CPLM-015016

Genbank Nucleotide ID

Protein lin-54 homolog

Protein Synonyms/Alias

CXC domain-containing protein 1

Homo sapiens (Human)

Position	Peptide	Type	References
92	ADSNTTVKPAFPSGL	acetylation	[1, 2]
92	ADSNTTVKPAFPSGL	ubiquitination	[3, 4]
101	AFPSGLQKLGAQTPV	ubiquitination	[3]
134	KLGNQTLKPDGQKLI	ubiquitination	[3, 4]
147	LILTTLGKSGSPIVL	ubiquitination	[3]
195	IGGRPEVKPVIGVSA	ubiquitination	[3]
244	TSGPVITKLIFAKPI	acetylation	[5]
249	ITKLIFAKPINSKAV	acetylation	[5]
249	ITKLIFAKPINSKAV	ubiquitination	[3]
254	FAKPINSKAVTGQTT	ubiquitination	[3]
313	KIAISPLKSPNKAVK	ubiquitination	[3]
357	QIQVPGSKFHYVRLV	acetylation	[5]
357	QIQVPGSKFHYVRLV	ubiquitination	[3, 4]
413	IVSAQAVKQVVPKPI	ubiquitination	[3]
418	AVKQVVPKPINPTSQ	ubiquitination	[3]
529	RKPCNCTKSLCLKLY	ubiquitination	[4]
580	DRNPEAFKPKIGKGK	ubiquitination	[4]
608	CKRSGCLKNYCECYE	ubiquitination	[3, 4, 6]
710	AQAEQADKKGKSKAA	ubiquitination	[3]
711	QAEQADKKGKSKAAA	ubiquitination	[3]
741	INSAGKAKSDPCAMN	ubiquitination	[3]

[1] 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]
[2] 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]
[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] 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]
[5] 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]
[6] 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

Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In G0 phase, the complex binds to more than 800 promoters and is required for repression of E2F target genes. In S phase, the complex selectively binds to the promoters of G2/M genes whose products are required for mitosis and participates in their cell cycle dependent activation. In the complex, acts as a DNA-binding protein that binds the promoter of CDK1 in a sequence-specific manner.

DOMAIN 521 634 CRC.
MOD_RES 244 244 N6-acetyllysine.
MOD_RES 249 249 N6-acetyllysine.
MOD_RES 310 310 Phosphoserine.
MOD_RES 314 314 Phosphoserine.

Acetylation; Activator; Alternative splicing; Cell cycle; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0000278; P:mitotic cell cycle; TAS:Reactome.
GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.