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P36874

- PP1GA_XENLA

UniProt

P36874 - PP1GA_XENLA

Protein

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A

Gene

ppp1cc-a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (03 Mar 2009)
      Previous versions | rss
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    Functioni

    Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis By similarity. Promotes nuclear envelope reassembly by targeting nuclear membrane vesicles to chromatin at the end of mitosis. Acts by dephosphorylating membrane proteins such as lamin B receptor (lbr) to regulate the binding of membrane proteins to chromatin.By similarity1 Publication

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi64 – 641Manganese 1By similarity
    Metal bindingi66 – 661Manganese 1By similarity
    Metal bindingi92 – 921Manganese 1By similarity
    Metal bindingi92 – 921Manganese 2By similarity
    Metal bindingi124 – 1241Manganese 2By similarity
    Active sitei125 – 1251Proton donorBy similarity
    Metal bindingi173 – 1731Manganese 2By similarity
    Metal bindingi248 – 2481Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein serine/threonine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. glycogen metabolic process Source: UniProtKB-KW
    2. mitotic nuclear division Source: UniProtKB-KW
    3. mitotic nuclear envelope reassembly Source: UniProtKB
    4. protein dephosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism, Mitosis

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A (EC:3.1.3.16)
    Short name:
    PP-1G-A
    Short name:
    xPP1-gamma1
    Gene namesi
    Name:ppp1cc-a
    Synonyms:ppp1cc
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-967940. ppp1cc.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus By similarity. Nucleusnucleolus By similarity. Cleavage furrow By similarity. Nucleusnucleoplasm By similarity. Chromosomecentromerekinetochore By similarity. Nucleus speckle By similarity. Midbody By similarity. Mitochondrion By similarity. Membrane 1 Publication

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB-SubCell
    2. condensed chromosome kinetochore Source: UniProtKB-SubCell
    3. membrane Source: UniProtKB
    4. midbody Source: UniProtKB-SubCell
    5. mitochondrion Source: UniProtKB
    6. nuclear speck Source: UniProtKB-SubCell
    7. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Kinetochore, Membrane, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Serine/threonine-protein phosphatase PP1-gamma catalytic subunit APRO_0000058790Add
    BLAST

    Proteomic databases

    PRIDEiP36874.

    Interactioni

    Subunit structurei

    PP1 comprises a catalytic subunit, ppp1c1, ppp1cb or ppp1cc, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then is complexed to one or several targeting or regulatory subunits.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    casp2Q9IB672EBI-2908704,EBI-7207360
    cenpeO422632EBI-2908704,EBI-2607221

    Protein-protein interaction databases

    IntActiP36874. 2 interactions.
    MINTiMINT-7978751.

    Structurei

    3D structure databases

    ProteinModelPortaliP36874.
    SMRiP36874. Positions 6-300.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

    Phylogenomic databases

    HOVERGENiHBG000216.
    KOiK06269.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P36874-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADVDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP    50
    ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS 100
    LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK 150
    TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL 200
    LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV 250
    VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE 300
    KKKPNASRPV TPPRGMITKQ AKK 323
    Length:323
    Mass (Da):36,956
    Last modified:March 3, 2009 - v2
    Checksum:i8CD4C5DE036A8C2B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti213 – 2131V → I in AAA49934. 1 PublicationCurated
    Sequence conflicti220 – 2201D → Y in AAA49934. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB106881 mRNA. Translation: BAF51554.1.
    L17039 mRNA. Translation: AAA49934.1.
    BC090213 mRNA. Translation: AAH90213.1.
    RefSeqiNP_001081308.1. NM_001087839.1.
    UniGeneiXl.6679.

    Genome annotation databases

    GeneIDi397767.
    KEGGixla:397767.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB106881 mRNA. Translation: BAF51554.1 .
    L17039 mRNA. Translation: AAA49934.1 .
    BC090213 mRNA. Translation: AAH90213.1 .
    RefSeqi NP_001081308.1. NM_001087839.1.
    UniGenei Xl.6679.

    3D structure databases

    ProteinModelPortali P36874.
    SMRi P36874. Positions 6-300.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P36874. 2 interactions.
    MINTi MINT-7978751.

    Proteomic databases

    PRIDEi P36874.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397767.
    KEGGi xla:397767.

    Organism-specific databases

    Xenbasei XB-GENE-967940. ppp1cc.

    Phylogenomic databases

    HOVERGENi HBG000216.
    KOi K06269.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nuclear envelope precursor vesicle targeting to chromatin is stimulated by protein phosphatase 1 in Xenopus egg extracts."
      Ito H., Koyama Y., Takano M., Ishii K., Maeno M., Furukawa K., Horigome T.
      Exp. Cell Res. 313:1897-1910(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
      Tissue: Oocyte.
    2. "The C-terminus of Xenopus protein phosphatase 1-gamma1 determines its cell cycle-dependent regulation and phosphorylation."
      Walker D.H., Rempel R., Maller J.L.
      Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. NIH - Xenopus Gene Collection (XGC) project
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Egg.

    Entry informationi

    Entry nameiPP1GA_XENLA
    AccessioniPrimary (citable) accession number: P36874
    Secondary accession number(s): Q5EAX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 95 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3