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Reviewed, UniProtKB/Swiss-Prot Q16878 (CDO1_HUMAN)

Last modified November 25, 2008. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cysteine dioxygenase type 1
    EC=1.13.11.20
Alternative name(s):
    Cysteine dioxygenase type I
      Short name=CDO-I
      Short name=CDO
Gene names
Name: CDO1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range.

Catalytic activity

L-cysteine + O(2) = 3-sulfinoalanine.

Cofactor

Binds 1 iron ion per subunit. Zinc to a much lesser extent.

Pathway

Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

Subunit structure

Monomer.

Tissue specificity

Highly expressed in liver and placenta. Low expression in heart, brain and pancreas. Also detected in hepatoblastoma HepG2 cells.

Induction

In hepatoblastoma HepG2 cells, down-regulated by phorbol 12-myristate 13-acetate.

Post-translational modification

The thioether cross-link between Cys-93 and Tyr-157 plays a structural role through stabilizing the ferrous ion, and prevents the production of highly damaging free hydroxyl radicals by holding the oxygen radical via hydroxyl hydrogen.

Sequence similarities

Belongs to the cysteine dioxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200Cysteine dioxygenase type 1
PRO_0000206606

Sites

Metal binding861Iron; catalytic
Metal binding881Iron; catalytic
Metal binding1401Iron; catalytic

Amino acid modifications

Modified residue591Phosphothreonine
Cross-link93 ↔ 1573'-(S-cysteinyl)-tyrosine (Cys-Tyr)

Natural variations

Natural variant451T → I: dbSNP rs1042867.
VAR_023536
Natural variant1431E → Q in a colorectal cancer sample; somatic mutation.
VAR_036170

Experimental info

Mutagenesis601R → Q: Reduces enzyme activity by 70%. Reduces iron and zinc incorporation by 50%
Mutagenesis931C → S: Reduces enzyme activity and iron incorporation by 50%. Zinc incorporation increased by 20%
Mutagenesis1571Y → F: Almost total loss of enzyme activity and iron incorporation. Reduces zinc incorporation by 20%
Mutagenesis1641C → S: Reduces enzyme activity by 20%. Little effect on iron incorporation. No effect on zinc incorporation
Sequence conflict1371I → V in AAH24241. Ref.5

Secondary structure

........................................ 200
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16878-1 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: E4EF87221D05C14D

FASTA20022,972
        10         20         30         40         50         60 
MEQTEVLKPR TLADLIRILH QLFAGDEVNV EEVQAIMEAY ESDPTEWAMY AKFDQYRYTR 

        70         80         90        100        110        120 
NLVDQGNGKF NLMILCWGEG HGSSIHDHTN SHCFLKMLQG NLKETLFAWP DKKSNEMVKK 

       130        140        150        160        170        180 
SERVLRENQC AYINDSIGLH RVENISHTEP AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT 

       190        200 
FHSKFGIRTP NATSGSLENN 

« Hide

References

« Hide 'large scale' references
[1]"Human cysteine dioxygenase type I: primary structure derived from base sequencing of cDNA."
McCann K.P., Akbari M.T., Williams A.C., Ramsden D.B.
Biochim. Biophys. Acta 1209:107-110(1994) [PubMed: 7524679] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-45.
Tissue: Liver.
[2]"Human cysteine dioxygenase gene: structural organization, tissue-specific expression and downregulation by phorbol 12-myristate 13-acetate."
Tsuboyama-Kasaoka N., Hosokawa Y., Kodama H., Matsumoto A., Oka J., Totani M.
Biosci. Biotechnol. Biochem. 63:1017-1024(1999) [PubMed: 10427686] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, TISSUE SPECIFICITY.
Tissue: Liver.
[3]"Human cysteine dioxygenase type I (CDO-I; EC 1.13.11.20): 5' flanking region and intron-exon structure of the gene."
Ramsden D.B., Kapadi A.L., Fitch N.J., Farmer M.J., Bennett P., Williams A.C.
Mol. Pathol. 50:269-271(1997) [PubMed: 9497919] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-45.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor."
Ye S., Wu X., Wei L., Tang D., Sun P., Bartlam M., Rao Z.
J. Biol. Chem. 282:3391-3402(2007) [PubMed: 17135237] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-200 OF WILD-TYPE AND MUTANTS ARG-60; CYS-93; TYR-157 AND CYS-164 IN COMPLEX WITH L-CYSTEINE AND DIVALENT METAL IONS, CROSS-LINK, SUBUNIT, MASS SPECTROMETRY.
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-143.
+Additional computationally mapped references.

Cross-references

Sequence databases

Z31357 mRNA. Translation: CAA83234.1.
Z23010 mRNA. Translation: CAA80552.1.
D85782 Genomic DNA. Translation: BAA12873.1.
D85777 mRNA. Translation: BAA12872.1.
U80055, U60232, U78979 Genomic DNA. Translation: AAB58352.1.
CR536540 mRNA. Translation: CAG38777.1.
BC024241 mRNA. Translation: AAH24241.1.
PIRS50192.
RefSeqNP_001792.2.
UniGeneHs.442378

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2IC1X-ray2.70A2-200[»]
ModBaseSearch...

PTM databases

PhosphoSiteQ16878.

Genome annotation databases

EnsemblENSG00000129596. Homo sapiens. [Contig view]
GeneID1036.
KEGGhsa:1036.

Organism-specific databases

HGNCHGNC:1795. CDO1.
MIM603943. gene.
PharmGKBPA26327.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ16878.
HOVERGENQ16878.

Gene expression databases

ArrayExpressQ16878.
CleanExHS_CDO1.
GermOnlineENSG00000129596. Homo sapiens.

Family and domain databases

InterProIPR010300. Cys_dOase_I.
[Graphical view]
PfamPF05995. CDO_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00151. L-Cysteine.
DB00157. NADH.
NextBio4353.
SOURCESearch...

Entry information

Entry nameCDO1_HUMAN
AccessionPrimary (citable) accession number: Q16878
Secondary accession number(s): P78513, Q6FHZ8, Q8TB64
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 27, 2005
Last modified: November 25, 2008
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents