CPLM-019281

Genbank Nucleotide ID

Cell division cycle-associated 7-like protein

Protein Synonyms/Alias

Protein JPO2; Transcription factor RAM2

Homo sapiens (Human)

Position	Peptide	Type	References
63	QDVRFHSKYFTEELR	ubiquitination	[1]
152	AFQFPTKKLANKPDK	ubiquitination	[1]
156	PTKKLANKPDKNSSS	ubiquitination	[1]
159	KLANKPDKNSSSEQL	ubiquitination	[1]
177	ARLQNEKKTILERKK	ubiquitination	[1]
280	RSARPPEKFALENFT	ubiquitination	[1, 2, 3, 4]
347	VRDKIYDKVLGNTCH	ubiquitination	[1, 2, 3, 4, 5]
364	RQKTIDTKTVCRNQG	ubiquitination	[1]
440	FYGYDNVKEYLESLQ	ubiquitination	[1, 4, 6]
448	EYLESLQKELVEDN*	ubiquitination	[4, 6]

[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] 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]
[3] 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]
[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] 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]
[6] 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]

Functional Description

Plays a role in transcriptional regulation as a repressor that inhibits monoamine oxidase A (MAOA) activity and gene expression by binding to the promoter. Plays an important oncogenic role in mediating the full transforming effect of MYC in medulloblastoma cells. Involved in apoptotic signaling pathways; May act downstream of P38-kinase and BCL-2, but upstream of CASP3/caspase-3 as well as CCND1/cyclin D1 and E2F1.

REGION 58 119 PSIP1-binding.
REGION 213 235 MYC-binding.
MOD_RES 21 21 Phosphoserine.
MOD_RES 77 77 Phosphothreonine.
MOD_RES 79 79 Phosphoserine.
MOD_RES 105 105 Phosphoserine.
MOD_RES 108 108 Phosphoserine.
MOD_RES 117 117 Phosphoserine.
MOD_RES 138 138 Phosphoserine.
MOD_RES 139 139 Phosphoserine.
MOD_RES 162 162 Phosphoserine.
MOD_RES 261 261 Phosphoserine.

Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005730; C:nucleolus; IDA:HPA.
GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR018866; Znf-4CXXC_R1.

PF10497; zf-4CXXC_R1