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Protein

DNA-directed RNA polymerase II subunit RPB7

Gene

POLR2G

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB7 is part of a subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA (By similarity). Binds RNA.By similarity1 Publication

GO - Molecular functioni

  1. DNA-directed RNA polymerase activity Source: UniProtKB-KW
  2. single-stranded DNA binding Source: GO_Central
  3. single-stranded RNA binding Source: GO_Central
  4. translation initiation factor binding Source: GO_Central

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: Reactome
  2. apoptotic process Source: Ensembl
  3. DNA repair Source: Reactome
  4. gene expression Source: Reactome
  5. mRNA splicing, via spliceosome Source: Reactome
  6. nuclear-transcribed mRNA catabolic process, exonucleolytic Source: GO_Central
  7. nucleotide-excision repair Source: Reactome
  8. positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: GO_Central
  9. positive regulation of translational initiation Source: GO_Central
  10. positive regulation of viral transcription Source: Reactome
  11. RNA splicing Source: Reactome
  12. transcription-coupled nucleotide-excision repair Source: Reactome
  13. transcription elongation from RNA polymerase II promoter Source: Reactome
  14. transcription from RNA polymerase II promoter Source: UniProtKB
  15. transcription initiation from RNA polymerase II promoter Source: GO_Central
  16. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transcription

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_12417. MicroRNA (miRNA) biogenesis.
REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1470. mRNA Capping.
REACT_1628. Transcription-coupled NER (TC-NER).
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_467. mRNA Splicing - Major Pathway.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6259. HIV elongation arrest and recovery.
REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase II subunit RPB7
Short name:
RNA polymerase II subunit B7
Alternative name(s):
DNA-directed RNA polymerase II subunit G
RNA polymerase II 19 kDa subunit
Short name:
RPB19
Gene namesi
Name:POLR2G
Synonyms:RPB7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9194. POLR2G.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: GO_Central
  2. DNA-directed RNA polymerase II, core complex Source: UniProtKB
  3. nucleolus Source: HPA
  4. nucleoplasm Source: HPA
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141H → E: Strongly reduces RNA-binding. 1 Publication
Mutagenesisi33 – 331E → K: Strongly reduces RNA-binding. 1 Publication
Mutagenesisi41 – 411K → E: Strongly reduces RNA-binding. 1 Publication
Mutagenesisi90 – 901T → A: Reduces RNA-binding. 1 Publication
Mutagenesisi93 – 931N → A: Reduces RNA-binding. 1 Publication
Mutagenesisi94 – 941K → E: Reduces RNA-binding. 1 Publication
Mutagenesisi107 – 1071F → E: Reduces RNA-binding. 1 Publication
Mutagenesisi109 – 1091S → A: Strongly reduces RNA-binding. 1 Publication
Mutagenesisi111 – 1111H → E: Strongly reduces RNA-binding. 1 Publication
Mutagenesisi151 – 1511R → E: Strongly reduces RNA-binding. 1 Publication
Mutagenesisi153 – 1531D → E: Strongly reduces RNA-binding. 1 Publication
Mutagenesisi158 – 1581F → A: Strongly reduces RNA-binding. 1 Publication

Organism-specific databases

PharmGKBiPA33514.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 172172DNA-directed RNA polymerase II subunit RPB7PRO_0000073986Add
BLAST

Proteomic databases

MaxQBiP62487.
PaxDbiP62487.
PeptideAtlasiP62487.
PRIDEiP62487.

PTM databases

PhosphoSiteiP62487.

Expressioni

Gene expression databases

BgeeiP62487.
CleanExiHS_POLR2G.
ExpressionAtlasiP62487. baseline and differential.
GenevestigatoriP62487.

Organism-specific databases

HPAiHPA053000.

Interactioni

Subunit structurei

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. RPB4 and RPB7 form a subcomplex that protrudes from the 10-subunit Pol II core complex.1 Publication

Protein-protein interaction databases

BioGridi111432. 62 interactions.
DIPiDIP-32663N.
IntActiP62487. 20 interactions.
MINTiMINT-1033626.
STRINGi9606.ENSP00000301788.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1312Combined sources
Helixi15 – 173Combined sources
Helixi22 – 3413Combined sources
Turni40 – 423Combined sources
Beta strandi43 – 5412Combined sources
Beta strandi64 – 7714Combined sources
Beta strandi84 – 9310Combined sources
Beta strandi96 – 1016Combined sources
Beta strandi104 – 1096Combined sources
Helixi110 – 1123Combined sources
Beta strandi117 – 1259Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi135 – 1384Combined sources
Beta strandi142 – 15312Combined sources
Beta strandi156 – 1627Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C35X-ray2.70B/D/F/H1-172[»]
ProteinModelPortaliP62487.
SMRiP62487. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62487.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1095.
GeneTreeiENSGT00390000008975.
HOGENOMiHOG000158201.
HOVERGENiHBG055233.
InParanoidiP62487.
KOiK03015.
OMAiKEDHLGV.
OrthoDBiEOG76MK9S.
PhylomeDBiP62487.
TreeFamiTF103042.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.1490.120. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR005576. RNA_pol_Rpb7_N.
IPR022967. S1_dom.
[Graphical view]
PfamiPF00575. S1. 1 hit.
PF03876. SHS2_Rpb7-N. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF88798. SSF88798. 1 hit.

Sequencei

Sequence statusi: Complete.

P62487-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT
60 70 80 90 100
IDNIGAGVIQ PGRGFVLYPV KYKAIVFRPF KGEVVDAVVT QVNKVGLFTE
110 120 130 140 150
IGPMSCFISR HSIPSEMEFD PNSNPPCYKT MDEDIVIQQD DEIRLKIVGT
160 170
RVDKNDIFAI GSLMDDYLGL VS
Length:172
Mass (Da):19,294
Last modified:July 19, 2004 - v1
Checksum:iAF3CE655F658CD5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20659 mRNA. Translation: AAA86500.1.
U52427 Genomic DNA. Translation: AAB96827.1.
AK312131 mRNA. Translation: BAG35067.1.
CH471076 Genomic DNA. Translation: EAW74092.1.
BC112162 mRNA. Translation: AAI12163.1.
BC112164 mRNA. Translation: AAI12165.1.
CCDSiCCDS31585.1.
RefSeqiNP_002687.1. NM_002696.2.
UniGeneiHs.14839.

Genome annotation databases

EnsembliENST00000301788; ENSP00000301788; ENSG00000168002.
GeneIDi5436.
KEGGihsa:5436.
UCSCiuc001nva.3. human.

Polymorphism databases

DMDMi50403601.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20659 mRNA. Translation: AAA86500.1.
U52427 Genomic DNA. Translation: AAB96827.1.
AK312131 mRNA. Translation: BAG35067.1.
CH471076 Genomic DNA. Translation: EAW74092.1.
BC112162 mRNA. Translation: AAI12163.1.
BC112164 mRNA. Translation: AAI12165.1.
CCDSiCCDS31585.1.
RefSeqiNP_002687.1. NM_002696.2.
UniGeneiHs.14839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C35X-ray2.70B/D/F/H1-172[»]
ProteinModelPortaliP62487.
SMRiP62487. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111432. 62 interactions.
DIPiDIP-32663N.
IntActiP62487. 20 interactions.
MINTiMINT-1033626.
STRINGi9606.ENSP00000301788.

PTM databases

PhosphoSiteiP62487.

Polymorphism databases

DMDMi50403601.

Proteomic databases

MaxQBiP62487.
PaxDbiP62487.
PeptideAtlasiP62487.
PRIDEiP62487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301788; ENSP00000301788; ENSG00000168002.
GeneIDi5436.
KEGGihsa:5436.
UCSCiuc001nva.3. human.

Organism-specific databases

CTDi5436.
GeneCardsiGC11P062529.
HGNCiHGNC:9194. POLR2G.
HPAiHPA053000.
MIMi602013. gene.
neXtProtiNX_P62487.
PharmGKBiPA33514.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1095.
GeneTreeiENSGT00390000008975.
HOGENOMiHOG000158201.
HOVERGENiHBG055233.
InParanoidiP62487.
KOiK03015.
OMAiKEDHLGV.
OrthoDBiEOG76MK9S.
PhylomeDBiP62487.
TreeFamiTF103042.

Enzyme and pathway databases

ReactomeiREACT_12417. MicroRNA (miRNA) biogenesis.
REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1470. mRNA Capping.
REACT_1628. Transcription-coupled NER (TC-NER).
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_467. mRNA Splicing - Major Pathway.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6259. HIV elongation arrest and recovery.
REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

ChiTaRSiPOLR2G. human.
EvolutionaryTraceiP62487.
GeneWikiiPOLR2G.
GenomeRNAii5436.
NextBioi21033.
PROiP62487.
SOURCEiSearch...

Gene expression databases

BgeeiP62487.
CleanExiHS_POLR2G.
ExpressionAtlasiP62487. baseline and differential.
GenevestigatoriP62487.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.1490.120. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR005576. RNA_pol_Rpb7_N.
IPR022967. S1_dom.
[Graphical view]
PfamiPF00575. S1. 1 hit.
PF03876. SHS2_Rpb7-N. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF88798. SSF88798. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human RNA polymerase II subunit hsRPB7 functions in yeast and influences stress survival and cell morphology."
    Khazak V., Sadhale P.P., Woychik N.A., Brent R., Golemis E.A.
    Mol. Biol. Cell 6:759-775(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human gene for the RNA polymerase II seventh subunit (hsRPB7): structure, expression and chromosomal localization."
    Schoen T.J., Chandrasekharappa S.C., Guru S.C., Mazuruk K., Chader G.J., Rodriguez I.R.
    Biochim. Biophys. Acta 1353:39-49(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
    Kershnar E., Wu S.-Y., Chiang C.-M.
    J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, SUBCELLULAR LOCATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human RNA polymerase II."
    Meka H., Werner F., Cordell S.C., Onesti S., Brick P.
    Nucleic Acids Res. 33:6435-6444(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF THE POL II RPB4-RPB7 SUBCOMPLEX, RNA-BINDING, MUTAGENESIS OF HIS-14; GLU-33; LYS-41; THR-90; ASN-93; LYS-94; PHE-107; SER-109; HIS-111; ARG-151; ASP-153 AND PHE-158.

Entry informationi

Entry nameiRPB7_HUMAN
AccessioniPrimary (citable) accession number: P62487
Secondary accession number(s): B2R5C0, P52433, Q2M1Z4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: February 4, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.