MYPT1_MOUSE
ID MYPT1_MOUSE Reviewed; 1029 AA.
AC Q9DBR7; Q05A74; Q8CBV2; Q99NB6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 12A;
DE AltName: Full=Myosin phosphatase-targeting subunit 1;
DE Short=Myosin phosphatase target subunit 1;
GN Name=Ppp1r12a {ECO:0000312|MGI:MGI:1309528};
GN Synonyms=Mypt1 {ECO:0000312|MGI:MGI:1309528};
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).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Urinary bladder;
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
RX PubMed=11342221; DOI=10.1016/s0167-4781(00)00285-2;
RA Machida H., Ito M., Okamoto R., Shiraki K., Isaka N., Hartshorne D.J.,
RA Nakano T.;
RT "Molecular cloning and analysis of the 5'-flanking region of human MYPT1
RT gene.";
RL Biochim. Biophys. Acta 1517:424-429(2001).
RN [5]
RP PHOSPHORYLATION, AND INTERACTION WITH ARHA AND CIT.
RX PubMed=8662509; DOI=10.1126/science.273.5272.245;
RA Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M.,
RA Yamamori B., Feng J., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.;
RT "Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-
RT kinase).";
RL Science 273:245-248(1996).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-445; TYR-446;
RP SER-801; SER-861; SER-870 AND SER-994, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [8]
RP INTERACTION WITH SMTNL1, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20634291; DOI=10.1074/jbc.m110.143966;
RA Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S.,
RA Zheng D., Devente J., Hickner R., Haystead T.A.;
RT "Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1
RT expression during sexual development and pregnancy.";
RL J. Biol. Chem. 285:29357-29366(2010).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=31883643; DOI=10.1016/j.ajhg.2019.12.004;
RA Hughes J.J., Alkhunaizi E., Kruszka P., Pyle L.C., Grange D.K.,
RA Berger S.I., Payne K.K., Masser-Frye D., Hu T., Christie M.R., Clegg N.J.,
RA Everson J.L., Martinez A.F., Walsh L.E., Bedoukian E., Jones M.C.,
RA Harris C.J., Riedhammer K.M., Choukair D., Fechner P.Y., Rutter M.M.,
RA Hufnagel S.B., Roifman M., Kletter G.B., Delot E., Vilain E.,
RA Lipinski R.J., Vezina C.M., Muenke M., Chitayat D.;
RT "Loss-of-function variants in PPP1R12A: from isolated sex reversal to
RT holoprosencephaly spectrum and urogenital malformations.";
RL Am. J. Hum. Genet. 106:121-128(2020).
CC -!- FUNCTION: Key regulator of protein phosphatase 1C (PPP1C). Mediates
CC binding to myosin. As part of the PPP1C complex, involved in
CC dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent
CC suppression of HIF1A activity (By similarity).
CC {ECO:0000250|UniProtKB:O14974, ECO:0000250|UniProtKB:Q10728}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC and one or several targeting or regulatory subunits. PPP1R12A mediates
CC binding to myosin. Interacts with ARHA and CIT (By similarity). Binds
CC PPP1R12B, ROCK1 and IL16. Interacts directly with PRKG1. Non-covalent
CC dimer of 2 dimers; PRKG1-PRKG1 and PPP1R12A-PPP1R12A. Interacts with
CC SMTNL1 (By similarity). Interacts with PPP1CB; the interaction is
CC direct. Interacts (when phosphorylated at Ser-445, Ser-472 and Ser-910)
CC with 14-3-3. Interacts with ROCK1 and ROCK2. Interacts with isoform 1
CC and isoform 2 of ZIPK/DAPK3. Interacts with RAF1. Interacts with HIF1AN
CC (By similarity). Interacts with NCKAP1L (By similarity).
CC {ECO:0000250|UniProtKB:O14974}.
CC -!- INTERACTION:
CC Q9DBR7; P0C605-1: Prkg1; NbExp=2; IntAct=EBI-1014335, EBI-15699851;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14974}.
CC Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O14974}.
CC Note=Also along actomyosin filaments. {ECO:0000250|UniProtKB:O14974}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DBR7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBR7-2; Sequence=VSP_038478;
CC -!- TISSUE SPECIFICITY: Expressed in striated and vascular smooth muscle,
CC specificcally in type 2a fibers (at protein level). Expression levels
CC are 20-30% higher in developed males than females (at protein level).
CC {ECO:0000269|PubMed:20634291}.
CC -!- DEVELOPMENTAL STAGE: In neonates, expressed at low levels in striated
CC and smooth muscles. As the animals mature sexually, expression
CC increases 10-20-fold. Pregnancy promotes a 2-3-fold increase in
CC expression in striated, vascular and uterine muscle (at protein level).
CC Expressed in the prosencephalic neural folds at 8.5 dpc. Expressed in
CC the lower urinary tract, specifically in epitheliumof the bladder,
CC urethra, and genital tubercle at 13.5 dpc (PubMed:31883643).
CC {ECO:0000269|PubMed:20634291, ECO:0000269|PubMed:31883643}.
CC -!- DOMAIN: Heterotetramerization is mediated by the interaction between a
CC coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS,
CC the myosin-binding subunit of the myosin phosphatase. {ECO:0000250}.
CC -!- DOMAIN: The KVKF motif mediates interaction with PPP1CB.
CC {ECO:0000250|UniProtKB:O14974}.
CC -!- PTM: Phosphorylated by CIT (Rho-associated kinase) (By similarity).
CC Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-694 (By
CC similarity). Phosphorylated on upon DNA damage, probably by ATM or ATR.
CC In vitro, phosphorylation of Ser-693 by PKA and PKG appears to prevent
CC phosphorylation of the inhibitory site Thr-694, probably mediated by
CC PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-909 by NUAK1
CC promotes interaction with 14-3-3, leading to inhibit interaction with
CC myosin light chain MLC2, preventing dephosphorylation of MLC2. May be
CC phosphorylated at Thr-694 by DMPK; may inhibit the myosin phosphatase
CC activity (By similarity). Phosphorylated at Ser-473 by CDK1 during
CC mitosis, creating docking sites for the POLO box domains of PLK1.
CC Subsequently, PLK1 binds and phosphorylates PPP1R12A (By similarity).
CC {ECO:0000250|UniProtKB:O14974}.
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DR EMBL; AK035230; BAC28990.1; -; mRNA.
DR EMBL; AK004785; BAB23563.1; -; mRNA.
DR EMBL; CH466539; EDL21703.1; -; Genomic_DNA.
DR EMBL; BC125381; AAI25382.1; -; mRNA.
DR EMBL; BC137630; AAI37631.1; -; mRNA.
DR EMBL; AB042280; BAB39108.1; -; Genomic_DNA.
DR CCDS; CCDS36052.1; -. [Q9DBR7-2]
DR CCDS; CCDS88083.1; -. [Q9DBR7-1]
DR RefSeq; NP_082168.1; NM_027892.2. [Q9DBR7-2]
DR RefSeq; XP_006513389.1; XM_006513326.3.
DR AlphaFoldDB; Q9DBR7; -.
DR BMRB; Q9DBR7; -.
DR SMR; Q9DBR7; -.
DR BioGRID; 201677; 27.
DR DIP; DIP-29982N; -.
DR IntAct; Q9DBR7; 8.
DR MINT; Q9DBR7; -.
DR STRING; 10090.ENSMUSP00000069257; -.
DR iPTMnet; Q9DBR7; -.
DR PhosphoSitePlus; Q9DBR7; -.
DR EPD; Q9DBR7; -.
DR jPOST; Q9DBR7; -.
DR MaxQB; Q9DBR7; -.
DR PaxDb; Q9DBR7; -.
DR PeptideAtlas; Q9DBR7; -.
DR PRIDE; Q9DBR7; -.
DR ProteomicsDB; 287660; -. [Q9DBR7-1]
DR ProteomicsDB; 287661; -. [Q9DBR7-2]
DR Antibodypedia; 29770; 637 antibodies from 38 providers.
DR Ensembl; ENSMUST00000070663; ENSMUSP00000069257; ENSMUSG00000019907. [Q9DBR7-2]
DR Ensembl; ENSMUST00000219263; ENSMUSP00000151842; ENSMUSG00000019907. [Q9DBR7-1]
DR GeneID; 17931; -.
DR KEGG; mmu:17931; -.
DR UCSC; uc007gzc.1; mouse. [Q9DBR7-2]
DR UCSC; uc007gzd.1; mouse. [Q9DBR7-1]
DR CTD; 4659; -.
DR MGI; MGI:1309528; Ppp1r12a.
DR VEuPathDB; HostDB:ENSMUSG00000019907; -.
DR eggNOG; KOG0505; Eukaryota.
DR GeneTree; ENSGT00940000156120; -.
DR HOGENOM; CLU_000134_54_0_1; -.
DR InParanoid; Q9DBR7; -.
DR OMA; RKYETNA; -.
DR OrthoDB; 477969at2759; -.
DR PhylomeDB; Q9DBR7; -.
DR TreeFam; TF105543; -.
DR BRENDA; 3.1.3.53; 3474.
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; 17931; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Ppp1r12a; mouse.
DR PRO; PR:Q9DBR7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9DBR7; protein.
DR Bgee; ENSMUSG00000019907; Expressed in ascending aorta and 222 other tissues.
DR ExpressionAtlas; Q9DBR7; baseline and differential.
DR Genevisible; Q9DBR7; MM.
DR GO; GO:0031672; C:A band; IDA:UniProtKB.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0043292; C:contractile fiber; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
DR GO; GO:0019208; F:phosphatase regulator activity; ISS:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0035508; P:positive regulation of myosin-light-chain-phosphatase activity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0035507; P:regulation of myosin-light-chain-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:MGI.
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 PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
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; Hydroxylation;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1029
FT /note="Protein phosphatase 1 regulatory subunit 12A"
FT /id="PRO_0000067026"
FT REPEAT 39..68
FT /note="ANK 1"
FT REPEAT 72..101
FT /note="ANK 2"
FT REPEAT 105..134
FT /note="ANK 3"
FT REPEAT 138..164
FT /note="ANK 4"
FT REPEAT 198..227
FT /note="ANK 5"
FT REPEAT 231..260
FT /note="ANK 6"
FT REGION 290..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..863
FT /note="Interaction with ROCK2"
FT /evidence="ECO:0000250"
FT REGION 808..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..38
FT /note="KVKF motif"
FT COMPBIAS 303..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 100
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 226
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT /evidence="ECO:0000250"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 445
FT /note="Phosphoserine; by NUAK1"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 446
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 472
FT /note="Phosphoserine; by NUAK1"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 473
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 690
FT /note="Phosphoserine; by PKA and PKG; in vitro"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 693
FT /note="Phosphoserine; by PKA and PKG; in vitro"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 694
FT /note="Phosphothreonine; by ROCK1, ROCK2, CDC42BP,
FT ZIPK/DAPK3 and RAF1"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 851
FT /note="Phosphoserine; by ROCK2"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 870
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 909
FT /note="Phosphoserine; by NUAK1"
FT /evidence="ECO:0000250|UniProtKB:O14974"
FT MOD_RES 994
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 985..1029
FT /note="ERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK -> VAG
FT KSQYLLGGTKSSRKKNI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038478"
SQ SEQUENCE 1029 AA; 114996 MW; C466573AC1DFC81F CRC64;
MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL
HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD
IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERVMLRD
ARQWLNSGHI SDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA
HWGKEEACRI LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQTLL HSEKRDKKSP
LIESTANMEN NQPQKAFKNK ETLIIEPEKN ASRIESLEHE KADEEEEGKK DESSCSSEED
EEDDSESEAE TDKTKPMASV SNAHTSSTQA APAAVTAPTL SSNQGTPTSP VKKFPISTTK
ISPKEEERKD ESPASWRLGL RKTGSYGALA EISASKEAQK EKDTAGVMRS ASSPRLSSSL
DNKEKEKDNK GTRLAYVTPT IPRRLASTSD IEEKENRESS SLRTSSSYTR RKWEDDLKKN
SSINEGSTYH RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQRSLPSST STAAKTPPGS
SSAGTQSSTS NRLWAEDSTE KEKDSAPTAV TIPVAPTVVN AAAPSTTTLT TTTAGTVSEV
RERRRSYLTP VRDEESESQR KARSRQARQS RRSTQGVTLT DLQEAEKTIG RSRSTRTREQ
ENEEKEKEEK EKQDKEKQEE KKESEASRED EYKQKYSRTY DETYTRYRPV STSSSSAPSS
SSLSTLGSTL YASSQLNRPN SLVGITSAYS RGLAKENERE GEKKEEEKEG EDKSQPKSIR
ERRRPREKRR STGVSFWTQD SDENEQERQS DTEDGSSKRE TQTDSVSRYD SSSTSSSDRY
DSLLGRSASY SYLEDRKPYS SRLEKDDSTD FKKLYEQILA ENEKLKAQLH DTNMELTDLK
LQLEKATQRQ ERFADRSQLE MEKRERRALE RRISEMEEEL KMLPDLKADN QRLKDENGAL
IRVISKLSK
