Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P62136 (PP1A_HUMAN)

Last modified July 7, 2009. Version 62. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
      Short name=PP-1A
    EC=3.1.3.16

Gene names

Name:	PPP1CA
Synonyms:	PPP1A

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

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 Ca²⁺/calmodulin dependent protein kinase II.
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
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.12
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, PPP1R3B, PPP1R3C and PPP1R3D mediate binding to glycogen. Interacts with PPP1R9A and PPP1R9B. Part of a complex containing PPP1R15B, PP1 and NCK1/2 By similarity. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Interacts with HHV-1 ICP34.5.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Hide | Top

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell cycle Cell division Glycogen metabolism
Cellular component	Cytoplasm
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	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 protein amino acid dephosphorylation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell histone methyltransferase complex Ref.16 Inferred from direct assay. Source: UniProtKB
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine phosphatase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
APAF1	O14727	2	EBI-357253,EBI-446492
ATM	Q13315	1	EBI-357253,EBI-495465
AURKB	Q96GD4	1	EBI-357253,EBI-624291
BAD	Q92934	1	EBI-357253,EBI-700771
BCL2	P10415	1	EBI-357253,EBI-77694
BCL2L1	Q07817	1	EBI-357253,EBI-78035
BRCA1	P38398	2	EBI-357253,EBI-349905
CDC2	P06493	1	EBI-357253,EBI-444308
CDH1	P12830	2	EBI-357253,EBI-727477
CDK2	P24941	1	EBI-357253,EBI-375096
CDK4	P11802	1	EBI-357253,EBI-295644
CUL1	Q13616	1	EBI-357253,EBI-359390
MAX	P61244	1	EBI-357253,EBI-878388
PTEN	P60484	2	EBI-357253,EBI-696162
RB1	P06400	2	EBI-357253,EBI-491274
SKP1	P63208	2	EBI-357253,EBI-307486

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 330

329

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

PRO_0000058774

Sites

Active site

125

Proton donor By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Manganese By similarity

Metal binding

124

Manganese By similarity

Metal binding

173

Manganese By similarity

Metal binding

248

Manganese By similarity

Amino acid modifications

Modified residue

N-acetylserine Ref.6

Modified residue

306

Phosphotyrosine By similarity

Modified residue

320

Phosphothreonine Ref.13 Ref.14

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P62136-1 [UniParc].

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

FASTA

330

37,512

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 8392016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[2]	Tung L. Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Synovial cell.
[4]	"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].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle, Pancreas and Placenta.
[6]	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, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[7]	"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: 2161401] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-330.
[8]	"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: 9023344] [Abstract] Cited for: INTERACTION WITH PPP1R15A AND HHV-1 ICP34.5.
[9]	"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: 11564868] [Abstract] Cited for: INTERACTION WITH PPP1R15A.
[10]	"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: 12226088] [Abstract] Cited for: INTERACTION WITH PPP1R7.
[11]	"Protein phosphatase 1 -- targeted in many directions." Cohen P.T.W. J. Cell Sci. 115:241-256(2002) [PubMed: 11839776] [Abstract] Cited for: REVIEW.
[12]	"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: 15705855] [Abstract] Cited for: ENZYME REGULATION.
[13]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, MASS SPECTROMETRY. Tissue: Platelet.
[14]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, MASS SPECTROMETRY.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"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 0:0-0(2009) [PubMed: 19377461] [Abstract] Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
+	Additional computationally mapped references.

Hide | Top

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Hide | Top

Cross-references

Sequence databases

X70848 mRNA. Translation: CAA50197.1.
M63960 mRNA. Translation: AAA36508.1.
AK313586 mRNA. Translation: BAG36355.1.
BT006629 mRNA. Translation: AAP35275.1.
BC001888 mRNA. Translation: AAH01888.1.
BC004482 mRNA. Translation: AAH04482.1.
BC008010 mRNA. Translation: AAH08010.1.
J04759 mRNA. Translation: AAA36475.1.

IPI

IPI00550451.

RefSeq

NP_002699.1.
NP_996756.1.

UniGene

Hs.183994

3D structure databases

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	[»]

SMR

P62136. Positions 7-300.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62136. 18 interactions.

PTM databases

PhosphoSite

P62136.

2-D gel databases

OGP

P08129.

Proteomic databases

PRIDE

P62136.

Genome annotation databases

Ensembl

ENSG00000172531. Homo sapiens. [Contig view]

GeneID

5499.

UCSC

uc001okw.1. human.

Organism-specific databases

GeneCards

GC11M066922.

H-InvDB

HIX0009860.

HGNC

HGNC:9281. PPP1CA.

HPA

CAB004545.

MIM

176875. gene.

PharmGKB

PA33609.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P62136.

Enzyme and pathway databases

BRENDA

3.1.3.16. 247.

Pathway_Interaction_DB

bmppathway. BMP receptor signaling.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_15295. Opioid Signalling.
REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

Bgee

P62136.

CleanEx

HS_PPP1CA.

GermOnline

ENSG00000172531. Homo sapiens.

Family and domain databases

InterPro

IPR004843. M-pesterase.
IPR006186. T_phtase_apaH.
[Graphical view]

PANTHER

PTHR11668. T_phtase_apaH. 1 hit.

Pfam

PF00149. Metallophos. 1 hit.
[Graphical view]

PRINTS

PR00114. STPHPHTASE.

ProDom

PD000252. T_phtase_apaH. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00156. PP2Ac. 1 hit.
[Graphical view]

PROSITE

PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

21272.

SOURCE

Search...

Hide | Top

Entry information

Entry name

PP1A_HUMAN

Accession

Primary (citable) accession number: P62136
Secondary accession number(s): B2R908

P22802

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	June 21, 2004
Last modified:	July 7, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 11

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents