Q6P549 (SHIP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Inppl1
Synonyms:	Ship2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1257 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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	Cytoplasm › cytosol. Cytoplasm › cytoskeleton By similarity. Membrane; Peripheral membrane protein. Cell projection › filopodium By similarity. Cell projection › lamellipodium 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 process	Cell adhesion Immunity
Cellular component	Cell projection Cytoplasm Cytoskeleton Membrane
Domain	SH2 domain SH3-binding
Ligand	Actin-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Inferred from electronic annotation. Source: Compara brain development Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW endocytosis Inferred from electronic annotation. Source: Compara glucose metabolic process Inferred from mutant phenotype Ref.6. Source: MGI inositol trisphosphate metabolic process Inferred from electronic annotation. Source: Compara negative regulation of DNA replication Inferred from electronic annotation. Source: Compara negative regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara 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 negative regulation of insulin receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of insulin-like growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of neuron projection development Inferred from electronic annotation. Source: Compara negative regulation of platelet-derived growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara phosphatidylinositol biosynthetic process Inferred from mutant phenotype PubMed 21624956. Source: MGI phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro post-embryonic development Inferred from mutant phenotype Ref.6. Source: MGI response to drug Inferred from electronic annotation. Source: Compara response to insulin stimulus Inferred from mutant phenotype Ref.6. Source: MGI ruffle assembly Inferred from mutant phenotype PubMed 21624956. Source: MGI
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara 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_function	inositol-polyphosphate 5-phosphatase activity Inferred from electronic annotation. Source: Compara phosphatidylinositol-3,4,5-trisphosphate binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1257	1257	Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2		PRO_0000302871
Regions
	Domain	21 – 117	97	SH2
	Domain	1195 – 1257	63	SAM
	Motif	945 – 950	6	SH3-binding
	Motif	984 – 987	4	NPXY motif
	Compositional bias	936 – 1170	235	Pro-rich
Amino acid modifications
	Modified residue	165	1	Phosphothreonine By similarity
	Modified residue	241	1	Phosphoserine By similarity
	Modified residue	987	1	Phosphotyrosine By similarity
	Modified residue	1136	1	Phosphotyrosine By similarity
	Modified residue	1161	1	Phosphotyrosine By similarity
Experimental info
	Mutagenesis	47	1	R → A: Does not affect the ability to inhibit PKB activity. Ref.5
	Mutagenesis	608	1	D → A: Abolishes both enzyme activity and ability to inhibit PKB activity. Ref.5
	Mutagenesis	690	1	C → A: Induces little effect. Ref.5
	Mutagenesis	692	1	R → A: Still partially active. Ref.5
	Mutagenesis	987	1	Y → F: Does not affect the ability to inhibit PKB activity. Ref.5
	Sequence conflict	412	1	M → I in AAF28187. Ref.1
	Sequence conflict	506	1	L → I in AAF28187. Ref.1
	Sequence conflict	705	1	C → S in AAB82337. Ref.3
	Sequence conflict	972	1	G → V in AAF28187. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6P549 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: B66DF96BEF22F01E	FASTA	1,257	138,973
	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

References

	« Hide 'large scale' referencesShow '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.
+	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.
IPI	IPI00312067.
RefSeq	NP_001116211.1. NM_001122739.1. NP_034697.2. NM_010567.2.
UniGene	Mm.476000. Mm.5028.
3D structure databases
HSSP	HSSP built from PDB template 1D1Z based on UniProtKB O60880.
ProteinModelPortal	Q6P549.
SMR	Q6P549. Positions 12-128, 423-732, 1193-1257.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6P549. 2 interactions.
STRING	10090.ENSMUSP00000048057.
PTM databases
PhosphoSite	Q6P549.
Proteomic databases
PaxDb	Q6P549.
PRIDE	Q6P549.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035836; ENSMUSP00000048057; ENSMUSG00000032737. ENSMUST00000165052; ENSMUSP00000132883; ENSMUSG00000032737.
GeneID	16332.
KEGG	mmu:16332.
UCSC	uc009ipg.2. mouse.
Organism-specific databases
CTD	3636.
MGI	MGI:1333787. Inppl1.
Phylogenomic databases
eggNOG	COG5411.
GeneTree	ENSGT00700000104142.
HOGENOM	HOG000004836.
HOVERGEN	HBG106726.
InParanoid	Q6P549.
KO	K15909.
OMA	YQKHVHT.
OrthoDB	EOG4GMTW4.
Gene expression databases
Bgee	Q6P549.
CleanEx	MM_INPPL1.
Genevestigator	Q6P549.
Family and domain databases
Gene3D	1.10.150.50. 1 hit. 3.30.505.10. 1 hit.
InterPro	IPR005135. Endo/exonuclease/phosphatase. IPR000300. IPPc. IPR001660. SAM. IPR013761. SAM/pointed. IPR011510. SAM_2. IPR000980. SH2. [Graphical view]
Pfam	PF03372. Exo_endo_phos. 1 hit. PF07647. SAM_2. 1 hit. PF00017. SH2. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN.
SMART	SM00128. IPPc. 1 hit. SM00454. SAM. 1 hit. SM00252. SH2. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit. SSF47769. SAM_homology. 1 hit.
PROSITE	PS50105. SAM_DOMAIN. 1 hit. PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	INPPL1. mouse.
NextBio	289422.
SOURCE	Search...

Entry information

Entry name

SHIP2_MOUSE

Accession

Primary (citable) accession number: Q6P549
Secondary accession number(s): O08611 , Q0VDX5, Q80YB9, Q9JLL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program