CPLM-001125

Genbank Nucleotide ID

Zinc finger CCCH domain-containing protein 11A

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
99	GLFLPPSKTVLPTVP	ubiquitination	[1]
114	ESPEEEVKASQLSVQ	ubiquitination	[1]
124	QLSVQQNKLSVQSNP	ubiquitination	[1, 2]
254	EPVPGPEKENVRTVV	ubiquitination	[1]
269	RTVTLSTKQGEEPLV	ubiquitination	[1, 3]
286	SLTERLGKRKFSAGG	acetylation	[4]
300	GDSDPPLKRSLAQRL	ubiquitination	[3]
349	DNEDATDKVNKVGEI	ubiquitination	[1]
381	GELQTKLKTEGPSKT	ubiquitination	[1]
387	LKTEGPSKTDDSTSG	ubiquitination	[1]
413	FSEVLAEKKHRQQEA	ubiquitination	[1]
414	SEVLAEKKHRQQEAE	ubiquitination	[1]
442	KIDSEIKKTVVLPPI	ubiquitination	[1]
464	EEPAGKTKSMQEVHI	ubiquitination	[1]
478	IKTLEEIKLEKALRV	ubiquitination	[1]
481	LEEIKLEKALRVQQS	ubiquitination	[1]
540	SSIRTEAKEASGETT	ubiquitination	[1]
665	VKVVSSPKLAPKRKA	acetylation	[5]
684	AAVIAAVKPLSSSSV	acetylation	[5]
764	LSSASTGKPPLSVED	acetylation	[5, 6, 7, 8]

[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] 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]
[3] 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]
[4] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[5] 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]
[6] 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]
[7] 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]
[8] 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]

Functional Description

ZN_FING 2 29 C3H1-type 1.
ZN_FING 31 57 C3H1-type 2.
ZN_FING 60 86 C3H1-type 3.
MOD_RES 108 108 Phosphoserine.
MOD_RES 132 132 Phosphoserine.
MOD_RES 171 171 Phosphoserine.
MOD_RES 290 290 Phosphoserine.
MOD_RES 321 321 Phosphothreonine.
MOD_RES 738 738 Phosphoserine.
MOD_RES 758 758 Phosphoserine.
MOD_RES 759 759 Phosphoserine (By similarity).
MOD_RES 762 762 Phosphothreonine (By similarity).
MOD_RES 764 764 N6-acetyllysine.
MOD_RES 768 768 Phosphoserine.

Acetylation; Coiled coil; Complete proteome; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO:0008270; F:zinc ion binding; IEA:InterPro.

IPR000571; Znf_CCCH.