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P32321

- DCTD_HUMAN

UniProt

P32321 - DCTD_HUMAN

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Protein
Deoxycytidylate deaminase
Gene
DCTD
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Zinc.

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; catalytic
Active sitei86 – 861Proton donor By similarity
Metal bindingi110 – 1101Zinc; catalytic
Metal bindingi113 – 1131Zinc; catalytic

GO - Molecular functioni

  1. dCMP deaminase activity Source: Reactome
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. nucleobase-containing small molecule metabolic process Source: Reactome
  2. nucleotide biosynthetic process Source: UniProtKB-KW
  3. pyrimidine nucleobase metabolic process Source: Reactome
  4. pyrimidine nucleoside biosynthetic process Source: Reactome
  5. pyrimidine nucleotide metabolic process Source: ProtInc
  6. small molecule metabolic process Source: Reactome
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: Chromosome 4

Organism-specific databases

HGNCiHGNC:2710. DCTD.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 178178Deoxycytidylate deaminase
PRO_0000171691Add
BLAST

Proteomic databases

MaxQBiP32321.
PaxDbiP32321.
PRIDEiP32321.

PTM databases

PhosphoSiteiP32321.

Expressioni

Gene expression databases

ArrayExpressiP32321.
BgeeiP32321.
CleanExiHS_DCTD.
GenevestigatoriP32321.

Organism-specific databases

HPAiHPA035894.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi108003. 7 interactions.
IntActiP32321. 4 interactions.
MINTiMINT-3013156.
STRINGi9606.ENSP00000349576.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP32321.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2131.
HOGENOMiHOG000015715.
HOVERGENiHBG025823.
InParanoidiP32321.
KOiK01493.
OMAiKCNKIII.
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 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

MSEVSCKKRD DYLEWPEYFM AVAFLSAQRS KDPNSQVGAC IVNSENKIVG    50
IGYNGMPNGC SDDVLPWRRT AENKLDTKYP YVCHAELNAI MNKNSTDVKG 100
CSMYVALFPC NECAKLIIQA GIKEVIFMSD KYHDSDEATA ARLLFNMAGV 150
TFRKFIPKCS KIVIDFDSIN SRPSQKLQ 178
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MVGGGQPCGPNM in isoform 2.
VSP_038094

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951S → L in AAH01286. 1 Publication
Sequence conflicti128 – 1281M → T in AAA35755. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005262779.1. [P32321-1]
XP_005262837.1. XM_005262780.1. [P32321-1]
UniGeneiHs.183850.

Genome annotation databases

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

Polymorphism databases

DMDMi23503055.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS34108.1. [P32321-2 ]
CCDS3831.1. [P32321-1 ]
PIRi A47288.
I55434.
RefSeqi NP_001012750.1. NM_001012732.1. [P32321-2 ]
NP_001912.2. NM_001921.2. [P32321-1 ]
XP_005262836.1. XM_005262779.1. [P32321-1 ]
XP_005262837.1. XM_005262780.1. [P32321-1 ]
UniGenei Hs.183850.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2W4L X-ray 2.10 A/B/C/D/E/F 5-173 [» ]
ProteinModelPortali P32321.
SMRi P32321. Positions 12-173.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108003. 7 interactions.
IntActi P32321. 4 interactions.
MINTi MINT-3013156.
STRINGi 9606.ENSP00000349576.

Chemistry

ChEMBLi CHEMBL5675.

PTM databases

PhosphoSitei P32321.

Polymorphism databases

DMDMi 23503055.

Proteomic databases

MaxQBi P32321.
PaxDbi P32321.
PRIDEi P32321.

Protocols and materials databases

DNASUi 1635.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357067 ; ENSP00000349576 ; ENSG00000129187 . [P32321-2 ]
ENST00000438320 ; ENSP00000398194 ; ENSG00000129187 . [P32321-1 ]
ENST00000510370 ; ENSP00000424017 ; ENSG00000129187 . [P32321-1 ]
GeneIDi 1635.
KEGGi hsa:1635.
UCSCi uc003ivf.3. human. [P32321-1 ]
uc003ivg.3. human. [P32321-2 ]

Organism-specific databases

CTDi 1635.
GeneCardsi GC04M183811.
HGNCi HGNC:2710. DCTD.
HPAi HPA035894.
MIMi 607638. gene.
neXtProti NX_P32321.
PharmGKBi PA138.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2131.
HOGENOMi HOG000015715.
HOVERGENi HBG025823.
InParanoidi P32321.
KOi K01493.
OMAi KCNKIII.
OrthoDBi EOG7JDQZR.
PhylomeDBi P32321.
TreeFami TF105971.

Enzyme and pathway databases

BioCyci MetaCyc:HS05252-MONOMER.
Reactomei REACT_21376. Pyrimidine biosynthesis.
SABIO-RK P32321.

Miscellaneous databases

ChiTaRSi DCTD. human.
EvolutionaryTracei P32321.
GenomeRNAii 1635.
NextBioi 6716.
PROi P32321.
SOURCEi Search...

Gene expression databases

ArrayExpressi P32321.
Bgeei P32321.
CleanExi HS_DCTD.
Genevestigatori P32321.

Family and domain databases

InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view ]
PANTHERi PTHR11086. PTHR11086. 1 hit.
Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMi SSF53927. SSF53927. 1 hit.
PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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: September 3, 2014
This is version 137 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

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