Q16878 (CDO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 100.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 200 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 HepG2 cells. Ref.2 |
| Induction | In hepatoblastoma HepG2 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 diversity | Polymorphism |
| Ligand | Iron Metal-binding |
| Molecular function | Dioxygenase Oxidoreductase |
| PTM | Phosphoprotein Thioether bond |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | inflammatory response Traceable author statement. Source: UniProtKB sulfur amino acid biosynthetic processTraceable author statement. Source: UniProtKB taurine biosynthetic processTraceable author statement. Source: UniProtKB |
| Cellular component | cytosol Traceable author statement. Source: UniProtKB |
| Molecular function | cysteine dioxygenase activity Inferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 200 | 200 | Cysteine dioxygenase type 1 | PRO_0000206606 | ||||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 86 | 1 | Iron; catalytic | |||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 88 | 1 | Iron; catalytic | |||||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 140 | 1 | Iron; catalytic | |||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 59 | 1 | Phosphothreonine Ref.8 | |||||||||||||||||||||||||||||||||||||||||||||
| Cross-link | 93 ↔ 157 | 3'-(S-cysteinyl)-tyrosine (Cys-Tyr) | ||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 45 | 1 | T → I. Ref.1 Ref.3 Corresponds to variant rs1042867 [ dbSNP | Ensembl ]. | VAR_023536 | ||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 143 | 1 | E → Q in a colorectal cancer sample; somatic mutation. Ref.10 | VAR_036170 | ||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 60 | 1 | R → Q: Reduces enzyme activity by 70%. Reduces iron and zinc incorporation by 50%. | |||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 93 | 1 | C → S: Reduces enzyme activity and iron incorporation by 50%. Zinc incorporation increased by 20%. | |||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 157 | 1 | Y → F: Almost total loss of enzyme activity and iron incorporation. Reduces zinc incorporation by 20%. | |||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 164 | 1 | C → S: Reduces enzyme activity by 20%. Little effect on iron incorporation. No effect on zinc incorporation. | |||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 137 | 1 | I → V in AAH24241. Ref.7 | |||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 12 – 22 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 30 – 39 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 44 – 47 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 48 – 50 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 55 – 57 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 64 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 66 – 68 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 71 – 77 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 92 – 100 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 102 – 107 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 119 – 124 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 130 – 133 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 135 – 137 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 139 – 144 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 147 – 149 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 151 – 159 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 162 – 167 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 169 – 171 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 174 – 178 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 182 – 184 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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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] | "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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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. 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [8] | "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: Cervix carcinoma. |
| [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: 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. |
| [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. 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 | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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. | ||||||||||||
| IPI | IPI00294447. | ||||||||||||
| PIR | S50192. | ||||||||||||
| RefSeq | NP_001792.2. NM_001801.2. | ||||||||||||
| UniGene | Hs.442378. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q16878. | ||||||||||||
| SMR | Q16878. Positions 6-190. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q16878. 1 interaction. | ||||||||||||
| STRING | Q16878. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q16878. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 76800649. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q16878. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000250535; ENSP00000250535; ENSG00000129596. | ||||||||||||
| GeneID | 1036. | ||||||||||||
| KEGG | hsa:1036. | ||||||||||||
| UCSC | uc003krg.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 1036. | ||||||||||||
| GeneCards | GC05M115168. | ||||||||||||
| H-InvDB | HIX0005104. | ||||||||||||
| HGNC | HGNC:1795. CDO1. | ||||||||||||
| HPA | HPA036573. | ||||||||||||
| MIM | 603943. gene. | ||||||||||||
| neXtProt | NX_Q16878. | ||||||||||||
| PharmGKB | PA26327. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | prNOG10157. | ||||||||||||
| GeneTree | ENSGT00390000018226. | ||||||||||||
| HOGENOM | HBG380588. | ||||||||||||
| HOVERGEN | HBG004469. | ||||||||||||
| InParanoid | Q16878. | ||||||||||||
| OMA | NDELGLH. | ||||||||||||
| OrthoDB | EOG4W6NWZ. | ||||||||||||
| PhylomeDB | Q16878. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q16878. | ||||||||||||
| Bgee | Q16878. | ||||||||||||
| CleanEx | HS_CDO1. | ||||||||||||
| Genevestigator | Q16878. | ||||||||||||
| GermOnline | ENSG00000129596. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR011051. Cupin_RmlC_type. IPR010300. Cys_dOase_I. IPR014710. RmlC-like_jellyroll. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit. | ||||||||||||
| KO | K00456. | ||||||||||||
| Pfam | PF05995. CDO_I. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF51182. RmlC_like_cupin. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| DrugBank | DB00151. L-Cysteine. DB00157. NADH. | ||||||||||||
| NextBio | 4353. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | CDO1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q16878 Secondary accession number(s): B2RAK4 Q8TB64 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with