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Q10728

- MYPT1_RAT

UniProt

Q10728 - MYPT1_RAT

Protein

Protein phosphatase 1 regulatory subunit 12A

Gene

Ppp1r12a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (16 Jan 2004)
      Previous versions | rss
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    Functioni

    Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity By similarity.By similarity

    GO - Molecular functioni

    1. 14-3-3 protein binding Source: UniProtKB
    2. enzyme inhibitor activity Source: UniProtKB
    3. phosphatase regulator activity Source: UniProtKB
    4. phosphoprotein phosphatase activity Source: RGD
    5. protein binding Source: IntAct

    GO - Biological processi

    1. centrosome organization Source: UniProtKB
    2. mitotic nuclear division Source: UniProtKB
    3. negative regulation of catalytic activity Source: UniProtKB
    4. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    5. protein dephosphorylation Source: UniProtKB
    6. regulation of cell adhesion Source: UniProtKB
    7. regulation of myosin-light-chain-phosphatase activity Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 1 regulatory subunit 12A
    Alternative name(s):
    MBSP
    Myosin phosphatase-targeting subunit 1
    Short name:
    Myosin phosphatase target subunit 1
    Protein phosphatase myosin-binding subunit
    Protein phosphatase subunit 1M
    Short name:
    PP-1M
    Serine/threonine protein phosphatase PP1 smooth muscle regulatory subunit M110
    Gene namesi
    Name:Ppp1r12a
    Synonyms:Mbs, Mypt1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620013. Ppp1r12a.

    Subcellular locationi

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

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB-SubCell
    3. kinetochore Source: UniProtKB
    4. PTW/PP1 phosphatase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10321032Protein phosphatase 1 regulatory subunit 12APRO_0000067027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
    Modified residuei100 – 1001(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
    Modified residuei226 – 2261(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
    Modified residuei299 – 2991PhosphoserineBy similarity
    Modified residuei422 – 4221PhosphoserineBy similarity
    Modified residuei432 – 4321PhosphoserineBy similarity
    Modified residuei443 – 4431PhosphothreonineBy similarity
    Modified residuei445 – 4451Phosphoserine; by NUAK1By similarity
    Modified residuei472 – 4721Phosphoserine; by NUAK1By similarity
    Modified residuei473 – 4731Phosphoserine; by CDK1By similarity
    Modified residuei477 – 4771PhosphoserineBy similarity
    Modified residuei507 – 5071PhosphoserineBy similarity
    Modified residuei601 – 6011PhosphoserineBy similarity
    Modified residuei669 – 6691PhosphoserineBy similarity
    Modified residuei693 – 6931Phosphoserine; by PKA and PKG; in vitroBy similarity
    Modified residuei696 – 6961Phosphoserine; by PKA and PKG; in vitroBy similarity
    Modified residuei697 – 6971Phosphothreonine; by ROCK1, ROCK2, CDC42BP, ZIPK/DAPK3 and RAF12 Publications
    Modified residuei854 – 8541Phosphoserine; by ROCK21 Publication
    Modified residuei864 – 8641PhosphoserineBy similarity
    Modified residuei873 – 8731PhosphoserineBy similarity
    Modified residuei912 – 9121Phosphoserine; by NUAK1Curated
    Modified residuei997 – 9971Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on upon DNA damage, probably by ATM or ATR By similarity. Phosphorylated by CIT (Rho-associated kinase). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-697. In vitro, phosphorylation of Ser-696 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-697, probably mediated by PRKG1 By similarity. Phosphorylated on upon DNA damage, probably by ATM or ATR By similarity. Phosphorylated by CIT (Rho-associated kinase). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-697. May be phosphorylated at Thr-697 by DMPK; may inhibit the myosin phosphatase activity. Phosphorylated at Ser-473 by CDK1 during mitosis, creating docking sites for the POLO box domains of PLK1. Subsequently, PLK1 binds and phosphorylates PPP1R12A By similarity.By similarity

    Keywords - PTMi

    Hydroxylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ10728.
    PRIDEiQ10728.

    PTM databases

    PhosphoSiteiQ10728.

    Expressioni

    Tissue specificityi

    Smooth muscle. Detected in aorta, portal vein, stomach, intestine, bladder and lung.1 Publication

    Gene expression databases

    GenevestigatoriQ10728.

    Interactioni

    Subunit structurei

    PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12A mediates binding to myosin. Binds PPP1R12B, ROCK1 and IL16. Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-912) with 14-3-3 By similarity. Interacts with ARHA and CIT. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A By similarity. Interacts with SMTNL1 By similarity. Interacts with ROCK1 and ROCK2. Interacts with ZIPK/DAPK3 By similarity. Interacts with RAF1 By similarity. Interacts with HIF1AN By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MPRIPQ6WCQ16EBI-918263,EBI-1022605From a different organism.
    NF2P352402EBI-918263,EBI-1014472From a different organism.

    Protein-protein interaction databases

    IntActiQ10728. 4 interactions.
    MINTiMINT-4596910.
    STRINGi10116.ENSRNOP00000062297.

    Structurei

    3D structure databases

    ProteinModelPortaliQ10728.
    SMRiQ10728. Positions 1-291.
    ModBaseiSearch...
    MobiDBiSearch...

    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
    Regioni683 – 866184Interaction with ROCK2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi35 – 384KVKF motif

    Domaini

    Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase.By similarity
    The KVKF motif mediates interaction with PPP1CB.By similarity

    Sequence similaritiesi

    Contains 6 ANK repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000290648.
    HOVERGENiHBG052561.
    InParanoidiQ10728.
    KOiK06270.
    PhylomeDBiQ10728.

    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. 2 hits.
    [Graphical view]
    PIRSFiPIRSF038141. PP1_12ABC_vert. 1 hit.
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 6 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q10728-1) [UniParc]FASTAAdd to Basket

    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 RQKTKVKFDD GAVFLAACSS     50
    GDTDEVLKLL HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN 100
    QPDNEGWIPL HAAASCGYLD IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA 150
    MEELLQNEVN RQGVDIEAAR KEEERIMLRD ARQWLNSGHI SDVRHAKSGG 200
    TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA HWGKEEACRI 250
    LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 300
    LIESTANMEN NQPQKTFKNK ETLIIEPEKN ASRIESLEQE KADEEEEGKK 350
    DESSCSSEED EEDDSESEAE TDKTKPMASV TNAHTASTQA APAAVTTPTL 400
    SSNQGTPTSP VKKFPTSTTK ISPKEEERKD ESPASWRLGL RKTGSYGALA 450
    EITASKEAQK EKDTAGVIRS ASSPRLSSSL DNKEKEKDNK GTRLAYVAPT 500
    IPRRLGSTSD IEEKENRESS NLRTSSSYTR RKWEDDLKKN SSINEGSTYH 550
    RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQKSFLSST STTAKTPPGS 600
    SPAGTQSSTS NRLWAEDSTE KEKDSAPTAA TILVAPTVVS AAASSTTALT 650
    TTTAGTLSST SEVRERRRSY LTPVRDEESE SQRKARSRQA RQSRRSTQGV 700
    TLTDLQEAEK TIGRSRSTRT REQENEEKDK EEKEKQDKEK QEEKKESEVS 750
    REDEYKQKYS RTYDETYARY RPVSTSSSST PSSSSLSTLG SSLYASSQLN 800
    RPNSLVGITS AYSRGLTKDN EREGEKKEEE KEGEDKSQPK SIRERRRPRE 850
    KRRSTGVSFW TQDSDENEQE RQSDTEDGSS KRDTQTDSVS RYDSSSTSSS 900
    DRYDSLLGRS ASYSYLEERK PYGSRLEKDD STDFKKLYEQ ILAENEKLKA 950
    QLHDTNMELT DLKLQLEKAT QRQERFADRS LLEMEKRERR ALERRISEME 1000
    EELKMLPDLK ADNQRLKDEN GALIRVISKL SK 1032
    Length:1,032
    Mass (Da):115,283
    Last modified:January 16, 2004 - v2
    Checksum:i43B9FC1569CD5DDB
    GO
    Isoform 2 (identifier: Q10728-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         608-667: Missing.

    Show »
    Length:972
    Mass (Da):109,116
    Checksum:iC9C80CD420FCE751
    GO
    Isoform 3 (identifier: Q10728-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         552-607: Missing.

    Show »
    Length:976
    Mass (Da):109,720
    Checksum:i9C25C0117ED89661
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111N → R in AAA92961. (PubMed:8543033)Curated
    Sequence conflicti316 – 3161T → N in AAA92961. (PubMed:8543033)Curated
    Sequence conflicti424 – 4241K → E in AAA92961. (PubMed:8543033)Curated
    Sequence conflicti579 – 5791A → P in AAA92961. (PubMed:8543033)Curated
    Sequence conflicti682 – 6821Q → H in AAA92961. (PubMed:8543033)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei552 – 60756Missing in isoform 3. 1 PublicationVSP_009255Add
    BLAST
    Alternative sequencei608 – 66760Missing in isoform 2. 1 PublicationVSP_009254Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S74907 mRNA. Translation: AAB32731.1.
    U50185 mRNA. Translation: AAA92961.1.
    AF110176 Genomic DNA. Translation: AAD34326.1.
    PIRiS68418.
    RefSeqiNP_446342.1. NM_053890.1. [Q10728-3]
    XP_006241377.1. XM_006241315.1. [Q10728-2]
    UniGeneiRn.162937.
    Rn.220285.

    Genome annotation databases

    GeneIDi116670.
    KEGGirno:116670.
    UCSCiRGD:620013. rat. [Q10728-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S74907 mRNA. Translation: AAB32731.1 .
    U50185 mRNA. Translation: AAA92961.1 .
    AF110176 Genomic DNA. Translation: AAD34326.1 .
    PIRi S68418.
    RefSeqi NP_446342.1. NM_053890.1. [Q10728-3 ]
    XP_006241377.1. XM_006241315.1. [Q10728-2 ]
    UniGenei Rn.162937.
    Rn.220285.

    3D structure databases

    ProteinModelPortali Q10728.
    SMRi Q10728. Positions 1-291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q10728. 4 interactions.
    MINTi MINT-4596910.
    STRINGi 10116.ENSRNOP00000062297.

    PTM databases

    PhosphoSitei Q10728.

    Proteomic databases

    PaxDbi Q10728.
    PRIDEi Q10728.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 116670.
    KEGGi rno:116670.
    UCSCi RGD:620013. rat. [Q10728-1 ]

    Organism-specific databases

    CTDi 4659.
    RGDi 620013. Ppp1r12a.

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000290648.
    HOVERGENi HBG052561.
    InParanoidi Q10728.
    KOi K06270.
    PhylomeDBi Q10728.

    Miscellaneous databases

    NextBioi 619487.
    PROi Q10728.

    Gene expression databases

    Genevestigatori Q10728.

    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. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF038141. PP1_12ABC_vert. 1 hit.
    PRINTSi PR01415. ANKYRIN.
    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. "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] (ISOFORM 3).
      Tissue: Aorta.
    2. "Molecular cloning and functional expression of a recombinant 72.5 kDa fragment of the 110 kDa regulatory subunit of smooth muscle protein phosphatase 1M."
      Haystead C.M.M., Gailly P., Somlyo A.P., Somlyo A.V., Haystead T.A.J.
      FEBS Lett. 377:123-127(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-728 (ISOFORM 2), FUNCTION.
      Strain: Wistar.
      Tissue: Kidney.
    3. "A myosin phosphatase targeting subunit isoform transition defines a smooth muscle developmental phenotypic switch."
      Dirksen W.P., Vladic F., Fisher S.A.
      Am. J. Physiol. 278:C589-C600(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 490-665 (ISOFORM 1), TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
      Strain: Sprague-Dawley.
    4. "Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)."
      Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M., Yamamori B., Feng J., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.
      Science 273:245-248(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH ARHA AND CIT.
    5. "Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo."
      Kawano Y., Fukata Y., Oshiro N., Amano M., Nakamura T., Ito M., Matsumura F., Inagaki M., Kaibuchi K.
      J. Cell Biol. 147:1023-1038(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-697 AND SER-854, INTERACTION WITH ROCK1.
    6. "Zipper-interacting protein kinase induces Ca(2+)-free smooth muscle contraction via myosin light chain phosphorylation."
      Niiro N., Ikebe M.
      J. Biol. Chem. 276:29567-29574(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-697 BY ZIPK/DAPK3.
    7. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
      Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
      Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-997, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "ROCK isoform regulation of myosin phosphatase and contractility in vascular smooth muscle cells."
      Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X., Surks H.K.
      Circ. Res. 104:531-540(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH ROCK1 AND ROCK2.

    Entry informationi

    Entry nameiMYPT1_RAT
    AccessioniPrimary (citable) accession number: Q10728
    Secondary accession number(s): Q62937, Q9WU33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: January 16, 2004
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3