Full text data of POLR2H
POLR2H
[Confidence: low (only semi-automatic identification from reviews)]
DNA-directed RNA polymerases I, II, and III subunit RPABC3; RNA polymerases I, II, and III subunit ABC3 (DNA-directed RNA polymerase II subunit H; DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide; RPB17; RPB8 homolog; hRPB8)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DNA-directed RNA polymerases I, II, and III subunit RPABC3; RNA polymerases I, II, and III subunit ABC3 (DNA-directed RNA polymerase II subunit H; DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide; RPB17; RPB8 homolog; hRPB8)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P52434
ID RPAB3_HUMAN Reviewed; 150 AA.
AC P52434; P53802; Q969R0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 140.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8524256;
RA McKune K., Moore P.A., Hull M.W., Woychik N.A.;
RT "Six human RNA polymerase subunits functionally substitute for their
RT yeast counterparts.";
RL Mol. Cell. Biol. 15:6895-6900(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7651387;
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
RT are functionally interchangeable between Homo sapiens and
RT Saccharomyces 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.,
RA Vigneron M., Kedinger C.;
RT "Organization of genes encoding subunits of eucaryotic nuclear RNA
RT polymerases shows non random intron distribution and correlates with
RT the subunit modular structure.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-13 AND 99-111, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) to UniProtKB.
RN [6]
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
RT that conditionally express epitope-tagged subunits of the multiprotein
RT complexes.";
RL J. Biol. Chem. 273:34444-34453(1998).
RN [7]
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
RT activation of transcription by upstream binding factor.";
RL Mol. Cell. Biol. 26:5436-5448(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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.,
RA Buerckstuemmer T., 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP STRUCTURE BY NMR, DNA-BINDING REGION, SUBUNIT, AND INTERACTION WITH
RP 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
CC of DNA into RNA using the four ribonucleoside triphosphates as
CC substrates. Common component of RNA polymerases I, II and III
CC which synthesize ribosomal RNA precursors, mRNA precursors and
CC many functional non-coding RNAs, and small RNAs, such as 5S rRNA
CC and tRNAs, respectively.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase
CC II (Pol II) and RNA polymerase III (Pol III) complexes consisting
CC of at least 13, 12 and 17 subunits, respectively. Directly
CC interacts with POLR2A.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB8 RNA polymerase subunit
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; BC000739; AAH00739.1; -; mRNA.
DR PIR; S55370; S55370.
DR RefSeq; NP_001265627.1; NM_001278698.1.
DR RefSeq; NP_001265628.1; NM_001278699.1.
DR RefSeq; NP_001265629.1; NM_001278700.1.
DR RefSeq; NP_001265644.1; NM_001278715.1.
DR RefSeq; NP_006223.2; NM_006232.3.
DR UniGene; Hs.432574; -.
DR PDB; 2F3I; NMR; -; A=1-150.
DR PDBsum; 2F3I; -.
DR DisProt; DP00504; -.
DR ProteinModelPortal; P52434; -.
DR SMR; P52434; 1-150.
DR DIP; DIP-27556N; -.
DR IntAct; P52434; 8.
DR MINT; MINT-1162805; -.
DR STRING; 9606.ENSP00000296223; -.
DR PhosphoSite; P52434; -.
DR DMDM; 20178325; -.
DR PaxDb; P52434; -.
DR PeptideAtlas; P52434; -.
DR PRIDE; P52434; -.
DR DNASU; 5437; -.
DR Ensembl; ENST00000296223; ENSP00000296223; ENSG00000163882.
DR Ensembl; ENST00000456318; ENSP00000392913; ENSG00000163882.
DR GeneID; 5437; -.
DR KEGG; hsa:5437; -.
DR UCSC; uc003fok.2; human.
DR CTD; 5437; -.
DR GeneCards; GC03P184079; -.
DR HGNC; HGNC:9195; POLR2H.
DR HPA; HPA037745; -.
DR MIM; 606023; gene.
DR neXtProt; NX_P52434; -.
DR PharmGKB; PA33515; -.
DR eggNOG; NOG279425; -.
DR HOGENOM; HOG000175572; -.
DR HOVERGEN; HBG036116; -.
DR InParanoid; P52434; -.
DR KO; K03016; -.
DR OrthoDB; EOG7SN8DR; -.
DR PhylomeDB; P52434; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_1892; Elongation arrest and recovery.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; POLR2H; human.
DR EvolutionaryTrace; P52434; -.
DR GeneWiki; POLR2H; -.
DR GenomeRNAi; 5437; -.
DR NextBio; 21037; -.
DR PRO; PR:P52434; -.
DR ArrayExpress; P52434; -.
DR Bgee; P52434; -.
DR CleanEx; HS_POLR2H; -.
DR Genevestigator; P52434; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005736; C:DNA-directed RNA polymerase I complex; IBA:RefGenome.
DR GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0005666; C:DNA-directed RNA polymerase III complex; IBA:RefGenome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; TAS:Reactome.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0006385; P:transcription elongation from RNA polymerase III promoter; TAS:Reactome.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
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; Complete proteome;
KW Direct protein sequencing; DNA-binding; DNA-directed RNA polymerase;
KW Nucleus; Reference proteome; Transcription.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 150 DNA-directed RNA polymerases I, II, and
FT III subunit RPABC3.
FT /FTId=PRO_0000073997.
FT REGION 16 40 Non-specific ssDNA binding.
FT MOD_RES 2 2 N-acetylalanine.
FT CONFLICT 19 19 G -> A (in Ref. 1; AAA91458).
FT STRAND 7 16
FT STRAND 25 35
FT STRAND 38 44
FT STRAND 48 50
FT STRAND 56 59
FT STRAND 66 70
FT TURN 71 73
FT STRAND 75 77
FT TURN 85 88
FT STRAND 89 92
FT STRAND 94 97
FT STRAND 104 107
FT STRAND 110 118
FT STRAND 121 127
FT HELIX 129 132
FT STRAND 142 147
SQ SEQUENCE 150 AA; 17143 MW; 944D0860809F1425 CRC64;
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV DLGDKFRLVI
ASTLYEDGTL DDGEYNPTDD RPSRADQFEY VMYGKVYRIE GDETSTEAAT RLSAYVSYGG
LLMRLQGDAN NLHGFEVDSR VYLLMKKLAF
//
ID RPAB3_HUMAN Reviewed; 150 AA.
AC P52434; P53802; Q969R0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 140.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8524256;
RA McKune K., Moore P.A., Hull M.W., Woychik N.A.;
RT "Six human RNA polymerase subunits functionally substitute for their
RT yeast counterparts.";
RL Mol. Cell. Biol. 15:6895-6900(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7651387;
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
RT are functionally interchangeable between Homo sapiens and
RT Saccharomyces 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.,
RA Vigneron M., Kedinger C.;
RT "Organization of genes encoding subunits of eucaryotic nuclear RNA
RT polymerases shows non random intron distribution and correlates with
RT the subunit modular structure.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-13 AND 99-111, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) to UniProtKB.
RN [6]
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
RT that conditionally express epitope-tagged subunits of the multiprotein
RT complexes.";
RL J. Biol. Chem. 273:34444-34453(1998).
RN [7]
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
RT activation of transcription by upstream binding factor.";
RL Mol. Cell. Biol. 26:5436-5448(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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.,
RA Buerckstuemmer T., 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP STRUCTURE BY NMR, DNA-BINDING REGION, SUBUNIT, AND INTERACTION WITH
RP 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
CC of DNA into RNA using the four ribonucleoside triphosphates as
CC substrates. Common component of RNA polymerases I, II and III
CC which synthesize ribosomal RNA precursors, mRNA precursors and
CC many functional non-coding RNAs, and small RNAs, such as 5S rRNA
CC and tRNAs, respectively.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase
CC II (Pol II) and RNA polymerase III (Pol III) complexes consisting
CC of at least 13, 12 and 17 subunits, respectively. Directly
CC interacts with POLR2A.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB8 RNA polymerase subunit
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; BC000739; AAH00739.1; -; mRNA.
DR PIR; S55370; S55370.
DR RefSeq; NP_001265627.1; NM_001278698.1.
DR RefSeq; NP_001265628.1; NM_001278699.1.
DR RefSeq; NP_001265629.1; NM_001278700.1.
DR RefSeq; NP_001265644.1; NM_001278715.1.
DR RefSeq; NP_006223.2; NM_006232.3.
DR UniGene; Hs.432574; -.
DR PDB; 2F3I; NMR; -; A=1-150.
DR PDBsum; 2F3I; -.
DR DisProt; DP00504; -.
DR ProteinModelPortal; P52434; -.
DR SMR; P52434; 1-150.
DR DIP; DIP-27556N; -.
DR IntAct; P52434; 8.
DR MINT; MINT-1162805; -.
DR STRING; 9606.ENSP00000296223; -.
DR PhosphoSite; P52434; -.
DR DMDM; 20178325; -.
DR PaxDb; P52434; -.
DR PeptideAtlas; P52434; -.
DR PRIDE; P52434; -.
DR DNASU; 5437; -.
DR Ensembl; ENST00000296223; ENSP00000296223; ENSG00000163882.
DR Ensembl; ENST00000456318; ENSP00000392913; ENSG00000163882.
DR GeneID; 5437; -.
DR KEGG; hsa:5437; -.
DR UCSC; uc003fok.2; human.
DR CTD; 5437; -.
DR GeneCards; GC03P184079; -.
DR HGNC; HGNC:9195; POLR2H.
DR HPA; HPA037745; -.
DR MIM; 606023; gene.
DR neXtProt; NX_P52434; -.
DR PharmGKB; PA33515; -.
DR eggNOG; NOG279425; -.
DR HOGENOM; HOG000175572; -.
DR HOVERGEN; HBG036116; -.
DR InParanoid; P52434; -.
DR KO; K03016; -.
DR OrthoDB; EOG7SN8DR; -.
DR PhylomeDB; P52434; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_1892; Elongation arrest and recovery.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; POLR2H; human.
DR EvolutionaryTrace; P52434; -.
DR GeneWiki; POLR2H; -.
DR GenomeRNAi; 5437; -.
DR NextBio; 21037; -.
DR PRO; PR:P52434; -.
DR ArrayExpress; P52434; -.
DR Bgee; P52434; -.
DR CleanEx; HS_POLR2H; -.
DR Genevestigator; P52434; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005736; C:DNA-directed RNA polymerase I complex; IBA:RefGenome.
DR GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0005666; C:DNA-directed RNA polymerase III complex; IBA:RefGenome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; TAS:Reactome.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0006385; P:transcription elongation from RNA polymerase III promoter; TAS:Reactome.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
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; Complete proteome;
KW Direct protein sequencing; DNA-binding; DNA-directed RNA polymerase;
KW Nucleus; Reference proteome; Transcription.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 150 DNA-directed RNA polymerases I, II, and
FT III subunit RPABC3.
FT /FTId=PRO_0000073997.
FT REGION 16 40 Non-specific ssDNA binding.
FT MOD_RES 2 2 N-acetylalanine.
FT CONFLICT 19 19 G -> A (in Ref. 1; AAA91458).
FT STRAND 7 16
FT STRAND 25 35
FT STRAND 38 44
FT STRAND 48 50
FT STRAND 56 59
FT STRAND 66 70
FT TURN 71 73
FT STRAND 75 77
FT TURN 85 88
FT STRAND 89 92
FT STRAND 94 97
FT STRAND 104 107
FT STRAND 110 118
FT STRAND 121 127
FT HELIX 129 132
FT STRAND 142 147
SQ SEQUENCE 150 AA; 17143 MW; 944D0860809F1425 CRC64;
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV DLGDKFRLVI
ASTLYEDGTL DDGEYNPTDD RPSRADQFEY VMYGKVYRIE GDETSTEAAT RLSAYVSYGG
LLMRLQGDAN NLHGFEVDSR VYLLMKKLAF
//
MIM
606023
*RECORD*
*FIELD* NO
606023
*FIELD* TI
*606023 POLYMERASE II, RNA, SUBUNIT H; POLR2H
;;RPB8, S. CEREVISIAE, HOMOLOG OF;;
RNA POLYMERASE II, 17-KD SUBUNIT
read more*FIELD* TX
The DNA-dependent RNA polymerase II (EC 2.7.7.6) is responsible for the
transcription of protein-encoding genes. It is composed of 10 to 14
subunits ranging in mass from approximately 220 kD (POLR2A; 180660) to
approximately 7 kD (POLR2K; 606033). For general information on the
structure and function of RNA polymerase II, see 180660.
CLONING
McKune et al. (1995) isolated cDNAs corresponding to the genes for
POLR2L and POLR2H, the human homologs of S. cerevisiae RPB10 and RPB8,
respectively. The POLR2H cDNA encodes a 150-amino acid protein.
GENE FUNCTION
McKune et al. (1995) showed by immunoprecipitation experiments that both
POLR2L and POLR2H are stable and assemble efficiently with yeast RNA pol
II. Yeast RPB8 and RPB10 are essential for cell growth and viability.
Shpakovski et al. (1995) showed that a human cDNA for POLR2H was able to
complement the yeast homolog.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the POLR2H
gene to chromosome 3q28 (TMAP stSG45560).
*FIELD* RF
1. McKune, K.; Moore, P. A.; Hull, M. W.; Woychik, N. A.: Six human
RNA polymerase subunits functionally substitute for their yeast counterparts. Molec.
Cell. Biol. 15: 6895-6900, 1995.
2. Shpakovski, G. V.; Acker, J.; Wintzerith, M.; Lacroix, J. F.; Thuriaux,
P.; Vigneron, M.: Four subunits that are shared by the three classes
of RNA polymerase are functionally interchangeable between Homo sapiens
and Saccharomyces cerevisiae. Molec. Cell. Biol. 15: 4702-4710,
1995.
*FIELD* CD
Carol A. Bocchini: 6/15/2001
*FIELD* ED
alopez: 06/19/2001
carol: 6/19/2001
mcapotos: 6/18/2001
carol: 6/15/2001
*RECORD*
*FIELD* NO
606023
*FIELD* TI
*606023 POLYMERASE II, RNA, SUBUNIT H; POLR2H
;;RPB8, S. CEREVISIAE, HOMOLOG OF;;
RNA POLYMERASE II, 17-KD SUBUNIT
read more*FIELD* TX
The DNA-dependent RNA polymerase II (EC 2.7.7.6) is responsible for the
transcription of protein-encoding genes. It is composed of 10 to 14
subunits ranging in mass from approximately 220 kD (POLR2A; 180660) to
approximately 7 kD (POLR2K; 606033). For general information on the
structure and function of RNA polymerase II, see 180660.
CLONING
McKune et al. (1995) isolated cDNAs corresponding to the genes for
POLR2L and POLR2H, the human homologs of S. cerevisiae RPB10 and RPB8,
respectively. The POLR2H cDNA encodes a 150-amino acid protein.
GENE FUNCTION
McKune et al. (1995) showed by immunoprecipitation experiments that both
POLR2L and POLR2H are stable and assemble efficiently with yeast RNA pol
II. Yeast RPB8 and RPB10 are essential for cell growth and viability.
Shpakovski et al. (1995) showed that a human cDNA for POLR2H was able to
complement the yeast homolog.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the POLR2H
gene to chromosome 3q28 (TMAP stSG45560).
*FIELD* RF
1. McKune, K.; Moore, P. A.; Hull, M. W.; Woychik, N. A.: Six human
RNA polymerase subunits functionally substitute for their yeast counterparts. Molec.
Cell. Biol. 15: 6895-6900, 1995.
2. Shpakovski, G. V.; Acker, J.; Wintzerith, M.; Lacroix, J. F.; Thuriaux,
P.; Vigneron, M.: Four subunits that are shared by the three classes
of RNA polymerase are functionally interchangeable between Homo sapiens
and Saccharomyces cerevisiae. Molec. Cell. Biol. 15: 4702-4710,
1995.
*FIELD* CD
Carol A. Bocchini: 6/15/2001
*FIELD* ED
alopez: 06/19/2001
carol: 6/19/2001
mcapotos: 6/18/2001
carol: 6/15/2001