CPLM-020149

Genbank Nucleotide ID

WW domain-containing adapter protein with coiled-coil

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
278	QSDHQPKKSFDANGA	ubiquitination	[1]
302	TSSVPAQKTERKEST	acetylation	[2, 3]
466	QTNTVPIKPLISTPP	acetylation	[3, 4]
466	QTNTVPIKPLISTPP	ubiquitination	[1, 5, 6, 7]
486	KVSTPVVKQGPVSQS	ubiquitination	[1, 5, 7, 8, 9]
634	LFLRQQIKELEKLKN	ubiquitination	[1]

[1] 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]
[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] 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]
[4] 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]
[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] 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]
[7] 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]
[8] 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]
[9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]

Functional Description

Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription. Regulates the cell-cycle checkpoint activation in response to DNA damage. Positive regulator of amino acid starvation-induced autophagy. May negatively regulate the ubiquitin proteasome pathway.

DOMAIN 129 162 WW.
MOD_RES 53 53 Phosphoserine.
MOD_RES 293 293 Phosphothreonine.
MOD_RES 302 302 N6-acetyllysine.
MOD_RES 471 471 Phosphothreonine.
MOD_RES 511 511 Phosphoserine.
MOD_RES 523 523 Phosphoserine.
MOD_RES 525 525 Phosphoserine.
MOD_RES 534 534 Phosphoserine (By similarity).

Acetylation; Alternative splicing; Chromatin regulator; Coiled coil; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; TAS:BHF-UCL.
GO:0005681; C:spliceosomal complex; IEA:Compara.
GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
GO:0000075; P:cell cycle checkpoint; IMP:UniProtKB.
GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IMP:UniProtKB.
GO:0010390; P:histone monoubiquitination; IMP:UniProtKB.
GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:BHF-UCL.
GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL.
GO:0045893; P:positive regulation of transcription, DNA-dependent; IMP:UniProtKB.
GO:0006974; P:response to DNA damage stimulus; IMP:UniProtKB.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

PS01159; WW_DOMAIN_1
PS50020; WW_DOMAIN_2