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P32320

- CDD_HUMAN

UniProt

P32320 - CDD_HUMAN

Protein

Cytidine deaminase

Gene

CDA

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

    This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.

    Catalytic activityi

    Cytidine + H2O = uridine + NH3.
    2'deoxycytidine + H2O = 2'-deoxyuridine + NH3.

    Cofactori

    Zinc.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi65 – 651Zinc; catalytic
    Active sitei67 – 671Proton donor
    Metal bindingi99 – 991Zinc; catalytic
    Metal bindingi102 – 1021Zinc; catalytic

    GO - Molecular functioni

    1. cytidine deaminase activity Source: UniProtKB
    2. nucleoside binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: UniProtKB
    2. cytidine deamination Source: UniProtKB
    3. cytosine metabolic process Source: UniProtKB
    4. negative regulation of cell growth Source: UniProtKB
    5. negative regulation of nucleotide metabolic process Source: UniProtKB
    6. nucleobase-containing small molecule metabolic process Source: Reactome
    7. protein homotetramerization Source: UniProtKB
    8. pyrimidine-containing compound salvage Source: UniProtKB
    9. pyrimidine nucleobase metabolic process Source: Reactome
    10. pyrimidine nucleoside salvage Source: Reactome
    11. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08334-MONOMER.
    ReactomeiREACT_655. Pyrimidine salvage reactions.
    SABIO-RKP32320.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytidine deaminase (EC:3.5.4.5)
    Alternative name(s):
    Cytidine aminohydrolase
    Gene namesi
    Name:CDA
    Synonyms:CDD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1712. CDA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular region Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA98.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 146146Cytidine deaminasePRO_0000171682Add
    BLAST

    Proteomic databases

    MaxQBiP32320.
    PaxDbiP32320.
    PeptideAtlasiP32320.
    PRIDEiP32320.

    PTM databases

    PhosphoSiteiP32320.

    Expressioni

    Tissue specificityi

    Highly expressed in granulocytes while expression is very low in fibroblasts, chondrocytes, monocytes, and T- as well as B-cell lines.

    Gene expression databases

    ArrayExpressiP32320.
    BgeeiP32320.
    CleanExiHS_CDA.
    GenevestigatoriP32320.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi107416. 2 interactions.
    STRINGi9606.ENSP00000364212.

    Structurei

    Secondary structure

    1
    146
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 2511
    Helixi26 – 283
    Turni32 – 343
    Beta strandi38 – 436
    Beta strandi49 – 535
    Helixi60 – 623
    Helixi66 – 7611
    Beta strandi83 – 908
    Helixi100 – 1078
    Beta strandi111 – 1188
    Beta strandi124 – 1285
    Helixi129 – 1324
    Helixi139 – 1413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MQ0X-ray2.40A/B11-146[»]
    ProteinModelPortaliP32320.
    SMRiP32320. Positions 13-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32320.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 116101CMP/dCMP deaminase zinc-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 607Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0295.
    HOGENOMiHOG000014707.
    HOVERGENiHBG005294.
    InParanoidiP32320.
    KOiK01489.
    OMAiTDWAVYM.
    OrthoDBiEOG75B872.
    PhylomeDBiP32320.
    TreeFamiTF314486.

    Family and domain databases

    InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR002125. CMP_dCMP_Zn-bd.
    IPR006262. Cyt_deam_tetra.
    IPR016193. Cytidine_deaminase-like.
    [Graphical view]
    PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53927. SSF53927. 1 hit.
    TIGRFAMsiTIGR01354. cyt_deam_tetra. 1 hit.
    PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32320-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQKRPACTL KPECVQQLLV CSQEAKKSAY CPYSHFPVGA ALLTQEGRIF    50
    KGCNIENACY PLGICAERTA IQKAVSEGYK DFRAIAIASD MQDDFISPCG 100
    ACRQVMREFG TNWPVYMTKP DGTYIVMTVQ ELLPSSFGPE DLQKTQ 146
    Length:146
    Mass (Da):16,185
    Last modified:October 1, 1996 - v2
    Checksum:iAF33D09EE4E176B3
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 271K → Q.2 Publications
    Corresponds to variant rs2072671 [ dbSNP | Ensembl ].
    VAR_021559

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27943 mRNA. Translation: AAA57254.1.
    AF061658
    , AF061655, AF061656, AF061657 Genomic DNA. Translation: AAD15828.1.
    AJ000474 mRNA. Translation: CAA04113.1.
    AL391357 Genomic DNA. Translation: CAH73474.1.
    BC054036 mRNA. Translation: AAH54036.1.
    S52873 mRNA. Translation: AAB24946.1.
    CCDSiCCDS210.1.
    PIRiI52710.
    RefSeqiNP_001776.1. NM_001785.2.
    UniGeneiHs.466910.

    Genome annotation databases

    EnsembliENST00000375071; ENSP00000364212; ENSG00000158825.
    GeneIDi978.
    KEGGihsa:978.
    UCSCiuc001bdk.3. human.

    Polymorphism databases

    DMDMi1705718.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27943 mRNA. Translation: AAA57254.1 .
    AF061658
    , AF061655 , AF061656 , AF061657 Genomic DNA. Translation: AAD15828.1 .
    AJ000474 mRNA. Translation: CAA04113.1 .
    AL391357 Genomic DNA. Translation: CAH73474.1 .
    BC054036 mRNA. Translation: AAH54036.1 .
    S52873 mRNA. Translation: AAB24946.1 .
    CCDSi CCDS210.1.
    PIRi I52710.
    RefSeqi NP_001776.1. NM_001785.2.
    UniGenei Hs.466910.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MQ0 X-ray 2.40 A/B 11-146 [» ]
    ProteinModelPortali P32320.
    SMRi P32320. Positions 13-142.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107416. 2 interactions.
    STRINGi 9606.ENSP00000364212.

    Chemistry

    BindingDBi P32320.
    ChEMBLi CHEMBL4502.
    DrugBanki DB00928. Azacitidine.
    DB01101. Capecitabine.
    DB00987. Cytarabine.
    DB00441. Gemcitabine.

    PTM databases

    PhosphoSitei P32320.

    Polymorphism databases

    DMDMi 1705718.

    Proteomic databases

    MaxQBi P32320.
    PaxDbi P32320.
    PeptideAtlasi P32320.
    PRIDEi P32320.

    Protocols and materials databases

    DNASUi 978.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375071 ; ENSP00000364212 ; ENSG00000158825 .
    GeneIDi 978.
    KEGGi hsa:978.
    UCSCi uc001bdk.3. human.

    Organism-specific databases

    CTDi 978.
    GeneCardsi GC01P020915.
    HGNCi HGNC:1712. CDA.
    MIMi 123920. gene.
    neXtProti NX_P32320.
    PharmGKBi PA98.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0295.
    HOGENOMi HOG000014707.
    HOVERGENi HBG005294.
    InParanoidi P32320.
    KOi K01489.
    OMAi TDWAVYM.
    OrthoDBi EOG75B872.
    PhylomeDBi P32320.
    TreeFami TF314486.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08334-MONOMER.
    Reactomei REACT_655. Pyrimidine salvage reactions.
    SABIO-RK P32320.

    Miscellaneous databases

    ChiTaRSi CDA. human.
    EvolutionaryTracei P32320.
    GeneWikii Cytidine_deaminase.
    GenomeRNAii 978.
    NextBioi 4112.
    PROi P32320.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P32320.
    Bgeei P32320.
    CleanExi HS_CDA.
    Genevestigatori P32320.

    Family and domain databases

    InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR002125. CMP_dCMP_Zn-bd.
    IPR006262. Cyt_deam_tetra.
    IPR016193. Cytidine_deaminase-like.
    [Graphical view ]
    Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53927. SSF53927. 1 hit.
    TIGRFAMsi TIGR01354. cyt_deam_tetra. 1 hit.
    PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA."
      Laliberte J., Momparler R.L.
      Cancer Res. 54:5401-5407(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Isolation and characterization of the gene coding for human cytidine deaminase."
      Demontis S., Terao M., Brivio M., Zanotta S., Bruschi M., Garattini E.
      Biochim. Biophys. Acta 1443:323-333(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Growth inhibition of granulocyte-macrophage colony forming cells by human cytidine deaminase requires the catalytic function of the protein."
      Gran C., Boyum A., Johansen R.F., Lovhaug D., Seeberg E.C.
      Blood 91:4127-4135(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANT GLN-27.
      Tissue: Liver.
    6. "Cloning of a functional cDNA for human cytidine deaminase (CDD) and its use as a marker of monocyte/macrophage differentiation."
      Kuhn K., Bertling W.M., Emmrich F.
      Biochem. Biophys. Res. Commun. 190:1-7(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-146, VARIANT GLN-27.
    7. "Structure of human cytidine deaminase bound to a potent inhibitor."
      Chung S.J., Fromme J.C., Verdine G.L.
      J. Med. Chem. 48:658-660(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-146 IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC IONS, SUBUNIT.

    Entry informationi

    Entry nameiCDD_HUMAN
    AccessioniPrimary (citable) accession number: P32320
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 139 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 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3