O75688 (PPM1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein phosphatase 1B
EC=3.1.3.16

Alternative name(s):
Protein phosphatase 2C isoform beta
Short name=PP2C-beta

Gene names

Name:	PPM1B
Synonyms:	PP2CB

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	479 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Subunit structure	Monomer By similarity. Interacts with PAK6. Ref.10
Tissue specificity	Highly expressed in heart and skeletal muscle.
Sequence similarities	Belongs to the PP2C family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokine-mediated signaling pathway Traceable author statement. Source: Reactome peptidyl-threonine dephosphorylation Inferred from direct assay PubMed 20801214. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: InterPro protein serine/threonine phosphatase activity Inferred from direct assay PubMed 20801214. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	4	EBI-1047039,EBI-743313
ARRB2	P32121	3	EBI-1047039,EBI-714559

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform Beta-1 (identifier: O75688-1)

Also known as: Beta-X; PPM1B2;

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 Beta-2 (identifier: O75688-2)

Also known as: PPM1B1;

The sequence of this isoform differs from the canonical sequence as follows:
     379-387: ASDEAEESG → GAGDLEDPW
     388-479: Missing.

Isoform Beta-X (identifier: O75688-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-287: Missing.

Isoform 4 (identifier: O75688-4)

The sequence of this isoform differs from the canonical sequence as follows:
     379-380: AS → QK
     381-387: Missing.
     388-479: Missing.

Isoform 5 (identifier: O75688-5)

The sequence of this isoform differs from the canonical sequence as follows:
     322-327: EIMEKS → GKTNAF
     328-380: Missing.
     381-387: Missing.
     388-479: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 479

479

Protein phosphatase 1B

PRO_0000057746

Sites

Metal binding

60

1

Manganese 1 By similarity

Metal binding

60

1

Manganese 2 By similarity

Metal binding

61

1

Manganese 1; via carbonyl oxygen By similarity

Metal binding

243

1

Manganese 2 By similarity

Metal binding

286

1

Manganese 2 By similarity

Natural variations

Alternative sequence

1 – 287

287

Missing in isoform Beta-X.

VSP_041085

Alternative sequence

322 – 327

6

EIMEKS → GKTNAF in isoform 5.

VSP_043641

Alternative sequence

328 – 380

53

Missing in isoform 5.

VSP_043642

Alternative sequence

379 – 387

9

ASDEAEESG → GAGDLEDPW in isoform Beta-2.

VSP_005087

Alternative sequence

379 – 380

2

AS → QK in isoform 4.

VSP_043643

Alternative sequence

381 – 387

7

Missing in isoform 4 and isoform 5.

VSP_043644

Alternative sequence

388 – 479

92

Missing in isoform Beta-2, isoform 4 and isoform 5.

VSP_005088

Secondary structure

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479

Helix Strand Turn

Details...

Beta strand

9 – 19

11

Beta strand

22 – 31

10

Beta strand

33 – 35

3

Beta strand

38 – 46

9

Turn

47 – 49

3

Beta strand

50 – 63

14

Helix

66 – 80

15

Turn

83 – 85

3

Helix

99 – 118

20

Turn

121 – 123

3

Beta strand

134 – 139

6

Beta strand

141 – 151

11

Beta strand

153 – 158

6

Beta strand

161 – 165

5

Helix

174 – 182

9

Turn

193 – 195

3

Helix

205 – 207

3

Helix

215 – 217

3

Beta strand

218 – 221

4

Beta strand

225 – 230

6

Beta strand

235 – 241

7

Helix

243 – 246

4

Helix

251 – 262

12

Helix

268 – 281

14

Beta strand

288 – 294

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta-1 (Beta-X) (PPM1B2) [UniParc]. Last modified November 1, 1998. Version 1. Checksum: A3A5797AD263DFBD	FASTA	479	52,643
	10 20 30 40 50 60 MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL EDWSFFAVYD 70 80 90 100 110 120 GHAGSRVANY CSTHLLEHIT TNEDFRAAGK SGSALELSVE NVKNGIRTGF LKIDEYMRNF 130 140 150 160 170 180 SDLRNGMDRS GSTAVGVMIS PKHIYFINCG DSRAVLYRNG QVCFSTQDHK PCNPREKERI 190 200 210 220 230 240 QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL 250 260 270 280 290 300 ACDGIWDVMS NEELCEYVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK 310 320 330 340 350 360 VSDEAVKKDS ELDKHLESRV EEIMEKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGKR 370 380 390 400 410 420 NVIEAVYSRL NPHRESDGAS DEAEESGSQG KLVEALRQMR INHRGNYRQL LEEMLTSYRL 430 440 450 460 470 AKVEGEESPA EPAATATSSN SDAGNPVTMQ ESHTESESGL AELDSSNEDA GTKMSGEKI
	Isoform Beta-2 (PPM1B1) [UniParc]. Checksum: 56A644A4E5E2B12B	FASTA	387	42,771
	10 20 30 40 50 60 MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL EDWSFFAVYD 70 80 90 100 110 120 GHAGSRVANY CSTHLLEHIT TNEDFRAAGK SGSALELSVE NVKNGIRTGF LKIDEYMRNF 130 140 150 160 170 180 SDLRNGMDRS GSTAVGVMIS PKHIYFINCG DSRAVLYRNG QVCFSTQDHK PCNPREKERI 190 200 210 220 230 240 QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL 250 260 270 280 290 300 ACDGIWDVMS NEELCEYVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK 310 320 330 340 350 360 VSDEAVKKDS ELDKHLESRV EEIMEKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGKR 370 380 NVIEAVYSRL NPHRESDGGA GDLEDPW
	Isoform Beta-X [UniParc]. Checksum: 46FA14838483534F	FASTA	192	20,753
	10 20 30 40 50 60 MSIVLVCFSN APKVSDEAVK KDSELDKHLE SRVEEIMEKS GEEGMPDLAH VMRILSAENI 70 80 90 100 110 120 PNLPPGGGLA GKRNVIEAVY SRLNPHRESD GASDEAEESG SQGKLVEALR QMRINHRGNY 130 140 150 160 170 180 RQLLEEMLTS YRLAKVEGEE SPAEPAATAT SSNSDAGNPV TMQESHTESE SGLAELDSSN 190 EDAGTKMSGE KI
	Isoform 4 [UniParc]. Checksum: E5C00B5FF4278013	FASTA	380	42,086
	10 20 30 40 50 60 MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL EDWSFFAVYD 70 80 90 100 110 120 GHAGSRVANY CSTHLLEHIT TNEDFRAAGK SGSALELSVE NVKNGIRTGF LKIDEYMRNF 130 140 150 160 170 180 SDLRNGMDRS GSTAVGVMIS PKHIYFINCG DSRAVLYRNG QVCFSTQDHK PCNPREKERI 190 200 210 220 230 240 QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL 250 260 270 280 290 300 ACDGIWDVMS NEELCEYVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK 310 320 330 340 350 360 VSDEAVKKDS ELDKHLESRV EEIMEKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGKR 370 380 NVIEAVYSRL NPHRESDGQK
	Isoform 5 [UniParc]. Checksum: E38A263FCF7F1692	FASTA	327	36,313
	10 20 30 40 50 60 MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL EDWSFFAVYD 70 80 90 100 110 120 GHAGSRVANY CSTHLLEHIT TNEDFRAAGK SGSALELSVE NVKNGIRTGF LKIDEYMRNF 130 140 150 160 170 180 SDLRNGMDRS GSTAVGVMIS PKHIYFINCG DSRAVLYRNG QVCFSTQDHK PCNPREKERI 190 200 210 220 230 240 QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL 250 260 270 280 290 300 ACDGIWDVMS NEELCEYVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK 310 320 VSDEAVKKDS ELDKHLESRV EGKTNAF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cloning expression and tissue distribution of human PP2Cbeta." Marely A.E., Kline A., Crabtree G., Sullivan J.E., Beri R.K. FEBS Lett. 431:121-124(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1). Tissue: Liver.
[2]	"Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2Calpha and beta2 isoforms." Cheng A., Kaldis P., Solomon M.J. J. Biol. Chem. 275:34744-34749(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
[3]	"Protein phosphatase 1B. Cloning and characterization of two major transcripts generated by alternative use of 3' exons." Seroussi E., Shani N., Hayut A., Faier S., Ben-Meir D., Divinski I., Smorodinsky N.I., Lavi S. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1 AND BETA-2).
[4]	"The 2p21 deletion syndrome: characterization of the transcription content." Parvari R., Gonen Y., Alshafee I., Buriakovsky S., Regev K., Hershkovitz E. Genomics 86:195-211(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-2; 4 AND 5).
[5]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2). Tissue: Adrenal gland.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1). Tissue: Stomach.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORMS BETA-1 AND BETA-X). Tissue: Brain and Urinary bladder.
[10]	"Increased PAK6 expression in prostate cancer and identification of PAK6 associated proteins." Kaur R., Yuan X., Lu M.L., Balk S.P. Prostate 68:1510-1516(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PAK6.
[11]	"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].
[12]	"Structural genomics of protein phosphatases." Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P., Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S., Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y., Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R. , Sali A., Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K. J. Struct. Funct. Genomics 8:121-140(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 2-297.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ005801 mRNA. Translation: CAA06704.1.
AF294792 mRNA. Translation: AAG02232.1.
AJ271832 mRNA. Translation: CAC27992.1.
AJ271835 mRNA. Translation: CAC27993.1.
DQ023508 mRNA. Translation: AAY89639.1.
DQ023509 mRNA. Translation: AAY89640.1.
DQ023510 mRNA. Translation: AAY89641.1.
AF136972 mRNA. Translation: AAG49433.1.
AL833035 mRNA. Translation: CAH56319.1.
AC013717 Genomic DNA. Translation: AAX88954.1.
AC019129 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00282.1.
CH471053 Genomic DNA. Translation: EAX00283.1.
BC012002 mRNA. Translation: AAH12002.1.
BC064381 mRNA. Translation: AAH64381.1.

IPI

IPI00026612.
IPI00219537.
IPI00651725.
IPI00743802.
IPI00917979.

RefSeq

NP_001028728.1. NM_001033556.1.
NP_001028729.1. NM_001033557.1.
NP_002697.1. NM_002706.4.
NP_808907.1. NM_177968.2.
NP_808908.1. NM_177969.2.

UniGene

Hs.416769.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2P8E	X-ray	1.82	A/B	2-297	[»]

ProteinModelPortal

O75688.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75688. 7 interactions.

MINT

MINT-2841839.

STRING

9606.ENSP00000282412.

PTM databases

PhosphoSite

O75688.

Proteomic databases

PaxDb

O75688.

PRIDE

O75688.

Protocols and materials databases

DNASU

5495.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000282412; ENSP00000282412; ENSG00000138032.
ENST00000345249; ENSP00000326089; ENSG00000138032.
ENST00000378551; ENSP00000367813; ENSG00000138032.
ENST00000409432; ENSP00000387287; ENSG00000138032.
ENST00000409895; ENSP00000387341; ENSG00000138032.

GeneID

5495.

KEGG

hsa:5495.

UCSC

uc002rtt.3. human.
uc002rtv.3. human.
uc002rtw.3. human.

Organism-specific databases

CTD

5495.

GeneCards

GC02P044307.

HGNC

HGNC:9276. PPM1B.

HPA

HPA016745.

MIM

603770. gene.

neXtProt

NX_O75688.

Orphanet

163693. 2p21 microdeletion syndrome.

PharmGKB

PA33604.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0631.

HOGENOM

HOG000233895.

HOVERGEN

HBG053647.

InParanoid

O75688.

KO

K04461.

OMA

VMISPEH.

PhylomeDB

O75688.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

O75688.

Bgee

O75688.

CleanEx

HS_PPM1B.

Genevestigator

O75688.

GermOnline

ENSG00000138032. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.430. 1 hit.
3.60.40.10. 1 hit.

InterPro

IPR001932. PP2C-like.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]

PANTHER

PTHR13832. PTHR13832. 1 hit.

Pfam

PF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]

SMART

SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]

SUPFAM

SSF81606. PP2C-related. 1 hit.
SSF81601. PP2C_C. 1 hit.

PROSITE

PS01032. PP2C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O75688.

ChEMBL

CHEMBL2845.

EvolutionaryTrace

O75688.

GenomeRNAi

5495.

NextBio

21250.

SOURCE

Search...

Entry information

Entry name

PPM1B_HUMAN

Accession

Primary (citable) accession number: O75688
Secondary accession number(s): Q461Q2 , Q4J6C1, Q4J6C2, Q658R4, Q96ER6, Q9HAY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 137 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.