ID PP12C_MOUSE Reviewed; 782 AA.
AC Q3UMT1; Q9CWD5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 24-JAN-2024, entry version 124.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 12C;
DE AltName: Full=Protein phosphatase 1 myosin-binding subunit of 85 kDa;
DE Short=Protein phosphatase 1 myosin-binding subunit p85;
GN Name=Ppp1r12c {ECO:0000312|MGI:MGI:1924258};
GN Synonyms=Mbs85 {ECO:0000303|PubMed:15469989};
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] {ECO:0000312|EMBL:BAE26017.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB27215.1};
RC TISSUE=Embryonic stem cell {ECO:0000312|EMBL:BAB27215.1}, and
RC Lung {ECO:0000312|EMBL:BAE26017.1};
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] {ECO:0000305}
RP INTERACTION WITH MPRIP.
RX PubMed=15469989; DOI=10.1091/mbc.e04-04-0275;
RA Mulder J., Ariaens A., van den Boomen D., Moolenaar W.H.;
RT "p116Rip targets myosin phosphatase to the actin cytoskeleton and is
RT essential for RhoA/ROCK-regulated neuritogenesis.";
RL Mol. Biol. Cell 15:5516-5527(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; THR-560 AND SER-647, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, Pancreas, Spleen, and 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.
CC {ECO:0000250|UniProtKB:Q9BZL4}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC and one or several targeting or regulatory subunits. PPP1R12C mediates
CC binding to myosin. Interacts via its N-terminus with PPP1CB. Interacts
CC with IL16. Interacts with the coiled-coil domain of MPRIP. Interacts
CC with NOD2 (By similarity). {ECO:0000250|UniProtKB:Q9BZL4,
CC ECO:0000269|PubMed:15469989}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BZL4}.
CC Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9BZL4}.
CC -!- PTM: Phosphorylation at Thr-560 is essential for its interaction with
CC PPP1CB. {ECO:0000250}.
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DR EMBL; AK010836; BAB27215.1; -; mRNA.
DR EMBL; AK144691; BAE26017.1; -; mRNA.
DR CCDS; CCDS39735.1; -.
DR RefSeq; NP_084110.2; NM_029834.3.
DR AlphaFoldDB; Q3UMT1; -.
DR SMR; Q3UMT1; -.
DR BioGRID; 231298; 6.
DR IntAct; Q3UMT1; 2.
DR STRING; 10090.ENSMUSP00000013886; -.
DR GlyGen; Q3UMT1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q3UMT1; -.
DR PhosphoSitePlus; Q3UMT1; -.
DR SwissPalm; Q3UMT1; -.
DR EPD; Q3UMT1; -.
DR jPOST; Q3UMT1; -.
DR MaxQB; Q3UMT1; -.
DR PaxDb; 10090-ENSMUSP00000013886; -.
DR PeptideAtlas; Q3UMT1; -.
DR ProteomicsDB; 289371; -.
DR Pumba; Q3UMT1; -.
DR Antibodypedia; 50850; 61 antibodies from 18 providers.
DR DNASU; 232807; -.
DR Ensembl; ENSMUST00000013886.9; ENSMUSP00000013886.9; ENSMUSG00000019254.17.
DR GeneID; 232807; -.
DR KEGG; mmu:232807; -.
DR UCSC; uc009exq.1; mouse.
DR AGR; MGI:1924258; -.
DR CTD; 54776; -.
DR MGI; MGI:1924258; Ppp1r12c.
DR VEuPathDB; HostDB:ENSMUSG00000019254; -.
DR eggNOG; KOG0505; Eukaryota.
DR GeneTree; ENSGT00940000161425; -.
DR InParanoid; Q3UMT1; -.
DR OMA; MTDARTW; -.
DR OrthoDB; 5482573at2759; -.
DR PhylomeDB; Q3UMT1; -.
DR TreeFam; TF105543; -.
DR BioGRID-ORCS; 232807; 1 hit in 115 CRISPR screens.
DR ChiTaRS; Ppp1r12c; mouse.
DR PRO; PR:Q3UMT1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UMT1; Protein.
DR Bgee; ENSMUSG00000019254; Expressed in granulocyte and 229 other cell types or tissues.
DR ExpressionAtlas; Q3UMT1; baseline and differential.
DR Genevisible; Q3UMT1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell.
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 CDD; cd21945; IPD_PPP1R12C; 1.
DR Gene3D; 6.10.140.390; -; 1.
DR Gene3D; 6.10.250.1820; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 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 PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR PANTHER; PTHR24179:SF27; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12C; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW Acetylation; ANK repeat; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL4"
FT CHAIN 2..782
FT /note="Protein phosphatase 1 regulatory subunit 12C"
FT /id="PRO_0000315864"
FT REPEAT 104..133
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 137..166
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 230..259
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 263..292
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..332
FT /evidence="ECO:0000255"
FT COILED 681..782
FT /evidence="ECO:0000255"
FT COMPBIAS 329..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL4"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL4"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL4"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL4"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL4"
FT MOD_RES 560
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 30
FT /note="Q -> R (in Ref. 1; BAB27215)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 782 AA; 84685 MW; 83C2708E36BFBD7B CRC64;
MSGEDGPAAG PGAAAAAAAA RERRQEQLRQ WGARAGADPG PGERRARTVR FERAAEFLAA
CAGGDLDEAR LMLRAADPGP GSGAASDPAV PPPARAVLDS TNADGISALH QACIDENLEV
VRFLVEQGAT VNQADNEGWT PLHVAASCGY LDIARYLLSH GANIAAVNSD GDLPLDLAES
DAMEGLLKAE ITRRGVDVEA AKRAEEELLL HDTRCWLNGG AMPEARHPRT GASALHVAAA
KGYIEVMRLL LQAGYDTELR DGDGWTPLHA AAHWGVEDAC RLLAEHGGGM DSLTHAGQRP
CDLADEDVMN LLEELAQKQE DLRNQKEGSQ GRGQESQVPS SSKHRRSSVC RLSSREKISL
QDLSKERRPG GAGGPPIGDE DEGGEASAEH PAVEPRALNG VSSPVSSNPK SPVLPEEAPF
SRRFGLQKTG STGALGPSER RATEGVLGLQ RSASSSLLEK ASTQAREPRL ARITPTPAQK
VPEPFTLYEA ATPPSLDHSV PPSRREPGSI VKPNVLTASA APLADSRDRR RSYQMPVRDE
ESESQRKARS RLMRQSRRST QGVTLTDLKE AEKVAGKVPE PEQPALPSLD PSRRPRVPGV
ENAEGPAQRE APEGQGQGPQ AAREHRKAGH ERRGPAEGEE AGPAERSPEC STVDGGSQVR
RQHSQRDLVL ESKQEHEEPD GGFRKMYTEL RRENERLREA LTETTLRLAQ LKVELERATQ
RQERFAERPA LLELERFERR ALERKAAELE EELKALSDLR ADNQRLKDEN AALIRVISKL
SK
//
