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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)

 MYPT1_RAT               Reviewed;        1032 AA.
Q10728; Q62937; Q9WU33;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
16-JAN-2004, sequence version 2.
02-JUN-2021, entry version 169.
RecName: Full=Protein phosphatase 1 regulatory subunit 12A;
AltName: Full=MBSP;
AltName: Full=Myosin phosphatase-targeting subunit 1;
Short=Myosin phosphatase target subunit 1;
AltName: Full=Protein phosphatase myosin-binding subunit;
AltName: Full=Protein phosphatase subunit 1M;
Short=PP-1M;
AltName: Full=Serine/threonine protein phosphatase PP1 smooth muscle regulatory subunit M110;
Name=Ppp1r12a {ECO:0000312|RGD:620013}; Synonyms=Mbs, Mypt1 {ECO:0000305};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Aorta;
PubMed=7988720; DOI=10.1016/0014-5793(94)01231-8;
Chen Y.H., Chen M.X., Alessi D.R., Campbell D.G., Shanahan C., Cohen P.,
Cohen P.T.W.;
"Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory
subunits of smooth muscle protein phosphatase 1M.";
FEBS Lett. 356:51-55(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-728 (ISOFORM 2), AND FUNCTION.
STRAIN=Wistar; TISSUE=Kidney;
PubMed=8543033; DOI=10.1016/0014-5793(95)01318-0;
Haystead C.M.M., Gailly P., Somlyo A.P., Somlyo A.V., Haystead T.A.J.;
"Molecular cloning and functional expression of a recombinant 72.5 kDa
fragment of the 110 kDa regulatory subunit of smooth muscle protein
phosphatase 1M.";
FEBS Lett. 377:123-127(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 490-665 (ISOFORM 1), TISSUE
SPECIFICITY, AND ALTERNATIVE SPLICING.
STRAIN=Sprague-Dawley;
PubMed=10712248; DOI=10.1152/ajpcell.2000.278.3.c589;
Dirksen W.P., Vladic F., Fisher S.A.;
"A myosin phosphatase targeting subunit isoform transition defines a smooth
muscle developmental phenotypic switch.";
Am. J. Physiol. 278:C589-C600(2000).
[4]
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).
[5]
PHOSPHORYLATION AT THR-697 AND SER-854, AND INTERACTION WITH ROCK1.
PubMed=10579722; DOI=10.1083/jcb.147.5.1023;
Kawano Y., Fukata Y., Oshiro N., Amano M., Nakamura T., Ito M.,
Matsumura F., Inagaki M., Kaibuchi K.;
"Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by
Rho-kinase in vivo.";
J. Cell Biol. 147:1023-1038(1999).
[6]
PHOSPHORYLATION AT THR-697 BY ZIPK/DAPK3.
PubMed=11384979; DOI=10.1074/jbc.m102753200;
Niiro N., Ikebe M.;
"Zipper-interacting protein kinase induces Ca(2+)-free smooth muscle
contraction via myosin light chain phosphorylation.";
J. Biol. Chem. 276:29567-29574(2001).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-997, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[8]
PHOSPHORYLATION, AND INTERACTION WITH ROCK1 AND ROCK2.
PubMed=19131646; DOI=10.1161/circresaha.108.188524;
Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X., Surks H.K.;
"ROCK isoform regulation of myosin phosphatase and contractility in
vascular smooth muscle cells.";
Circ. Res. 104:531-540(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-445; SER-507;
SER-864; SER-873; SER-912 AND SER-997, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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:0000269|PubMed:8543033}.
-!- 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, ECO:0000250|UniProtKB:Q9DBR7}.
-!- INTERACTION:
Q10728; O43293-2: DAPK3; Xeno; NbExp=2; IntAct=EBI-918263, EBI-9691390;
Q10728; Q6WCQ1: MPRIP; Xeno; NbExp=6; IntAct=EBI-918263, EBI-1022605;
Q10728; P35240: NF2; Xeno; NbExp=2; IntAct=EBI-918263, EBI-1014472;
-!- 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=3;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q10728-1; Sequence=Displayed;
Name=2;
IsoId=Q10728-2; Sequence=VSP_009254;
Name=3;
IsoId=Q10728-3; Sequence=VSP_009255;
-!- TISSUE SPECIFICITY: Smooth muscle. Detected in aorta, portal vein,
stomach, intestine, bladder and lung. {ECO:0000269|PubMed:10712248}.
-!- 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 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).
{ECO:0000250|UniProtKB:O14974}.
---------------------------------------------------------------------------
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EMBL; S74907; AAB32731.1; -; mRNA.
EMBL; U50185; AAA92961.1; -; mRNA.
EMBL; AF110176; AAD34326.1; -; Genomic_DNA.
PIR; S68418; S68418.
RefSeq; NP_446342.1; NM_053890.1. [Q10728-3]
RefSeq; XP_006241377.1; XM_006241315.2. [Q10728-2]
BMRB; Q10728; -.
SMR; Q10728; -.
IntAct; Q10728; 5.
MINT; Q10728; -.
STRING; 10116.ENSRNOP00000006773; -.
iPTMnet; Q10728; -.
PhosphoSitePlus; Q10728; -.
jPOST; Q10728; -.
PaxDb; Q10728; -.
PRIDE; Q10728; -.
GeneID; 116670; -.
KEGG; rno:116670; -.
UCSC; RGD:620013; rat. [Q10728-1]
CTD; 4659; -.
RGD; 620013; Ppp1r12a.
eggNOG; KOG0505; Eukaryota.
InParanoid; Q10728; -.
OrthoDB; 477969at2759; -.
PhylomeDB; Q10728; -.
BRENDA; 3.1.3.53; 5301.
Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
Reactome; R-RNO-5627123; RHO GTPases activate PAKs.
PRO; PR:Q10728; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031672; C:A band; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0043292; C:contractile fiber; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
GO; GO:0030018; C:Z disc; ISS: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:0004721; F:phosphoprotein phosphatase activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0035690; P:cellular response to drug; ISO:RGD.
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:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
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; ISO:RGD.
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..1032
/note="Protein phosphatase 1 regulatory subunit 12A"
/id="PRO_0000067027"
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..553
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 588..928
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 683..866
/note="Interaction with ROCK2"
/evidence="ECO:0000269|PubMed:19131646"
MOTIF 35..38
/note="KVKF motif"
COMPBIAS 303..319
/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..418
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 419..436
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 588..614
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 638..660
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 661..687
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 709..765
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 769..815
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 816..844
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 864..888
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 889..907
/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:22673903"
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"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 446
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:O14974"
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:0007744|PubMed:22673903"
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 693
/note="Phosphoserine; by PKA and PKG; in vitro"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 696
/note="Phosphoserine; by PKA and PKG; in vitro"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 697
/note="Phosphothreonine; by ROCK1, ROCK2, CDC42BP,
ZIPK/DAPK3 and RAF1"
/evidence="ECO:0000269|PubMed:10579722,
ECO:0000269|PubMed:11384979"
MOD_RES 804
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9DBR7"
MOD_RES 854
/note="Phosphoserine; by ROCK2"
/evidence="ECO:0000269|PubMed:10579722"
MOD_RES 864
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 873
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 905
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 910
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O14974"
MOD_RES 912
/note="Phosphoserine; by NUAK1"
/evidence="ECO:0000305, ECO:0007744|PubMed:22673903"
MOD_RES 997
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16641100,
ECO:0007744|PubMed:22673903"
VAR_SEQ 552..607
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:7988720"
/id="VSP_009255"
VAR_SEQ 608..667
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:8543033"
/id="VSP_009254"
CONFLICT 11
/note="N -> R (in Ref. 2; AAA92961)"
/evidence="ECO:0000305"
CONFLICT 316
/note="T -> N (in Ref. 2; AAA92961)"
/evidence="ECO:0000305"
CONFLICT 424
/note="K -> E (in Ref. 2; AAA92961)"
/evidence="ECO:0000305"
CONFLICT 579
/note="A -> P (in Ref. 2; AAA92961)"
/evidence="ECO:0000305"
CONFLICT 682
/note="Q -> H (in Ref. 2; AAA92961)"
/evidence="ECO:0000305"
SEQUENCE 1032 AA; 115283 MW; 43B9FC1569CD5DDB CRC64;
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL
HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD
IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERIMLRD
ARQWLNSGHI SDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA
HWGKEEACRI LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQNLL HSEKRDKKSP
LIESTANMEN NQPQKTFKNK ETLIIEPEKN ASRIESLEQE KADEEEEGKK DESSCSSEED
EEDDSESEAE TDKTKPMASV TNAHTASTQA APAAVTTPTL SSNQGTPTSP VKKFPTSTTK
ISPKEEERKD ESPASWRLGL RKTGSYGALA EITASKEAQK EKDTAGVIRS ASSPRLSSSL
DNKEKEKDNK GTRLAYVAPT IPRRLGSTSD IEEKENRESS NLRTSSSYTR RKWEDDLKKN
SSINEGSTYH RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQKSFLSST STTAKTPPGS
SPAGTQSSTS NRLWAEDSTE KEKDSAPTAA TILVAPTVVS AAASSTTALT TTTAGTLSST
SEVRERRRSY LTPVRDEESE SQRKARSRQA RQSRRSTQGV TLTDLQEAEK TIGRSRSTRT
REQENEEKDK EEKEKQDKEK QEEKKESEVS REDEYKQKYS RTYDETYARY RPVSTSSSST
PSSSSLSTLG SSLYASSQLN RPNSLVGITS AYSRGLTKDN EREGEKKEEE KEGEDKSQPK
SIRERRRPRE KRRSTGVSFW TQDSDENEQE RQSDTEDGSS KRDTQTDSVS RYDSSSTSSS
DRYDSLLGRS ASYSYLEERK PYGSRLEKDD STDFKKLYEQ ILAENEKLKA QLHDTNMELT
DLKLQLEKAT QRQERFADRS LLEMEKRERR ALERRISEME EELKMLPDLK ADNQRLKDEN
GALIRVISKL SK


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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
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
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
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
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
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
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 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 :
WP2292: Chemokine signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP1644: DNA replication
WP1654: gamma-Hexachlorocyclohexane degradation
WP1694: Pyrimidine metabolism
WP1693: Purine metabolism
WP1566: Citrate cycle (TCA cycle)
WP1663: Homologous recombination
WP1672: Mismatch repair
WP731: Sterol regulatory element binding protein related
WP1626: Benzoate degradation via CoA ligation
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2353: vitamin B9 (folate) 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
WP76: TCA Cycle
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP1659: Glycine, serine and threonine metabolism
WP1909: Signal regulatory protein (SIRP) family interactions
WP1709: Thiamine metabolism

Related Genes :
[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] 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)
[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)
[Ppp1cc] Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit)
[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)
[PPP1CB] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (PPP1CD) (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)
[PPP1CB] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)
[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)
[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)
[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)
[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)
[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)
[PPP1CB] Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)
[ppp1cc-a ppp1cc] Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A (PP-1G-A) (xPP1-gamma1) (EC 3.1.3.16)
[PPP1CA] Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PP-1A) (EC 3.1.3.16)

Bibliography :
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