INP4B_HUMAN - dbPTM
INP4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INP4B_HUMAN
UniProt AC O15327
Protein Name Type II inositol 3,4-bisphosphate 4-phosphatase
Gene Name INPP4B
Organism Homo sapiens (Human).
Sequence Length 924
Subcellular Localization
Protein Description Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate..
Protein Sequence MEIKEEGASEEGQHFLPTAQANDPGDCQFTSIQKTPNEPQLEFILACKDLVAPVRDRKLNTLVQISVIHPVEQSLTRYSSTEIVEGTRDPLFLTGVTFPSEYPIYEETKIKLTVYDVKDKSHDTVRTSVLPEHKDPPPEVGRSFLGYASFKVGELLKSKEQLLVLSLRTSDGGKVVGTIEVSVVKMGEIEDGEADHITTDVQGQKCALVCECTAPESVSGKDNLPFLNSVLKNPVCKLYRFPTSDNKWMRIREQMSESILSFHIPKELISLHIKEDLCRNQEIKELGELSPHWDNLRKNVLTHCDQMVNMYQDILTELSKETGSSFKSSSSKGEKTLEFVPINLHLQRMQVHSPHLKDALYDVITVGAPAAHFQGFKNGGLRKLLHRFETERRNTGYQFIYYSPENTAKAKEVLSNINQLQPLIATHADLLLNSASQHSPDSLKNSLKMLSEKTELFVHAFKDQLVRSALLALYTARPGGILKKPPSPKSSTEESSPQDQPPVMRGQDSIPHHSDYDEEEWDRVWANVGKSLNCIIAMVDKLIERDGGSEGSGGNNDGEKEPSLTDAIPSHPREDWYEQLYPLILTLKDCMGEVVNRAKQSLTFVLLQELAYSLPQCLMLTLRRDIVFSQALAGLVCGFIIKLQTSLYDPGFLQQLHTVGLIVQYEGLLSTYSDEIGMLEDMAVGISDLKKVAFKIIEAKSNDVLPVITGRREHYVVEVKLPARMFESLPLQIKEGQLLHVYPVLFNVGINEQQTLAERFGDVSLQESINQENFELLQEYYKIFMEKMPPDYISHFQEQNDLKALLENLLQNIQSKKRKNVEIMWLAATICRKLNGIRFTCCKSAKDRTSMSVTLEQCSILRDEHQLHKDFFIRALDCMRREGCRIENVLKNIKCRKYAFNMLQLMAFPKYYRPPEGTYGKADT
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
35PhosphorylationQFTSIQKTPNEPQLE
CEEECEECCCCCCHH
18.2527251275
61PhosphorylationVRDRKLNTLVQISVI
CCCCCCCCEEEEEEE
38.45-
66PhosphorylationLNTLVQISVIHPVEQ
CCCEEEEEEEECCCC
9.64-
74PhosphorylationVIHPVEQSLTRYSST
EEECCCCCCCCCCCC
20.43-
76PhosphorylationHPVEQSLTRYSSTEI
ECCCCCCCCCCCCCC
32.57-
79PhosphorylationEQSLTRYSSTEIVEG
CCCCCCCCCCCCEEC
27.7428348404
80PhosphorylationQSLTRYSSTEIVEGT
CCCCCCCCCCCEECC
22.5628348404
81PhosphorylationSLTRYSSTEIVEGTR
CCCCCCCCCCEECCC
24.6428348404
87PhosphorylationSTEIVEGTRDPLFLT
CCCCEECCCCCCEEE
20.5628348404
94PhosphorylationTRDPLFLTGVTFPSE
CCCCCEEECCCCCCC
23.4426074081
97PhosphorylationPLFLTGVTFPSEYPI
CCEEECCCCCCCCCC
31.0426074081
100PhosphorylationLTGVTFPSEYPIYEE
EECCCCCCCCCCCCC
45.6426074081
102PhosphorylationGVTFPSEYPIYEETK
CCCCCCCCCCCCCCE
10.1626074081
105PhosphorylationFPSEYPIYEETKIKL
CCCCCCCCCCCEEEE
11.8326074081
108PhosphorylationEYPIYEETKIKLTVY
CCCCCCCCEEEEEEE
26.5726074081
113PhosphorylationEETKIKLTVYDVKDK
CCCEEEEEEEECCCC
16.4228102081
115PhosphorylationTKIKLTVYDVKDKSH
CEEEEEEEECCCCCC
15.1328102081
121PhosphorylationVYDVKDKSHDTVRTS
EEECCCCCCCCEEEC
36.41-
147PhosphorylationVGRSFLGYASFKVGE
CCHHHHHHHHHHHHH
10.96-
149PhosphorylationRSFLGYASFKVGELL
HHHHHHHHHHHHHHH
19.6724719451
198PhosphorylationDGEADHITTDVQGQK
CCCCCCEEECCCCCE
17.3318452278
237UbiquitinationVLKNPVCKLYRFPTS
HHCCCCCEEEECCCC
49.11-
270PhosphorylationHIPKELISLHIKEDL
CCCHHHHHHHHHHHH
26.90-
290PhosphorylationIKELGELSPHWDNLR
HHHHHHCCCCHHHHH
15.4923898821
353PhosphorylationLQRMQVHSPHLKDAL
EEECCCCCHHHHHHH
18.37-
361PhosphorylationPHLKDALYDVITVGA
HHHHHHHHHHEECCC
15.1927642862
397PhosphorylationTERRNTGYQFIYYSP
HCCCCCCCEEEEECC
9.7527642862
401PhosphorylationNTGYQFIYYSPENTA
CCCCEEEEECCCCHH
10.1227642862
448AcetylationDSLKNSLKMLSEKTE
HHHHHHHHHHHHHHH
37.3020167786
4622-HydroxyisobutyrylationELFVHAFKDQLVRSA
HHHHHHHHHHHHHHH
45.40-
468PhosphorylationFKDQLVRSALLALYT
HHHHHHHHHHHHHHH
18.78-
487PhosphorylationGILKKPPSPKSSTEE
CCCCCCCCCCCCCCC
54.1928176443
490PhosphorylationKKPPSPKSSTEESSP
CCCCCCCCCCCCCCC
45.9728270605
491PhosphorylationKPPSPKSSTEESSPQ
CCCCCCCCCCCCCCC
46.0628270605
492PhosphorylationPPSPKSSTEESSPQD
CCCCCCCCCCCCCCC
51.3628270605
495PhosphorylationPKSSTEESSPQDQPP
CCCCCCCCCCCCCCC
40.8830278072
496PhosphorylationKSSTEESSPQDQPPV
CCCCCCCCCCCCCCC
29.8425849741
509PhosphorylationPVMRGQDSIPHHSDY
CCCCCCCCCCCCCCC
30.0823401153
516PhosphorylationSIPHHSDYDEEEWDR
CCCCCCCCCHHHHHH
28.4127642862
552PhosphorylationRDGGSEGSGGNNDGE
CCCCCCCCCCCCCCC
39.2025056879
563PhosphorylationNDGEKEPSLTDAIPS
CCCCCCCCHHHCCCC
45.0227251275
565PhosphorylationGEKEPSLTDAIPSHP
CCCCCCHHHCCCCCC
27.9427251275
601PhosphorylationVVNRAKQSLTFVLLQ
HHHHHHHHHHHHHHH
28.7724043423
603PhosphorylationNRAKQSLTFVLLQEL
HHHHHHHHHHHHHHH
19.5624043423
612PhosphorylationVLLQELAYSLPQCLM
HHHHHHHHCHHHHHH
24.3024043423
613PhosphorylationLLQELAYSLPQCLML
HHHHHHHCHHHHHHH
28.1524043423
621PhosphorylationLPQCLMLTLRRDIVF
HHHHHHHHHHHHHHH
12.3123532336
629PhosphorylationLRRDIVFSQALAGLV
HHHHHHHHHHHHHHH
12.0325404012
792PhosphorylationMEKMPPDYISHFQEQ
HHHCCHHHHHHHHHH
15.3117322306
794PhosphorylationKMPPDYISHFQEQND
HCCHHHHHHHHHHHH
16.4217322306
898PhosphorylationKNIKCRKYAFNMLQL
HHCCCHHHHHHHHHH
9.3222817900
919PhosphorylationYRPPEGTYGKADT--
CCCCCCCCCCCCC--
27.7327642862

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 INP4B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INP4B_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 INP4B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of INP4B_HUMAN !!

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 INP4B_HUMAN

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Related Literatures of Post-Translational Modification

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