RPAB3_HUMAN
ID RPAB3_HUMAN Reviewed; 150 AA.
AC P52434; C9J413; C9JBJ6; C9JCU7; C9JUA8; P53802; Q969R0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC3;
DE Short=RNA polymerases I, II, and III subunit ABC3;
DE AltName: Full=DNA-directed RNA polymerase II subunit H;
DE AltName: Full=DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide;
DE AltName: Full=RPB17;
DE AltName: Full=RPB8 homolog;
DE Short=hRPB8;
GN Name=POLR2H;
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] (ISOFORM 1).
RX PubMed=8524256; DOI=10.1128/mcb.15.12.6895;
RA McKune K., Moore P.A., Hull M.W., Woychik N.A.;
RT "Six human RNA polymerase subunits functionally substitute for their yeast
RT counterparts.";
RL Mol. Cell. Biol. 15:6895-6900(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP PROTEIN SEQUENCE OF 2-13 AND 99-111, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) 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 IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=16809778; DOI=10.1128/mcb.00230-06;
RA Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J.,
RA Zomerdijk J.C.B.M.;
RT "RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation
RT of transcription by upstream binding factor.";
RL Mol. Cell. Biol. 26:5436-5448(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP STRUCTURE BY NMR, DNA-BINDING REGION, SUBUNIT, AND INTERACTION WITH POLR2A.
RX PubMed=16632472; DOI=10.1074/jbc.m513241200;
RA Kang X., Hu Y., Li Y., Guo X., Jiang X., Lai L., Xia B., Jin C.;
RT "Structural, biochemical, and dynamic characterizations of the hRPB8
RT subunit of human RNA polymerases.";
RL J. Biol. Chem. 281:18216-18226(2006).
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 small RNAs, such as 5S rRNA and tRNAs, respectively.
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. Directly interacts with
CC POLR2A. {ECO:0000269|PubMed:16632472, ECO:0000269|PubMed:16809778,
CC ECO:0000269|PubMed:9852112}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9852112,
CC ECO:0000269|Ref.6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P52434-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52434-2; Sequence=VSP_055018;
CC Name=3;
CC IsoId=P52434-3; Sequence=VSP_055017;
CC Name=4;
CC IsoId=P52434-4; Sequence=VSP_055019;
CC Name=5;
CC IsoId=P52434-5; Sequence=VSP_055017, VSP_055018;
CC -!- SIMILARITY: Belongs to the eukaryotic RPB8 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; U37689; AAA91458.1; -; mRNA.
DR EMBL; Z49199; CAA89060.1; -; mRNA.
DR EMBL; AJ252079; CAB92189.1; -; Genomic_DNA.
DR EMBL; AJ252080; CAB92189.1; JOINED; Genomic_DNA.
DR EMBL; AC078797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000739; AAH00739.1; -; mRNA.
DR CCDS; CCDS3264.1; -. [P52434-1]
DR CCDS; CCDS63859.1; -. [P52434-4]
DR CCDS; CCDS63860.1; -. [P52434-2]
DR CCDS; CCDS63861.1; -. [P52434-3]
DR CCDS; CCDS63862.1; -. [P52434-5]
DR PIR; S55370; S55370.
DR RefSeq; NP_001265627.1; NM_001278698.1. [P52434-4]
DR RefSeq; NP_001265628.1; NM_001278699.2. [P52434-3]
DR RefSeq; NP_001265629.1; NM_001278700.1. [P52434-3]
DR RefSeq; NP_001265643.1; NM_001278714.1. [P52434-2]
DR RefSeq; NP_001265644.1; NM_001278715.1. [P52434-5]
DR RefSeq; NP_006223.2; NM_006232.4. [P52434-1]
DR RefSeq; XP_006713729.1; XM_006713666.2. [P52434-4]
DR RefSeq; XP_006713730.1; XM_006713667.2. [P52434-4]
DR RefSeq; XP_016862125.1; XM_017006636.1. [P52434-2]
DR RefSeq; XP_016862126.1; XM_017006637.1. [P52434-5]
DR PDB; 2F3I; NMR; -; A=1-150.
DR PDB; 5IY6; EM; 7.20 A; H=1-150.
DR PDB; 5IY7; EM; 8.60 A; H=1-150.
DR PDB; 5IY8; EM; 7.90 A; H=1-150.
DR PDB; 5IY9; EM; 6.30 A; H=1-150.
DR PDB; 5IYA; EM; 5.40 A; H=1-150.
DR PDB; 5IYB; EM; 3.90 A; H=1-150.
DR PDB; 5IYC; EM; 3.90 A; H=1-150.
DR PDB; 5IYD; EM; 3.90 A; H=1-150.
DR PDB; 6DRD; EM; 3.90 A; H=1-150.
DR PDB; 6O9L; EM; 7.20 A; H=1-150.
DR PDB; 6XRE; EM; 4.60 A; H=1-150.
DR PDB; 7A6H; EM; 3.30 A; H=1-150.
DR PDB; 7AE1; EM; 2.80 A; H=1-150.
DR PDB; 7AE3; EM; 3.10 A; H=1-150.
DR PDB; 7AEA; EM; 3.40 A; H=1-150.
DR PDB; 7AST; EM; 4.00 A; D=1-150.
DR PDB; 7D58; EM; 2.90 A; H=1-150.
DR PDB; 7D59; EM; 3.10 A; H=1-150.
DR PDB; 7DN3; EM; 3.50 A; H=1-150.
DR PDB; 7DU2; EM; 3.35 A; H=1-150.
DR PDB; 7FJI; EM; 3.60 A; H=1-150.
DR PDB; 7FJJ; EM; 3.60 A; H=1-150.
DR PDB; 7LBM; EM; 4.80 A; H=1-150.
DR PDB; 7OB9; EM; 2.70 A; H=1-150.
DR PDB; 7OBA; EM; 3.10 A; H=1-150.
DR PDB; 7OBB; EM; 3.30 A; H=1-150.
DR PDB; 7VBA; EM; 2.89 A; H=1-150.
DR PDB; 7VBB; EM; 2.81 A; H=1-150.
DR PDB; 7VBC; EM; 3.01 A; H=1-150.
DR PDBsum; 2F3I; -.
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; P52434; -.
DR BMRB; P52434; -.
DR SMR; P52434; -.
DR BioGRID; 111433; 150.
DR CORUM; P52434; -.
DR DIP; DIP-27556N; -.
DR IntAct; P52434; 44.
DR MINT; P52434; -.
DR STRING; 9606.ENSP00000415536; -.
DR iPTMnet; P52434; -.
DR MetOSite; P52434; -.
DR PhosphoSitePlus; P52434; -.
DR BioMuta; POLR2H; -.
DR DMDM; 20178325; -.
DR EPD; P52434; -.
DR jPOST; P52434; -.
DR MassIVE; P52434; -.
DR MaxQB; P52434; -.
DR PaxDb; P52434; -.
DR PeptideAtlas; P52434; -.
DR PRIDE; P52434; -.
DR ProteomicsDB; 11707; -.
DR ProteomicsDB; 56485; -. [P52434-1]
DR ProteomicsDB; 8418; -.
DR ProteomicsDB; 9473; -.
DR ProteomicsDB; 9641; -.
DR TopDownProteomics; P52434-1; -. [P52434-1]
DR Antibodypedia; 33820; 277 antibodies from 30 providers.
DR DNASU; 5437; -.
DR Ensembl; ENST00000429568.1; ENSP00000415536.1; ENSG00000163882.10. [P52434-4]
DR Ensembl; ENST00000430783.5; ENSP00000411883.1; ENSG00000163882.10. [P52434-2]
DR Ensembl; ENST00000438240.5; ENSP00000398622.1; ENSG00000163882.10. [P52434-3]
DR Ensembl; ENST00000443489.5; ENSP00000393773.1; ENSG00000163882.10. [P52434-5]
DR Ensembl; ENST00000452961.5; ENSP00000399882.1; ENSG00000163882.10. [P52434-3]
DR Ensembl; ENST00000456318.6; ENSP00000392913.1; ENSG00000163882.10. [P52434-1]
DR GeneID; 5437; -.
DR KEGG; hsa:5437; -.
DR MANE-Select; ENST00000456318.6; ENSP00000392913.1; NM_006232.5; NP_006223.2.
DR UCSC; uc032smc.2; human. [P52434-1]
DR CTD; 5437; -.
DR GeneCards; POLR2H; -.
DR HGNC; HGNC:9195; POLR2H.
DR HPA; ENSG00000163882; Low tissue specificity.
DR MIM; 606023; gene.
DR neXtProt; NX_P52434; -.
DR OpenTargets; ENSG00000163882; -.
DR PharmGKB; PA33515; -.
DR VEuPathDB; HostDB:ENSG00000163882; -.
DR eggNOG; KOG3400; Eukaryota.
DR GeneTree; ENSGT00390000018195; -.
DR HOGENOM; CLU_103864_1_1_1; -.
DR InParanoid; P52434; -.
DR OMA; TINAYVS; -.
DR OrthoDB; 1504067at2759; -.
DR PhylomeDB; P52434; -.
DR TreeFam; TF103043; -.
DR PathwayCommons; P52434; -.
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; P52434; -.
DR SIGNOR; P52434; -.
DR BioGRID-ORCS; 5437; 786 hits in 1081 CRISPR screens.
DR ChiTaRS; POLR2H; human.
DR EvolutionaryTrace; P52434; -.
DR GeneWiki; POLR2H; -.
DR GenomeRNAi; 5437; -.
DR Pharos; P52434; Tbio.
DR PRO; PR:P52434; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P52434; protein.
DR Bgee; ENSG00000163882; Expressed in mucosa of transverse colon and 201 other tissues.
DR ExpressionAtlas; P52434; baseline and differential.
DR Genevisible; P52434; 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:0032993; C:protein-DNA complex; IDA:CAFA.
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:0003697; F:single-stranded DNA binding; IDA:CAFA.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR005570; RNA_pol_Rpb8.
DR PANTHER; PTHR10917; PTHR10917; 1.
DR Pfam; PF03870; RNA_pol_Rpb8; 1.
DR PIRSF; PIRSF000779; RNA_pol_Rpb8; 1.
DR SMART; SM00658; RPOL8c; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW DNA-binding; DNA-directed RNA polymerase; Nucleus; Reference proteome;
KW Transcription.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..150
FT /note="DNA-directed RNA polymerases I, II, and III subunit
FT RPABC3"
FT /id="PRO_0000073997"
FT REGION 16..40
FT /note="Non-specific ssDNA binding"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_055017"
FT VAR_SEQ 84..112
FT /note="RADQFEYVMYGKVYRIEGDETSTEAATRL -> S (in isoform 2 and
FT isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_055018"
FT VAR_SEQ 113..150
FT /note="SAYVSYGGLLMRLQGDANNLHGFEVDSRVYLLMKKLAF -> LRLRAAEWQC
FT SRITGWGLLFQLCVRVLWGPAHEAAGGCQQPAWIRGGLQSLSPDEEASLLNLA (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_055019"
FT CONFLICT 19
FT /note="G -> A (in Ref. 1; AAA91458)"
FT /evidence="ECO:0000305"
FT STRAND 4..15
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2F3I"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:7D59"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2F3I"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2F3I"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:7OB9"
SQ SEQUENCE 150 AA; 17143 MW; 944D0860809F1425 CRC64;
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV DLGDKFRLVI
ASTLYEDGTL DDGEYNPTDD RPSRADQFEY VMYGKVYRIE GDETSTEAAT RLSAYVSYGG
LLMRLQGDAN NLHGFEVDSR VYLLMKKLAF
