L2GL1_HUMAN - dbPTM
L2GL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID L2GL1_HUMAN
UniProt AC Q15334
Protein Name Lethal(2) giant larvae protein homolog 1
Gene Name LLGL1
Organism Homo sapiens (Human).
Sequence Length 1064
Subcellular Localization Early endosome membrane. Golgi apparatus, trans-Golgi network membrane. Golgi apparatus membrane. Cell projection, axon. Cytoplasm, cytoskeleton . Localized to the lateral membrane during the polarization and formation cell-cell contacts. Enriched in
Protein Description Cortical cytoskeleton protein found in a complex involved in maintaining cell polarity and epithelial integrity. Involved in the regulation of mitotic spindle orientation, proliferation, differentiation and tissue organization of neuroepithelial cells. Involved in axonogenesis through RAB10 activation thereby regulating vesicular membrane trafficking toward the axonal plasma membrane..
Protein Sequence MMKFRFRRQGADPQREKLKQELFAFNKTVEHGFPNQPSALAFDPELRIMAIGTRSGAVKIYGAPGVEFTGLHRDAATVTQMHFLTGQGRLLSLLDDSSLHLWEIVHHNGCAHLEEALSFQLPSRPGFDGASAPLSLTRVTVVLLVAASDIAALGTEGSSVFFLDVTTLTLLEGQTLAPGEVLRSVPDDYRCGKALGPVESLQGHLRDPTKILIGYSRGLLVIWNQASQCVDHIFLGNQQLESLCWGRDSSTVVSSHSDGSYAVWSVDAGSFPTLQPTVATTPYGPFPCKAINKILWRNCESGGHFIIFSGGMPRASYGDRHCVSVLRAETLVTLDFTSRIIDFFTVHSTRPEDEFDDPQALAVLLEEELVVLDLQTPGWPAVPAPYLAPLHSSAITCSAHVASVPAKLWARIVSAGEQQSPQPVSSALSWPITGGRNLAQEPSQRGLLLTGHEDGTVRFWDASGVALRPLYKLSTAGLFQTDCEHADSLAQAAEDDWPPFRKVGCFDPYSDDPRLGVQKVALCKYTAQMVVAGTAGQVLVLELSDVPVEQAVSVAIIDLLQDREGFTWKGHERLSPRTGPLPWPAGFQPRVLVQCLPPAAVTAVTLHTEWSLVAFGTSHGFGLFDYQRKSPVLARCTLHPNDSLAMEGPLSRVKSLKKSLRQSFRRIRKSRVSGKKRAANASSKLQEANAQLAEQACPHDVEMTPVQRRIEPRSADDSLSGVVRCLYFADTFLRDGAHHGPTMWAGTNSGSVFAYALEVPAAAVGGEKRPEQAVEAVLGKEVQLMHRAPVVAIAVLDGRGRPLPEPYEASRDLAQAPDMQGGHAVLIASEEQFKVFTLPKVSAKTKFKLTAHEGCRVRKVALATFASVACEDYAETCLACLTNLGDVHVFSVPGLRPQVHYSCIRKEDISGIASCVFTRHGQGFYLISPSEFERFSLSARNITEPLCSLDINWPRDATQASYRIRESPKLSQANGTPSILLAPQSLDGSPDPAHSMGPDTPEPPEAALSPMSIDSATSADTTLDTTGDVTVEDVKDFLGSSEESEKNLRNLAEDEAHACAILIK
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
17UbiquitinationGADPQREKLKQELFA
CCCHHHHHHHHHHHH		64.2723000965
19UbiquitinationDPQREKLKQELFAFN
CHHHHHHHHHHHHHH		53.4423000965
27UbiquitinationQELFAFNKTVEHGFP
HHHHHHHCCCCCCCC		47.7122817900
59UbiquitinationGTRSGAVKIYGAPGV
ECCCCCEEEECCCCC		29.67-
123O-linked_GlycosylationALSFQLPSRPGFDGA
HHHCCCCCCCCCCCC		60.7530379171
135PhosphorylationDGASAPLSLTRVTVV
CCCCCCCCCCHHHHH		27.0024719451
184PhosphorylationAPGEVLRSVPDDYRC
CCCCHHHCCCCCCCC		33.5624719451
288UbiquitinationTPYGPFPCKAINKIL
CCCCCCCCHHHHHHH		4.8122817900
289UbiquitinationPYGPFPCKAINKILW
CCCCCCCHHHHHHHE		53.1722817900
292UbiquitinationPFPCKAINKILWRNC
CCCCHHHHHHHEEEC		30.1221890473
293UbiquitinationFPCKAINKILWRNCE
CCCHHHHHHHEEECC		32.8221890473
414PhosphorylationKLWARIVSAGEQQSP
HHHHHHHHCCCCCCC		28.3425850435
420PhosphorylationVSAGEQQSPQPVSSA
HHCCCCCCCCCCHHH		25.7924076635
425PhosphorylationQQSPQPVSSALSWPI
CCCCCCCHHHHCCCC		19.3125850435
426PhosphorylationQSPQPVSSALSWPIT
CCCCCCHHHHCCCCC		33.2025850435
474PhosphorylationLRPLYKLSTAGLFQT
CEEEEEHHCCCCEEC		16.4428122231
475PhosphorylationRPLYKLSTAGLFQTD
EEEEEHHCCCCEECC		34.8728122231
481PhosphorylationSTAGLFQTDCEHADS
HCCCCEECCCCCHHH		34.9724719451
488PhosphorylationTDCEHADSLAQAAED
CCCCCHHHHHHHHHC		26.7925159151
502UbiquitinationDDWPPFRKVGCFDPY
CCCCCCCCCCCCCCC		43.2730230243
509PhosphorylationKVGCFDPYSDDPRLG
CCCCCCCCCCCCCCC		26.9525884760
510PhosphorylationVGCFDPYSDDPRLGV
CCCCCCCCCCCCCCH		40.7128152594
518UbiquitinationDDPRLGVQKVALCKY
CCCCCCHHHHHHHHH		32.4827667366
519UbiquitinationDPRLGVQKVALCKYT
CCCCCHHHHHHHHHE		27.3727667366
526PhosphorylationKVALCKYTAQMVVAG
HHHHHHHEEEEEEEC		8.9127251275
553PhosphorylationVPVEQAVSVAIIDLL
CCHHHHHHHHHHHHH		14.6227251275
567PhosphorylationLQDREGFTWKGHERL
HHCCCCCCCCCCCCC		36.80-
569UbiquitinationDREGFTWKGHERLSP
CCCCCCCCCCCCCCC		47.54-
575PhosphorylationWKGHERLSPRTGPLP
CCCCCCCCCCCCCCC		20.6826091039
630PhosphorylationLFDYQRKSPVLARCT
CCCCCCCCCEEEEEE		23.5624425749
637PhosphorylationSPVLARCTLHPNDSL
CCEEEEEEECCCCCC		23.6522210691
643PhosphorylationCTLHPNDSLAMEGPL
EEECCCCCCHHCCCH		25.3522210691
651PhosphorylationLAMEGPLSRVKSLKK
CHHCCCHHHHHHHHH		37.8522210691
655PhosphorylationGPLSRVKSLKKSLRQ
CCHHHHHHHHHHHHH		42.4329496963
657MethylationLSRVKSLKKSLRQSF
HHHHHHHHHHHHHHH		47.62-
659PhosphorylationRVKSLKKSLRQSFRR
HHHHHHHHHHHHHHH		27.4822167270
663PhosphorylationLKKSLRQSFRRIRKS
HHHHHHHHHHHHHHH		17.8130266825
670PhosphorylationSFRRIRKSRVSGKKR
HHHHHHHHHHHCHHH		28.24-
682PhosphorylationKKRAANASSKLQEAN
HHHHHHHHHHHHHHH		28.0125002506
683PhosphorylationKRAANASSKLQEANA
HHHHHHHHHHHHHHH		34.6725002506
683UbiquitinationKRAANASSKLQEANA
HHHHHHHHHHHHHHH		34.6721963094
684UbiquitinationRAANASSKLQEANAQ
HHHHHHHHHHHHHHH		52.2521963094
704PhosphorylationCPHDVEMTPVQRRIE
CCCCCCCCCCCCCCC		13.5521712546
780UbiquitinationAVEAVLGKEVQLMHR
HHHHHHCCHHHHHHC		51.0230230243
837PhosphorylationEEQFKVFTLPKVSAK
HHHEEEEEECCCCCC		45.1724719451
840UbiquitinationFKVFTLPKVSAKTKF
EEEEEECCCCCCCCE		52.51-
848UbiquitinationVSAKTKFKLTAHEGC
CCCCCCEEEECCCCC		46.6229967540
906UbiquitinationVHYSCIRKEDISGIA
EEEEEEEHHHCCEEE		39.57-
925PhosphorylationTRHGQGFYLISPSEF
EECCCEEEEECHHHH		15.2227642862
930PhosphorylationGFYLISPSEFERFSL
EEEEECHHHHHHEEE		48.39-
936PhosphorylationPSEFERFSLSARNIT
HHHHHHEEEECCCCC		27.8625954137
938PhosphorylationEFERFSLSARNITEP
HHHHEEEECCCCCCC		24.8025278378
947GlutathionylationRNITEPLCSLDINWP
CCCCCCCEECCCCCC		5.7822555962
958PhosphorylationINWPRDATQASYRIR
CCCCCCCHHHHHHHH		29.0227251275
961PhosphorylationPRDATQASYRIRESP
CCCCHHHHHHHHCCC		12.7226699800
962PhosphorylationRDATQASYRIRESPK
CCCHHHHHHHHCCCC		17.0527251275
967PhosphorylationASYRIRESPKLSQAN
HHHHHHCCCCHHHCC		19.9321406692
985PhosphorylationSILLAPQSLDGSPDP
EEEECCCCCCCCCCC		27.63-
1040PhosphorylationDVKDFLGSSEESEKN
HHHHHHCCCHHHHHH		36.4022199227
1041PhosphorylationVKDFLGSSEESEKNL
HHHHHCCCHHHHHHH		43.5122199227
1044UbiquitinationFLGSSEESEKNLRNL
HHCCCHHHHHHHHHH		50.2323000965
1044PhosphorylationFLGSSEESEKNLRNL
HHCCCHHHHHHHHHH		50.2326657352
1046UbiquitinationGSSEESEKNLRNLAE
CCCHHHHHHHHHHHH		71.2423000965
1059GlutathionylationAEDEAHACAILIK--
HHHHHHHHHHCCC--		1.4122555962
1066UbiquitinationCAILIK---------
HHHCCC---------		23000965
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
663SPhosphorylationKinasePRKCIQ62074
GPS
-KUbiquitinationE3 ubiquitin ligaseUBE3AQ05086
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
663SPhosphorylation

12725730
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 L2GL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RANB9_HUMANRANBP9physical
20829363
KPCI_HUMANPRKCIphysical
26344197
AL1B1_HUMANALDH1B1physical
26496610
COPB_HUMANCOPB1physical
26496610
HD_HUMANHTTphysical
26496610
KPCI_HUMANPRKCIphysical
26496610
STX3_HUMANSTX3physical
26496610
TRIB1_HUMANTRIB1physical
26496610
TIM13_HUMANTIMM13physical
26496610
PAR6B_HUMANPARD6Bphysical
26496610
SPB12_HUMANSERPINB12physical
26496610
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 L2GL1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Mammalian Lgl forms a protein complex with PAR-6 and aPKCindependently of PAR-3 to regulate epithelial cell polarity.";
Yamanaka T., Horikoshi Y., Sugiyama Y., Ishiyama C., Suzuki A.,Hirose T., Iwamatsu A., Shinohara A., Ohno S.;
Curr. Biol. 13:734-743(2003).
Cited for: INTERACTION WITH PARD6B/PAR-6 AND PRKCI/APKC, SUBCELLULAR LOCATION,AND PHOSPHORYLATION AT SER-663.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-704, AND MASSSPECTROMETRY.
"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-509, AND MASSSPECTROMETRY.

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