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Protein Page:
SHIP-2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
SHIP-2 an SH2-containing inositol phosphatase. Recruited to activated receptor complexes including insulin R, PDGFR and Fc-gamma-R. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.3.n1; Carbohydrate Metabolism - inositol phosphate; EC 3.1.3.86; Phosphatase, lipid; Motility/polarity/chemotaxis
Cellular Component: cytoskeleton; lamellipodium; plasma membrane; cytosol; filopodium
Molecular Function: protein binding; hydrolase activity; SH2 domain binding; actin binding; SH3 domain binding
Biological Process: inositol phosphate metabolic process; immune system process; glucose metabolic process; actin filament organization; endocytosis; response to insulin stimulus; post-embryonic development; negative regulation of cell proliferation; phospholipid metabolic process; phosphatidylinositol biosynthetic process; phosphoinositide dephosphorylation; cell adhesion; endochondral ossification
Reference #:  O15357 (UniProtKB)
Alt. Names/Synonyms: 51C protein; inositol polyphosphate phosphatase-like 1; Inositol polyphosphate phosphatase-like protein 1; INPPL-1; INPPL1; Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2; Protein 51C; SH2 domain-containing inositol phosphatase 2; SH2 domain-containing inositol-5'-phosphatase 2; SHIP-2; SHIP2
Gene Symbols: INPPL1
Molecular weight: 138,599 Da
Basal Isoelectric point: 6.1  Predict pI for various phosphorylation states
CST Pathways:  B Cell Receptor Signaling  |  Insulin Receptor Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SHIP-2

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
intracellular localization: S132‑p
phosphorylation: T958‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
2 10 S132-p PPDDRDAsDGEDEKP
0 1 S158-p SAPTGPSsPLPAPEt
0 1 T165-p sPLPAPEtPtAPAAE
0 1 T167-p LPAPEtPtAPAAESA
0 2 S189-p SHDYLKGsyGLDLEA
0 18 Y190-p HDYLKGsyGLDLEAV
0 1 K224-u RLHSEVDkVLSGLEI
0 1 K234-u SGLEILSkVFDQQSs
0 4 S241-p kVFDQQSsPMVTRLL
0 1 T306 PSTRKAKTIPVQAFE
1 0 K315-u PVQAFEVkLDVTLGD
0 2 K331-u TKIGKSQkFTLSVDV
0 1 S352-p LLRRQRDsQEDWTTF
0 1 K412-u CQLLQLMkNKHSKQD
0 46 Y622-p DIQEILNyISRKEFE
0 9 Y661-p EISFPPTyRyERGSR
0 13 Y663-p SFPPTyRyERGSRDT
0 108 Y671-p ERGSRDTyAWHKQKP
0 3 S827-p HLLLTVKsMDGyESY
0 138 Y831-p TVKsMDGyESYGECV
0 12 T881-p VPTERLGtRERLyEW
0 518 Y886-p LGtRERLyEWIsIDK
0 4 S890-p ERLyEWIsIDKDEAG
1 3 T958-p APREEPLtPRLKPEG
0 1 P963 PLtPRLKPEGAPEPE
0 78 S980-p AAPPPKNsFNNPAyy
2 930 Y986-p NsFNNPAyyVLEGVP
1 218 Y987-p sFNNPAyyVLEGVPH
0 150 S1003-p LLPPEPPsPARAPVP
0 25 S1011-p PARAPVPsAtKNKVA
0 18 T1013-p RAPVPsAtKNKVAIT
1 3 S1104-p PPLPPGPsPASTFLG
0 12 S1131-p LQMAKTLsEVDyAPA
0 704 Y1135-p KTLsEVDyAPAGPAR
0 26 S1160-p QPPRGLPsDyGRPLs
0 342 Y1162-p PRGLPsDyGRPLsFP
0 9 S1167-p sDyGRPLsFPPPRIR
0 1 S1176-p PPPRIREsIQEDLAE
0 7 Y1213-p RAIGLERyEEGLVHN
1 0 T1253-p HKRLLLDtLQLsK__
1 1 S1257-p LLDtLQLsK______
2008 : Phospho-SHIP2 (Tyr986/987) Antibody
2008 : Phospho-SHIP2 (Tyr986/987) Antibody
2007 : Phospho-SHIP2 (Tyr1135) Antibody
5445 : Phospho-SHIP2 (Tyr1135) (D33C6) XP(R) Rabbit mAb
  mouse

 
S132-p PPDDRDAsDVEDEKP
S158-p SAPVGPSsPLPTPET
T165 sPLPTPETPTTPAAE
T167 LPTPETPTTPAAEST
S189 SHEYLKGSYGLDLEA
Y190 HEYLKGSYGLDLEAV
K224 RLHSEVDKVLSGLEI
K234 SGLEILSKVFDQQSs
S241-p KVFDQQSsPMVTRLL
T307-p PSIRKAKtIPVQAFE
K316 PVQAFEVKLDVTLGD
K332-u TKIGKSQkFTLSVDV
S353 LLRRQRDSQEDWTTF
K413 CQLLQLMKNRHSKQD
Y623 DIQEILNYISRREFE
Y662-p EISFPPTyRYERGSR
Y664 SFPPTyRYERGSRDT
Y672-p ERGSRDTyAWHKQKP
S828 HLLLTVKSMDGYESY
Y832 TVKSMDGYESYGECV
T882 VPTERLGTRERLyEW
Y887-p LGTRERLyEWISIDK
S891 ERLyEWISIDKDDTG
N959 VPREEPLNPRLKsEG
S964-p PLNPRLKsEGTSEQE
S981 AAPPPKNSFNNPAyy
Y987-p NSFNNPAyyVLEGVP
Y988-p SFNNPAyyVLEGVPH
S1004 LLPLEPPSLARAPLP
P1012 LARAPLPPATKNKVA
T1014 RAPLPPATKNKVAIT
S1105 PPLPPGTSPASTFLG
S1132-p LQMAKTLsEVDyAPG
Y1136-p KTLsEVDyAPGPGRS
S1159 LQPPRGPSDyGRPLS
Y1161-p PPRGPSDyGRPLSFP
S1166 SDyGRPLSFPPPRIR
S1175 PPPRIRESIQEDLAE
Y1212 RAIGLERYEEGLVHN
T1252 HKRLLLDTLQLSK__
S1256 LLDTLQLSK______
2008 : Phospho-SHIP2 (Tyr986/987) Antibody
2008 : Phospho-SHIP2 (Tyr986/987) Antibody
  rat

 
S132-p PPDDRDAsDVEDEKP
S158 SVPAGPSSPLPAPET
T165 SPLPAPETPTTPAAE
T167 LPAPETPTTPAAEST
S189 SHEYLKGSYGLDLEA
Y190 HEYLKGSYGLDLEAV
K224 RLHSEVDKVLSGLEI
K234 SGLEILSKVFDQQSS
S241 KVFDQQSSPMVTRLL
T307 PSIRKAKTIPVQAFE
K316 PVQAFEVKLDVTLGD
K332 TKIGKSQKFTLSVDV
S353 LLRRQRDSQEDWTTF
K413 CQLLQLMKNKHSKQD
Y623 DIQEILNYISRREFE
Y662 EISFPPTYRYERGSR
Y664 SFPPTYRYERGSRDT
Y672 ERGSRDTYAWHKQKP
S828 HLLLTVKSMDGYESY
Y832 TVKSMDGYESYGECV
T882 VPTERLGTRERLYEW
Y887 LGTRERLYEWISIDK
S891 ERLYEWISIDKDDTG
N959 VPREESLNPRLKSEG
S964 SLNPRLKSEGTPEQE
S981 AAPPPKNSFNNPAyy
Y987-p NSFNNPAyyVLEGVP
Y988-p SFNNPAyyVLEGVPH
S1004 LLPLEPTSFARAPIP
P1012 FARAPIPPTTKNKVA
T1014 RAPIPPTTKNKVAIT
S1105 PPLPPGTSPASTFLE
S1132 LQMAKTLSEVDySPG
Y1136-p KTLSEVDySPGPGRS
S1159 LQLPRGPSDYGRPLS
Y1161 LPRGPSDYGRPLSFP
S1166 SDYGRPLSFPPPRIR
S1175 PPPRIRESIQEDLAE
Y1212 RAIGLERYEEGLVHN
T1252 HKRLLLDTLQLSK__
S1256 LLDTLQLSK______
2008 : Phospho-SHIP2 (Tyr986/987) Antibody
2008 : Phospho-SHIP2 (Tyr986/987) Antibody
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