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Protein

N-acylneuraminate cytidylyltransferase

Gene

Cmas

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate.2 Publications

Pathwayi: N-acetylneuraminate metabolism

This protein is involved in the pathway N-acetylneuraminate metabolism, which is part of Amino-sugar metabolism.
View all proteins of this organism that are known to be involved in the pathway N-acetylneuraminate metabolism and in Amino-sugar metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei50Substrate1
Binding sitei60Substrate1
Binding sitei109Substrate1
Binding sitei118Substrate1
Binding sitei120Substrate1
Binding sitei141Substrate1
Active sitei1991

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14521.
BRENDAi2.7.7.43. 3474.
SABIO-RKQ99KK2.
UniPathwayiUPA00628.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acylneuraminate cytidylyltransferase (EC:2.7.7.43)
Alternative name(s):
CMP-N-acetylneuraminic acid synthase
Short name:
CMP-NeuNAc synthase
Gene namesi
Name:Cmas
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1337124. Cmas.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi196P → A: Does not affect the nuclear localization. 1
Mutagenesisi198K → A: Abolishes the nuclear localization but does not affect the enzyme activity; when associated with A-201. 1 Publication1
Mutagenesisi199R → A: Abolishes both the nuclear localization and the enzyme activity. 1 Publication1
Mutagenesisi200P → A: Does not affect neither the nuclear localization nor the enzyme activity. 1 Publication1
Mutagenesisi201R → A: Abolishes the nuclear localization but does not affect the enzyme activity; when associated with A-198. 1 Publication1
Mutagenesisi202R → A: Does not strongly affect the nuclear localization but strongly affects the enzyme activity. 1 Publication1
Mutagenesisi203Q → A: Does not affect the nuclear localization but affects the enzyme activity. 1 Publication1
Mutagenesisi204D → A: Does not affect the nuclear localization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002132001 – 432N-acylneuraminate cytidylyltransferaseAdd BLAST432

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei35Omega-N-methylarginineCombined sources1
Modified residuei50Omega-N-methylarginineCombined sources1

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

EPDiQ99KK2.
PaxDbiQ99KK2.
PeptideAtlasiQ99KK2.
PRIDEiQ99KK2.

PTM databases

iPTMnetiQ99KK2.
PhosphoSitePlusiQ99KK2.

Expressioni

Tissue specificityi

Highly expressed in brain and heart, and at intermediate level muscle and liver.1 Publication

Gene expression databases

BgeeiENSMUSG00000030282.

Interactioni

Subunit structurei

Homotetramer; the active enzyme is formed by a dimer of dimers.1 Publication

Protein-protein interaction databases

BioGridi198764. 1 interactor.
IntActiQ99KK2. 2 interactors.
MINTiMINT-4103350.
STRINGi10090.ENSMUSP00000032419.

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 48Combined sources6
Beta strandi54 – 57Combined sources4
Turni59 – 61Combined sources3
Beta strandi62 – 64Combined sources3
Helixi69 – 80Combined sources12
Beta strandi84 – 91Combined sources8
Helixi93 – 101Combined sources9
Beta strandi105 – 108Combined sources4
Helixi111 – 113Combined sources3
Helixi120 – 128Combined sources9
Beta strandi135 – 140Combined sources6
Helixi149 – 160Combined sources12
Beta strandi165 – 173Combined sources9
Beta strandi191 – 195Combined sources5
Turni202 – 204Combined sources3
Beta strandi208 – 219Combined sources12
Helixi220 – 224Combined sources5
Beta strandi231 – 237Combined sources7
Helixi240 – 242Combined sources3
Helixi246 – 249Combined sources4
Helixi252 – 262Combined sources11
Beta strandi275 – 279Combined sources5
Helixi280 – 284Combined sources5
Beta strandi298 – 302Combined sources5
Helixi303 – 314Combined sources12
Beta strandi318 – 322Combined sources5
Helixi329 – 333Combined sources5
Helixi348 – 358Combined sources11
Helixi363 – 365Combined sources3
Beta strandi366 – 369Combined sources4
Helixi373 – 375Combined sources3
Helixi376 – 381Combined sources6
Beta strandi382 – 387Combined sources6
Helixi393 – 396Combined sources4
Beta strandi400 – 402Combined sources3
Turni407 – 410Combined sources4
Helixi411 – 426Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QWJX-ray2.80A/B/C/D40-268[»]
3EWIX-ray1.90A/B267-432[»]
ProteinModelPortaliQ99KK2.
SMRiQ99KK2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99KK2.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi15 – 31BC1 motifAdd BLAST17
Motifi198 – 204BC2 motif7
Motifi267 – 274BC3 motif8

Domaini

The BC2 (basic cluster 2) motif is necessary and sufficient for the nuclear localization and contains the catalytic active site. The localization in the nucleus is however not required for the enzyme activity.

Sequence similaritiesi

Belongs to the CMP-NeuNAc synthase family.Curated

Phylogenomic databases

eggNOGiENOG410IJVA. Eukaryota.
COG1083. LUCA.
COG1778. LUCA.
HOGENOMiHOG000284760.
HOVERGENiHBG052605.
InParanoidiQ99KK2.
KOiK00983.
PhylomeDBiQ99KK2.
TreeFamiTF324840.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
3.90.550.10. 1 hit.
InterProiIPR003329. Cytidylyl_trans.
IPR023214. HAD-like_dom.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF02348. CTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
SSF56784. SSF56784. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99KK2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDALEKGAVT SGPAPRGRPS RGRPPKLQRS RGAGRGLEKP PHLAALVLAR
60 70 80 90 100
GGSKGIPLKN IKRLAGVPLI GWVLRAALDA GVFQSVWVST DHDEIENVAK
110 120 130 140 150
QFGAQVHRRS SETSKDSSTS LDAIVEFLNY HNEVDIVGNI QATSPCLHPT
160 170 180 190 200
DLQKVAEMIR EEGYDSVFSV VRRHQFRWSE IQKGVREVTE PLNLNPAKRP
210 220 230 240 250
RRQDWDGELY ENGSFYFAKR HLIEMGYLQG GKMAYYEMRA EHSVDIDVDI
260 270 280 290 300
DWPIAEQRVL RFGYFGKEKL KEIKLLVCNI DGCLTNGHIY VSGDQKEIIS
310 320 330 340 350
YDVKDAIGIS LLKKSGIEVR LISERACSKQ TLSALKLDCK TEVSVSDKLA
360 370 380 390 400
TVDEWRKEMG LCWKEVAYLG NEVSDEECLK RVGLSAVPAD ACSGAQKAVG
410 420 430
YICKCSGGRG AIREFAEHIF LLIEKVNNSC QK
Length:432
Mass (Da):48,058
Last modified:February 1, 2005 - v2
Checksum:iBF7295535E7F6CE5
GO
Isoform 2 (identifier: Q99KK2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-232: Missing.

Note: Inactive. No experimental confirmation available.
Show »
Length:200
Mass (Da):22,277
Checksum:i0D3C036CD8EC4F31
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9V → A in AAH31500 (PubMed:15489334).Curated1
Sequence conflicti9V → A in AAH63776 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0127651 – 232Missing in isoform 2. 1 PublicationAdd BLAST232

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006215 mRNA. Translation: CAA06915.1.
AK087150 mRNA. Translation: BAC39813.1.
BC004606 mRNA. Translation: AAH04606.1.
BC031500 mRNA. Translation: AAH31500.1.
BC063776 mRNA. Translation: AAH63776.1.
CCDSiCCDS20687.1. [Q99KK2-1]
RefSeqiNP_034038.2. NM_009908.2.
UniGeneiMm.3820.

Genome annotation databases

GeneIDi12764.
KEGGimmu:12764.
UCSCiuc009eps.2. mouse. [Q99KK2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006215 mRNA. Translation: CAA06915.1.
AK087150 mRNA. Translation: BAC39813.1.
BC004606 mRNA. Translation: AAH04606.1.
BC031500 mRNA. Translation: AAH31500.1.
BC063776 mRNA. Translation: AAH63776.1.
CCDSiCCDS20687.1. [Q99KK2-1]
RefSeqiNP_034038.2. NM_009908.2.
UniGeneiMm.3820.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QWJX-ray2.80A/B/C/D40-268[»]
3EWIX-ray1.90A/B267-432[»]
ProteinModelPortaliQ99KK2.
SMRiQ99KK2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198764. 1 interactor.
IntActiQ99KK2. 2 interactors.
MINTiMINT-4103350.
STRINGi10090.ENSMUSP00000032419.

PTM databases

iPTMnetiQ99KK2.
PhosphoSitePlusiQ99KK2.

Proteomic databases

EPDiQ99KK2.
PaxDbiQ99KK2.
PeptideAtlasiQ99KK2.
PRIDEiQ99KK2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi12764.
KEGGimmu:12764.
UCSCiuc009eps.2. mouse. [Q99KK2-1]

Organism-specific databases

CTDi55907.
MGIiMGI:1337124. Cmas.

Phylogenomic databases

eggNOGiENOG410IJVA. Eukaryota.
COG1083. LUCA.
COG1778. LUCA.
HOGENOMiHOG000284760.
HOVERGENiHBG052605.
InParanoidiQ99KK2.
KOiK00983.
PhylomeDBiQ99KK2.
TreeFamiTF324840.

Enzyme and pathway databases

UniPathwayiUPA00628.
BioCyciMetaCyc:MONOMER-14521.
BRENDAi2.7.7.43. 3474.
SABIO-RKQ99KK2.

Miscellaneous databases

ChiTaRSiCmas. mouse.
EvolutionaryTraceiQ99KK2.
PROiQ99KK2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030282.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
3.90.550.10. 1 hit.
InterProiIPR003329. Cytidylyl_trans.
IPR023214. HAD-like_dom.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF02348. CTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
SSF56784. SSF56784. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNEUA_MOUSE
AccessioniPrimary (citable) accession number: Q99KK2
Secondary accession number(s): O88719, Q8C330, Q8K2G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: November 2, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.