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P62137

- PP1A_MOUSE

UniProt

P62137 - PP1A_MOUSE

Protein

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Gene

Ppp1ca

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (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.4 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.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. phosphatase activity Source: UniProtKB
    3. phosphoprotein phosphatase activity Source: MGI
    4. protein binding Source: IntAct
    5. protein serine/threonine phosphatase activity Source: MGI
    6. ribonucleoprotein complex binding Source: Ensembl

    GO - Biological processi

    1. branching morphogenesis of an epithelial tube Source: MGI
    2. cellular process Source: MGI
    3. circadian regulation of gene expression Source: UniProtKB
    4. entrainment of circadian clock by photoperiod Source: UniProtKB
    5. female meiotic division Source: MGI
    6. glycogen metabolic process Source: MGI
    7. lung development Source: MGI
    8. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
    9. protein dephosphorylation Source: UniProtKB
    10. regulation of circadian rhythm Source: UniProtKB
    11. regulation of glycogen biosynthetic process Source: Ensembl
    12. regulation of glycogen catabolic process Source: Ensembl
    13. regulation of translation Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_203795. DARPP-32 events.
    REACT_215733. Downregulation of TGF-beta receptor signaling.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:103016. Ppp1ca.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Nucleusnucleoplasm By similarity. Nucleusnucleolus By similarity
    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 By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. dendritic spine Source: Ensembl
    3. glycogen granule Source: Ensembl
    4. MLL5-L complex Source: Ensembl
    5. nucleolus Source: UniProtKB-SubCell
    6. nucleoplasm Source: MGI
    7. nucleus Source: MGI
    8. perikaryon Source: Ensembl
    9. protein phosphatase type 1 complex Source: Ensembl
    10. PTW/PP1 phosphatase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641D → N: Dominant negatif, severely disrupts circadian rhythmicity of transcription. 1 Publication
    Mutagenesisi95 – 951D → N: Dominant negatif, severely disrupts circadian rhythmicity of transcription. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 330329Serine/threonine-protein phosphatase PP1-alpha catalytic subunitPRO_0000058775Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei305 – 3051N6-acetyllysine1 Publication
    Modified residuei306 – 3061Phosphotyrosine1 Publication
    Modified residuei320 – 3201PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP62137.
    PaxDbiP62137.
    PRIDEiP62137.

    PTM databases

    PhosphoSiteiP62137.

    Expressioni

    Gene expression databases

    BgeeiP62137.
    GenevestigatoriP62137.

    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. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R9A, PPP1R9B and PPP1R7. Interacts with PPP1R15A; the interaction mediates binding to EIF2S1. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8. 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 PPP1R39. Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site By similarity. Interacts with PPP1R15B; the interaction mediates binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with NEK2. Interacts with FER; this promotes phosphorylation at Thr-320 By similarity. Interacts with PHACTR4; which acts as an activator of PP1 activity.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ArntlQ9WTL82EBI-357187,EBI-644534
    Axin1O356252EBI-357187,EBI-2365912
    Id2P411362EBI-357187,EBI-309167
    PcnaP179182EBI-357187,EBI-1173716
    Skp1Q9WTX52EBI-357187,EBI-1202363

    Protein-protein interaction databases

    BioGridi202335. 30 interactions.
    IntActiP62137. 28 interactions.
    MINTiMINT-4108290.

    Structurei

    3D structure databases

    ProteinModelPortaliP62137.
    SMRiP62137. Positions 7-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000062911.
    HOGENOMiHOG000172697.
    HOVERGENiHBG000216.
    InParanoidiP62137.
    KOiK06269.
    OMAiMGDVMNI.
    OrthoDBiEOG7TJ3K3.
    PhylomeDBiP62137.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P62137-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP    50
    ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS 100
    LETICLLLAY KIRYPENFFL 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):37,540
    Last modified:June 21, 2004 - v1
    Checksum:i8FBFD158A52282E0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25809 mRNA. Translation: AAC99814.1.
    AK007932 mRNA. Translation: BAB25358.1.
    AK028392 mRNA. Translation: BAC25928.1.
    AK090070 mRNA. Translation: BAC41078.1.
    AK151582 mRNA. Translation: BAE30522.1.
    AK152667 mRNA. Translation: BAE31402.1.
    AK153517 mRNA. Translation: BAE32060.1.
    AK159575 mRNA. Translation: BAE35196.1.
    AK167244 mRNA. Translation: BAE39365.1.
    AK167538 mRNA. Translation: BAE39605.1.
    AK167880 mRNA. Translation: BAE39893.1.
    AK167981 mRNA. Translation: BAE39973.1.
    BC014828 mRNA. Translation: AAH14828.1.
    CCDSiCCDS29421.1.
    RefSeqiNP_114074.1. NM_031868.2.
    UniGeneiMm.1970.
    Mm.474260.

    Genome annotation databases

    EnsembliENSMUST00000046094; ENSMUSP00000039109; ENSMUSG00000040385.
    ENSMUST00000180575; ENSMUSP00000137997; ENSMUSG00000096994.
    GeneIDi19045.
    KEGGimmu:19045.
    UCSCiuc008fzg.1. mouse.

    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
    U25809 mRNA. Translation: AAC99814.1 .
    AK007932 mRNA. Translation: BAB25358.1 .
    AK028392 mRNA. Translation: BAC25928.1 .
    AK090070 mRNA. Translation: BAC41078.1 .
    AK151582 mRNA. Translation: BAE30522.1 .
    AK152667 mRNA. Translation: BAE31402.1 .
    AK153517 mRNA. Translation: BAE32060.1 .
    AK159575 mRNA. Translation: BAE35196.1 .
    AK167244 mRNA. Translation: BAE39365.1 .
    AK167538 mRNA. Translation: BAE39605.1 .
    AK167880 mRNA. Translation: BAE39893.1 .
    AK167981 mRNA. Translation: BAE39973.1 .
    BC014828 mRNA. Translation: AAH14828.1 .
    CCDSi CCDS29421.1.
    RefSeqi NP_114074.1. NM_031868.2.
    UniGenei Mm.1970.
    Mm.474260.

    3D structure databases

    ProteinModelPortali P62137.
    SMRi P62137. Positions 7-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202335. 30 interactions.
    IntActi P62137. 28 interactions.
    MINTi MINT-4108290.

    PTM databases

    PhosphoSitei P62137.

    Proteomic databases

    MaxQBi P62137.
    PaxDbi P62137.
    PRIDEi P62137.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000046094 ; ENSMUSP00000039109 ; ENSMUSG00000040385 .
    ENSMUST00000180575 ; ENSMUSP00000137997 ; ENSMUSG00000096994 .
    GeneIDi 19045.
    KEGGi mmu:19045.
    UCSCi uc008fzg.1. mouse.

    Organism-specific databases

    CTDi 5499.
    MGIi MGI:103016. Ppp1ca.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00530000062911.
    HOGENOMi HOG000172697.
    HOVERGENi HBG000216.
    InParanoidi P62137.
    KOi K06269.
    OMAi MGDVMNI.
    OrthoDBi EOG7TJ3K3.
    PhylomeDBi P62137.
    TreeFami TF354243.

    Enzyme and pathway databases

    Reactomei REACT_203795. DARPP-32 events.
    REACT_215733. Downregulation of TGF-beta receptor signaling.

    Miscellaneous databases

    ChiTaRSi PPP1CA. mouse.
    NextBioi 21272.
    PROi P62137.
    SOURCEi Search...

    Gene expression databases

    Bgeei P62137.
    Genevestigatori P62137.

    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. Ortiz J.M., Lorenzo M.L., Eguiraun A., Andres I., Sangrador A., Allshire R., Hastie N.D.
      Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and DBA/2.
      Tissue: Extraembryonic tissue, Liver, Pancreas and Placenta.
    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].
      Tissue: Kidney.
    4. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 44-74; 114-122 AND 247-260, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    5. "Molecular cloning of a protein serine/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain."
      Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.
      J. Biol. Chem. 269:22586-22592(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-90.
    6. "Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells."
      Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P., Ron D.
      J. Cell Biol. 163:767-775(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R15B.
    7. "Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress."
      Latreille M., Larose L.
      J. Biol. Chem. 281:26633-26644(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
    8. "Phactr4 regulates neural tube and optic fissure closure by controlling PP1-, Rb-, and E2F1-regulated cell-cycle progression."
      Kim T.H., Goodman J., Anderson K.V., Niswander L.
      Dev. Cell 13:87-102(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PHACTR4.
    9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    10. "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.
    11. "The period of the circadian oscillator is primarily determined by the balance between casein kinase 1 and protein phosphatase 1."
      Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.
      Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK, MUTAGENESIS OF ASP-64 AND ASP-95.
    12. "Phactr4 regulates directional migration of enteric neural crest through PP1, integrin signaling, and cofilin activity."
      Zhang Y., Kim T.H., Niswander L.
      Genes Dev. 26:69-81(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiPP1A_MOUSE
    AccessioniPrimary (citable) accession number: P62137
    Secondary accession number(s): P08129
    , P20653, P22802, Q3U7G7, Q9Z1G2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: June 21, 2004
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3