Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P62207

- PP1B_CHICK

UniProt

P62207 - PP1B_CHICK

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.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. glycogen metabolic process Source: UniProtKB-KW
    4. protein dephosphorylation Source: Ensembl
    5. regulation of cell adhesion Source: UniProtKB

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

    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 – 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.
    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

    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: October 1, 2014
    This is version 84 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