SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P62207

- PP1B_CHICK

UniProt

P62207 - PP1B_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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.

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 donor By similarity
Metal bindingi172 – 1721Manganese 2
Metal bindingi247 – 2471Manganese 2

GO - Molecular functioni

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

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. glycogen metabolic process Source: UniProtKB-KW
  4. protein dephosphorylation Source: Ensembl
  5. 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.

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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 3

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. MLL5-L complex Source: Ensembl
  2. PTW/PP1 phosphatase complex Source: UniProtKB
  3. cytoplasm Source: UniProtKB-SubCell
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 subunit
PRO_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.2 Publications

Protein-protein interaction databases

BioGridi676289. 2 interactions.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S70X-ray2.70A1-327[»]
ProteinModelPortaliP62207.
SMRiP62207. Positions 1-308.

Miscellaneous databases

EvolutionaryTraceiP62207.

Family & Domainsi

Sequence similaritiesi

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

MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI    50
LLELEAPLKI CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL 100
ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRFNIKLWKT 150
FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDTGLL 200
CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL DLICRAHQVV 250
EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK 300
KAKYQYGGLN SGRPVTPPRT ANPPKKR 327
Length:327
Mass (Da):37,187
Last modified:January 23, 2007 - v3
Checksum:iE8356022E9B94ECD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D37987 mRNA. Translation: BAA07203.1 .
RefSeqi NP_990453.1. NM_205122.1.
UniGenei Gga.1250.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Chemistry

BindingDBi P62207.

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.

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: September 3, 2014
This is version 83 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

Similar proteinsi