Gene name:
PPP1CA (PPP1A) ;
Protein name:
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) ;
Alternative:
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
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, PPP1R3B, PPP1R3C and PPP1R3D mediate binding to glycogen. Interacts with SH3RF2 (By similarity). Interacts with PPP1R9A and PPP1R9B. Part of a complex containing PPP1R15B, PP1 and NCK1/2 (By similarity). Interacts with PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1. Component of the MLL5-L complex, at least composed of 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.
Function:
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 Ca(2+)/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.
Subcellular Location:
Cytoplasm
Nucleus
Nucleus
nucleoplasm
Nucleus
nucleolus
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.
Protein Attributes:
50:
MSDSEKLNLD | SIIGRLLEVQ | GSRPGKNVQL | TENEIRGLCL | KSREIFLSQP |
100:
ILLELEAPLK | ICGDIHGQYY | DLLRLFEYGG | FPPESNYLFL | GDYVDRGKQS |
150:
LETICLLLAY | KIKYPENFFL | LRGNHECASI | NRIYGFYDEC | KRRYNIKLWK |
200:
TFTDCFNCLP | IAAIVDEKIF | CCHGGLSPDL | QSMEQIRRIM | RPTDVPDQGL |
250:
LCDLLWSDPD | KDVQGWGEND | RGVSFTFGAE | VVAKFLHKHD | LDLICRAHQV |
300:
VEDGYEFFAK | RQLVTLFSAP | NYCGEFDNAG | AMMSVDETLM | CSFQILKPAD |
330:
KNKGKYGQFS | GLNPGGRPIT | PPRNSAKAKK |
Vaild Sequence:
Related Databases
Uniprot:
ELISA Kit
CLIA Kit
Polyclonal Antibody
Monoclonal Antibody
Protein
FOR
Human
Dog
Bovine
Mouse
Rat
Rabbit
ELISA Kit for Human PP-1A
ELISA Kit for Human PP-1A
ELISA Kit for Human PP-1A
ELISA Kit for Human PP-1A
ELISA Kit for Human PP-1A
ELISA Kit for Human PP-1A
Polyclonal Antibody for Human PP-1A
Polyclonal Antibody for Human PP-1A
Polyclonal Antibody for Human PP-1A
Polyclonal Antibody for Human PP-1A
Polyclonal Antibody for Human PP-1A
Polyclonal Antibody for Human PP-1A
Monoclonal Antibody for Human PP-1A
Monoclonal Antibody for Human PP-1A
Monoclonal Antibody for Human PP-1A
Monoclonal Antibody for Human PP-1A
Monoclonal Antibody for Human PP-1A
Monoclonal Antibody for Human PP-1A
R&D Technical Data
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Precision
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Recovery
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Linearity
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References
1.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
tissue :
Lung .
2.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
tissue :
Liver .
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Synovial cell .
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
7.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
tissue :
Muscle .
tissue :
Pancreas .
tissue :
Placenta .
8.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : PROTEIN SEQUENCE OF 2-15 AND 247-261;CLEAVAGE OF INITIATOR METHIONINE;ACETYLATION AT SER-2;IDENTIFICATION BY MASS SPECTROMETRY
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Colon carcinoma .
9.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [MRNA] OF 23-330 (ISOFORM 1)
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INTERACTION WITH PPP1R15A AND HHV-1 ICP34.5
11.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : SUBCELLULAR LOCATION;INTERACTION WITH PPP1R8
12.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INTERACTION WITH PPP1R15A
13.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INTERACTION WITH PPP1R7
14.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : REVIEW
15.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INTERACTION WITH PPP1R16B AND RPSA
16.
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Science307:935-939(2005)
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : ENZYME REGULATION
17.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INTERACTION WITH FER;PHOSPHORYLATION AT THR-320
18.
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Biochim. Biophys. Acta1774:1339-1350(2007)
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[
Europe PMC ]
[
Abstract ]
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Cited for : IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; RBMX AND NCOA5;INTERACTION WITH YLPM1
19.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION;INTERACTION WITH NEK2;DEPHOSPHORYLATION
20.
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Cited for : INTERACTION WITH NEK2
21.
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Cited for : SUBCELLULAR LOCATION;INTERACTION WITH NOM1
22.
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Cited for : PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
tissue :
Platelet .
23.
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Cited for : PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
tissue :
Cervix carcinoma .
24.
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Cited for : IDENTIFICATION IN THE MLL5-L COMPLEX
25.
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Cited for : INTERACTION WITH DAB2
26.
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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 ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
tissue :
Cervix carcinoma .
28.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INTERACTION WITH TRIM28
29.
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Cited for : IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
30.
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Cited for : FUNCTION IN CIRCADIAN CLOCK
31.
"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P.
,
Lasa M.
,
Polevoda B.
,
Gazquez C.
,
Elosegui-Artola A.
,
Kim D.S.
,
De Juan-Pardo E.
,
Demeyer K.
,
Hole K.
,
Larrea E.
,
Timmerman E.
,
Prieto J.
,
Arnesen T.
,
Sherman F.
,
Gevaert K.
,
Aldabe R.
Proc. Natl. Acad. Sci. U.S.A.109:12449-12454(2012)
[
PubMed ]
[
Europe PMC ]
[
Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
32.
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Cited for : X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 7-300 IN COMPLEX WITH INHIBITORS;COFACTOR;MANGANESE-BINDING SITES;SUBUNIT
33.
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Cited for : X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 7-330 IN COMPLEX WITH RAT PPP1R9A AND PPP1R9B