PI5PA_HUMAN - dbPTM
PI5PA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PI5PA_HUMAN
UniProt AC Q15735
Protein Name Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
Gene Name INPP5J
Organism Homo sapiens (Human).
Sequence Length 1006
Subcellular Localization Cytoplasm. Predominantly localized to membrane ruffles..
Protein Description Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles (By similarity)..
Protein Sequence MEGQSSRGSRRPGTRAGLGSLPMPQGVAQTGAPSKVDSSFQLPAKKNAALGPSEPRLALAPVGPRAAMSASSEGPRLALASPRPILAPLCTPEGQKTATAHRSSSLAPTSVGQLVMSASAGPKPPPATTGSVLAPTSLGLVMPASAGPRSPPVTLGPNLAPTSRDQKQEPPASVGPKPTLAASGLSLALASEEQPPELPSTPSPVPSPVLSPTQEQALAPASTASGAASVGQTSARKRDAPAPRPLPASEGHLQPPAQTSGPTGSPPCIQTSPDPRLSPSFRARPEALHSSPEDPVLPRPPQTLPLDVGQGPSEPGTHSPGLLSPTFRPGAPSGQTVPPPLPKPPRSPSRSPSHSPNRSPCVPPAPDMALPRLGTQSTGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPTWKSDPGFRITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGADMIAIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSDHKPVAAQFLLQFAFRDDMPLVRLEVADEWVRPEQAVVRYRMETVFARSSWDWIGLYRVGFRHCKDYVAYVWAKHEDVDGNTYQVTFSEESLPKGHGDFILGYYSHNHSILIGITEPFQISLPSSELASSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPGLALRPSSRERRGASRSPSPQSRRLSRVAPDRSSNGSSRGSSEEGPSGLPGPWAFPPAVPRSLGLLPALRLETVDPGGGGSWGPDREALAPNSLSPSPQGHRGLEEGGLGP
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
7Methylation-MEGQSSRGSRRPGT
-CCCCCCCCCCCCCC		52.97115487509
20PhosphorylationGTRAGLGSLPMPQGV
CCCCCCCCCCCCCCC		34.05-
30PhosphorylationMPQGVAQTGAPSKVD
CCCCCCCCCCCCCCC		26.10-
34PhosphorylationVAQTGAPSKVDSSFQ
CCCCCCCCCCCCCCC		44.79-
38PhosphorylationGAPSKVDSSFQLPAK
CCCCCCCCCCCCCCC		35.72-
39PhosphorylationAPSKVDSSFQLPAKK
CCCCCCCCCCCCCCC		16.7324670416
56Asymmetric dimethylarginineALGPSEPRLALAPVG
CCCCCCCCEEECCCC		28.65-
56MethylationALGPSEPRLALAPVG
CCCCCCCCEEECCCC		28.6558858901
65MethylationALAPVGPRAAMSASS
EECCCCHHHHHCCCC		29.1158858909
71PhosphorylationPRAAMSASSEGPRLA
HHHHHCCCCCCCCEE		22.9330631047
72PhosphorylationRAAMSASSEGPRLAL
HHHHCCCCCCCCEEE		46.4124114839
76Asymmetric dimethylarginineSASSEGPRLALASPR
CCCCCCCCEEECCCC		43.37-
76MethylationSASSEGPRLALASPR
CCCCCCCCEEECCCC		43.3754549903
81PhosphorylationGPRLALASPRPILAP
CCCEEECCCCCEECC		23.4521712546
83MethylationRLALASPRPILAPLC
CEEECCCCCEECCCC		28.5358858917
83Asymmetric dimethylarginineRLALASPRPILAPLC
CEEECCCCCEECCCC		28.53-
91PhosphorylationPILAPLCTPEGQKTA
CEECCCCCCCCCCCC		31.8721712546
103PhosphorylationKTATAHRSSSLAPTS
CCCCCCCCCCCCCCC		17.8921955146
104PhosphorylationTATAHRSSSLAPTSV
CCCCCCCCCCCCCCH		29.3621955146
105PhosphorylationATAHRSSSLAPTSVG
CCCCCCCCCCCCCHH		29.7821955146
109PhosphorylationRSSSLAPTSVGQLVM
CCCCCCCCCHHHHHH		30.3621955146
110PhosphorylationSSSLAPTSVGQLVMS
CCCCCCCCHHHHHHH		24.1621955146
117PhosphorylationSVGQLVMSASAGPKP
CHHHHHHHCCCCCCC		16.1621955146
119PhosphorylationGQLVMSASAGPKPPP
HHHHHHCCCCCCCCC		26.8421955146
128PhosphorylationGPKPPPATTGSVLAP
CCCCCCCCCCCCCCC		37.1521955146
129PhosphorylationPKPPPATTGSVLAPT
CCCCCCCCCCCCCCC		29.5721955146
131PhosphorylationPPPATTGSVLAPTSL
CCCCCCCCCCCCCEE		16.3321955146
136PhosphorylationTGSVLAPTSLGLVMP
CCCCCCCCEECEEEE		30.8621955146
137PhosphorylationGSVLAPTSLGLVMPA
CCCCCCCEECEEEEC		21.2721955146
145PhosphorylationLGLVMPASAGPRSPP
ECEEEECCCCCCCCC		28.0821955146
150PhosphorylationPASAGPRSPPVTLGP
ECCCCCCCCCCCCCC		36.3730266825
154O-linked_GlycosylationGPRSPPVTLGPNLAP
CCCCCCCCCCCCCCC		31.6028657654
154PhosphorylationGPRSPPVTLGPNLAP
CCCCCCCCCCCCCCC		31.6023312004
163O-linked_GlycosylationGPNLAPTSRDQKQEP
CCCCCCCCCCCCCCC		32.5728657654
249PhosphorylationAPRPLPASEGHLQPP
CCCCCCCCCCCCCCC		42.0227732954
259PhosphorylationHLQPPAQTSGPTGSP
CCCCCCCCCCCCCCC		37.4427732954
260PhosphorylationLQPPAQTSGPTGSPP
CCCCCCCCCCCCCCC		30.6027732954
263PhosphorylationPAQTSGPTGSPPCIQ
CCCCCCCCCCCCCCC		54.5427732954
265PhosphorylationQTSGPTGSPPCIQTS
CCCCCCCCCCCCCCC		28.3127732954
271PhosphorylationGSPPCIQTSPDPRLS
CCCCCCCCCCCCCCC		23.4727732954
272PhosphorylationSPPCIQTSPDPRLSP
CCCCCCCCCCCCCCH		15.7827732954
278PhosphorylationTSPDPRLSPSFRARP
CCCCCCCCHHHHCCH		21.5622210691
291PhosphorylationRPEALHSSPEDPVLP
CHHHHHCCCCCCCCC		22.89-
324PhosphorylationTHSPGLLSPTFRPGA
CCCCCCCCCCCCCCC		27.26-
377PhosphorylationLPRLGTQSTGPGRCL
CCCCCCCCCCCCCCC		34.8624275569
520PhosphorylationAKYYHLPFLRDVQTD
HHHHCCHHHHCCCCC		12.5927251275
534PhosphorylationDCTRTGLGGYWGNKG
CCCCCCCCCCCCCCC		28.6124719451
535PhosphorylationCTRTGLGGYWGNKGG
CCCCCCCCCCCCCCC		21.7727251275
622PhosphorylationFVKFAIDSDQLHQLW
EEEEEECHHHHHHHH		22.5727251275
624PhosphorylationKFAIDSDQLHQLWEK
EEEECHHHHHHHHHH		44.8127251275
657PhosphorylationGPLNFAPTFKFDVGT
CCCCCCCEEEEECCC		35.7130377224
664PhosphorylationTFKFDVGTNKYDTSA
EEEEECCCCCCCCCC		28.5230377224
667PhosphorylationFDVGTNKYDTSAKKR
EECCCCCCCCCCHHC		26.9030377224
669PhosphorylationVGTNKYDTSAKKRKP
CCCCCCCCCCHHCCC		27.7430377224
670PhosphorylationGTNKYDTSAKKRKPA
CCCCCCCCCHHCCCC		34.8830377224
694PhosphorylationKAPGGGPSPSGRKSH
ECCCCCCCCCCCCCC		34.6721712546
696PhosphorylationPGGGPSPSGRKSHRL
CCCCCCCCCCCCCEE		56.4126270265
875PhosphorylationLLAPKSRSPSPGKSK
EECCCCCCCCCCCCC		36.5028985074
877PhosphorylationAPKSRSPSPGKSKRH
CCCCCCCCCCCCCCH		47.7528985074
881PhosphorylationRSPSPGKSKRHRSRS
CCCCCCCCCCHHCCC		40.62-
886PhosphorylationGKSKRHRSRSPGLAR
CCCCCHHCCCCCCCC		30.8720363803
888PhosphorylationSKRHRSRSPGLARFP
CCCHHCCCCCCCCCC		25.2720363803
902PhosphorylationPGLALRPSSRERRGA
CCCCCCCCHHCCCCC		35.2830266825
903PhosphorylationGLALRPSSRERRGAS
CCCCCCCHHCCCCCC		40.6230266825
910PhosphorylationSRERRGASRSPSPQS
HHCCCCCCCCCCHHH		35.7920363803
912PhosphorylationERRGASRSPSPQSRR
CCCCCCCCCCHHHHH		27.5120363803
914PhosphorylationRGASRSPSPQSRRLS
CCCCCCCCHHHHHHH		36.5020363803
917PhosphorylationSRSPSPQSRRLSRVA
CCCCCHHHHHHHCCC		23.8128102081
957PhosphorylationFPPAVPRSLGLLPAL
CCCCCCCHHCCCCCE		22.2528555341
976PhosphorylationVDPGGGGSWGPDREA
ECCCCCCCCCCCHHH		31.9428102081
988PhosphorylationREALAPNSLSPSPQG
HHHCCCCCCCCCCCC		29.2129978859
990PhosphorylationALAPNSLSPSPQGHR
HCCCCCCCCCCCCCC		24.1329116813
992PhosphorylationAPNSLSPSPQGHRGL
CCCCCCCCCCCCCCC		26.8629978859
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 PI5PA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PI5PA_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 PI5PA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI54_HUMANTRIM54physical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PI5PA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND MASSSPECTROMETRY.

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