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Protein

Protein phosphatase 1 regulatory subunit 12A

Gene

Ppp1r12a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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 similarity1 Publication

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620013. Ppp1r12a.

Subcellular locationi

  • Cytoplasm By similarity

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000670271 – 1032Protein phosphatase 1 regulatory subunit 12AAdd BLAST1032

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1
Modified residuei100(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1
Modified residuei226(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1
Modified residuei299PhosphoserineCombined sources1
Modified residuei422PhosphoserineBy similarity1
Modified residuei432PhosphoserineBy similarity1
Modified residuei443PhosphothreonineBy similarity1
Modified residuei445PhosphoserineCombined sources1
Modified residuei446PhosphotyrosineBy similarity1
Modified residuei472Phosphoserine; by NUAK1By similarity1
Modified residuei473Phosphoserine; by CDK1By similarity1
Modified residuei477PhosphoserineBy similarity1
Modified residuei507PhosphoserineCombined sources1
Modified residuei509PhosphoserineBy similarity1
Modified residuei601PhosphoserineBy similarity1
Modified residuei618PhosphoserineBy similarity1
Modified residuei693Phosphoserine; by PKA and PKG; in vitroBy similarity1
Modified residuei696Phosphoserine; by PKA and PKG; in vitroBy similarity1
Modified residuei697Phosphothreonine; by ROCK1, ROCK2, CDC42BP, ZIPK/DAPK3 and RAF12 Publications1
Modified residuei804PhosphoserineBy similarity1
Modified residuei854Phosphoserine; by ROCK21 Publication1
Modified residuei864PhosphoserineCombined sources1
Modified residuei873PhosphoserineCombined sources1
Modified residuei905PhosphoserineBy similarity1
Modified residuei910PhosphoserineBy similarity1
Modified residuei912Phosphoserine; by NUAK1Combined sourcesCurated1
Modified residuei997PhosphoserineCombined sources1

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

iPTMnetiQ10728.
PhosphoSitePlusiQ10728.

Expressioni

Tissue specificityi

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

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.

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ10728. 5 interactors.
MINTiMINT-4596910.
STRINGi10116.ENSRNOP00000006773.

Structurei

3D structure databases

ProteinModelPortaliQ10728.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati39 – 68ANK 1Add BLAST30
Repeati72 – 101ANK 2Add BLAST30
Repeati105 – 134ANK 3Add BLAST30
Repeati138 – 164ANK 4Add BLAST27
Repeati198 – 227ANK 5Add BLAST30
Repeati231 – 260ANK 6Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni683 – 866Interaction with ROCK21 PublicationAdd BLAST184

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi35 – 38KVKF motif4

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

eggNOGiKOG0505. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000290648.
HOVERGENiHBG052561.
InParanoidiQ10728.
KOiK06270.
PhylomeDBiQ10728.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. MYPT1/MYPT2_chordates.
IPR031775. PRKG1_interact.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF15898. PRKG1_interact. 1 hit.
[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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti11N → R in AAA92961 (PubMed:8543033).Curated1
Sequence conflicti316T → N in AAA92961 (PubMed:8543033).Curated1
Sequence conflicti424K → E in AAA92961 (PubMed:8543033).Curated1
Sequence conflicti579A → P in AAA92961 (PubMed:8543033).Curated1
Sequence conflicti682Q → H in AAA92961 (PubMed:8543033).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_009255552 – 607Missing in isoform 3. 1 PublicationAdd BLAST56
Alternative sequenceiVSP_009254608 – 667Missing in isoform 2. 1 PublicationAdd BLAST60

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_006241315.2. [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.
PIRiS68418.
RefSeqiNP_446342.1. NM_053890.1. [Q10728-3]
XP_006241377.1. XM_006241315.2. [Q10728-2]
UniGeneiRn.162937.
Rn.220285.

3D structure databases

ProteinModelPortaliQ10728.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ10728. 5 interactors.
MINTiMINT-4596910.
STRINGi10116.ENSRNOP00000006773.

PTM databases

iPTMnetiQ10728.
PhosphoSitePlusiQ10728.

Proteomic databases

PaxDbiQ10728.
PRIDEiQ10728.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4659.
RGDi620013. Ppp1r12a.

Phylogenomic databases

eggNOGiKOG0505. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000290648.
HOVERGENiHBG052561.
InParanoidiQ10728.
KOiK06270.
PhylomeDBiQ10728.

Miscellaneous databases

PROiQ10728.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. MYPT1/MYPT2_chordates.
IPR031775. PRKG1_interact.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF15898. PRKG1_interact. 1 hit.
[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]
ProtoNetiSearch...

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: November 2, 2016
This is version 142 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.