P62140 (PP1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Short name=PP-1B
Short name=PPP1CD
EC=3.1.3.16
EC=3.1.3.53

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. 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. Ref.23
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate. [Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Enzyme regulation	Inhibited by the toxins okadaic acid, tautomycin and microcystin Leu-Arg By similarity. 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.17
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. The targeting or regulatory subunits determine the substrate specificity of PP1. 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. 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 and PPP1R12C. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Interacts with PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with TRIM28; the interaction is weak. Interacts with PPP1R12A and NUAK1; the interaction is direct. Ref.12 Ref.14 Ref.15 Ref.19 Ref.23 Ref.24 Ref.25
Subcellular location	Cytoplasm. Nucleus. Nucleus › nucleoplasm. Nucleus › nucleolus. Note: Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. Ref.13
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
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
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 regulation of cell adhesion Inferred from direct assay Ref.24. Source: UniProtKB triglyceride catabolic process Traceable author statement. Source: Reactome
Cellular component	MLL5-L complex Inferred from direct assay Ref.22. Source: UniProtKB PTW/PP1 phosphatase complex Inferred from direct assay Ref.24Ref.23. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW myosin phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB myosin-light-chain-phosphatase activity Inferred from direct assay Ref.24. Source: UniProtKB protein kinase binding Inferred from physical interaction Ref.24. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRCA1	P38398	3	EBI-352350,EBI-349905

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.11
	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 Ref.11 Ref.21
	Modified residue	41	1	Phosphoserine Ref.16
	Modified residue	47	1	Phosphoserine Ref.16
	Modified residue	306	1	Phosphotyrosine Ref.18
	Modified residue	316	1	Phosphothreonine Ref.20 Ref.21
Experimental info
	Sequence conflict	51	1	L → P in AAV38549. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P62140 [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]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[7]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Endometrium.
[8]	"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].
[9]	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].
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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: 11739654] [Abstract] Cited for: SUBCELLULAR LOCATION.
[14]	"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.
[15]	"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.
[16]	"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: Cervix carcinoma.
[17]	"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.
[18]	"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. Tissue: Lung carcinoma.
[19]	"TIMAP is a positive regulator of pulmonary endothelial barrier function." Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C., Olah G., Verin A.D. Am. J. Physiol. 295:L440-L450(2008) [PubMed: 18586956] [Abstract] Cited for: INTERACTION WITH PPP1R16B.
[20]	"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. Tissue: Cervix carcinoma.
[21]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[22]	"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: 19377461] [Abstract] Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
[23]	"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: 20516061] [Abstract] Cited for: IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, INTERACTION WITH PPP1R8.
[24]	"New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion." Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M., Aizawa S., Prescott A.R., Alessi D.R. Sci. Signal. 3:RA25-RA25(2010) [PubMed: 20354225] [Abstract] Cited for: INTERACTION WITH NUAK1 AND PPP1R12A.
[25]	"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: 20424263] [Abstract] Cited for: INTERACTION WITH TRIM28.
[26]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases
EMBL GenBank DDBJ	X80910 mRNA. Translation: CAA56870.1. U11005 , U10998, U10999, U11000, U11001, U11002, U11003, U11004 Genomic DNA. Translation: AAA85093.1. AF092905 mRNA. Translation: AAF01137.1. CR542263 mRNA. Translation: CAG47059.1. CR542285 mRNA. Translation: CAG47080.1. BT019744 mRNA. Translation: AAV38549.1. AK312329 mRNA. Translation: BAG35251.1. BX647970 mRNA. No translation available. AC097724 Genomic DNA. Translation: AAY24124.1. CH471053 Genomic DNA. Translation: EAX00527.1. CH471053 Genomic DNA. Translation: EAX00528.1. CH471053 Genomic DNA. Translation: EAX00529.1. CH471053 Genomic DNA. Translation: EAX00530.1. BC002697 mRNA. Translation: AAH02697.1. BC012045 mRNA. Translation: AAH12045.1.
IPI	IPI00218236.
PIR	S41052.
RefSeq	NP_002700.1. NM_002709.2. NP_996759.1. NM_206876.1.
UniGene	Hs.591571. Hs.702907.
3D structure databases
ProteinModelPortal	P62140.
SMR	P62140. Positions 1-308.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62140. 15 interactions.
MINT	MINT-208135.
STRING	P62140.
PTM databases
PhosphoSite	P62140.
Polymorphism databases
DMDM	49065814.
2D gel databases
OGP	P37140.
Proteomic databases
PRIDE	P62140.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296122; ENSP00000296122; ENSG00000213639. ENST00000358506; ENSP00000351298; ENSG00000213639. ENST00000395366; ENSP00000378769; ENSG00000213639.
GeneID	5500.
KEGG	hsa:5500.
UCSC	uc002rmg.1. human.
Organism-specific databases
CTD	5500.
GeneCards	GC02P028974.
H-InvDB	HIX0001938.
HGNC	HGNC:9282. PPP1CB.
HPA	CAB022558.
MIM	600590. gene.
neXtProt	NX_P62140.
PharmGKB	PA33610.
GenAtlas	Search...
Phylogenomic databases
eggNOG	maNOG15965.
GeneTree	ENSGT00530000062911.
HOGENOM	HBG716770.
HOVERGEN	HBG000216.
InParanoid	P62140.
OMA	PDLQGME.
PhylomeDB	P62140.
Enzyme and pathway databases
Reactome	REACT_22258. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	P62140.
Bgee	P62140.
CleanEx	HS_PPP1CB.
Genevestigator	P62140.
GermOnline	ENSG00000163806. Homo sapiens.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
KO	K06269.
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
NextBio	21280.
SOURCE	Search...

Entry information

Entry name

PP1B_HUMAN

Accession

Primary (citable) accession number: P62140
Secondary accession number(s): B2R5V4 , D6W565, P37140, Q5U087, Q6FG45

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 99 of the entry and version 3 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.