P62136 (PP1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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 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 phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Ref.30 Binds 1 manganese ion per subunit. Ref.30
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 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. 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.30
Subcellular location	Cytoplasm. Nucleus. Nucleus › nucleoplasm. Nucleus › nucleolus. 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 process	Carbohydrate metabolism Cell cycle Cell division Glycogen metabolism
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	branching morphogenesis of an epithelial tube Inferred from electronic annotation. Source: Compara 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: Compara negative regulation of transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome protein dephosphorylation Traceable author statement Ref.1. Source: ProtInc regulation of glycogen biosynthetic process Inferred from electronic annotation. Source: Compara regulation of glycogen catabolic process Inferred from electronic annotation. Source: Compara 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_component	MLL5-L complex Inferred from direct assay Ref.24. Source: UniProtKB PTW/PP1 phosphatase complex Inferred from direct assay Ref.26. Source: UniProtKB cytosol Traceable author statement. Source: Reactome dendritic spine Inferred from electronic annotation. Source: Compara glycogen granule Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell perikaryon Inferred from electronic annotation. Source: Compara protein phosphatase type 1 complex Inferred from electronic annotation. Source: Compara
Molecular_function	metal 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: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APAF1	O14727	2	EBI-357253,EBI-446492
BRCA1	P38398	2	EBI-357253,EBI-349905
CDH1	P12830	2	EBI-357253,EBI-727477
CEP192	Q8TEP8	2	EBI-357253,EBI-2339778
CHCHD3	Q9NX63	2	EBI-357253,EBI-743375
Clock	O08785	2	EBI-357253,EBI-79859	From a different organism.
CNST	Q6PJW8	3	EBI-357253,EBI-750390
CSRNP2	Q9H175	2	EBI-357253,EBI-5235958
DLG3	Q92796	2	EBI-357253,EBI-80440
ELL	P55199	2	EBI-357253,EBI-1245868
PPP1R27	Q86WC6	2	EBI-357253,EBI-5235602
PPP1R32	Q7Z5V6	3	EBI-357253,EBI-4311771
PTEN	P60484	2	EBI-357253,EBI-696162
RB1	P06400	2	EBI-357253,EBI-491274
SFI1	A8K8P3	2	EBI-357253,EBI-743371
SH2D4A	Q9H788	2	EBI-357253,EBI-747035
SH3RF2	Q8TEC5	3	EBI-357253,EBI-2130111
SKP1	P63208	3	EBI-357253,EBI-307486
SPRED1	Q7Z699	3	EBI-357253,EBI-5235340
TMEM132D	Q14C87	2	EBI-357253,EBI-5235567
TRPC4AP	Q8TEL6	2	EBI-357253,EBI-2559060
TSC2	P49815	2	EBI-357253,EBI-396587
WNK1	Q9H4A3	2	EBI-357253,EBI-457907
ZFYVE1	Q9HBF4	2	EBI-357253,EBI-4401611

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 330

329

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

PRO_0000058774

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

Metal binding

124

1

Manganese

Metal binding

173

1

Manganese

Metal binding

248

1

Manganese

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.8

Modified residue

306

1

Phosphotyrosine By similarity

Modified residue

320

1

Phosphothreonine Ref.17 Ref.22 Ref.23 Ref.27

Natural variations

Alternative sequence

18

1

E → EGSRVLTPHCAP in isoform 2.

VSP_043377

Secondary structure

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330

Helix Strand Turn

Details...

Helix

9 – 17

9

Turn

18 – 21

4

Helix

32 – 48

17

Beta strand

51 – 55

5

Beta strand

57 – 62

6

Helix

69 – 79

11

Beta strand

87 – 89

3

Beta strand

94 – 98

5

Helix

100 – 113

14

Turn

115 – 117

3

Beta strand

118 – 120

3

Helix

128 – 134

7

Helix

136 – 143

8

Helix

146 – 156

11

Beta strand

162 – 165

4

Turn

166 – 168

3

Beta strand

169 – 174

6

Helix

184 – 187

4

Beta strand

197 – 199

3

Helix

200 – 206

7

Beta strand

214 – 218

5

Beta strand

222 – 227

6

Helix

229 – 239

11

Beta strand

242 – 246

5

Beta strand

254 – 258

5

Turn

259 – 262

4

Beta strand

263 – 267

5

Helix

272 – 274

3

Beta strand

280 – 285

6

Beta strand

291 – 296

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 21, 2004. Version 1. Checksum: 60C37E1AD9831DAC	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
	Isoform 2 [UniParc]. Checksum: CE50F8B9DC84AB6F	FASTA	341	38,631
	10 20 30 40 50 60 MSDSEKLNLD SIIGRLLEGS RVLTPHCAPV QGSRPGKNVQ LTENEIRGLC LKSREIFLSQ 70 80 90 100 110 120 PILLELEAPL KICGDIHGQY YDLLRLFEYG GFPPESNYLF LGDYVDRGKQ SLETICLLLA 130 140 150 160 170 180 YKIKYPENFF LLRGNHECAS INRIYGFYDE CKRRYNIKLW KTFTDCFNCL PIAAIVDEKI 190 200 210 220 230 240 FCCHGGLSPD LQSMEQIRRI MRPTDVPDQG LLCDLLWSDP DKDVQGWGEN DRGVSFTFGA 250 260 270 280 290 300 EVVAKFLHKH DLDLICRAHQ VVEDGYEFFA KRQLVTLFSA PNYCGEFDNA GAMMSVDETL 310 320 330 340 MCSFQILKPA DKNKGKYGQF SGLNPGGRPI TPPRNSAKAK K

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] [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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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.
[31]	"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.

IPI

IPI00027423.
IPI00550451.

RefSeq

NP_001008709.1. NM_001008709.1.
NP_002699.1. NM_002708.3.
NP_996756.1. NM_206873.1.

UniGene

Hs.183994.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3EGG	X-ray	1.85	A/B	7-330	[»]
3EGH	X-ray	2.00	A/B	7-330	[»]
3HVQ	X-ray	2.20	A/B	7-330	[»]
3N5U	X-ray	3.20	A/B	1-300	[»]
3V4Y	X-ray	2.10	A/C/E/G	7-307	[»]
4G9J	X-ray	3.10	A/B	1-330	[»]

ProteinModelPortal

P62136.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-221N.
DIP-38195N.

IntAct

P62136. 177 interactions.

MINT

MINT-242686.

STRING

9606.ENSP00000326031.

PTM databases

PhosphoSite

P62136.

Polymorphism databases

DMDM

49065811.

2D gel databases

OGP

P08129.

Proteomic databases

PaxDb

P62136.

PRIDE

P62136.

Protocols and materials databases

DNASU

5499.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000312989; ENSP00000326031; ENSG00000172531.
ENST00000376745; ENSP00000365936; ENSG00000172531.

GeneID

5499.

KEGG

hsa:5499.

UCSC

uc001okw.1. human.

Organism-specific databases

CTD

5499.

GeneCards

GC11M067165.

HGNC

HGNC:9281. PPP1CA.

HPA

CAB004545.

MIM

176875. gene.

neXtProt

NX_P62136.

PharmGKB

PA33609.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0639.

HOGENOM

HOG000172697.

HOVERGEN

HBG000216.

KO

K06269.

OMA

APNYCNE.

PhylomeDB

P62136.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P62136.

Bgee

P62136.

CleanEx

HS_PPP1CA.

Genevestigator

P62136.

GermOnline

ENSG00000172531. Homo sapiens.

Family and domain databases

InterPro

IPR004843. Metallo_PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]

Pfam

PF00149. Metallophos. 1 hit.
[Graphical view]

PRINTS

PR00114. STPHPHTASE.

SMART

SM00156. PP2Ac. 1 hit.
[Graphical view]

PROSITE

PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P62136.

ChEMBL

CHEMBL2164.

ChiTaRS

PPP1CA. human.

EvolutionaryTrace

P62136.

GenomeRNAi

5499.

NextBio

21272.

SOURCE

Search...

Entry information

Entry name

PP1A_HUMAN

Accession

Primary (citable) accession number: P62136
Secondary accession number(s): B2R908 , P08129, P20653, P22802, Q07161

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	June 21, 2004
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.