CPLM-021621

Genbank Nucleotide ID

NmrA-like family domain-containing protein 1

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
31	LLEDGTFKVRVVTRN	ubiquitination	[1]
95	EQEVKQGKLLADLAR	ubiquitination	[1]
118	YSGLENIKKLTAGRL	ubiquitination	[1]
119	SGLENIKKLTAGRLA	ubiquitination	[1]
133	AAAHFDGKGEVEEYF	ubiquitination	[1, 2]
167	LSHFLPQKAPDGKSY	ubiquitination	[1]
206	SLLKMPEKYVGQNIG	ubiquitination	[1]
230	EYAALLTKHTRKVVH	ubiquitination	[1]
240	RKVVHDAKMTPEDYE	ubiquitination	[1]
248	MTPEDYEKLGFPGAR	ubiquitination	[1]
281	LTLRLNPKALTLDQW	ubiquitination	[1, 2, 3, 4]

[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] 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]
[4] 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]

Functional Description

Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer.

NP_BIND 11 16 NADP.
NP_BIND 37 41 NADP.
NP_BIND 58 59 NADP.
NP_BIND 79 81 NADP.
NP_BIND 155 158 NADP.
REGION 153 189 Interaction with ASS1.
BINDING 62 62 NADP; shared with dimeric partner.
BINDING 92 92 NADP; shared with dimeric partner.
BINDING 133 133 NADP.

3D-structure; Complete proteome; Cytoplasm; NADP; Nucleus; Polymorphism; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005730; C:nucleolus; IDA:HPA.
GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.

IPR016040; NAD(P)-bd_dom.
IPR008030; NmrA.