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P62136

- PP1A_HUMAN

UniProt

P62136 - PP1A_HUMAN

Protein

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Gene

PPP1CA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (21 Jun 2004)
      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. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.2 Publications

    Catalytic activityi

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

    Cofactori

    Binds 1 iron ion per subunit.By similarity
    Binds 2 manganese ions per subunit.1 Publication

    Enzyme regulationi

    The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress.1 Publication

    Sites

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

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphatase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein serine/threonine phosphatase activity Source: ProtInc
    5. ribonucleoprotein complex binding Source: Ensembl

    GO - Biological processi

    1. branching morphogenesis of an epithelial tube Source: Ensembl
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB-KW
    4. circadian regulation of gene expression Source: UniProtKB
    5. entrainment of circadian clock by photoperiod Source: UniProtKB
    6. glycogen metabolic process Source: UniProtKB-KW
    7. lung development Source: Ensembl
    8. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    9. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    10. protein dephosphorylation Source: UniProtKB
    11. regulation of circadian rhythm Source: UniProtKB
    12. regulation of glycogen biosynthetic process Source: Ensembl
    13. regulation of glycogen catabolic process Source: Ensembl
    14. small molecule metabolic process Source: Reactome
    15. transforming growth factor beta receptor signaling pathway Source: Reactome
    16. triglyceride catabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_15334. DARPP-32 events.
    REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
    SignaLinkiP62136.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (EC:3.1.3.16)
    Short name:
    PP-1A
    Gene namesi
    Name:PPP1CA
    Synonyms:PPP1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9281. PPP1CA.

    Subcellular locationi

    Cytoplasm. Nucleus. Nucleusnucleoplasm. Nucleusnucleolus
    Note: Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this protein to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. dendritic spine Source: Ensembl
    4. extracellular vesicular exosome Source: UniProt
    5. glycogen granule Source: Ensembl
    6. MLL5-L complex Source: UniProtKB
    7. nucleolus Source: UniProtKB-SubCell
    8. nucleus Source: UniProtKB
    9. perikaryon Source: Ensembl
    10. protein phosphatase type 1 complex Source: Ensembl
    11. PTW/PP1 phosphatase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33609.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 330329Serine/threonine-protein phosphatase PP1-alpha catalytic subunitPRO_0000058774Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei305 – 3051N6-acetyllysineBy similarity
    Modified residuei306 – 3061PhosphotyrosineBy similarity
    Modified residuei320 – 3201Phosphothreonine4 Publications

    Post-translational modificationi

    Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP62136.
    PaxDbiP62136.
    PRIDEiP62136.

    2D gel databases

    OGPiP08129.

    PTM databases

    PhosphoSiteiP62136.

    Expressioni

    Gene expression databases

    ArrayExpressiP62136.
    BgeeiP62136.
    CleanExiHS_PPP1CA.
    GenevestigatoriP62136.

    Organism-specific databases

    HPAiCAB004545.

    Interactioni

    Subunit structurei

    PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts with PPP1R39 By similarity. Interacts with PPP1R9A and PPP1R9B. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with PHACTR4; which acts as an activator of PP1 activity By similarity. Interacts with PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8. Interacts with HHV-1 ICP34.5. Interacts with PPP1R16B. Interacts with RPSA only in the presence of PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of PPP1R10/PNUTS. Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site. Interacts with isoform 1 and isoform 4 of NEK2. Interacts with FER; this promotes phosphorylation at Thr-320. Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction.By similarity16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKT1P317496EBI-357253,EBI-296087
    APAF1O147272EBI-357253,EBI-446492
    AXIN1O151694EBI-357253,EBI-710484
    BRCA1P383982EBI-357253,EBI-349905
    CASC5Q8NG312EBI-357253,EBI-1001161
    CD2BP2O954002EBI-357253,EBI-768015
    CDH1P128302EBI-357253,EBI-727477
    CEP192Q8TEP82EBI-357253,EBI-2339778
    CHCHD3Q9NX632EBI-357253,EBI-743375
    ClockO087852EBI-357253,EBI-79859From a different organism.
    CNSTQ6PJW83EBI-357253,EBI-750390
    CSRNP2Q9H1753EBI-357253,EBI-5235958
    DLG3Q927962EBI-357253,EBI-80440
    ELLP551992EBI-357253,EBI-1245868
    MPHOSPH10O005662EBI-357253,EBI-5235884
    PPP1R13BQ96KQ45EBI-357253,EBI-1105153
    PPP1R13LQ8WUF54EBI-357253,EBI-5550163
    PPP1R15BQ5SWA13EBI-357253,EBI-2815482
    PPP1R2P412362EBI-357253,EBI-1056517
    PPP1R26Q5T8A72EBI-357253,EBI-308500
    PPP1R27Q86WC62EBI-357253,EBI-5235602
    PPP1R32Q7Z5V63EBI-357253,EBI-4311771
    PPP1R37O758642EBI-357253,EBI-5235692
    PPP1R8Q129723EBI-357253,EBI-716633
    PPP1R9BQ96SB35EBI-357253,EBI-351275
    PTENP604842EBI-357253,EBI-696162
    RB1P064002EBI-357253,EBI-491274
    RL1P363134EBI-357253,EBI-6149234From a different organism.
    SFI1A8K8P32EBI-357253,EBI-743371
    SGOL2Q562F64EBI-357253,EBI-989213
    SH2D4AQ9H7882EBI-357253,EBI-747035
    SH3RF2Q8TEC53EBI-357253,EBI-2130111
    SKP1P632083EBI-357253,EBI-307486
    SPRED1Q7Z6994EBI-357253,EBI-5235340
    SYTL2Q9HCH52EBI-357253,EBI-2690103
    TMEM132DQ14C872EBI-357253,EBI-5235567
    TP53BP2Q136257EBI-357253,EBI-77642
    TRPC4APQ8TEL62EBI-357253,EBI-2559060
    TSC2P498152EBI-357253,EBI-396587
    WNK1Q9H4A32EBI-357253,EBI-457907
    ZFYVE1Q9HBF42EBI-357253,EBI-4401611
    ZFYVE9O954053EBI-357253,EBI-296817

    Protein-protein interaction databases

    BioGridi111493. 216 interactions.
    DIPiDIP-221N.
    DIP-38195N.
    IntActiP62136. 217 interactions.
    MINTiMINT-5001223.
    STRINGi9606.ENSP00000326031.

    Structurei

    Secondary structure

    1
    330
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 1810
    Turni19 – 213
    Helixi32 – 4817
    Beta strandi51 – 555
    Beta strandi57 – 626
    Helixi69 – 7911
    Beta strandi87 – 893
    Beta strandi94 – 985
    Helixi100 – 11314
    Turni115 – 1173
    Beta strandi118 – 1203
    Helixi128 – 1347
    Helixi136 – 1438
    Helixi146 – 15611
    Beta strandi162 – 1654
    Turni166 – 1683
    Beta strandi169 – 1713
    Helixi184 – 1874
    Beta strandi197 – 1993
    Helixi200 – 2067
    Beta strandi214 – 2185
    Beta strandi222 – 2276
    Helixi229 – 23911
    Beta strandi242 – 2465
    Beta strandi254 – 2585
    Turni259 – 2624
    Beta strandi263 – 2675
    Helixi272 – 2743
    Beta strandi280 – 2856
    Beta strandi291 – 2966

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3E7AX-ray1.63A/B7-300[»]
    3E7BX-ray1.70A/B7-300[»]
    3EGGX-ray1.85A/B7-330[»]
    3EGHX-ray2.00A/B7-330[»]
    3HVQX-ray2.20A/B7-330[»]
    3N5UX-ray3.20A/B1-300[»]
    3V4YX-ray2.10A/C/E/G7-307[»]
    4G9JX-ray3.10A/B1-330[»]
    4MOVX-ray1.45A/B7-300[»]
    4MOYX-ray2.20A7-300[»]
    4MP0X-ray2.10A/C7-300[»]
    ProteinModelPortaliP62136.
    SMRiP62136. Positions 7-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62136.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172697.
    HOVERGENiHBG000216.
    KOiK06269.
    OMAiMGDVMNI.
    OrthoDBiEOG7TJ3K3.
    PhylomeDBiP62136.
    TreeFamiTF354243.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P62136-1) [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

    MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP    50
    ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS 100
    LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK 150
    TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL 200
    LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV 250
    VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD 300
    KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK 330
    Length:330
    Mass (Da):37,512
    Last modified:June 21, 2004 - v1
    Checksum:i60C37E1AD9831DAC
    GO
    Isoform 2 (identifier: P62136-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         18-18: E → EGSRVLTPHCAP

    Note: No experimental confirmation available.

    Show »
    Length:341
    Mass (Da):38,631
    Checksum:iCE50F8B9DC84AB6F
    GO
    Isoform 3 (identifier: P62136-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         19-62: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:286
    Mass (Da):32,595
    Checksum:iE0560E7C422C353C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei18 – 181E → EGSRVLTPHCAP in isoform 2. 1 PublicationVSP_043377
    Alternative sequencei19 – 6244Missing in isoform 3. CuratedVSP_046754Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70848 mRNA. Translation: CAA50197.1.
    S57501 mRNA. Translation: AAB26015.1.
    M63960 mRNA. Translation: AAA36508.1.
    AK313586 mRNA. Translation: BAG36355.1.
    BT006629 mRNA. Translation: AAP35275.1.
    AP003419 Genomic DNA. No translation available.
    BC001888 mRNA. Translation: AAH01888.1.
    BC004482 mRNA. Translation: AAH04482.1.
    BC008010 mRNA. Translation: AAH08010.1.
    J04759 mRNA. Translation: AAA36475.1.
    CCDSiCCDS31618.1. [P62136-2]
    CCDS8160.1. [P62136-1]
    CCDS8161.1. [P62136-3]
    RefSeqiNP_001008709.1. NM_001008709.1. [P62136-2]
    NP_002699.1. NM_002708.3. [P62136-1]
    NP_996756.1. NM_206873.1. [P62136-3]
    UniGeneiHs.183994.

    Genome annotation databases

    EnsembliENST00000312989; ENSP00000326031; ENSG00000172531. [P62136-2]
    ENST00000358239; ENSP00000350974; ENSG00000172531. [P62136-3]
    ENST00000376745; ENSP00000365936; ENSG00000172531. [P62136-1]
    GeneIDi5499.
    KEGGihsa:5499.
    UCSCiuc001oku.1. human. [P62136-2]
    uc001okw.1. human. [P62136-1]

    Polymorphism databases

    DMDMi49065811.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The things we forget - Issue 32 of March 2003

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70848 mRNA. Translation: CAA50197.1 .
    S57501 mRNA. Translation: AAB26015.1 .
    M63960 mRNA. Translation: AAA36508.1 .
    AK313586 mRNA. Translation: BAG36355.1 .
    BT006629 mRNA. Translation: AAP35275.1 .
    AP003419 Genomic DNA. No translation available.
    BC001888 mRNA. Translation: AAH01888.1 .
    BC004482 mRNA. Translation: AAH04482.1 .
    BC008010 mRNA. Translation: AAH08010.1 .
    J04759 mRNA. Translation: AAA36475.1 .
    CCDSi CCDS31618.1. [P62136-2 ]
    CCDS8160.1. [P62136-1 ]
    CCDS8161.1. [P62136-3 ]
    RefSeqi NP_001008709.1. NM_001008709.1. [P62136-2 ]
    NP_002699.1. NM_002708.3. [P62136-1 ]
    NP_996756.1. NM_206873.1. [P62136-3 ]
    UniGenei Hs.183994.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3E7A X-ray 1.63 A/B 7-300 [» ]
    3E7B X-ray 1.70 A/B 7-300 [» ]
    3EGG X-ray 1.85 A/B 7-330 [» ]
    3EGH X-ray 2.00 A/B 7-330 [» ]
    3HVQ X-ray 2.20 A/B 7-330 [» ]
    3N5U X-ray 3.20 A/B 1-300 [» ]
    3V4Y X-ray 2.10 A/C/E/G 7-307 [» ]
    4G9J X-ray 3.10 A/B 1-330 [» ]
    4MOV X-ray 1.45 A/B 7-300 [» ]
    4MOY X-ray 2.20 A 7-300 [» ]
    4MP0 X-ray 2.10 A/C 7-300 [» ]
    ProteinModelPortali P62136.
    SMRi P62136. Positions 7-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111493. 216 interactions.
    DIPi DIP-221N.
    DIP-38195N.
    IntActi P62136. 217 interactions.
    MINTi MINT-5001223.
    STRINGi 9606.ENSP00000326031.

    Chemistry

    BindingDBi P62136.
    ChEMBLi CHEMBL2164.

    PTM databases

    PhosphoSitei P62136.

    Polymorphism databases

    DMDMi 49065811.

    2D gel databases

    OGPi P08129.

    Proteomic databases

    MaxQBi P62136.
    PaxDbi P62136.
    PRIDEi P62136.

    Protocols and materials databases

    DNASUi 5499.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312989 ; ENSP00000326031 ; ENSG00000172531 . [P62136-2 ]
    ENST00000358239 ; ENSP00000350974 ; ENSG00000172531 . [P62136-3 ]
    ENST00000376745 ; ENSP00000365936 ; ENSG00000172531 . [P62136-1 ]
    GeneIDi 5499.
    KEGGi hsa:5499.
    UCSCi uc001oku.1. human. [P62136-2 ]
    uc001okw.1. human. [P62136-1 ]

    Organism-specific databases

    CTDi 5499.
    GeneCardsi GC11M067165.
    HGNCi HGNC:9281. PPP1CA.
    HPAi CAB004545.
    MIMi 176875. gene.
    neXtProti NX_P62136.
    PharmGKBi PA33609.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172697.
    HOVERGENi HBG000216.
    KOi K06269.
    OMAi MGDVMNI.
    OrthoDBi EOG7TJ3K3.
    PhylomeDBi P62136.
    TreeFami TF354243.

    Enzyme and pathway databases

    Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_15334. DARPP-32 events.
    REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
    SignaLinki P62136.

    Miscellaneous databases

    ChiTaRSi PPP1CA. human.
    EvolutionaryTracei P62136.
    GeneWikii PPP1CA.
    GenomeRNAii 5499.
    NextBioi 21272.
    PROi P62136.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62136.
    Bgeei P62136.
    CleanExi HS_PPP1CA.
    Genevestigatori P62136.

    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. "Cloning and characterization of a human protein phosphatase 1-encoding cDNA."
      Song Q., Khanna K.K., Lu H., Lavin M.F.
      Gene 129:291-295(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung.
    2. "The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit."
      Durfee T., Becherer K., Chen P.L., Yeh S.H., Yang Y., Kilburn A.E., Lee W.H., Elledge S.J.
      Genes Dev. 7:555-569(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. Tung L.
      Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    4. "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).
      Tissue: Synovial cell.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Muscle, Pancreas and Placenta.
    8. Bienvenut W.V., Heiserich L., Gottlieb E.
      Submitted (OCT-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15 AND 247-261, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    9. "Localization of the gene encoding a type I protein phosphatase catalytic subunit to human chromosome band 11q13."
      Barker H.M., Jones T.A., da Cruz e Silva E.F., Spurr N.K., Sheer D., Cohen P.T.W.
      Genomics 7:159-166(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-330 (ISOFORM 1).
    10. "The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase."
      He B., Gross M., Roizman B.
      Proc. Natl. Acad. Sci. U.S.A. 94:843-848(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R15A AND HHV-1 ICP34.5.
    11. "Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
      Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
      J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8.
    12. "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1."
      Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.
      Mol. Cell. Biol. 21:6841-6850(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R15A.
    13. "Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1."
      Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W., Bollen M.
      J. Biol. Chem. 277:47331-47337(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R7.
    14. "Protein phosphatase 1 -- targeted in many directions."
      Cohen P.T.W.
      J. Cell Sci. 115:241-256(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    15. "The protein phosphatase-1 targeting subunit TIMAP regulates LAMR1 phosphorylation."
      Kim K., Li L., Kozlowski K., Suh H.S., Cao W., Ballermann B.J.
      Biochem. Biophys. Res. Commun. 338:1327-1334(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R16B AND RPSA.
    16. "A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress."
      Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D., Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.
      Science 307:935-939(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    17. "Downregulation of Fer induces PP1 activation and cell-cycle arrest in malignant cells."
      Pasder O., Shpungin S., Salem Y., Makovsky A., Vilchick S., Michaeli S., Malovani H., Nir U.
      Oncogene 25:4194-4206(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FER, PHOSPHORYLATION AT THR-320.
    18. "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."
      Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.
      Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; RBMX AND NCOA5, INTERACTION WITH YLPM1.
    19. "Protein phosphatase-1alpha regulates centrosome splitting through Nek2."
      Mi J., Guo C., Brautigan D.L., Larner J.M.
      Cancer Res. 67:1082-1089(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NEK2, DEPHOSPHORYLATION.
    20. "Alternative splicing controls nuclear translocation of the cell cycle-regulated Nek2 kinase."
      Wu W., Baxter J.E., Wattam S.L., Hayward D.G., Fardilha M., Knebel A., Ford E.M., da Cruz e Silva E.F., Fry A.M.
      J. Biol. Chem. 282:26431-26440(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEK2.
    21. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NOM1.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
      Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
      Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
    25. "Dab2 stabilizes Axin and attenuates Wnt/beta-catenin signaling by preventing protein phosphatase 1 (PP1)-Axin interactions."
      Jiang Y., Luo W., Howe P.H.
      Oncogene 28:2999-3007(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2.
    26. "Identification and characterization of a novel human PP1 phosphatase complex."
      Lee J.H., You J., Dobrota E., Skalnik D.G.
      J. Biol. Chem. 285:24466-24476(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, INTERACTION WITH WDR82; PPP1R8 AND PPP1R10/PNUTS.
    27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. "SUMOylation of the transcriptional co-repressor KAP1 is regulated by the serine and threonine phosphatase PP1."
      Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.
      Sci. Signal. 3:RA32-RA32(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM28.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock."
      Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.
      PLoS ONE 6:E21325-E21325(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK.
    31. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors."
      Kelker M.S., Page R., Peti W.
      J. Mol. Biol. 385:11-21(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 7-300 IN COMPLEX WITH INHIBITORS, COFACTOR, MANGANESE-BINDING SITES, SUBUNIT.
    33. "Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites."
      Ragusa M.J., Dancheck B., Critton D.A., Nairn A.C., Page R., Peti W.
      Nat. Struct. Mol. Biol. 17:459-464(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 7-330 IN COMPLEX WITH RAT PPP1R9A AND PPP1R9B.

    Entry informationi

    Entry nameiPP1A_HUMAN
    AccessioniPrimary (citable) accession number: P62136
    Secondary accession number(s): A6NNR3
    , B2R908, P08129, P20653, P22802, Q07161
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: June 21, 2004
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3