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Reviewed, UniProtKB/Swiss-Prot P32321 (DCTD_HUMAN)

Last modified June 16, 2009. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Deoxycytidylate deaminase
    EC=3.5.4.12
Alternative name(s):
    dCMP deaminase
Gene names
Name: DCTD
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Supplies the nucleotide substrate for thymidylate synthetase.

Catalytic activity

dCMP + H2O = dUMP + NH3.

Cofactor

Zinc.

Enzyme regulation

Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP.

Subunit structure

Homohexamer.

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Direct protein sequencing
Gene Ontology (GO)
   Biological processnucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

pyrimidine nucleotide metabolic process Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytosol Ref.1

Inferred from Experiment. Source: Reactome

   Molecular functiondCMP deaminase activity Ref.1

Inferred from Experiment. Source: Reactome

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 178178Deoxycytidylate deaminase
PRO_0000171691

Sites

Active site861Proton donor By similarity
Metal binding841Zinc; catalytic By similarity
Metal binding1101Zinc; catalytic By similarity
Metal binding1131Zinc; catalytic By similarity

Amino acid modifications

Modified residue791Phosphotyrosine Ref.4

Experimental info

Sequence conflict951S → L in AAH01286. Ref.3
Sequence conflict1281M → T in AAA35755. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32321-1 [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: 2B8DA5EAC85F3666

FASTA17820,016
        10         20         30         40         50         60 
MSEVSCKKRD DYLEWPEYFM AVAFLSAQRS KDPNSQVGAC IVNSENKIVG IGYNGMPNGC 

        70         80         90        100        110        120 
SDDVLPWRRT AENKLDTKYP YVCHAELNAI MNKNSTDVKG CSMYVALFPC NECAKLIIQA 

       130        140        150        160        170 
GIKEVIFMSD KYHDSDEATA ARLLFNMAGV TFRKFIPKCS KIVIDFDSIN SRPSQKLQ 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of human deoxycytidylate deaminase and overexpression of its functional protein in Escherichia coli."
Weiner K.X., Weiner R.S., Maley F., Maley G.F.
J. Biol. Chem. 268:12983-12989(1993) [PubMed: 7685356] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Chromosomal location and structural organization of the human deoxycytidylate deaminase gene."
Weiner K.X., Ciesla J., Jaffe A.B., Ketring R., Maley F., Maley G.F.
J. Biol. Chem. 270:18727-18729(1995) [PubMed: 7642519] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lung.
[3]"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: Cervix.
[4]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-79, MASS SPECTROMETRY.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

L12136 mRNA. Translation: AAA35755.1.
L39874 Genomic DNA. Translation: AAC37579.1.
BC001286 mRNA. Translation: AAH01286.1.
IPIIPI00296863.
PIRA47288.
I55434.
RefSeqNP_001912.2.
UniGeneHs.183850

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2W4LX-ray2.10A/B/C/D/E/F5-173[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP32321. 5 interactions.

PTM databases

PhosphoSiteP32321.

Proteomic databases

PRIDEP32321.

Genome annotation databases

EnsemblENSG00000129187. Homo sapiens. [Contig view]
GeneID1635.

Organism-specific databases

GeneCardsGC04M184048.
H-InvDBHIX0004657.
HGNCHGNC:2710. DCTD.
MIM607638. gene.
PharmGKBPA138.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP32321.

Enzyme and pathway databases

BRENDA3.5.4.12. 247.
ReactomeREACT_1698. Nucleotide metabolism.

Gene expression databases

ArrayExpressP32321.
BgeeP32321.
CleanExHS_DCTD.
GermOnlineENSG00000129187. Homo sapiens.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn_bd.
IPR015517. Cyt_deaminase.
IPR016473. dCMP_deaminase.
[Graphical view]
PANTHERPTHR11086. Cyt_deaminase. 1 hit.
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFPIRSF006019. dCMP_deaminase. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio6716.
SOURCESearch...

Entry information

Entry nameDCTD_HUMAN
AccessionPrimary (citable) accession number: P32321
Secondary accession number(s): Q9BVD8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 19, 2002
Last modified: June 16, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents