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Protein

Cysteine dioxygenase type 1

Gene

CDO1

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

Functioni

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 activityi

L-cysteine + O2 = 3-sulfinoalanine.

Cofactori

Fe2+Note: Binds 1 Fe(2+) cation per subunit. Zn2+ can be used to a much lesser extent.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi86 – 861Iron; catalytic1 Publication
Metal bindingi88 – 881Iron; catalytic1 Publication
Metal bindingi140 – 1401Iron; catalytic1 Publication

GO - Molecular functioni

  1. cysteine dioxygenase activity Source: UniProtKB
  2. ferrous iron binding Source: Ensembl

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. cysteine metabolic process Source: UniProtKB
  3. inflammatory response Source: UniProtKB
  4. lactation Source: Ensembl
  5. L-cysteine catabolic process Source: Ensembl
  6. oxidation-reduction process Source: UniProtKB
  7. response to amino acid Source: Ensembl
  8. response to cAMP Source: Ensembl
  9. response to ethanol Source: Ensembl
  10. response to glucagon Source: Ensembl
  11. response to glucocorticoid Source: Ensembl
  12. small molecule metabolic process Source: Reactome
  13. sulfur amino acid biosynthetic process Source: UniProtKB
  14. sulfur amino acid catabolic process Source: Reactome
  15. sulfur amino acid metabolic process Source: Reactome
  16. taurine biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05299-MONOMER.
ReactomeiREACT_115654. Degradation of cysteine and homocysteine.
SignaLinkiQ16878.
UniPathwayiUPA00012; UER00537.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CDO1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:1795. CDO1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601R → Q: Reduces enzyme activity by 70%. Reduces iron and zinc incorporation by 50%.
Mutagenesisi93 – 931C → S: Reduces enzyme activity and iron incorporation by 50%. Zinc incorporation increased by 20%.
Mutagenesisi157 – 1571Y → F: Almost total loss of enzyme activity and iron incorporation. Reduces zinc incorporation by 20%.
Mutagenesisi164 – 1641C → S: Reduces enzyme activity by 20%. Little effect on iron incorporation. No effect on zinc incorporation.

Organism-specific databases

PharmGKBiPA26327.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 200200Cysteine dioxygenase type 1PRO_0000206606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki93 ↔ 1573'-(S-cysteinyl)-tyrosine (Cys-Tyr)1 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Thioether bond

Proteomic databases

PaxDbiQ16878.
PRIDEiQ16878.

PTM databases

PhosphoSiteiQ16878.

Expressioni

Tissue specificityi

Highly expressed in liver and placenta. Low expression in heart, brain and pancreas. Also detected in hepatoblastoma Hep-G2 cells.1 Publication

Inductioni

In hepatoblastoma Hep-G2 cells, down-regulated by phorbol 12-myristate 13-acetate (PMA).1 Publication

Gene expression databases

BgeeiQ16878.
CleanExiHS_CDO1.
GenevestigatoriQ16878.

Organism-specific databases

HPAiHPA036573.
HPA057503.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi107468. 3 interactions.
IntActiQ16878. 1 interaction.
STRINGi9606.ENSP00000250535.

Structurei

Secondary structure

1
200
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 2211Combined sources
Helixi30 – 3910Combined sources
Helixi44 – 474Combined sources
Helixi48 – 503Combined sources
Beta strandi55 – 573Combined sources
Beta strandi59 – 646Combined sources
Helixi66 – 683Combined sources
Beta strandi71 – 777Combined sources
Beta strandi92 – 1009Combined sources
Beta strandi102 – 1076Combined sources
Beta strandi119 – 1246Combined sources
Beta strandi130 – 1334Combined sources
Turni135 – 1373Combined sources
Beta strandi139 – 1446Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi151 – 1599Combined sources
Beta strandi162 – 1676Combined sources
Turni169 – 1713Combined sources
Beta strandi174 – 1785Combined sources
Beta strandi182 – 1843Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IC1X-ray2.70A1-200[»]
ProteinModelPortaliQ16878.
SMRiQ16878. Positions 6-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16878.

Family & Domainsi

Sequence similaritiesi

Belongs to the cysteine dioxygenase family.Curated

Phylogenomic databases

eggNOGiNOG126313.
GeneTreeiENSGT00390000018226.
HOGENOMiHOG000177818.
HOVERGENiHBG004469.
InParanoidiQ16878.
KOiK00456.
OMAiCFMKLLQ.
OrthoDBiEOG77M8PK.
PhylomeDBiQ16878.
TreeFamiTF105636.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR010300. Cys_dOase_I.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF05995. CDO_I. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

Q16878-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQTEVLKPR TLADLIRILH QLFAGDEVNV EEVQAIMEAY ESDPTEWAMY
60 70 80 90 100
AKFDQYRYTR NLVDQGNGKF NLMILCWGEG HGSSIHDHTN SHCFLKMLQG
110 120 130 140 150
NLKETLFAWP DKKSNEMVKK SERVLRENQC AYINDSIGLH RVENISHTEP
160 170 180 190 200
AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT FHSKFGIRTP NATSGSLENN
Length:200
Mass (Da):22,972
Last modified:September 27, 2005 - v2
Checksum:iE4EF87221D05C14D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371I → V in AAH24241 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451T → I.2 Publications
Corresponds to variant rs1042867 [ dbSNP | Ensembl ].
VAR_023536
Natural varianti143 – 1431E → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036170

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4121.1.
PIRiS50192.
RefSeqiNP_001792.2. NM_001801.2.
UniGeneiHs.442378.

Genome annotation databases

EnsembliENST00000250535; ENSP00000250535; ENSG00000129596.
GeneIDi1036.
KEGGihsa:1036.
UCSCiuc003krg.3. human.

Polymorphism databases

DMDMi76800649.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4121.1.
PIRiS50192.
RefSeqiNP_001792.2. NM_001801.2.
UniGeneiHs.442378.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IC1X-ray2.70A1-200[»]
ProteinModelPortaliQ16878.
SMRiQ16878. Positions 6-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107468. 3 interactions.
IntActiQ16878. 1 interaction.
STRINGi9606.ENSP00000250535.

Chemistry

DrugBankiDB00151. L-Cysteine.

PTM databases

PhosphoSiteiQ16878.

Polymorphism databases

DMDMi76800649.

Proteomic databases

PaxDbiQ16878.
PRIDEiQ16878.

Protocols and materials databases

DNASUi1036.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000250535; ENSP00000250535; ENSG00000129596.
GeneIDi1036.
KEGGihsa:1036.
UCSCiuc003krg.3. human.

Organism-specific databases

CTDi1036.
GeneCardsiGC05M115140.
HGNCiHGNC:1795. CDO1.
HPAiHPA036573.
HPA057503.
MIMi603943. gene.
neXtProtiNX_Q16878.
PharmGKBiPA26327.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG126313.
GeneTreeiENSGT00390000018226.
HOGENOMiHOG000177818.
HOVERGENiHBG004469.
InParanoidiQ16878.
KOiK00456.
OMAiCFMKLLQ.
OrthoDBiEOG77M8PK.
PhylomeDBiQ16878.
TreeFamiTF105636.

Enzyme and pathway databases

UniPathwayiUPA00012; UER00537.
BioCyciMetaCyc:HS05299-MONOMER.
ReactomeiREACT_115654. Degradation of cysteine and homocysteine.
SignaLinkiQ16878.

Miscellaneous databases

EvolutionaryTraceiQ16878.
GenomeRNAii1036.
NextBioi4353.
PROiQ16878.
SOURCEiSearch...

Gene expression databases

BgeeiQ16878.
CleanExiHS_CDO1.
GenevestigatoriQ16878.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR010300. Cys_dOase_I.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF05995. CDO_I. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-143.

Entry informationi

Entry nameiCDO1_HUMAN
AccessioniPrimary (citable) accession number: Q16878
Secondary accession number(s): B2RAK4
, P78513, Q6FHZ8, Q8TB64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 27, 2005
Last modified: March 4, 2015
This is version 129 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.