SHIP2_HUMAN - dbPTM
SHIP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHIP2_HUMAN
UniProt AC O15357
Protein Name Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
Gene Name INPPL1
Organism Homo sapiens (Human).
Sequence Length 1258
Subcellular Localization Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Membrane
Peripheral membrane protein. Cell projection, filopodium. Cell projection, lamellipodium. Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms de
Protein Description 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. [PubMed: 21624956 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.]
Protein Sequence MASACGAPGPGGALGSQAPSWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCVLYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEGEREPDPPDDRDASDGEDEKPPLPPRSGSTSISAPTGPSSPLPAPETPTAPAAESAPNGLSTVSHDYLKGSYGLDLEAVRGGASHLPHLTRTLATSCRRLHSEVDKVLSGLEILSKVFDQQSSPMVTRLLQQQNLPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPQPSTRKAKTIPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFTHDRIRQLIKSQRVQNKLGVVFEKEKDRTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDEPDMISVFIGTWNMGSVPPPKNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDREWLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLNAFDISLRFTHLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPTYRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSYPETHIICNSYGCTDDIVTSDHSPVFGTFEVGVTSQFISKKGLSKTSDQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKSFENDAQSSDNINFLKVQWSSRQLPTLKPILADIEYLQDQHLLLTVKSMDGYESYGECVVALKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKSKAPSVSRGSQEPRSGSRKPAFTEASCPLSRLFEEPEKPPPTGRPPAPPRAAPREEPLTPRLKPEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPSATKNKVAITVPAPQLGHHRHPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSLDPLPGPVVRGRGGAEARGPPPPKAHPRPPLPPGPSPASTFLGEVASGDDRSCSVLQMAKTLSEVDYAPAGPARSALLPGPLELQPPRGLPSDYGRPLSFPPPRIRESIQEDLAEEAPCLQGGRASGLGEAGMSAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
43PhosphorylationARAGRDGSFLVRDSE
HHCCCCCCEEECCCC		21.5020873877
49PhosphorylationGSFLVRDSESVAGAF
CCEEECCCCCHHHHH		22.6229083192
51PhosphorylationFLVRDSESVAGAFAL
EEECCCCCHHHHHHH		22.6329083192
62PhosphorylationAFALCVLYQKHVHTY
HHHHHHHHHCCEEEE		8.6329083192
132PhosphorylationPPDDRDASDGEDEKP
CCCCCCCCCCCCCCC		50.9023401153
145PhosphorylationKPPLPPRSGSTSISA
CCCCCCCCCCCCCCC		42.7523663014
147PhosphorylationPLPPRSGSTSISAPT
CCCCCCCCCCCCCCC		21.8923663014
148PhosphorylationLPPRSGSTSISAPTG
CCCCCCCCCCCCCCC		33.3423663014
149PhosphorylationPPRSGSTSISAPTGP
CCCCCCCCCCCCCCC		19.0828450419
151PhosphorylationRSGSTSISAPTGPSS
CCCCCCCCCCCCCCC		28.1523663014
154PhosphorylationSTSISAPTGPSSPLP
CCCCCCCCCCCCCCC		62.5323663014
157PhosphorylationISAPTGPSSPLPAPE
CCCCCCCCCCCCCCC		46.0323663014
158PhosphorylationSAPTGPSSPLPAPET
CCCCCCCCCCCCCCC		33.3225159151
165PhosphorylationSPLPAPETPTAPAAE
CCCCCCCCCCCCCHH		25.5328348404
167PhosphorylationLPAPETPTAPAAESA
CCCCCCCCCCCHHCC		53.3328450419
170 (in isoform 2)Ubiquitination-22.7721906983
173PhosphorylationPTAPAAESAPNGLST
CCCCCHHCCCCCCCC		44.2828270605
179PhosphorylationESAPNGLSTVSHDYL
HCCCCCCCCCCHHHH		28.3223186163
180PhosphorylationSAPNGLSTVSHDYLK
CCCCCCCCCCHHHHC		30.9423186163
182PhosphorylationPNGLSTVSHDYLKGS
CCCCCCCCHHHHCCC		15.6623312004
185PhosphorylationLSTVSHDYLKGSYGL
CCCCCHHHHCCCCCC		12.6123312004
189PhosphorylationSHDYLKGSYGLDLEA
CHHHHCCCCCCCHHH		17.91-
190PhosphorylationHDYLKGSYGLDLEAV
HHHHCCCCCCCHHHH		30.3122817900
198MethylationGLDLEAVRGGASHLP
CCCHHHHCCCHHCHH		44.89115916913
224UbiquitinationRLHSEVDKVLSGLEI
HHHHHHHHHHHHHHH		50.6921890473
224 (in isoform 1)Ubiquitination-50.6921890473
227PhosphorylationSEVDKVLSGLEILSK
HHHHHHHHHHHHHHH		44.3025867546
233PhosphorylationLSGLEILSKVFDQQS
HHHHHHHHHHHCCCC		32.2225867546
234UbiquitinationSGLEILSKVFDQQSS
HHHHHHHHHHCCCCC		43.4023000965
234 (in isoform 1)Ubiquitination-43.4021890473
236UbiquitinationLEILSKVFDQQSSPM
HHHHHHHHCCCCCHH		8.9021890473
240PhosphorylationSKVFDQQSSPMVTRL
HHHHCCCCCHHHHHH		30.6729255136
241PhosphorylationKVFDQQSSPMVTRLL
HHHCCCCCHHHHHHH		16.8123401153
245PhosphorylationQQSSPMVTRLLQQQN
CCCCHHHHHHHHHCC		14.8929255136
246UbiquitinationQSSPMVTRLLQQQNL
CCCHHHHHHHHHCCC		23.2221890473
256UbiquitinationQQQNLPQTGEQELES
HHCCCCCCCHHHHHH		40.5221890473
267UbiquitinationELESLVLKLSVLKDF
HHHHHHHHHHHHHHH		31.10-
272AcetylationVLKLSVLKDFLSGIQ
HHHHHHHHHHHHHHH		44.2519824147
276O-linked_GlycosylationSVLKDFLSGIQKKAL
HHHHHHHHHHHHHHH		33.5730379171
284UbiquitinationGIQKKALKALQDMSS
HHHHHHHHHHHHHHC		52.4929967540
289SulfoxidationALKALQDMSSTAPPA
HHHHHHHHHCCCCCC		1.8928183972
290PhosphorylationLKALQDMSSTAPPAP
HHHHHHHHCCCCCCC		32.5920068231
291PhosphorylationKALQDMSSTAPPAPQ
HHHHHHHCCCCCCCC		23.1920068231
292PhosphorylationALQDMSSTAPPAPQP
HHHHHHCCCCCCCCC		35.5620068231
300PhosphorylationAPPAPQPSTRKAKTI
CCCCCCCCCCCCCCC		35.2820068231
301PhosphorylationPPAPQPSTRKAKTIP
CCCCCCCCCCCCCCC		42.7629978859
306PhosphorylationPSTRKAKTIPVQAFE
CCCCCCCCCCEEEEE		35.0624719451
315UbiquitinationPVQAFEVKLDVTLGD
CEEEEEEEEEEEHHH		31.6022817900
319PhosphorylationFEVKLDVTLGDLTKI
EEEEEEEEHHHHEEE		25.3723403867
324PhosphorylationDVTLGDLTKIGKSQK
EEEHHHHEEECCCCC		25.9223403867
327UbiquitinationLGDLTKIGKSQKFTL
HHHHEEECCCCCEEE		25.7222817900
328UbiquitinationGDLTKIGKSQKFTLS
HHHEEECCCCCEEEE		53.8622817900
329PhosphorylationDLTKIGKSQKFTLSV
HHEEECCCCCEEEEE		33.1323403867
331UbiquitinationTKIGKSQKFTLSVDV
EEECCCCCEEEEEEE		47.6222053931
331UbiquitinationTKIGKSQKFTLSVDV
EEECCCCCEEEEEEE		47.6222053931
337UbiquitinationQKFTLSVDVEGGRLV
CCEEEEEEEECCEEE		29.4022817900
340UbiquitinationTLSVDVEGGRLVLLR
EEEEEEECCEEEEEE		26.7722817900
343UbiquitinationVDVEGGRLVLLRRQR
EEEECCEEEEEEECC		3.4422053931
350UbiquitinationLVLLRRQRDSQEDWT
EEEEEECCCCCCCCC		43.6822817900
352PhosphorylationLLRRQRDSQEDWTTF
EEEECCCCCCCCCCC		37.3423917254
353UbiquitinationLRRQRDSQEDWTTFT
EEECCCCCCCCCCCC		57.8922053931
376UbiquitinationKSQRVQNKLGVVFEK
HHHHHHHHHCCEEEE		29.5323000965
383MalonylationKLGVVFEKEKDRTQR
HHCCEEEECCCCCCC		59.6126320211
388UbiquitinationFEKEKDRTQRKDFIF
EEECCCCCCCCCEEE		42.7423000965
391MalonylationEKDRTQRKDFIFVSA
CCCCCCCCCEEEEEH		47.3626320211
398UbiquitinationKDFIFVSARKREAFC
CCEEEEEHHHHHHHH		18.7323000965
412UbiquitinationCQLLQLMKNKHSKQD
HHHHHHHHCCCCCCC		72.0122817900
412 (in isoform 1)Ubiquitination-72.0121890473
414UbiquitinationLLQLMKNKHSKQDEP
HHHHHHCCCCCCCCC		43.6822817900
417UbiquitinationLMKNKHSKQDEPDMI
HHHCCCCCCCCCCCE		62.5822817900
424UbiquitinationKQDEPDMISVFIGTW
CCCCCCCEEEEEEEC		4.0722817900
426UbiquitinationDEPDMISVFIGTWNM
CCCCCEEEEEEECCC		2.5422817900
429UbiquitinationDMISVFIGTWNMGSV
CCEEEEEEECCCCCC		17.1422817900
434UbiquitinationFIGTWNMGSVPPPKN
EEEECCCCCCCCCCC		23.4422817900
436UbiquitinationGTWNMGSVPPPKNVT
EECCCCCCCCCCCCC		7.3622817900
439UbiquitinationNMGSVPPPKNVTSWF
CCCCCCCCCCCCHHH		34.4822817900
531UbiquitinationHVSTSSVKTGIANTL
EECHHHCHHCCCCCC		42.8729967540
537PhosphorylationVKTGIANTLGNKGAV
CHHCCCCCCCCCCCE		27.3330108239
547PhosphorylationNKGAVGVSFMFNGTS
CCCCEEEEEEECCEE		12.6921601212
622PhosphorylationDIQEILNYISRKEFE
CHHHHHHHHCHHHCH		9.2323917254
661PhosphorylationEISFPPTYRYERGSR
HHCCCCCCCCCCCCC		19.5722817900
663PhosphorylationSFPPTYRYERGSRDT
CCCCCCCCCCCCCCC		10.2820090780
671PhosphorylationERGSRDTYAWHKQKP
CCCCCCCCCCCCCCC		16.3912522270
741UbiquitinationISKKGLSKTSDQAYI
HCCCCCCCCCCCEEE		58.03-
742PhosphorylationSKKGLSKTSDQAYIE
CCCCCCCCCCCEEEE		33.8729759185
743PhosphorylationKKGLSKTSDQAYIEF
CCCCCCCCCCEEEEE		31.3129759185
747PhosphorylationSKTSDQAYIEFESIE
CCCCCCEEEEEEHHH		8.7129759185
752PhosphorylationQAYIEFESIEAIVKT
CEEEEEEHHHHHHHH		30.9329759185
778UbiquitinationSTCLEEYKKSFENDA
HHHHHHHHHHHCCCC		45.2623000965
779UbiquitinationTCLEEYKKSFENDAQ
HHHHHHHHHHCCCCC		60.5223000965
790UbiquitinationNDAQSSDNINFLKVQ
CCCCCCCCCCEEEEE		32.8123000965
791UbiquitinationDAQSSDNINFLKVQW
CCCCCCCCCEEEEEE		4.6523000965
800UbiquitinationFLKVQWSSRQLPTLK
EEEEEECCCCCCCCH		22.5323000965
801UbiquitinationLKVQWSSRQLPTLKP
EEEEECCCCCCCCHH		36.2223000965
827PhosphorylationHLLLTVKSMDGYESY
EEEEEEECCCCCCHH		20.12-
831PhosphorylationTVKSMDGYESYGECV
EEECCCCCCHHHHHH		9.4621447384
833PhosphorylationKSMDGYESYGECVVA
ECCCCCCHHHHHHHH		29.92-
854PhosphorylationSTAQQFLTFLSHRGE
HHHHHHHHHHHHCCC		24.66-
857PhosphorylationQQFLTFLSHRGEETG
HHHHHHHHHCCCCCC		13.62-
881PhosphorylationVPTERLGTRERLYEW
CCCCCCCCHHHHHHH		33.67-
886PhosphorylationLGTRERLYEWISIDK
CCCHHHHHHHEECCC		18.5527273156
890PhosphorylationERLYEWISIDKDEAG
HHHHHHEECCCCCCC		26.3022617229
904PhosphorylationGAKSKAPSVSRGSQE
CCCCCCCCCCCCCCC		37.2723403867
906PhosphorylationKSKAPSVSRGSQEPR
CCCCCCCCCCCCCCC		34.9521601212
909PhosphorylationAPSVSRGSQEPRSGS
CCCCCCCCCCCCCCC		30.2022468782
914PhosphorylationRGSQEPRSGSRKPAF
CCCCCCCCCCCCCCH		52.4123403867
916PhosphorylationSQEPRSGSRKPAFTE
CCCCCCCCCCCCHHH		38.0830576142
918MalonylationEPRSGSRKPAFTEAS
CCCCCCCCCCHHHCC		42.2526320211
922PhosphorylationGSRKPAFTEASCPLS
CCCCCCHHHCCCCHH		32.5223312004
958PhosphorylationAPREEPLTPRLKPEG
CCCCCCCCCCCCCCC		19.6517219406
980PhosphorylationAAPPPKNSFNNPAYY
CCCCCCCCCCCCCEE		35.1621945579
986PhosphorylationNSFNNPAYYVLEGVP
CCCCCCCEEEECCCC		8.7222167270
987PhosphorylationSFNNPAYYVLEGVPH
CCCCCCEEEECCCCH		10.7221945579
1003PhosphorylationLLPPEPPSPARAPVP
CCCCCCCCCCCCCCC		41.7422167270
1011PhosphorylationPARAPVPSATKNKVA
CCCCCCCCCCCCCEE		49.1328450419
1013PhosphorylationRAPVPSATKNKVAIT
CCCCCCCCCCCEEEE		39.2128450419
1038PhosphorylationHPRVGEGSSSDEESG
CCCCCCCCCCCCCCC		23.5120068231
1039PhosphorylationPRVGEGSSSDEESGG
CCCCCCCCCCCCCCC		53.3020068231
1040PhosphorylationRVGEGSSSDEESGGT
CCCCCCCCCCCCCCC		51.2220873877
1044PhosphorylationGSSSDEESGGTLPPP
CCCCCCCCCCCCCCC		40.2420068231
1047PhosphorylationSDEESGGTLPPPDFP
CCCCCCCCCCCCCCC		39.3520068231
1061PhosphorylationPPPPLPDSAIFLPPS
CCCCCCCCCEECCCC		22.7120873877
1068PhosphorylationSAIFLPPSLDPLPGP
CCEECCCCCCCCCCC		43.3920068231
1080MethylationPGPVVRGRGGAEARG
CCCCCCCCCCCCCCC		29.7997770751
1086MethylationGRGGAEARGPPPPKA
CCCCCCCCCCCCCCC		50.05115916905
1096MethylationPPPKAHPRPPLPPGP
CCCCCCCCCCCCCCC		35.28115916909
1104PhosphorylationPPLPPGPSPASTFLG
CCCCCCCCCCHHHHH		38.7312522270
1129PhosphorylationSVLQMAKTLSEVDYA
HHHHHHHCHHHCCCC		26.4421945579
1131PhosphorylationLQMAKTLSEVDYAPA
HHHHHCHHHCCCCCC		40.5821945579
1135PhosphorylationKTLSEVDYAPAGPAR
HCHHHCCCCCCCCCC		21.4721945579
1142MethylationYAPAGPARSALLPGP
CCCCCCCCCCCCCCC		26.1230761017
1160PhosphorylationQPPRGLPSDYGRPLS
CCCCCCCCCCCCCCC		48.8121945579
1162PhosphorylationPRGLPSDYGRPLSFP
CCCCCCCCCCCCCCC		21.2621945579
1167PhosphorylationSDYGRPLSFPPPRIR
CCCCCCCCCCCHHHH		38.0921945579
1176PhosphorylationPPPRIRESIQEDLAE
CCHHHHHHHHHHHHH		21.5226657352
1194PhosphorylationCLQGGRASGLGEAGM
CCCCCCCCCCHHHHH		32.9428555341
1202PhosphorylationGLGEAGMSAWLRAIG
CCHHHHHHHHHHHHC		18.51-
1213PhosphorylationRAIGLERYEEGLVHN
HHHCCHHHHCCCCCC		14.68-
1253PhosphorylationHKRLLLDTLQLSK--
HHHHHHHHHHCCC--		19.1721770892
1257PhosphorylationLLDTLQLSK------
HHHHHHCCC------		24.2925159151
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
986YPhosphorylationKinaseSRCP12931
Uniprot
986YPhosphorylationKinaseSRC64-PhosphoELM
987YPhosphorylationKinaseSRCP12931
GPS
987YPhosphorylationKinaseSRC64-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
958TPhosphorylation

17219406
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SHIP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRBS1_HUMANSORBS1physical
12504111
BCAR1_HUMANBCAR1physical
11158326
FLNC_HUMANFLNCphysical
11739414
SHC1_HUMANSHC1physical
9660833
CBL_HUMANCBLphysical
15668240
CBL_HUMANCBLphysical
19880507
EGFR_HUMANEGFRphysical
19713535
MET_HUMANMETphysical
19713535
IQGA1_HUMANIQGAP1physical
19380743
K1C10_HUMANKRT10physical
19380743
K2C1_HUMANKRT1physical
19380743
K22E_HUMANKRT2physical
19380743
HSP7C_HUMANHSPA8physical
19380743
K2C5_HUMANKRT5physical
19380743
K2C6C_HUMANKRT6Cphysical
19380743
K2C6B_HUMANKRT6Bphysical
19380743
TBB5_HUMANTUBBphysical
19380743
K1C9_HUMANKRT9physical
19380743
K1C14_HUMANKRT14physical
19380743
ACACA_HUMANACACAphysical
19380743
TBB4B_HUMANTUBB4Bphysical
19380743
K1C16_HUMANKRT16physical
19380743
TBA1B_HUMANTUBA1Bphysical
19380743
TBB2B_HUMANTUBB2Bphysical
19380743
SHC1_HUMANSHC1physical
19380743
HS71L_HUMANHSPA1Lphysical
19380743
HNRPU_HUMANHNRNPUphysical
19380743
TBB3_HUMANTUBB3physical
19380743
GRB2_HUMANGRB2physical
19380743
HSP76_HUMANHSPA6physical
19380743
K1C17_HUMANKRT17physical
19380743
EF1A1_HUMANEEF1A1physical
19380743
ADT2_HUMANSLC25A5physical
19380743
P85A_HUMANPIK3R1physical
19380743
K2C79_HUMANKRT79physical
19380743
TBB6_HUMANTUBB6physical
19380743
GRP78_HUMANHSPA5physical
19380743
GRP75_HUMANHSPA9physical
19380743
K2C73_HUMANKRT73physical
19380743
P85B_HUMANPIK3R2physical
19380743
ADT3_HUMANSLC25A6physical
19380743
HS90B_HUMANHSP90AB1physical
19380743
K2C3_HUMANKRT3physical
19380743
DDX3X_HUMANDDX3Xphysical
19380743
PCCB_HUMANPCCBphysical
19380743
MCCB_HUMANMCCC2physical
19380743
RLA0_HUMANRPLP0physical
19380743
SHIP1_HUMANINPP5Dphysical
19380743
DDX6_HUMANDDX6physical
19380743
DDX5_HUMANDDX5physical
19380743
XK_HUMANXKphysical
19380743
RS19_HUMANRPS19physical
19380743
GTF2I_HUMANGTF2Iphysical
19380743
TCPG_HUMANCCT3physical
19380743
HID1_HUMANHID1physical
20368287
AMPD2_HUMANAMPD2physical
22863883
E41L1_HUMANEPB41L1physical
22863883
KIF15_HUMANKIF15physical
22863883
LRBA_HUMANLRBAphysical
22863883
MLF2_HUMANMLF2physical
22863883
POP1_HUMANPOP1physical
22863883
PP4R2_HUMANPPP4R2physical
22863883
RPP30_HUMANRPP30physical
22863883
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
125853Diabetes mellitus, non-insulin-dependent (NIDDM)
0000269|PubMedNote=Genetic variations in INPPL1 may be a cause of susceptibility to metabolic syndrome. Metabolic syndrome is characterized by diabetes, insulin resistance, hypertension, and hypertriglyceridemia is absent. {ECO
258480
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHIP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; THR-165 ANDSER-241, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; TYR-986; SER-1003AND TYR-1135, AND MASS SPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-986 AND SER-1003, ANDMASS SPECTROMETRY.
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry.";
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-671; TYR-886; TYR-986;SER-1003; TYR-1135 AND TYR-1162, AND MASS SPECTROMETRY.
"Regulation of PDGF-stimulated SHIP2 tyrosine phosphorylation andassociation with Shc in 3T3-L1 preadipocytes.";
Artemenko Y., Gagnon A., Ibrahim S., Sorisky A.;
J. Cell. Physiol. 211:598-607(2007).
Cited for: PHOSPHORYLATION AT THR-958, AND MUTAGENESIS OF THR-958.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-886; TYR-986; TYR-987AND TYR-1135, AND MASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-886; TYR-986 ANDTYR-1135, AND MASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-986, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-886 AND TYR-986, ANDMASS SPECTROMETRY.
"Src family tyrosine kinases regulate adhesion-dependent tyrosinephosphorylation of 5'-inositol phosphatase SHIP2 during cellattachment and spreading on collagen I.";
Prasad N., Topping R.S., Decker S.J.;
J. Cell Sci. 115:3807-3815(2002).
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-986, AND MUTAGENESIS OF986-TYR-TYR-987.
"Tyrosine phosphorylation mapping of the epidermal growth factorreceptor signaling pathway.";
Steen H., Kuster B., Fernandez M., Pandey A., Mann M.;
J. Biol. Chem. 277:1031-1039(2002).
Cited for: PHOSPHORYLATION AT TYR-1162.
"The Src homology 2 domain containing inositol 5-phosphatase SHIP2 isrecruited to the epidermal growth factor (EGF) receptor anddephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells.";
Pesesse X., Dewaste V., De Smedt F., Laffargue M., Giuriato S.,Moreau C., Payrastre B., Erneux C.;
J. Biol. Chem. 276:28348-28355(2001).
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EGFR AND SHC1, ANDPHOSPHORYLATION AT TYR-986.

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