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Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1)

 MYPT1_MOUSE             Reviewed;        1029 AA.
Q9DBR7; Q05A74; Q8CBV2; Q99NB6;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
15-DEC-2009, sequence version 2.
02-JUN-2021, entry version 170.
RecName: Full=Protein phosphatase 1 regulatory subunit 12A;
AltName: Full=Myosin phosphatase-targeting subunit 1;
Short=Myosin phosphatase target subunit 1;
Name=Ppp1r12a {ECO:0000312|MGI:MGI:1309528};
Synonyms=Mypt1 {ECO:0000312|MGI:MGI:1309528};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Lung, and Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
PubMed=11342221; DOI=10.1016/s0167-4781(00)00285-2;
Machida H., Ito M., Okamoto R., Shiraki K., Isaka N., Hartshorne D.J.,
Nakano T.;
"Molecular cloning and analysis of the 5'-flanking region of human MYPT1
gene.";
Biochim. Biophys. Acta 1517:424-429(2001).
[5]
PHOSPHORYLATION, AND INTERACTION WITH ARHA AND CIT.
PubMed=8662509; DOI=10.1126/science.273.5272.245;
Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M.,
Yamamori B., Feng J., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.;
"Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-
kinase).";
Science 273:245-248(1996).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-445; TYR-446;
SER-801; SER-861; SER-870 AND SER-994, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[8]
INTERACTION WITH SMTNL1, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=20634291; DOI=10.1074/jbc.m110.143966;
Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S.,
Zheng D., Devente J., Hickner R., Haystead T.A.;
"Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1
expression during sexual development and pregnancy.";
J. Biol. Chem. 285:29357-29366(2010).
[9]
DEVELOPMENTAL STAGE.
PubMed=31883643; DOI=10.1016/j.ajhg.2019.12.004;
Hughes J.J., Alkhunaizi E., Kruszka P., Pyle L.C., Grange D.K.,
Berger S.I., Payne K.K., Masser-Frye D., Hu T., Christie M.R., Clegg N.J.,
Everson J.L., Martinez A.F., Walsh L.E., Bedoukian E., Jones M.C.,
Harris C.J., Riedhammer K.M., Choukair D., Fechner P.Y., Rutter M.M.,
Hufnagel S.B., Roifman M., Kletter G.B., Delot E., Vilain E.,
Lipinski R.J., Vezina C.M., Muenke M., Chitayat D.;
"Loss-of-function variants in PPP1R12A: from isolated sex reversal to
holoprosencephaly spectrum and urogenital malformations.";
Am. J. Hum. Genet. 106:121-128(2020).
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:O14974, ECO:0000250|UniProtKB:Q10728}.
-!- SUBUNIT: 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
(By similarity). Interacts with NCKAP1L (By similarity).
{ECO:0000250|UniProtKB:O14974}.
-!- INTERACTION:
Q9DBR7; P0C605-1: Prkg1; NbExp=2; IntAct=EBI-1014335, EBI-15699851;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14974}.
Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O14974}.
Note=Also along actomyosin filaments. {ECO:0000250|UniProtKB:O14974}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9DBR7-1; Sequence=Displayed;
Name=2;
IsoId=Q9DBR7-2; Sequence=VSP_038478;
-!- TISSUE SPECIFICITY: Expressed in striated and vascular smooth muscle,
specificcally in type 2a fibers (at protein level). Expression levels
are 20-30% higher in developed males than females (at protein level).
{ECO:0000269|PubMed:20634291}.
-!- DEVELOPMENTAL STAGE: In neonates, expressed at low levels in striated
and smooth muscles. As the animals mature sexually, expression
increases 10-20-fold. Pregnancy promotes a 2-3-fold increase in
expression in striated, vascular and uterine muscle (at protein level).
Expressed in the prosencephalic neural folds at 8.5 dpc. Expressed in
the lower urinary tract, specifically in epitheliumof the bladder,
urethra, and genital tubercle at 13.5 dpc (PubMed:31883643).
{ECO:0000269|PubMed:20634291, ECO:0000269|PubMed:31883643}.
-!- 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. {ECO:0000250}.
-!- DOMAIN: The KVKF motif mediates interaction with PPP1CB.
{ECO:0000250|UniProtKB:O14974}.
-!- PTM: Phosphorylated by CIT (Rho-associated kinase) (By similarity).
Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-694 (By
similarity). Phosphorylated on upon DNA damage, probably by ATM or ATR.
In vitro, phosphorylation of Ser-693 by PKA and PKG appears to prevent
phosphorylation of the inhibitory site Thr-694, probably mediated by
PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-909 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-694 by DMPK; may inhibit the myosin phosphatase
activity (By similarity). 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).
{ECO:0000250|UniProtKB:O14974}.
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EMBL; AK035230; BAC28990.1; -; mRNA.
EMBL; AK004785; BAB23563.1; -; mRNA.
EMBL; CH466539; EDL21703.1; -; Genomic_DNA.
EMBL; BC125381; AAI25382.1; -; mRNA.
EMBL; BC137630; AAI37631.1; -; mRNA.
EMBL; AB042280; BAB39108.1; -; Genomic_DNA.
CCDS; CCDS36052.1; -. [Q9DBR7-2]
CCDS; CCDS88083.1; -. [Q9DBR7-1]
RefSeq; NP_082168.1; NM_027892.2. [Q9DBR7-2]
RefSeq; XP_006513389.1; XM_006513326.3.
BMRB; Q9DBR7; -.
SMR; Q9DBR7; -.
BioGRID; 201677; 27.
DIP; DIP-29982N; -.
IntAct; Q9DBR7; 8.
MINT; Q9DBR7; -.
STRING; 10090.ENSMUSP00000069257; -.
iPTMnet; Q9DBR7; -.
PhosphoSitePlus; Q9DBR7; -.
EPD; Q9DBR7; -.
jPOST; Q9DBR7; -.
PaxDb; Q9DBR7; -.
PeptideAtlas; Q9DBR7; -.
PRIDE; Q9DBR7; -.
ProteomicsDB; 287660; -. [Q9DBR7-1]
ProteomicsDB; 287661; -. [Q9DBR7-2]
Antibodypedia; 29770; 612 antibodies.
Ensembl; ENSMUST00000070663; ENSMUSP00000069257; ENSMUSG00000019907. [Q9DBR7-2]
Ensembl; ENSMUST00000219263; ENSMUSP00000151842; ENSMUSG00000019907. [Q9DBR7-1]
GeneID; 17931; -.
KEGG; mmu:17931; -.
UCSC; uc007gzc.1; mouse. [Q9DBR7-2]
UCSC; uc007gzd.1; mouse. [Q9DBR7-1]
CTD; 4659; -.
MGI; MGI:1309528; Ppp1r12a.
eggNOG; KOG0505; Eukaryota.
GeneTree; ENSGT00940000156120; -.
HOGENOM; CLU_000134_54_0_1; -.
InParanoid; Q9DBR7; -.
OMA; ETQVNNI; -.
OrthoDB; 477969at2759; -.
PhylomeDB; Q9DBR7; -.
TreeFam; TF105543; -.
BRENDA; 3.1.3.53; 3474.
Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
BioGRID-ORCS; 17931; 21 hits in 50 CRISPR screens.
ChiTaRS; Ppp1r12a; mouse.
PRO; PR:Q9DBR7; -.
Proteomes; UP000000589; Chromosome 10.
RNAct; Q9DBR7; protein.
Bgee; ENSMUSG00000019907; Expressed in urinary bladder and 265 other tissues.
Genevisible; Q9DBR7; MM.
GO; GO:0031672; C:A band; IDA:UniProtKB.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0043292; C:contractile fiber; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
GO; GO:0030018; C:Z disc; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
GO; GO:0019208; F:phosphatase regulator activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0035690; P:cellular response to drug; IDA:MGI.
GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0035508; P:positive regulation of myosin-light-chain-phosphatase activity; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0035507; P:regulation of myosin-light-chain-phosphatase activity; ISS:UniProtKB.
GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:MGI.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR017401; MYPT1/MYPT2/Mbs85.
InterPro; IPR031775; PRKG1_interact.
Pfam; PF12796; Ank_2; 2.
Pfam; PF15898; PRKG1_interact; 1.
PIRSF; PIRSF038141; PP1_12ABC_vert; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 6.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 4.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Cytoplasm; Cytoskeleton; Hydroxylation;
Phosphoprotein; Reference proteome; Repeat.
CHAIN 1..1029
/note="Protein phosphatase 1 regulatory subunit 12A"
/id="PRO_0000067026"
REPEAT 39..68
/note="ANK 1"
REPEAT 72..101
/note="ANK 2"
REPEAT 105..134
/note="ANK 3"
REPEAT 138..164
/note="ANK 4"
REPEAT 198..227
/note="ANK 5"
REPEAT 231..260
/note="ANK 6"
REGION 290..786
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 680..863
/note="Interaction with ROCK2"
/evidence="ECO:0000250"
REGION 808..927
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 35..38
/note="KVKF motif"
COMPBIAS 303..318
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 321..355
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 374..416
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 419..436
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 563..614
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 640..657
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 658..684
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 706..762
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 764..786
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 813..841
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 861..885
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 886..904
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 67
/note="(3S)-3-hydroxyasparagine; by HIF1AN"
/evidence="ECO:0000250"
MOD_RES 100
/note="(3S)-3-hydroxyasparagine; by HIF1AN"
/evidence="ECO:0000250"
MOD_RES 226
/note="(3S)-3-hydroxyasparagine; by HIF1AN"
/evidence="ECO:0000250"
MOD_RES 299
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 422
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 432
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 443
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 445
/note="Phosphoserine; by NUAK1"
/evidence="ECO:0007744|PubMed:17242355,
ECO:0007744|PubMed:21183079"
MOD_RES 446
/note="Phosphotyrosine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 472
/note="Phosphoserine; by NUAK1"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 473
/note="Phosphoserine; by CDK1"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 477
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 507
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 509
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 601
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 618
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 690
/note="Phosphoserine; by PKA and PKG; in vitro"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 693
/note="Phosphoserine; by PKA and PKG; in vitro"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 694
/note="Phosphothreonine; by ROCK1, ROCK2, CDC42BP,
ZIPK/DAPK3 and RAF1"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 801
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 851
/note="Phosphoserine; by ROCK2"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 861
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 870
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 902
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 907
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 909
/note="Phosphoserine; by NUAK1"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 994
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
VAR_SEQ 985..1029
/note="ERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK -> VAG
KSQYLLGGTKSSRKKNI (in isoform 2)"
/evidence="ECO:0000303|PubMed:16141072"
/id="VSP_038478"
SEQUENCE 1029 AA; 114996 MW; C466573AC1DFC81F CRC64;
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL
HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD
IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERVMLRD
ARQWLNSGHI SDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA
HWGKEEACRI LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQTLL HSEKRDKKSP
LIESTANMEN NQPQKAFKNK ETLIIEPEKN ASRIESLEHE KADEEEEGKK DESSCSSEED
EEDDSESEAE TDKTKPMASV SNAHTSSTQA APAAVTAPTL SSNQGTPTSP VKKFPISTTK
ISPKEEERKD ESPASWRLGL RKTGSYGALA EISASKEAQK EKDTAGVMRS ASSPRLSSSL
DNKEKEKDNK GTRLAYVTPT IPRRLASTSD IEEKENRESS SLRTSSSYTR RKWEDDLKKN
SSINEGSTYH RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQRSLPSST STAAKTPPGS
SSAGTQSSTS NRLWAEDSTE KEKDSAPTAV TIPVAPTVVN AAAPSTTTLT TTTAGTVSEV
RERRRSYLTP VRDEESESQR KARSRQARQS RRSTQGVTLT DLQEAEKTIG RSRSTRTREQ
ENEEKEKEEK EKQDKEKQEE KKESEASRED EYKQKYSRTY DETYTRYRPV STSSSSAPSS
SSLSTLGSTL YASSQLNRPN SLVGITSAYS RGLAKENERE GEKKEEEKEG EDKSQPKSIR
ERRRPREKRR STGVSFWTQD SDENEQERQS DTEDGSSKRE TQTDSVSRYD SSSTSSSDRY
DSLLGRSASY SYLEDRKPYS SRLEKDDSTD FKKLYEQILA ENEKLKAQLH DTNMELTDLK
LQLEKATQRQ ERFADRSQLE MEKRERRALE RRISEMEEEL KMLPDLKADN QRLKDENGAL
IRVISKLSK


Related products :

Catalog number Product name Quantity
EIAAB26151 Homo sapiens,Human,MBS,Myosin phosphatase target subunit 1,Myosin phosphatase-targeting subunit 1,MYPT1,PPP1R12A,Protein phosphatase 1 regulatory subunit 12A,Protein phosphatase myosin-binding subunit
EIAAB26152 Mbs,MBSP,Myosin phosphatase target subunit 1,Myosin phosphatase-targeting subunit 1,Mypt1,PP-1M,Ppp1r12a,Protein phosphatase 1 regulatory subunit 12A,Protein phosphatase myosin-binding subunit,Protein
EIAAB26156 Homo sapiens,Human,Myosin phosphatase target subunit 2,Myosin phosphatase-targeting subunit 2,MYPT2,PPP1R12B,Protein phosphatase 1 regulatory subunit 12B
EIAAB26154 Mouse,Mus musculus,Myosin phosphatase target subunit 1,Myosin phosphatase-targeting subunit 1,Mypt1,Ppp1r12a,Protein phosphatase 1 regulatory subunit 12A
EIAAB26155 Mouse,Mus musculus,Myosin phosphatase target subunit 2,Myosin phosphatase-targeting subunit 2,Mypt2,Ppp1r12b,Protein phosphatase 1 regulatory subunit 12B
EIAAB26153 130 kDa myosin-binding subunit of smooth muscle myosin phophatase,Chicken,Gallus gallus,MBS,Myosin phosphatase target subunit 1,Myosin phosphatase-targeting subunit 1,MYPT1,PP1M subunit M110,PPP1R12A,
EIAAB31868 Mouse,Mus musculus,Myosin phosphatase targeting subunit 3,Mypt3,Ppp1r16a,Protein phosphatase 1 regulatory subunit 16A
EIAAB31869 Homo sapiens,Human,Myosin phosphatase-targeting subunit 3,MYPT3,PPP1R16A,Protein phosphatase 1 regulatory subunit 16A
EIAAB31850 Homo sapiens,Human,LENG3,MBS85,PPP1R12C,Protein phosphatase 1 myosin-binding subunit of 85 kDa,Protein phosphatase 1 myosin-binding subunit p85,Protein phosphatase 1 regulatory subunit 12C
EIAAB31851 Mbs85,Mouse,Mus musculus,Ppp1r12c,Protein phosphatase 1 myosin-binding subunit of 85 kDa,Protein phosphatase 1 myosin-binding subunit p85,Protein phosphatase 1 regulatory subunit 12C
EIAAB32117 Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL,Homo sapiens,Human,PP1 subunit R4,PPP1R3B,PPP1R4,Protein phosphatase 1 regulatory subunit 3B,Protein phosphatase 1 regulatory sub
EIAAB32116 Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL,Mouse,Mus musculus,PP1 subunit R4,Ppp1r3b,Ppp1r4,Protein phosphatase 1 regulatory subunit 3B,Protein phosphatase 1 regulatory sub
EIAAB32113 Homo sapiens,Human,PP1G,PPP1R3A,Protein phosphatase 1 glycogen-associated regulatory subunit,Protein phosphatase 1 regulatory subunit 3A,Protein phosphatase type-1 glycogen targeting subunit,RG1
EIAAB32112 Oryctolagus cuniculus,PP1G,PPP1R3A,Protein phosphatase 1 glycogen-associated regulatory subunit,Protein phosphatase 1 regulatory subunit 3A,Protein phosphatase type-1 glycogen targeting subunit,Rabbit
EIAAB32111 Mouse,Mus musculus,Pp1g,Ppp1r3a,Protein phosphatase 1 glycogen-associated regulatory subunit,Protein phosphatase 1 regulatory subunit 3A,Protein phosphatase type-1 glycogen targeting subunit,RG1
EIAAB32120 Homo sapiens,Human,PP1 subunit R5,PPP1R3C,PPP1R5,Protein phosphatase 1 regulatory subunit 3C,Protein phosphatase 1 regulatory subunit 5,Protein targeting to glycogen,PTG
EIAAB32121 Mouse,Mus musculus,PP1 subunit R5,Ppp1r3c,Ppp1r5,Protein phosphatase 1 regulatory subunit 3C,Protein phosphatase 1 regulatory subunit 5,Protein targeting to glycogen,PTG
EIAAB32119 Bos taurus,Bovine,PP1 subunit R5,PPP1R3C,PPP1R5,Protein phosphatase 1 regulatory subunit 3C,Protein phosphatase 1 regulatory subunit 5,Protein targeting to glycogen,PTG
EIAAB32118 PP1 subunit R5,Ppp1r3c,Ppp1r5,Protein phosphatase 1 regulatory subunit 3C,Protein phosphatase 1 regulatory subunit 5,Protein targeting to glycogen,PTG,Rat,Rattus norvegicus
EIAAB32114 33 kDa glycogen-binding protein,Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL,PP1 subunit R4,Ppp1r3b,Ppp1r4,Protein phosphatase 1 regulatory subunit 3B,Protein phosphatase 1 r
EIAAB32122 Homo sapiens,Human,PP1 subunit R6,PPP1R3D,PPP1R6,Protein phosphatase 1 regulatory subunit 3D,Protein phosphatase 1 regulatory subunit 6,Protein phosphatase 1-binding subunit R6
EIAAB29458 Homo sapiens,Human,PP2A subunit B isoform PR48,PPP2R3B,PPP2R3L,Protein phosphatase 2A 48 kDa regulatory subunit,Serine_threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
E1323h ELISA Calcineurin subunit B type 1,CNA2,CNB,Homo sapiens,Human,PPP3R1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
U1323h CLIA Calcineurin subunit B type 1,CNA2,CNB,Homo sapiens,Human,PPP3R1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
E1323h ELISA kit Calcineurin subunit B type 1,CNA2,CNB,Homo sapiens,Human,PPP3R1,Protein phosphatase 2B regulatory subunit 1,Protein phosphatase 3 regulatory subunit B alpha isoform 1 96T
Pathways :
WP1644: DNA replication
WP1654: gamma-Hexachlorocyclohexane degradation
WP1694: Pyrimidine metabolism
WP2292: Chemokine signaling pathway
WP1693: Purine metabolism
WP1663: Homologous recombination
WP1566: Citrate cycle (TCA cycle)
WP1672: Mismatch repair
WP2272: Pathogenic Escherichia coli infection
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP1655: Geraniol degradation
WP1696: Riboflavin metabolism
WP1671: Methane metabolism
WP1614: 1- and 2-Methylnaphthalene degradation
WP1711: Trinitrotoluene degradation
WP1718: Vitamin B6 metabolism
WP1680: Oxidative phosphorylation
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1709: Thiamine metabolism
WP76: TCA Cycle
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1634: Butanoate metabolism
WP1652: Fructose and mannose metabolism
WP2353: vitamin B9 (folate) biosynthesis pathway
WP1626: Benzoate degradation via CoA ligation

Related Genes :
[PPP1R12A MBS MYPT1] Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit)
[Ppp1r12a Mbs Mypt1] Protein phosphatase 1 regulatory subunit 12A (MBSP) (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit) (Protein phosphatase subunit 1M) (PP-1M) (Serine/threonine protein phosphatase PP1 smooth muscle regulatory subunit M110)
[PPP1R12A MBS MYPT1] Protein phosphatase 1 regulatory subunit 12A (130 kDa myosin-binding subunit of smooth muscle myosin phosphatase) (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (PP1M subunit M110) (Protein phosphatase myosin-binding subunit)
[ppp1r12a mbs mypt1 si:dkey-28j4.1 zgc:110448] Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1) (Protein phosphatase myosin-binding subunit)
[Ppp1r12a Mypt1] Protein phosphatase 1 regulatory subunit 12A (Myosin phosphatase-targeting subunit 1) (Myosin phosphatase target subunit 1)
[PPP1R12B MYPT2] Protein phosphatase 1 regulatory subunit 12B (Myosin phosphatase-targeting subunit 2) (Myosin phosphatase target subunit 2)
[PPP1R12C LENG3 MBS85] Protein phosphatase 1 regulatory subunit 12C (Protein phosphatase 1 myosin-binding subunit of 85 kDa) (Protein phosphatase 1 myosin-binding subunit p85)
[Ppp1cc] Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit)
[Ppp1r3c Ppp1r5] Protein phosphatase 1 regulatory subunit 3C (Protein phosphatase 1 regulatory subunit 5) (PP1 subunit R5) (Protein targeting to glycogen) (PTG)
[Ppp1r12b Mypt2] Protein phosphatase 1 regulatory subunit 12B (Myosin phosphatase-targeting subunit 2) (Myosin phosphatase target subunit 2)
[PPP1CC] Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit)
[Ppp1cc] Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit)
[PPP1CC] Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit)
[PPP1CB] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (PPP1CD) (EC 3.1.3.16) (EC 3.1.3.53)
[Ppp1r10 Cat53 Pnuts] Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53) (Phosphatase 1 nuclear targeting subunit) (Protein PNUTS)
[PPP1R10 CAT53 FB19 PNUTS] Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53) (PP1-binding protein of 114 kDa) (Phosphatase 1 nuclear targeting subunit) (Protein FB19) (p99)
[PPP1CB] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)
[Ppp1cb] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)
[PPP1CB] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)
[Ppp1cb] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)
[PPP1CB] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)
[PPP1CB] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)
[PPP1CB] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)
[PPP1CA PPP1A] Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)
[Ppp1ca Ppp1a] Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)
[PPP1CC] Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit)
[PPP1CA PPP1A] Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)
[Ppp1ca Ppp1a] Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)
[PPP1CA] Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

Bibliography :