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Protein phosphatase 1 regulatory subunit 15A (Growth arrest and DNA damage-inducible protein GADD34) (Myeloid differentiation primary response protein MyD116 homolog)

 PR15A_HUMAN             Reviewed;         674 AA.
O75807; B4DKQ3; Q6IA96; Q9NVU6;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
28-FEB-2018, entry version 127.
RecName: Full=Protein phosphatase 1 regulatory subunit 15A;
AltName: Full=Growth arrest and DNA damage-inducible protein GADD34;
AltName: Full=Myeloid differentiation primary response protein MyD116 homolog;
Name=PPP1R15A; Synonyms=GADD34;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
PubMed=9153226; DOI=10.1074/jbc.272.21.13731;
Hollander M.C., Zhan Q., Bae I., Fornace A.J. Jr.;
"Mammalian GADD34, an apoptosis- and DNA damage-inducible gene.";
J. Biol. Chem. 272:13731-13737(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-32.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS GLU-277; SER-312; PRO-316; SER-476 AND ALA-597.
TISSUE=Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION.
PubMed=8139541; DOI=10.1128/MCB.14.4.2361;
Zhan Q., Lord K.A., Alamo I. Jr., Hollander M.C., Carrier F., Ron D.,
Kohn K.W., Hoffman B., Liebermann D.A., Fornace A.J. Jr.;
"The gadd and MyD genes define a novel set of mammalian genes encoding
acidic proteins that synergistically suppress cell growth.";
Mol. Cell. Biol. 14:2361-2371(1994).
[7]
INTERACTION WITH KMT2A/MLL1 AND SMARCB1, AND INDUCTION.
PubMed=10490642; DOI=10.1128/MCB.19.10.7050;
Adler H.T., Chinery R., Wu D.Y., Kussick S.J., Payne J.M.,
Fornace A.J. Jr., Tkachuk D.C.;
"Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and
associate with the GADD34 and hSNF5/INI1 proteins.";
Mol. Cell. Biol. 19:7050-7060(1999).
[8]
INTERACTION WITH LYN, AND PHOSPHORYLATION.
PubMed=11517336; DOI=10.1073/pnas.191130798;
Grishin A.V., Azhipa O., Semenov I., Corey S.J.;
"Interaction between growth arrest-DNA damage protein 34 and Src
kinase Lyn negatively regulates genotoxic apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 98:10172-10177(2001).
[9]
INTERACTION WITH PP1 AND PPP1R1A, AND FUNCTION.
PubMed=11564868; DOI=10.1128/MCB.21.20.6841-6850.2001;
Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.;
"Growth arrest and DNA damage-inducible protein GADD34 assembles a
novel signaling complex containing protein phosphatase 1 and inhibitor
1.";
Mol. Cell. Biol. 21:6841-6850(2001).
[10]
INTERACTION WITH SMARCB1 AND PP1, AND MUTAGENESIS OF 555-LYS--PHE-558.
PubMed=12016208; DOI=10.1074/jbc.M200955200;
Wu D.Y., Tkachuck D.C., Roberson R.S., Schubach W.H.;
"The human SNF5/INI1 protein facilitates the function of the growth
arrest and DNA damage-inducible protein (GADD34) and modulates GADD34-
bound protein phosphatase-1 activity.";
J. Biol. Chem. 277:27706-27715(2002).
[11]
INDUCTION.
PubMed=12114539; DOI=10.1073/pnas.152327199;
Sarkar D., Su Z.-Z., Lebedeva I.V., Sauane M., Gopalkrishnan R.V.,
Valerie K., Dent P., Fisher P.B.;
"mda-7 (IL-24) Mediates selective apoptosis in human melanoma cells by
inducing the coordinated overexpression of the GADD family of genes by
means of p38 MAPK.";
Proc. Natl. Acad. Sci. U.S.A. 99:10054-10059(2002).
[12]
FUNCTION.
PubMed=14635196; DOI=10.1002/jcb.10711;
Yagi A., Hasegawa Y., Xiao H., Haneda M., Kojima E., Nishikimi A.,
Hasegawa T., Shimokata K., Isobe K.;
"GADD34 induces p53 phosphorylation and p21/WAF1 transcription.";
J. Cell. Biochem. 90:1242-1249(2003).
[13]
FUNCTION, MUTAGENESIS OF 556-VAL--SER-558; ARG-612; ARG-614 AND
ARG-618, AND SUBCELLULAR LOCATION.
PubMed=12556489; DOI=10.1128/MCB.23.4.1292-1303.2003;
Brush M.H., Weiser D.C., Shenolikar S.;
"Growth arrest and DNA damage-inducible protein GADD34 targets protein
phosphatase 1 alpha to the endoplasmic reticulum and promotes
dephosphorylation of the alpha subunit of eukaryotic translation
initiation factor 2.";
Mol. Cell. Biol. 23:1292-1303(2003).
[14]
INTERACTION WITH BAG1.
PubMed=12724406; DOI=10.1128/MCB.23.10.3477-3486.2003;
Hung W.J., Roberson R.S., Taft J., Wu D.Y.;
"Human BAG-1 proteins bind to the cellular stress response protein
GADD34 and interfere with GADD34 functions.";
Mol. Cell. Biol. 23:3477-3486(2003).
[15]
FUNCTION, AND INTERACTION WITH SMAD7.
PubMed=14718519; DOI=10.1083/jcb.200307151;
Shi W., Sun C., He B., Xiong W., Shi X., Yao D., Cao X.;
"GADD34-PP1c recruited by Smad7 dephosphorylates TGFbeta type I
receptor.";
J. Cell Biol. 164:291-300(2004).
[16]
INTERACTION WITH PP1.
PubMed=15705855; DOI=10.1126/science.1101902;
Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D.,
Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.;
"A selective inhibitor of eIF2alpha dephosphorylation protects cells
from ER stress.";
Science 307:935-939(2005).
[17]
SUBCELLULAR LOCATION, TOPOLOGY, INTRAMEMBRANE REGION, AND MUTAGENESIS
OF VAL-25 AND LEU-29.
PubMed=21518769; DOI=10.1074/jbc.M110.212787;
Zhou W., Brush M.H., Choy M.S., Shenolikar S.;
"Association with endoplasmic reticulum promotes proteasomal
degradation of GADD34 protein.";
J. Biol. Chem. 286:21687-21696(2011).
[18]
PHOSPHORYLATION AT TYR-262; TYR-391; TYR-434 AND TYR-512,
UBIQUITINATION, AND MUTAGENESIS OF TYR-262.
PubMed=24092754; DOI=10.1074/jbc.M113.504407;
Zhou W., Jeyaraman K., Yusoff P., Shenolikar S.;
"Phosphorylation at tyrosine 262 promotes GADD34 protein turnover.";
J. Biol. Chem. 288:33146-33155(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Recruits the serine/threonine-protein phosphatase PP1 to
dephosphorylate the translation initiation factor eIF-2A/EIF2S1,
thereby reversing the shut-off of protein synthesis initiated by
stress-inducible kinases and facilitating recovery of cells from
stress. Down-regulates the TGF-beta signaling pathway by promoting
dephosphorylation of TGFB1 by PP1. May promote apoptosis by
inducing TP53 phosphorylation on 'Ser-15'.
{ECO:0000269|PubMed:11564868, ECO:0000269|PubMed:12556489,
ECO:0000269|PubMed:14635196, ECO:0000269|PubMed:14718519,
ECO:0000269|PubMed:8139541}.
-!- SUBUNIT: Interacts with PCNA (By similarity). Interacts with LYN
and KMT2A/MLL1. Interacts with PP1, PPP1R1A and SMARCB1. Interacts
with SMAD7. Interacts with BAG1. {ECO:0000250,
ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:11517336,
ECO:0000269|PubMed:11564868, ECO:0000269|PubMed:12016208,
ECO:0000269|PubMed:12724406, ECO:0000269|PubMed:14718519,
ECO:0000269|PubMed:15705855}.
-!- INTERACTION:
P56545:CTBP2; NbExp=2; IntAct=EBI-714746, EBI-741533;
Q13522:PPP1R1A; NbExp=4; IntAct=EBI-714746, EBI-1568511;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein; Cytoplasmic side {ECO:0000269|PubMed:12556489,
ECO:0000269|PubMed:21518769}. Mitochondrion outer membrane;
Peripheral membrane protein; Cytoplasmic side
{ECO:0000269|PubMed:21518769}. Note=Associates with membranes via
an N-terminal amphipathic intramembrane region.
{ECO:0000269|PubMed:21518769}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75807-1; Sequence=Displayed;
Name=2;
IsoId=O75807-2; Sequence=VSP_057083, VSP_057084;
Note=No experimental confirmation available.;
-!- INDUCTION: By methyl methanesulfonate and ionizing irradiation. By
IL24/interleukin-24 in melanoma cells; which induces apoptosis.
{ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:12114539,
ECO:0000269|PubMed:9153226}.
-!- PTM: Phosphorylated at multiple Ser/Thr residues. Phosphorylated
on tyrosine by LYN; which impairs its antiproliferative activity.
Phosphorylation at Tyr-262 enhances proteasomal degradation, this
position is dephosphorylated by PTPN2.
{ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:24092754}.
-!- PTM: Polyubiquitinated. Exhibits a rapid proteasomal degradation
with a half-life under 1 hour, ubiquitination depends on
endoplasmic reticulum association. {ECO:0000269|PubMed:24092754}.
-!- MISCELLANEOUS: The phosphatase activity of the PPP1R15A-PP1
complex toward EIF2S1 is specifically inhibited by Salubrinal, a
drug that protects cells from endoplasmic reticulum stress.
-!- SIMILARITY: Belongs to the PPP1R15 family. {ECO:0000305}.
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EMBL; U83981; AAC25631.1; -; mRNA.
EMBL; CR457259; CAG33540.1; -; mRNA.
EMBL; AK001361; BAA91649.1; -; mRNA.
EMBL; AK296668; BAG59265.1; -; mRNA.
EMBL; CH471177; EAW52409.1; -; Genomic_DNA.
EMBL; BC003067; AAH03067.1; -; mRNA.
CCDS; CCDS12738.1; -. [O75807-1]
RefSeq; NP_055145.3; NM_014330.3. [O75807-1]
UniGene; Hs.631593; -.
PDB; 4XPN; X-ray; 2.29 A; B/D=552-591.
PDBsum; 4XPN; -.
ProteinModelPortal; O75807; -.
SMR; O75807; -.
BioGrid; 117172; 32.
IntAct; O75807; 12.
MINT; O75807; -.
STRING; 9606.ENSP00000200453; -.
iPTMnet; O75807; -.
PhosphoSitePlus; O75807; -.
BioMuta; PPP1R15A; -.
MaxQB; O75807; -.
PaxDb; O75807; -.
PeptideAtlas; O75807; -.
PRIDE; O75807; -.
DNASU; 23645; -.
Ensembl; ENST00000200453; ENSP00000200453; ENSG00000087074. [O75807-1]
GeneID; 23645; -.
KEGG; hsa:23645; -.
UCSC; uc002pky.5; human. [O75807-1]
CTD; 23645; -.
DisGeNET; 23645; -.
EuPathDB; HostDB:ENSG00000087074.7; -.
GeneCards; PPP1R15A; -.
H-InvDB; HIX0015305; -.
H-InvDB; HIX0174313; -.
HGNC; HGNC:14375; PPP1R15A.
HPA; CAB018395; -.
HPA; HPA020240; -.
MIM; 611048; gene.
neXtProt; NX_O75807; -.
OpenTargets; ENSG00000087074; -.
PharmGKB; PA33632; -.
eggNOG; ENOG410ITE6; Eukaryota.
eggNOG; ENOG410Y1YJ; LUCA.
GeneTree; ENSGT00510000049287; -.
HOGENOM; HOG000060154; -.
HOVERGEN; HBG052542; -.
InParanoid; O75807; -.
KO; K14019; -.
OMA; VRAWVYR; -.
OrthoDB; EOG091G19MD; -.
PhylomeDB; O75807; -.
TreeFam; TF105547; -.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
SignaLink; O75807; -.
SIGNOR; O75807; -.
ChiTaRS; PPP1R15A; human.
GeneWiki; PPP1R15A; -.
GenomeRNAi; 23645; -.
PRO; PR:O75807; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000087074; -.
CleanEx; HS_PPP1R15A; -.
ExpressionAtlas; O75807; baseline and differential.
Genevisible; O75807; HS.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:ParkinsonsUK-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:ParkinsonsUK-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0008157; F:protein phosphatase 1 binding; IDA:ParkinsonsUK-UCL.
GO; GO:0072542; F:protein phosphatase activator activity; IC:ParkinsonsUK-UCL.
GO; GO:0019888; F:protein phosphatase regulator activity; IC:ParkinsonsUK-UCL.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:ProtInc.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL.
GO; GO:1903898; P:negative regulation of PERK-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:1903917; P:positive regulation of endoplasmic reticulum stress-induced eIF2 alpha dephosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:1902310; P:positive regulation of peptidyl-serine dephosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0032058; P:positive regulation of translational initiation in response to stress; IC:ParkinsonsUK-UCL.
GO; GO:0070972; P:protein localization to endoplasmic reticulum; IMP:ParkinsonsUK-UCL.
GO; GO:0036496; P:regulation of translational initiation by eIF2 alpha dephosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
InterPro; IPR019523; Prot_Pase1_reg-su15A/B_C.
Pfam; PF10488; PP1c_bdg; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Endoplasmic reticulum; Membrane; Mitochondrion;
Mitochondrion outer membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Stress response; Translation regulation;
Ubl conjugation.
CHAIN 1 674 Protein phosphatase 1 regulatory subunit
15A.
/FTId=PRO_0000320518.
TOPO_DOM 1 21 Cytoplasmic.
{ECO:0000305|PubMed:21518769}.
INTRAMEM 22 39 Helical. {ECO:0000305|PubMed:21518769}.
TOPO_DOM 40 674 Cytoplasmic.
{ECO:0000305|PubMed:21518769}.
REPEAT 337 369 1.
REPEAT 384 417 2.
REPEAT 427 460 3.
REPEAT 477 510 4.
REGION 1 60 Required for localization in the
endoplasmic reticulum.
REGION 337 510 4 X 34 AA approximate repeats.
REGION 337 510 Interaction with SMAD7.
{ECO:0000269|PubMed:14718519}.
REGION 483 555 Interaction with KMT2A/MLL1.
REGION 536 583 Interaction with SMARCB1.
COMPBIAS 112 115 Poly-Asp.
COMPBIAS 160 503 Glu-rich.
COMPBIAS 518 521 Poly-Pro.
COMPBIAS 661 666 Poly-Ala.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 262 262 Phosphotyrosine.
{ECO:0000269|PubMed:24092754}.
MOD_RES 391 391 Phosphotyrosine.
{ECO:0000269|PubMed:24092754}.
MOD_RES 434 434 Phosphotyrosine.
{ECO:0000269|PubMed:24092754}.
MOD_RES 512 512 Phosphotyrosine.
{ECO:0000269|PubMed:24092754}.
VAR_SEQ 16 16 A -> D (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057083.
VAR_SEQ 17 175 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057084.
VARIANT 31 31 R -> H (in dbSNP:rs564196).
/FTId=VAR_039186.
VARIANT 32 32 A -> T (in dbSNP:rs3786734).
{ECO:0000269|Ref.2}.
/FTId=VAR_039187.
VARIANT 199 199 V -> A (in dbSNP:rs611251).
/FTId=VAR_039188.
VARIANT 251 251 R -> P (in dbSNP:rs557806).
/FTId=VAR_039189.
VARIANT 277 277 K -> E (in dbSNP:rs610308).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_039190.
VARIANT 312 312 G -> S (in dbSNP:rs11541192).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_062226.
VARIANT 316 316 A -> P (in dbSNP:rs556052).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_039191.
VARIANT 381 381 A -> V (in dbSNP:rs1050166).
/FTId=VAR_039192.
VARIANT 476 476 R -> S (in dbSNP:rs35087747).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_039193.
VARIANT 594 594 R -> C (in dbSNP:rs2270946).
/FTId=VAR_039194.
VARIANT 597 597 T -> A (in dbSNP:rs500079).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_039195.
MUTAGEN 25 25 V->R: Localizes to cytoplasm, degraded
more slowly.
{ECO:0000269|PubMed:21518769}.
MUTAGEN 29 29 L->R: Localizes to cytoplasm.
{ECO:0000269|PubMed:21518769}.
MUTAGEN 262 262 Y->F: Significantly reduced turnover.
{ECO:0000269|PubMed:24092754}.
MUTAGEN 555 558 KVRF->AAAA: Reduces interaction with
SMARCB1. {ECO:0000269|PubMed:12016208}.
MUTAGEN 556 558 VRF->ARA: Impairs PP1 activation.
{ECO:0000269|PubMed:12556489}.
MUTAGEN 612 612 R->K: Reduces PP1-binding; when
associated with K-614.
{ECO:0000269|PubMed:12556489}.
MUTAGEN 614 614 R->K: Reduces PP1-binding; when
associated with K-612.
{ECO:0000269|PubMed:12556489}.
MUTAGEN 618 618 R->D: Reduces PP1-binding.
{ECO:0000269|PubMed:12556489}.
CONFLICT 80 80 E -> G (in Ref. 3; BAA91649).
{ECO:0000305}.
CONFLICT 297 297 P -> L (in Ref. 2; CAG33540).
{ECO:0000305}.
CONFLICT 669 669 L -> P (in Ref. 3; BAG59265).
{ECO:0000305}.
STRAND 563 565 {ECO:0000244|PDB:4XPN}.
SEQUENCE 674 AA; 73478 MW; B257AA17456D1403 CRC64;
MAPGQAPHQA TPWRDAHPFF LLSPVMGLLS RAWSRLRGLG PLEPWLVEAV KGAALVEAGL
EGEARTPLAI PHTPWGRRPE EEAEDSGGPG EDRETLGLKT SSSLPEAWGL LDDDDGMYGE
REATSVPRGQ GSQFADGQRA PLSPSLLIRT LQGSDKNPGE EKAEEEGVAE EEGVNKFSYP
PSHRECCPAV EEEDDEEAVK KEAHRTSTSA LSPGSKPSTW VSCPGEEENQ ATEDKRTERS
KGARKTSVSP RSSGSDPRSW EYRSGEASEE KEEKAHKETG KGEAAPGPQS SAPAQRPQLK
SWWCQPSDEE EGEVKALGAA EKDGEAECPP CIPPPSAFLK AWVYWPGEDT EEEEDEEEDE
DSDSGSDEEE GEAEASSSTP ATGVFLKSWV YQPGEDTEEE EDEDSDTGSA EDEREAETSA
STPPASAFLK AWVYRPGEDT EEEEDEDVDS EDKEDDSEAA LGEAESDPHP SHPDQRAHFR
GWGYRPGKET EEEEAAEDWG EAEPCPFRVA IYVPGEKPPP PWAPPRLPLR LQRRLKRPET
PTHDPDPETP LKARKVRFSE KVTVHFLAVW AGPAQAARQG PWEQLARDRS RFARRITQAQ
EELSPCLTPA ARARAWARLR NPPLAPIPAL TQTLPSSSVP SSPVQTTPLS QAVATPSRSS
AAAAAALDLS GRRG


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