Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A4D256

- CC14C_HUMAN

UniProt

A4D256 - CC14C_HUMAN

Protein

Dual specificity protein phosphatase CDC14C

Gene

CDC14C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 2 (24 Nov 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Dual-specificity phosphatase. Preferentially dephosphorylates proteins modified by proline-directed kinases By similarity.By similarity

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    GO - Molecular functioni

    1. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
    2. protein tyrosine phosphatase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase CDC14C (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    CDC14 cell division cycle 14 homolog C
    Gene namesi
    Name:CDC14C
    Synonyms:CDC14B2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:22427. CDC14C.

    Subcellular locationi

    Membrane Curated; Single-pass membrane protein Curated. Nucleusnucleolus
    Note: Nucleolar during interphase.By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 554554Dual specificity protein phosphatase CDC14CPRO_0000315822Add
    BLAST

    Proteomic databases

    PaxDbiA4D256.
    PRIDEiA4D256.

    PTM databases

    PhosphoSiteiA4D256.

    Expressioni

    Gene expression databases

    CleanExiHS_CDC14C.
    GenevestigatoriA4D256.

    Organism-specific databases

    HPAiHPA013312.

    Structurei

    3D structure databases

    ProteinModelPortaliA4D256.
    SMRiA4D256. Positions 119-456.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei522 – 54423HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni121 – 275155ABy similarityAdd
    BLAST
    Regioni276 – 28914LinkerBy similarityAdd
    BLAST
    Regioni290 – 456167BBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi78 – 13154Nucleolar localization signalBy similarityAdd
    BLAST

    Domaini

    Composed of two structurally equivalent A and B domains that adopt a dual specificity protein phosphatase (DSP) fold.

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2453.
    HOVERGENiHBG050818.
    PhylomeDBiA4D256.

    Family and domain databases

    Gene3Di3.90.190.10. 2 hits.
    InterProiIPR029260. DSPn.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PfamiPF00782. DSPc. 1 hit.
    PF14671. DSPn. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 2 hits.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A4D256-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNEVSSECGK KCEPLGCSST NGDLQGEAGA VVSIFLRMVP RIKSNEGYGY    50
    SNRNWRKENT MHSLDRNIVD GGQALGQWKR KSKGRSSWAA APHCSPRCSL 100
    TSQGVKKMRS STLQDPRRRD PQDDVYVDIT DRLRFAILYS RPKSASNVHY 150
    FSIDNELEYE NFSEDFGPLN LAMVYRYCCK INKKLKSITM LRKKIVHFTG 200
    SDQRKQANAA FLVGCYMVIY LGRTPEAAYR ILIFGDTPYI PFRDAAYGSC 250
    NFYITLLDCF HAVKKAMQYG FLNFNSFNLD EYEHYEKAEN GDLNWIIPDR 300
    FIAFCGPHSR ARLESGYHQH SPETYIQYFK NHNVTTIIRL NKRMYDAKRF 350
    TDAGFDHHDL FFADGSTPTD AIVKRFLDIC ENAEGAIAVH CKAGLGRTGT 400
    LIACYIMKHY RMTAAETIAW VRICRPGLVI GPQQQFLVMK QTSLWLEGDY 450
    FRQRLKGQEN GQHRAAFSKL LSGVDDISIN GVENQDQQEP KPYSDDDEIN 500
    GVTQGDRSRA LKRRRQSKTN DILLPSPLAV LTFTLCSVVI WWIVCDYILP 550
    ILLF 554
    Length:554
    Mass (Da):63,299
    Last modified:November 24, 2009 - v2
    Checksum:i22B7014D4C2A60A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 8818GGQAL…GRSSW → LIGRGRLQEAEKQGAVEL in BC068452. (PubMed:15489334)CuratedAdd
    BLAST
    Sequence conflicti75 – 784LGQW → AASR in BC028690. (PubMed:15489334)Curated
    Sequence conflicti78 – 781W → R in ABB92421. (PubMed:16201836)Curated
    Sequence conflicti93 – 931H → L in EAL23906. (PubMed:12690205)Curated
    Sequence conflicti96 – 961P → Q in EAL23906. (PubMed:12690205)Curated
    Sequence conflicti102 – 1021S → L in EAL23906. (PubMed:12690205)Curated
    Sequence conflicti103 – 1031Q → P in BC068452. (PubMed:15489334)Curated
    Sequence conflicti103 – 1031Q → P in ABB92421. (PubMed:16201836)Curated
    Sequence conflicti119 – 1191R → W in EAL23906. (PubMed:12690205)Curated
    Sequence conflicti127 – 1271V → L in EAL23906. (PubMed:12690205)Curated
    Sequence conflicti127 – 1271V → L in BC028690. (PubMed:15489334)Curated
    Sequence conflicti454 – 4541R → K in EAL23906. (PubMed:12690205)Curated
    Sequence conflicti494 – 4941S → G in EAL23906. (PubMed:12690205)Curated
    Sequence conflicti494 – 4941S → G in BC068452. (PubMed:15489334)Curated
    Sequence conflicti494 – 4941S → G in ABB92421. (PubMed:16201836)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti238 – 2381P → S.
    Corresponds to variant rs1615556 [ dbSNP | Ensembl ].
    VAR_038327
    Natural varianti296 – 2961I → L.
    Corresponds to variant rs421206 [ dbSNP | Ensembl ].
    VAR_038328

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC006024 Genomic DNA. No translation available.
    CH236955 Genomic DNA. Translation: EAL23906.1.
    BC028690 mRNA. No translation available.
    BC068452 mRNA. No translation available.
    DQ120635 Genomic DNA. Translation: ABB92421.1.
    UniGeneiHs.567757.

    Genome annotation databases

    UCSCiuc010kyv.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC006024 Genomic DNA. No translation available.
    CH236955 Genomic DNA. Translation: EAL23906.1 .
    BC028690 mRNA. No translation available.
    BC068452 mRNA. No translation available.
    DQ120635 Genomic DNA. Translation: ABB92421.1 .
    UniGenei Hs.567757.

    3D structure databases

    ProteinModelPortali A4D256.
    SMRi A4D256. Positions 119-456.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei A4D256.

    Proteomic databases

    PaxDbi A4D256.
    PRIDEi A4D256.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi uc010kyv.1. human.

    Organism-specific databases

    GeneCardsi GC07P048960.
    H-InvDB HIX0033628.
    HGNCi HGNC:22427. CDC14C.
    HPAi HPA013312.
    neXtProti NX_A4D256.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOVERGENi HBG050818.
    PhylomeDBi A4D256.

    Miscellaneous databases

    PROi A4D256.

    Gene expression databases

    CleanExi HS_CDC14C.
    Genevestigatori A4D256.

    Family and domain databases

    Gene3Di 3.90.190.10. 2 hits.
    InterProi IPR029260. DSPn.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    Pfami PF00782. DSPc. 1 hit.
    PF14671. DSPn. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 2 hits.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 71-554.
      Tissue: Testis.
    4. "Emergence of young human genes after a burst of retroposition in primates."
      Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.
      PLoS Biol. 3:E357-E357(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-536.

    Entry informationi

    Entry nameiCC14C_HUMAN
    AccessioniPrimary (citable) accession number: A4D256
    Secondary accession number(s): Q2VIP7, Q6NUS3, Q8NCT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 62 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

    Miscellaneous

    May act as an autosomal functional substitute.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3