Full text data of POLR2G
POLR2G
(RPB7)
[Confidence: low (only semi-automatic identification from reviews)]
DNA-directed RNA polymerase II subunit RPB7; RNA polymerase II subunit B7 (DNA-directed RNA polymerase II subunit G; RNA polymerase II 19 kDa subunit; RPB19)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DNA-directed RNA polymerase II subunit RPB7; RNA polymerase II subunit B7 (DNA-directed RNA polymerase II subunit G; RNA polymerase II 19 kDa subunit; RPB19)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62487
ID RPB7_HUMAN Reviewed; 172 AA.
AC P62487; B2R5C0; P52433; Q2M1Z4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB7;
DE Short=RNA polymerase II subunit B7;
DE AltName: Full=DNA-directed RNA polymerase II subunit G;
DE AltName: Full=RNA polymerase II 19 kDa subunit;
DE Short=RPB19;
GN Name=POLR2G; Synonyms=RPB7;
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=7579693; DOI=10.1091/mbc.6.7.759;
RA Khazak V., Sadhale P.P., Woychik N.A., Brent R., Golemis E.A.;
RT "Human RNA polymerase II subunit hsRPB7 functions in yeast and
RT influences stress survival and cell morphology.";
RL Mol. Biol. Cell 6:759-775(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9256063; DOI=10.1016/S0167-4781(97)00041-9;
RA Schoen T.J., Chandrasekharappa S.C., Guru S.C., Mazuruk K.,
RA Chader G.J., Rodriguez I.R.;
RT "Human gene for the RNA polymerase II seventh subunit (hsRPB7):
RT structure, expression and chromosomal localization.";
RL Biochim. Biophys. Acta 1353:39-49(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [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 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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF THE POL II RPB4-RPB7
RP SUBCOMPLEX, RNA-BINDING, AND MUTAGENESIS OF HIS-14; GLU-33; LYS-41;
RP THR-90; ASN-93; LYS-94; PHE-107; SER-109; HIS-111; ARG-151; ASP-153
RP AND PHE-158.
RX PubMed=16282592; DOI=10.1093/nar/gki945;
RA Meka H., Werner F., Cordell S.C., Onesti S., Brick P.;
RT "Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human
RT RNA polymerase II.";
RL Nucleic Acids Res. 33:6435-6444(2005).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC of DNA into RNA using the four ribonucleoside triphosphates as
CC substrates. Component of RNA polymerase II which synthesizes mRNA
CC precursors and many functional non-coding RNAs. Pol II is the
CC central component of the basal RNA polymerase II transcription
CC machinery. It is composed of mobile elements that move relative to
CC each other. RPB7 is part of a subcomplex with RPB4 that binds to a
CC pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp
CC element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7
CC in the closed conformation thus preventing double-stranded DNA to
CC enter the active site cleft. The RPB4-RPB7 subcomplex binds
CC single-stranded DNA and RNA (By similarity). Binds RNA.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex
CC consisting of 12 subunits. RPB4 and RPB7 form a subcomplex that
CC protrudes from the 10-subunit Pol II core complex.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase
CC subunit 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; U20659; AAA86500.1; -; mRNA.
DR EMBL; U52427; AAB96827.1; -; Genomic_DNA.
DR EMBL; AK312131; BAG35067.1; -; mRNA.
DR EMBL; CH471076; EAW74092.1; -; Genomic_DNA.
DR EMBL; BC112162; AAI12163.1; -; mRNA.
DR EMBL; BC112164; AAI12165.1; -; mRNA.
DR RefSeq; NP_002687.1; NM_002696.2.
DR UniGene; Hs.14839; -.
DR PDB; 2C35; X-ray; 2.70 A; B/D/F/H=1-172.
DR PDBsum; 2C35; -.
DR ProteinModelPortal; P62487; -.
DR SMR; P62487; 1-171.
DR DIP; DIP-32663N; -.
DR IntAct; P62487; 20.
DR MINT; MINT-1033626; -.
DR STRING; 9606.ENSP00000301788; -.
DR PhosphoSite; P62487; -.
DR DMDM; 50403601; -.
DR PaxDb; P62487; -.
DR PeptideAtlas; P62487; -.
DR PRIDE; P62487; -.
DR Ensembl; ENST00000301788; ENSP00000301788; ENSG00000168002.
DR GeneID; 5436; -.
DR KEGG; hsa:5436; -.
DR UCSC; uc001nva.3; human.
DR CTD; 5436; -.
DR GeneCards; GC11P062529; -.
DR HGNC; HGNC:9194; POLR2G.
DR HPA; HPA053000; -.
DR MIM; 602013; gene.
DR neXtProt; NX_P62487; -.
DR PharmGKB; PA33514; -.
DR eggNOG; COG1095; -.
DR HOGENOM; HOG000158201; -.
DR HOVERGEN; HBG055233; -.
DR InParanoid; P62487; -.
DR KO; K03015; -.
DR OMA; KEDHLGV; -.
DR OrthoDB; EOG76MK9S; -.
DR PhylomeDB; P62487; -.
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_71; Gene Expression.
DR EvolutionaryTrace; P62487; -.
DR GeneWiki; POLR2G; -.
DR GenomeRNAi; 5436; -.
DR NextBio; 21033; -.
DR PRO; PR:P62487; -.
DR ArrayExpress; P62487; -.
DR Bgee; P62487; -.
DR CleanEx; HS_POLR2G; -.
DR Genevestigator; P62487; -.
DR GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II 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 Gene3D; 3.30.1490.120; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR InterPro; IPR022967; RNA-binding_domain_S1.
DR InterPro; IPR005576; RNA_pol_Rpb7_N.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF88798; SSF88798; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; DNA-directed RNA polymerase; Nucleus;
KW Reference proteome; RNA-binding; Transcription.
FT CHAIN 1 172 DNA-directed RNA polymerase II subunit
FT RPB7.
FT /FTId=PRO_0000073986.
FT MUTAGEN 14 14 H->E: Strongly reduces RNA-binding.
FT MUTAGEN 33 33 E->K: Strongly reduces RNA-binding.
FT MUTAGEN 41 41 K->E: Strongly reduces RNA-binding.
FT MUTAGEN 90 90 T->A: Reduces RNA-binding.
FT MUTAGEN 93 93 N->A: Reduces RNA-binding.
FT MUTAGEN 94 94 K->E: Reduces RNA-binding.
FT MUTAGEN 107 107 F->E: Reduces RNA-binding.
FT MUTAGEN 109 109 S->A: Strongly reduces RNA-binding.
FT MUTAGEN 111 111 H->E: Strongly reduces RNA-binding.
FT MUTAGEN 151 151 R->E: Strongly reduces RNA-binding.
FT MUTAGEN 153 153 D->E: Strongly reduces RNA-binding.
FT MUTAGEN 158 158 F->A: Strongly reduces RNA-binding.
FT STRAND 2 13
FT HELIX 15 17
FT HELIX 22 34
FT TURN 40 42
FT STRAND 43 54
FT STRAND 64 77
FT STRAND 84 93
FT STRAND 96 101
FT STRAND 104 109
FT HELIX 110 112
FT STRAND 117 125
FT STRAND 127 130
FT STRAND 135 138
FT STRAND 142 153
FT STRAND 156 162
SQ SEQUENCE 172 AA; 19294 MW; AF3CE655F658CD5C CRC64;
MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT IDNIGAGVIQ
PGRGFVLYPV KYKAIVFRPF KGEVVDAVVT QVNKVGLFTE IGPMSCFISR HSIPSEMEFD
PNSNPPCYKT MDEDIVIQQD DEIRLKIVGT RVDKNDIFAI GSLMDDYLGL VS
//
ID RPB7_HUMAN Reviewed; 172 AA.
AC P62487; B2R5C0; P52433; Q2M1Z4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB7;
DE Short=RNA polymerase II subunit B7;
DE AltName: Full=DNA-directed RNA polymerase II subunit G;
DE AltName: Full=RNA polymerase II 19 kDa subunit;
DE Short=RPB19;
GN Name=POLR2G; Synonyms=RPB7;
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=7579693; DOI=10.1091/mbc.6.7.759;
RA Khazak V., Sadhale P.P., Woychik N.A., Brent R., Golemis E.A.;
RT "Human RNA polymerase II subunit hsRPB7 functions in yeast and
RT influences stress survival and cell morphology.";
RL Mol. Biol. Cell 6:759-775(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9256063; DOI=10.1016/S0167-4781(97)00041-9;
RA Schoen T.J., Chandrasekharappa S.C., Guru S.C., Mazuruk K.,
RA Chader G.J., Rodriguez I.R.;
RT "Human gene for the RNA polymerase II seventh subunit (hsRPB7):
RT structure, expression and chromosomal localization.";
RL Biochim. Biophys. Acta 1353:39-49(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [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 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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF THE POL II RPB4-RPB7
RP SUBCOMPLEX, RNA-BINDING, AND MUTAGENESIS OF HIS-14; GLU-33; LYS-41;
RP THR-90; ASN-93; LYS-94; PHE-107; SER-109; HIS-111; ARG-151; ASP-153
RP AND PHE-158.
RX PubMed=16282592; DOI=10.1093/nar/gki945;
RA Meka H., Werner F., Cordell S.C., Onesti S., Brick P.;
RT "Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human
RT RNA polymerase II.";
RL Nucleic Acids Res. 33:6435-6444(2005).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC of DNA into RNA using the four ribonucleoside triphosphates as
CC substrates. Component of RNA polymerase II which synthesizes mRNA
CC precursors and many functional non-coding RNAs. Pol II is the
CC central component of the basal RNA polymerase II transcription
CC machinery. It is composed of mobile elements that move relative to
CC each other. RPB7 is part of a subcomplex with RPB4 that binds to a
CC pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp
CC element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7
CC in the closed conformation thus preventing double-stranded DNA to
CC enter the active site cleft. The RPB4-RPB7 subcomplex binds
CC single-stranded DNA and RNA (By similarity). Binds RNA.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex
CC consisting of 12 subunits. RPB4 and RPB7 form a subcomplex that
CC protrudes from the 10-subunit Pol II core complex.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase
CC subunit 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; U20659; AAA86500.1; -; mRNA.
DR EMBL; U52427; AAB96827.1; -; Genomic_DNA.
DR EMBL; AK312131; BAG35067.1; -; mRNA.
DR EMBL; CH471076; EAW74092.1; -; Genomic_DNA.
DR EMBL; BC112162; AAI12163.1; -; mRNA.
DR EMBL; BC112164; AAI12165.1; -; mRNA.
DR RefSeq; NP_002687.1; NM_002696.2.
DR UniGene; Hs.14839; -.
DR PDB; 2C35; X-ray; 2.70 A; B/D/F/H=1-172.
DR PDBsum; 2C35; -.
DR ProteinModelPortal; P62487; -.
DR SMR; P62487; 1-171.
DR DIP; DIP-32663N; -.
DR IntAct; P62487; 20.
DR MINT; MINT-1033626; -.
DR STRING; 9606.ENSP00000301788; -.
DR PhosphoSite; P62487; -.
DR DMDM; 50403601; -.
DR PaxDb; P62487; -.
DR PeptideAtlas; P62487; -.
DR PRIDE; P62487; -.
DR Ensembl; ENST00000301788; ENSP00000301788; ENSG00000168002.
DR GeneID; 5436; -.
DR KEGG; hsa:5436; -.
DR UCSC; uc001nva.3; human.
DR CTD; 5436; -.
DR GeneCards; GC11P062529; -.
DR HGNC; HGNC:9194; POLR2G.
DR HPA; HPA053000; -.
DR MIM; 602013; gene.
DR neXtProt; NX_P62487; -.
DR PharmGKB; PA33514; -.
DR eggNOG; COG1095; -.
DR HOGENOM; HOG000158201; -.
DR HOVERGEN; HBG055233; -.
DR InParanoid; P62487; -.
DR KO; K03015; -.
DR OMA; KEDHLGV; -.
DR OrthoDB; EOG76MK9S; -.
DR PhylomeDB; P62487; -.
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_71; Gene Expression.
DR EvolutionaryTrace; P62487; -.
DR GeneWiki; POLR2G; -.
DR GenomeRNAi; 5436; -.
DR NextBio; 21033; -.
DR PRO; PR:P62487; -.
DR ArrayExpress; P62487; -.
DR Bgee; P62487; -.
DR CleanEx; HS_POLR2G; -.
DR Genevestigator; P62487; -.
DR GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II 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 Gene3D; 3.30.1490.120; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR InterPro; IPR022967; RNA-binding_domain_S1.
DR InterPro; IPR005576; RNA_pol_Rpb7_N.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF88798; SSF88798; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; DNA-directed RNA polymerase; Nucleus;
KW Reference proteome; RNA-binding; Transcription.
FT CHAIN 1 172 DNA-directed RNA polymerase II subunit
FT RPB7.
FT /FTId=PRO_0000073986.
FT MUTAGEN 14 14 H->E: Strongly reduces RNA-binding.
FT MUTAGEN 33 33 E->K: Strongly reduces RNA-binding.
FT MUTAGEN 41 41 K->E: Strongly reduces RNA-binding.
FT MUTAGEN 90 90 T->A: Reduces RNA-binding.
FT MUTAGEN 93 93 N->A: Reduces RNA-binding.
FT MUTAGEN 94 94 K->E: Reduces RNA-binding.
FT MUTAGEN 107 107 F->E: Reduces RNA-binding.
FT MUTAGEN 109 109 S->A: Strongly reduces RNA-binding.
FT MUTAGEN 111 111 H->E: Strongly reduces RNA-binding.
FT MUTAGEN 151 151 R->E: Strongly reduces RNA-binding.
FT MUTAGEN 153 153 D->E: Strongly reduces RNA-binding.
FT MUTAGEN 158 158 F->A: Strongly reduces RNA-binding.
FT STRAND 2 13
FT HELIX 15 17
FT HELIX 22 34
FT TURN 40 42
FT STRAND 43 54
FT STRAND 64 77
FT STRAND 84 93
FT STRAND 96 101
FT STRAND 104 109
FT HELIX 110 112
FT STRAND 117 125
FT STRAND 127 130
FT STRAND 135 138
FT STRAND 142 153
FT STRAND 156 162
SQ SEQUENCE 172 AA; 19294 MW; AF3CE655F658CD5C CRC64;
MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT IDNIGAGVIQ
PGRGFVLYPV KYKAIVFRPF KGEVVDAVVT QVNKVGLFTE IGPMSCFISR HSIPSEMEFD
PNSNPPCYKT MDEDIVIQQD DEIRLKIVGT RVDKNDIFAI GSLMDDYLGL VS
//
MIM
602013
*RECORD*
*FIELD* NO
602013
*FIELD* TI
*602013 POLYMERASE II, RNA, SUBUNIT G; POLR2G
;;RPB7, S. CEREVISIAE, HOMOLOG OF
*FIELD* TX
read moreRNA polymerase II is the enzymatic complex responsible for transcription
of genes that result in mRNA production. For general information on the
structure and function of RNA polymerase II, see 180660.
CLONING
Schoen et al. (1997) stated that 7 of the RNA polymerase II complex
genes had been isolated and assigned to chromosomal sites. The complete
genomic sequence had been reported for only the 220-kD (POLR2A; 180660)
and 14.5-kD (POLR2I; 180662) subunits. Schoen et al. (1997) cloned,
sequenced, and mapped the seventh subunit of the RNA polymerase II
complex, which they designated hsRPB7. Southern blots of genomic and
cloned DNA suggested that it is encoded by a single gene. The sequence
of the 5-prime flanking region did not contain a TATA element, but did
contain several Sp1-binding sites, an AP-1 site, and a novel inverted
polymorphic GATA tandem repeat. Schoen et al. (1997) stated that this
novel GATA repeat should be useful for linkage analysis. The gene seemed
to be highly conserved among eukaryotic species, showing general
sequence conservation with yeast and Drosophila. Northern blot analysis
revealed a high degree of tissue-specific expression. Expression was
relatively high in adult retina, brain, and kidney.
GENE STRUCTURE
The POLR2G gene consists of 8 exons and spans approximately 5.1 kb
(Schoen et al., 1997).
GENE FUNCTION
Khazak et al. (1998) demonstrated that POLR2D (606017) associates
strongly and specifically with POLR2G in the nuclei of human cells. The
association appeared to require sequences spanning the N-terminal half
of the POLR2D protein, whereas no truncation of POLR2G was observed to
associate with POLR2D.
MAPPING
Using human radiation hybrids and YACs, Schoen et al. (1997) localized
the POLR2G gene to 11q13.1, within 70 kb of marker D11S1765.
*FIELD* RF
1. Khazak, V.; Estojak, J.; Cho, H.; Majors, J.; Sonoda, G.; Testa,
J. R.; Golemis, E. A.: Analysis of the interaction of the novel RNA
polymerase II (pol II) subunit hsRPB4 with its partner hsRPB7 and
with pol II. Molec. Cell. Biol. 18: 1935-1945, 1998.
2. Schoen, T. J.; Chandrasekharappa, S. C.; Guru, S. C.; Mazuruk,
K.; Chader, G. J.; Rodriguez, I. R.: Human gene for the RNA polymerase
II seventh subunit (hsRPB7): structure, expression and chromosomal
localization. Biochim. Biophys. Acta 1353: 39-49, 1997.
*FIELD* CN
Carol A. Bocchini - updated: 6/15/2001
*FIELD* CD
Victor A. McKusick: 9/23/1997
*FIELD* ED
alopez: 06/19/2001
mgross: 6/19/2001
carol: 6/15/2001
psherman: 9/2/1999
mark: 9/24/1997
mark: 9/23/1997
*RECORD*
*FIELD* NO
602013
*FIELD* TI
*602013 POLYMERASE II, RNA, SUBUNIT G; POLR2G
;;RPB7, S. CEREVISIAE, HOMOLOG OF
*FIELD* TX
read moreRNA polymerase II is the enzymatic complex responsible for transcription
of genes that result in mRNA production. For general information on the
structure and function of RNA polymerase II, see 180660.
CLONING
Schoen et al. (1997) stated that 7 of the RNA polymerase II complex
genes had been isolated and assigned to chromosomal sites. The complete
genomic sequence had been reported for only the 220-kD (POLR2A; 180660)
and 14.5-kD (POLR2I; 180662) subunits. Schoen et al. (1997) cloned,
sequenced, and mapped the seventh subunit of the RNA polymerase II
complex, which they designated hsRPB7. Southern blots of genomic and
cloned DNA suggested that it is encoded by a single gene. The sequence
of the 5-prime flanking region did not contain a TATA element, but did
contain several Sp1-binding sites, an AP-1 site, and a novel inverted
polymorphic GATA tandem repeat. Schoen et al. (1997) stated that this
novel GATA repeat should be useful for linkage analysis. The gene seemed
to be highly conserved among eukaryotic species, showing general
sequence conservation with yeast and Drosophila. Northern blot analysis
revealed a high degree of tissue-specific expression. Expression was
relatively high in adult retina, brain, and kidney.
GENE STRUCTURE
The POLR2G gene consists of 8 exons and spans approximately 5.1 kb
(Schoen et al., 1997).
GENE FUNCTION
Khazak et al. (1998) demonstrated that POLR2D (606017) associates
strongly and specifically with POLR2G in the nuclei of human cells. The
association appeared to require sequences spanning the N-terminal half
of the POLR2D protein, whereas no truncation of POLR2G was observed to
associate with POLR2D.
MAPPING
Using human radiation hybrids and YACs, Schoen et al. (1997) localized
the POLR2G gene to 11q13.1, within 70 kb of marker D11S1765.
*FIELD* RF
1. Khazak, V.; Estojak, J.; Cho, H.; Majors, J.; Sonoda, G.; Testa,
J. R.; Golemis, E. A.: Analysis of the interaction of the novel RNA
polymerase II (pol II) subunit hsRPB4 with its partner hsRPB7 and
with pol II. Molec. Cell. Biol. 18: 1935-1945, 1998.
2. Schoen, T. J.; Chandrasekharappa, S. C.; Guru, S. C.; Mazuruk,
K.; Chader, G. J.; Rodriguez, I. R.: Human gene for the RNA polymerase
II seventh subunit (hsRPB7): structure, expression and chromosomal
localization. Biochim. Biophys. Acta 1353: 39-49, 1997.
*FIELD* CN
Carol A. Bocchini - updated: 6/15/2001
*FIELD* CD
Victor A. McKusick: 9/23/1997
*FIELD* ED
alopez: 06/19/2001
mgross: 6/19/2001
carol: 6/15/2001
psherman: 9/2/1999
mark: 9/24/1997
mark: 9/23/1997