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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501Substrate
Binding sitei60 – 601Substrate
Binding sitei109 – 1091Substrate
Binding sitei118 – 1181Substrate
Binding sitei120 – 1201Substrate
Binding sitei141 – 1411Substrate
Active sitei199 – 1991

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi196 – 1961P → A: Does not affect the nuclear localization.
Mutagenesisi198 – 1981K → A: Abolishes the nuclear localization but does not affect the enzyme activity; when associated with A-201. 1 Publication
Mutagenesisi199 – 1991R → A: Abolishes both the nuclear localization and the enzyme activity. 1 Publication
Mutagenesisi200 – 2001P → A: Does not affect neither the nuclear localization nor the enzyme activity. 1 Publication
Mutagenesisi201 – 2011R → A: Abolishes the nuclear localization but does not affect the enzyme activity; when associated with A-198. 1 Publication
Mutagenesisi202 – 2021R → A: Does not strongly affect the nuclear localization but strongly affects the enzyme activity. 1 Publication
Mutagenesisi203 – 2031Q → A: Does not affect the nuclear localization but affects the enzyme activity. 1 Publication
Mutagenesisi204 – 2041D → A: Does not affect the nuclear localization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432N-acylneuraminate cytidylyltransferasePRO_0000213200Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99KK2.
MaxQBiQ99KK2.
PaxDbiQ99KK2.
PRIDEiQ99KK2.

PTM databases

iPTMnetiQ99KK2.
PhosphoSiteiQ99KK2.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ99KK2.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi198764. 1 interaction.
IntActiQ99KK2. 2 interactions.
MINTiMINT-4103350.
STRINGi10090.ENSMUSP00000032419.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 486Combined sources
Beta strandi54 – 574Combined sources
Turni59 – 613Combined sources
Beta strandi62 – 643Combined sources
Helixi69 – 8012Combined sources
Beta strandi84 – 918Combined sources
Helixi93 – 1019Combined sources
Beta strandi105 – 1084Combined sources
Helixi111 – 1133Combined sources
Helixi120 – 1289Combined sources
Beta strandi135 – 1406Combined sources
Helixi149 – 16012Combined sources
Beta strandi165 – 1739Combined sources
Beta strandi191 – 1955Combined sources
Turni202 – 2043Combined sources
Beta strandi208 – 21912Combined sources
Helixi220 – 2245Combined sources
Beta strandi231 – 2377Combined sources
Helixi240 – 2423Combined sources
Helixi246 – 2494Combined sources
Helixi252 – 26211Combined sources
Beta strandi275 – 2795Combined sources
Helixi280 – 2845Combined sources
Beta strandi298 – 3025Combined sources
Helixi303 – 31412Combined sources
Beta strandi318 – 3225Combined sources
Helixi329 – 3335Combined sources
Helixi348 – 35811Combined sources
Helixi363 – 3653Combined sources
Beta strandi366 – 3694Combined sources
Helixi373 – 3753Combined sources
Helixi376 – 3816Combined sources
Beta strandi382 – 3876Combined sources
Helixi393 – 3964Combined sources
Beta strandi400 – 4023Combined sources
Turni407 – 4104Combined sources
Helixi411 – 42616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QWJX-ray2.80A/B/C/D40-268[»]
3EWIX-ray1.90A/B267-432[»]
ProteinModelPortaliQ99KK2.
SMRiQ99KK2. Positions 40-268, 272-429.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99KK2.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi15 – 3117BC1 motifAdd
BLAST
Motifi198 – 2047BC2 motif
Motifi267 – 2748BC3 motif

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.
OrthoDBiEOG779P07.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91V → A in AAH31500 (PubMed:15489334).Curated
Sequence conflicti9 – 91V → A in AAH63776 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 232232Missing in isoform 2. 1 PublicationVSP_012765Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1QWJX-ray2.80A/B/C/D40-268[»]
3EWIX-ray1.90A/B267-432[»]
ProteinModelPortaliQ99KK2.
SMRiQ99KK2. Positions 40-268, 272-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198764. 1 interaction.
IntActiQ99KK2. 2 interactions.
MINTiMINT-4103350.
STRINGi10090.ENSMUSP00000032419.

PTM databases

iPTMnetiQ99KK2.
PhosphoSiteiQ99KK2.

Proteomic databases

EPDiQ99KK2.
MaxQBiQ99KK2.
PaxDbiQ99KK2.
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.
OrthoDBiEOG779P07.
PhylomeDBiQ99KK2.
TreeFamiTF324840.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiCmas. mouse.
EvolutionaryTraceiQ99KK2.
NextBioi282118.
PROiQ99KK2.
SOURCEiSearch...

Gene expression databases

BgeeiQ99KK2.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian cytidine 5-prime-monophosphate N-acetylneuraminic acid synthetase: a nuclear protein with evolutionarily conserved structural motifs."
    Muenster A.-K., Eckhardt M., Potvin B., Muehlenhoff M., Stanley P., Gerardy-Schahn R.
    Proc. Natl. Acad. Sci. U.S.A. 95:9140-9145(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Lung.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Colon and Mammary tumor.
  4. "Nuclear localization signal of murine CMP-Neu5Ac synthetase includes residues required for both nuclear targeting and enzymatic activity."
    Muenster A.-K., Weinhold B., Gotza B., Muehlenhoff M., Frosch M., Gerardy-Schahn R.
    J. Biol. Chem. 277:19688-19696(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ENZYME ACTIVITY, MUTAGENESIS OF LYS-198; ARG-199; PRO-200; ARG-201; ARG-202; GLN-203 AND ASP-204.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Liver and Pancreas.
  6. "The crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase."
    Krapp S., Muenster-Kuehnel A.-K., Kaiser J.T., Huber R., Tiralongo J., Gerardy-Schahn R., Jacob U.
    J. Mol. Biol. 334:625-637(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 40-268 IN COMPLEX WITH CMP-NEUNAC, SUBUNIT.

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: May 11, 2016
This is version 117 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.