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O14974 (MYPT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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):
Myosin phosphatase-targeting subunit 1
Short name=Myosin phosphatase target subunit 1
Protein phosphatase myosin-binding subunit
Gene names
Name:PPP1R12A
Synonyms:MBS, MYPT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1030 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.24 Ref.34

Subunit structure

PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12A mediates binding to myosin. Interacts with ARHA and CIT By similarity. Binds PPP1R12B, ROCK1 and IL16. Interacts directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with SMTNL1 By similarity. Interacts with PPP1CB; the interaction is direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-910) with 14-3-3. Interacts with ROCK1 and ROCK2. Interacts with isoform 1 and isoform 2 of ZIPK/DAPK3. Interacts with RAF1. Interacts with HIF1AN. Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.21 Ref.23 Ref.25 Ref.31 Ref.34

Subcellular location

Cytoplasm. Note: Along actomyosin filaments and stress fibers. Ref.16 Ref.24

Tissue specificity

Expressed in striated muscles, specifically in type 2a fibers (at protein level). Ref.35

Developmental stage

Induced by 2-fold during pregnancy, including in abdominus rectus muscle. Ref.35

Domain

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. Ref.34

The KVKF motif mediates interaction with PPP1CB. Ref.34

Post-translational modification

Phosphorylated by CIT (Rho-associated kinase) By similarity. Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-696. Phosphorylated on upon DNA damage, probably by ATM or ATR. In vitro, phosphorylation of Ser-695 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-696, probably mediated by PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-910 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2. May be phosphorylated at Thr-696 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. Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.17 Ref.19 Ref.20 Ref.21 Ref.24 Ref.29 Ref.31 Ref.32 Ref.34 Ref.38 Ref.41

Sequence similarities

Contains 6 ANK repeats.

Sequence caution

The sequence AAH47898.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH92481.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainANK repeat
Repeat
   PTMHydroxylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

centrosome organization

Inferred from mutant phenotype Ref.24. Source: UniProtKB

mitosis

Inferred from mutant phenotype Ref.24. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of catalytic activity

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.8. Source: UniProtKB

protein dephosphorylation

Inferred from mutant phenotype Ref.24. Source: UniProtKB

regulation of cell adhesion

Inferred from direct assay Ref.34. Source: UniProtKB

regulation of myosin-light-chain-phosphatase activity

Inferred from direct assay Ref.34. Source: UniProtKB

regulation of nucleocytoplasmic transport

Inferred from electronic annotation. Source: Ensembl

signal transduction

Non-traceable author statement PubMed 8662509. Source: GOC

   Cellular_componentPTW/PP1 phosphatase complex

Inferred from direct assay Ref.34. Source: UniProtKB

actin cytoskeleton

Inferred from direct assay. Source: HPA

centrosome

Inferred from direct assay Ref.24. Source: UniProtKB

contractile fiber

Inferred from direct assay Ref.35. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

kinetochore

Inferred from direct assay Ref.24. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_function14-3-3 protein binding

Inferred from direct assay Ref.34. Source: UniProtKB

enzyme inhibitor activity

Inferred from direct assay Ref.8. Source: UniProtKB

phosphatase regulator activity

Inferred from direct assay Ref.34. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.24. Source: UniProtKB

signal transducer activity

Non-traceable author statement PubMed 8662509. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14974-1)

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: O14974-2)

Also known as: Myosin phosphatase target subunit 1 variant;

The sequence of this isoform differs from the canonical sequence as follows:
     935-969: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O14974-3)

Also known as: Myosin phosphatase target subunit 1 variant 2;

The sequence of this isoform differs from the canonical sequence as follows:
     552-607: Missing.
Isoform 4 (identifier: O14974-4)

The sequence of this isoform differs from the canonical sequence as follows:
     608-666: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: O14974-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10301030Protein phosphatase 1 regulatory subunit 12A
PRO_0000067025

Regions

Repeat39 – 6830ANK 1
Repeat72 – 10130ANK 2
Repeat105 – 13430ANK 3
Repeat138 – 16427ANK 4
Repeat198 – 22730ANK 5
Repeat231 – 26030ANK 6
Region682 – 864183Interaction with ROCK2
Motif35 – 384KVKF motif
Compositional bias519 – 660142Ser/Thr-rich
Compositional bias721 – 75333Glu/Lys-rich
Compositional bias773 – 79523Ser-rich

Amino acid modifications

Modified residue671(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.8
Modified residue1001(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.8
Modified residue2261(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.8
Modified residue2991Phosphoserine Ref.28 Ref.36 Ref.39
Modified residue4221Phosphoserine Ref.28 Ref.36 Ref.39
Modified residue4321Phosphoserine Ref.24
Modified residue4431Phosphothreonine By similarity
Modified residue4451Phosphoserine; by NUAK1 Ref.28 Ref.29 Ref.34
Modified residue4721Phosphoserine; by NUAK1 Ref.34
Modified residue4731Phosphoserine; by CDK1 Ref.24
Modified residue4771Phosphoserine Ref.28
Modified residue5071Phosphoserine Ref.28 Ref.39
Modified residue6011Phosphoserine Ref.24
Modified residue6681Phosphoserine By similarity
Modified residue6921Phosphoserine; by PKA and PKG; in vitro
Modified residue6951Phosphoserine; by PKA and PKG; in vitro
Modified residue6961Phosphothreonine; by ROCK1; ROCK2; CDC42BP; ZIPK/DAPK3 and RAF1 Ref.14 Ref.20 Ref.28 Ref.32 Ref.41
Modified residue8521Phosphoserine; by ROCK2 Ref.12
Modified residue8621Phosphoserine Ref.28
Modified residue8711Phosphoserine Ref.28 Ref.33 Ref.36
Modified residue9101Phosphoserine; by NUAK1 Ref.34
Modified residue9951Phosphoserine By similarity

Natural variations

Alternative sequence1 – 8787Missing in isoform 5.
VSP_045079
Alternative sequence552 – 60756Missing in isoform 3.
VSP_009251
Alternative sequence608 – 66659Missing in isoform 4.
VSP_009252
Alternative sequence935 – 96935Missing in isoform 2.
VSP_009253
Natural variant1161C → W.
Corresponds to variant rs12582646 [ dbSNP | Ensembl ].
VAR_038949
Natural variant3051T → P.
Corresponds to variant rs2596781 [ dbSNP | Ensembl ].
VAR_038950
Natural variant7341K → N.
Corresponds to variant rs12820960 [ dbSNP | Ensembl ].
VAR_038951

Experimental info

Mutagenesis4451S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-472 and A-910.
Mutagenesis4721S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-910.
Mutagenesis4731S → A: Abolishes binding to the POLO box domains of PLK1. Ref.24
Mutagenesis9101S → A: Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-472.
Mutagenesis10071L → A: Loss of binding to PRKG1; when associated with A-1014. Ref.15
Mutagenesis10141L → A: Loss of binding to PRKG1; when associated with A-1007. Ref.15
Mutagenesis10211L → A: Loss of binding to PRKG1; when associated with A-1028. Ref.15
Mutagenesis10281L → A: Loss of binding to PRKG1; when associated with A-1021. Ref.15
Sequence conflict21K → Q in AAI11753. Ref.6
Sequence conflict3221T → A in AAH92481. Ref.6
Sequence conflict3501K → R in BAG63921. Ref.4
Sequence conflict6531A → V in AAH92481. Ref.6
Sequence conflict6901R → G in AAQ88438. Ref.2
Sequence conflict7831S → P in AAQ88438. Ref.2
Sequence conflict9301T → P in AAQ88438. Ref.2
Sequence conflict9591D → G in AAQ88438. Ref.2
Sequence conflict10271K → Q in AAQ88438. Ref.2

Secondary structure

........ 1030
Helix Strand Turn

Details...

Sequences

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

Last modified January 1, 1998. Version 1.
Checksum: EA43E9BFF5DA08FF

FASTA1,030115,281
        10         20         30         40         50         60 
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL 

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

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

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

       250        260        270        280        290        300 
HWGKEEACRI LVDNLCDMEM VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP 

       310        320        330        340        350        360 
LIESTANMDN NQSQKTFKNK ETLIIEPEKN ASRIESLEQE KVDEEEEGKK DESSCSSEED 

       370        380        390        400        410        420 
EEDDSESEAE TDKTKPLASV TNANTSSTQA APVAVTTPTV SSGQATPTSP IKKFPTTATK 

       430        440        450        460        470        480 
ISPKEEERKD ESPATWRLGL RKTGSYGALA EITASKEGQK EKDTAGVTRS ASSPRLSSSL 

       490        500        510        520        530        540 
DNKEKEKDSK GTRLAYVAPT IPRRLASTSD IEEKENRDSS SLRTSSSYTR RKWEDDLKKN 

       550        560        570        580        590        600 
SSVNEGSTYH KSCSFGRRQD DLISSSVPST TSTPTVTSAA GLQKSLLSST STTTKITTGS 

       610        620        630        640        650        660 
SSAGTQSSTS NRLWAEDSTE KEKDSVPTAV TIPVAPTVVN AAASTTTLTT TTAGTVSSTT 

       670        680        690        700        710        720 
EVRERRRSYL TPVRDEESES QRKARSRQAR QSRRSTQGVT LTDLQEAEKT IGRSRSTRTR 

       730        740        750        760        770        780 
EQENEEKEKE EKEKQDKEKQ EEKKESETSR EDEYKQKYSR TYDETYQRYR PVSTSSSTTP 

       790        800        810        820        830        840 
SSSLSTMSSS LYASSQLNRP NSLVGITSAY SRGITKENER EGEKREEEKE GEDKSQPKSI 

       850        860        870        880        890        900 
RERRRPREKR RSTGVSFWTQ DSDENEQEQQ SDTEEGSNKK ETQTDSISRY ETSSTSAGDR 

       910        920        930        940        950        960 
YDSLLGRSGS YSYLEERKPY SSRLEKDDST DFKKLYEQIL AENEKLKAQL HDTNMELTDL 

       970        980        990       1000       1010       1020 
KLQLEKATQR QERFADRSLL EMEKRERRAL ERRISEMEEE LKMLPDLKAD NQRLKDENGA 

      1030 
LIRVISKLSK 

« Hide

Isoform 2 (Myosin phosphatase target subunit 1 variant) [UniParc].

Checksum: 67E4FF32DDCCBD78
Show »

FASTA995111,185
Isoform 3 (Myosin phosphatase target subunit 1 variant 2) [UniParc].

Checksum: D211212480EF48DE
Show »

FASTA974109,728
Isoform 4 [UniParc].

Checksum: 351DE33C5EB3C276
Show »

FASTA971109,104
Isoform 5 [UniParc].

Checksum: 0C4751FF983E49F9
Show »

FASTA943105,641

References

« Hide 'large scale' references
[1]"Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21."
Takahashi N., Ito M., Tanaka J., Nakano T., Kaibuchi K., Odai H., Takemura K.
Genomics 44:150-152(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain and Liver.
[2]Guo J.H., Chen X.Y., Yu L.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Liver.
[3]"Molecular cloning and functional analysis of a new isoform of human MYPT1."
Xia D., Kamm K., Stull J.T.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Testis.
[5]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-722 (ISOFORM 4).
Tissue: Blood and Brain.
[7]"Molecular cloning and analysis of the 5'-flanking region of human MYPT1 gene."
Machida H., Ito M., Okamoto R., Shiraki K., Isaka N., Hartshorne D.J., Nakano T.
Biochim. Biophys. Acta 1517:424-429(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
[8]"MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)."
Webb J.D., Muranyi A., Pugh C.W., Ratcliffe P.J., Coleman M.L.
Biochem. J. 420:327-333(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 63-76; 95-105 AND 217-228, FUNCTION, HYDROXYLATION AT ASN-67; ASN-100 AND ASN-226 BY HIF1AN.
[9]"Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Ialpha."
Surks H.K., Mochizuki N., Kasai Y., Georgescu S.P., Tang K.M., Ito M., Lincoln T.M., Mendelsohn M.E.
Science 286:1583-1587(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKG1, PHOSPHORYLATION BY PRKG1, SUBUNIT.
[10]"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.
[11]"Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit."
Arimura T., Suematsu N., Zhou Y.-B., Nishimura J., Satoh S., Takeshita A., Kanaide H., Kimura A.
J. Biol. Chem. 276:6073-6082(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R12B.
[12]"Rho-kinase--mediated contraction of isolated stress fibers."
Katoh K., Kano Y., Amano M., Onishi H., Kaibuchi K., Fujiwara K.
J. Cell Biol. 153:569-584(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-852.
[13]"Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing."
Sebbagh M., Renvoize C., Hamelin J., Riche N., Bertoglio J., Breard J.
Nat. Cell Biol. 3:346-352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ROCK1, PHOSPHORYLATION.
[14]"Phosphorylation of the myosin-binding subunit of myosin phosphatase by Raf-1 and inhibition of phosphatase activity."
Broustas C.G., Grammatikakis N., Eto M., Dent P., Brautigan D.L., Kasid U.
J. Biol. Chem. 277:3053-3059(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-696 BY RAF1, INTERACTION WITH RAF1.
[15]"Dimerization of cGMP-dependent protein kinase 1alpha and the myosin-binding subunit of myosin phosphatase: role of leucine zipper domains."
Surks H.K., Mendelsohn M.E.
Cell. Signal. 15:937-944(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF LEU-1007; LEU-1014; LEU-1021 AND LEU-1028, INTERACTION WITH PRKG1.
[16]"PDZ domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits."
Bannert N., Vollhardt K., Asomuddinov B., Haag M., Koenig H., Norley S., Kurth R.
J. Biol. Chem. 278:42190-42199(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IL16, SUBCELLULAR LOCATION.
[17]"RhoE binds to ROCK I and inhibits downstream signaling."
Riento K., Guasch R.M., Garg R., Jin B., Ridley A.J.
Mol. Cell. Biol. 23:4219-4229(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ROCK1, PHOSPHORYLATION.
[18]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides."
Wooldridge A.A., MacDonald J.A., Erdodi F., Ma C., Borman M.A., Hartshorne D.J., Haystead T.A.J.
J. Biol. Chem. 279:34496-34504(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PRKG1 ON SER-692; SER-695; THR-696 AND SER-852.
[20]"Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion."
Wilkinson S., Paterson H.F., Marshall C.J.
Nat. Cell Biol. 7:255-261(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-696.
Tissue: Colon.
[21]"Novel ZIP kinase isoform lacks leucine zipper."
Takamoto N., Komatsu S., Komaba S., Niiro N., Ikebe M.
Arch. Biochem. Biophys. 456:194-203(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY ZIPK/DAPK3, INTERACTION WITH ZIPK/DAPK3.
[22]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase."
Lee E., Hayes D.B., Langsetmo K., Sundberg E.J., Tao T.C.
J. Mol. Biol. 373:1198-1212(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKG1.
[24]"Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1."
Yamashiro S., Yamakita Y., Totsukawa G., Goto H., Kaibuchi K., Ito M., Hartshorne D.J., Matsumura F.
Dev. Cell 14:787-797(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-432; SER-473 AND SER-601, PHOSPHORYLATION BY PLK1, MUTAGENESIS OF SER-473.
[25]"Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase."
Sharma A.K., Zhou G.-P., Kupferman J., Surks H.K., Christensen E.N., Chou J.J., Mendelsohn M.E., Rigby A.C.
J. Biol. Chem. 283:32860-32869(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKG1, SUBUNIT.
[26]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[27]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[28]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-422; SER-445; SER-477; SER-507; THR-696; SER-862 AND SER-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]Carrascal M., Abian J.
Submitted (JAN-2008) to UniProtKB
Cited for: PHOSPHORYLATION AT SER-445, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[30]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"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.
[32]"Distinct roles for ROCK1 and ROCK2 in the regulation of keratinocyte differentiation."
Lock F.E., Hotchin N.A.
PLoS ONE 4:E8190-E8190(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-696.
[33]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[34]"New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion."
Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M., Aizawa S., Prescott A.R., Alessi D.R.
Sci. Signal. 3:RA25-RA25(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP1CB AND 14-3-3, DOMAIN KVKF MOTIF, PHOSPHORYLATION AT SER-445; SER-472 AND SER-910.
[35]"Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy."
Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S., Zheng D., Devente J., Hickner R., Haystead T.A.
J. Biol. Chem. 285:29357-29366(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[36]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-422 AND SER-871, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[37]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase."
Tan I., Lai J., Yong J., Li S.F., Leung T.
FEBS Lett. 585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CDC42BP AND DMPK.
[39]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-422 AND SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"Solution structure of the inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1."
Mori S., Iwaoka R., Eto M., Ohki S.-Y.
Proteins 77:732-735(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 658-714, PHOSPHORYLATION AT THR-696.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D87930 mRNA. Translation: BAA22378.1.
AY380574 mRNA. Translation: AAQ88438.1.
AF458589 mRNA. Translation: AAM49717.1.
AK302692 mRNA. Translation: BAG63921.1.
AC018476 Genomic DNA. No translation available.
AC073569 Genomic DNA. No translation available.
AC074270 Genomic DNA. No translation available.
BC047898 mRNA. Translation: AAH47898.1. Sequence problems.
BC092481 mRNA. Translation: AAH92481.1. Sequence problems.
BC111752 mRNA. Translation: AAI11753.1.
AB042196 Genomic DNA. Translation: BAB39107.1.
RefSeqNP_001137357.1. NM_001143885.1.
NP_001137358.1. NM_001143886.1.
NP_001231919.1. NM_001244990.1.
NP_001231921.1. NM_001244992.1.
NP_002471.1. NM_002480.2.
UniGeneHs.49582.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KJYNMR-A658-714[»]
ProteinModelPortalO14974.
SMRO14974. Positions 1-291, 658-714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110742. 50 interactions.
DIPDIP-33186N.
IntActO14974. 27 interactions.
MINTMINT-195983.
STRING9606.ENSP00000261207.

PTM databases

PhosphoSiteO14974.

2D gel databases

OGPO14974.

Proteomic databases

PaxDbO14974.
PRIDEO14974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261207; ENSP00000261207; ENSG00000058272. [O14974-1]
ENST00000437004; ENSP00000416769; ENSG00000058272. [O14974-2]
ENST00000450142; ENSP00000389168; ENSG00000058272. [O14974-1]
ENST00000546369; ENSP00000449514; ENSG00000058272. [O14974-5]
ENST00000550107; ENSP00000446855; ENSG00000058272. [O14974-3]
GeneID4659.
KEGGhsa:4659.
UCSCuc001syz.3. human. [O14974-1]
uc001sza.3. human. [O14974-3]
uc001szb.3. human. [O14974-2]
uc001szc.2. human. [O14974-4]

Organism-specific databases

CTD4659.
GeneCardsGC12M080142.
H-InvDBHIX0010848.
HGNCHGNC:7618. PPP1R12A.
HPAHPA039443.
HPA041296.
MIM602021. gene.
neXtProtNX_O14974.
PharmGKBPA33617.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000290648.
HOVERGENHBG052561.
InParanoidO14974.
KOK06270.
OMATDKQTTT.
OrthoDBEOG7060Q5.
PhylomeDBO14974.
TreeFamTF105543.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressO14974.
BgeeO14974.
CleanExHS_PPP1R12A.
GenevestigatorO14974.

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]
PfamPF00023. Ank. 4 hits.
[Graphical view]
PIRSFPIRSF038141. PP1_12ABC_vert. 1 hit.
PRINTSPR01415. ANKYRIN.
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

ChiTaRSPPP1R12A. human.
EvolutionaryTraceO14974.
GeneWikiPPP1R12A.
GenomeRNAi4659.
NextBio17954.
PROO14974.
SOURCESearch...

Entry information

Entry nameMYPT1_HUMAN
AccessionPrimary (citable) accession number: O14974
Secondary accession number(s): B4DZ09 expand/collapse secondary AC list , F8VWB4, Q2NKL4, Q569H0, Q86WU3, Q8NFR6, Q9BYH0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM