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P62207

- PP1B_CHICK

UniProt

P62207 - PP1B_CHICK

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Protein

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Gene

PPP1CB

Organism
Gallus gallus (Chicken)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Manganese 1
Metal bindingi65 – 651Manganese 1
Metal bindingi91 – 911Manganese 1
Metal bindingi91 – 911Manganese 2
Metal bindingi123 – 1231Manganese 2
Active sitei124 – 1241Proton donorBy similarity
Metal bindingi172 – 1721Manganese 2
Metal bindingi247 – 2471Manganese 2

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. myosin-light-chain-phosphatase activity Source: UniProtKB
  3. myosin phosphatase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. circadian regulation of gene expression Source: Ensembl
  4. entrainment of circadian clock by photoperiod Source: Ensembl
  5. glycogen metabolic process Source: UniProtKB-KW
  6. protein dephosphorylation Source: Ensembl
  7. regulation of cell adhesion Source: UniProtKB
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.
ReactomeiREACT_197901. Regulation of PLK1 Activity at G2/M Transition.
REACT_252130. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 3

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: Ensembl
  3. MLL5-L complex Source: Ensembl
  4. PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 327326Serine/threonine-protein phosphatase PP1-beta catalytic subunitPRO_0000058784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP62207.
PRIDEiP62207.

Expressioni

Tissue specificityi

Detected in gizzard (at protein level).1 Publication

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 interactions.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 169Combined sources
Turni17 – 204Combined sources
Helixi31 – 4515Combined sources
Beta strandi50 – 545Combined sources
Beta strandi56 – 616Combined sources
Helixi68 – 7811Combined sources
Beta strandi86 – 883Combined sources
Beta strandi93 – 975Combined sources
Helixi99 – 11214Combined sources
Turni114 – 1163Combined sources
Beta strandi117 – 1193Combined sources
Helixi127 – 1304Combined sources
Helixi135 – 1428Combined sources
Helixi145 – 15511Combined sources
Beta strandi161 – 1644Combined sources
Turni165 – 1673Combined sources
Beta strandi168 – 1703Combined sources
Helixi183 – 1864Combined sources
Beta strandi196 – 1983Combined sources
Helixi199 – 2057Combined sources
Beta strandi213 – 2175Combined sources
Beta strandi221 – 2266Combined sources
Helixi228 – 23811Combined sources
Beta strandi241 – 2455Combined sources
Beta strandi252 – 2576Combined sources
Turni258 – 2614Combined sources
Beta strandi262 – 2665Combined sources
Helixi271 – 2733Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi289 – 2924Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S70X-ray2.70A1-327[»]
ProteinModelPortaliP62207.
SMRiP62207. Positions 1-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62207.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP62207.
KOiK06269.
OMAiPDLQGME.
OrthoDBiEOG7TJ3K3.
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.
[Graphical view]
PfamiPF00149. Metallophos. 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

EnsembliENSGALT00000031908; ENSGALP00000031272; ENSGALG00000010026.
GeneIDi396019.
KEGGigga:396019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37987 mRNA. Translation: BAA07203.1 .
RefSeqi NP_990453.1. NM_205122.1.
UniGenei Gga.1250.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1S70 X-ray 2.70 A 1-327 [» ]
ProteinModelPortali P62207.
SMRi P62207. Positions 1-308.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 676289. 2 interactions.

Proteomic databases

PaxDbi P62207.
PRIDEi P62207.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSGALT00000031908 ; ENSGALP00000031272 ; ENSGALG00000010026 .
GeneIDi 396019.
KEGGi gga:396019.

Organism-specific databases

CTDi 5500.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000062911.
HOGENOMi HOG000172697.
HOVERGENi HBG000216.
InParanoidi P62207.
KOi K06269.
OMAi PDLQGME.
OrthoDBi EOG7TJ3K3.
PhylomeDBi P62207.
TreeFami TF354243.

Enzyme and pathway databases

BRENDAi 3.1.3.16. 1306.
Reactomei REACT_197901. Regulation of PLK1 Activity at G2/M Transition.
REACT_252130. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

EvolutionaryTracei P62207.
NextBioi 20816081.
PROi P62207.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase."
    Shimizu H., Ito M., Miyahara M., Ichikawa K., Okubo S., Konishi T., Naka M., Tanaka T., Hirano K., Hartshorne D.J., Nakano T.
    J. Biol. Chem. 269:30407-30411(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Gizzard.
  2. Bienvenut W.V., Black E.J., Gillespie D.A.
    Submitted (JAN-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14 AND 111-121, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  3. "The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1."
    Alessi D., MacDougall L.K., Sola M.M., Ikebe M., Cohen P.
    Eur. J. Biochem. 210:1023-1035(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 147-149; 168-185; 221-233; 246-259 AND 304-319, CATALYTIC ACTIVITY, SUBUNIT.
    Tissue: Gizzard.
  4. "Structural basis of protein phosphatase 1 regulation."
    Terrak M., Kerff F., Langsetmo K., Tao T., Dominguez R.
    Nature 429:780-784(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND PPP1R12A, COFACTOR, TISSUE SPECIFICITY, SUBUNIT.

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 26, 2014
This is version 86 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

External Data

Dasty 3