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Protein

Protein phosphatase 1 regulatory subunit 12A

Gene

PPP1R12A

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates myosin phosphatase activity.1 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):
130 kDa myosin-binding subunit of smooth muscle myosin phosphatase
Myosin phosphatase-targeting subunit 1
Short name:
Myosin phosphatase target subunit 1
PP1M subunit M110
Protein phosphatase myosin-binding subunit
Gene namesi
Name:PPP1R12A
Synonyms:MBS, MYPT1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm By similarity

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi695 – 6951T → A: Reduces phosphorylation. Reduces phosphorylation on serine and threonine residues by 80%; when associated with A-850. 1 Publication
Mutagenesisi850 – 8501T → A: Reduces phosphorylation. Reduces phosphorylation on serine and threonine residues by 80%; when associated with A-695. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10041004Protein phosphatase 1 regulatory subunit 12APRO_0000355556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei695 – 6951Phosphothreonine; by ROCK22 Publications
Modified residuei850 – 8501Phosphothreonine; by ROCK22 Publications

Post-translational modificationi

Phosphorylated by CIT (Rho-associated kinase) and by ROCK2 on serine and threonine residues. Phosphorylation at Thr-695 leads to inhibition of myosin phosphatase activity. Phosphorylation at Thr-850 abolishes myosin binding. May be phosphorylated at Thr-695 by DMPK; may inhibit the myosin phosphatase activity.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ90623.
PRIDEiQ90623.

Expressioni

Tissue specificityi

Detected in brain, lung, aorta, heart, gizzard, stomach, oviduct, spleen, kidney and small intestine.1 Publication

Interactioni

Subunit structurei

PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits (By similarity). PPP1R12A mediates binding to myosin.By similarity2 Publications

Protein-protein interaction databases

BioGridi676290. 1 interaction.
IntActiQ90623. 1 interaction.
STRINGi9031.ENSGALP00000016789.

Structurei

Secondary structure

1
1004
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1916Combined sources
Turni20 – 223Combined sources
Helixi40 – 5011Combined sources
Helixi53 – 6210Combined sources
Helixi76 – 827Combined sources
Helixi86 – 949Combined sources
Helixi109 – 1168Combined sources
Helixi119 – 1279Combined sources
Helixi142 – 1454Combined sources
Helixi149 – 16214Combined sources
Helixi166 – 18722Combined sources
Turni196 – 1983Combined sources
Helixi202 – 2098Combined sources
Helixi212 – 2198Combined sources
Turni220 – 2223Combined sources
Helixi235 – 2417Combined sources
Helixi245 – 2539Combined sources
Turni268 – 2703Combined sources
Helixi275 – 2773Combined sources
Helixi278 – 2869Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S70X-ray2.70B1-299[»]
DisProtiDP00218.
ProteinModelPortaliQ90623.
SMRiQ90623. Positions 1-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ90623.

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
Regioni35 – 384Important for interaction with PPP1CB

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi343 – 37028Asp/Glu-richAdd
BLAST
Compositional biasi514 – 660147Ser/Thr-richAdd
BLAST
Compositional biasi720 – 75132Asp/Glu/Lys-richAdd
BLAST
Compositional biasi771 – 81141Ser-richAdd
BLAST
Compositional biasi771 – 79323Ser/Thr-richAdd
BLAST

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000290648.
HOVERGENiHBG052561.
InParanoidiQ90623.
KOiK06270.
PhylomeDBiQ90623.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. MYPT1/MYPT2_chordates.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
[Graphical view]
PIRSFiPIRSF038141. PP1_12ABC_vert. 1 hit.
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. AlignAdd to basket

Isoform 1 (identifier: Q90623-1) [UniParc]FASTAAdd to basket

Also known as: M133

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 RKKTKVKFDD GAVFLAACSS
60 70 80 90 100
GDTEEVLRLL ERGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN
110 120 130 140 150
QPDNEGWIPL HAAASCGYLD IAEYLISQGA HVGAVNSEGD TPLDIAEEEA
160 170 180 190 200
MEELLQNEVN RQGVDIEAAR KEEERIMLRD ARQWLNSGHI NDVRHAKSGG
210 220 230 240 250
TALHVAAAKG YTEVLKLLIQ ARYDVNIKDY DGWTPLHAAA HWGKEEACRI
260 270 280 290 300
LVENLCDMEA VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKREKKSP
310 320 330 340 350
LIESTANLDN NQTQKTFKNK ETLIMEQEKN ASSIESLEHE KADEEEEGKK
360 370 380 390 400
DESSCSSEEE EDDDSESEAE TDKAKTLANA NTTSTQSASM TAPSVAGGQG
410 420 430 440 450
TPTSPLKKFP TSTTKVSPKE EERKDESPAS WRLGLRKTGS YGALAEITAS
460 470 480 490 500
KEAQKEKDSA GVIRSASSPR LSSSLDNKEK EKDGKGTRLA YVAPTIPRRL
510 520 530 540 550
ASTSDIDEKE NRDSSASSIR SGSSYARRKW EEDVKKNSLN EGPTSLNTSY
560 570 580 590 600
QRSGSFGRRQ DDLVSSNVPS TASTVTSSAG LQKTLPASAN TTTKSTTGST
610 620 630 640 650
SAGVQSSTSN RLWAEDSTEK EKDSVPTAVT VPVAPSVVNA AATTTAMTTA
660 670 680 690 700
TSGTVSSTSE VRERRRSYLT PVRDEESESQ RKARSRQARQ SRRSTQGVTL
710 720 730 740 750
TDLQEAEKTI GRSRSTRTRE QENEEKEKEE KEKQDKEKQE EKKESETKDD
760 770 780 790 800
DYRQRYSRTV EEPYHRYRPT STSTSTSSTS SLSTSTSSLS SSSQLNRPNS
810 820 830 840 850
LIGITSAYSR SGTKESEREG GKKEEEKEED KSQPKSIRER RRPREKRRST
860 870 880 890 900
GVSFWTQDSD ENEQEHQSDS EEGTNKKETQ SDSLSRYDTG SLSVSSGDRY
910 920 930 940 950
DSAQGRSGSQ SYLEDRKPYC SRLEKEDSTD FKKLYEQILA ENEKLKAQLH
960 970 980 990 1000
DTNMELTDLK LQLEKTTQRQ ERFADRSLLE MEKRVSGKSQ YLLGGKKSSR

KKDI
Length:1,004
Mass (Da):111,606
Last modified:November 1, 1996 - v1
Checksum:i7ED870DB87046929
GO
Isoform 2 (identifier: Q90623-2) [UniParc]FASTAAdd to basket

Also known as: M130

The sequence of this isoform differs from the canonical sequence as follows:
     512-552: Missing.

Show »
Length:963
Mass (Da):106,975
Checksum:i819D017491D02DB4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei512 – 55241Missing in isoform 2. 1 PublicationVSP_035912Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37985 mRNA. Translation: BAA07201.1.
D37986 mRNA. Translation: BAA07202.1.
S74623 mRNA. Translation: AAB32730.1.
PIRiA55142.
RefSeqiNP_990454.1. NM_205123.1. [Q90623-1]
UniGeneiGga.3159.

Genome annotation databases

GeneIDi396020.
KEGGigga:396020.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37985 mRNA. Translation: BAA07201.1.
D37986 mRNA. Translation: BAA07202.1.
S74623 mRNA. Translation: AAB32730.1.
PIRiA55142.
RefSeqiNP_990454.1. NM_205123.1. [Q90623-1]
UniGeneiGga.3159.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S70X-ray2.70B1-299[»]
DisProtiDP00218.
ProteinModelPortaliQ90623.
SMRiQ90623. Positions 1-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676290. 1 interaction.
IntActiQ90623. 1 interaction.
STRINGi9031.ENSGALP00000016789.

Proteomic databases

PaxDbiQ90623.
PRIDEiQ90623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396020.
KEGGigga:396020.

Organism-specific databases

CTDi4659.

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000290648.
HOVERGENiHBG052561.
InParanoidiQ90623.
KOiK06270.
PhylomeDBiQ90623.

Miscellaneous databases

EvolutionaryTraceiQ90623.
NextBioi20816082.
PROiQ90623.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. MYPT1/MYPT2_chordates.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
[Graphical view]
PIRSFiPIRSF038141. PP1_12ABC_vert. 1 hit.
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase."
    Shimizu H., Ito M., Miyahara M., Ichikawa K., Okubo S., Konishi T., Naka M., Tanaka T., Hirano K., Hartshorne D.J., Nakano T.
    J. Biol. Chem. 269:30407-30411(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, INTERACTION WITH MYOSIN, TISSUE SPECIFICITY.
    Tissue: Gizzard.
  2. "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] OF 681-1004, PARTIAL PROTEIN SEQUENCE.
    Tissue: Gizzard.
  3. "Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin."
    Velasco G., Armstrong C., Morrice N., Frame S., Cohen P.
    FEBS Lett. 527:101-104(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-695 AND THR-850.
  4. "Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase."
    Feng J., Ito M., Ichikawa K., Isaka N., Nishikawa M., Hartshorne D.J., Nakano T.
    J. Biol. Chem. 274:37385-37390(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-695 AND THR-850, MUTAGENESIS OF THR-695 AND THR-850.
  5. "Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity."
    Muranyi A., Zhang R., Liu F., Hirano K., Ito M., Epstein H.F., Hartshorne D.J.
    FEBS Lett. 493:80-84(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY DMPK.
  6. "Structural basis of protein phosphatase 1 regulation."
    Terrak M., Kerff F., Langsetmo K., Tao T., Dominguez R.
    Nature 429:780-784(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-299 IN COMPLEX WITH PPP1CB.

Entry informationi

Entry nameiMYPT1_CHICK
AccessioniPrimary (citable) accession number: Q90623
Secondary accession number(s): Q10727, Q90624
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.