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Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (AblSH3-binding protein) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)

 SHIP2_MOUSE             Reviewed;        1257 AA.
Q6P549; O08611; Q0VDX5; Q80YB9; Q9JLL7;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 116.
RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2;
EC=3.1.3.86;
AltName: Full=AblSH3-binding protein;
AltName: Full=Inositol polyphosphate phosphatase-like protein 1;
Short=INPPL-1;
AltName: Full=SH2 domain-containing inositol 5'-phosphatase 2;
Short=SH2 domain-containing inositol phosphatase 2;
Short=SHIP-2;
Name=Inppl1; Synonyms=Ship2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=10610720; DOI=10.1006/geno.1999.5995;
Schurmans S., Carrio R., Behrends J., Pouillon V., Merino J.,
Clement S.;
"The mouse SHIP2 (Inppl1) gene: complementary DNA, genomic structure,
promoter analysis, and gene expression in the embryo and adult
mouse.";
Genomics 62:260-271(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 705-1183.
PubMed=9126384; DOI=10.1006/abio.1997.2040;
Yamabhai M., Kay B.K.;
"Examining the specificity of Src homology 3 domain -- ligand
interactions with alkaline phosphatase fusion proteins.";
Anal. Biochem. 247:143-151(1997).
[4]
INTERACTION WITH FCGR2B, AND PHOSPHORYLATION.
PubMed=10789675; DOI=10.1016/S0165-2478(00)00162-0;
Muraille E., Bruhns P., Pesesse X., Daeeron M., Erneux C.;
"The SH2 domain containing inositol 5-phosphatase SHIP2 associates to
the immunoreceptor tyrosine-based inhibition motif of Fc gammaRIIB in
B cells under negative signaling.";
Immunol. Lett. 72:7-15(2000).
[5]
FUNCTION, ENZYME ACTIVITY, AND MUTAGENESIS OF ARG-47; ASP-608;
CYS-690; ARG-692 AND TYR-987.
PubMed=10958682; DOI=10.1128/MCB.20.18.6860-6871.2000;
Taylor V., Wong M., Brandts C., Reilly L., Dean N.M., Cowsert L.M.,
Moodie S., Stokoe D.;
"5' phospholipid phosphatase SHIP-2 causes protein kinase B
inactivation and cell cycle arrest in glioblastoma cells.";
Mol. Cell. Biol. 20:6860-6871(2000).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11343120; DOI=10.1038/35051094;
Clement S., Krause U., Desmedt F., Tanti J.-F., Behrends J.,
Pesesse X., Sasaki T., Penninger J., Doherty M., Malaisse W.,
Dumont J.E., Le Marchand-Brustel Y., Erneux C., Hue L., Schurmans S.;
"The lipid phosphatase SHIP2 controls insulin sensitivity.";
Nature 409:92-97(2001).
[7]
ERRATUM.
Clement S., Krause U., Desmedt F., Tanti J.-F., Behrends J.,
Pesesse X., Sasaki T., Penninger J., Doherty M., Malaisse W.,
Dumont J.E., Le Marchand-Brustel Y., Erneux C., Hue L., Schurmans S.;
Nature 431:878-878(2004).
[8]
INDUCTION.
PubMed=12145149; DOI=10.2337/diabetes.51.8.2387;
Hori H., Sasaoka T., Ishihara H., Wada T., Murakami S., Ishiki M.,
Kobayashi M.;
"Association of SH2-containing inositol phosphatase 2 with the insulin
resistance of diabetic db/db mice.";
Diabetes 51:2387-2394(2002).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14744864; DOI=10.1074/jbc.M311534200;
Sasaoka T., Wada T., Fukui K., Murakami S., Ishihara H., Suzuki R.,
Tobe K., Kadowaki T., Kobayashi M.;
"SH2-containing inositol phosphatase 2 predominantly regulates Akt2,
and not Akt1, phosphorylation at the plasma membrane in response to
insulin in 3T3-L1 adipocytes.";
J. Biol. Chem. 279:14835-14843(2004).
[10]
INTERACTION WITH FCGR2B.
PubMed=15456754; DOI=10.1074/jbc.M410261200;
Isnardi I., Lesourne R., Bruhns P., Fridman W.H., Cambier J.C.,
Daeeron M.;
"Two distinct tyrosine-based motifs enable the inhibitory receptor
FcgammaRIIB to cooperatively recruit the inositol phosphatases SHIP1/2
and the adapters Grb2/Grap.";
J. Biol. Chem. 279:51931-51938(2004).
[11]
INTERACTION WITH TEC.
PubMed=15492005; DOI=10.1074/jbc.M408141200;
Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., Weiss A.;
"SHIP family inositol phosphatases interact with and negatively
regulate the Tec tyrosine kinase.";
J. Biol. Chem. 279:55089-55096(2004).
[12]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
CSF1R.
PubMed=15557176; DOI=10.4049/jimmunol.173.11.6820;
Wang Y., Keogh R.J., Hunter M.G., Mitchell C.A., Frey R.S., Javaid K.,
Malik A.B., Schurmans S., Tridandapani S., Marsh C.B.;
"SHIP2 is recruited to the cell membrane upon macrophage colony-
stimulating factor (M-CSF) stimulation and regulates M-CSF-induced
signaling.";
J. Immunol. 173:6820-6830(2004).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15654325; DOI=10.1038/nm1178;
Sleeman M.W., Wortley K.E., Lai K.-M.V., Gowen L.C., Kintner J.,
Kline W.O., Garcia K., Stitt T.N., Yancopoulos G.D., Wiegand S.J.,
Glass D.J.;
"Absence of the lipid phosphatase SHIP2 confers resistance to dietary
obesity.";
Nat. Med. 11:199-205(2005).
[14]
FUNCTION.
PubMed=16179375; DOI=10.1182/blood-2005-05-1841;
Ai J., Maturu A., Johnson W., Wang Y., Marsh C.B., Tridandapani S.;
"The inositol phosphatase SHIP-2 down-regulates FcgammaR-mediated
phagocytosis in murine macrophages independently of SHIP-1.";
Blood 107:813-820(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[17]
INTERACTION WITH SH3YL1.
PubMed=21624956; DOI=10.1083/jcb.201012161;
Hasegawa J., Tokuda E., Tenno T., Tsujita K., Sawai H., Hiroaki H.,
Takenawa T., Itoh T.;
"SH3YL1 regulates dorsal ruffle formation by a novel phosphoinositide-
binding domain.";
J. Cell Biol. 193:901-916(2011).
-!- FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that
specifically hydrolyzes the 5-phosphate of phosphatidylinositol-
3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2,
thereby negatively regulating the PI3K (phosphoinositide 3-kinase)
pathways. Plays a central role in regulation of PI3K-dependent
insulin signaling, although the precise molecular mechanisms and
signaling pathways remain unclear. While overexpression reduces
both insulin-stimulated MAP kinase and Akt activation, its absence
does not affect insulin signaling or GLUT4 trafficking. Confers
resistance to dietary obesity. May act by regulating AKT2, but not
AKT1, phosphorylation at the plasma membrane. Part of a signaling
pathway that regulates actin cytoskeleton remodeling. Required for
the maintenance and dynamic remodeling of actin structures as well
as in endocytosis, having a major impact on ligand-induced EGFR
internalization and degradation. Participates in regulation of
cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3
thereby regulating membrane ruffling (By similarity). Regulates
cell adhesion and cell spreading. Required for HGF-mediated
lamellipodium formation, cell scattering and spreading. Acts as a
negative regulator of EPHA2 receptor endocytosis by inhibiting via
PI3K-dependent Rac1 activation. Acts as a regulator of
neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required
to form an initial protrusive pattern, and later, maintain proper
neurite outgrowth. Acts as a negative regulator of the FC-gamma-
RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB
receptor (FCGR2B), playing a central role in terminating signal
transduction from activating immune/hematopoietic cell receptor
systems. Involved in EGF signaling pathway. Upon stimulation by
EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3.
Plays a negative role in regulating the PI3K-PKB pathway, possibly
by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated
phagocytosis in macrophages independently of INPP5D/SHIP1. In
macrophages, down-regulates NF-kappa-B-dependent gene
transcription by regulating macrophage colony-stimulating factor
(M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4,
and could thus affect the levels of the higher inositol
polyphosphates like InsP6. Involved in endochondral ossification
(By similarity). {ECO:0000250|UniProtKB:O15357,
ECO:0000269|PubMed:10958682, ECO:0000269|PubMed:11343120,
ECO:0000269|PubMed:14744864, ECO:0000269|PubMed:15557176,
ECO:0000269|PubMed:15654325, ECO:0000269|PubMed:16179375}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3,4,5-
triphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 3,4-
diphosphate + phosphate. {ECO:0000269|PubMed:10958682}.
-!- ENZYME REGULATION: Activated upon translocation to the sites of
synthesis of PtdIns(3,4,5)P3 in the membrane. Enzymatic activity
is enhanced in the presence of phosphatidylserine (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with tyrosine phosphorylated form of SHC1 (By
similarity). Interacts with EGFR (By similarity). Upon stimulation
by the EGF signaling pathway, it forms a complex with SHC1 and
EGFR (By similarity). Interacts with cytoskeletal protein
SORBS3/vinexin, promoting its localization to the periphery of
cells (By similarity). Forms a complex with filamin (FLNA or
FLNB), actin, GPIb (GP1BA or GP1BB) that regulates cortical and
submembraneous actin (By similarity). Interacts with c-Met/MET,
when c-Met/MET is phosphorylated on 'Tyr-1356' (By similarity).
Interacts with p130Cas/BCAR1 (By similarity). Interacts with
CENTD3/ARAP3 via its SAM domain (By similarity). Interacts with c-
Cbl/CBL and CAP/SORBS1 (By similarity). Interacts with activated
EPHA2 receptor (By similarity). Interacts with receptors FCGR2A
(By similarity). Interacts with FCGR2B (PubMed:10789675,
PubMed:15456754). Interacts with tyrosine kinase ABL1 (By
similarity). Interacts with tyrosine kinase TEC (PubMed:15492005).
Interacts with CSF1R (PubMed:15557176). Interacts (via N-terminus)
with SH3YL1 (via SH3 domain) (PubMed:21624956).
{ECO:0000250|UniProtKB:O15357, ECO:0000269|PubMed:10789675,
ECO:0000269|PubMed:15456754, ECO:0000269|PubMed:15492005,
ECO:0000269|PubMed:15557176, ECO:0000269|PubMed:21624956}.
-!- INTERACTION:
Q9Z0R4-2:Itsn1; NbExp=2; IntAct=EBI-2642932, EBI-8052786;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton
{ECO:0000250}. Membrane; Peripheral membrane protein. Cell
projection, filopodium {ECO:0000250}. Cell projection,
lamellipodium {ECO:0000250}. Note=Translocates to membrane ruffles
when activated, translocation is probably due to different
mechanisms depending on the stimulus and cell type. Partly
translocated via its SH2 domain which mediates interaction with
tyrosine phosphorylated receptors such as the FC-gamma-RIIB
receptor (FCGR2B). Tyrosine phosphorylation may also participate
in membrane localization. Insulin specifically stimulates its
redistribution from the cytosol to the plasma membrane. Recruited
to the membrane following M-CSF stimulation. In activated
spreading platelets, localizes with actin at filopodia,
lamellipodia and the central actin ring.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10610720}.
-!- DEVELOPMENTAL STAGE: In E15.5 embryos, it is strongly expressed in
the liver, specific regions of the central nervous system, the
thymus, the lung, and the cartilage perichondrium. In adult it is
markedly present in the brain and the thymus and at different
stages of spermatozoa maturation in the seminiferous tubules.
{ECO:0000269|PubMed:10610720}.
-!- INDUCTION: Overexpressed in diabetic db/db mice.
{ECO:0000269|PubMed:12145149}.
-!- DOMAIN: The SH2 domain interacts with tyrosine phosphorylated
forms of proteins such as SHC1 or FCGR2A. It also mediates the
interaction with p130Cas/BCAR1 (By similarity). {ECO:0000250}.
-!- DOMAIN: The NPXY sequence motif found in many tyrosine-
phosphorylated proteins is required for the specific binding of
the PID domain. {ECO:0000250}.
-!- PTM: Tyrosine phosphorylated by the members of the SRC family
after exposure to a diverse array of extracellular stimuli such as
insulin, growth factors such as EGF or PDGF, chemokines, integrin
ligands and hypertonic and oxidative stress. May be phosphorylated
upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-987
following cell attachment and spreading. Phosphorylated at Tyr-
1161 following EGF signaling pathway stimulation (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice are viable, have normal glucose and
insulin levels, and normal insulin and glucose tolerance. They are
however highly resistant to weight gain when placed on a high-fat
diet, suggesting that inhibition of Inppl1 would be useful in the
effort to ameliorate diet-induced obesity. According to
preliminary results from PubMed:11343120, mice display increased
sensitivity to insulin, characterized by severe neonatal
hypoglycemia, deregulated expression of the genes involved in
gluconeogenesis, and perinatal death. They display increased
glucose tolerance and insulin sensitivity associated with an
increased recruitment of the Slc2a4/Glut4 glucose transporter and
increased glycogen synthesis in skeletal muscles. However, these
knockout mice also contain a deletion of the last exon of Phox2a
gene. It is therefore unknown whether the insulin sensitivity
observed in these mice result from inactivation of either Inppl1
or Phox2a. {ECO:0000269|PubMed:11343120,
ECO:0000269|PubMed:15654325}.
-!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
phosphatase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI19454.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF162781; AAF28187.1; -; mRNA.
EMBL; BC049961; AAH49961.1; -; mRNA.
EMBL; BC063080; AAH63080.1; -; mRNA.
EMBL; BC119453; AAI19454.1; ALT_INIT; mRNA.
EMBL; U92477; AAB82337.1; -; mRNA.
CCDS; CCDS21515.1; -.
RefSeq; NP_001116211.1; NM_001122739.1.
RefSeq; NP_034697.2; NM_010567.2.
RefSeq; XP_006507454.1; XM_006507391.3.
RefSeq; XP_011239984.1; XM_011241682.2.
RefSeq; XP_017177480.1; XM_017321991.1.
UniGene; Mm.476000; -.
ProteinModelPortal; Q6P549; -.
SMR; Q6P549; -.
BioGrid; 200770; 5.
IntAct; Q6P549; 5.
STRING; 10090.ENSMUSP00000048057; -.
ChEMBL; CHEMBL2331063; -.
iPTMnet; Q6P549; -.
PhosphoSitePlus; Q6P549; -.
EPD; Q6P549; -.
MaxQB; Q6P549; -.
PaxDb; Q6P549; -.
PeptideAtlas; Q6P549; -.
PRIDE; Q6P549; -.
Ensembl; ENSMUST00000035836; ENSMUSP00000048057; ENSMUSG00000032737.
Ensembl; ENSMUST00000165052; ENSMUSP00000132883; ENSMUSG00000032737.
GeneID; 16332; -.
KEGG; mmu:16332; -.
UCSC; uc009ipg.2; mouse.
CTD; 3636; -.
MGI; MGI:1333787; Inppl1.
eggNOG; KOG0565; Eukaryota.
eggNOG; KOG4384; Eukaryota.
eggNOG; COG5411; LUCA.
GeneTree; ENSGT00760000119075; -.
HOGENOM; HOG000004836; -.
HOVERGEN; HBG106726; -.
InParanoid; Q6P549; -.
KO; K15909; -.
OMA; VKSMDGY; -.
OrthoDB; EOG091G00P6; -.
PhylomeDB; Q6P549; -.
TreeFam; TF323475; -.
BRENDA; 3.1.3.36; 3474.
Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
ChiTaRS; Inppl1; mouse.
PRO; PR:Q6P549; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000032737; -.
CleanEx; MM_INPPL1; -.
ExpressionAtlas; Q6P549; baseline and differential.
Genevisible; Q6P549; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0007015; P:actin filament organization; ISO:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0044255; P:cellular lipid metabolic process; IMP:MGI.
GO; GO:0001958; P:endochondral ossification; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; ISO:MGI.
GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IMP:MGI.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0032868; P:response to insulin; IMP:MGI.
GO; GO:0097178; P:ruffle assembly; IMP:MGI.
Gene3D; 3.30.505.10; -; 1.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR000300; IPPc.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
Pfam; PF03372; Exo_endo_phos; 1.
Pfam; PF00536; SAM_1; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00128; IPPc; 1.
SMART; SM00454; SAM; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56219; SSF56219; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Actin-binding; Cell adhesion; Cell projection; Complete proteome;
Cytoplasm; Cytoskeleton; Hydrolase; Immunity; Membrane;
Phosphoprotein; Reference proteome; SH2 domain; SH3-binding.
CHAIN 1 1257 Phosphatidylinositol 3,4,5-trisphosphate
5-phosphatase 2.
/FTId=PRO_0000302871.
DOMAIN 21 117 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 1195 1257 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
MOTIF 945 950 SH3-binding.
MOTIF 984 987 NPXY motif.
COMPBIAS 936 1170 Pro-rich.
MOD_RES 132 132 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 165 165 Phosphothreonine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 353 353 Phosphoserine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 887 887 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 891 891 Phosphoserine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 987 987 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 1132 1132 Phosphoserine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 1136 1136 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 1161 1161 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15357}.
MOD_RES 1256 1256 Phosphoserine.
{ECO:0000250|UniProtKB:O15357}.
MUTAGEN 47 47 R->A: Does not affect the ability to
inhibit PKB activity.
{ECO:0000269|PubMed:10958682}.
MUTAGEN 608 608 D->A: Abolishes both enzyme activity and
ability to inhibit PKB activity.
{ECO:0000269|PubMed:10958682}.
MUTAGEN 690 690 C->A: Induces little effect.
{ECO:0000269|PubMed:10958682}.
MUTAGEN 692 692 R->A: Still partially active.
{ECO:0000269|PubMed:10958682}.
MUTAGEN 987 987 Y->F: Does not affect the ability to
inhibit PKB activity.
{ECO:0000269|PubMed:10958682}.
CONFLICT 412 412 M -> I (in Ref. 1; AAF28187).
{ECO:0000305}.
CONFLICT 506 506 L -> I (in Ref. 1; AAF28187).
{ECO:0000305}.
CONFLICT 705 705 C -> S (in Ref. 3; AAB82337).
{ECO:0000305}.
CONFLICT 972 972 G -> V (in Ref. 1; AAF28187).
{ECO:0000305}.
SEQUENCE 1257 AA; 138973 MW; B66DF96BEF22F01E CRC64;
MASVCGTPSP GGALGSPAPA WYHRDLSRAA AEELLARAGR DGSFLVRDSE SVAGAFALCV
LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG LYAQPNQGLV CALLLPVEGE
REPDPPDDRD ASDVEDEKPP LPPRSGSTSI SAPVGPSSPL PTPETPTTPA AESTPNGLST
VSHEYLKGSY GLDLEAVRGG ASNLPHLTRT LVTSCRRLHS EVDKVLSGLE ILSKVFDQQS
SPMVTRLLQQ QSLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPLQP
SIRKAKTIPV QAFEVKLDVT LGDLTKIGKS QKFTLSVDVE GGRLVLLRRQ RDSQEDWTTF
THDRIRQLIK SQRVQNKLGV VFEKEKDRTQ RKDFIFVSAR KREAFCQLLQ LMKNRHSKQD
EPDMISVFIG TWNMGSVPPP KNVTSWFTSK GLGKALDEVT VTIPHDIYVF GTQENSVGDR
EWLDLLRGGL KELTDLDYRP IAMQSLWNIK VAVLVKPEHE NRISHVSTSS VKTGIANTLG
NKGAVGVSFM FNGTSFGFVN CHLTSGNEKT TRRNQNYLDI LRLLSLGDRQ LSAFDISLRF
THLFWFGDLN YRLDMDIQEI LNYISRREFE PLLRVDQLNL EREKHKVFLR FSEEEISFPP
TYRYERGSRD TYAWHKQKPT GVRTNVPSWC DRILWKSYPE THIICNSYGC TDDIVTSDHS
PVFGTFEVGV TSQFISKKGL SKTSDQAYIE FESIEAIVKT ASRTKFFIEF YSTCLEEYKK
SFENDAQSSD NINFLKVQWS SRQLPTLKPI LADIEYLQDQ HLLLTVKSMD GYESYGECVV
ALKSMIGSTA QQFLTFLSHR GEETGNIRGS MKVRVPTERL GTRERLYEWI SIDKDDTGAK
SKVPSVSRGS QEHRSGSRKP ASTETSCPLS KLFEEPEKPP PTGRPPAPPR AVPREEPLNP
RLKSEGTSEQ EGVAAPPPKN SFNNPAYYVL EGVPHQLLPL EPPSLARAPL PPATKNKVAI
TVPAPQLGRH RTPRVGEGSS SDEDSGGTLP PPDFPPPPLP DSAIFLPPNL DPLSMPVVRG
RSGGEARGPP PPKAHPRPPL PPGTSPASTF LGEVASGDDR SCSVLQMAKT LSEVDYAPGP
GRSALLPNPL ELQPPRGPSD YGRPLSFPPP RIRESIQEDL AEEAPCPQGG RASGLGEAGM
GAWLRAIGLE RYEEGLVHNG WDDLEFLSDI TEEDLEEAGV QDPAHKRLLL DTLQLSK


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