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P11084

- PP4C_RABIT

UniProt

P11084 - PP4C_RABIT

Protein

Serine/threonine-protein phosphatase 4 catalytic subunit

Gene

PPP4C

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on Ser-140 (gamma-H2AFX) generated during DNA replication and required for DNA DSB repair. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase By similarity. In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi54 – 541Manganese 1By similarity
    Metal bindingi56 – 561Manganese 1By similarity
    Metal bindingi82 – 821Manganese 1By similarity
    Metal bindingi82 – 821Manganese 2By similarity
    Metal bindingi114 – 1141Manganese 2By similarity
    Active sitei115 – 1151Proton donorBy similarity
    Metal bindingi164 – 1641Manganese 2By similarity
    Metal bindingi238 – 2381Manganese 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. regulation of double-strand break repair via homologous recombination Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 4 catalytic subunit (EC:3.1.3.16)
    Short name:
    PP4C
    Short name:
    Pp4
    Alternative name(s):
    Protein phosphatase X
    Short name:
    PP-X
    Gene namesi
    Name:PPP4C
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 307306Serine/threonine-protein phosphatase 4 catalytic subunitPRO_0000058885Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei307 – 3071Leucine methyl ester1 Publication

    Keywords - PTMi

    Acetylation, Methylation

    Interactioni

    Subunit structurei

    Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complexes PPP4C-PPP4R1, PPP4C-PPP4R2, PPP4C-PPP4R2-PPP4R3A, PPP4C-PPP4R2-PPP4R3B and PPP4C-PPP4R4. The PPP4C-PPP4R2 complex appears to be a tetramer composed of 2 molecules of PPP4C and 2 molecules of PPP4R2. Interacts with REL, NFKB1/p50 and RELA. Interacts with SMN1 AND GEMIN4. Interacts with IRS4 (phosphorylated). Interacts with SMEK1/PPP4R3A; the interaction requires PP4R2. Interacts with HDAC3 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000005480.

    Structurei

    3D structure databases

    ProteinModelPortaliP11084.
    SMRiP11084. Positions 6-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172696.
    HOVERGENiHBG000216.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11084-1 [UniParc]FASTAAdd to Basket

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    MAEISDLDRQ IEQLLRCELI KESEVKALCA KAREILVEES NVQRVDSPVT    50
    VCGDIHGQFY DLKELFRVGG DVPETNYLFM GDFVDRGFYS VETFLLLLAL 100
    KVRYPDRITL IRGNHESRQI TQVYGFYDEC LRKYGSVTVW RYCTEIFDYL 150
    SLSAIIDGKI FCVHGGLSPS IQTLDQIRTI DRKQEVPHDG PMCDLLWSDP 200
    EDTTGWGVSP RGAGYLFGSD VVAQFNAAND IDMICRAHQL VMEGYKWHFN 250
    ETVLTVWSAP NYCYRCGNVA AILELDEHLQ KDFIIFEAAP QETRGIPSKK 300
    PVADYFL 307
    Length:307
    Mass (Da):35,037
    Last modified:August 1, 1992 - v2
    Checksum:i364A1641F8B22B41
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14031 mRNA. Translation: CAA32191.1.
    S57412 mRNA. Translation: AAB25913.1.
    PIRiS36193. PARBA2.
    RefSeqiNP_001075792.1. NM_001082323.1.
    UniGeneiOcu.3272.

    Genome annotation databases

    GeneIDi100009163.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14031 mRNA. Translation: CAA32191.1 .
    S57412 mRNA. Translation: AAB25913.1 .
    PIRi S36193. PARBA2.
    RefSeqi NP_001075792.1. NM_001082323.1.
    UniGenei Ocu.3272.

    3D structure databases

    ProteinModelPortali P11084.
    SMRi P11084. Positions 6-307.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000005480.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009163.

    Organism-specific databases

    CTDi 5531.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172696.
    HOVERGENi HBG000216.

    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. "Protein serine/threonine phosphatases; an expanding family."
      Cohen P.T.W., Brewis N.D., Hughes V., Mann D.J.
      FEBS Lett. 268:355-359(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: New Zealand white.
      Tissue: Liver.
    2. "PPX, a novel protein serine/threonine phosphatase localized to centrosomes."
      Brewis N.D., Street A.J., Prescott A.R., Cohen P.T.W.
      EMBO J. 12:987-996(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: New Zealand white.
      Tissue: Liver.
    3. "Identification of a novel protein phosphatase catalytic subunit by cDNA cloning."
      da Cruz e Silva O.B., da Cruz e Silva E.F., Cohen P.T.W.
      FEBS Lett. 242:106-110(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-307.
      Strain: New Zealand white.
      Tissue: Liver.
    4. "Carboxymethylation of nuclear protein serine/threonine phosphatase X."
      Kloeker S., Bryant J.C., Strack S., Colbran R.J., Wadzinski B.E.
      Biochem. J. 327:481-486(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LEU-307.
    5. "A novel 50 kDa protein forms complexes with protein phosphatase 4 and is located at centrosomal microtubule organizing centres."
      Hastie C.J., Carnegie G.K., Morrice N., Cohen P.T.W.
      Biochem. J. 347:845-855(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP4R2.

    Entry informationi

    Entry nameiPP4C_RABIT
    AccessioniPrimary (citable) accession number: P11084
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3