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Q10728

- MYPT1_RAT

UniProt

Q10728 - MYPT1_RAT

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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

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

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-KW
  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 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
DAPK3O43293-22EBI-918263,EBI-9691390From a different organism.
MPRIPQ6WCQ16EBI-918263,EBI-1022605From a different organism.
NF2P352402EBI-918263,EBI-1014472From a different organism.

Protein-protein interaction databases

IntActiQ10728. 5 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

        10         20         30         40         50
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS
60 70 80 90 100
GDTDEVLKLL HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN
110 120 130 140 150
QPDNEGWIPL HAAASCGYLD IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA
160 170 180 190 200
MEELLQNEVN RQGVDIEAAR KEEERIMLRD ARQWLNSGHI SDVRHAKSGG
210 220 230 240 250
TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA HWGKEEACRI
260 270 280 290 300
LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP
310 320 330 340 350
LIESTANMEN NQPQKTFKNK ETLIIEPEKN ASRIESLEQE KADEEEEGKK
360 370 380 390 400
DESSCSSEED EEDDSESEAE TDKTKPMASV TNAHTASTQA APAAVTTPTL
410 420 430 440 450
SSNQGTPTSP VKKFPTSTTK ISPKEEERKD ESPASWRLGL RKTGSYGALA
460 470 480 490 500
EITASKEAQK EKDTAGVIRS ASSPRLSSSL DNKEKEKDNK GTRLAYVAPT
510 520 530 540 550
IPRRLGSTSD IEEKENRESS NLRTSSSYTR RKWEDDLKKN SSINEGSTYH
560 570 580 590 600
RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQKSFLSST STTAKTPPGS
610 620 630 640 650
SPAGTQSSTS NRLWAEDSTE KEKDSAPTAA TILVAPTVVS AAASSTTALT
660 670 680 690 700
TTTAGTLSST SEVRERRRSY LTPVRDEESE SQRKARSRQA RQSRRSTQGV
710 720 730 740 750
TLTDLQEAEK TIGRSRSTRT REQENEEKDK EEKEKQDKEK QEEKKESEVS
760 770 780 790 800
REDEYKQKYS RTYDETYARY RPVSTSSSST PSSSSLSTLG SSLYASSQLN
810 820 830 840 850
RPNSLVGITS AYSRGLTKDN EREGEKKEEE KEGEDKSQPK SIRERRRPRE
860 870 880 890 900
KRRSTGVSFW TQDSDENEQE RQSDTEDGSS KRDTQTDSVS RYDSSSTSSS
910 920 930 940 950
DRYDSLLGRS ASYSYLEERK PYGSRLEKDD STDFKKLYEQ ILAENEKLKA
960 970 980 990 1000
QLHDTNMELT DLKLQLEKAT QRQERFADRS LLEMEKRERR ALERRISEME
1010 1020 1030
EELKMLPDLK ADNQRLKDEN GALIRVISKL SK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 5 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: October 29, 2014
This is version 126 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