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Q16878 (CDO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
Cysteine dioxygenase type 1

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

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
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 + O2 = 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. Ref.9

Tissue specificity

Highly expressed in liver and placenta. Low expression in heart, brain and pancreas. Also detected in hepatoblastoma Hep-G2 cells. Ref.2

Induction

In hepatoblastoma Hep-G2 cells, down-regulated by phorbol 12-myristate 13-acetate (PMA). Ref.2

Post-translational modification

The thioether cross-link between Cys-93 and Tyr-157 plays a structural role through stabilizing the Fe2+ 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.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   PTMThioether bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-cysteine catabolic process

Inferred from electronic annotation. Source: Ensembl

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cysteine metabolic process

Traceable author statement PubMed 12110289. Source: UniProtKB

inflammatory response

Traceable author statement PubMed 12110289. Source: UniProtKB

lactation

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Traceable author statement PubMed 12110289. Source: UniProtKB

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to glucagon

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

sulfur amino acid biosynthetic process

Traceable author statement PubMed 12110289. Source: UniProtKB

sulfur amino acid catabolic process

Traceable author statement. Source: Reactome

sulfur amino acid metabolic process

Traceable author statement. Source: Reactome

taurine biosynthetic process

Traceable author statement PubMed 12871209. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement PubMed 12110289. Source: UniProtKB

   Molecular_functioncysteine dioxygenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ferrous iron binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

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

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

Natural variations

Natural variant451T → I. Ref.1 Ref.3
Corresponds to variant rs1042867 [ dbSNP | Ensembl ].
VAR_023536
Natural variant1431E → Q in a colorectal cancer sample; somatic mutation. Ref.10
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.7

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16878 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Brain.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-143.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z31357 mRNA. Translation: CAA83234.1.
Z23010 mRNA. Translation: CAA80552.1.
D85782 Genomic DNA. Translation: BAA12873.1.
D85777 mRNA. Translation: BAA12872.1.
AK314231 mRNA. Translation: BAG36901.1.
U80055, U60232, U78979 Genomic DNA. Translation: AAB58352.1.
CR536540 mRNA. Translation: CAG38777.1.
CH471086 Genomic DNA. Translation: EAW48957.1.
BC024241 mRNA. Translation: AAH24241.1.
CCDSCCDS4121.1.
PIRS50192.
RefSeqNP_001792.2. NM_001801.2.
UniGeneHs.442378.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IC1X-ray2.70A1-200[»]
ProteinModelPortalQ16878.
SMRQ16878. Positions 6-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107468. 3 interactions.
IntActQ16878. 1 interaction.
STRING9606.ENSP00000250535.

Chemistry

DrugBankDB00151. L-Cysteine.
DB00157. NADH.

PTM databases

PhosphoSiteQ16878.

Polymorphism databases

DMDM76800649.

Proteomic databases

PaxDbQ16878.
PRIDEQ16878.

Protocols and materials databases

DNASU1036.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250535; ENSP00000250535; ENSG00000129596.
GeneID1036.
KEGGhsa:1036.
UCSCuc003krg.3. human.

Organism-specific databases

CTD1036.
GeneCardsGC05M115168.
HGNCHGNC:1795. CDO1.
HPAHPA057503.
MIM603943. gene.
neXtProtNX_Q16878.
PharmGKBPA26327.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG126313.
HOGENOMHOG000177818.
HOVERGENHBG004469.
InParanoidQ16878.
KOK00456.
OMAKMTFWSK.
OrthoDBEOG77M8PK.
PhylomeDBQ16878.
TreeFamTF105636.

Enzyme and pathway databases

BioCycMetaCyc:HS05299-MONOMER.
ReactomeREACT_111217. Metabolism.
SignaLinkQ16878.
UniPathwayUPA00012; UER00537.

Gene expression databases

BgeeQ16878.
CleanExHS_CDO1.
GenevestigatorQ16878.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR010300. Cys_dOase_I.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF05995. CDO_I. 1 hit.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ16878.
GenomeRNAi1036.
NextBio4353.
PROQ16878.
SOURCESearch...

Entry information

Entry nameCDO1_HUMAN
AccessionPrimary (citable) accession number: Q16878
Secondary accession number(s): B2RAK4 expand/collapse secondary AC list , P78513, Q6FHZ8, Q8TB64
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 27, 2005
Last modified: July 9, 2014
This is version 123 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

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 5

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