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Q10728

- MYPT1_RAT

UniProt

Q10728 - MYPT1_RAT

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Protein

Protein phosphatase 1 regulatory subunit 12A

Gene
Ppp1r12a, Mbs, Mypt1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

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
Complete GO annotation...

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
Complete GO annotation...

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 HIF1AN By similarity
Modified residuei100 – 1001(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residuei226 – 2261(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residuei299 – 2991Phosphoserine By similarity
Modified residuei422 – 4221Phosphoserine By similarity
Modified residuei432 – 4321Phosphoserine By similarity
Modified residuei443 – 4431Phosphothreonine By similarity
Modified residuei445 – 4451Phosphoserine; by NUAK1 By similarity
Modified residuei472 – 4721Phosphoserine; by NUAK1 By similarity
Modified residuei473 – 4731Phosphoserine; by CDK1 By similarity
Modified residuei477 – 4771Phosphoserine By similarity
Modified residuei507 – 5071Phosphoserine By similarity
Modified residuei601 – 6011Phosphoserine By similarity
Modified residuei669 – 6691Phosphoserine By similarity
Modified residuei693 – 6931Phosphoserine; by PKA and PKG; in vitro By similarity
Modified residuei696 – 6961Phosphoserine; by PKA and PKG; in vitro By similarity
Modified residuei697 – 6971Phosphothreonine; by ROCK1, ROCK2, CDC42BP, ZIPK/DAPK3 and RAF12 Publications
Modified residuei854 – 8541Phosphoserine; by ROCK21 Publication
Modified residuei864 – 8641Phosphoserine By similarity
Modified residuei873 – 8731Phosphoserine By similarity
Modified residuei912 – 9121Phosphoserine; by NUAK1 Inferred
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.4 Publications

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.3 Publications

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.

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.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei552 – 60756Missing in isoform 3. VSP_009255Add
BLAST
Alternative sequencei608 – 66760Missing in isoform 2. VSP_009254Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111N → R in AAA92961. 1 Publication
Sequence conflicti316 – 3161T → N in AAA92961. 1 Publication
Sequence conflicti424 – 4241K → E in AAA92961. 1 Publication
Sequence conflicti579 – 5791A → P in AAA92961. 1 Publication
Sequence conflicti682 – 6821Q → H in AAA92961. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 124 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

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