PR15A_MOUSE
ID PR15A_MOUSE Reviewed; 657 AA.
AC P17564; Q3TJS6; Q3U3L5; Q8C579;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 15A;
DE AltName: Full=Growth arrest and DNA damage-inducible protein GADD34;
DE AltName: Full=Myeloid differentiation primary response protein MyD116;
GN Name=Ppp1r15a; Synonyms=Gadd34, Myd116;
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 [MRNA] (ISOFORM 1).
RC STRAIN=SL;
RX PubMed=2339071; DOI=10.1093/nar/18.9.2823;
RA Lord K.A., Hoffman-Liebermann B., Liebermann D.A.;
RT "Sequence of MyD116 cDNA: a novel myeloid differentiation primary response
RT gene induced by IL6.";
RL Nucleic Acids Res. 18:2823-2823(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Placenta;
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 [3]
RP INDUCTION.
RX PubMed=8139541; DOI=10.1128/mcb.14.4.2361-2371.1994;
RA Zhan Q., Lord K.A., Alamo I. Jr., Hollander M.C., Carrier F., Ron D.,
RA Kohn K.W., Hoffman B., Liebermann D.A., Fornace A.J. Jr.;
RT "The gadd and MyD genes define a novel set of mammalian genes encoding
RT acidic proteins that synergistically suppress cell growth.";
RL Mol. Cell. Biol. 14:2361-2371(1994).
RN [4]
RP INTERACTION WITH PCNA.
RX PubMed=9371605; DOI=10.1128/jvi.71.12.9442-9449.1997;
RA Brown S.M., MacLean A.R., McKie E.A., Harland J.;
RT "The herpes simplex virus virulence factor ICP34.5 and the cellular protein
RT MyD116 complex with proliferating cell nuclear antigen through the 63-
RT amino-acid domain conserved in ICP34.5, MyD116, and GADD34.";
RL J. Virol. 71:9442-9449(1997).
RN [5]
RP INTERACTION WITH PPP1CA.
RX PubMed=9023344; DOI=10.1073/pnas.94.3.843;
RA He B., Gross M., Roizman B.;
RT "The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein
RT phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic
RT translation initiation factor 2 and preclude the shutoff of protein
RT synthesis by double-stranded RNA-activated protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:843-848(1997).
RN [6]
RP FUNCTION, INTERACTION WITH PPP1CA, AND MUTAGENESIS OF VAL-549.
RX PubMed=11381086; DOI=10.1083/jcb.153.5.1011;
RA Novoa I., Zeng H., Harding H.P., Ron D.;
RT "Feedback inhibition of the unfolded protein response by GADD34-mediated
RT dephosphorylation of eIF2alpha.";
RL J. Cell Biol. 153:1011-1022(2001).
RN [7]
RP INTERACTION WITH LYN.
RX PubMed=11517336; DOI=10.1073/pnas.191130798;
RA Grishin A.V., Azhipa O., Semenov I., Corey S.J.;
RT "Interaction between growth arrest-DNA damage protein 34 and Src kinase Lyn
RT negatively regulates genotoxic apoptosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10172-10177(2001).
RN [8]
RP INDUCTION, AND FUNCTION.
RX PubMed=12606582; DOI=10.1093/emboj/cdg112;
RA Novoa I., Zhang Y., Zeng H., Jungreis R., Harding H.P., Ron D.;
RT "Stress-induced gene expression requires programmed recovery from
RT translational repression.";
RL EMBO J. 22:1180-1187(2003).
RN [9]
RP FUNCTION, INDUCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12824288; DOI=10.1096/fj.02-1184fje;
RA Kojima E., Takeuchi A., Haneda M., Yagi A., Hasegawa T., Yamaki K.,
RA Takeda K., Akira S., Shimokata K., Isobe K.;
RT "The function of GADD34 is a recovery from a shutoff of protein synthesis
RT induced by ER stress: elucidation by GADD34-deficient mice.";
RL FASEB J. 17:1573-1575(2003).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16478986; DOI=10.1128/mcb.26.5.1644-1653.2006;
RA Patterson A.D., Hollander M.C., Miller G.F., Fornace A.J. Jr.;
RT "Gadd34 requirement for normal hemoglobin synthesis.";
RL Mol. Cell. Biol. 26:1644-1653(2006).
RN [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=17670836; DOI=10.1128/jvi.01063-07;
RA Minami K., Tambe Y., Watanabe R., Isono T., Haneda M., Isobe K.,
RA Kobayashi T., Hino O., Okabe H., Chano T., Inoue H.;
RT "Suppression of viral replication by stress-inducible GADD34 protein via
RT the mammalian serine/threonine protein kinase mTOR pathway.";
RL J. Virol. 81:11106-11115(2007).
RN [12]
RP INDUCTION.
RX PubMed=19131336; DOI=10.1074/jbc.m806735200;
RA Lee Y.Y., Cevallos R.C., Jan E.;
RT "An upstream open reading frame regulates translation of GADD34 during
RT cellular stresses that induce eIF2alpha phosphorylation.";
RL J. Biol. Chem. 284:6661-6673(2009).
CC -!- FUNCTION: Recruits the serine/threonine-protein phosphatase PPP1CA to
CC prevents excessive phosphorylation of the translation initiation factor
CC eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis
CC initiated by stress-inducible kinases and facilitating recovery of
CC cells from stress (PubMed:11381086, PubMed:12824288). Down-regulates
CC the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1
CC by PP1 (By similarity). May promote apoptosis by inducing TP53
CC phosphorylation on 'Ser-15' (By similarity). Plays an essential role in
CC autophagy by tuning translation during starvation, thus enabling
CC lysosomal biogenesis and a sustained autophagic flux (By similarity).
CC Acts also a viral restriction factor by attenuating vesicular
CC stomatitis virus (VSV) replication (PubMed:17670836).
CC {ECO:0000250|UniProtKB:O75807, ECO:0000269|PubMed:11381086,
CC ECO:0000269|PubMed:12606582, ECO:0000269|PubMed:12824288,
CC ECO:0000269|PubMed:16478986, ECO:0000269|PubMed:17670836}.
CC -!- SUBUNIT: Interacts with PPP1CA (PubMed:9023344, PubMed:11381086).
CC Interacts with EIF2S1 (By similarity). Interacts with PCNA
CC (PubMed:9371605). Interacts with LYN and KMT2A/MLL1 (PubMed:11517336).
CC Interacts with PPP1R1A and SMARCB1. Interacts with SMAD7. Interacts
CC with BAG1. Interacts with NOX4 (By similarity).
CC {ECO:0000250|UniProtKB:O75807, ECO:0000269|PubMed:11381086,
CC ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:9023344,
CC ECO:0000269|PubMed:9371605}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:O75807}.
CC Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic
CC side {ECO:0000250|UniProtKB:O75807}. Note=Associates with membranes via
CC an N-terminal amphipathic intramembrane region.
CC {ECO:0000250|UniProtKB:O75807}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P17564-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P17564-2; Sequence=VSP_031651;
CC -!- TISSUE SPECIFICITY: Expressed strongly in spleen and lung, moderately
CC in thymus and muscle, and weakly in brain.
CC {ECO:0000269|PubMed:12824288}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at 8.5 dpc, and decreases to
CC undetectable levels at 10.5 dpc and 11.5 dpc. Expression is strongly
CC up-regulated at 12.5 dpc, decreases at 16.5 dpc and reappears at 18.5
CC dpc. At 12.5 dpc, ubiquitously expressed, with high levels in brain,
CC spinal cord, tongue, lung and genital tubercle.
CC {ECO:0000269|PubMed:12824288}.
CC -!- INDUCTION: Specifically produced in response to stress: in absence of
CC stress, some upstream open reading frame (uORF) of this transcript is
CC translated, thereby preventing its translation (PubMed:19131336). By
CC IL6 and various endoplasmic stresses such as methyl methanesulfonate
CC (PubMed:12606582, PubMed:12824288, PubMed:8139541).
CC {ECO:0000269|PubMed:12606582, ECO:0000269|PubMed:12824288,
CC ECO:0000269|PubMed:19131336, ECO:0000269|PubMed:8139541}.
CC -!- INDUCTION: (Microbial infection) By infection with various viruses such
CC as vesicular stomatitis virus (VSV). {ECO:0000269|PubMed:17670836}.
CC -!- PTM: Phosphorylated at multiple Ser/Thr residues. Phosphorylated on
CC tyrosine by LYN; which impairs its antiproliferative activity.
CC Phosphorylation at Tyr-239 enhances proteasomal degradation, this
CC position is dephosphorylated by PTPN2. {ECO:0000250|UniProtKB:O75807}.
CC -!- PTM: Polyubiquitinated. Exhibits a rapid proteasomal degradation with a
CC half-life under 1 hour, ubiquitination depends on endoplasmic reticulum
CC association. {ECO:0000250|UniProtKB:O75807}.
CC -!- DISRUPTION PHENOTYPE: Mice display abnormal erythrocytes and reduced
CC hemoglobin content due to defects in hemoglobin synthesis.
CC {ECO:0000269|PubMed:12824288, ECO:0000269|PubMed:16478986}.
CC -!- SIMILARITY: Belongs to the PPP1R15 family. {ECO:0000305}.
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DR EMBL; X51829; CAA36128.1; -; mRNA.
DR EMBL; AK079339; BAC37613.1; -; mRNA.
DR EMBL; AK154697; BAE32770.1; -; mRNA.
DR EMBL; AK167317; BAE39419.1; -; mRNA.
DR CCDS; CCDS21249.1; -. [P17564-1]
DR PIR; S10001; S10001.
DR RefSeq; NP_032680.1; NM_008654.2. [P17564-1]
DR AlphaFoldDB; P17564; -.
DR BioGRID; 201637; 2.
DR STRING; 10090.ENSMUSP00000049488; -.
DR iPTMnet; P17564; -.
DR PhosphoSitePlus; P17564; -.
DR PaxDb; P17564; -.
DR PRIDE; P17564; -.
DR Antibodypedia; 4340; 305 antibodies from 34 providers.
DR DNASU; 17872; -.
DR Ensembl; ENSMUST00000042105; ENSMUSP00000049488; ENSMUSG00000040435. [P17564-1]
DR Ensembl; ENSMUST00000167273; ENSMUSP00000128497; ENSMUSG00000040435. [P17564-1]
DR GeneID; 17872; -.
DR KEGG; mmu:17872; -.
DR UCSC; uc009gvt.3; mouse. [P17564-1]
DR CTD; 23645; -.
DR MGI; MGI:1927072; Ppp1r15a.
DR VEuPathDB; HostDB:ENSMUSG00000040435; -.
DR eggNOG; ENOG502S745; Eukaryota.
DR GeneTree; ENSGT00940000154404; -.
DR HOGENOM; CLU_028812_0_0_1; -.
DR InParanoid; P17564; -.
DR OMA; VRAWVYR; -.
DR PhylomeDB; P17564; -.
DR TreeFam; TF105547; -.
DR BioGRID-ORCS; 17872; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Ppp1r15a; mouse.
DR PRO; PR:P17564; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P17564; protein.
DR Bgee; ENSMUSG00000040435; Expressed in fetal liver hematopoietic progenitor cell and 195 other tissues.
DR ExpressionAtlas; P17564; baseline and differential.
DR Genevisible; P17564; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1903912; P:negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0010955; P:negative regulation of protein processing; ISO:MGI.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
DR GO; GO:1990441; P:negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:1903917; P:positive regulation of endoplasmic reticulum stress-induced eIF2 alpha dephosphorylation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ParkinsonsUK-UCL.
DR GO; GO:1902310; P:positive regulation of peptidyl-serine dephosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; ISO:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; ISO:MGI.
DR GO; GO:0060734; P:regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0036496; P:regulation of translational initiation by eIF2 alpha dephosphorylation; ISO:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
DR InterPro; IPR019523; Prot_Pase1_reg-su15A/B_C.
DR Pfam; PF10488; PP1c_bdg; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Endoplasmic reticulum; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; Repeat; Stress response; Translation regulation;
KW Ubl conjugation.
FT CHAIN 1..657
FT /note="Protein phosphatase 1 regulatory subunit 15A"
FT /id="PRO_0000096665"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT INTRAMEM 22..39
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT TOPO_DOM 40..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT REPEAT 283..322
FT /note="1"
FT REPEAT 323..360
FT /note="2"
FT REPEAT 361..398
FT /note="3"
FT REPEAT 399..436
FT /note="4"
FT REPEAT 437..451
FT /note="5; truncated"
FT REGION 1..60
FT /note="Required for localization in the endoplasmic
FT reticulum"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT REGION 65..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..451
FT /note="4.5 X approximate repeats"
FT REGION 291..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..503
FT /note="Interaction with SMAD7"
FT /evidence="ECO:0000250"
FT REGION 443..548
FT /note="Interaction with KMT2A/MLL1"
FT /evidence="ECO:0000250"
FT REGION 529..576
FT /note="Interaction with SMARCB1"
FT /evidence="ECO:0000250"
FT REGION 610..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT MOD_RES 368
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT MOD_RES 406
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT MOD_RES 505
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75807"
FT VAR_SEQ 284..360
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031651"
FT MUTAGEN 549
FT /note="V->E: Abolishes interaction with PP1."
FT /evidence="ECO:0000269|PubMed:11381086"
FT CONFLICT 224
FT /note="P -> H (in Ref. 2; BAE39419)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="E -> G (in Ref. 2; BAE32770)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="Y -> C (in Ref. 2; BAE32770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 71840 MW; 9B217001019C38A7 CRC64;
MAPSPRPQHV LHWRDAHNFY LLSPLMGLLS RAWSRLRGPE VPEAWLAKTV TGADQIEAAA
LLTPTPVSGN LLPHGETEES GSPEQSQAAQ RLCLVEAESS PPETWGLSNV DEYNAKPGQD
DLREKEMERT AGKATLQPAG LQGADKRLGE VVAREEGVAE PAYPTSQLEG GPAENEEDGE
TVKTYQASAA SIAPGYKPST PVPFLGEAEH QATEEKGTEN KADPSNSPSS GSHSRAWEYY
SREKPKQEGE AKVEAHRAGQ GHPCRNAEAE EGGPETTFVC TGNAFLKAWV YRPGEDTEEE
DNSDSDSAEE DTAQTGATPH TSAFLKAWVY RPGEDTEEED SDSDSAEEDT AQTGATPHTS
AFLKAWVYRP GEDTEEENSD LDSAEEDTAQ TGATPHTSAF LKAWVYRPGE DTEEENSDLD
SAEEDTAQTG ATPHTSPFLK AWVYRPGEDT EDDTEEEEDS ENVAPGDSET ADSSQSPCLQ
PQRCLPGEKT KGRGEEPPLF QVAFYLPGEK PESPWAAPKL PLRLQRRLRL FKAPTRDQDP
EIPLKARKVH FAEKVTVHFL AVWAGPAQAA RRGPWEQFAR DRSRFARRIA QAEEKLGPYL
TPDSRARAWA RLRNPSLPQS EPRSSSEATP LTQDVTTPSP LPSETPSPSL YLGGRRG
