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P62487 (RPB7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:POLR2G
Synonyms:RPB7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

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. Ref.6

Subcellular location

Nucleus Ref.6.

Sequence similarities

Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.

Ontologies

Keywords
   Biological processTranscription
   Cellular componentDNA-directed RNA polymerase
Nucleus
   LigandRNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

DNA repair

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

apoptotic process

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, exonucleolytic

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleotide-excision repair

Traceable author statement. Source: Reactome

positive regulation of nuclear-transcribed mRNA poly(A) tail shortening

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of translational initiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of viral transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.6. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentDNA-directed RNA polymerase II, core complex

Inferred from direct assay Ref.6. Source: UniProtKB

cytoplasmic mRNA processing body

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionDNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

single-stranded DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

single-stranded RNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

translation initiation factor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 172172DNA-directed RNA polymerase II subunit RPB7
PRO_0000073986

Experimental info

Mutagenesis141H → E: Strongly reduces RNA-binding. Ref.8
Mutagenesis331E → K: Strongly reduces RNA-binding. Ref.8
Mutagenesis411K → E: Strongly reduces RNA-binding. Ref.8
Mutagenesis901T → A: Reduces RNA-binding. Ref.8
Mutagenesis931N → A: Reduces RNA-binding. Ref.8
Mutagenesis941K → E: Reduces RNA-binding. Ref.8
Mutagenesis1071F → E: Reduces RNA-binding. Ref.8
Mutagenesis1091S → A: Strongly reduces RNA-binding. Ref.8
Mutagenesis1111H → E: Strongly reduces RNA-binding. Ref.8
Mutagenesis1511R → E: Strongly reduces RNA-binding. Ref.8
Mutagenesis1531D → E: Strongly reduces RNA-binding. Ref.8
Mutagenesis1581F → A: Strongly reduces RNA-binding. Ref.8

Secondary structure

............................. 172
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62487 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: AF3CE655F658CD5C

FASTA17219,294
        10         20         30         40         50         60 
MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT IDNIGAGVIQ 

        70         80         90        100        110        120 
PGRGFVLYPV KYKAIVFRPF KGEVVDAVVT QVNKVGLFTE IGPMSCFISR HSIPSEMEFD 

       130        140        150        160        170 
PNSNPPCYKT MDEDIVIQQD DEIRLKIVGT RVDKNDIFAI GSLMDDYLGL VS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_002687.1. NM_002696.2.
UniGeneHs.14839.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C35X-ray2.70B/D/F/H1-172[»]
ProteinModelPortalP62487.
SMRP62487. Positions 1-171.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111432. 44 interactions.
DIPDIP-32663N.
IntActP62487. 20 interactions.
MINTMINT-1033626.
STRING9606.ENSP00000301788.

PTM databases

PhosphoSiteP62487.

Polymorphism databases

DMDM50403601.

Proteomic databases

PaxDbP62487.
PeptideAtlasP62487.
PRIDEP62487.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301788; ENSP00000301788; ENSG00000168002.
GeneID5436.
KEGGhsa:5436.
UCSCuc001nva.3. human.

Organism-specific databases

CTD5436.
GeneCardsGC11P062529.
HGNCHGNC:9194. POLR2G.
HPAHPA053000.
MIM602013. gene.
neXtProtNX_P62487.
PharmGKBPA33514.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1095.
HOGENOMHOG000158201.
HOVERGENHBG055233.
InParanoidP62487.
KOK03015.
OMAKEDHLGV.
OrthoDBEOG76MK9S.
PhylomeDBP62487.
TreeFamTF103042.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP62487.
BgeeP62487.
CleanExHS_POLR2G.
GenevestigatorP62487.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.30.1490.120. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR022967. RNA-binding_domain_S1.
IPR005576. RNA_pol_Rpb7_N.
[Graphical view]
PfamPF00575. S1. 1 hit.
PF03876. SHS2_Rpb7-N. 1 hit.
[Graphical view]
SMARTSM00316. S1. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
SSF88798. SSF88798. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP62487.
GeneWikiPOLR2G.
GenomeRNAi5436.
NextBio21033.
PROP62487.
SOURCESearch...

Entry information

Entry nameRPB7_HUMAN
AccessionPrimary (citable) accession number: P62487
Secondary accession number(s): B2R5C0, P52433, Q2M1Z4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM