MYPT2_MOUSE
ID MYPT2_MOUSE Reviewed; 976 AA.
AC Q8BG95; Q8BXY7; Q9D8S6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 12B;
DE AltName: Full=Myosin phosphatase-targeting subunit 2;
DE Short=Myosin phosphatase target subunit 2;
GN Name=Ppp1r12b; Synonyms=Mypt2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-484 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, Cerebellum, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; THR-444; SER-502;
RP THR-802; SER-833 AND SER-941, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulates myosin phosphatase activity. Augments Ca(2+)
CC sensitivity of the contractile apparatus (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC and one or several targeting or regulatory subunits. PPP1R12B mediates
CC binding to myosin. Isoform 3 and isoform 4 bind PPP1R12A, but not
CC isoform 1 of PPP1R12B itself. Binds IL16 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O60237}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:O60237}. Note=Along actomyosin filaments.
CC {ECO:0000250|UniProtKB:O60237}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BG95-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BG95-2; Sequence=VSP_009260, VSP_009261;
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DR EMBL; AK007727; BAB25216.1; -; mRNA.
DR EMBL; AK042847; BAC31381.1; -; mRNA.
DR EMBL; AK046012; BAC32572.1; -; mRNA.
DR EMBL; AK046167; BAC32618.1; -; mRNA.
DR EMBL; AK080855; BAC38046.1; -; mRNA.
DR EMBL; AC117827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS87881.1; -. [Q8BG95-1]
DR RefSeq; XP_006529773.1; XM_006529710.2.
DR AlphaFoldDB; Q8BG95; -.
DR SMR; Q8BG95; -.
DR BioGRID; 236730; 7.
DR IntAct; Q8BG95; 1.
DR STRING; 10090.ENSMUSP00000131406; -.
DR iPTMnet; Q8BG95; -.
DR PhosphoSitePlus; Q8BG95; -.
DR EPD; Q8BG95; -.
DR jPOST; Q8BG95; -.
DR MaxQB; Q8BG95; -.
DR PaxDb; Q8BG95; -.
DR PeptideAtlas; Q8BG95; -.
DR PRIDE; Q8BG95; -.
DR ProteomicsDB; 287538; -. [Q8BG95-1]
DR ProteomicsDB; 287539; -. [Q8BG95-2]
DR Antibodypedia; 20653; 58 antibodies from 16 providers.
DR Ensembl; ENSMUST00000045665; ENSMUSP00000047463; ENSMUSG00000073557. [Q8BG95-1]
DR Ensembl; ENSMUST00000112163; ENSMUSP00000107788; ENSMUSG00000073557. [Q8BG95-2]
DR MGI; MGI:1916417; Ppp1r12b.
DR VEuPathDB; HostDB:ENSMUSG00000073557; -.
DR eggNOG; KOG0505; Eukaryota.
DR GeneTree; ENSGT00940000157067; -.
DR HOGENOM; CLU_000134_54_0_1; -.
DR InParanoid; Q8BG95; -.
DR OrthoDB; 477969at2759; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR BioGRID-ORCS; 329251; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp1r12b; mouse.
DR PRO; PR:Q8BG95; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BG95; protein.
DR Bgee; ENSMUSG00000073557; Expressed in rostral migratory stream and 200 other tissues.
DR ExpressionAtlas; Q8BG95; baseline and differential.
DR Genevisible; Q8BG95; MM.
DR GO; GO:0031672; C:A band; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR GO; GO:0019208; F:phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017401; MYPT1/MYPT2/Mbs85.
DR InterPro; IPR031775; PRKG1_interact.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..976
FT /note="Protein phosphatase 1 regulatory subunit 12B"
FT /id="PRO_0000067029"
FT REPEAT 57..86
FT /note="ANK 1"
FT REPEAT 90..119
FT /note="ANK 2"
FT REPEAT 123..152
FT /note="ANK 3"
FT REPEAT 216..245
FT /note="ANK 4"
FT REPEAT 249..278
FT /note="ANK 5"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 444
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 645
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60237"
FT MOD_RES 802
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 98..105
FT /note="ACIDENLD -> RNHKPRGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009260"
FT VAR_SEQ 106..976
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009261"
SQ SEQUENCE 976 AA; 109049 MW; 7694AC50766A8890 CRC64;
MAELEHLGGK RAESARARRA EQLRRWRGSL TEQEPAERQG AGRQLQTRRG SPRVRFEDGA
VFLAACSSGD TDEVKKLLAR GADINTVNVD GLTALHQACI DENLDMVKFL VENRANVNQQ
DNEGWTPLHA AASCGYLNIA EYFISHGASV GIVNSEGEVP SDLAEEPAMK DLLLEQVKKQ
GVDLEQSRKE EEQQMLQDAR QWLNSGRIED VRQARSGATA LHVAAAKGYS EVLRLLIQAG
YELNVQDHDG WTPLHAAAHW GVKEACSILA EALCDMDIRN KLGQTPFDVA DEGLVEHLEM
LQKKQDVLRS EKETRNKLIE SDLNSKFQSG LFKNKEKMLY EEEIPKSQDT EEENKESSSS
SSEEEEGEDE VSESETEKEA DKKPEATVNH SNSEIKSRIM EQIPAPAQNT FSASSARRLS
SLFNKAEEPK DESPSSWRLG LRKTGSHNML SEVANSREAL RDRGSSIYRS SSSPRISALL
DDKDKERENK SYFSMLVPRR LSSTSDIEEK ENRESAVNLV RSGSHTRQLW RDEAKGSETP
QTIAPSTYTS TYLKRTPYKS QADSTAEKTA DSVSSSTPLC VITNRPAPST ANGVPAATVF
SSAGTDPSVE AREKRRSYLT PVRDEEAESL RKARSRQARQ TRRSTQGVTL TDLQEAEKTF
SRSRAERQAQ EQPGEKLEDP GGLEGSTKKQ EPSAAPTKGA GEGRSLEEEP IYHRLRYPTQ
PDKPTTPVSP SASRPSLYTG SHLLRTSRAS GPDSENSETS THATAAKEMD TSEKGEADLD
DQSSNRLSVR ERRRAKDRRR GTGINFWTND EDETDVSEEV KEALHERLSR LESGGTNPTS
SDSYSDRASA RARREAREAR LASLTSRVEE DSNRDYKKLY ESALTENQKL KTKLQEAQLE
LADIKAKLEK MAQQKQEKTS DRSSVLEVEK RERRALERKM SEMEEEMKVL TELKSDNQRL
KDENGALIRV ISKLSK
