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RPAB4_HUMAN
ID   RPAB4_HUMAN             Reviewed;          58 AA.
AC   P53803; Q6IBD4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC4;
DE            Short=RNA polymerases I, II, and III subunit ABC4;
DE   AltName: Full=ABC10-alpha;
DE   AltName: Full=DNA-directed RNA polymerase II subunit K;
DE   AltName: Full=RNA polymerase II 7.0 kDa subunit;
DE            Short=RPB7.0;
DE   AltName: Full=RPB10alpha;
GN   Name=POLR2K;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7651387; DOI=10.1128/mcb.15.9.4702;
RA   Shpakovski G.V., Acker J., Wintzerith M., Lacroix J.F., Thuriaux P.,
RA   Vigneron M.;
RT   "Four subunits that are shared by the three classes of RNA polymerase are
RT   functionally interchangeable between Homo sapiens and Saccharomyces
RT   cerevisiae.";
RL   Mol. Cell. Biol. 15:4702-4710(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RA   Shpakovski G.V., Lebedenko E.N., Grandemange S., Schaller S., Vigneron M.,
RA   Kedinger C.;
RT   "Organization of genes encoding subunits of eucaryotic nuclear RNA
RT   polymerases shows non random intron distribution and correlates with the
RT   subunit modular structure.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Common component of RNA polymerases I, II and III which synthesize
CC       ribosomal RNA precursors, mRNA precursors and many functional non-
CC       coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively.
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC       (Pol II) and RNA polymerase III (Pol III) complexes consisting of at
CC       least 13, 12 and 17 subunits, respectively. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P53803; Q96B97: SH3KBP1; NbExp=3; IntAct=EBI-395357, EBI-346595;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA
CC       polymerase subunit family. {ECO:0000305}.
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DR   EMBL; Z47727; CAA87656.1; -; mRNA.
DR   EMBL; AJ252078; CAB91873.1; -; Genomic_DNA.
DR   EMBL; CR456870; CAG33151.1; -; mRNA.
DR   EMBL; CH471060; EAW91798.1; -; Genomic_DNA.
DR   EMBL; BC000806; AAH00806.1; -; mRNA.
DR   EMBL; BC018157; AAH18157.1; -; mRNA.
DR   CCDS; CCDS6285.1; -.
DR   PIR; I37558; I37558.
DR   RefSeq; NP_005025.1; NM_005034.3.
DR   PDB; 5IY6; EM; 7.20 A; L=1-58.
DR   PDB; 5IY7; EM; 8.60 A; L=1-58.
DR   PDB; 5IY8; EM; 7.90 A; L=1-58.
DR   PDB; 5IY9; EM; 6.30 A; L=1-58.
DR   PDB; 5IYA; EM; 5.40 A; L=1-58.
DR   PDB; 5IYB; EM; 3.90 A; L=1-58.
DR   PDB; 5IYC; EM; 3.90 A; L=1-58.
DR   PDB; 5IYD; EM; 3.90 A; L=1-58.
DR   PDB; 6DRD; EM; 3.90 A; L=1-58.
DR   PDB; 6O9L; EM; 7.20 A; L=1-58.
DR   PDB; 6XRE; EM; 4.60 A; L=1-58.
DR   PDB; 7A6H; EM; 3.30 A; L=1-58.
DR   PDB; 7AE1; EM; 2.80 A; L=1-58.
DR   PDB; 7AE3; EM; 3.10 A; L=1-58.
DR   PDB; 7AEA; EM; 3.40 A; L=1-58.
DR   PDB; 7AST; EM; 4.00 A; C=1-58.
DR   PDB; 7D58; EM; 2.90 A; L=1-58.
DR   PDB; 7D59; EM; 3.10 A; L=1-58.
DR   PDB; 7DN3; EM; 3.50 A; L=1-58.
DR   PDB; 7DU2; EM; 3.35 A; L=1-58.
DR   PDB; 7FJI; EM; 3.60 A; L=1-58.
DR   PDB; 7FJJ; EM; 3.60 A; L=1-58.
DR   PDB; 7LBM; EM; 4.80 A; L=1-58.
DR   PDB; 7OB9; EM; 2.70 A; L=1-58.
DR   PDB; 7OBA; EM; 3.10 A; L=1-58.
DR   PDB; 7OBB; EM; 3.30 A; L=1-58.
DR   PDB; 7VBA; EM; 2.89 A; L=1-58.
DR   PDB; 7VBB; EM; 2.81 A; L=1-58.
DR   PDB; 7VBC; EM; 3.01 A; L=1-58.
DR   PDBsum; 5IY6; -.
DR   PDBsum; 5IY7; -.
DR   PDBsum; 5IY8; -.
DR   PDBsum; 5IY9; -.
DR   PDBsum; 5IYA; -.
DR   PDBsum; 5IYB; -.
DR   PDBsum; 5IYC; -.
DR   PDBsum; 5IYD; -.
DR   PDBsum; 6DRD; -.
DR   PDBsum; 6O9L; -.
DR   PDBsum; 6XRE; -.
DR   PDBsum; 7A6H; -.
DR   PDBsum; 7AE1; -.
DR   PDBsum; 7AE3; -.
DR   PDBsum; 7AEA; -.
DR   PDBsum; 7AST; -.
DR   PDBsum; 7D58; -.
DR   PDBsum; 7D59; -.
DR   PDBsum; 7DN3; -.
DR   PDBsum; 7DU2; -.
DR   PDBsum; 7FJI; -.
DR   PDBsum; 7FJJ; -.
DR   PDBsum; 7LBM; -.
DR   PDBsum; 7OB9; -.
DR   PDBsum; 7OBA; -.
DR   PDBsum; 7OBB; -.
DR   PDBsum; 7VBA; -.
DR   PDBsum; 7VBB; -.
DR   PDBsum; 7VBC; -.
DR   AlphaFoldDB; P53803; -.
DR   SMR; P53803; -.
DR   BioGRID; 111436; 73.
DR   CORUM; P53803; -.
DR   DIP; DIP-32968N; -.
DR   IntAct; P53803; 15.
DR   MINT; P53803; -.
DR   STRING; 9606.ENSP00000342889; -.
DR   iPTMnet; P53803; -.
DR   PhosphoSitePlus; P53803; -.
DR   BioMuta; POLR2K; -.
DR   DMDM; 1710664; -.
DR   EPD; P53803; -.
DR   jPOST; P53803; -.
DR   MassIVE; P53803; -.
DR   MaxQB; P53803; -.
DR   PaxDb; P53803; -.
DR   PeptideAtlas; P53803; -.
DR   PRIDE; P53803; -.
DR   ProteomicsDB; 56622; -.
DR   TopDownProteomics; P53803; -.
DR   Antibodypedia; 26170; 104 antibodies from 20 providers.
DR   DNASU; 5440; -.
DR   Ensembl; ENST00000353107.8; ENSP00000342889.3; ENSG00000147669.11.
DR   GeneID; 5440; -.
DR   KEGG; hsa:5440; -.
DR   MANE-Select; ENST00000353107.8; ENSP00000342889.3; NM_005034.4; NP_005025.1.
DR   UCSC; uc003yjf.4; human.
DR   CTD; 5440; -.
DR   DisGeNET; 5440; -.
DR   GeneCards; POLR2K; -.
DR   HGNC; HGNC:9198; POLR2K.
DR   HPA; ENSG00000147669; Low tissue specificity.
DR   MIM; 606033; gene.
DR   neXtProt; NX_P53803; -.
DR   OpenTargets; ENSG00000147669; -.
DR   PharmGKB; PA33518; -.
DR   VEuPathDB; HostDB:ENSG00000147669; -.
DR   eggNOG; KOG3507; Eukaryota.
DR   GeneTree; ENSGT00390000008918; -.
DR   HOGENOM; CLU_179456_1_0_1; -.
DR   InParanoid; P53803; -.
DR   OMA; VIRCREC; -.
DR   OrthoDB; 1620152at2759; -.
DR   PhylomeDB; P53803; -.
DR   TreeFam; TF103045; -.
DR   PathwayCommons; P53803; -.
DR   Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR   Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR   Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR   Reactome; R-HSA-167161; HIV Transcription Initiation.
DR   Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR   Reactome; R-HSA-167172; Transcription of the HIV genome.
DR   Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR   Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR   Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR   Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR   Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR   Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR   Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR   Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR   Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR   Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
DR   Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR   Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR   Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR   Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR   Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR   Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-HSA-72086; mRNA Capping.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
DR   Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR   Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR   Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR   Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR   Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR   Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR   Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR   SignaLink; P53803; -.
DR   SIGNOR; P53803; -.
DR   BioGRID-ORCS; 5440; 713 hits in 1000 CRISPR screens.
DR   ChiTaRS; POLR2K; human.
DR   GeneWiki; POLR2K; -.
DR   GenomeRNAi; 5440; -.
DR   Pharos; P53803; Tbio.
DR   PRO; PR:P53803; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P53803; protein.
DR   Bgee; ENSG00000147669; Expressed in islet of Langerhans and 210 other tissues.
DR   ExpressionAtlas; P53803; baseline and differential.
DR   Genevisible; P53803; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
DR   GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR   GO; GO:0006356; P:regulation of transcription by RNA polymerase I; TAS:ProtInc.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006383; P:transcription by RNA polymerase III; TAS:ProtInc.
DR   InterPro; IPR006591; RNAP_P/RPABC4.
DR   InterPro; IPR039747; RPABC4.
DR   InterPro; IPR029040; RPABC4/Spt4.
DR   PANTHER; PTHR12056; PTHR12056; 1.
DR   Pfam; PF03604; DNA_RNApol_7kD; 1.
DR   SMART; SM00659; RPOLCX; 1.
DR   SUPFAM; SSF63393; SSF63393; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Metal-binding; Nucleus;
KW   Reference proteome; Transcription; Zinc; Zinc-finger.
FT   CHAIN           1..58
FT                   /note="DNA-directed RNA polymerases I, II, and III subunit
FT                   RPABC4"
FT                   /id="PRO_0000159750"
FT   ZN_FING         19..39
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   STRAND          16..22
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          42..46
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:7OB9"
SQ   SEQUENCE   58 AA;  7004 MW;  239BA3A67416F02C CRC64;
     MDTQKDVQPP KQQPMIYICG ECHTENEIKS RDPIRCRECG YRIMYKKRTK RLVVFDAR
 
 
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