P62141 (PP1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

Ppp1cb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. 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 By similarity.
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. The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress 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. 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. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7 and PPP1R12C. Interacts with PPP1R12A and NUAK1; the interaction is direct. Interacts with TRIM28; the interaction is weak By similarity. Interacts with PPP1R15A; the interaction mediates 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 By similarity. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R15B; the interaction mediates binding to EIF2S1. Ref.5 Ref.6
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Nucleus › nucleoplasm By similarity. Nucleus › nucleolus By similarity. 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 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 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 protein dephosphorylation Inferred from direct assay PubMed 14640981. Source: MGI regulation of cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB regulation of glycogen biosynthetic process Inferred from electronic annotation. Source: Compara regulation of glycogen catabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	MLL5-L complex Inferred from electronic annotation. Source: Compara PTW/PP1 phosphatase complex Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from direct assay PubMed 21471512. Source: MGI glycogen granule Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell protein phosphatase type 1 complex Inferred from electronic annotation. Source: Compara
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 sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 327	326	Serine/threonine-protein phosphatase PP1-beta catalytic subunit		PRO_0000058780
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 By similarity
	Modified residue	316	1	Phosphothreonine Ref.7
Experimental info
	Sequence conflict	64	1	I → N in BAC40733. Ref.2
	Sequence conflict	148	1	W → R in BAE42366. Ref.2
	Sequence conflict	223	1	S → F in BAE38902. Ref.2
	Sequence conflict	250	1	V → E in BAB23473. Ref.2
	Sequence conflict	269	1	P → S in BAE42366. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P62141 [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]	"The fission yeast dis2+ gene required for chromosome disjoining encodes one of two putative type 1 protein phosphatases." Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M. Cell 57:997-1007(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Dendritic cell, Embryonic head, Embryonic heart, Embryonic kidney, Lung, Mammary gland, Morula and Thymus.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[4]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 26-35; 60-73 AND 150-167, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[5]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP1R15B.
[6]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27073 mRNA. Translation: AAA37527.1. AK004686 mRNA. Translation: BAB23473.1. AK088893 mRNA. Translation: BAC40636.1. AK089067 mRNA. Translation: BAC40733.1. AK147112 mRNA. Translation: BAE27684.1. AK160743 mRNA. Translation: BAE35984.1. AK166168 mRNA. Translation: BAE38608.1. AK166623 mRNA. Translation: BAE38902.1. AK168141 mRNA. Translation: BAE40108.1. AK169379 mRNA. Translation: BAE41126.1. AK171283 mRNA. Translation: BAE42366.1. BC046832 mRNA. Translation: AAH46832.1.
IPI	IPI00311873.
PIR	D32550.
RefSeq	NP_766295.2. NM_172707.3.
UniGene	Mm.241931. Mm.456635.
3D structure databases
ProteinModelPortal	P62141.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62141. 6 interactions.
STRING	10090.ENSMUSP00000015100.
PTM databases
PhosphoSite	P62141.
Proteomic databases
PaxDb	P62141.
PRIDE	P62141.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000015100; ENSMUSP00000015100; ENSMUSG00000014956. ENSMUST00000131300; ENSMUSP00000121550; ENSMUSG00000014956.
GeneID	19046.
KEGG	mmu:19046.
Organism-specific databases
CTD	5500.
MGI	MGI:104871. Ppp1cb.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000062911.
HOVERGEN	HBG000216.
InParanoid	Q542E7.
KO	K06269.
OMA	PDLQGME.
OrthoDB	EOG4MKNGK.
Gene expression databases
Bgee	P62141.
Genevestigator	P62141.
GermOnline	ENSMUSG00000014956. Mus musculus.
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	P62141.
ChEMBL	CHEMBL2296.
ChiTaRS	PPP1CB. mouse.
NextBio	295509.
SOURCE	Search...

Entry information

Entry name

PP1B_MOUSE

Accession

Primary (citable) accession number: P62141
Secondary accession number(s): P37140 , Q3TBE5, Q3TL90, Q542E7, Q8C285, Q9DBY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program