPHQPPHQPPPQHQPPPQHPPQHPPQHQHHHHHHHLSVPPPPLMPMSQPQFRPHVQTAQPQASSSRMQCPQRQGLRHNTTSQNVSKRPMQQMQPTAPRNSNLRELPIAPSHVIEMSSSRCSATPSAQVKPIVSASPPSRAVAGSRSSQGKTEVKVKPASPVAQPKEEAKTETEFPDEDEETRLYRLKIEEQKRLREEILKQKELRRQQQAGARKKELLERLAQQQQQLYAPPPPAEQEEQALSPSPTNGNPLLPFPGAQVRQNVKNRLLVKNQDVSISNVQPKTSNFVPSSANMQYQGQQMKALKHLRQTRTVPQSQTQPLHKVLPIKPADVEEPAVPQTPRVASIQGRPQDTKPGVKRTVTHRTNSGGGDGPHISSKVRVIKLSGGGGESDGFFHPEGQPQRLPQPPEVGPQPARKVTLTRGGLQQPPHLPAGPHAHSPVPPGIKSIQGIHPAKKAIMHGRGRGVAGPMGRGRLMPNKQNLRVVECKPQPCVVSVEGLSSSTTDAQLKSLLMSVGPIQSLQMLPQQRKAIAKFKEPAHALAFQQKFHRHMIDLSHINVALIVE