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Q90623

- MYPT1_CHICK

UniProt

Q90623 - MYPT1_CHICK

Protein

Protein phosphatase 1 regulatory subunit 12A

Gene

PPP1R12A

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Regulates myosin phosphatase activity.1 Publication

    GO - Molecular functioni

    1. 14-3-3 protein binding Source: UniProtKB
    2. phosphatase regulator activity Source: UniProtKB

    GO - Biological processi

    1. regulation of cell adhesion Source: UniProtKB
    2. regulation of myosin-light-chain-phosphatase activity Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 1 regulatory subunit 12A
    Alternative name(s):
    130 kDa myosin-binding subunit of smooth muscle myosin phosphatase
    Myosin phosphatase-targeting subunit 1
    Short name:
    Myosin phosphatase target subunit 1
    PP1M subunit M110
    Protein phosphatase myosin-binding subunit
    Gene namesi
    Name:PPP1R12A
    Synonyms:MBS, MYPT1
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Cytoplasm By similarity
    Note: Along actomyosin filaments and stress fibers.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. PTW/PP1 phosphatase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi695 – 6951T → A: Reduces phosphorylation. Reduces phosphorylation on serine and threonine residues by 80%; when associated with A-850. 1 Publication
    Mutagenesisi850 – 8501T → A: Reduces phosphorylation. Reduces phosphorylation on serine and threonine residues by 80%; when associated with A-695. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10041004Protein phosphatase 1 regulatory subunit 12APRO_0000355556Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei695 – 6951Phosphothreonine; by ROCK23 Publications
    Modified residuei850 – 8501Phosphothreonine; by ROCK23 Publications

    Post-translational modificationi

    Phosphorylated by CIT (Rho-associated kinase) and by ROCK2 on serine and threonine residues. Phosphorylation at Thr-695 leads to inhibition of myosin phosphatase activity. Phosphorylation at Thr-850 abolishes myosin binding. May be phosphorylated at Thr-695 by DMPK; may inhibit the myosin phosphatase activity.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ90623.
    PRIDEiQ90623.

    Expressioni

    Tissue specificityi

    Detected in brain, lung, aorta, heart, gizzard, stomach, oviduct, spleen, kidney and small intestine.1 Publication

    Interactioni

    Subunit structurei

    PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits By similarity. PPP1R12A mediates binding to myosin.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi676290. 1 interaction.
    IntActiQ90623. 1 interaction.
    STRINGi9031.ENSGALP00000016789.

    Structurei

    Secondary structure

    1
    1004
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1916
    Turni20 – 223
    Helixi40 – 5011
    Helixi53 – 6210
    Helixi76 – 827
    Helixi86 – 949
    Helixi109 – 1168
    Helixi119 – 1279
    Helixi142 – 1454
    Helixi149 – 16214
    Helixi166 – 18722
    Turni196 – 1983
    Helixi202 – 2098
    Helixi212 – 2198
    Turni220 – 2223
    Helixi235 – 2417
    Helixi245 – 2539
    Turni268 – 2703
    Helixi275 – 2773
    Helixi278 – 2869

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S70X-ray2.70B1-299[»]
    DisProtiDP00218.
    ProteinModelPortaliQ90623.
    SMRiQ90623. Positions 1-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ90623.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati39 – 6830ANK 1Add
    BLAST
    Repeati72 – 10130ANK 2Add
    BLAST
    Repeati105 – 13430ANK 3Add
    BLAST
    Repeati138 – 16427ANK 4Add
    BLAST
    Repeati198 – 22730ANK 5Add
    BLAST
    Repeati231 – 26030ANK 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 384Important for interaction with PPP1CB

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi343 – 37028Asp/Glu-richAdd
    BLAST
    Compositional biasi514 – 660147Ser/Thr-richAdd
    BLAST
    Compositional biasi720 – 75132Asp/Glu/Lys-richAdd
    BLAST
    Compositional biasi771 – 81141Ser-richAdd
    BLAST
    Compositional biasi771 – 79323Ser/Thr-richAdd
    BLAST

    Sequence similaritiesi

    Contains 6 ANK repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000290648.
    HOVERGENiHBG052561.
    KOiK06270.
    PhylomeDBiQ90623.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR017401. Pase-1_reg_su_12A/B/C_euk.
    [Graphical view]
    PfamiPF12796. Ank_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038141. PP1_12ABC_vert. 1 hit.
    SMARTiSM00248. ANK. 6 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q90623-1) [UniParc]FASTAAdd to Basket

    Also known as: M133

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RKKTKVKFDD GAVFLAACSS     50
    GDTEEVLRLL ERGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN 100
    QPDNEGWIPL HAAASCGYLD IAEYLISQGA HVGAVNSEGD TPLDIAEEEA 150
    MEELLQNEVN RQGVDIEAAR KEEERIMLRD ARQWLNSGHI NDVRHAKSGG 200
    TALHVAAAKG YTEVLKLLIQ ARYDVNIKDY DGWTPLHAAA HWGKEEACRI 250
    LVENLCDMEA VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKREKKSP 300
    LIESTANLDN NQTQKTFKNK ETLIMEQEKN ASSIESLEHE KADEEEEGKK 350
    DESSCSSEEE EDDDSESEAE TDKAKTLANA NTTSTQSASM TAPSVAGGQG 400
    TPTSPLKKFP TSTTKVSPKE EERKDESPAS WRLGLRKTGS YGALAEITAS 450
    KEAQKEKDSA GVIRSASSPR LSSSLDNKEK EKDGKGTRLA YVAPTIPRRL 500
    ASTSDIDEKE NRDSSASSIR SGSSYARRKW EEDVKKNSLN EGPTSLNTSY 550
    QRSGSFGRRQ DDLVSSNVPS TASTVTSSAG LQKTLPASAN TTTKSTTGST 600
    SAGVQSSTSN RLWAEDSTEK EKDSVPTAVT VPVAPSVVNA AATTTAMTTA 650
    TSGTVSSTSE VRERRRSYLT PVRDEESESQ RKARSRQARQ SRRSTQGVTL 700
    TDLQEAEKTI GRSRSTRTRE QENEEKEKEE KEKQDKEKQE EKKESETKDD 750
    DYRQRYSRTV EEPYHRYRPT STSTSTSSTS SLSTSTSSLS SSSQLNRPNS 800
    LIGITSAYSR SGTKESEREG GKKEEEKEED KSQPKSIRER RRPREKRRST 850
    GVSFWTQDSD ENEQEHQSDS EEGTNKKETQ SDSLSRYDTG SLSVSSGDRY 900
    DSAQGRSGSQ SYLEDRKPYC SRLEKEDSTD FKKLYEQILA ENEKLKAQLH 950
    DTNMELTDLK LQLEKTTQRQ ERFADRSLLE MEKRVSGKSQ YLLGGKKSSR 1000
    KKDI 1004
    Length:1,004
    Mass (Da):111,606
    Last modified:November 1, 1996 - v1
    Checksum:i7ED870DB87046929
    GO
    Isoform 2 (identifier: Q90623-2) [UniParc]FASTAAdd to Basket

    Also known as: M130

    The sequence of this isoform differs from the canonical sequence as follows:
         512-552: Missing.

    Show »
    Length:963
    Mass (Da):106,975
    Checksum:i819D017491D02DB4
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei512 – 55241Missing in isoform 2. 1 PublicationVSP_035912Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D37985 mRNA. Translation: BAA07201.1.
    D37986 mRNA. Translation: BAA07202.1.
    S74623 mRNA. Translation: AAB32730.1.
    PIRiA55142.
    RefSeqiNP_990454.1. NM_205123.1. [Q90623-1]
    UniGeneiGga.3159.

    Genome annotation databases

    GeneIDi396020.
    KEGGigga:396020.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D37985 mRNA. Translation: BAA07201.1 .
    D37986 mRNA. Translation: BAA07202.1 .
    S74623 mRNA. Translation: AAB32730.1 .
    PIRi A55142.
    RefSeqi NP_990454.1. NM_205123.1. [Q90623-1 ]
    UniGenei Gga.3159.

    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 B 1-299 [» ]
    DisProti DP00218.
    ProteinModelPortali Q90623.
    SMRi Q90623. Positions 1-291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 676290. 1 interaction.
    IntActi Q90623. 1 interaction.
    STRINGi 9031.ENSGALP00000016789.

    Proteomic databases

    PaxDbi Q90623.
    PRIDEi Q90623.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396020.
    KEGGi gga:396020.

    Organism-specific databases

    CTDi 4659.

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000290648.
    HOVERGENi HBG052561.
    KOi K06270.
    PhylomeDBi Q90623.

    Miscellaneous databases

    EvolutionaryTracei Q90623.
    NextBioi 20816082.
    PROi Q90623.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR017401. Pase-1_reg_su_12A/B/C_euk.
    [Graphical view ]
    Pfami PF12796. Ank_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038141. PP1_12ABC_vert. 1 hit.
    SMARTi SM00248. ANK. 6 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    [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] (ISOFORMS 1 AND 2), PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, INTERACTION WITH MYOSIN, TISSUE SPECIFICITY.
      Tissue: Gizzard.
    2. "Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M."
      Chen Y.H., Chen M.X., Alessi D.R., Campbell D.G., Shanahan C., Cohen P., Cohen P.T.W.
      FEBS Lett. 356:51-55(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 681-1004, PARTIAL PROTEIN SEQUENCE.
      Tissue: Gizzard.
    3. "Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin."
      Velasco G., Armstrong C., Morrice N., Frame S., Cohen P.
      FEBS Lett. 527:101-104(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-695 AND THR-850.
    4. "Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase."
      Feng J., Ito M., Ichikawa K., Isaka N., Nishikawa M., Hartshorne D.J., Nakano T.
      J. Biol. Chem. 274:37385-37390(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-695 AND THR-850, MUTAGENESIS OF THR-695 AND THR-850.
    5. "Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity."
      Muranyi A., Zhang R., Liu F., Hirano K., Ito M., Epstein H.F., Hartshorne D.J.
      FEBS Lett. 493:80-84(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY DMPK.
    6. "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) OF 1-299 IN COMPLEX WITH PPP1CB.

    Entry informationi

    Entry nameiMYPT1_CHICK
    AccessioniPrimary (citable) accession number: Q90623
    Secondary accession number(s): Q10727, Q90624
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 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