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RPAB2_HUMAN
ID   RPAB2_HUMAN             Reviewed;         127 AA.
AC   P61218; P41584; Q6IAY3;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC2;
DE            Short=RNA polymerases I, II, and III subunit ABC2;
DE   AltName: Full=DNA-directed RNA polymerase II subunit F;
DE   AltName: Full=DNA-directed RNA polymerases I, II, and III 14.4 kDa polypeptide;
DE   AltName: Full=RPABC14.4;
DE            Short=RPB14.4;
DE   AltName: Full=RPB6 homolog;
DE   AltName: Full=RPC15;
GN   Name=POLR2F; Synonyms=POLRF;
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 [GENOMIC DNA].
RX   PubMed=7803819; DOI=10.3109/10425179409020860;
RA   Acker J., Wintzerith M., Vigneron M., Kedinger C.;
RT   "A 14.4 KDa acidic subunit of human RNA polymerase II with a putative
RT   leucine-zipper.";
RL   DNA Seq. 4:329-331(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8786150; DOI=10.1006/geno.1996.0312;
RA   Pusch C., Wang Z., Roe B., Blin N.;
RT   "Genomic structure of the RNA polymerase II small subunit (hRPB14.4) locus
RT   (POLRF) and mapping to 22q13.1 by sequence identity.";
RL   Genomics 34:440-442(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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).
RN   [8]
RP   FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
RA   Kershnar E., Wu S.-Y., Chiang C.-M.;
RT   "Immunoaffinity purification and functional characterization of human
RT   transcription factor IIH and RNA polymerase II from clonal cell lines that
RT   conditionally express epitope-tagged subunits of the multiprotein
RT   complexes.";
RL   J. Biol. Chem. 273:34444-34453(1998).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   STRUCTURE BY NMR.
RX   PubMed=10542096; DOI=10.1038/14923;
RA   del Rio-Portilla F., Gaskell A., Gilbert D., Ladias J.A., Wagner G.;
RT   "Solution structure of the hRPABC14.4 subunit of human RNA polymerases.";
RL   Nat. Struct. Biol. 6:1039-1042(1999).
RN   [12]
RP   VARIANT [LARGE SCALE ANALYSIS] ASN-60.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: DNA-dependent RNA polymerases catalyze 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 small RNAs, such as 5S rRNA and tRNAs, respectively.
CC       Pol II is the central component of the basal RNA polymerase II
CC       transcription machinery. Pols are composed of mobile elements that move
CC       relative to each other. In Pol II, POLR2F/RPB6 is part of the clamp
CC       element and together with parts of RPB1 and RPB2 forms a pocket to
CC       which the RPB4-RPB7 subcomplex binds (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:9852112}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852112}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC       subunit family. {ECO:0000305}.
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DR   EMBL; Z27113; CAA81629.1; -; Genomic_DNA.
DR   EMBL; AF006501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR456546; CAG30432.1; -; mRNA.
DR   EMBL; CR457021; CAG33302.1; -; mRNA.
DR   EMBL; AL031587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471095; EAW60203.1; -; Genomic_DNA.
DR   EMBL; BC003582; AAH03582.1; -; mRNA.
DR   CCDS; CCDS13963.1; -.
DR   PIR; I38175; S38627.
DR   RefSeq; NP_068809.1; NM_021974.4.
DR   PDB; 1QKL; NMR; -; A=1-127.
DR   PDB; 5IY6; EM; 7.20 A; F=1-127.
DR   PDB; 5IY7; EM; 8.60 A; F=1-127.
DR   PDB; 5IY8; EM; 7.90 A; F=1-127.
DR   PDB; 5IY9; EM; 6.30 A; F=1-127.
DR   PDB; 5IYA; EM; 5.40 A; F=1-127.
DR   PDB; 5IYB; EM; 3.90 A; F=1-127.
DR   PDB; 5IYC; EM; 3.90 A; F=1-127.
DR   PDB; 5IYD; EM; 3.90 A; F=1-127.
DR   PDB; 6DRD; EM; 3.90 A; F=1-127.
DR   PDB; 6O9L; EM; 7.20 A; F=1-127.
DR   PDB; 6XRE; EM; 4.60 A; F=1-127.
DR   PDB; 7A6H; EM; 3.30 A; F=1-127.
DR   PDB; 7AE1; EM; 2.80 A; F=1-127.
DR   PDB; 7AE3; EM; 3.10 A; F=1-127.
DR   PDB; 7AEA; EM; 3.40 A; F=1-127.
DR   PDB; 7AST; EM; 4.00 A; E=1-127.
DR   PDB; 7D58; EM; 2.90 A; F=1-127.
DR   PDB; 7D59; EM; 3.10 A; F=1-127.
DR   PDB; 7DN3; EM; 3.50 A; F=1-127.
DR   PDB; 7DTH; NMR; -; A=1-127.
DR   PDB; 7DU2; EM; 3.35 A; F=1-127.
DR   PDB; 7FJI; EM; 3.60 A; F=1-127.
DR   PDB; 7FJJ; EM; 3.60 A; F=1-127.
DR   PDB; 7LBM; EM; 4.80 A; F=1-127.
DR   PDB; 7OB9; EM; 2.70 A; F=1-127.
DR   PDB; 7OBA; EM; 3.10 A; F=1-127.
DR   PDB; 7OBB; EM; 3.30 A; F=1-127.
DR   PDB; 7VBA; EM; 2.89 A; F=1-127.
DR   PDB; 7VBB; EM; 2.81 A; F=1-127.
DR   PDB; 7VBC; EM; 3.01 A; F=1-127.
DR   PDBsum; 1QKL; -.
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; 7DTH; -.
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; P61218; -.
DR   SMR; P61218; -.
DR   BioGRID; 111431; 109.
DR   CORUM; P61218; -.
DR   DIP; DIP-32915N; -.
DR   IntAct; P61218; 68.
DR   MINT; P61218; -.
DR   STRING; 9606.ENSP00000403852; -.
DR   iPTMnet; P61218; -.
DR   PhosphoSitePlus; P61218; -.
DR   SwissPalm; P61218; -.
DR   BioMuta; POLR2F; -.
DR   DMDM; 47117761; -.
DR   EPD; P61218; -.
DR   jPOST; P61218; -.
DR   MassIVE; P61218; -.
DR   MaxQB; P61218; -.
DR   PaxDb; P61218; -.
DR   PeptideAtlas; P61218; -.
DR   PRIDE; P61218; -.
DR   ProteomicsDB; 57275; -.
DR   Antibodypedia; 227; 131 antibodies from 26 providers.
DR   DNASU; 5435; -.
DR   Ensembl; ENST00000442738.7; ENSP00000403852.2; ENSG00000100142.16.
DR   GeneID; 5435; -.
DR   KEGG; hsa:5435; -.
DR   MANE-Select; ENST00000442738.7; ENSP00000403852.2; NM_021974.5; NP_068809.1.
DR   UCSC; uc003aul.4; human.
DR   CTD; 5435; -.
DR   DisGeNET; 5435; -.
DR   GeneCards; POLR2F; -.
DR   HGNC; HGNC:9193; POLR2F.
DR   HPA; ENSG00000100142; Low tissue specificity.
DR   MalaCards; POLR2F; -.
DR   MIM; 604414; gene.
DR   neXtProt; NX_P61218; -.
DR   OpenTargets; ENSG00000100142; -.
DR   PharmGKB; PA33513; -.
DR   VEuPathDB; HostDB:ENSG00000100142; -.
DR   eggNOG; KOG3405; Eukaryota.
DR   GeneTree; ENSGT00390000010415; -.
DR   InParanoid; P61218; -.
DR   OMA; QEEDGYN; -.
DR   PhylomeDB; P61218; -.
DR   TreeFam; TF103041; -.
DR   PathwayCommons; P61218; -.
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; P61218; -.
DR   SIGNOR; P61218; -.
DR   BioGRID-ORCS; 5435; 783 hits in 1078 CRISPR screens.
DR   ChiTaRS; POLR2F; human.
DR   EvolutionaryTrace; P61218; -.
DR   GeneWiki; POLR2F; -.
DR   GenomeRNAi; 5435; -.
DR   Pharos; P61218; Tbio.
DR   PRO; PR:P61218; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; P61218; protein.
DR   Bgee; ENSG00000100142; Expressed in C1 segment of cervical spinal cord and 208 other tissues.
DR   ExpressionAtlas; P61218; baseline and differential.
DR   Genevisible; P61218; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR   Gene3D; 3.90.940.10; -; 1.
DR   InterPro; IPR020708; DNA-dir_RNA_polK_14-18kDa_CS.
DR   InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR   InterPro; IPR028363; RPB6.
DR   InterPro; IPR036161; RPB6/omega-like_sf.
DR   InterPro; IPR006111; Rpo6/Rpb6.
DR   Pfam; PF01192; RNA_pol_Rpb6; 1.
DR   PIRSF; PIRSF500154; RPB6; 1.
DR   PIRSF; PIRSF000778; RpoK/RPB6; 1.
DR   SMART; SM01409; RNA_pol_Rpb6; 1.
DR   SUPFAM; SSF63562; SSF63562; 1.
DR   PROSITE; PS01111; RNA_POL_K_14KD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; DNA-directed RNA polymerase; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   CHAIN           2..127
FT                   /note="DNA-directed RNA polymerases I, II, and III subunit
FT                   RPABC2"
FT                   /id="PRO_0000133799"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         2
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:O88828"
FT   VARIANT         60
FT                   /note="Y -> N (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036571"
FT   HELIX           3..6
FT                   /evidence="ECO:0007829|PDB:7DTH"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:1QKL"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:1QKL"
FT   STRAND          35..40
FT                   /evidence="ECO:0007829|PDB:1QKL"
FT   HELIX           59..74
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:1QKL"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:1QKL"
FT   HELIX           89..98
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          105..108
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:7D58"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:7OB9"
FT   STRAND          123..125
FT                   /evidence="ECO:0007829|PDB:7DTH"
SQ   SEQUENCE   127 AA;  14478 MW;  6362B0D7EB3F0921 CRC64;
     MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK RITTPYMTKY
     ERARVLGTRA LQIAMCAPVM VELEGETDPL LIAMKELKAR KIPIIIRRYL PDGSYEDWGV
     DELIITD
 
 
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