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Q9DBR7

- MYPT1_MOUSE

UniProt

Q9DBR7 - MYPT1_MOUSE

Protein

Protein phosphatase 1 regulatory subunit 12A

Gene

Ppp1r12a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (15 Dec 2009)
      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. protein binding Source: UniProtKB

    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: MGI
    6. regulation of cell adhesion Source: UniProtKB
    7. regulation of myosin-light-chain-phosphatase activity Source: UniProtKB
    8. regulation of nucleocytoplasmic transport Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 1 regulatory subunit 12A
    Alternative name(s):
    Myosin phosphatase-targeting subunit 1
    Short name:
    Myosin phosphatase target subunit 1
    Gene namesi
    Name:Ppp1r12a
    Synonyms:Mypt1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1309528. Ppp1r12a.

    Subcellular locationi

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

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. contractile fiber Source: Ensembl
    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 – 10291029Protein phosphatase 1 regulatory subunit 12APRO_0000067026Add
    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 – 4431Phosphothreonine1 Publication
    Modified residuei445 – 4451Phosphoserine; alternate2 Publications
    Modified residuei445 – 4451Phosphoserine; by NUAK1; alternate2 Publications
    Modified residuei472 – 4721Phosphoserine; by NUAK1By similarity
    Modified residuei473 – 4731Phosphoserine; by CDK1By similarity
    Modified residuei477 – 4771PhosphoserineBy similarity
    Modified residuei507 – 5071Phosphoserine1 Publication
    Modified residuei601 – 6011PhosphoserineBy similarity
    Modified residuei666 – 6661Phosphoserine1 Publication
    Modified residuei690 – 6901Phosphoserine; by PKA and PKG; in vitroBy similarity
    Modified residuei693 – 6931Phosphoserine; by PKA and PKG; in vitroBy similarity
    Modified residuei694 – 6941Phosphothreonine; by ROCK1, ROCK2, CDC42BP, ZIPK/DAPK3 and RAF11 Publication
    Modified residuei851 – 8511Phosphoserine; by ROCK2By similarity
    Modified residuei861 – 8611PhosphoserineBy similarity
    Modified residuei870 – 8701Phosphoserine1 Publication
    Modified residuei909 – 9091Phosphoserine; by NUAK11 Publication
    Modified residuei994 – 9941PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by CIT (Rho-associated kinase) By similarity. Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-694 By similarity. Phosphorylated on upon DNA damage, probably by ATM or ATR. In vitro, phosphorylation of Ser-693 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-694, probably mediated by PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-909 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2. May be phosphorylated at Thr-694 by DMPK; may inhibit the myosin phosphatase activity By similarity. 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

    MaxQBiQ9DBR7.
    PaxDbiQ9DBR7.
    PRIDEiQ9DBR7.

    PTM databases

    PhosphoSiteiQ9DBR7.

    Miscellaneous databases

    PMAP-CutDBQ9DBR7.

    Expressioni

    Tissue specificityi

    Expressed in striated and vascular smooth muscle, specificcally in type 2a fibers (at protein level). Expression levels are 20-30% higher in developed males than females (at protein level).1 Publication

    Developmental stagei

    In neonates, expressed at low levels in striated and smooth muscles. As the animals mature sexually, expression increases 10-20-fold. Pregnancy promotes a 2-3-fold increase in expression in striated, vascular and uterine muscle (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9DBR7.
    GenevestigatoriQ9DBR7.

    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 By similarity. Interacts with ARHA and CIT. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-909) with 14-3-3 By similarity. Interacts with SMTNL1. Interacts with ZIPK/DAPK3 By similarity. Interacts with RAF1 By similarity. Interacts with HIF1AN By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-29982N.
    IntActiQ9DBR7. 3 interactions.
    MINTiMINT-4102998.
    STRINGi10090.ENSMUSP00000100915.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBR7.
    SMRiQ9DBR7. Positions 1-291, 656-712.
    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
    Regioni680 – 863184Interaction with ROCK2By similarityAdd
    BLAST

    Motif

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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi335 – 37036Glu/Ser-richAdd
    BLAST
    Compositional biasi771 – 79424Ser-richAdd
    BLAST

    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.
    GeneTreeiENSGT00730000110434.
    HOGENOMiHOG000290648.
    HOVERGENiHBG052561.
    InParanoidiQ05A74.
    KOiK06270.
    OMAiTDKQTTT.
    OrthoDBiEOG7060Q5.
    PhylomeDBiQ9DBR7.
    TreeFamiTF105543.

    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9DBR7-1) [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 KEEERVMLRD ARQWLNSGHI SDVRHAKSGG 200
    TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA HWGKEEACRI 250
    LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQTLL HSEKRDKKSP 300
    LIESTANMEN NQPQKAFKNK ETLIIEPEKN ASRIESLEHE KADEEEEGKK 350
    DESSCSSEED EEDDSESEAE TDKTKPMASV SNAHTSSTQA APAAVTAPTL 400
    SSNQGTPTSP VKKFPISTTK ISPKEEERKD ESPASWRLGL RKTGSYGALA 450
    EISASKEAQK EKDTAGVMRS ASSPRLSSSL DNKEKEKDNK GTRLAYVTPT 500
    IPRRLASTSD IEEKENRESS SLRTSSSYTR RKWEDDLKKN SSINEGSTYH 550
    RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQRSLPSST STAAKTPPGS 600
    SSAGTQSSTS NRLWAEDSTE KEKDSAPTAV TIPVAPTVVN AAAPSTTTLT 650
    TTTAGTVSEV RERRRSYLTP VRDEESESQR KARSRQARQS RRSTQGVTLT 700
    DLQEAEKTIG RSRSTRTREQ ENEEKEKEEK EKQDKEKQEE KKESEASRED 750
    EYKQKYSRTY DETYTRYRPV STSSSSAPSS SSLSTLGSTL YASSQLNRPN 800
    SLVGITSAYS RGLAKENERE GEKKEEEKEG EDKSQPKSIR ERRRPREKRR 850
    STGVSFWTQD SDENEQERQS DTEDGSSKRE TQTDSVSRYD SSSTSSSDRY 900
    DSLLGRSASY SYLEDRKPYS SRLEKDDSTD FKKLYEQILA ENEKLKAQLH 950
    DTNMELTDLK LQLEKATQRQ ERFADRSQLE MEKRERRALE RRISEMEEEL 1000
    KMLPDLKADN QRLKDENGAL IRVISKLSK 1029
    Length:1,029
    Mass (Da):114,996
    Last modified:December 15, 2009 - v2
    Checksum:iC466573AC1DFC81F
    GO
    Isoform 2 (identifier: Q9DBR7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         985-1029: ERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK → VAGKSQYLLGGTKSSRKKNI

    Show »
    Length:1,004
    Mass (Da):111,809
    Checksum:i1CF7118111B85BF1
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei985 – 102945ERRAL…SKLSK → VAGKSQYLLGGTKSSRKKNI in isoform 2. 1 PublicationVSP_038478Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK035230 mRNA. Translation: BAC28990.1.
    AK004785 mRNA. Translation: BAB23563.1.
    CH466539 Genomic DNA. Translation: EDL21703.1.
    BC125381 mRNA. Translation: AAI25382.1.
    BC137630 mRNA. Translation: AAI37631.1.
    AB042280 Genomic DNA. Translation: BAB39108.1.
    CCDSiCCDS36052.1. [Q9DBR7-2]
    RefSeqiNP_082168.1. NM_027892.2. [Q9DBR7-2]
    XP_006513389.1. XM_006513326.1. [Q9DBR7-1]
    UniGeneiMm.422959.
    Mm.489819.

    Genome annotation databases

    EnsembliENSMUST00000070663; ENSMUSP00000069257; ENSMUSG00000019907. [Q9DBR7-2]
    GeneIDi17931.
    KEGGimmu:17931.
    UCSCiuc007gzc.1. mouse. [Q9DBR7-2]
    uc007gzd.1. mouse. [Q9DBR7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK035230 mRNA. Translation: BAC28990.1 .
    AK004785 mRNA. Translation: BAB23563.1 .
    CH466539 Genomic DNA. Translation: EDL21703.1 .
    BC125381 mRNA. Translation: AAI25382.1 .
    BC137630 mRNA. Translation: AAI37631.1 .
    AB042280 Genomic DNA. Translation: BAB39108.1 .
    CCDSi CCDS36052.1. [Q9DBR7-2 ]
    RefSeqi NP_082168.1. NM_027892.2. [Q9DBR7-2 ]
    XP_006513389.1. XM_006513326.1. [Q9DBR7-1 ]
    UniGenei Mm.422959.
    Mm.489819.

    3D structure databases

    ProteinModelPortali Q9DBR7.
    SMRi Q9DBR7. Positions 1-291, 656-712.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29982N.
    IntActi Q9DBR7. 3 interactions.
    MINTi MINT-4102998.
    STRINGi 10090.ENSMUSP00000100915.

    PTM databases

    PhosphoSitei Q9DBR7.

    Proteomic databases

    MaxQBi Q9DBR7.
    PaxDbi Q9DBR7.
    PRIDEi Q9DBR7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000070663 ; ENSMUSP00000069257 ; ENSMUSG00000019907 . [Q9DBR7-2 ]
    GeneIDi 17931.
    KEGGi mmu:17931.
    UCSCi uc007gzc.1. mouse. [Q9DBR7-2 ]
    uc007gzd.1. mouse. [Q9DBR7-1 ]

    Organism-specific databases

    CTDi 4659.
    MGIi MGI:1309528. Ppp1r12a.

    Phylogenomic databases

    eggNOGi COG0666.
    GeneTreei ENSGT00730000110434.
    HOGENOMi HOG000290648.
    HOVERGENi HBG052561.
    InParanoidi Q05A74.
    KOi K06270.
    OMAi TDKQTTT.
    OrthoDBi EOG7060Q5.
    PhylomeDBi Q9DBR7.
    TreeFami TF105543.

    Enzyme and pathway databases

    Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    ChiTaRSi PPP1R12A. mouse.
    NextBioi 292815.
    PMAP-CutDB Q9DBR7.
    PROi Q9DBR7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9DBR7.
    Genevestigatori Q9DBR7.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Lung and Urinary bladder.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Molecular cloning and analysis of the 5'-flanking region of human MYPT1 gene."
      Machida H., Ito M., Okamoto R., Shiraki K., Isaka N., Hartshorne D.J., Nakano T.
      Biochim. Biophys. Acta 1517:424-429(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
    5. "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.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy."
      Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S., Zheng D., Devente J., Hickner R., Haystead T.A.
      J. Biol. Chem. 285:29357-29366(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMTNL1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiMYPT1_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBR7
    Secondary accession number(s): Q05A74, Q8CBV2, Q99NB6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 114 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3