CPLM-023145

Genbank Nucleotide ID

Malignant T-cell-amplified sequence 1

Protein Synonyms/Alias

MCT-1; Multiple copies T-cell malignancies

Homo sapiens (Human)

Position	Peptide	Type	References
23	QLKTSVIKGIKNQLI	ubiquitination	[1]
51	MPKKDPVKIVRCHEH	acetylation	[2]
87	PTLRLLHKYPFILPH	acetylation	[3]
87	PTLRLLHKYPFILPH	ubiquitination	[4]
99	LPHQQVDKGAIKFVL	acetylation	[5]
157	MSAEDIEKVNKGIGI	acetylation	[3]
160	EDIEKVNKGIGIENI	ubiquitination	[1, 6]
178	NDGLWHMKTYK****	ubiquitination	[1]
181	LWHMKTYK*******	ubiquitination	[1]

[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] 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]
[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] 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]
[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

Anti-oncogene that play a role in cell cycle regulation; decreases cell doubling time and anchorage-dependent growth; shortens the duration of G1 transit time and G1/S transition. When constituvely expressed, increases CDK4 and CDK6 kinases activity and CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK complex formation. Plays a role as translation enhancer; Recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, subsequently altering the mRNA translation profile; Up-regulates protein levels of BCL2L2, TFDP1, MRE11A, CCND1 and E2F1, while mRNA levels remains constant. Hyperactivates DNA damage signaling pathway; increased gamma- irradiation-induced phosphorylation of histone H2AX, and induces damage foci formation. Increases the overall number of chromosomal abnormalities such as larger chromosomes formation and multiples chromosomal fusions when overexpressed in gamma-irradiated cells. May play a role in promoting lymphoid tumor development: lymphoid cell lines overexpressing MCTS1 exhibit increased growth rates and display increased protection against apoptosis. May contribute to the pathogenesis and progression of breast cancer via promotion of angiogenesis through the decline of inhibitory THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in the process of proteasome degradation to down-regulate Tumor suppressor p53/TP53 in breast cancer cell; Positively regulates phosphorylation of MAPK1 and MAPK3.

DOMAIN 92 171 PUA.
MOD_RES 81 81 Phosphothreonine; by MAPK1 and MAPK3.
MOD_RES 118 118 Phosphoserine; by CDK1.

3D-structure; Alternative splicing; Cell cycle; Complete proteome; Cytoplasm; DNA damage; Growth regulation; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Tumor suppressor.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0003723; F:RNA binding; IEA:InterPro.
GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006974; P:response to DNA damage stimulus; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR002478; PUA.
IPR015947; PUA-like_domain.
IPR016437; Transl_RNA-bd_prd.
IPR004521; Uncharacterised_CHP00451.