CPLM-012543

Genbank Nucleotide ID

Transcription elongation factor B polypeptide 1

Protein Synonyms/Alias

Elongin 15 kDa subunit; Elongin-C; EloC; RNA polymerase II transcription factor SIII subunit C; SIII p15

Homo sapiens (Human)

Position	Peptide	Type	References
6	**MDGEEKTYGGCEG	ubiquitination	[1]
20	GPDAMYVKLISSDGH	ubiquitination	[1]
32	DGHEFIVKREHALTS	acetylation	[2]
32	DGHEFIVKREHALTS	ubiquitination	[1, 3, 4, 5, 6]
43	ALTSGTIKAMLSGPG	ubiquitination	[1, 4, 5, 7, 8]

[1] 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]
[2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[3] 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]
[4] 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]
[5] 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]
[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] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
Xu G, Paige JS, Jaffrey SR.
Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
[8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]

Functional Description

SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).

3D-structure; Alternative splicing; Complete proteome; Host-virus interaction; Nucleus; Reference proteome; Transcription; Transcription regulation; Ubl conjugation pathway.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0030891; C:VCB complex; IEA:Compara.
GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:Compara.
GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
GO:0022415; P:viral reproductive process; TAS:Reactome.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.

IPR011333; BTB/POZ_fold.
IPR001232; Skp1_comp.
IPR016073; Skp1_comp_POZ.