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Protein

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Gene

PPP1CB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208).3 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
[Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

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.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi63Manganese 1By similarity1
Metal bindingi65Manganese 1By similarity1
Metal bindingi91Manganese 1By similarity1
Metal bindingi91Manganese 2By similarity1
Metal bindingi123Manganese 2By similarity1
Active sitei124Proton donorBy similarity1
Metal bindingi172Manganese 2By similarity1
Metal bindingi247Manganese 2By similarity1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • myosin-light-chain-phosphatase activity Source: UniProtKB
  • myosin phosphatase activity Source: UniProtKB
  • phosphatase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163806-MONOMER.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-400253. Circadian Clock.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5627117. RHO GTPases Activate ROCKs.
R-HSA-5627123. RHO GTPases activate PAKs.
SIGNORiP62140.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-beta catalytic subunit (EC:3.1.3.16, EC:3.1.3.53)
Short name:
PP-1B
Short name:
PPP1CD
Gene namesi
Name:PPP1CB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9282. PPP1CB.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication
  • Nucleusnucleoplasm 1 Publication
  • Nucleusnucleolus 1 Publication

  • 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.

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • glycogen granule Source: Ensembl
  • MLL5-L complex Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein phosphatase type 1 complex Source: Ensembl
  • PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Variants in PPP1CB may be a cause of susceptibility to rasopathy reminiscent of Noonan syndrome-like disorder with loose anagen hair (NSLH). Affected individuals show Noonan dysmorphic features such as macrocephaly, high forehead and low-set and posteriorly rotated ears, in association with some hair abnormality (slow-growing, very fine hair or unruly hair texture), developmental delay and mild ventriculomegaly.

Keywords - Diseasei

Disease mutation

Organism-specific databases

OpenTargetsiENSG00000213639.
PharmGKBiPA33610.

Polymorphism and mutation databases

BioMutaiPPP1CB.
DMDMi49065814.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000587792 – 327Serine/threonine-protein phosphatase PP1-beta catalytic subunitAdd BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei316PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62140.
PaxDbiP62140.
PeptideAtlasiP62140.
PRIDEiP62140.
TopDownProteomicsiP62140.

2D gel databases

OGPiP37140.

PTM databases

DEPODiP62140.
iPTMnetiP62140.
PhosphoSitePlusiP62140.
SwissPalmiP62140.

Expressioni

Inductioni

Up-regulated in synovial fluid mononuclear cells and peripheral blood mononuclear cells from patients with rheumatoid arthritis.1 Publication

Gene expression databases

BgeeiENSG00000213639.
CleanExiHS_PPP1CB.
ExpressionAtlasiP62140. baseline and differential.
GenevisibleiP62140. HS.

Organism-specific databases

HPAiCAB022558.
CAB069426.
HPA065425.

Interactioni

Subunit structurei

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 KMT2E/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. Interacts with FOXP3.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRCA1P383983EBI-352350,EBI-349905
ClockO087852EBI-352350,EBI-79859From a different organism.
CSRNP2Q9H1755EBI-352350,EBI-5235958
PPP1R13LQ8WUF53EBI-352350,EBI-5550163
PPP1R16AQ96I348EBI-352350,EBI-710402
PPP1R2P3Q6NXS15EBI-352350,EBI-10251630
PPP1R3CQ9UQK13EBI-352350,EBI-2506727
PPP1R7Q154354EBI-352350,EBI-1024281
SH2D4AQ9H78811EBI-352350,EBI-747035
TP53BP2Q13625-33EBI-352350,EBI-10175039

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111494. 237 interactors.
DIPiDIP-33220N.
IntActiP62140. 220 interactors.
MINTiMINT-208135.
STRINGi9606.ENSP00000296122.

Structurei

3D structure databases

ProteinModelPortaliP62140.
SMRiP62140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiENOG410IN85. Eukaryota.
ENOG410XPVF. LUCA.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP62140.
KOiK06269.
OMAiEFVRSCR.
OrthoDBiEOG091G0EKF.
PhylomeDBiP62140.
TreeFamiTF354243.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR031675. STPPase_N.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
PF16891. STPPase_N. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62140-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI
60 70 80 90 100
LLELEAPLKI CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL
110 120 130 140 150
ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRFNIKLWKT
160 170 180 190 200
FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDTGLL
210 220 230 240 250
CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL DLICRAHQVV
260 270 280 290 300
EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK
310 320
KAKYQYGGLN SGRPVTPPRT ANPPKKR
Length:327
Mass (Da):37,187
Last modified:January 23, 2007 - v3
Checksum:iE8356022E9B94ECD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51L → P in AAV38549 (Ref. 5) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07683949P → R Probable disease-associated mutation found in patients with rasopathy reminiscent of NSLH. 1 Publication1
Natural variantiVAR_07684056A → P Probable disease-associated mutation found in patients with rasopathy reminiscent of NSLH. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33169.1.
PIRiS41052.
RefSeqiNP_002700.1. NM_002709.2.
NP_996759.1. NM_206876.1.
UniGeneiHs.702907.

Genome annotation databases

EnsembliENST00000296122; ENSP00000296122; ENSG00000213639.
ENST00000358506; ENSP00000351298; ENSG00000213639.
ENST00000395366; ENSP00000378769; ENSG00000213639.
GeneIDi5500.
KEGGihsa:5500.

Cross-referencesi

Web resourcesi

Protein Spotlight

The things we forget - Issue 32 of March 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33169.1.
PIRiS41052.
RefSeqiNP_002700.1. NM_002709.2.
NP_996759.1. NM_206876.1.
UniGeneiHs.702907.

3D structure databases

ProteinModelPortaliP62140.
SMRiP62140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111494. 237 interactors.
DIPiDIP-33220N.
IntActiP62140. 220 interactors.
MINTiMINT-208135.
STRINGi9606.ENSP00000296122.

PTM databases

DEPODiP62140.
iPTMnetiP62140.
PhosphoSitePlusiP62140.
SwissPalmiP62140.

Polymorphism and mutation databases

BioMutaiPPP1CB.
DMDMi49065814.

2D gel databases

OGPiP37140.

Proteomic databases

EPDiP62140.
PaxDbiP62140.
PeptideAtlasiP62140.
PRIDEiP62140.
TopDownProteomicsiP62140.

Protocols and materials databases

DNASUi5500.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296122; ENSP00000296122; ENSG00000213639.
ENST00000358506; ENSP00000351298; ENSG00000213639.
ENST00000395366; ENSP00000378769; ENSG00000213639.
GeneIDi5500.
KEGGihsa:5500.

Organism-specific databases

CTDi5500.
GeneCardsiPPP1CB.
HGNCiHGNC:9282. PPP1CB.
HPAiCAB022558.
CAB069426.
HPA065425.
MIMi600590. gene.
neXtProtiNX_P62140.
OpenTargetsiENSG00000213639.
PharmGKBiPA33610.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IN85. Eukaryota.
ENOG410XPVF. LUCA.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP62140.
KOiK06269.
OMAiEFVRSCR.
OrthoDBiEOG091G0EKF.
PhylomeDBiP62140.
TreeFamiTF354243.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163806-MONOMER.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-400253. Circadian Clock.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5627117. RHO GTPases Activate ROCKs.
R-HSA-5627123. RHO GTPases activate PAKs.
SIGNORiP62140.

Miscellaneous databases

ChiTaRSiPPP1CB. human.
GeneWikiiPPP1CB.
GenomeRNAii5500.
PROiP62140.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000213639.
CleanExiHS_PPP1CB.
ExpressionAtlasiP62140. baseline and differential.
GenevisibleiP62140. HS.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR031675. STPPase_N.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
PF16891. STPPase_N. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPP1B_HUMAN
AccessioniPrimary (citable) accession number: P62140
Secondary accession number(s): B2R5V4
, D6W565, P37140, Q5U087, Q6FG45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.