PP12C_HUMAN
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 03-AUG-2022, entry version 159.
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; Q9UI12: ATP6V1H; NbExp=3; IntAct=EBI-721802, EBI-724719;
CC Q9BZL4; Q7RTU4: BHLHA9; NbExp=3; IntAct=EBI-721802, EBI-17508719;
CC Q9BZL4; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-721802, EBI-8643161;
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: C1orf109; 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; 49.
DR ELM; Q9BZL4; -.
DR IntAct; Q9BZL4; 38.
DR MINT; Q9BZL4; -.
DR STRING; 9606.ENSP00000263433; -.
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; Q9BZL4; -.
DR PeptideAtlas; Q9BZL4; -.
DR PRIDE; 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 Antibodypedia; 50850; 57 antibodies from 17 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 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; INCCDHE; -.
DR OrthoDB; 477969at2759; -.
DR PhylomeDB; Q9BZL4; -.
DR TreeFam; TF105543; -.
DR PathwayCommons; Q9BZL4; -.
DR SignaLink; Q9BZL4; -.
DR SIGNOR; Q9BZL4; -.
DR BioGRID-ORCS; 54776; 21 hits in 1070 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 177 other tissues.
DR ExpressionAtlas; Q9BZL4; baseline and differential.
DR Genevisible; Q9BZL4; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; 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 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; IPR031205; PPP1R12C.
DR InterPro; IPR031775; PRKG1_interact.
DR PANTHER; PTHR24179:SF27; PTHR24179:SF27; 2.
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; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
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
