I5P2_HUMAN - dbPTM
I5P2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID I5P2_HUMAN
UniProt AC P32019
Protein Name Type II inositol 1,4,5-trisphosphate 5-phosphatase
Gene Name INPP5B
Organism Homo sapiens (Human).
Sequence Length 993
Subcellular Localization Cytoplasm, cytosol . Endoplasmic reticulum-Golgi intermediate compartment . Early endosome membrane . Membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasmic vesicle, phagosome membrane . Golgi apparatus .
Protein Description Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events..
Protein Sequence MDQSVAIQETLAEGEYCVIAVQGVLCEGDSRQSRLLGLVRYRLEHGGQEHALFLYTHRRMAITGDDVSLDQIVPVSRDFTLEEVSPDGELYILGSDVTVQLDTAELSLVFQLPFGSQTRMFLHEVARACPGFDSATRDPEFLWLSRYRCAELELEMPTPRGCNSALVTWPGYATIGGGRYPSRKKRWGLEEARPQGAGSVLFWGGAMEKTGFRLMERAHGGGFVWGRSARDGRRDEELEEAGREMSAAAGSRERNTAGGSNFDGLRPNGKGVPMDQSSRGQDKPESLQPRQNKSKSEITDMVRSSTITVSDKAHILSMQKFGLRDTIVKSHLLQKEEDYTYIQNFRFFAGTYNVNGQSPKECLRLWLSNGIQAPDVYCVGFQELDLSKEAFFFHDTPKEEEWFKAVSEGLHPDAKYAKVKLIRLVGIMLLLYVKQEHAAYISEVEAETVGTGIMGRMGNKGGVAIRFQFHNTSICVVNSHLAAHIEEYERRNQDYKDICSRMQFCQPDPSLPPLTISNHDVILWLGDLNYRIEELDVEKVKKLIEEKDFQMLYAYDQLKIQVAAKTVFEGFTEGELTFQPTYKYDTGSDDWDTSEKCRAPAWCDRILWKGKNITQLSYQSHMALKTSDHKPVSSVFDIGVRVVNDELYRKTLEEIVRSLDKMENANIPSVSLSKREFCFQNVKYMQLKVESFTIHNGQVPCHFEFINKPDEESYCKQWLNANPSRGFLLPDSDVEIDLELFVNKMTATKLNSGEDKIEDILVLHLDRGKDYFLSVSGNYLPSCFGSPIHTLCYMREPILDLPLETISELTLMPVWTGDDGSQLDSPMEIPKELWMMVDYLYRNAVQQEDLFQQPGLRSEFEHIRDCLDTGMIDNLSASNHSVAEALLLFLESLPEPVICYSTYHNCLECSGNYTASKQVISTLPIFHKNVFHYLMAFLRELLKNSAKNHLDENILASIFGSLLLRNPAGHQKLDMTEKKKAQEFIHQFLCNPL
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
68 (in isoform 3)Ubiquitination-32.9721890473
116PhosphorylationVFQLPFGSQTRMFLH
EEECCCCCHHHHHHH		28.8529496963
118PhosphorylationQLPFGSQTRMFLHEV
ECCCCCHHHHHHHHH		26.2929449344
160 (in isoform 3)Ubiquitination-65.8521890473
164PhosphorylationPTPRGCNSALVTWPG
CCCCCCCCCCEECCC		27.3628509920
168PhosphorylationGCNSALVTWPGYATI
CCCCCCEECCCCCCC		27.1328509920
172 (in isoform 2)Phosphorylation-9.1127642862
180PhosphorylationATIGGGRYPSRKKRW
CCCCCCCCCCHHHCC		14.6128509920
182PhosphorylationIGGGRYPSRKKRWGL
CCCCCCCCHHHCCCC		48.0428509920
214 (in isoform 2)Phosphorylation-3.7924719451
232 (in isoform 2)Ubiquitination-22.4421890473
270AcetylationDGLRPNGKGVPMDQS
CCCCCCCCCCCCCCC		64.4726051181
294PhosphorylationLQPRQNKSKSEITDM
CCCCCCCCHHHHHHH		49.3030108239
296PhosphorylationPRQNKSKSEITDMVR
CCCCCCHHHHHHHHH		41.1230108239
306PhosphorylationTDMVRSSTITVSDKA
HHHHHHCEEEECCHH		23.1628857561
312UbiquitinationSTITVSDKAHILSMQ
CEEEECCHHHHHHCH		34.0721890473
312 (in isoform 4)Ubiquitination-34.0721890473
312UbiquitinationSTITVSDKAHILSMQ
CEEEECCHHHHHHCH		34.0721890473
312 (in isoform 1)Ubiquitination-34.0721890473
324 (in isoform 2)Ubiquitination-39.1321890473
352PhosphorylationFRFFAGTYNVNGQSP
EEEEEEEECCCCCCH		19.0519413330
360UbiquitinationNVNGQSPKECLRLWL
CCCCCCHHHHHHHHH		67.32-
404UbiquitinationPKEEEWFKAVSEGLH
CCHHHHHHHHHCCCC		49.2921890473
404 (in isoform 1)Ubiquitination-49.2921890473
404UbiquitinationPKEEEWFKAVSEGLH
CCHHHHHHHHHCCCC		49.2921890473
404 (in isoform 4)Ubiquitination-49.2921890473
430 (in isoform 3)Ubiquitination-1.4721890473
432PhosphorylationVGIMLLLYVKQEHAA
HHHHHHHHHHHHHHH		12.9319413330
496UbiquitinationERRNQDYKDICSRMQ
HHHCCCHHHHHHHCC		49.24-
542UbiquitinationLDVEKVKKLIEEKDF
CCHHHHHHHHHHCCH		58.65-
547UbiquitinationVKKLIEEKDFQMLYA
HHHHHHHCCHHHHHH		51.56-
571 (in isoform 2)Phosphorylation-4.4127251275
586PhosphorylationQPTYKYDTGSDDWDT
ECEEECCCCCCCCCC		35.18-
594 (in isoform 2)Ubiquitination-32.3621890473
596UbiquitinationDDWDTSEKCRAPAWC
CCCCCCHHCCCCHHH		28.87-
620PhosphorylationITQLSYQSHMALKTS
HHHHHHHHCCCCCCC		13.6529396449
630UbiquitinationALKTSDHKPVSSVFD
CCCCCCCCCCCHHEE		52.70-
650UbiquitinationVNDELYRKTLEEIVR
ECHHHHHHHHHHHHH		43.86-
651PhosphorylationNDELYRKTLEEIVRS
CHHHHHHHHHHHHHH		30.3327251275
669PhosphorylationMENANIPSVSLSKRE
HHHCCCCCCCCCHHH		22.1226437602
671PhosphorylationNANIPSVSLSKREFC
HCCCCCCCCCHHHHH		31.1226437602
673PhosphorylationNIPSVSLSKREFCFQ
CCCCCCCCHHHHHCC		23.3528270605
674UbiquitinationIPSVSLSKREFCFQN
CCCCCCCHHHHHCCC		62.3321906983
674 (in isoform 1)Ubiquitination-62.3321890473
674 (in isoform 4)Ubiquitination-62.3321890473
684PhosphorylationFCFQNVKYMQLKVES
HHCCCCEEEEEEEEE		5.94-
728 (in isoform 3)Ubiquitination-8.2621890473
892 (in isoform 2)Ubiquitination-51.9121890473
933PhosphorylationFHKNVFHYLMAFLRE
CCHHHHHHHHHHHHH		6.1622817900
961PhosphorylationILASIFGSLLLRNPA
HHHHHHHHHHHHCCC		12.70-
972 (in isoform 1)Ubiquitination-40.5621890473
972UbiquitinationRNPAGHQKLDMTEKK
HCCCCCCCCCCCHHH		40.562190698
990MethylationEFIHQFLCNPL----
HHHHHHHHCCC----		5.35-
990FarnesylationEFIHQFLCNPL----
HHHHHHHHCCC----		5.35-
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 I5P2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of I5P2_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 I5P2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 I5P2_HUMAN

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Related Literatures of Post-Translational Modification

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