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P62136 (PP1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Short name=PP-1A
EC=3.1.3.16
Gene names
Name:PPP1CA
Synonyms:PPP1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.19

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit By similarity. Ref.31

Binds 1 manganese ion per subunit. Ref.31

Enzyme regulation

The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress. Ref.16

Subunit structure

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 4of NEK2. Interacts with FER; this promotes phosphorylation at Thr-320. Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.24 Ref.25 Ref.26 Ref.28 Ref.31

Subcellular location

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. Ref.11 Ref.21

Post-translational modification

Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation. Ref.17 Ref.19

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell cycle
Cell division
Glycogen metabolism
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbranching morphogenesis of an epithelial tube

Inferred from electronic annotation. Source: Ensembl

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

glycogen metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

lung development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Traceable author statement Ref.1. Source: ProtInc

regulation of glycogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of glycogen catabolic process

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

triglyceride catabolic process

Traceable author statement. Source: Reactome

   Cellular_componentMLL5-L complex

Inferred from direct assay Ref.24. Source: UniProtKB

PTW/PP1 phosphatase complex

Inferred from direct assay Ref.26. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

glycogen granule

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

perikaryon

Inferred from electronic annotation. Source: Ensembl

protein phosphatase type 1 complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine phosphatase activity

Traceable author statement Ref.1. Source: ProtInc

ribonucleoprotein complex binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62136-1)

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.
Isoform 2 (identifier: P62136-2)

The sequence of this isoform differs from the canonical sequence as follows:
     18-18: E → EGSRVLTPHCAP
Note: No experimental confirmation available.
Isoform 3 (identifier: P62136-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 330329Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
PRO_0000058774

Sites

Active site1251Proton donor By similarity
Metal binding641Iron By similarity
Metal binding661Iron By similarity
Metal binding921Iron By similarity
Metal binding921Manganese
Metal binding1241Manganese
Metal binding1731Manganese
Metal binding2481Manganese

Amino acid modifications

Modified residue21N-acetylserine Ref.8 Ref.30
Modified residue3051N6-acetyllysine By similarity
Modified residue3061Phosphotyrosine By similarity
Modified residue3201Phosphothreonine Ref.17 Ref.22 Ref.23 Ref.27

Natural variations

Alternative sequence181E → EGSRVLTPHCAP in isoform 2.
VSP_043377
Alternative sequence19 – 6244Missing in isoform 3.
VSP_046754

Secondary structure

...................................................... 330
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 21, 2004. Version 1.
Checksum: 60C37E1AD9831DAC

FASTA33037,512
        10         20         30         40         50         60 
MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK 

        70         80         90        100        110        120 
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL 

       130        140        150        160        170        180 
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL 

       190        200        210        220        230        240 
QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD 

       250        260        270        280        290        300 
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD 

       310        320        330 
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK 

« Hide

Isoform 2 [UniParc].

Checksum: CE50F8B9DC84AB6F
Show »

FASTA34138,631
Isoform 3 [UniParc].

Checksum: E0560E7C422C353C
Show »

FASTA28632,595

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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]"NOM1 targets protein phosphatase I to the nucleolus."
Gunawardena S.R., Ruis B.L., Meyer J.A., Kapoor M., Conklin K.F.
J. Biol. Chem. 283:398-404(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NOM1.
[22]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"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.
[32]"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.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001008709.1. NM_001008709.1.
NP_002699.1. NM_002708.3.
NP_996756.1. NM_206873.1.
UniGeneHs.183994.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP62136.
SMRP62136. Positions 7-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111493. 215 interactions.
DIPDIP-221N.
DIP-38195N.
IntActP62136. 217 interactions.
MINTMINT-5001223.
STRING9606.ENSP00000326031.

Chemistry

BindingDBP62136.
ChEMBLCHEMBL2164.

PTM databases

PhosphoSiteP62136.

Polymorphism databases

DMDM49065811.

2D gel databases

OGPP08129.

Proteomic databases

PaxDbP62136.
PRIDEP62136.

Protocols and materials databases

DNASU5499.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312989; ENSP00000326031; ENSG00000172531. [P62136-2]
ENST00000358239; ENSP00000350974; ENSG00000172531. [P62136-3]
ENST00000376745; ENSP00000365936; ENSG00000172531. [P62136-1]
GeneID5499.
KEGGhsa:5499.
UCSCuc001oku.1. human. [P62136-2]
uc001okw.1. human. [P62136-1]

Organism-specific databases

CTD5499.
GeneCardsGC11M067165.
HGNCHGNC:9281. PPP1CA.
HPACAB004545.
MIM176875. gene.
neXtProtNX_P62136.
PharmGKBPA33609.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172697.
HOVERGENHBG000216.
KOK06269.
OMALEHEIRY.
OrthoDBEOG7TJ3K3.
PhylomeDBP62136.
TreeFamTF354243.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
SignaLinkP62136.

Gene expression databases

ArrayExpressP62136.
BgeeP62136.
CleanExHS_PPP1CA.
GenevestigatorP62136.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP1CA. human.
EvolutionaryTraceP62136.
GeneWikiPPP1CA.
GenomeRNAi5499.
NextBio21272.
PROP62136.
SOURCESearch...

Entry information

Entry namePP1A_HUMAN
AccessionPrimary (citable) accession number: P62136
Secondary accession number(s): A6NNR3 expand/collapse secondary AC list , B2R908, P08129, P20653, P22802, Q07161
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 21, 2004
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM