INP5E_HUMAN - dbPTM
INP5E_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INP5E_HUMAN
UniProt AC Q9NRR6
Protein Name 72 kDa inositol polyphosphate 5-phosphatase
Gene Name INPP5E
Organism Homo sapiens (Human).
Sequence Length 644
Subcellular Localization Cytoplasm, cytoskeleton, cilium axoneme . Golgi apparatus, Golgi stack membrane
Peripheral membrane protein
Cytoplasmic side . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, ruffle . Cytoplasm . Peripheral membr
Protein Description Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns-P2, and phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate. Specific for lipid substrates, inactive towards water soluble inositol phosphates..
Protein Sequence MPSKAENLRPSEPAPQPPEGRTLQGQLPGAPPAQRAGSPPDAPGSESPALACSTPATPSGEDPPARAAPIAPRPPARPRLERALSLDDKGWRRRRFRGSQEDLEARNGTSPSRGSVQSEGPGAPAHSCSPPCLSTSLQEIPKSRGVLSSERGSPSSGGNPLSGVASSSPNLPHRDAAVAGSSPRLPSLLPPRPPPALSLDIASDSLRTANKVDSDLADYKLRAQPLLVRAHSSLGPGRPRSPLACDDCSLRSAKSSFSLLAPIRSKDVRSRSYLEGSLLASGALLGADELARYFPDRNVALFVATWNMQGQKELPPSLDEFLLPAEADYAQDLYVIGVQEGCSDRREWETRLQETLGPHYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTSGDGKVAERLLDYTRTVQALVLPRNVPDTNPYRSSAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRVKVRPGRDNIPLAAGKFDRELYLLGIKRRISKEIQRQQALQSQNSSTICSVS
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
38PhosphorylationPPAQRAGSPPDAPGS
CHHHHCCCCCCCCCC		32.0725850435
45PhosphorylationSPPDAPGSESPALAC
CCCCCCCCCCCCCCC		33.5727251275
47PhosphorylationPDAPGSESPALACST
CCCCCCCCCCCCCCC		19.7125850435
53PhosphorylationESPALACSTPATPSG
CCCCCCCCCCCCCCC		31.6422210691
54PhosphorylationSPALACSTPATPSGE
CCCCCCCCCCCCCCC		19.4825850435
85PhosphorylationPRLERALSLDDKGWR
HHHHHHHCCCCHHHH		28.8623401153
99PhosphorylationRRRRFRGSQEDLEAR
HHHHCCCCHHHHHHH		26.5817525332
109PhosphorylationDLEARNGTSPSRGSV
HHHHHCCCCCCCCCC		40.8022817900
153PhosphorylationVLSSERGSPSSGGNP
CCCCCCCCCCCCCCC		28.0329759185
155PhosphorylationSSERGSPSSGGNPLS
CCCCCCCCCCCCCCC		43.2227732954
156PhosphorylationSERGSPSSGGNPLSG
CCCCCCCCCCCCCCC		54.8527732954
162PhosphorylationSSGGNPLSGVASSSP
CCCCCCCCCCCCCCC		32.2627732954
166PhosphorylationNPLSGVASSSPNLPH
CCCCCCCCCCCCCCC		29.0127732954
167PhosphorylationPLSGVASSSPNLPHR
CCCCCCCCCCCCCCC		39.8227732954
168PhosphorylationLSGVASSSPNLPHRD
CCCCCCCCCCCCCCC		18.4728985074
181PhosphorylationRDAAVAGSSPRLPSL
CCHHCCCCCCCCHHH		27.6822210691
182PhosphorylationDAAVAGSSPRLPSLL
CHHCCCCCCCCHHHC		17.0822210691
220UbiquitinationDSDLADYKLRAQPLL
CCHHHHHHHHHCCEE		31.8529967540
232PhosphorylationPLLVRAHSSLGPGRP
CEEEEECCCCCCCCC		26.6929214152
233PhosphorylationLLVRAHSSLGPGRPR
EEEEECCCCCCCCCC		27.7223312004
241PhosphorylationLGPGRPRSPLACDDC
CCCCCCCCCCCCCCC		27.2729255136
249PhosphorylationPLACDDCSLRSAKSS
CCCCCCCCCCCCCHH		33.5425850435
252PhosphorylationCDDCSLRSAKSSFSL
CCCCCCCCCCHHCHH		45.3924719451
254UbiquitinationDCSLRSAKSSFSLLA
CCCCCCCCHHCHHHH		48.1327667366
255PhosphorylationCSLRSAKSSFSLLAP
CCCCCCCHHCHHHHC		36.0128857561
256PhosphorylationSLRSAKSSFSLLAPI
CCCCCCHHCHHHHCC		20.3928857561
270PhosphorylationIRSKDVRSRSYLEGS
CCCCCCCCCHHHHHC		25.9822798277
273PhosphorylationKDVRSRSYLEGSLLA
CCCCCCHHHHHCHHH		13.9922798277
281PhosphorylationLEGSLLASGALLGAD
HHHCHHHHHHCCCHH		25.2722798277
293PhosphorylationGADELARYFPDRNVA
CHHHHHHHCCCCCEE		17.5422817900
439PhosphorylationVAERLLDYTRTVQAL
HHHHHHHHHCEEEEE		9.70-
455PhosphorylationLPRNVPDTNPYRSSA
CCCCCCCCCCCCCCC		31.83-
487 (in isoform 2)Ubiquitination-28.3121890473
515UbiquitinationDQLIREMRKGSIFKG
HHHHHHHHCCCCCCC		35.1222817900
516UbiquitinationQLIREMRKGSIFKGF
HHHHHHHCCCCCCCC		56.5522817900
518PhosphorylationIREMRKGSIFKGFQE
HHHHHCCCCCCCCCC		28.0824719451
520UbiquitinationEMRKGSIFKGFQEPD
HHHCCCCCCCCCCCC		7.2921890473
521UbiquitinationMRKGSIFKGFQEPDI
HHCCCCCCCCCCCCC		58.0822817900
521 (in isoform 1)Ubiquitination-58.0821890473
542PhosphorylationKFDIGKDTYDSTSKQ
CEECCCCCCCCCCCC		32.49-
555PhosphorylationKQRTPSYTDRVLYRS
CCCCCCHHHHHHHHC		22.9729759185
560PhosphorylationSYTDRVLYRSRHKGD
CHHHHHHHHCCCCCC		12.0429759185
565UbiquitinationVLYRSRHKGDICPVS
HHHHCCCCCCCCCCC		58.11-
641MethylationSQNSSTICSVS----
HCCCCCCCCCC----		3.1324166846
641FarnesylationSQNSSTICSVS----
HCCCCCCCCCC----		3.1324166846
641FarnesylationSQNSSTICSVS----
HCCCCCCCCCC----		3.1324166846
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

Oops, there are no upstream regulatory protein records of INP5E_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INP5E_HUMAN !!
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 INP5E_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE6D_HUMANPDE6Dphysical
27173435
KCTD3_HUMANKCTD3physical
27173435
CING_HUMANCGNphysical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
RGPS2_HUMANRALGPS2physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
MAST3_HUMANMAST3physical
27173435
LRFN1_HUMANLRFN1physical
27173435
GGYF2_HUMANGIGYF2physical
27173435
NF1_HUMANNF1physical
27173435
CBY1_HUMANCBY1physical
27173435
SRGP2_HUMANSRGAP2physical
27173435
TANC2_HUMANTANC2physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
HDAC4_HUMANHDAC4physical
27173435
NADK_HUMANNADKphysical
27173435
NGAP_HUMANRASAL2physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
TIAM1_HUMANTIAM1physical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
NAV1_HUMANNAV1physical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
STA13_HUMANSTARD13physical
27173435
CWC25_HUMANCWC25physical
27173435
RPTOR_HUMANRPTORphysical
27173435
HDAC7_HUMANHDAC7physical
27173435
MFR1L_HUMANMTFR1Lphysical
27173435
RPGR_HUMANRPGRphysical
27173435
CE170_HUMANCEP170physical
27173435
1433E_HUMANYWHAEphysical
27173435
Drug and Disease Associations
Kegg Disease
H00530 Joubert syndrome
OMIM Disease
213300Joubert syndrome 1 (JBTS1)
610156Mental retardation, truncal obesity, retinal dystrophy, and micropenis (MORMS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INP5E_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, AND MASSSPECTROMETRY.

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