Reviewed, UniProtKB/Swiss-Prot P62137 (PP1A_MOUSE)

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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.

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.
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. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R9A, PPP1R9B and PPP1R7 By similarity. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

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	Direct protein sequencing
Gene Ontology (GO)
Biological process	branching morphogenesis of a tube Inferred from mutant phenotype. Source: MGI cell division Inferred from electronic annotation. Source: UniProtKB-KW female meiosis Traceable author statement. Source: MGI glycogen metabolic process Traceable author statement. Source: MGI lung development Inferred from mutant phenotype. Source: MGI protein amino acid dephosphorylation Inferred from direct assay. Source: MGI regulation of translation Traceable author statement. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleoplasm Inferred from direct assay. Source: MGI
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 Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Apaf1	O88879	1	EBI-357187,EBI-1202386
Atm	Q62388	1	EBI-357187,EBI-1202183
Atr	Q9JKK8	1	EBI-357187,EBI-1202426
Bcl2	P10417	1	EBI-357187,EBI-526314
Ccnd3	P30282	1	EBI-357187,EBI-847337
Cdc34	Q8CFI2	1	EBI-357187,EBI-1202331
Cdkn2a	Q64364	1	EBI-357187,EBI-1202287
Eif2s1	Q6ZWX6	1	EBI-357187,EBI-1202234
Hdac1	O09106	1	EBI-357187,EBI-301912
Id2	P41136	2	EBI-357187,EBI-309167
Mapt	P10637	1	EBI-357187,EBI-774043
Max	P28574	1	EBI-357187,EBI-1183003
Nek2	O35942	1	EBI-357187,EBI-1202268
Pcna	P17918	2	EBI-357187,EBI-1173716
Rb1	P13405	1	EBI-357187,EBI-971782
Skp1	Q9WTX5	2	EBI-357187,EBI-1202363
Tsc1	Q9EP53	1	EBI-357187,EBI-1202690

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 330	329	Serine/threonine-protein phosphatase PP1-alpha catalytic subunit		PRO_0000058775
Sites
	Active site	125	1	Proton donor By similarity
	Metal binding	64	1	Iron By similarity
	Metal binding	66	1	Iron By similarity
	Metal binding	92	1	Iron By similarity
	Metal binding	92	1	Manganese By similarity
	Metal binding	124	1	Manganese By similarity
	Metal binding	173	1	Manganese By similarity
	Metal binding	248	1	Manganese By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	306	1	Phosphotyrosine
	Modified residue	320	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62137-1 [UniParc]. Last modified June 21, 2004. Version 1. Checksum: 8FBFD158A52282E0	FASTA	330	37,540
	10 20 30 40 50 60 MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK 70 80 90 100 110 120 ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIRYPENFFL 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 16141072] [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: 15489334] [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, 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: 8077208] [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: 14638860] [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: 16835242] [Abstract] Cited for: IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
[8]	"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: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00130185.
RefSeq	NP_114074.1.
UniGene	Mm.1970 Mm.474260
3D structure databases
HSSP	HSSP built from PDB template 1FJM based on UniProtKB P08129.
SMR	P62137. Positions 7-300.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62137. 19 interactions.
PTM databases
PhosphoSite	P62137.
Proteomic databases
PRIDE	P62137.
Genome annotation databases
Ensembl	ENSMUSG00000040385. Mus musculus. [Contig view]
GeneID	19045.
KEGG	mmu:19045.
Organism-specific databases
MGI	MGI:103016. Ppp1ca.
Phylogenomic databases
HOGENOM	P62137.
HOVERGEN	P62137.
OMA	P62137. FFSKRQL.
Enzyme and pathway databases
BRENDA	3.1.3.16. 244.
Gene expression databases
ArrayExpress	P62137.
Bgee	P62137.
GermOnline	ENSMUSG00000040385. Mus musculus.
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	295505.
SOURCE	Search...

Entry information

Entry name

PP1A_MOUSE

Accession

Primary (citable) accession number: P62137
Secondary accession number(s): P08129 , P20653, P22802, Q3U7G7, Q9Z1G2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	June 21, 2004
Last modified:	July 7, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)