SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q16878

- CDO1_HUMAN

UniProt

Q16878 - CDO1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Cysteine dioxygenase type 1
Gene
CDO1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

Pathwayi

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. L-cysteine catabolic process Source: Ensembl
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. cysteine metabolic process Source: UniProtKB
  4. inflammatory response Source: UniProtKB
  5. lactation 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 1
PRO_0000206606Add
BLAST

Amino acid modifications

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

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.

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

HPAiHPA057503.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IC1X-ray2.70A1-200[»]
ProteinModelPortaliQ16878.
SMRiQ16878. Positions 6-190.

Miscellaneous databases

EvolutionaryTraceiQ16878.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG126313.
HOGENOMiHOG000177818.
HOVERGENiHBG004469.
InParanoidiQ16878.
KOiK00456.
OMAiKMTFWSK.
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

MEQTEVLKPR TLADLIRILH QLFAGDEVNV EEVQAIMEAY ESDPTEWAMY    50
AKFDQYRYTR NLVDQGNGKF NLMILCWGEG HGSSIHDHTN SHCFLKMLQG 100
NLKETLFAWP DKKSNEMVKK SERVLRENQC AYINDSIGLH RVENISHTEP 150
AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT FHSKFGIRTP NATSGSLENN 200
Length:200
Mass (Da):22,972
Last modified:September 27, 2005 - v2
Checksum:iE4EF87221D05C14D
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371I → V in AAH24241. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4121.1.
PIRi S50192.
RefSeqi NP_001792.2. NM_001801.2.
UniGenei Hs.442378.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IC1 X-ray 2.70 A 1-200 [» ]
ProteinModelPortali Q16878.
SMRi Q16878. Positions 6-190.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107468. 3 interactions.
IntActi Q16878. 1 interaction.
STRINGi 9606.ENSP00000250535.

Chemistry

DrugBanki DB00151. L-Cysteine.
DB00157. NADH.

PTM databases

PhosphoSitei Q16878.

Polymorphism databases

DMDMi 76800649.

Proteomic databases

PaxDbi Q16878.
PRIDEi Q16878.

Protocols and materials databases

DNASUi 1036.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000250535 ; ENSP00000250535 ; ENSG00000129596 .
GeneIDi 1036.
KEGGi hsa:1036.
UCSCi uc003krg.3. human.

Organism-specific databases

CTDi 1036.
GeneCardsi GC05M115168.
HGNCi HGNC:1795. CDO1.
HPAi HPA057503.
MIMi 603943. gene.
neXtProti NX_Q16878.
PharmGKBi PA26327.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG126313.
HOGENOMi HOG000177818.
HOVERGENi HBG004469.
InParanoidi Q16878.
KOi K00456.
OMAi KMTFWSK.
OrthoDBi EOG77M8PK.
PhylomeDBi Q16878.
TreeFami TF105636.

Enzyme and pathway databases

UniPathwayi UPA00012 ; UER00537 .
BioCyci MetaCyc:HS05299-MONOMER.
Reactomei REACT_115654. Degradation of cysteine and homocysteine.
SignaLinki Q16878.

Miscellaneous databases

EvolutionaryTracei Q16878.
GenomeRNAii 1036.
NextBioi 4353.
PROi Q16878.
SOURCEi Search...

Gene expression databases

Bgeei Q16878.
CleanExi HS_CDO1.
Genevestigatori Q16878.

Family and domain databases

Gene3Di 2.60.120.10. 1 hit.
InterProi IPR010300. Cys_dOase_I.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view ]
Pfami PF05995. CDO_I. 1 hit.
[Graphical view ]
SUPFAMi SSF51182. SSF51182. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 124 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