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Q6P549 (SHIP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Inppl1
Synonyms:Ship2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1257 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Ref.5 Ref.6 Ref.9 Ref.12 Ref.13 Ref.14

Catalytic activity

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

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.

Subunit structure

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. Ref.4 Ref.10 Ref.11 Ref.12

Subcellular location

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. Ref.9 Ref.12

Tissue specificity

Widely expressed. Ref.1

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. Ref.1

Induction

Overexpressed in diabetic db/db mice. Ref.8

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.

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

Post-translational modification

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. Ref.4 Ref.12

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 Ref.6, 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. Ref.6 Ref.13

Sequence similarities

Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.

Contains 1 SAM (sterile alpha motif) domain.

Contains 1 SH2 domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
Immunity
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
Membrane
   DomainSH2 domain
SH3-binding
   LigandActin-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cellular lipid metabolic process

Inferred from mutant phenotype Ref.13. Source: MGI

endochondral ossification

Inferred from sequence or structural similarity. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: Ensembl

glucose metabolic process

Inferred from mutant phenotype Ref.6. Source: MGI

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of cell proliferation

Inferred from direct assay PubMed 14502564. Source: MGI

negative regulation of gene expression

Inferred from mutant phenotype Ref.13. Source: MGI

phosphatidylinositol biosynthetic process

Inferred from mutant phenotype PubMed 21624956. Source: MGI

phosphatidylinositol dephosphorylation

Inferred from electronic annotation. Source: InterPro

post-embryonic development

Inferred from mutant phenotype Ref.6. Source: MGI

response to insulin

Inferred from mutant phenotype Ref.6. Source: MGI

ruffle assembly

Inferred from mutant phenotype PubMed 21624956. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 14502564. Source: MGI

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

filopodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 14502564. Source: MGI

   Molecular_functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Itsn1Q9Z0R4-22EBI-2642932,EBI-8052786

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12571257Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
PRO_0000302871

Regions

Domain21 – 11797SH2
Domain1195 – 125763SAM
Motif945 – 9506SH3-binding
Motif984 – 9874NPXY motif
Compositional bias936 – 1170235Pro-rich

Amino acid modifications

Modified residue1321Phosphoserine Ref.15
Modified residue1651Phosphothreonine By similarity
Modified residue2411Phosphoserine By similarity
Modified residue9871Phosphotyrosine By similarity
Modified residue11361Phosphotyrosine By similarity
Modified residue11611Phosphotyrosine By similarity

Experimental info

Mutagenesis471R → A: Does not affect the ability to inhibit PKB activity. Ref.5
Mutagenesis6081D → A: Abolishes both enzyme activity and ability to inhibit PKB activity. Ref.5
Mutagenesis6901C → A: Induces little effect. Ref.5
Mutagenesis6921R → A: Still partially active. Ref.5
Mutagenesis9871Y → F: Does not affect the ability to inhibit PKB activity. Ref.5
Sequence conflict4121M → I in AAF28187. Ref.1
Sequence conflict5061L → I in AAF28187. Ref.1
Sequence conflict7051C → S in AAB82337. Ref.3
Sequence conflict9721G → V in AAF28187. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6P549 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B66DF96BEF22F01E

FASTA1,257138,973
        10         20         30         40         50         60 
MASVCGTPSP GGALGSPAPA WYHRDLSRAA AEELLARAGR DGSFLVRDSE SVAGAFALCV 

        70         80         90        100        110        120 
LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG LYAQPNQGLV CALLLPVEGE 

       130        140        150        160        170        180 
REPDPPDDRD ASDVEDEKPP LPPRSGSTSI SAPVGPSSPL PTPETPTTPA AESTPNGLST 

       190        200        210        220        230        240 
VSHEYLKGSY GLDLEAVRGG ASNLPHLTRT LVTSCRRLHS EVDKVLSGLE ILSKVFDQQS 

       250        260        270        280        290        300 
SPMVTRLLQQ QSLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPLQP 

       310        320        330        340        350        360 
SIRKAKTIPV QAFEVKLDVT LGDLTKIGKS QKFTLSVDVE GGRLVLLRRQ RDSQEDWTTF 

       370        380        390        400        410        420 
THDRIRQLIK SQRVQNKLGV VFEKEKDRTQ RKDFIFVSAR KREAFCQLLQ LMKNRHSKQD 

       430        440        450        460        470        480 
EPDMISVFIG TWNMGSVPPP KNVTSWFTSK GLGKALDEVT VTIPHDIYVF GTQENSVGDR 

       490        500        510        520        530        540 
EWLDLLRGGL KELTDLDYRP IAMQSLWNIK VAVLVKPEHE NRISHVSTSS VKTGIANTLG 

       550        560        570        580        590        600 
NKGAVGVSFM FNGTSFGFVN CHLTSGNEKT TRRNQNYLDI LRLLSLGDRQ LSAFDISLRF 

       610        620        630        640        650        660 
THLFWFGDLN YRLDMDIQEI LNYISRREFE PLLRVDQLNL EREKHKVFLR FSEEEISFPP 

       670        680        690        700        710        720 
TYRYERGSRD TYAWHKQKPT GVRTNVPSWC DRILWKSYPE THIICNSYGC TDDIVTSDHS 

       730        740        750        760        770        780 
PVFGTFEVGV TSQFISKKGL SKTSDQAYIE FESIEAIVKT ASRTKFFIEF YSTCLEEYKK 

       790        800        810        820        830        840 
SFENDAQSSD NINFLKVQWS SRQLPTLKPI LADIEYLQDQ HLLLTVKSMD GYESYGECVV 

       850        860        870        880        890        900 
ALKSMIGSTA QQFLTFLSHR GEETGNIRGS MKVRVPTERL GTRERLYEWI SIDKDDTGAK 

       910        920        930        940        950        960 
SKVPSVSRGS QEHRSGSRKP ASTETSCPLS KLFEEPEKPP PTGRPPAPPR AVPREEPLNP 

       970        980        990       1000       1010       1020 
RLKSEGTSEQ EGVAAPPPKN SFNNPAYYVL EGVPHQLLPL EPPSLARAPL PPATKNKVAI 

      1030       1040       1050       1060       1070       1080 
TVPAPQLGRH RTPRVGEGSS SDEDSGGTLP PPDFPPPPLP DSAIFLPPNL DPLSMPVVRG 

      1090       1100       1110       1120       1130       1140 
RSGGEARGPP PPKAHPRPPL PPGTSPASTF LGEVASGDDR SCSVLQMAKT LSEVDYAPGP 

      1150       1160       1170       1180       1190       1200 
GRSALLPNPL ELQPPRGPSD YGRPLSFPPP RIRESIQEDL AEEAPCPQGG RASGLGEAGM 

      1210       1220       1230       1240       1250 
GAWLRAIGLE RYEEGLVHNG WDDLEFLSDI TEEDLEEAGV QDPAHKRLLL DTLQLSK 

« Hide

References

« Hide 'large scale' references
[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]"The lipid phosphatase SHIP2 controls insulin sensitivity."
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 409:92-97(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[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]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"Absence of the lipid phosphatase SHIP2 confers resistance to dietary obesity."
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.
Nat. Med. 11:199-205(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[14]"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.
[15]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001116211.1. NM_001122739.1.
NP_034697.2. NM_010567.2.
XP_006507454.1. XM_006507391.1.
UniGeneMm.476000.

3D structure databases

ProteinModelPortalQ6P549.
SMRQ6P549. Positions 12-147, 423-732, 1193-1257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200770. 5 interactions.
IntActQ6P549. 5 interactions.
STRING10090.ENSMUSP00000048057.

Chemistry

ChEMBLCHEMBL2331063.

PTM databases

PhosphoSiteQ6P549.

Proteomic databases

PaxDbQ6P549.
PRIDEQ6P549.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035836; ENSMUSP00000048057; ENSMUSG00000032737.
ENSMUST00000165052; ENSMUSP00000132883; ENSMUSG00000032737.
GeneID16332.
KEGGmmu:16332.
UCSCuc009ipg.2. mouse.

Organism-specific databases

CTD3636.
MGIMGI:1333787. Inppl1.

Phylogenomic databases

eggNOGCOG5411.
GeneTreeENSGT00750000117420.
HOGENOMHOG000004836.
HOVERGENHBG106726.
InParanoidQ6P549.
KOK15909.
OMAYQKHVHT.
OrthoDBEOG75F4CD.
PhylomeDBQ6P549.
TreeFamTF323475.

Gene expression databases

BgeeQ6P549.
CleanExMM_INPPL1.
GenevestigatorQ6P549.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR000980. SH2.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
PF00536. SAM_1. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
SMARTSM00128. IPPc. 1 hit.
SM00454. SAM. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEPS50105. SAM_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSINPPL1. mouse.
NextBio289422.
PROQ6P549.
SOURCESearch...

Entry information

Entry nameSHIP2_MOUSE
AccessionPrimary (citable) accession number: Q6P549
Secondary accession number(s): O08611 expand/collapse secondary AC list , Q0VDX5, Q80YB9, Q9JLL7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot