LAP4B_HUMAN - dbPTM
LAP4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAP4B_HUMAN
UniProt AC Q86VI4
Protein Name Lysosomal-associated transmembrane protein 4B {ECO:0000305}
Gene Name LAPTM4B {ECO:0000312|HGNC:HGNC:13646}
Organism Homo sapiens (Human).
Sequence Length 370
Subcellular Localization Endomembrane system
Multi-pass membrane protein . Late endosome membrane . Cell membrane . Cell projection . Lysosome membrane . Endosome membrane. Endosome, multivesicular body membrane . Endosome, multivesicular body lumen .
Protein Description Required for optimal lysosomal function. [PubMed: 21224396 Blocks EGF-stimulated EGFR intraluminal sorting and degradation. Conversely by binding with the phosphatidylinositol 4,5-bisphosphate, regulates its PIP5K1C interaction, inhibits HGS ubiquitination and relieves LAPTM4B inhibition of EGFR degradation]
Protein Sequence MELHERPDERRKARTSTQGRLGDWRRVHADGFTHRVLGAPAAAWSSSSWLEPAMTSRTRVTWPSPPRPLPVPAAAAVAFGAKGTDPAEARSSRGIEEAGPRAHGRAGREPERRRSRQQRRGGLQARRSTLLKTCARARATAPGAMKMVAPWTRFYSNSCCLCCHVRTGTILLGVWYLIINAVVLLILLSALADPDQYNFSSSELGGDFEFMDDANMCIAIAISLLMILICAMATYGAYKQRAAWIIPFFCYQIFDFALNMLVAITVLIYPNSIQEYIRQLPPNFPYRDDVMSVNPTCLVLIILLFISIILTFKGYLISCVWNCYRYINGRNSSDVLVYVTSNDTTVLLPPYDDATVNGAAKEPPPPYVSA
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
2 (in isoform 2)Ubiquitination-59.85-
15PhosphorylationDERRKARTSTQGRLG
HHHHHCCCCCCCCCC
40.7724425749
16PhosphorylationERRKARTSTQGRLGD
HHHHCCCCCCCCCCC
17.1223532336
17PhosphorylationRRKARTSTQGRLGDW
HHHCCCCCCCCCCCC
34.1423532336
64PhosphorylationRTRVTWPSPPRPLPV
CCEEECCCCCCCCCC
38.8117081983
93UbiquitinationPAEARSSRGIEEAGP
HHHHHHHCCCHHHCC
51.8927667366
146UbiquitinationATAPGAMKMVAPWTR
CCCCCHHHHHCCCHH
29.68-
159S-palmitoylationTRFYSNSCCLCCHVR
HHHCCCCEEHHHCCC
2.1029575903
160S-palmitoylationRFYSNSCCLCCHVRT
HHCCCCEEHHHCCCC
3.0629575903
162S-palmitoylationYSNSCCLCCHVRTGT
CCCCEEHHHCCCCCC
0.6629575903
163S-palmitoylationSNSCCLCCHVRTGTI
CCCEEHHHCCCCCCH
1.8329575903
286PhosphorylationQLPPNFPYRDDVMSV
CCCCCCCCCCCCCCC
23.65-
367PhosphorylationAKEPPPPYVSA----
CCCCCCCCCCC----
16.8925884760

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 LAP4B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAP4B_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 LAP4B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TFR1_HUMANTFRCphysical
22096579
NADL2_HUMANNAALADL2physical
25416956
PI51C_HUMANPIP5K1Cphysical
25588945
HGS_HUMANHGSphysical
25588945
NEDD4_HUMANNEDD4physical
25588945
SNX5_HUMANSNX5physical
25588945

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 LAP4B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-367, AND MASSSPECTROMETRY.

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