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Protein

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Gene

PPP1CB

Organism
Gallus gallus (Chicken)
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.

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication
[Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate.1 Publication

Cofactori

Mn2+1 PublicationNote: Binds 2 manganese ions per subunit.1 Publication

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi63Manganese 11
Metal bindingi65Manganese 11
Metal bindingi91Manganese 11
Metal bindingi91Manganese 21
Metal bindingi123Manganese 21
Active sitei124Proton donorBy similarity1
Metal bindingi172Manganese 21
Metal bindingi247Manganese 21

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.16. 1306.
ReactomeiR-GGA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-GGA-5627123. RHO GTPases activate PAKs.

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
Gene namesi
Name:PPP1CB
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 3

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000587842 – 327Serine/threonine-protein phosphatase PP1-beta catalytic subunitAdd BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP62207.

Expressioni

Tissue specificityi

Detected in gizzard (at protein level).1 Publication

Gene expression databases

BgeeiENSGALG00000010026.

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, PPP1R3B, PPP1R3C and PPP1R3D mediate binding to glycogen (By similarity).By similarity

Protein-protein interaction databases

BioGridi676289. 2 interactors.
STRINGi9031.ENSGALP00000031272.

Structurei

Secondary structure

1327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 16Combined sources9
Turni17 – 20Combined sources4
Helixi31 – 45Combined sources15
Beta strandi50 – 54Combined sources5
Beta strandi56 – 61Combined sources6
Helixi68 – 78Combined sources11
Beta strandi86 – 88Combined sources3
Beta strandi93 – 97Combined sources5
Helixi99 – 112Combined sources14
Turni114 – 116Combined sources3
Beta strandi117 – 119Combined sources3
Helixi127 – 130Combined sources4
Helixi135 – 142Combined sources8
Helixi145 – 155Combined sources11
Beta strandi161 – 164Combined sources4
Turni165 – 167Combined sources3
Beta strandi168 – 170Combined sources3
Helixi183 – 186Combined sources4
Beta strandi196 – 198Combined sources3
Helixi199 – 205Combined sources7
Beta strandi213 – 217Combined sources5
Beta strandi221 – 226Combined sources6
Helixi228 – 238Combined sources11
Beta strandi241 – 245Combined sources5
Beta strandi252 – 257Combined sources6
Turni258 – 261Combined sources4
Beta strandi262 – 266Combined sources5
Helixi271 – 273Combined sources3
Beta strandi282 – 284Combined sources3
Beta strandi289 – 292Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S70X-ray2.70A1-327[»]
ProteinModelPortaliP62207.
SMRiP62207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62207.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IN85. Eukaryota.
ENOG410XPVF. LUCA.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP62207.
KOiK06269.
OMAiEFVRSCR.
OrthoDBiEOG091G0EKF.
PhylomeDBiP62207.
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.

P62207-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37987 mRNA. Translation: BAA07203.1.
RefSeqiNP_990453.1. NM_205122.1.
UniGeneiGga.1250.

Genome annotation databases

GeneIDi396019.
KEGGigga:396019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37987 mRNA. Translation: BAA07203.1.
RefSeqiNP_990453.1. NM_205122.1.
UniGeneiGga.1250.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S70X-ray2.70A1-327[»]
ProteinModelPortaliP62207.
SMRiP62207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676289. 2 interactors.
STRINGi9031.ENSGALP00000031272.

Proteomic databases

PaxDbiP62207.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396019.
KEGGigga:396019.

Organism-specific databases

CTDi5500.

Phylogenomic databases

eggNOGiENOG410IN85. Eukaryota.
ENOG410XPVF. LUCA.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP62207.
KOiK06269.
OMAiEFVRSCR.
OrthoDBiEOG091G0EKF.
PhylomeDBiP62207.
TreeFamiTF354243.

Enzyme and pathway databases

BRENDAi3.1.3.16. 1306.
ReactomeiR-GGA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-GGA-5627123. RHO GTPases activate PAKs.

Miscellaneous databases

EvolutionaryTraceiP62207.
PROiP62207.

Gene expression databases

BgeeiENSGALG00000010026.

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_CHICK
AccessioniPrimary (citable) accession number: P62207
Secondary accession number(s): P37140
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.