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Q6P549

- SHIP2_MOUSE

UniProt

Q6P549 - SHIP2_MOUSE

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Protein

Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2

Gene

Inppl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. 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).By similarity

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3,4-diphosphate + phosphate.1 Publication

Enzyme regulationi

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).By similarity

GO - Molecular functioni

  1. hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  1. actin filament organization Source: Ensembl
  2. cell adhesion Source: UniProtKB-KW
  3. cellular lipid metabolic process Source: MGI
  4. endochondral ossification Source: UniProtKB
  5. endocytosis Source: Ensembl
  6. glucose metabolic process Source: MGI
  7. immune system process Source: UniProtKB-KW
  8. negative regulation of cell proliferation Source: MGI
  9. negative regulation of gene expression Source: MGI
  10. phosphatidylinositol biosynthetic process Source: MGI
  11. phosphatidylinositol dephosphorylation Source: InterPro
  12. post-embryonic development Source: MGI
  13. response to insulin Source: MGI
  14. ruffle assembly Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell adhesion, Immunity

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_196473. Synthesis of IP3 and IP4 in the cytosol.
REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_210793. Interleukin receptor SHC signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC:3.1.3.86)
Alternative name(s):
AblSH3-binding protein
Inositol polyphosphate phosphatase-like protein 1
Short name:
INPPL-1
SH2 domain-containing inositol 5'-phosphatase 2
Short name:
SH2 domain-containing inositol phosphatase 2
Short name:
SHIP-2
Gene namesi
Name:Inppl1
Synonyms:Ship2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1333787. Inppl1.

Subcellular locationi

Cytoplasmcytosol. Cytoplasmcytoskeleton By similarity. Membrane; Peripheral membrane protein. Cell projectionfilopodium By similarity. Cell projectionlamellipodium By similarity
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.

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cytoplasm Source: MGI
  3. cytoskeleton Source: UniProtKB-KW
  4. Golgi apparatus Source: Ensembl
  5. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471R → A: Does not affect the ability to inhibit PKB activity. 1 Publication
Mutagenesisi608 – 6081D → A: Abolishes both enzyme activity and ability to inhibit PKB activity. 1 Publication
Mutagenesisi690 – 6901C → A: Induces little effect. 1 Publication
Mutagenesisi692 – 6921R → A: Still partially active. 1 Publication
Mutagenesisi987 – 9871Y → F: Does not affect the ability to inhibit PKB activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12571257Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2PRO_0000302871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei132 – 1321Phosphoserine1 Publication
Modified residuei165 – 1651PhosphothreonineBy similarity
Modified residuei241 – 2411PhosphoserineBy similarity
Modified residuei987 – 9871PhosphotyrosineBy similarity
Modified residuei1136 – 11361PhosphotyrosineBy similarity
Modified residuei1161 – 11611PhosphotyrosineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6P549.
PaxDbiQ6P549.
PRIDEiQ6P549.

PTM databases

PhosphoSiteiQ6P549.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Developmental stagei

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.1 Publication

Inductioni

Overexpressed in diabetic db/db mice.1 Publication

Gene expression databases

BgeeiQ6P549.
CleanExiMM_INPPL1.
GenevestigatoriQ6P549.

Interactioni

Subunit structurei

Interacts with tyrosine phosphorylated form of SHC1, Interacts with EGFR. Upon stimulation by the EGF signaling pathway, it forms a complex with SHC1 and EGFR. Interacts with cytoskeletal protein SORBS3/vinexin, promoting its localization to the periphery of cells. Forms a complex with filamin (FLNA or FLNB), actin, GPIb (GP1BA or GP1BB) that regulates cortical and submembraneous actin. Interacts with c-Met/MET, when c-Met/MET is phosphorylated on 'Tyr-1356'. Interacts with p130Cas/BCAR1. Interacts with CENTD3/ARAP3 via its SAM domain. Interacts with c-Cbl/CBL and CAP/SORBS1. Interacts with activated EPHA2 receptor. Interacts with receptors FCGR2A and FCGR2B. Interacts with tyrosine kinases ABL1 and TEC. Interacts with CSF1R.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Itsn1Q9Z0R4-22EBI-2642932,EBI-8052786

Protein-protein interaction databases

BioGridi200770. 5 interactions.
IntActiQ6P549. 5 interactions.
STRINGi10090.ENSMUSP00000048057.

Structurei

3D structure databases

ProteinModelPortaliQ6P549.
SMRiQ6P549. Positions 20-147, 423-732, 1193-1257.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 11797SH2PROSITE-ProRule annotationAdd
BLAST
Domaini1195 – 125763SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi945 – 9506SH3-binding
Motifi984 – 9874NPXY motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi936 – 1170235Pro-richAdd
BLAST

Domaini

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).By similarity
The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain.By similarity

Sequence similaritiesi

Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3-binding

Phylogenomic databases

eggNOGiCOG5411.
GeneTreeiENSGT00760000119075.
HOGENOMiHOG000004836.
HOVERGENiHBG106726.
InParanoidiQ6P549.
KOiK15909.
OMAiYQKHVHT.
OrthoDBiEOG75F4CD.
PhylomeDBiQ6P549.
TreeFamiTF323475.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR000980. SH2.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF00536. SAM_1. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00128. IPPc. 1 hit.
SM00454. SAM. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6P549-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASVCGTPSP GGALGSPAPA WYHRDLSRAA AEELLARAGR DGSFLVRDSE
60 70 80 90 100
SVAGAFALCV LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG
110 120 130 140 150
LYAQPNQGLV CALLLPVEGE REPDPPDDRD ASDVEDEKPP LPPRSGSTSI
160 170 180 190 200
SAPVGPSSPL PTPETPTTPA AESTPNGLST VSHEYLKGSY GLDLEAVRGG
210 220 230 240 250
ASNLPHLTRT LVTSCRRLHS EVDKVLSGLE ILSKVFDQQS SPMVTRLLQQ
260 270 280 290 300
QSLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPLQP
310 320 330 340 350
SIRKAKTIPV QAFEVKLDVT LGDLTKIGKS QKFTLSVDVE GGRLVLLRRQ
360 370 380 390 400
RDSQEDWTTF THDRIRQLIK SQRVQNKLGV VFEKEKDRTQ RKDFIFVSAR
410 420 430 440 450
KREAFCQLLQ LMKNRHSKQD EPDMISVFIG TWNMGSVPPP KNVTSWFTSK
460 470 480 490 500
GLGKALDEVT VTIPHDIYVF GTQENSVGDR EWLDLLRGGL KELTDLDYRP
510 520 530 540 550
IAMQSLWNIK VAVLVKPEHE NRISHVSTSS VKTGIANTLG NKGAVGVSFM
560 570 580 590 600
FNGTSFGFVN CHLTSGNEKT TRRNQNYLDI LRLLSLGDRQ LSAFDISLRF
610 620 630 640 650
THLFWFGDLN YRLDMDIQEI LNYISRREFE PLLRVDQLNL EREKHKVFLR
660 670 680 690 700
FSEEEISFPP TYRYERGSRD TYAWHKQKPT GVRTNVPSWC DRILWKSYPE
710 720 730 740 750
THIICNSYGC TDDIVTSDHS PVFGTFEVGV TSQFISKKGL SKTSDQAYIE
760 770 780 790 800
FESIEAIVKT ASRTKFFIEF YSTCLEEYKK SFENDAQSSD NINFLKVQWS
810 820 830 840 850
SRQLPTLKPI LADIEYLQDQ HLLLTVKSMD GYESYGECVV ALKSMIGSTA
860 870 880 890 900
QQFLTFLSHR GEETGNIRGS MKVRVPTERL GTRERLYEWI SIDKDDTGAK
910 920 930 940 950
SKVPSVSRGS QEHRSGSRKP ASTETSCPLS KLFEEPEKPP PTGRPPAPPR
960 970 980 990 1000
AVPREEPLNP RLKSEGTSEQ EGVAAPPPKN SFNNPAYYVL EGVPHQLLPL
1010 1020 1030 1040 1050
EPPSLARAPL PPATKNKVAI TVPAPQLGRH RTPRVGEGSS SDEDSGGTLP
1060 1070 1080 1090 1100
PPDFPPPPLP DSAIFLPPNL DPLSMPVVRG RSGGEARGPP PPKAHPRPPL
1110 1120 1130 1140 1150
PPGTSPASTF LGEVASGDDR SCSVLQMAKT LSEVDYAPGP GRSALLPNPL
1160 1170 1180 1190 1200
ELQPPRGPSD YGRPLSFPPP RIRESIQEDL AEEAPCPQGG RASGLGEAGM
1210 1220 1230 1240 1250
GAWLRAIGLE RYEEGLVHNG WDDLEFLSDI TEEDLEEAGV QDPAHKRLLL

DTLQLSK
Length:1,257
Mass (Da):138,973
Last modified:July 5, 2004 - v1
Checksum:iB66DF96BEF22F01E
GO

Sequence cautioni

The sequence AAI19454.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti412 – 4121M → I in AAF28187. (PubMed:10610720)Curated
Sequence conflicti506 – 5061L → I in AAF28187. (PubMed:10610720)Curated
Sequence conflicti705 – 7051C → S in AAB82337. (PubMed:9126384)Curated
Sequence conflicti972 – 9721G → V in AAF28187. (PubMed:10610720)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF162781 mRNA. Translation: AAF28187.1.
BC049961 mRNA. Translation: AAH49961.1.
BC063080 mRNA. Translation: AAH63080.1.
BC119453 mRNA. Translation: AAI19454.1. Different initiation.
U92477 mRNA. Translation: AAB82337.1.
CCDSiCCDS21515.1.
RefSeqiNP_001116211.1. NM_001122739.1.
NP_034697.2. NM_010567.2.
XP_006507454.1. XM_006507391.1.
UniGeneiMm.476000.

Genome annotation databases

EnsembliENSMUST00000035836; ENSMUSP00000048057; ENSMUSG00000032737.
ENSMUST00000165052; ENSMUSP00000132883; ENSMUSG00000032737.
GeneIDi16332.
KEGGimmu:16332.
UCSCiuc009ipg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF162781 mRNA. Translation: AAF28187.1 .
BC049961 mRNA. Translation: AAH49961.1 .
BC063080 mRNA. Translation: AAH63080.1 .
BC119453 mRNA. Translation: AAI19454.1 . Different initiation.
U92477 mRNA. Translation: AAB82337.1 .
CCDSi CCDS21515.1.
RefSeqi NP_001116211.1. NM_001122739.1.
NP_034697.2. NM_010567.2.
XP_006507454.1. XM_006507391.1.
UniGenei Mm.476000.

3D structure databases

ProteinModelPortali Q6P549.
SMRi Q6P549. Positions 20-147, 423-732, 1193-1257.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200770. 5 interactions.
IntActi Q6P549. 5 interactions.
STRINGi 10090.ENSMUSP00000048057.

Chemistry

ChEMBLi CHEMBL2331063.

PTM databases

PhosphoSitei Q6P549.

Proteomic databases

MaxQBi Q6P549.
PaxDbi Q6P549.
PRIDEi Q6P549.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035836 ; ENSMUSP00000048057 ; ENSMUSG00000032737 .
ENSMUST00000165052 ; ENSMUSP00000132883 ; ENSMUSG00000032737 .
GeneIDi 16332.
KEGGi mmu:16332.
UCSCi uc009ipg.2. mouse.

Organism-specific databases

CTDi 3636.
MGIi MGI:1333787. Inppl1.

Phylogenomic databases

eggNOGi COG5411.
GeneTreei ENSGT00760000119075.
HOGENOMi HOG000004836.
HOVERGENi HBG106726.
InParanoidi Q6P549.
KOi K15909.
OMAi YQKHVHT.
OrthoDBi EOG75F4CD.
PhylomeDBi Q6P549.
TreeFami TF323475.

Enzyme and pathway databases

Reactomei REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
REACT_198973. Synthesis of PIPs at the plasma membrane.
REACT_210793. Interleukin receptor SHC signaling.

Miscellaneous databases

ChiTaRSi Inppl1. mouse.
NextBioi 289422.
PROi Q6P549.
SOURCEi Search...

Gene expression databases

Bgeei Q6P549.
CleanExi MM_INPPL1.
Genevestigatori Q6P549.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProi IPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR000980. SH2.
[Graphical view ]
Pfami PF03372. Exo_endo_phos. 1 hit.
PF00536. SAM_1. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
SMARTi SM00128. IPPc. 1 hit.
SM00454. SAM. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEi PS50105. SAM_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse SHIP2 (Inppl1) gene: complementary DNA, genomic structure, promoter analysis, and gene expression in the embryo and adult mouse."
    Schurmans S., Carrio R., Behrends J., Pouillon V., Merino J., Clement S.
    Genomics 62:260-271(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Kidney.
  3. "Examining the specificity of Src homology 3 domain -- ligand interactions with alkaline phosphatase fusion proteins."
    Yamabhai M., Kay B.K.
    Anal. Biochem. 247:143-151(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 705-1183.
  4. "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."
    Muraille E., Bruhns P., Pesesse X., Daeeron M., Erneux C.
    Immunol. Lett. 72:7-15(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCGR2B, PHOSPHORYLATION.
  5. "5' phospholipid phosphatase SHIP-2 causes protein kinase B inactivation and cell cycle arrest in glioblastoma cells."
    Taylor V., Wong M., Brandts C., Reilly L., Dean N.M., Cowsert L.M., Moodie S., Stokoe D.
    Mol. Cell. Biol. 20:6860-6871(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF ARG-47; ASP-608; CYS-690; ARG-692 AND TYR-987.
  6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Association of SH2-containing inositol phosphatase 2 with the insulin resistance of diabetic db/db mice."
    Hori H., Sasaoka T., Ishihara H., Wada T., Murakami S., Ishiki M., Kobayashi M.
    Diabetes 51:2387-2394(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "SH2-containing inositol phosphatase 2 predominantly regulates Akt2, and not Akt1, phosphorylation at the plasma membrane in response to insulin in 3T3-L1 adipocytes."
    Sasaoka T., Wada T., Fukui K., Murakami S., Ishihara H., Suzuki R., Tobe K., Kadowaki T., Kobayashi M.
    J. Biol. Chem. 279:14835-14843(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Two distinct tyrosine-based motifs enable the inhibitory receptor FcgammaRIIB to cooperatively recruit the inositol phosphatases SHIP1/2 and the adapters Grb2/Grap."
    Isnardi I., Lesourne R., Bruhns P., Fridman W.H., Cambier J.C., Daeeron M.
    J. Biol. Chem. 279:51931-51938(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCGR2B.
  10. "SHIP family inositol phosphatases interact with and negatively regulate the Tec tyrosine kinase."
    Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., Weiss A.
    J. Biol. Chem. 279:55089-55096(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TEC.
  11. "SHIP2 is recruited to the cell membrane upon macrophage colony-stimulating factor (M-CSF) stimulation and regulates M-CSF-induced signaling."
    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.
    J. Immunol. 173:6820-6830(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH CSF1R.
  12. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  13. "The inositol phosphatase SHIP-2 down-regulates FcgammaR-mediated phagocytosis in murine macrophages independently of SHIP-1."
    Ai J., Maturu A., Johnson W., Wang Y., Marsh C.B., Tridandapani S.
    Blood 107:813-820(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSHIP2_MOUSE
AccessioniPrimary (citable) accession number: Q6P549
Secondary accession number(s): O08611
, Q0VDX5, Q80YB9, Q9JLL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3