ID PP12C_HUMAN Reviewed; 782 AA. AC Q9BZL4; B4DME2; Q59FK8; Q6ZPD1; Q7L8F7; Q96HW1; Q9H5H5; Q9NT00; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 168. 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|HGNC:HGNC:14947}; GN Synonyms=LENG3, MBS85 {ECO:0000303|PubMed:12923170}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG60045.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH PPP1CB, RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT THR-560. RX PubMed=11399775; DOI=10.1074/jbc.m102615200; RA Tan I., Ng C.H., Lim L., Leung T.; RT "Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 RT reveals a conserved mechanism in the regulation of actin cytoskeleton."; RL J. Biol. Chem. 276:21209-21216(2001). RN [2] {ECO:0000305, ECO:0000312|EMBL:BAB15651.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 103-782 (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [LARGE RP SCALE MRNA] OF 487-782 (ISOFORM 2). RC TISSUE=Brain, Kidney epithelium {ECO:0000312|EMBL:BAB15651.1}, and RC Pericardium {ECO:0000312|EMBL:BAC85179.1}; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] {ECO:0000305, ECO:0000312|EMBL:BAD92689.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-782 (ISOFORM 3). RC TISSUE=Brain {ECO:0000312|EMBL:BAD92689.1}; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 107-191 (ISOFORM 1). RC TISSUE=Thymus; RX PubMed=10941842; DOI=10.1007/s002510000187; RA Wende H., Volz A., Ziegler A.; RT "Extensive gene duplications and a large inversion characterize the human RT leukocyte receptor cluster."; RL Immunogenetics 51:703-713(2000). RN [6] RP ERRATUM OF PUBMED:10941842. RA Wende H., Volz A., Ziegler A.; RL Immunogenetics 52:3-4(2001). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 304-782 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 420-782 (ISOFORM 4). RC TISSUE=Endometrial adenocarcinoma {ECO:0000312|EMBL:AAH08030.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP INTERACTION WITH IL16, AND SUBCELLULAR LOCATION. RX PubMed=12923170; DOI=10.1074/jbc.m306669200; RA Bannert N., Vollhardt K., Asomuddinov B., Haag M., Koenig H., Norley S., RA Kurth R.; RT "PDZ domain-mediated interaction of interleukin-16 precursor proteins with RT myosin phosphatase targeting subunits."; RL J. Biol. Chem. 278:42190-42199(2003). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399; SER-407; SER-427; RP SER-452; SER-509; THR-560 AND SER-604, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427 AND SER-509, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP INTERACTION WITH NOD2. RX PubMed=27812135; DOI=10.1371/journal.pone.0165420; RA Thiebaut R., Esmiol S., Lecine P., Mahfouz B., Hermant A., Nicoletti C., RA Parnis S., Perroy J., Borg J.P., Pascoe L., Hugot J.P., Ollendorff V.; RT "Characterization and Genetic Analyses of New Genes Coding for NOD2 RT Interacting Proteins."; RL PLoS ONE 11:E0165420-E0165420(2016). CC -!- FUNCTION: Regulates myosin phosphatase activity. CC {ECO:0000269|PubMed:11399775}. 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 (PubMed:27812135). {ECO:0000269|PubMed:11399775, CC ECO:0000269|PubMed:12923170, ECO:0000269|PubMed:27812135}. CC -!- INTERACTION: CC Q9BZL4; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-721802, EBI-8643161; CC Q9BZL4; Q9UI12: ATP6V1H; NbExp=3; IntAct=EBI-721802, EBI-724719; CC Q9BZL4; Q7RTU4: BHLHA9; NbExp=3; IntAct=EBI-721802, EBI-17508719; CC Q9BZL4; Q8N715: CCDC185; NbExp=3; IntAct=EBI-721802, EBI-740814; CC Q9BZL4; Q08426: EHHADH; NbExp=3; IntAct=EBI-721802, EBI-2339219; CC Q9BZL4; O60645: EXOC3; NbExp=3; IntAct=EBI-721802, EBI-1052278; CC Q9BZL4; Q9NV31: IMP3; NbExp=3; IntAct=EBI-721802, EBI-747481; CC Q9BZL4; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-721802, EBI-398874; CC Q9BZL4; Q96I25: RBM17; NbExp=3; IntAct=EBI-721802, EBI-740272; CC Q9BZL4; P84022: SMAD3; NbExp=2; IntAct=EBI-721802, EBI-347161; CC Q9BZL4; Q69YQ0: SPECC1L; NbExp=3; IntAct=EBI-721802, EBI-351113; CC Q9BZL4; Q96FV9: THOC1; NbExp=3; IntAct=EBI-721802, EBI-1765605; CC Q9BZL4; Q9H2K2: TNKS2; NbExp=2; IntAct=EBI-721802, EBI-4398527; CC Q9BZL4; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-721802, EBI-739895; CC Q9BZL4-5; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-10289057, EBI-8643161; CC Q9BZL4-5; Q96I25: RBM17; NbExp=3; IntAct=EBI-10289057, EBI-740272; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11399775, CC ECO:0000269|PubMed:12923170}. Cytoplasm, cytoskeleton, stress fiber CC {ECO:0000269|PubMed:11399775, ECO:0000269|PubMed:12923170}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1 {ECO:0000269|PubMed:11399775, ECO:0000269|PubMed:14702039, CC ECO:0000269|PubMed:15489334}; CC IsoId=Q9BZL4-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:14702039}; CC IsoId=Q9BZL4-2; Sequence=VSP_052643; CC Name=3; CC IsoId=Q9BZL4-3; Sequence=VSP_030750, VSP_030751; CC Name=4; CC IsoId=Q9BZL4-4; Sequence=VSP_030751; CC Name=5; CC IsoId=Q9BZL4-5; Sequence=VSP_057216, VSP_057217, VSP_030751; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in heart. CC {ECO:0000269|PubMed:11399775}. CC -!- PTM: Phosphorylation at Thr-560 is essential for its interaction with CC PPP1CB. {ECO:0000269|PubMed:11399775}. CC -!- CAUTION: Although assigned as two separate genes (PPP1R12C and LENG3), CC it is probable that LENG3 does not exist by itself and is a part of the CC PPP1R12C gene. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AF211968; Type=Miscellaneous discrepancy; Note=Unspliced mRNA.; Evidence={ECO:0000305}; CC Sequence=BAB15651.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC85179.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF312028; AAG60045.1; -; mRNA. DR EMBL; AB209452; BAD92689.1; -; mRNA. DR EMBL; AK129529; BAC85179.1; ALT_INIT; mRNA. DR EMBL; AK297426; BAG59854.1; -; mRNA. DR EMBL; AK027086; BAB15651.1; ALT_INIT; mRNA. DR EMBL; AC005782; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010327; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF211968; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL137618; CAB70844.1; -; mRNA. DR EMBL; BC008030; AAH08030.1; -; mRNA. DR CCDS; CCDS12916.1; -. [Q9BZL4-1] DR PIR; T46318; T46318. DR RefSeq; NP_001258547.1; NM_001271618.1. [Q9BZL4-3] DR RefSeq; NP_060077.1; NM_017607.3. [Q9BZL4-1] DR RefSeq; XP_005259070.1; XM_005259013.3. [Q9BZL4-4] DR AlphaFoldDB; Q9BZL4; -. DR SMR; Q9BZL4; -. DR BioGRID; 120144; 59. DR ELM; Q9BZL4; -. DR IntAct; Q9BZL4; 46. DR MINT; Q9BZL4; -. DR STRING; 9606.ENSP00000263433; -. DR GlyGen; Q9BZL4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BZL4; -. DR PhosphoSitePlus; Q9BZL4; -. DR BioMuta; PPP1R12C; -. DR DMDM; 74752476; -. DR EPD; Q9BZL4; -. DR jPOST; Q9BZL4; -. DR MassIVE; Q9BZL4; -. DR MaxQB; Q9BZL4; -. DR PaxDb; 9606-ENSP00000263433; -. DR PeptideAtlas; Q9BZL4; -. DR ProteomicsDB; 4602; -. DR ProteomicsDB; 79868; -. [Q9BZL4-1] DR ProteomicsDB; 79869; -. [Q9BZL4-2] DR ProteomicsDB; 79870; -. [Q9BZL4-3] DR ProteomicsDB; 79871; -. [Q9BZL4-4] DR Pumba; Q9BZL4; -. DR Antibodypedia; 50850; 61 antibodies from 18 providers. DR DNASU; 54776; -. DR Ensembl; ENST00000263433.8; ENSP00000263433.1; ENSG00000125503.13. [Q9BZL4-1] DR Ensembl; ENST00000435544.6; ENSP00000387833.2; ENSG00000125503.13. [Q9BZL4-5] DR GeneID; 54776; -. DR KEGG; hsa:54776; -. DR MANE-Select; ENST00000263433.8; ENSP00000263433.1; NM_017607.4; NP_060077.1. DR UCSC; uc002qix.5; human. [Q9BZL4-1] DR AGR; HGNC:14947; -. DR CTD; 54776; -. DR DisGeNET; 54776; -. DR GeneCards; PPP1R12C; -. DR HGNC; HGNC:14947; PPP1R12C. DR HPA; ENSG00000125503; Low tissue specificity. DR MIM; 613245; gene. DR neXtProt; NX_Q9BZL4; -. DR OpenTargets; ENSG00000125503; -. DR PharmGKB; PA33619; -. DR VEuPathDB; HostDB:ENSG00000125503; -. DR eggNOG; KOG0505; Eukaryota. DR GeneTree; ENSGT00940000161425; -. DR InParanoid; Q9BZL4; -. DR OMA; MTDARTW; -. DR OrthoDB; 5482573at2759; -. DR PhylomeDB; Q9BZL4; -. DR TreeFam; TF105543; -. DR PathwayCommons; Q9BZL4; -. DR SignaLink; Q9BZL4; -. DR SIGNOR; Q9BZL4; -. DR BioGRID-ORCS; 54776; 24 hits in 1146 CRISPR screens. DR ChiTaRS; PPP1R12C; human. DR GenomeRNAi; 54776; -. DR Pharos; Q9BZL4; Tdark. DR PRO; PR:Q9BZL4; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9BZL4; Protein. DR Bgee; ENSG00000125503; Expressed in lower esophagus muscularis layer and 179 other cell types or tissues. DR ExpressionAtlas; Q9BZL4; baseline and differential. 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. DR Genevisible; Q9BZL4; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ANK repeat; Coiled coil; Cytoplasm; KW Cytoskeleton; Phosphoprotein; Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..782 FT /note="Protein phosphatase 1 regulatory subunit 12C" FT /id="PRO_0000315863" FT REPEAT 100..129 FT /note="ANK 1" FT /evidence="ECO:0000255" FT REPEAT 133..162 FT /note="ANK 2" FT /evidence="ECO:0000255" FT REPEAT 226..255 FT /note="ANK 3" FT /evidence="ECO:0000255" FT REPEAT 259..288 FT /note="ANK 4" FT /evidence="ECO:0000255" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 316..686 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 297..329 FT /evidence="ECO:0000255" FT COILED 681..782 FT /evidence="ECO:0000255" FT COMPBIAS 325..353 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 447..467 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 494..512 FT /note="Pro 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..647 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 660..686 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 399 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 407 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 452 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 560 FT /note="Phosphothreonine; by CDC42BP and ROCK2" FT /evidence="ECO:0000269|PubMed:11399775, FT ECO:0007744|PubMed:23186163" FT MOD_RES 604 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 647 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3UMT1" FT VAR_SEQ 1..32 FT /note="MSGEDGPAAGPGAAAAAARERRREQLRQWGAR -> MRNGGPCQPLAAGPRA FT EGASVNWSVTAWGPGT (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057216" FT VAR_SEQ 33..106 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057217" FT VAR_SEQ 410 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3" FT /id="VSP_030750" FT VAR_SEQ 576..638 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_052643" FT VAR_SEQ 609 FT /note="Missing (in isoform 3, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_030751" FT VARIANT 419 FT /note="R -> C (in dbSNP:rs35849605)" FT /id="VAR_048310" FT CONFLICT 438 FT /note="T -> I (in Ref. 8; AAH08030)" FT /evidence="ECO:0000305" FT CONFLICT 527 FT /note="R -> W (in Ref. 2; BAB15651)" FT /evidence="ECO:0000305" FT CONFLICT 537 FT /note="V -> A (in Ref. 2; BAC85179)" FT /evidence="ECO:0000305" SQ SEQUENCE 782 AA; 84881 MW; 677E7EB1B62C2CC8 CRC64; MSGEDGPAAG PGAAAAAARE RRREQLRQWG ARAGAEPGPG ERRARTVRFE RAAEFLAACA GGDLDEARLM LRAADPGPGA ELDPAAPPPA RAVLDSTNAD GISALHQACI DENLEVVRFL VEQGATVNQA DNEGWTPLHV AASCGYLDIA RYLLSHGANI AAVNSDGDLP LDLAESDAME GLLKAEIARR GVDVEAAKRA EEELLLHDTR CWLNGGAMPE ARHPRTGASA LHVAAAKGYI EVMRLLLQAG YDPELRDGDG WTPLHAAAHW GVEDACRLLA EHGGGMDSLT HAGQRPCDLA DEEVLSLLEE LARKQEDLRN QKEASQSRGQ EPQAPSSSKH RRSSVCRLSS REKISLQDLS KERRPGGAGG PPIQDEDEGE EGPTEPPPAE PRTLNGVSSP PHPSPKSPVQ LEEAPFSRRF GLLKTGSSGA LGPPERRTAE GAPGAGLQRS ASSSWLEGTS TQAKELRLAR ITPTPSPKLP EPSVLSEVTK PPPCLENSSP PSRIPEPESP AKPNVPTAST APPADSRDRR RSYQMPVRDE ESESQRKARS RLMRQSRRST QGVTLTDLKE AEKAAGKAPE SEKPAQSLDP SRRPRVPGVE NSDSPAQRAE APDGQGPGPQ AAREHRKVGK EWRGPAEGEE AEPADRSQES STLEGGPSAR RQRWQRDLNP EPEPESEEPD GGFRTLYAEL RRENERLREA LTETTLRLAQ LKVELERATQ RQERFAERPA LLELERFERR ALERKAAELE EELKALSDLR ADNQRLKDEN AALIRVISKL SK //