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P32321

- DCTD_HUMAN

UniProt

P32321 - DCTD_HUMAN

Protein

Deoxycytidylate deaminase

Gene

DCTD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      Previous versions | rss
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    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; catalytic1 Publication
    Active sitei86 – 861Proton donorBy similarity
    Metal bindingi110 – 1101Zinc; catalytic1 Publication
    Metal bindingi113 – 1131Zinc; catalytic1 Publication

    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

    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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA138.

    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

    ArrayExpressiP32321.
    BgeeiP32321.
    CleanExiHS_DCTD.
    GenevestigatoriP32321.

    Organism-specific databases

    HPAiHPA035894.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    178
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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:
    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

    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: October 1, 2014
    This is version 138 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