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P62207 (PP1B_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.3

[Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate. Ref.3

Cofactor

Binds 2 manganese ions per subunit. Ref.4

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, PPP1R3B, PPP1R3C and PPP1R3D mediate binding to glycogen By similarity. Ref.3 Ref.4

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Detected in gizzard (at protein level). Ref.4

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 327326Serine/threonine-protein phosphatase PP1-beta catalytic subunit
PRO_0000058784

Sites

Active site1241Proton donor By similarity
Metal binding631Manganese 1
Metal binding651Manganese 1
Metal binding911Manganese 1
Metal binding911Manganese 2
Metal binding1231Manganese 2
Metal binding1721Manganese 2
Metal binding2471Manganese 2

Amino acid modifications

Modified residue21N-acetylalanine Ref.2

Secondary structure

...................................................... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62207 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E8356022E9B94ECD

FASTA32737,187
        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 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D37987 mRNA. Translation: BAA07203.1.
RefSeqNP_990453.1. NM_205122.1.
UniGeneGga.1250.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S70X-ray2.70A1-327[»]
ProteinModelPortalP62207.
SMRP62207. Positions 1-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676289. 2 interactions.

Chemistry

BindingDBP62207.

Proteomic databases

PaxDbP62207.
PRIDEP62207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000031908; ENSGALP00000031272; ENSGALG00000010026.
GeneID396019.
KEGGgga:396019.

Organism-specific databases

CTD5500.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000062911.
HOGENOMHOG000172697.
HOVERGENHBG000216.
InParanoidP62207.
KOK06269.
OMAPDLQGME.
OrthoDBEOG7TJ3K3.
PhylomeDBP62207.
TreeFamTF354243.

Enzyme and pathway databases

BRENDA3.1.3.16. 1306.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62207.
NextBio20816081.
PROP62207.

Entry information

Entry namePP1B_CHICK
AccessionPrimary (citable) accession number: P62207
Secondary accession number(s): P37140
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 82 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references