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P62137

- PP1A_MOUSE

UniProt

P62137 - PP1A_MOUSE

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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

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

Protein has several cofactor binding sites:
  • Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity
  • Mn2+By similarityNote: 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 serine/threonine phosphatase activity Source: MGI
  5. 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
Complete GO annotation...

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.
REACT_245618. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

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, UP000000589: Unplaced

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. extracellular vesicular exosome Source: Ensembl
  4. glycogen granule Source: Ensembl
  5. MLL5-L complex Source: Ensembl
  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
Complete GO annotation...

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. Interacts with BTBD10 (PubMed:18160256). Interacts with KCTD20 (PubMed:24156551).By similarity5 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

        10         20         30         40         50
MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP
60 70 80 90 100
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS
110 120 130 140 150
LETICLLLAY KIRYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK
160 170 180 190 200
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL
210 220 230 240 250
LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV
260 270 280 290 300
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD
310 320 330
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK
Length:330
Mass (Da):37,540
Last modified:June 21, 2004 - v1
Checksum:i8FBFD158A52282E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
REACT_245618. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

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

« Hide 'large scale' publications
  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. "A novel Akt/PKB-interacting protein promotes cell adhesion and inhibits familial amyotrophic lateral sclerosis-linked mutant SOD1-induced neuronal death via inhibition of PP2A-mediated dephosphorylation of Akt/PKB."
    Nawa M., Kanekura K., Hashimoto Y., Aiso S., Matsuoka M.
    Cell. Signal. 20:493-505(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BTBD10.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "KCTD20, a relative of BTBD10, is a positive regulator of Akt."
    Nawa M., Matsuoka M.
    BMC Biochem. 14:27-27(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCTD20.
  15. "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: November 26, 2014
This is version 114 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