P62487 (RPB7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	POLR2G
Synonyms:	RPB7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	172 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
Ligand	RNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Traceable author statement. Source: Reactome apoptotic process Inferred from electronic annotation. Source: Compara mRNA splicing, via spliceosome Traceable author statement. Source: Reactome positive regulation of viral transcription Traceable author statement. Source: Reactome protein phosphorylation Inferred from direct assay Ref.6. Source: GOC transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription-coupled nucleotide-excision repair Traceable author statement. Source: Reactome viral reproductive process Traceable author statement. Source: Reactome
Cellular_component	DNA-directed RNA polymerase II, core complex Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	DNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 172

172

DNA-directed RNA polymerase II subunit RPB7

PRO_0000073986

Experimental info

Mutagenesis

14

1

H → E: Strongly reduces RNA-binding. Ref.8

Mutagenesis

33

1

E → K: Strongly reduces RNA-binding. Ref.8

Mutagenesis

41

1

K → E: Strongly reduces RNA-binding. Ref.8

Mutagenesis

90

1

T → A: Reduces RNA-binding. Ref.8

Mutagenesis

93

1

N → A: Reduces RNA-binding. Ref.8

Mutagenesis

94

1

K → E: Reduces RNA-binding. Ref.8

Mutagenesis

107

1

F → E: Reduces RNA-binding. Ref.8

Mutagenesis

109

1

S → A: Strongly reduces RNA-binding. Ref.8

Mutagenesis

111

1

H → E: Strongly reduces RNA-binding. Ref.8

Mutagenesis

151

1

R → E: Strongly reduces RNA-binding. Ref.8

Mutagenesis

153

1

D → E: Strongly reduces RNA-binding. Ref.8

Mutagenesis

158

1

F → A: Strongly reduces RNA-binding. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

172

Helix Strand Turn

Details...

Beta strand

2 – 13

12

Helix

15 – 17

3

Helix

22 – 34

13

Turn

40 – 42

3

Beta strand

43 – 54

12

Beta strand

64 – 77

14

Beta strand

84 – 93

10

Beta strand

96 – 101

6

Beta strand

104 – 109

6

Helix

110 – 112

3

Beta strand

117 – 125

9

Beta strand

127 – 130

4

Beta strand

135 – 138

4

Beta strand

142 – 153

12

Beta strand

156 – 162

7

Sequences

	Sequence		Length	Mass (Da)
	P62487 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: AF3CE655F658CD5C	FASTA	172	19,294
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00218895.

RefSeq

NP_002687.1. NM_002696.2.

UniGene

Hs.14839.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C35	X-ray	2.70	B/D/F/H	1-172	[»]

ProteinModelPortal

P62487.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32663N.

IntAct

P62487. 20 interactions.

MINT

MINT-1033626.

STRING

9606.ENSP00000301788.

PTM databases

PhosphoSite

P62487.

Polymorphism databases

DMDM

50403601.

Proteomic databases

PaxDb

P62487.

PeptideAtlas

P62487.

PRIDE

P62487.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000301788; ENSP00000301788; ENSG00000168002.

GeneID

5436.

KEGG

hsa:5436.

UCSC

uc001nva.3. human.

Organism-specific databases

CTD

5436.

GeneCards

GC11P062529.

HGNC

HGNC:9194. POLR2G.

HPA

HPA053000.

MIM

602013. gene.

neXtProt

NX_P62487.

PharmGKB

PA33514.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1095.

HOGENOM

HOG000158201.

HOVERGEN

HBG055233.

InParanoid

P62487.

KO

K03015.

OMA

TRVDAND.

OrthoDB

EOG451DRZ.

PhylomeDB

P62487.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P62487.

Bgee

P62487.

CleanEx

HS_POLR2G.

Genevestigator

P62487.

GermOnline

ENSG00000168002. Homo sapiens.

Family and domain databases

Gene3D

2.40.50.140. 1 hit.
3.30.1490.120. 1 hit.

InterPro

IPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR022967. RNA-binding_domain_S1.
IPR005576. RNA_pol_Rpb7_N.
[Graphical view]

Pfam

PF00575. S1. 1 hit.
PF03876. SHS2_Rpb7-N. 1 hit.
[Graphical view]

SMART

SM00316. S1. 1 hit.
[Graphical view]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.
SSF88798. RNA_pol_Rpb7_N. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P62487.

GenomeRNAi

5436.

NextBio

21033.

SOURCE

Search...

Entry information

Entry name

RPB7_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.