UniProt Accession

 NEUA_HUMAN; Q8NFW8; Q96AX5; Q9NQZ0 

Genbank Protein ID

 AF397212; AF271388; AK022927; AL832975; BC016609 

Genbank Nucleotide ID

 AAM90580.1; AAF76203.1; BAB14311.1; CAH56346.1; AAH16609.1 

Protein Name

 N-acylneuraminate cytidylyltransferase 

Protein Synonyms/Alias

 CMP-N-acetylneuraminic acid synthase; CMP-NeuNAc synthase 

Gene Name

 CMAS 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MDSVEKGAATSVS	ubiquitination	[1]
41	GQGRGVEKPPHLAAL	ubiquitination	[1]
56	ILARGGSKGIPLKNI	ubiquitination	[1]
61	GSKGIPLKNIKHLAG	ubiquitination	[1, 2, 3]
64	GIPLKNIKHLAGVPL	ubiquitination	[1]
185	FRWSEIQKGVREVTE	ubiquitination	[1, 4]
200	PLNLNPAKRPRRQDW	ubiquitination	[1]
382	VSDEECLKRVGLSGA	ubiquitination	[1, 5]
399	DACSTAQKAVGYICK	methylation	[6]
399	DACSTAQKAVGYICK	ubiquitination	[1, 5]

Reference

 [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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.
 Moore KE, Carlson SM, Camp ND, Cheung P, James RG, Chua KF, Wolf-Yadlin A, Gozani O.
 Mol Cell. 2013 May 9;50(3):444-56. [PMID: 23583077] 

Functional Description

 Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). 

Sequence Annotation

 MOTIF 15 31 BC1 motif.
 MOTIF 200 206 BC2 motif.
 MOTIF 269 276 BC3 motif.
 ACT_SITE 201 201 By similarity.
 BINDING 52 52 Substrate (By similarity).
 BINDING 62 62 Substrate (By similarity).
 BINDING 111 111 Substrate (By similarity).
 BINDING 120 120 Substrate (By similarity).
 BINDING 122 122 Substrate (By similarity).
 BINDING 143 143 Substrate (By similarity).
 MOD_RES 1 1 N-acetylmethionine.  

Keyword

 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Nucleotidyltransferase; Nucleus; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 434 AA 

Protein Sequence

Gene Ontology

 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IEA:EC.
 GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
 GO:0006054; P:N-acetylneuraminate metabolic process; IEA:UniProtKB-UniPathway. 

Interpro

 IPR003329; Cytidylyl_trans.
 IPR023214; HAD-like_dom. 

Pfam

 PF02348; CTP_transf_3 

SMART

  

PROSITE

  

PRINTS