SHIP1_MOUSE - dbPTM
SHIP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHIP1_MOUSE
UniProt AC Q9ES52
Protein Name Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
Gene Name Inpp5d
Organism Mus musculus (Mouse).
Sequence Length 1191
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein . Membrane raft . Cytoplasm, cytoskeleton . Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type (Pub
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. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6..
Protein Sequence MPAMVPGWNHGNITRSKAEELLSRAGKDGSFLVRASESIPRAYALCVLFRNCVYTYRILPNEDDKFTVQASEGVPMRFFTKLDQLIDFYKKENMGLVTHLQYPVPLEEEDAIDEAEEDTVESVMSPPELPPRNIPMSAGPSEAKDLPLATENPRAPEVTRLSLSETLFQRLQSMDTSGLPEEHLKAIQDYLSTQLLLDSDFLKTGSSNLPHLKKLMSLLCKELHGEVIRTLPSLESLQRLFDQQLSPGLRPRPQVPGEASPITMVAKLSQLTSLLSSIEDKVKSLLHEGSESTNRRSLIPPVTFEVKSESLGIPQKMHLKVDVESGKLIVKKSKDGSEDKFYSHKKILQLIKSQKFLNKLVILVETEKEKILRKEYVFADSKKREGFCQLLQQMKNKHSEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLGEKEWLELLRHSLQEVTSMTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWLGDLNYRVELPTWEAEAIIQKIKQQQYSDLLAHDQLLLERKDQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLACYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVRFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLETTEAQHPIYTPLTHHGEMTGHFRGEIKLQTSQGKMREKLYDFVKTERDESSGMKCLKNLTSHDPMRQWEPSGRVPACGVSSLNEMINPNYIGMGPFGQPLHGKSTLSPDQQLTAWSYDQLPKDSSLGPGRGEGPPTPPSQPPLSPKKFSSSTANRGPCPRVQEARPGDLGKVEALLQEDLLLTKPEMFENPLYGSVSSFPKLVPRKEQESPKMLRKEPPPCPDPGISSPSIVLPKAQEVESVKGTSKQAPVPVLGPTPRIRSFTCSSSAEGRMTSGDKSQGKPKASASSQAPVPVKRPVKPSRSEMSQQTTPIPAPRPPLPVKSPAVLQLQHSKGRDYRDNTELPHHGKHRQEEGLLGRTAMQ
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
30PhosphorylationSRAGKDGSFLVRASE
HHCCCCCCEEEECCC		26.0720810657
38PhosphorylationFLVRASESIPRAYAL
EEEECCCCCCHHHHH		35.0820810657
150PhosphorylationAKDLPLATENPRAPE
HCCCCCCCCCCCCCH		43.9320531401
162PhosphorylationAPEVTRLSLSETLFQ
CCHHHEECHHHHHHH		26.9320810657
173PhosphorylationTLFQRLQSMDTSGLP
HHHHHHHCCCCCCCC		24.1820810657
176PhosphorylationQRLQSMDTSGLPEEH
HHHHCCCCCCCCHHH		18.9530635358
177PhosphorylationRLQSMDTSGLPEEHL
HHHCCCCCCCCHHHH		33.7830635358
246PhosphorylationRLFDQQLSPGLRPRP
HHHHCCCCCCCCCCC		16.7526824392
260PhosphorylationPQVPGEASPITMVAK
CCCCCCCCCHHHHHH		16.7222942356
263PhosphorylationPGEASPITMVAKLSQ
CCCCCCHHHHHHHHH		14.6925159016
269PhosphorylationITMVAKLSQLTSLLS
HHHHHHHHHHHHHHH		23.5720810657
297PhosphorylationSESTNRRSLIPPVTF
CCCCCCCCCCCCEEE		27.6728833060
376PhosphorylationEKILRKEYVFADSKK
HHHHHCHHEECCCHH		12.1425367039
441PhosphorylationQGKTRDDSADYIPHD
CCCCCCCCCCCCCCE		27.5920810657
509GlutathionylationENRISHICTDNVKTG
CCCCEEECCCCCCCC		3.0724333276
520PhosphorylationVKTGIANTLGNKGAV
CCCCHHHCCCCCCCE		27.3328833060
647PhosphorylationEITFAPTYRFERLTR
ECCCCCCCCCEECCC		16.55-
655 (in isoform 6)Phosphorylation-42.9825367039
657PhosphorylationERLTRDKYAYTKQKA
EECCCCCCCCCCCCC		14.7721183079
740PhosphorylationQIEFLACYATLKTKS
HEEEEEEEEEECCCC		9.30-
749PhosphorylationTLKTKSQTKFYLEFH
EECCCCCCEEEEEEH		30.1628059163
775PhosphorylationEGENEEGSEGELVVR
CCCCCCCCCCEEEEE		45.7920810657
799PhosphorylationPIISDPEYLLDQHIL
CCCCCHHHHHCCEEE		20.25-
837PhosphorylationTEAQHPIYTPLTHHG
CCCCCCCCCCCCCCC		13.5222817900
838PhosphorylationEAQHPIYTPLTHHGE
CCCCCCCCCCCCCCE		16.7325367039
855AcetylationGHFRGEIKLQTSQGK
CEEEEEEEEECCCCH		30.1815614465
868PhosphorylationGKMREKLYDFVKTER
CHHHHHHHHHHHHHC		20.5725521595
888PhosphorylationMKCLKNLTSHDPMRQ
CCHHHHCCCCCHHHC		33.1525266776
889PhosphorylationKCLKNLTSHDPMRQW
CHHHHCCCCCHHHCC		29.1127566939
899PhosphorylationPMRQWEPSGRVPACG
HHHCCCCCCCCCCCC		27.9325367039
905GlutathionylationPSGRVPACGVSSLNE
CCCCCCCCCCCHHHH		4.5324333276
908PhosphorylationRVPACGVSSLNEMIN
CCCCCCCCHHHHCCC		17.8725367039
909PhosphorylationVPACGVSSLNEMINP
CCCCCCCHHHHCCCC		32.5725367039
918PhosphorylationNEMINPNYIGMGPFG
HHCCCCCCCCCCCCC		10.5025159016
918 (in isoform 3)Phosphorylation-10.5025367039
932PhosphorylationGQPLHGKSTLSPDQQ
CCCCCCCCCCCHHHC		38.8928833060
933PhosphorylationQPLHGKSTLSPDQQL
CCCCCCCCCCHHHCC		34.4428833060
935PhosphorylationLHGKSTLSPDQQLTA
CCCCCCCCHHHCCEE		26.9021082442
941PhosphorylationLSPDQQLTAWSYDQL
CCHHHCCEECCCCCC		23.0328833060
944PhosphorylationDQQLTAWSYDQLPKD
HHCCEECCCCCCCCC		19.1728833060
945PhosphorylationQQLTAWSYDQLPKDS
HCCEECCCCCCCCCC		9.3028833060
952PhosphorylationYDQLPKDSSLGPGRG
CCCCCCCCCCCCCCC		33.3228833060
953PhosphorylationDQLPKDSSLGPGRGE
CCCCCCCCCCCCCCC		47.6928833060
964PhosphorylationGRGEGPPTPPSQPPL
CCCCCCCCCCCCCCC		51.4727742792
967PhosphorylationEGPPTPPSQPPLSPK
CCCCCCCCCCCCCCC		57.4327742792
972PhosphorylationPPSQPPLSPKKFSSS
CCCCCCCCCCCCCCC		40.2125521595
977PhosphorylationPLSPKKFSSSTANRG
CCCCCCCCCCCCCCC		32.0520810657
986GlutathionylationSTANRGPCPRVQEAR
CCCCCCCCCCCCCCC		3.6124333276
1011PhosphorylationLQEDLLLTKPEMFEN
HHHCCCCCCHHHHCC		44.5122345495
1021PhosphorylationEMFENPLYGSVSSFP
HHHCCCCCCCHHHCC		14.4911567986
1023PhosphorylationFENPLYGSVSSFPKL
HCCCCCCCHHHCCCC		12.7920810657
1025PhosphorylationNPLYGSVSSFPKLVP
CCCCCCHHHCCCCCC		28.1422345495
1026PhosphorylationPLYGSVSSFPKLVPR
CCCCCHHHCCCCCCC		43.3322345495
1038PhosphorylationVPRKEQESPKMLRKE
CCCCCCCCCCHHCCC		29.5227600695
1049GlutathionylationLRKEPPPCPDPGISS
HCCCCCCCCCCCCCC		8.0224333276
1055PhosphorylationPCPDPGISSPSIVLP
CCCCCCCCCCCEEEC		41.9530635358
1056PhosphorylationCPDPGISSPSIVLPK
CCCCCCCCCCEEECC		22.2729109428
1058PhosphorylationDPGISSPSIVLPKAQ
CCCCCCCCEEECCCE		27.5529109428
1069PhosphorylationPKAQEVESVKGTSKQ
CCCEEEEECCCCCCC		34.0129109428
1073PhosphorylationEVESVKGTSKQAPVP
EEEECCCCCCCCCCC		27.3429109428
1074PhosphorylationVESVKGTSKQAPVPV
EEECCCCCCCCCCCC		31.2929109428
1085PhosphorylationPVPVLGPTPRIRSFT
CCCCCCCCCCEEEEE		24.33-
1090PhosphorylationGPTPRIRSFTCSSSA
CCCCCEEEEEECCCC		23.6521082442
1092PhosphorylationTPRIRSFTCSSSAEG
CCCEEEEEECCCCCC		16.8420810657
1093GlutathionylationPRIRSFTCSSSAEGR
CCEEEEEECCCCCCC		3.3224333276
1094PhosphorylationRIRSFTCSSSAEGRM
CEEEEEECCCCCCCC		25.0328833060
1095PhosphorylationIRSFTCSSSAEGRMT
EEEEEECCCCCCCCC		35.4028833060
1096PhosphorylationRSFTCSSSAEGRMTS
EEEEECCCCCCCCCC		17.6628833060
1114PhosphorylationSQGKPKASASSQAPV
CCCCCCCCCCCCCCC		34.5120810657
1152PhosphorylationRPPLPVKSPAVLQLQ
CCCCCCCCCHHHEEE		20.5122817900
1161PhosphorylationAVLQLQHSKGRDYRD
HHHEEECCCCCCCCC		24.6820810657
1166PhosphorylationQHSKGRDYRDNTELP
ECCCCCCCCCCCCCC		20.6422817900
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
30SPhosphorylationKinasePRKACAP17612
GPS
38SPhosphorylationKinasePRKACAP17612
GPS
162SPhosphorylationKinasePRKACAP17612
GPS
173SPhosphorylationKinasePRKACAP17612
GPS
246SPhosphorylationKinasePRKACAP17612
GPS
260SPhosphorylationKinasePRKACAP17612
GPS
269SPhosphorylationKinasePRKACAP17612
GPS
441SPhosphorylationKinasePKA-FAMILY-GPS
441SPhosphorylationKinasePRKACAP17612
GPS
775SPhosphorylationKinasePRKACAP17612
GPS
918YPhosphorylationKinaseLCKP06240
PSP
935SPhosphorylationKinasePRKACAP17612
GPS
964TPhosphorylationKinasePRKACAP17612
GPS
972SPhosphorylationKinasePRKACAP17612
GPS
977SPhosphorylationKinasePRKACAP17612
GPS
1021YPhosphorylationKinaseLCKP06240
PSP
1023SPhosphorylationKinasePRKACAP17612
GPS
1092TPhosphorylationKinasePRKACAP17612
GPS
1114SPhosphorylationKinasePRKACAP17612
GPS
1161SPhosphorylationKinasePRKACAP17612
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHIP1_MOUSE !!
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 SHIP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZO2_MOUSETjp2physical
16601135
BCAR1_MOUSEBcar1physical
16601135
CBL_MOUSECblphysical
16601135
CTND1_MOUSECtnnd1physical
16601135
SC23A_MOUSESec23aphysical
16601135
BTK_MOUSEBtkphysical
16601135
DOK3_MOUSEDok3physical
16601135
PPIP1_MOUSEPstpip1physical
16601135
DCTN2_MOUSEDctn2physical
16601135
LPXN_MOUSELpxnphysical
16601135
PARVG_MOUSEParvgphysical
16601135
ACTZ_MOUSEActr1aphysical
16601135
PTN11_MOUSEPtpn11physical
9393882
SHC1_MOUSEShc1physical
9393882
ABL1_MOUSEAbl1physical
9393882
CBL_MOUSECblphysical
9393882
SH3K1_MOUSESh3kbp1physical
21725061
DOK1_MOUSEDok1physical
11031258
ABL1_MOUSEAbl1physical
11031258
CRKL_MOUSECrklphysical
11031258
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHIP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-868 AND SER-972, ANDMASS SPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-868; SER-935 ANDTYR-945, AND MASS SPECTROMETRY.
"Shc interaction with Src homology 2 domain containing inositolphosphatase (SHIP) in vivo requires the Shc-phosphotyrosine bindingdomain and two specific phosphotyrosines on SHIP.";
Lamkin T.D., Walk S.F., Liu L., Damen J.E., Krystal G.,Ravichandran K.S.;
J. Biol. Chem. 272:10396-10401(1997).
Cited for: PHOSPHORYLATION AT TYR-918 AND TYR-1021, INTERACTION WITH SHC1, ANDMUTAGENESIS OF TYR-918 AND TYR-1021.

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