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A6N3Q4

- CC14C_HYLSY

UniProt

A6N3Q4 - CC14C_HYLSY

Protein

Dual specificity protein phosphatase CDC14C

Gene

CDC14C

Organism
Hylobates syndactylus (Siamang) (Symphalangus syndactylus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 30 (01 Oct 2014)
      Sequence version 1 (24 Jul 2007)
      Previous versions | rss
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    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
    OrganismiHylobates syndactylus (Siamang) (Symphalangus syndactylus)
    Taxonomic identifieri9590 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHylobatidaeSymphalangus

    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 – 483483Dual specificity protein phosphatase CDC14CPRO_0000315823Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliA6N3Q4.
    SMRiA6N3Q4. Positions 41-378.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei444 – 46623HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 197155ABy similarityAdd
    BLAST
    Regioni198 – 21114LinkerBy similarityAdd
    BLAST
    Regioni212 – 378167BBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1 – 5353Nucleolar 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

    HOVERGENiHBG050818.

    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.

    A6N3Q4-1 [UniParc]FASTAAdd to Basket

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    MKRKSEGRSS WAAATCSPCC SLTSPSVKKI RSPTQQDPRH RDPQDDVYLD    50
    ITDRLRLAIL YSRPKSASNV HYFSIDNELE YENFSEDFGP LNLAMVYRYC 100
    CKINKKLKSI TMLRKKIVHF TGSDQRKQAN AAFLVGCYMV IYLGRTPEEA 150
    YRTLIFGDTS YIPFRDAAYG SCNFYITLLD CFHAVKKAMQ YGFLNFNSFN 200
    LDEYEHYEKA ENGDLNWIIP DRFIAFCGPH SRARLESGYH QHSPETYIQY 250
    FKNRNVTTII RLNKKMYDAK CFTDAGFDHH DLFFADGSSP TDAIVKGFLD 300
    ICENAEGAIA VHCKAGLGRT GTLIACYIMK HYRMTAAETI AWVRICRPGL 350
    VIGPQQQFLV MKQTSLWLEG DYFCQKLKGQ ENGQHRAAFP KLHSGVDDIS 400
    INGVENQDQQ EPEPYSDDDE INGGTQGDRL RALKSRRQSK TNAILLTCPL 450
    AVLTSALCSV VIWWIVCDYI LPILLFCLDG FGT 483
    Length:483
    Mass (Da):54,961
    Last modified:July 24, 2007 - v1
    Checksum:i8895A87FEBA3E5F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF606887 Genomic DNA. Translation: ABR10606.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF606887 Genomic DNA. Translation: ABR10606.1 .

    3D structure databases

    ProteinModelPortali A6N3Q4.
    SMRi A6N3Q4. Positions 41-378.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG050818.

    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. "Subcellular adaptation of a hominoid cell cycle protein expressed in the brain."
      Rosso L., Marques A.C., Kaessmann H.
      Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiCC14C_HYLSY
    AccessioniPrimary (citable) accession number: A6N3Q4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 30 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    May act as an autosomal functional substitute.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3