ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P32320


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CDD_HUMAN
Primary accession number P32320
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 81)
Name and origin of the protein
Protein name Cytidine deaminase
Synonyms EC 3.5.4.5
Cytidine aminohydrolase
Gene name
Name: CDA
Synonyms: CDD
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=7923172 [NCBI, ExPASy, EBI, Israel, Japan]
Laliberte J., Momparler R.L.;
"Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA.";
Cancer Res. 54:5401-5407(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0167-4781(98)00235-8; PubMed=9878810 [NCBI, ExPASy, EBI, Israel, Japan]
Demontis S., Terao M., Brivio M., Zanotta S., Bruschi M., Garattini E.;
"Isolation and characterization of the gene coding for human cytidine deaminase.";
Biochim. Biophys. Acta 1443:323-333(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
PubMed=9596658 [NCBI, ExPASy, EBI, Israel, Japan]
Gran C., Boyum A., Johansen R.F., Lovhaug D., Seeberg E.C.;
"Growth inhibition of granulocyte-macrophage colony forming cells by human cytidine deaminase requires the catalytic function of the protein.";
Blood 91:4127-4135(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-27.
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-146, AND VARIANT GLN-27.
DOI=10.1006/bbrc.1993.1001; PubMed=8422236 [NCBI, ExPASy, EBI, Israel, Japan]
Kuhn K., Bertling W.M., Emmrich F.;
"Cloning of a functional cDNA for human cytidine deaminase (CDD) and its use as a marker of monocyte/macrophage differentiation.";
Biochem. Biophys. Res. Commun. 190:1-7(1993).
[7]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-146 IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC IONS, AND SUBUNIT.
DOI=10.1021/jm0496279; PubMed=15689149 [NCBI, ExPASy, EBI, Israel, Japan]
Chung S.J., Fromme J.C., Verdine G.L.;
"Structure of human cytidine deaminase bound to a potent inhibitor.";
J. Med. Chem. 48:658-660(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L27943; AAA57254.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061658; AAD15828.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061655; AAD15828.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061656; AAD15828.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061657; AAD15828.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ000474; CAA04113.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391357; CAH73474.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054036; AAH54036.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S52873; AAB24946.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I52710; I52710.
RefSeq NP_001776.1; -.
UniGene Hs.466910
3D structure databases
PDB
1MQ0; X-ray; 2.40 A; A/B=11-146.[ExPASy / RCSB / EBI]
PDBsum 1MQ0; -.
ModBase P32320.
PTM databases
PhosphoSite P32320; -.
Enzyme and pathway databases
Reactome REACT_1698; Nucleotide metabolism.
Organism-specific databases
H-InvDB HIX0023648; -.
HGNC HGNC:1712; CDA.
GenAtlas CDA.
MIM 123920; gene. [NCBI / EBI]
PharmGKB PA24644; -.
GeneCards P32320.
Gene expression databases
ArrayExpress P32320; -.
CleanEx HS_CDA; -.
GermOnline ENSG00000158825; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from UniProtKB).
GO:0005576; Cellular component: extracellular region (traceable author statement from UniProtKB).
GO:0004126; Molecular function: cytidine deaminase activity (inferred from direct assay from UniProtKB).
GO:0001882; Molecular function: nucleoside binding (inferred from direct assay from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (inferred from direct assay from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0007166; Biological process: cell surface receptor linked signal transduction (non-traceable author statement from UniProtKB).
GO:0009972; Biological process: cytidine deamination (inferred from direct assay from UniProtKB).
GO:0019858; Biological process: cytosine metabolic process (traceable author statement from UniProtKB).
GO:0030308; Biological process: negative regulation of cell growth (inferred from direct assay from UniProtKB).
GO:0045980; Biological process: negative regulation of nucleotide metabolic process (inferred from direct assay from UniProtKB).
GO:0051289; Biological process: protein homotetramerization (inferred from direct assay from UniProtKB).
GO:0008655; Biological process: pyrimidine salvage (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016192; APOBEC/CMP_deaminase_Zn-bd.
IPR002125; CMP_dCMP_Zn_bd.
IPR006262; Cyt_deam_tetra.
Graphical view of domain structure.
PANTHER PTHR11644:SF2; Cyt_deam_tetra; 1.
Pfam PF00383; dCMP_cyt_deam_1; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01354; cyt_deam_tetra; 1.
PROSITE PS00903; CYT_DCMP_DEAMINASES; 1.
BLOCKS P32320.
ProtoNet P32320.
Proteomic databases
PeptideAtlas P32320; -.
Genome annotation databases
Ensembl ENSG00000158825; Homo sapiens. [Contig view]
GeneID 978; -.
KEGG hsa:978; -.
Phylogenomic databases
HOGENOM P32320; -.
HOVERGEN P32320; -.
Other
DrugBank DB00928; Azacitidine.
DB01101; Capecitabine.
DB00987; Cytarabine.
DB00441; Gemcitabine.
NextBio 4112; -.
SOURCE CDA; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Hydrolase; Metal-binding; Polymorphism; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   146  146     Cytidine deaminase. PRO_0000171682
REGION   54    60  7     Substrate binding. 
ACT_SITE   67    67        Proton donor. 
METAL   65    65        Zinc; catalytic. 
METAL   99    99        Zinc; catalytic. 
METAL   102   102        Zinc; catalytic. 
VARIANT   27    27  1     K -> Q (in dbSNP:rs2072671 [NCBI]). VAR_021559 [3D]
HELIX   15    25  11      
HELIX   26    28  3      
TURN   32    34  3      
STRAND   38    43  6      
STRAND   49    53  5      
HELIX   60    62  3      
HELIX   66    76  11      
STRAND   83    90  8      
HELIX   100   107  8      
STRAND   111   118  8      
STRAND   124   128  5      
HELIX   129   132  4      
HELIX   139   141  3      
Sequence information
Length: 146 AA [This is the length of the unprocessed precursor] Molecular weight: 16185 Da [This is the MW of the unprocessed precursor] CRC64: AF33D09EE4E176B3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQKRPACTL KPECVQQLLV CSQEAKKSAY CPYSHFPVGA ALLTQEGRIF KGCNIENACY 

        70         80         90        100        110        120 
PLGICAERTA IQKAVSEGYK DFRAIAIASD MQDDFISPCG ACRQVMREFG TNWPVYMTKP 

       130        140 
DGTYIVMTVQ ELLPSSFGPE DLQKTQ 

P32320 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!