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Q90623 (MYPT1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PPP1R12A
Synonyms:MBS, MYPT1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1004 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates myosin phosphatase activity. Ref.1

Subunit structure

PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits By similarity. PPP1R12A mediates binding to myosin. Ref.1

Subcellular location

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

Tissue specificity

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

Post-translational modification

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. Ref.3 Ref.4 Ref.5

Sequence similarities

Contains 6 ANK repeats.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q90623-1)

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.
Isoform 2 (identifier: Q90623-2)

Also known as: M130;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10041004Protein phosphatase 1 regulatory subunit 12A
PRO_0000355556

Regions

Repeat39 – 6830ANK 1
Repeat72 – 10130ANK 2
Repeat105 – 13430ANK 3
Repeat138 – 16427ANK 4
Repeat198 – 22730ANK 5
Repeat231 – 26030ANK 6
Region35 – 384Important for interaction with PPP1CB
Compositional bias343 – 37028Asp/Glu-rich
Compositional bias514 – 660147Ser/Thr-rich
Compositional bias720 – 75132Asp/Glu/Lys-rich
Compositional bias771 – 81141Ser-rich
Compositional bias771 – 79323Ser/Thr-rich

Amino acid modifications

Modified residue6951Phosphothreonine; by ROCK2 Ref.3 Ref.4
Modified residue8501Phosphothreonine; by ROCK2 Ref.3 Ref.4

Natural variations

Alternative sequence512 – 55241Missing in isoform 2.
VSP_035912

Experimental info

Mutagenesis6951T → A: Reduces phosphorylation. Reduces phosphorylation on serine and threonine residues by 80%; when associated with A-850. Ref.4
Mutagenesis8501T → A: Reduces phosphorylation. Reduces phosphorylation on serine and threonine residues by 80%; when associated with A-695. Ref.4

Secondary structure

...................................... 1004
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (M133) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7ED870DB87046929

FASTA1,004111,606
        10         20         30         40         50         60 
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RKKTKVKFDD GAVFLAACSS GDTEEVLRLL 

        70         80         90        100        110        120 
ERGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD 

       130        140        150        160        170        180 
IAEYLISQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD 

       190        200        210        220        230        240 
ARQWLNSGHI NDVRHAKSGG TALHVAAAKG YTEVLKLLIQ ARYDVNIKDY DGWTPLHAAA 

       250        260        270        280        290        300 
HWGKEEACRI LVENLCDMEA VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKREKKSP 

       310        320        330        340        350        360 
LIESTANLDN NQTQKTFKNK ETLIMEQEKN ASSIESLEHE KADEEEEGKK DESSCSSEEE 

       370        380        390        400        410        420 
EDDDSESEAE TDKAKTLANA NTTSTQSASM TAPSVAGGQG TPTSPLKKFP TSTTKVSPKE 

       430        440        450        460        470        480 
EERKDESPAS WRLGLRKTGS YGALAEITAS KEAQKEKDSA GVIRSASSPR LSSSLDNKEK 

       490        500        510        520        530        540 
EKDGKGTRLA YVAPTIPRRL ASTSDIDEKE NRDSSASSIR SGSSYARRKW EEDVKKNSLN 

       550        560        570        580        590        600 
EGPTSLNTSY QRSGSFGRRQ DDLVSSNVPS TASTVTSSAG LQKTLPASAN TTTKSTTGST 

       610        620        630        640        650        660 
SAGVQSSTSN RLWAEDSTEK EKDSVPTAVT VPVAPSVVNA AATTTAMTTA TSGTVSSTSE 

       670        680        690        700        710        720 
VRERRRSYLT PVRDEESESQ RKARSRQARQ SRRSTQGVTL TDLQEAEKTI GRSRSTRTRE 

       730        740        750        760        770        780 
QENEEKEKEE KEKQDKEKQE EKKESETKDD DYRQRYSRTV EEPYHRYRPT STSTSTSSTS 

       790        800        810        820        830        840 
SLSTSTSSLS SSSQLNRPNS LIGITSAYSR SGTKESEREG GKKEEEKEED KSQPKSIRER 

       850        860        870        880        890        900 
RRPREKRRST GVSFWTQDSD ENEQEHQSDS EEGTNKKETQ SDSLSRYDTG SLSVSSGDRY 

       910        920        930        940        950        960 
DSAQGRSGSQ SYLEDRKPYC SRLEKEDSTD FKKLYEQILA ENEKLKAQLH DTNMELTDLK 

       970        980        990       1000 
LQLEKTTQRQ ERFADRSLLE MEKRVSGKSQ YLLGGKKSSR KKDI 

« Hide

Isoform 2 (M130) [UniParc].

Checksum: 819D017491D02DB4
Show »

FASTA963106,975

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D37985 mRNA. Translation: BAA07201.1.
D37986 mRNA. Translation: BAA07202.1.
S74623 mRNA. Translation: AAB32730.1.
PIRA55142.
RefSeqNP_990454.1. NM_205123.1.
UniGeneGga.3159.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S70X-ray2.70B1-299[»]
DisProtDP00218.
ProteinModelPortalQ90623.
SMRQ90623. Positions 1-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676290. 1 interaction.
IntActQ90623. 1 interaction.
STRING9031.ENSGALP00000016789.

Proteomic databases

PaxDbQ90623.
PRIDEQ90623.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396020.
KEGGgga:396020.

Organism-specific databases

CTD4659.

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000290648.
HOVERGENHBG052561.
KOK06270.
PhylomeDBQ90623.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017401. Pase-1_reg_su_12A/B/C_euk.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
[Graphical view]
PIRSFPIRSF038141. PP1_12ABC_vert. 1 hit.
SMARTSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ90623.
NextBio20816082.
PROQ90623.

Entry information

Entry nameMYPT1_CHICK
AccessionPrimary (citable) accession number: Q90623
Secondary accession number(s): Q10727, Q90624
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references