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Q8NE62 (CHDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Choline dehydrogenase, mitochondrial

Short name=CDH
Short name=CHD
EC=1.1.99.1
Gene names
Name:CHDH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Choline + acceptor = betaine aldehyde + reduced acceptor.

Cofactor

FAD By similarity.

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1.

Subcellular location

Mitochondrion inner membrane By similarity.

Sequence similarities

Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycine betaine biosynthetic process from choline

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncholine dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion By similarity
Chain30 – 594565Choline dehydrogenase, mitochondrial
PRO_0000012329

Regions

Nucleotide binding42 – 7130FAD By similarity

Sites

Active site5111 By similarity

Amino acid modifications

Modified residue4361N6-succinyllysine By similarity
Modified residue4841N6-acetyllysine; alternate By similarity
Modified residue4841N6-succinyllysine; alternate By similarity
Modified residue4961N6-acetyllysine; alternate By similarity
Modified residue4961N6-succinyllysine; alternate By similarity
Modified residue5801N6-acetyllysine By similarity

Natural variations

Natural variant401E → A.
Corresponds to variant rs9001 [ dbSNP | Ensembl ].
VAR_020421
Natural variant781L → R. Ref.2
Corresponds to variant rs12676 [ dbSNP | Ensembl ].
VAR_055097
Natural variant4411N → S.
Corresponds to variant rs34974961 [ dbSNP | Ensembl ].
VAR_049357

Experimental info

Sequence conflict1131R → A in CAB75961. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8NE62 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: E9764CD0F325A501

FASTA59465,358
        10         20         30         40         50         60 
MWCLLRGLGR PGALARGALG QQQSLGARAL ASAGSESRDE YSYVVVGAGS AGCVLAGRLT 

        70         80         90        100        110        120 
EDPAERVLLL EAGPKDVLAG SKRLSWKIHM PAALVANLCD DRYNWCYHTE VQRGLDGRVL 

       130        140        150        160        170        180 
YWPRGRVWGG SSSLNAMVYV RGHAEDYERW QRQGARGWDY AHCLPYFRKA QGHELGASRY 

       190        200        210        220        230        240 
RGADGPLRVS RGKTNHPLHC AFLEATQQAG YPLTEDMNGF QQEGFGWMDM TIHEGKRWSA 

       250        260        270        280        290        300 
ACAYLHPALS RTNLKAEAET LVSRVLFEGT RAVGVEYVKN GQSHRAYASK EVILSGGAIN 

       310        320        330        340        350        360 
SPQLLMLSGI GNADDLKKLG IPVVCHLPGV GQNLQDHLEI YIQQACTRPI TLHSAQKPLR 

       370        380        390        400        410        420 
KVCIGLEWLW KFTGEGATAH LETGGFIRSQ PGVPHPDIQF HFLPSQVIDH GRVPTQQEAY 

       430        440        450        460        470        480 
QVHVGPMRGT SVGWLKLRSA NPQDHPVIQP NYLSTETDIE DFRLCVKLTR EIFAQEALAP 

       490        500        510        520        530        540 
FRGKELQPGS HIQSDKEIDA FVRAKADSAY HPSCTCKMGQ PSDPTAVVDP QTRVLGVENL 

       550        560        570        580        590 
RVVDASIMPS MVSGNLNAPT IMIAEKAADI IKGQPALWDK DVPVYKPRTL ATQR 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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], VARIANT ARG-78.
Tissue: Testis.
[3]"Analysis of a putative tumor suppressor gene region of 100 kb at chromosome 3p21.1 in conventional renal cell carcinoma."
Bugert P., Hanke S., Chudek J., Kovacs G.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 113-594.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC012467 Genomic DNA. No translation available.
BC034502 mRNA. Translation: AAH34502.1.
AJ272267 mRNA. Translation: CAB75961.1.
RefSeqNP_060867.2. NM_018397.4.
UniGeneHs.126688.
Hs.729536.

3D structure databases

ProteinModelPortalQ8NE62.
SMRQ8NE62. Positions 41-568.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120629. 3 interactions.
IntActQ8NE62. 2 interactions.
STRING9606.ENSP00000319851.

Chemistry

DrugBankDB00122. Choline.

PTM databases

PhosphoSiteQ8NE62.

Polymorphism databases

DMDM229462828.

Proteomic databases

PaxDbQ8NE62.
PRIDEQ8NE62.

Protocols and materials databases

DNASU55349.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315251; ENSP00000319851; ENSG00000016391.
GeneID55349.
KEGGhsa:55349.
UCSCuc003dgz.3. human.

Organism-specific databases

CTD55349.
GeneCardsGC03M053850.
HGNCHGNC:24288. CHDH.
HPAHPA036633.
neXtProtNX_Q8NE62.
PharmGKBPA134873121.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2303.
HOGENOMHOG000139600.
HOVERGENHBG023639.
InParanoidQ8NE62.
KOK00108.
OMAMWCLLRG.
OrthoDBEOG7DFXBR.
PhylomeDBQ8NE62.
TreeFamTF313911.

Enzyme and pathway databases

BioCycMetaCyc:HS00375-MONOMER.
UniPathwayUPA00529; UER00385.

Gene expression databases

ArrayExpressQ8NE62.
BgeeQ8NE62.
CleanExHS_CHDH.
GenevestigatorQ8NE62.

Family and domain databases

InterProIPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFPIRSF000137. Alcohol_oxidase. 1 hit.
PROSITEPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHDH. human.
GenomeRNAi55349.
NextBio59691.
PROQ8NE62.

Entry information

Entry nameCHDH_HUMAN
AccessionPrimary (citable) accession number: Q8NE62
Secondary accession number(s): Q9NY17
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 5, 2009
Last modified: March 19, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM