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Q16878

- CDO1_HUMAN

UniProt

Q16878 - CDO1_HUMAN

Protein

Cysteine dioxygenase type 1

Gene

CDO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (27 Sep 2005)
      Previous versions | rss
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    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. 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

    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

    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)

    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

    1
    200
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16878.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cysteine dioxygenase family.Curated

    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

    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:
    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

    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: October 1, 2014
    This is version 125 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