Reviewed, UniProtKB/Swiss-Prot P62140 (PP1B_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

PPP1CB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	327 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 (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity.
Catalytic activity	A phosphoprotein + H(2)O = 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.
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. Part of a complex containing PPP1R15B, PP1 and NCK1/2 By similarity. Interacts with PPP1R7 and PPP1R12C. PPP1R15A and PPP1R15B mediate binding to EIF2S1.
Subcellular location	CytoplasmBy 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	3D-structure 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
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q90624	1	EBI-352350,EBI-1038997	From a different organism.
BCL2	P10415	1	EBI-352350,EBI-77694
BRCA1	P38398	2	EBI-352350,EBI-349905
CCND1	P24385	1	EBI-352350,EBI-375001
CCND3	P30281	1	EBI-352350,EBI-375013
CDC34	P49427	1	EBI-352350,EBI-975634
CDKN2A	Q8N726	1	EBI-352350,EBI-625922
MAX	P61244	1	EBI-352350,EBI-878388
PPP1R11	O60927	1	EBI-352350,EBI-1048104
PPP1R12A	O14974	1	EBI-352350,EBI-351726
PPP1R2	P41236	1	EBI-352350,EBI-1056517
PPP1R7	Q15435	1	EBI-352350,EBI-1024281
PPP1R8	Q12972	1	EBI-352350,EBI-716633
SH2D4A	Q9H788	1	EBI-352350,EBI-747035
TMEM33	P57088	1	EBI-352350,EBI-1048629

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 327

326

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

PRO_0000058779

Sites

Active site

124

1

Proton donor By similarity

Metal binding

63

1

Iron By similarity

Metal binding

65

1

Iron By similarity

Metal binding

91

1

Iron By similarity

Metal binding

91

1

Manganese By similarity

Metal binding

123

1

Manganese By similarity

Metal binding

172

1

Manganese By similarity

Metal binding

247

1

Manganese By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine

Modified residue

41

1

Phosphoserine

Modified residue

47

1

Phosphoserine

Modified residue

306

1

Phosphotyrosine

Modified residue

316

1

Phosphothreonine

Experimental info

Sequence conflict

51

1

L → P in AAV38549. Ref.5

Secondary structure

1

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327

Helix Strand Turn

Details...

Helix

8 – 16

9

Turn

17 – 20

4

Helix

31 – 45

15

Beta strand

50 – 54

5

Beta strand

56 – 61

6

Helix

68 – 78

11

Beta strand

86 – 88

3

Beta strand

93 – 97

5

Helix

99 – 112

14

Turn

114 – 116

3

Beta strand

117 – 119

3

Helix

127 – 130

4

Helix

135 – 142

8

Helix

145 – 155

11

Beta strand

161 – 164

4

Turn

165 – 167

3

Beta strand

168 – 170

3

Helix

183 – 186

4

Beta strand

196 – 198

3

Helix

199 – 205

7

Beta strand

213 – 217

5

Beta strand

221 – 226

6

Helix

228 – 238

11

Beta strand

241 – 245

5

Beta strand

252 – 257

6

Turn

258 – 261

4

Beta strand

262 – 266

5

Helix

271 – 273

3

Beta strand

282 – 284

3

Beta strand

289 – 292

4

Sequences

	Sequence		Length	Mass (Da)
	P62140-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E8356022E9B94ECD	FASTA	327	37,187
	10 20 30 40 50 60 MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI 70 80 90 100 110 120 CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL 130 140 150 160 170 180 RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ 190 200 210 220 230 240 SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL 250 260 270 280 290 300 DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK 310 320 KAKYQYGGLN SGRPVTPPRT ANPPKKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Three genes for protein phosphatase 1 map to different human chromosomes: sequence, expression and gene localisation of protein serine/threonine phosphatase 1 beta (PPP1CB)." Barker H.M., Brewis N.D., Street A.J., Spurr N.K., Cohen P.T.W. Biochim. Biophys. Acta 1220:212-218(1994) [PubMed: 8312365] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular and linkage analysis of type-1 protein phosphatase catalytic beta-subunit gene: lack of evidence for its major role in insulin resistance in Pima Indians." Prochazka M., Mochizuki H., Baier L.J., Cohen P.T.W., Bogardus C. Diabetologia 38:461-466(1995) [PubMed: 7796987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Characterization of the protein phosphatase 1 catalytic subunit in endothelium: involvement in contractile responses." Verin A.D., Csortos C., Durbin S.D., Aydanyan A., Wang P., Patterson C.E., Garcia J.G. J. Cell. Biochem. 79:113-125(2000) [PubMed: 10906760] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Umbilical vein.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[8]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14, ACETYLATION AT ALA-2. Tissue: Platelet.
[9]	"Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton." Tan I., Ng C.H., Lim L., Leung T. J. Biol. Chem. 276:21209-21216(2001) [PubMed: 11399775] [Abstract] Cited for: INTERACTION WITH PPP1R12C.
[10]	"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.
[11]	"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.
[12]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-47, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"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.
[14]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, MASS SPECTROMETRY.
[15]	"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-316, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases
EMBLGenBankDDBJ	X80910 mRNA. Translation: CAA56870.1.