CPLM-009503

Genbank Nucleotide ID

DNA-directed RNA polymerase II subunit RPB7

Protein Synonyms/Alias

RNA polymerase II subunit B7; DNA-directed RNA polymerase II subunit G; RNA polymerase II 19 kDa subunit; RPB19

Homo sapiens (Human)

Position	Peptide	Type	References
27	PNLLNTVKQKLFTEV	ubiquitination	[1, 2, 3, 4]
29	LLNTVKQKLFTEVEG	ubiquitination	[3]
71	GFVLYPVKYKAIVFR	ubiquitination	[1, 3, 5, 6]
73	VLYPVKYKAIVFRPF	ubiquitination	[3]
81	AIVFRPFKGEVVDAV	ubiquitination	[1, 3, 4, 5, 6, 7, 8]
129	NSNPPCYKTMDEDIV	ubiquitination	[3, 9]
146	QDDEIRLKIVGTRVD	ubiquitination	[1, 3, 4, 5, 6]
154	IVGTRVDKNDIFAIG	ubiquitination	[1]

[1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[9] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]

Functional Description

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.

3D-structure; Complete proteome; DNA-directed RNA polymerase; Nucleus; Reference proteome; RNA-binding; Transcription.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
GO:0006915; P:apoptotic process; IEA:Compara.
GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO:0022415; P:viral reproductive process; TAS:Reactome.

IPR012340; NA-bd_OB-fold.
IPR003029; Rbsml_prot_S1_RNA-bd_dom.
IPR022967; RNA-binding_domain_S1.
IPR005576; RNA_pol_Rpb7_N.

PF00575; S1
PF03876; SHS2_Rpb7-N