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Protein

Inactive cytidine monophosphate-N-acetylneuraminic acid hydroxylase

Gene

CMAHP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Sialic acids are components of carbohydrate chains of glycoconjugates and are involved in cell-cell recognition and cell-pathogen interactions. That protein has no CMP-N-acetylneuraminate monooxygenase activity and is not able to convert CMP-N-acetylneuraminic acid (CMP-Neu5Ac) into its hydroxylated derivative CMP-N-glycolylneuraminic acid (CMP-Neu5Gc), a sialic acid abundantly expressed at the surface of many cells in vertebrates (PubMed:9624188). However, it may play a role in Wnt signaling (PubMed:19890979).3 Publications2 Publications

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: InterPro
  2. oxidoreductase activity Source: InterPro

GO - Biological processi

  1. CMP-N-acetylneuraminate metabolic process Source: InterPro
  2. regulation of Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive cytidine monophosphate-N-acetylneuraminic acid hydroxylase1 Publication
Short name:
CMP-NeuAc hydroxylase-like protein
Alternative name(s):
Cytidine monophosphate-N-acetylneuraminic acid hydroxylase pseudogene
Gene namesi
Name:CMAHP
Synonyms:CMAH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:2098. CMAHP.

Subcellular locationi

  1. Cytoplasm 1 Publication

  2. Note: May localize to membranes, nucleus and cytoskeleton.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB
  3. membrane Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi223590237.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Inactive cytidine monophosphate-N-acetylneuraminic acid hydroxylasePRO_0000127801Add
BLAST

Proteomic databases

PaxDbiQ9Y471.
PRIDEiQ9Y471.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in thymus. Not expressed in brain. May be expressed in adult stem cells (at protein level) (PubMed:19890979).2 Publications

Gene expression databases

GenevestigatoriQ9Y471.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000367228.

Family & Domainsi

Sequence similaritiesi

Belongs to the CMP-Neu5Ac hydroxylase family.Curated

Phylogenomic databases

eggNOGiNOG74230.
HOVERGENiHBG107724.
InParanoidiQ9Y471.
OrthoDBiEOG71P29R.
PhylomeDBiQ9Y471.
TreeFamiTF331273.

Family and domain databases

InterProiIPR027033. Cnh.
IPR017941. Rieske_2Fe-2S.
[Graphical view]
PANTHERiPTHR15032:SF10. PTHR15032:SF10. 1 hit.
SUPFAMiSSF50022. SSF50022. 1 hit.
PROSITEiPS51296. RIESKE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9Y471-1) [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
MDENNGLLLL ELNPPNPWDL QPRSPEELAF GEVQITYLTH ACMDLKLGDK
60 70 80 90 100
RMVFDPWLIG PAFARGWWLL HEPPSDWLER LCQADLIYIS HLHSDHLSYP
110 120 130 140 150
TLKKLAGRRP DIPIYVGNTE RPVFWNLNQS GVQLTNINVV PFGIWQQVDK
160 170 180 190 200
NLRFMILMDG VHPEMDTCII VEYKGHKILN IVDCTRPNGG RLPMKVALMM
210 220 230 240 250
SDFAGGASGF PMTFSGGKFT EEWKAQFIKT ERKKLLNYKA RLVKNLQPRI
260 270 280 290 300
YCPFAGYFVE SHPSDKYIKE TNTKNDPNEL NNLIKKNSDV ITWTPRPGAT
310 320 330 340 350
LDLGRMLKDR TDSKGIIEPP EGTKIYKDSW DFEPYLEILN AALGDEIFLH
360 370 380 390 400
SSWIKEYFTW AGFKDYNLVV RMIETDEDFN PFPGGYDYLV DFLDLSFPKE
410 420 430 440 450
RPQREHPYEE IHSRVDVIRH VVKNGLLWDE LYIGFQTRLQ RDPDIYHHLF
460 470 480 490 500
WNHFQIKLPL TPPNWKSFLM CCEQNGPVIL QFSTERTNEP NRNKFSVENK

A
Length:501
Mass (Da):58,380
Last modified:April 29, 2015 - v4
Checksum:i7C340A121B5ACA4D
GO
Isoform 2 (identifier: Q9Y471-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     478-486: VILQFSTER → AILQECKTT
     487-501: Missing.

Show »
Length:486
Mass (Da):56,564
Checksum:i5C6B710F64F85CDD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871I → V in BAA31160 (PubMed:9624188).Curated
Sequence conflicti181 – 1811I → T in BAA31160 (PubMed:9624188).Curated
Sequence conflicti241 – 2411R → W in BAA31160 (PubMed:9624188).Curated
Sequence conflicti310 – 3101R → P in BAA31160 (PubMed:9624188).Curated
Sequence conflicti478 – 4781V → A in ACN93797 (PubMed:19890979).Curated
Sequence conflicti478 – 4781V → A in AAC68881 (PubMed:9751737).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei478 – 4869VILQFSTER → AILQECKTT in isoform 2. VSP_057565
Alternative sequencei487 – 50115Missing in isoform 2. VSP_057566Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074480 mRNA. Translation: AAC68881.1. Sequence problems.
FJ794466 mRNA. Translation: ACN93797.1.
AL133268 Genomic DNA. No translation available.
AB009668 Genomic DNA. Translation: BAA31198.1.
D86324 mRNA. Translation: BAA31160.1.
UniGeneiHs.484918.

Genome annotation databases

EnsembliENST00000377989; ENSP00000367228; ENSG00000168405.
ENST00000377993; ENSP00000367232; ENSG00000168405.
ENST00000399346; ENSP00000382283; ENSG00000168405.
ENST00000436589; ENSP00000397893; ENSG00000168405.
ENST00000458373; ENSP00000401225; ENSG00000168405.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074480 mRNA. Translation: AAC68881.1. Sequence problems.
FJ794466 mRNA. Translation: ACN93797.1.
AL133268 Genomic DNA. No translation available.
AB009668 Genomic DNA. Translation: BAA31198.1.
D86324 mRNA. Translation: BAA31160.1.
UniGeneiHs.484918.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000367228.

Polymorphism and mutation databases

DMDMi223590237.

Proteomic databases

PaxDbiQ9Y471.
PRIDEiQ9Y471.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377989; ENSP00000367228; ENSG00000168405.
ENST00000377993; ENSP00000367232; ENSG00000168405.
ENST00000399346; ENSP00000382283; ENSG00000168405.
ENST00000436589; ENSP00000397893; ENSG00000168405.
ENST00000458373; ENSP00000401225; ENSG00000168405.

Organism-specific databases

GeneCardsiGC06M025082.
HGNCiHGNC:2098. CMAHP.
MIMi603209. gene.
neXtProtiNX_Q9Y471.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG74230.
HOVERGENiHBG107724.
InParanoidiQ9Y471.
OrthoDBiEOG71P29R.
PhylomeDBiQ9Y471.
TreeFamiTF331273.

Miscellaneous databases

ChiTaRSiCMAHP. human.
SOURCEiSearch...

Gene expression databases

GenevestigatoriQ9Y471.

Family and domain databases

InterProiIPR027033. Cnh.
IPR017941. Rieske_2Fe-2S.
[Graphical view]
PANTHERiPTHR15032:SF10. PTHR15032:SF10. 1 hit.
SUPFAMiSSF50022. SSF50022. 1 hit.
PROSITEiPS51296. RIESKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), LACK OF ENZYME ACTIVITY.
  2. "Human CMP-N-acetylneuraminic acid hydroxylase is a novel stem cell marker linked to stem cell-specific mechanisms."
    Nystedt J., Anderson H., Hirvonen T., Impola U., Jaatinen T., Heiskanen A., Blomqvist M., Satomaa T., Natunen J., Saarinen J., Lehenkari P., Valmu L., Laine J.
    Stem Cells 28:258-267(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, LACK OF ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The molecular basis for the absence of N-glycolylneuraminic acid in humans."
    Irie A., Koyama S., Kozutsumi Y., Kawasaki T., Suzuki A.
    J. Biol. Chem. 273:15866-15871(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), LACK OF ENZYME ACTIVITY, TISSUE SPECIFICITY.
  5. "Alu-mediated inactivation of the human CMP-N-acetylneuraminic acid hydroxylase gene."
    Hayakawa T., Satta Y., Gagneux P., Varki A., Takahata N.
    Proc. Natl. Acad. Sci. U.S.A. 98:11399-11404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME INACTIVATION.
  6. "Inactivation of CMP-N-acetylneuraminic acid hydroxylase occurred prior to brain expansion during human evolution."
    Chou H.-H., Hayakawa T., Diaz S., Krings M., Indriati E., Leakey M., Paabo S., Satta Y., Takahata N., Varki A.
    Proc. Natl. Acad. Sci. U.S.A. 99:11736-11741(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME INACTIVATION.

Entry informationi

Entry nameiCMAH_HUMAN
AccessioniPrimary (citable) accession number: Q9Y471
Secondary accession number(s): C1K3L2
, O95250, Q5TD41, Q5TD42, Q5TD43, Q5TD44, Q68DC3, Q9UEE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: April 29, 2015
Last modified: April 29, 2015
This is version 89 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

An Alu-mediated mutation of this gene occured in a common ancestor of homo sapiens and homo sapiens neanderthalis, approximately 2.1-2.2 million years ago, before brain expansion. It is generally accepted that the product of this gene, if any, is catalytically inactive as suggested by the absence of CMP-Neu5Gc sialic acid in human, while it is abundantly expressed at the surface of many cells in other vertebrates. The gene is however, significantly transcribed and the product described here might be expressed in vivo (PubMed:19890979). The putative protein is N-terminally truncated compared to orthologs and lacks a region probably essential to the CMP-N-acetylneuraminate monooxygenase activity.4 Publications1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.