CPLM-022137

Genbank Nucleotide ID

Protein Synonyms/Alias

DNA damage-regulated overexpressed in cancer 45; DOC45; GTP-binding protein 9

GTPBP9; PRO2455; PTD004

Homo sapiens (Human)

Position	Peptide	Type	References
83	QYHKPASKIPAFLNV	ubiquitination	[1]
166	MIGPIIDKLEKVAVR	acetylation	[2]
180	RGGDKKLKPEYDIMC	ubiquitination	[3]
190	YDIMCKVKSWVIDQK	ubiquitination	[1, 3, 4, 5]
198	SWVIDQKKPVRFYHD	ubiquitination	[3]
216	KEIEVLNKHLFLTSK	acetylation	[6]
216	KEIEVLNKHLFLTSK	ubiquitination	[1]
242	DYIRKKNKWLIKIKE	acetylation	[6]
281	LSAEERQKYLEANMT	ubiquitination	[1, 5]
294	MTQSALPKIIKAGFA	acetylation	[6]
294	MTQSALPKIIKAGFA	ubiquitination	[1]
333	KAPQAAGKIHTDFEK	ubiquitination	[3]
354	VMKYEDFKEEGSENA	ubiquitination	[3, 5]
363	EGSENAVKAAGKYRQ	ubiquitination	[5]

[1] 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]
[2] 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]
[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] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[5] 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]
[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]

Functional Description

Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP.

DOMAIN 24 131 G.
NP_BIND 32 37 ATP.
MOTIF 267 274 Nuclear export signal (Potential).
BINDING 231 231 ATP; via carbonyl oxygen.
MOD_RES 294 294 N6-acetyllysine.

3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Hydrolase; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:LIFEdb.
GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IDA:HGNC.
GO:0005525; F:GTP binding; IEA:InterPro.
GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO:0006200; P:ATP catabolic process; IDA:HGNC.

IPR012675; Beta-grasp_dom.
IPR004396; CHP00092.
IPR013029; DUF933.
IPR006073; GTP_binding_domain.
IPR027417; P-loop_NTPase.
IPR012676; TGS-like.
IPR023192; TGS-like_dom.

PF01926; MMR_HSR1
PF06071; YchF-GTPase_C