RPB3_HUMAN
ID RPB3_HUMAN Reviewed; 275 AA.
AC P19387; O15161;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB3 {ECO:0000305};
DE Short=RNA polymerase II subunit 3;
DE Short=RNA polymerase II subunit B3;
DE AltName: Full=DNA-directed RNA polymerase II 33 kDa polypeptide;
DE Short=RPB33;
DE AltName: Full=DNA-directed RNA polymerase II subunit C;
DE AltName: Full=RPB31 {ECO:0000250|UniProtKB:P97760};
GN Name=POLR2C {ECO:0000312|HGNC:HGNC:9189}; ORFNames=A-152E5.7;
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=2187864; DOI=10.1016/s0021-9258(19)38900-8;
RA Pati U.K., Weissman S.M.;
RT "The amino acid sequence of the human RNA polymerase II 33-kDa subunit hRPB
RT 33 is highly conserved among eukaryotes.";
RL J. Biol. Chem. 265:8400-8403(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9540830; DOI=10.1016/s0167-4781(97)00206-6;
RA Dammann R., Pfeifer G.P.;
RT "Cloning and characterization of the human RNA polymerase I subunit
RT hRPA40.";
RL Biochim. Biophys. Acta 1396:153-157(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Bruno T., di Padova M., de Angelis R., Iacobini C., Lovari S.,
RA Passananti C., Fanciulli M.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Kidney, and Muscle;
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 [6]
RP PROTEIN SEQUENCE OF 2-35; 68-86; 134-152; 176-193 AND 256-275, CLEAVAGE OF
RP INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase II which synthesizes mRNA precursors and
CC many functional non-coding RNAs. Pol II is the central component of the
CC basal RNA polymerase II transcription machinery. It is composed of
CC mobile elements that move relative to each other. RPB3 is part of the
CC core element with the central large cleft and the clamp element that
CC moves to open and close the cleft (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9852112}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. RPB11/POLR2J and RPB3/POLR2C subunits interact with
CC each other. {ECO:0000269|PubMed:9852112}.
CC -!- INTERACTION:
CC P19387; P18848: ATF4; NbExp=6; IntAct=EBI-394729, EBI-492498;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852112}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; J05448; AAA36586.1; -; mRNA.
DR EMBL; AF008443; AAC14355.1; -; mRNA.
DR EMBL; AJ224143; CAA11842.1; -; mRNA.
DR EMBL; AJ224144; CAA11843.1; -; mRNA.
DR EMBL; AC004382; AAC24309.1; -; Genomic_DNA.
DR EMBL; BC000409; AAH00409.1; -; mRNA.
DR EMBL; BC003159; AAH03159.1; -; mRNA.
DR EMBL; BC028157; AAH28157.1; -; mRNA.
DR CCDS; CCDS10782.1; -.
DR PIR; A36264; A36264.
DR RefSeq; NP_116558.1; NM_032940.2.
DR PDB; 5IY6; EM; 7.20 A; C=1-275.
DR PDB; 5IY7; EM; 8.60 A; C=1-275.
DR PDB; 5IY8; EM; 7.90 A; C=1-275.
DR PDB; 5IY9; EM; 6.30 A; C=1-275.
DR PDB; 5IYA; EM; 5.40 A; C=1-275.
DR PDB; 5IYB; EM; 3.90 A; C=1-275.
DR PDB; 5IYC; EM; 3.90 A; C=1-275.
DR PDB; 5IYD; EM; 3.90 A; C=1-275.
DR PDB; 6DRD; EM; 3.90 A; C=1-275.
DR PDB; 6O9L; EM; 7.20 A; C=1-275.
DR PDB; 6XRE; EM; 4.60 A; C=1-275.
DR PDB; 7LBM; EM; 4.80 A; C=1-275.
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; 7LBM; -.
DR AlphaFoldDB; P19387; -.
DR SMR; P19387; -.
DR BioGRID; 111428; 308.
DR CORUM; P19387; -.
DR DIP; DIP-32911N; -.
DR IntAct; P19387; 96.
DR MINT; P19387; -.
DR STRING; 9606.ENSP00000219252; -.
DR iPTMnet; P19387; -.
DR PhosphoSitePlus; P19387; -.
DR BioMuta; POLR2C; -.
DR DMDM; 3915850; -.
DR EPD; P19387; -.
DR jPOST; P19387; -.
DR MassIVE; P19387; -.
DR PaxDb; P19387; -.
DR PeptideAtlas; P19387; -.
DR PRIDE; P19387; -.
DR ProteomicsDB; 53652; -.
DR Antibodypedia; 28873; 181 antibodies from 27 providers.
DR DNASU; 5432; -.
DR Ensembl; ENST00000219252.10; ENSP00000219252.4; ENSG00000102978.13.
DR GeneID; 5432; -.
DR KEGG; hsa:5432; -.
DR MANE-Select; ENST00000219252.10; ENSP00000219252.4; NM_032940.3; NP_116558.1.
DR CTD; 5432; -.
DR DisGeNET; 5432; -.
DR GeneCards; POLR2C; -.
DR HGNC; HGNC:9189; POLR2C.
DR HPA; ENSG00000102978; Low tissue specificity.
DR MIM; 180663; gene.
DR neXtProt; NX_P19387; -.
DR OpenTargets; ENSG00000102978; -.
DR PharmGKB; PA33509; -.
DR VEuPathDB; HostDB:ENSG00000102978; -.
DR eggNOG; KOG1522; Eukaryota.
DR GeneTree; ENSGT00950000183100; -.
DR HOGENOM; CLU_038421_1_0_1; -.
DR InParanoid; P19387; -.
DR OMA; PENIVMM; -.
DR OrthoDB; 834009at2759; -.
DR PhylomeDB; P19387; -.
DR TreeFam; TF103038; -.
DR PathwayCommons; P19387; -.
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-203927; MicroRNA (miRNA) biogenesis.
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-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
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-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; P19387; -.
DR SIGNOR; P19387; -.
DR BioGRID-ORCS; 5432; 802 hits in 1078 CRISPR screens.
DR ChiTaRS; POLR2C; human.
DR GeneWiki; POLR2C; -.
DR GenomeRNAi; 5432; -.
DR Pharos; P19387; Tbio.
DR PRO; PR:P19387; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P19387; protein.
DR Bgee; ENSG00000102978; Expressed in islet of Langerhans and 209 other tissues.
DR ExpressionAtlas; P19387; baseline and differential.
DR Genevisible; P19387; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1.
DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1.
DR InterPro; IPR036643; RNApol_insert_sf.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-directed RNA polymerase;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..275
FT /note="DNA-directed RNA polymerase II subunit RPB3"
FT /id="PRO_0000132743"
FT REGION 203..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT 194
FT /note="H -> T (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 31441 MW; EF663BE096046A4B CRC64;
MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH
DEFIAHRLGL IPLISDDIVD KLQYSRDCTC EEFCPECSVE FTLDVRCNED QTRHVTSRDL
ISNSPRVIPV TSRNRDNDPN DYVEQDDILI VKLRKGQELR LRAYAKKGFG KEHAKWNPTA
GVAFEYDPDN ALRHTVYPKP EEWPKSEYSE LDEDESQAPY DPNGKPERFY YNVESCGSLR
PETIVLSALS GLKKKLSDLQ TQLSHEIQSD VLTIN
