L2GL2_HUMAN - dbPTM
L2GL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID L2GL2_HUMAN
UniProt AC Q6P1M3
Protein Name Lethal(2) giant larvae protein homolog 2
Gene Name LLGL2
Organism Homo sapiens (Human).
Sequence Length 1020
Subcellular Localization Cytoplasm . Localized in the perinuclear structure and faintly at the cell-cell contacts sites in the interphase. Localized at the cell periphery during metaphase. Cortical localization in mitotic cells. Found in the lateral region of polarized epith
Protein Description Part of a complex with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-6, which may ensure the correct organization and orientation of bipolar spindles for normal cell division. This complex plays roles in the initial phase of the establishment of epithelial cell polarity..
Protein Sequence MRRFLRPGHDPVRERLKRDLFQFNKTVEHGFPHQPSALGYSPSLRILAIGTRSGAIKLYGAPGVEFMGLHQENNAVTQIHLLPGQCQLVTLLDDNSLHLWSLKVKGGASELQEDESFTLRGPPGAAPSATQITVVLPHSSCELLYLGTESGNVFVVQLPAFRALEDRTISSDAVLQRLPEEARHRRVFEMVEALQEHPRDPNQILIGYSRGLVVIWDLQGSRVLYHFLSSQQLENIWWQRDGRLLVSCHSDGSYCQWPVSSEAQQPEPLRSLVPYGPFPCKAITRILWLTTRQGLPFTIFQGGMPRASYGDRHCISVIHDGQQTAFDFTSRVIGFTVLTEADPAATFDDPYALVVLAEEELVVIDLQTAGWPPVQLPYLASLHCSAITCSHHVSNIPLKLWERIIAAGSRQNAHFSTMEWPIDGGTSLTPAPPQRDLLLTGHEDGTVRFWDASGVCLRLLYKLSTVRVFLTDTDPNENFSAQGEDEWPPLRKVGSFDPYSDDPRLGIQKIFLCKYSGYLAVAGTAGQVLVLELNDEAAEQAVEQVEADLLQDQEGYRWKGHERLAARSGPVRFEPGFQPFVLVQCQPPAVVTSLALHSEWRLVAFGTSHGFGLFDHQQRRQVFVKCTLHPSDQLALEGPLSRVKSLKKSLRQSFRRMRRSRVSSRKRHPAGPPGEAQEGSAKAERPGLQNMELAPVQRKIEARSAEDSFTGFVRTLYFADTYLKDSSRHCPSLWAGTNGGTIYAFSLRVPPAERRMDEPVRAEQAKEIQLMHRAPVVGILVLDGHSVPLPEPLEVAHDLSKSPDMQGSHQLLVVSEEQFKVFTLPKVSAKLKLKLTALEGSRVRRVSVAHFGSRRAEDYGEHHLAVLTNLGDIQVVSLPLLKPQVRYSCIRREDVSGIASCVFTKYGQGFYLISPSEFERFSLSTKWLVEPRCLVDSAETKNHRPGNGAGPKKAPSRARNSGTQSDGEEKQPGLVMERALLSDERVLKEIQSTLEGDRGSGNWRSHRAAVGCSLSNGGAE
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
25UbiquitinationRDLFQFNKTVEHGFP
HHHHHHCCCCCCCCC
56.06-
26PhosphorylationDLFQFNKTVEHGFPH
HHHHHCCCCCCCCCC
32.03-
36PhosphorylationHGFPHQPSALGYSPS
CCCCCCCCCCCCCCC
29.56-
40PhosphorylationHQPSALGYSPSLRIL
CCCCCCCCCCCEEEE
20.47-
105UbiquitinationHLWSLKVKGGASELQ
EEEEEEEECCCCCCC
50.4621906983
105 (in isoform 3)Ubiquitination-50.4621906983
105 (in isoform 2)Ubiquitination-50.4621890473
105 (in isoform 1)Ubiquitination-50.4621890473
118PhosphorylationLQEDESFTLRGPPGA
CCCCCCEEECCCCCC
25.4824719451
253PhosphorylationVSCHSDGSYCQWPVS
EEEECCCCCCCCCCC
27.94-
275PhosphorylationPLRSLVPYGPFPCKA
CHHHCCCCCCCCHHH
29.9228509920
281UbiquitinationPYGPFPCKAITRILW
CCCCCCHHHHHHHHH
42.96-
284PhosphorylationPFPCKAITRILWLTT
CCCHHHHHHHHHEEC
19.2728509920
453PhosphorylationTVRFWDASGVCLRLL
CEEEEEHHHHHHHHH
29.3227251275
471PhosphorylationSTVRVFLTDTDPNEN
CEEEEEECCCCCCCC
25.9523663014
473PhosphorylationVRVFLTDTDPNENFS
EEEEECCCCCCCCCC
48.3923663014
480PhosphorylationTDPNENFSAQGEDEW
CCCCCCCCCCCCCCC
31.1228355574
492UbiquitinationDEWPPLRKVGSFDPY
CCCCCCCCCCCCCCC
59.64-
495PhosphorylationPPLRKVGSFDPYSDD
CCCCCCCCCCCCCCC
29.4828857561
499PhosphorylationKVGSFDPYSDDPRLG
CCCCCCCCCCCCCCC
26.9527273156
500PhosphorylationVGSFDPYSDDPRLGI
CCCCCCCCCCCCCCC
40.7128152594
625 (in isoform 1)Ubiquitination-15.2721890473
625 (in isoform 2)Ubiquitination-15.2721890473
625UbiquitinationQRRQVFVKCTLHPSD
HHCEEEEEEEECHHH
15.2721890473
625MethylationQRRQVFVKCTLHPSD
HHCEEEEEEEECHHH
15.2744493853
627PhosphorylationRQVFVKCTLHPSDQL
CEEEEEEEECHHHHH
23.5322210691
645PhosphorylationGPLSRVKSLKKSLRQ
CCHHHHHHHHHHHHH
42.4324719451
647MethylationLSRVKSLKKSLRQSF
HHHHHHHHHHHHHHH
47.62-
649PhosphorylationRVKSLKKSLRQSFRR
HHHHHHHHHHHHHHH
27.4822167270
653PhosphorylationLKKSLRQSFRRMRRS
HHHHHHHHHHHHHHH
17.8130266825
660PhosphorylationSFRRMRRSRVSSRKR
HHHHHHHHHHHHCCC
27.0324719451
663PhosphorylationRMRRSRVSSRKRHPA
HHHHHHHHHCCCCCC
24.2624719451
666 (in isoform 2)Ubiquitination-57.94-
666UbiquitinationRSRVSSRKRHPAGPP
HHHHHHCCCCCCCCC
57.94-
680PhosphorylationPGEAQEGSAKAERPG
CCCCCCCCCCCCCCC
26.3325159151
682UbiquitinationEAQEGSAKAERPGLQ
CCCCCCCCCCCCCCC
53.10-
704PhosphorylationQRKIEARSAEDSFTG
HHHHHHHHHCHHHHH
42.9525849741
708PhosphorylationEARSAEDSFTGFVRT
HHHHHCHHHHHHHHH
19.0628857561
724 (in isoform 2)Ubiquitination-45.1921890473
724 (in isoform 1)Ubiquitination-45.1921890473
724UbiquitinationYFADTYLKDSSRHCP
HCCCCCCCCCCCCCC
45.1921890473
726PhosphorylationADTYLKDSSRHCPSL
CCCCCCCCCCCCCEE
27.9024719451
732PhosphorylationDSSRHCPSLWAGTNG
CCCCCCCEEEEECCC
41.7724719451
737PhosphorylationCPSLWAGTNGGTIYA
CCEEEEECCCCEEEE
23.9621712546
741PhosphorylationWAGTNGGTIYAFSLR
EEECCCCEEEEEEEE
16.5321712546
802PhosphorylationVAHDLSKSPDMQGSH
HHCCCCCCCCCCCCC
23.8225159151
823PhosphorylationEEQFKVFTLPKVSAK
HHHEEEEECCCCCCE
45.1724719451
826UbiquitinationFKVFTLPKVSAKLKL
EEEEECCCCCCEEEE
52.51-
847PhosphorylationGSRVRRVSVAHFGSR
CCEEEEEEEEECCCC
16.2725849741
853PhosphorylationVSVAHFGSRRAEDYG
EEEEECCCCCHHHCC
20.0428348404
916PhosphorylationGFYLISPSEFERFSL
EEEEECHHHHCCCEE
48.39-
926 (in isoform 2)Ubiquitination-34.84-
961PhosphorylationAPSRARNSGTQSDGE
CCCCCCCCCCCCCCC
37.3530266825
963PhosphorylationSRARNSGTQSDGEEK
CCCCCCCCCCCCCCC
25.4030266825
965PhosphorylationARNSGTQSDGEEKQP
CCCCCCCCCCCCCCC
47.6323401153
965 (in isoform 2)Phosphorylation-47.63-
970UbiquitinationTQSDGEEKQPGLVME
CCCCCCCCCCCHHHH
58.452190698
970 (in isoform 1)Ubiquitination-58.4521890473
970 (in isoform 2)Ubiquitination-58.4521890473
982PhosphorylationVMERALLSDERVLKE
HHHHHHHCCHHHHHH
37.9724719451
988UbiquitinationLSDERVLKEIQSTLE
HCCHHHHHHHHHHHC
50.33-
992PhosphorylationRVLKEIQSTLEGDRG
HHHHHHHHHHCCCCC
40.3929978859
993PhosphorylationVLKEIQSTLEGDRGS
HHHHHHHHHCCCCCC
16.6829978859
1000PhosphorylationTLEGDRGSGNWRSHR
HHCCCCCCCCCCCCC
29.8225159151
1013PhosphorylationHRAAVGCSLSNGGAE
CCEECCCCCCCCCCC
28.9825159151
1015PhosphorylationAAVGCSLSNGGAE--
EECCCCCCCCCCC--
19.6930278072

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
653SPhosphorylationKinasePRKCIQ62074
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
653SPhosphorylation

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 L2GL2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAR6A_HUMANPARD6Aphysical
20360068
KPCI_HUMANPRKCIphysical
20360068
PAR6B_HUMANPARD6Bphysical
20360068
L2GL2_HUMANLLGL2physical
20360068
BAG5_HUMANBAG5physical
24366813
CHIP_HUMANSTUB1physical
24366813
DNJA1_HUMANDNAJA1physical
24366813
DNJA2_HUMANDNAJA2physical
24366813
DNJB1_HUMANDNAJB1physical
24366813
KBTB7_HUMANKBTBD7physical
24366813
KPCI_HUMANPRKCIphysical
24366813
KPCZ_HUMANPRKCZphysical
24366813
L2GL2_HUMANLLGL2physical
24366813
NUDC_HUMANNUDCphysical
24366813
PAR6B_HUMANPARD6Bphysical
24366813
PAR6G_HUMANPARD6Gphysical
24366813
RAD18_HUMANRAD18physical
24366813
SQSTM_HUMANSQSTM1physical
24366813
SGT1_HUMANSUGT1physical
24366813
TIM13_HUMANTIMM13physical
24366813
PAR6A_HUMANPARD6Aphysical
26344197
CCNB1_HUMANCCNB1physical
26496610
LYST_HUMANLYSTphysical
26496610
ATF2_HUMANATF2physical
26496610
BPTF_HUMANBPTFphysical
26496610
MTOR_HUMANMTORphysical
26496610
M3K1_HUMANMAP3K1physical
26496610
KPCI_HUMANPRKCIphysical
26496610
P5CS_HUMANALDH18A1physical
26496610
RBBP6_HUMANRBBP6physical
26496610
ST5_HUMANST5physical
26496610
SVIL_HUMANSVILphysical
26496610
TAF9_HUMANTAF9physical
26496610
SF01_HUMANSF1physical
26496610
BAG6_HUMANBAG6physical
26496610
MKNK1_HUMANMKNK1physical
26496610
EXO1_HUMANEXO1physical
26496610
NOLC1_HUMANNOLC1physical
26496610
ZNHI3_HUMANZNHIT3physical
26496610
DCAF1_HUMANVPRBPphysical
26496610
HMGX4_HUMANHMGXB4physical
26496610
DNM1L_HUMANDNM1Lphysical
26496610
ABCA7_HUMANABCA7physical
26496610
CASC3_HUMANCASC3physical
26496610
PALLD_HUMANPALLDphysical
26496610
ZC3H3_HUMANZC3H3physical
26496610
K0556_HUMANKIAA0556physical
26496610
DAPK2_HUMANDAPK2physical
26496610
ATP5S_HUMANATP5Sphysical
26496610
PAR6A_HUMANPARD6Aphysical
26496610
ECSIT_HUMANECSITphysical
26496610
PF21A_HUMANPHF21Aphysical
26496610
E41LB_HUMANEPB41L4Bphysical
26496610
CK057_HUMANC11orf57physical
26496610
IMP3_HUMANIMP3physical
26496610
IMPCT_HUMANIMPACTphysical
26496610
IWS1_HUMANIWS1physical
26496610
BRE1A_HUMANRNF20physical
26496610
BIRC6_HUMANBIRC6physical
26496610
PKHG1_HUMANPLEKHG1physical
26496610
RBM26_HUMANRBM26physical
26496610
PHAR4_HUMANPHACTR4physical
26496610
BHE41_HUMANBHLHE41physical
26496610
GCC1_HUMANGCC1physical
26496610
ZN668_HUMANZNF668physical
26496610
LNP_HUMANKIAA1715physical
26496610
FIP1_HUMANFIP1L1physical
26496610
C99L2_HUMANCD99L2physical
26496610
PAR6B_HUMANPARD6Bphysical
26496610
ZN707_HUMANZNF707physical
26496610
FMN1_HUMANFMN1physical
26496610
RAD18_HUMANRAD18physical
28514442
PAR6G_HUMANPARD6Gphysical
28514442
BRWD3_HUMANBRWD3physical
28514442
PKCB1_HUMANZMYND8physical
28514442
GSE1_HUMANGSE1physical
28514442
KPCI_HUMANPRKCIphysical
28514442
DCAF1_HUMANVPRBPphysical
28514442
ZN592_HUMANZNF592physical
28514442
TOPRS_HUMANTOPORSphysical
28514442
CATIN_HUMANCACTINphysical
28514442
ZN687_HUMANZNF687physical
28514442
LIPA1_HUMANPPFIA1physical
28514442
DDA1_HUMANDDA1physical
28514442
TRI26_HUMANTRIM26physical
28514442
C1QBP_HUMANC1QBPphysical
28514442
HM20A_HUMANHMG20Aphysical
28514442
UBE2O_HUMANUBE2Ophysical
28514442
CR025_HUMANC18orf25physical
28514442
NKTR_HUMANNKTRphysical
28514442
HM20B_HUMANHMG20Bphysical
28514442
NKAP_HUMANNKAPphysical
28514442
RCOR3_HUMANRCOR3physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
KBTB6_HUMANKBTBD6physical
28514442
UBE2A_HUMANUBE2Aphysical
28514442
NEK7_HUMANNEK7physical
28514442
RCOR1_HUMANRCOR1physical
28514442
NOG1_HUMANGTPBP4physical
28514442
TR150_HUMANTHRAP3physical
28514442
DIEXF_HUMANDIEXFphysical
28514442

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 L2GL2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1015, AND MASSSPECTROMETRY.
"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, PHOSPHORYLATION ATSER-653, AND MUTAGENESIS OF SER-641; SER-645; SER-649; SER-653;SER-660 AND SER-663.

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