SHIP1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SHIP1_RAT
• UniProt AC: P97573
• Protein Name: Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
• Gene Name: Inpp5d
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 1190
• 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. Tra
• 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 (By similarity)..
• Protein Sequence: MPAMVPGWNHGNITRSKAEELLSRAGKDGSFLVRASESIPRAYALCVLFRNCVYTYRILPNEDDKFTVQASEGVPMRFFTKLDQLIEFYKKENMGLVTHLQFPVPLEEEDAIDEPEEDTESVMSPPELPPRNIPVSGGPCEAKDLPLPTENPRAPEVTRLSLSETLFQRLQSMDTSGLPEEHLKAIQDYLSTQLMLDSDFLKTGSSNLPHLKKLTSLLCKELHGEVIRTLPSLESLQRLFDQQLSPGLRPRPQVPGEANPITMVAKLSQLTSLLSSIEDKVKALLHEGSESTNRRSLIPPVTFEVKSESLGIPQKMHLKVDVESGKLIIKKSRDGSEDKFYSHKKILQLIKSQKFLNKLVILVETEKEKILRKEYVFSDSKKREGFCQLLQQMKNKHSEQSEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLGEKEWLEILRHSLQEVTSMTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWLGDLNYRVELPTWEAEAIIQKIKQQQYSDLLAHDQLLLERKEQEVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGAVDSQGQIEFLACYATLKTKSQTKFYLELHSSCLESFVKSQEGENEEGDEGELVVRFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLETTESQLPIYTPLTHHGEMTGHFRGEIKLQTSEGKMREKLYDFVKTERDESSGMKCLKNLTSHDPMRQWEPAGRVPACGISSLNEIINPNYIGMGPFGQPLHGKSTLSPDQQLTAWSYDQLPKDSSLGPGRGEGPPTPPSQPPLSPKKFSSSTANRGSCPRVQETRPGDLGKVEALPQEDLPLTKPEMFENPLYGSVSPFPKLVPRKEQESPKMMRKEPPPCPDPGVSSPSIMLPKAQEVENVKGTSKQAPVPVFGPTPRIRSFTCSSSAEGRMPSGDKSQGKPKAPASSQAPVPVKRPVKPSRSEMSQQTTPIPAPRPPLPVKSPAVLQLQHSKGRDYRDNTELPHHGKHRQEESLLGRTAMQ

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
23	Phosphorylation	SKAEELLSRAGKDGS HHHHHHHHHCCCCCC	32.48	30181290
30	Phosphorylation	SRAGKDGSFLVRASE HHCCCCCCEEEECCC	26.07	27097102
245	Phosphorylation	RLFDQQLSPGLRPRP HHHHCCCCCCCCCCC	16.75	22673903
373	Acetylation	EKEKILRKEYVFSDS HHHHHHHHHHHCCCC	50.37	22902405
425	Phosphorylation	APPPKKITSWFLSKG CCCCHHHEEEHHHCC	28.87	26022182
431	Acetylation	ITSWFLSKGQGKTRD HEEEHHHCCCCCCCC	58.35	22902405
435	Acetylation	FLSKGQGKTRDDSAD HHHCCCCCCCCCCCC	32.28	22902405
519	Phosphorylation	VKTGIANTLGNKGAV CCCCHHHCCCCCCCE	27.33	28432305
764	Acetylation	SCLESFVKSQEGENE HHHHHHHHCCCCCCC	44.40	22902405
867	Phosphorylation	GKMREKLYDFVKTER CHHHHHHHHHHHHHC	20.57	28689409
917	Phosphorylation	NEIINPNYIGMGPFG HHHCCCCCCCCCCCC	10.50	-
931	Phosphorylation	GQPLHGKSTLSPDQQ CCCCCCCCCCCHHHC	38.89	23984901
932	Phosphorylation	QPLHGKSTLSPDQQL CCCCCCCCCCHHHCH	34.44	23984901
934	Phosphorylation	LHGKSTLSPDQQLTA CCCCCCCCHHHCHHH	26.90	25532521
940	Phosphorylation	LSPDQQLTAWSYDQL CCHHHCHHHCCCCCC	23.03	23984901
944	Phosphorylation	QQLTAWSYDQLPKDS HCHHHCCCCCCCCCC	9.30	-
963	Phosphorylation	GRGEGPPTPPSQPPL CCCCCCCCCCCCCCC	51.47	22673903
966	Phosphorylation	EGPPTPPSQPPLSPK CCCCCCCCCCCCCCC	57.43	22673903
971	Phosphorylation	PPSQPPLSPKKFSSS CCCCCCCCCCCCCCC	40.21	21738781
1020	Phosphorylation	EMFENPLYGSVSPFP HHHCCCCCCCCCCCC	14.49	25532521
1037	Phosphorylation	VPRKEQESPKMMRKE CCCCCCCCCCHHCCC	29.52	25575281
1182	Phosphorylation	GKHRQEESLLGRTAM CCCHHHHHHHCCCCC	28.30	25532521

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SHIP1_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SHIP1_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SHIP1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FCGR2_RAT	Fcgr2b	physical	11970986
DOK1_RAT	Dok1	physical	11970986
FCERB_RAT	Ms4a2	physical	11970986

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.