UniProt Accession

 TCP4_HUMAN; P53999; Q96L29 

Genbank Protein ID

 X79805; U12979; BC009610; BC010537; BC018189; BC022339 

Genbank Nucleotide ID

 CAA56200.1; AAA20980.1; AAH09610.1; AAH10537.1; AAH18189.1; AAH22339.1 

Protein Name

 Activated RNA polymerase II transcriptional coactivator p15 

Protein Synonyms/Alias

 Positive cofactor 4; PC4; SUB1 homolog; p14 

Gene Name

 SUB1 

Gene Synonyms/Alias

 PC4; RPO2TC1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MPKSKELVSSSS	acetylation	[1]
35	KKQVAPEKPVKKQKT	acetylation	[2]
53	SRALSSSKQSSSSRD	acetylation	[1]
53	SRALSSSKQSSSSRD	ubiquitination	[3, 4]
68	DNMFQIGKMRYVSVR	acetylation	[2, 5, 6]
68	DNMFQIGKMRYVSVR	ubiquitination	[3, 4, 7, 8, 9, 10, 11, 12, 13]
80	SVRDFKGKVLIDIRE	ubiquitination	[4, 7, 12, 13]
97	MDPEGEMKPGRKGIS	acetylation	[6, 13]
97	MDPEGEMKPGRKGIS	ubiquitination	[4]
101	GEMKPGRKGISLNPE	ubiquitination	[4]
114	PEQWSQLKEQISDID	ubiquitination	[3, 8, 9]

Reference

 [1] Identification of lysine acetyltransferase p300 substrates using 4-pentynoyl-coenzyme A and bioorthogonal proteomics.
 Yang YY, Grammel M, Hang HC.
 Bioorg Med Chem Lett. 2011 Sep 1;21(17):4976-9. [PMID: 21669532]
 [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] 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]
 [4] 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]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] 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] 

Functional Description

 General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA). 

Sequence Annotation

 REGION 2 50 Regulatory.
 REGION 77 101 Interaction with ssDNA.
 MOD_RES 9 9 Phosphoserine (By similarity).
 MOD_RES 10 10 Phosphoserine (By similarity).
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 12 12 Phosphoserine (By similarity).
 MOD_RES 13 13 Phosphoserine.
 MOD_RES 15 15 Phosphoserine.
 MOD_RES 17 17 Phosphoserine.
 MOD_RES 19 19 Phosphoserine.
 MOD_RES 35 35 N6-acetyllysine.
 MOD_RES 68 68 N6-acetyllysine.
 MOD_RES 118 118 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Activator; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 127 AA 

Protein Sequence

Gene Ontology

 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005667; C:transcription factor complex; IDA:UniProtKB.
 GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR003173; PC4.
 IPR009044; ssDNA-bd_transcriptional_reg. 

Pfam

 PF02229; PC4 

SMART

  

PROSITE

  

PRINTS