Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Deoxycytidylate deaminase

Gene

DCTD

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

Functioni

Supplies the nucleotide substrate for thymidylate synthetase.

Catalytic activityi

dCMP + H2O = dUMP + NH3.

Cofactori

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi84 – 841Zinc; catalytic1 Publication
Active sitei86 – 861Proton donorBy similarity
Metal bindingi110 – 1101Zinc; catalytic1 Publication
Metal bindingi113 – 1131Zinc; catalytic1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS05252-MONOMER.
ReactomeiREACT_21376. Pyrimidine biosynthesis.
SABIO-RKP32321.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxycytidylate deaminase (EC:3.5.4.12)
Alternative name(s):
dCMP deaminase
Gene namesi
Name:DCTD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:2710. DCTD.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA138.

Chemistry

DrugBankiDB00987. Cytarabine.

Polymorphism and mutation databases

BioMutaiDCTD.
DMDMi23503055.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 178178Deoxycytidylate deaminasePRO_0000171691Add
BLAST

Proteomic databases

MaxQBiP32321.
PaxDbiP32321.
PRIDEiP32321.

PTM databases

PhosphoSiteiP32321.

Expressioni

Gene expression databases

BgeeiP32321.
CleanExiHS_DCTD.
ExpressionAtlasiP32321. baseline and differential.
GenevisibleiP32321. HS.

Organism-specific databases

HPAiHPA035894.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FGF12P613283EBI-739870,EBI-6657662
GORASP2Q9H8Y83EBI-739870,EBI-739467
MALSU1Q96EH33EBI-739870,EBI-2339737
SDCBPO005603EBI-739870,EBI-727004
TXN2Q997573EBI-739870,EBI-2932492

Protein-protein interaction databases

BioGridi108003. 11 interactions.
IntActiP32321. 9 interactions.
MINTiMINT-3013156.
STRINGi9606.ENSP00000349576.

Structurei

Secondary structure

1
178
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2713Combined sources
Beta strandi38 – 425Combined sources
Beta strandi48 – 558Combined sources
Turni62 – 643Combined sources
Helixi74 – 763Combined sources
Turni79 – 813Combined sources
Helixi85 – 917Combined sources
Beta strandi102 – 1076Combined sources
Helixi111 – 1199Combined sources
Beta strandi124 – 1296Combined sources
Turni131 – 1344Combined sources
Helixi136 – 14813Combined sources
Beta strandi151 – 1544Combined sources
Beta strandi160 – 1656Combined sources
Helixi166 – 1683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W4LX-ray2.10A/B/C/D/E/F5-173[»]
ProteinModelPortaliP32321.
SMRiP32321. Positions 12-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32321.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 145132CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2131.
GeneTreeiENSGT00390000000501.
HOGENOMiHOG000015715.
HOVERGENiHBG025823.
InParanoidiP32321.
KOiK01493.
OMAiCSDDVFP.
OrthoDBiEOG7JDQZR.
PhylomeDBiP32321.
TreeFamiTF105971.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P32321-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSEVSCKKRD DYLEWPEYFM AVAFLSAQRS KDPNSQVGAC IVNSENKIVG
60 70 80 90 100
IGYNGMPNGC SDDVLPWRRT AENKLDTKYP YVCHAELNAI MNKNSTDVKG
110 120 130 140 150
CSMYVALFPC NECAKLIIQA GIKEVIFMSD KYHDSDEATA ARLLFNMAGV
160 170
TFRKFIPKCS KIVIDFDSIN SRPSQKLQ
Length:178
Mass (Da):20,016
Last modified:September 19, 2002 - v2
Checksum:i2B8DA5EAC85F3666
GO
Isoform 2 (identifier: P32321-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVGGGQPCGPNM

Show »
Length:189
Mass (Da):21,014
Checksum:i973677A3294EBB97
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951S → L in AAH01286 (PubMed:15489334).Curated
Sequence conflicti128 – 1281M → T in AAA35755 (PubMed:7685356).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MVGGGQPCGPNM in isoform 2. 1 PublicationVSP_038094

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12136 mRNA. Translation: AAA35755.1.
L39874 Genomic DNA. Translation: AAC37579.1.
AK313221 mRNA. Translation: BAG36033.1.
AC079766 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04697.1.
CH471056 Genomic DNA. Translation: EAX04698.1.
CH471056 Genomic DNA. Translation: EAX04700.1.
CH471056 Genomic DNA. Translation: EAX04701.1.
BC001286 mRNA. Translation: AAH01286.1.
BC088357 mRNA. Translation: AAH88357.2.
CCDSiCCDS34108.1. [P32321-2]
CCDS3831.1. [P32321-1]
PIRiA47288.
I55434.
RefSeqiNP_001012750.1. NM_001012732.1. [P32321-2]
NP_001912.2. NM_001921.2. [P32321-1]
XP_005262836.1. XM_005262779.2. [P32321-1]
XP_005262837.1. XM_005262780.2. [P32321-1]
XP_011529976.1. XM_011531674.1. [P32321-1]
UniGeneiHs.183850.

Genome annotation databases

EnsembliENST00000357067; ENSP00000349576; ENSG00000129187. [P32321-2]
ENST00000438320; ENSP00000398194; ENSG00000129187.
ENST00000510370; ENSP00000424017; ENSG00000129187.
GeneIDi1635.
KEGGihsa:1635.
UCSCiuc003ivf.3. human. [P32321-1]
uc003ivg.3. human. [P32321-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12136 mRNA. Translation: AAA35755.1.
L39874 Genomic DNA. Translation: AAC37579.1.
AK313221 mRNA. Translation: BAG36033.1.
AC079766 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04697.1.
CH471056 Genomic DNA. Translation: EAX04698.1.
CH471056 Genomic DNA. Translation: EAX04700.1.
CH471056 Genomic DNA. Translation: EAX04701.1.
BC001286 mRNA. Translation: AAH01286.1.
BC088357 mRNA. Translation: AAH88357.2.
CCDSiCCDS34108.1. [P32321-2]
CCDS3831.1. [P32321-1]
PIRiA47288.
I55434.
RefSeqiNP_001012750.1. NM_001012732.1. [P32321-2]
NP_001912.2. NM_001921.2. [P32321-1]
XP_005262836.1. XM_005262779.2. [P32321-1]
XP_005262837.1. XM_005262780.2. [P32321-1]
XP_011529976.1. XM_011531674.1. [P32321-1]
UniGeneiHs.183850.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W4LX-ray2.10A/B/C/D/E/F5-173[»]
ProteinModelPortaliP32321.
SMRiP32321. Positions 12-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108003. 11 interactions.
IntActiP32321. 9 interactions.
MINTiMINT-3013156.
STRINGi9606.ENSP00000349576.

Chemistry

ChEMBLiCHEMBL5675.
DrugBankiDB00987. Cytarabine.

PTM databases

PhosphoSiteiP32321.

Polymorphism and mutation databases

BioMutaiDCTD.
DMDMi23503055.

Proteomic databases

MaxQBiP32321.
PaxDbiP32321.
PRIDEiP32321.

Protocols and materials databases

DNASUi1635.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357067; ENSP00000349576; ENSG00000129187. [P32321-2]
ENST00000438320; ENSP00000398194; ENSG00000129187.
ENST00000510370; ENSP00000424017; ENSG00000129187.
GeneIDi1635.
KEGGihsa:1635.
UCSCiuc003ivf.3. human. [P32321-1]
uc003ivg.3. human. [P32321-2]

Organism-specific databases

CTDi1635.
GeneCardsiGC04M183811.
HGNCiHGNC:2710. DCTD.
HPAiHPA035894.
MIMi607638. gene.
neXtProtiNX_P32321.
PharmGKBiPA138.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2131.
GeneTreeiENSGT00390000000501.
HOGENOMiHOG000015715.
HOVERGENiHBG025823.
InParanoidiP32321.
KOiK01493.
OMAiCSDDVFP.
OrthoDBiEOG7JDQZR.
PhylomeDBiP32321.
TreeFamiTF105971.

Enzyme and pathway databases

BioCyciMetaCyc:HS05252-MONOMER.
ReactomeiREACT_21376. Pyrimidine biosynthesis.
SABIO-RKP32321.

Miscellaneous databases

ChiTaRSiDCTD. human.
EvolutionaryTraceiP32321.
GenomeRNAii1635.
NextBioi6716.
PROiP32321.
SOURCEiSearch...

Gene expression databases

BgeeiP32321.
CleanExiHS_DCTD.
ExpressionAtlasiP32321. baseline and differential.
GenevisibleiP32321. HS.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Lung.
  3. "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] (ISOFORM 1).
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 2).
    Tissue: Cervix and Testis.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "The crystal structure of human dCMP deaminase."
    Structural genomics consortium (SGC)
    Submitted (NOV-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 5-173 IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiDCTD_HUMAN
AccessioniPrimary (citable) accession number: P32321
Secondary accession number(s): B2R836
, D3DP49, D3DP50, Q5M7Z8, Q9BVD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 19, 2002
Last modified: July 22, 2015
This is version 148 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, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.