LMBL2_HUMAN - dbPTM
LMBL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMBL2_HUMAN
UniProt AC Q969R5
Protein Name Lethal(3)malignant brain tumor-like protein 2
Gene Name L3MBTL2
Organism Homo sapiens (Human).
Sequence Length 705
Subcellular Localization Nucleus .
Protein Description Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'..
Protein Sequence MEKPRSIEETPSSEPMEEEEDDDLELFGGYDSFRSYNSSVGSESSSYLEESSEAENEDREAGELPTSPLHLLSPGTPRSLDGSGSEPAVCEMCGIVGTREAFFSKTKRFCSVSCSRSYSSNSKKASILARLQGKPPTKKAKVLHKAAWSAKIGAFLHSQGTGQLADGTPTGQDALVLGFDWGKFLKDHSYKAAPVSCFKHVPLYDQWEDVMKGMKVEVLNSDAVLPSRVYWIASVIQTAGYRVLLRYEGFENDASHDFWCNLGTVDVHPIGWCAINSKILVPPRTIHAKFTDWKGYLMKRLVGSRTLPVDFHIKMVESMKYPFRQGMRLEVVDKSQVSRTRMAVVDTVIGGRLRLLYEDGDSDDDFWCHMWSPLIHPVGWSRRVGHGIKMSERRSDMAHHPTFRKIYCDAVPYLFKKVRAVYTEGGWFEEGMKLEAIDPLNLGNICVATVCKVLLDGYLMICVDGGPSTDGLDWFCYHASSHAIFPATFCQKNDIELTPPKGYEAQTFNWENYLEKTKSKAAPSRLFNMDCPNHGFKVGMKLEAVDLMEPRLICVATVKRVVHRLLSIHFDGWDSEYDQWVDCESPDIYPVGWCELTGYQLQPPVAAEPATPLKAKEATKKKKKQFGKKRKRIPPTKTRPLRQGSKKPLLEDDPQGARKISSEPVPGEIIAVRVKEEHLDVASPDKASSPELPVSVENIKQETDD
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
6Phosphorylation--MEKPRSIEETPSS
--CCCCCCCCCCCCC		42.7630177828
10 (in isoform 2)Phosphorylation-18.71-
10PhosphorylationKPRSIEETPSSEPME
CCCCCCCCCCCCCCC		18.7127251275
12PhosphorylationRSIEETPSSEPMEEE
CCCCCCCCCCCCCCC		55.5426657352
12 (in isoform 2)Phosphorylation-55.54-
13 (in isoform 2)Phosphorylation-47.09-
13PhosphorylationSIEETPSSEPMEEEE
CCCCCCCCCCCCCCC		47.0918669648
30PhosphorylationDLELFGGYDSFRSYN
CCHHHCCCHHHHHCC		14.5930576142
36PhosphorylationGYDSFRSYNSSVGSE
CCHHHHHCCCCCCCC		18.1430576142
38PhosphorylationDSFRSYNSSVGSESS
HHHHHCCCCCCCCCH		20.4030576142
42PhosphorylationSYNSSVGSESSSYLE
HCCCCCCCCCHHHHH		31.9530576142
44PhosphorylationNSSVGSESSSYLEES
CCCCCCCCHHHHHHC		26.7030576142
45PhosphorylationSSVGSESSSYLEESS
CCCCCCCHHHHHHCC		20.9630576142
52PhosphorylationSSYLEESSEAENEDR
HHHHHHCCHHCCCCH		44.0730576142
66PhosphorylationREAGELPTSPLHLLS
HHCCCCCCCCCEECC		56.4525463755
66 (in isoform 2)Phosphorylation-56.45-
67 (in isoform 2)Phosphorylation-24.43-
67PhosphorylationEAGELPTSPLHLLSP
HCCCCCCCCCEECCC		24.4330266825
73PhosphorylationTSPLHLLSPGTPRSL
CCCCEECCCCCCCCC		27.8730266825
76PhosphorylationLHLLSPGTPRSLDGS
CEECCCCCCCCCCCC		20.9325463755
79 (in isoform 2)Phosphorylation-31.83-
79PhosphorylationLSPGTPRSLDGSGSE
CCCCCCCCCCCCCCC		31.8325159151
83PhosphorylationTPRSLDGSGSEPAVC
CCCCCCCCCCCCHHH		38.5223927012
85PhosphorylationRSLDGSGSEPAVCEM
CCCCCCCCCCHHHHH		41.9523927012
98PhosphorylationEMCGIVGTREAFFSK
HHCCCEECHHHHHHC		17.9123927012
104PhosphorylationGTREAFFSKTKRFCS
ECHHHHHHCCCEEEE		32.7221815630
106O-linked_GlycosylationREAFFSKTKRFCSVS
HHHHHHCCCEEEEEE		26.6730379171
117PhosphorylationCSVSCSRSYSSNSKK
EEEECCCCCCCCCCH		17.05-
120PhosphorylationSCSRSYSSNSKKASI
ECCCCCCCCCCHHHH		36.57-
124UbiquitinationSYSSNSKKASILARL
CCCCCCCHHHHHHHH		47.38-
126PhosphorylationSSNSKKASILARLQG
CCCCCHHHHHHHHCC		27.3224719451
145UbiquitinationKKAKVLHKAAWSAKI
HHHHHHHHHHHHHHH		35.32-
186UbiquitinationFDWGKFLKDHSYKAA
ECHHHHHHHCCCCCC		57.43-
191UbiquitinationFLKDHSYKAAPVSCF
HHHHCCCCCCCCCHH		40.88-
221PhosphorylationMKVEVLNSDAVLPSR
CEEEEECCCCCCHHH		23.84-
227PhosphorylationNSDAVLPSRVYWIAS
CCCCCCHHHHHHHHH		30.16-
230PhosphorylationAVLPSRVYWIASVIQ
CCCHHHHHHHHHHHH		7.03-
289UbiquitinationPPRTIHAKFTDWKGY
CCCEEEEECCCCHHH		34.33-
294UbiquitinationHAKFTDWKGYLMKRL
EEECCCCHHHHHHHH		40.25-
304PhosphorylationLMKRLVGSRTLPVDF
HHHHHHCCCCCCCEE		18.02-
306PhosphorylationKRLVGSRTLPVDFHI
HHHHCCCCCCCEEEE		36.7920860994
318PhosphorylationFHIKMVESMKYPFRQ
EEEHHHHHCCCCCCC		14.7920860994
320UbiquitinationIKMVESMKYPFRQGM
EHHHHHCCCCCCCCC		60.08-
321PhosphorylationKMVESMKYPFRQGMR
HHHHHCCCCCCCCCE		10.0424719451
335PhosphorylationRLEVVDKSQVSRTRM
EEEEECHHHCCCCEE		31.2023025827
338PhosphorylationVVDKSQVSRTRMAVV
EECHHHCCCCEEEEE		21.9423025827
347PhosphorylationTRMAVVDTVIGGRLR
CEEEEEEHHHCCEEE		11.4726356563
395PhosphorylationIKMSERRSDMAHHPT
CCCCHHCCCCCCCCH		37.6528555341
405UbiquitinationAHHPTFRKIYCDAVP
CCCCHHHHHHCCHHH		33.56-
405SumoylationAHHPTFRKIYCDAVP
CCCCHHHHHHCCHHH		33.5628112733
501UbiquitinationDIELTPPKGYEAQTF
CCCCCCCCCCCCEEC		75.28-
516UbiquitinationNWENYLEKTKSKAAP
CHHHHHHHHCCCCCC		59.67-
517PhosphorylationWENYLEKTKSKAAPS
HHHHHHHHCCCCCCH		31.0426657352
519PhosphorylationNYLEKTKSKAAPSRL
HHHHHHCCCCCCHHH		32.5326657352
524PhosphorylationTKSKAAPSRLFNMDC
HCCCCCCHHHHCCCC		36.5726657352
537UbiquitinationDCPNHGFKVGMKLEA
CCCCCCCCCCCEEEE		42.33-
541UbiquitinationHGFKVGMKLEAVDLM
CCCCCCCEEEEEECC		36.93-
611PhosphorylationPVAAEPATPLKAKEA
CCCCCCCCCCCHHHH		39.6126074081
647SumoylationPLRQGSKKPLLEDDP
CCCCCCCCCCCCCCC		42.4628112733
647UbiquitinationPLRQGSKKPLLEDDP
CCCCCCCCCCCCCCC		42.46-
647AcetylationPLRQGSKKPLLEDDP
CCCCCCCCCCCCCCC		42.4626822725
659SumoylationDDPQGARKISSEPVP
CCCCCCCCCCCCCCC		46.5428112733
659UbiquitinationDDPQGARKISSEPVP
CCCCCCCCCCCCCCC		46.54-
661PhosphorylationPQGARKISSEPVPGE
CCCCCCCCCCCCCCC		31.5130108239
662PhosphorylationQGARKISSEPVPGEI
CCCCCCCCCCCCCCE		49.7630108239
675SumoylationEIIAVRVKEEHLDVA
CEEEEEEEHHHCCCC		46.9828112733
675SumoylationEIIAVRVKEEHLDVA
CEEEEEEEHHHCCCC		46.98-
683PhosphorylationEEHLDVASPDKASSP
HHHCCCCCCCCCCCC		33.2230266825
688PhosphorylationVASPDKASSPELPVS
CCCCCCCCCCCCCCC		52.7629255136
689PhosphorylationASPDKASSPELPVSV
CCCCCCCCCCCCCCH		27.5329255136
695PhosphorylationSSPELPVSVENIKQE
CCCCCCCCHHHHHHH		23.0530266825
700SumoylationPVSVENIKQETDD--
CCCHHHHHHHCCC--		54.3825114211
700SumoylationPVSVENIKQETDD--
CCCHHHHHHHCCC--		54.38-
703PhosphorylationVENIKQETDD-----
HHHHHHHCCC-----		42.8724144214
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
335SPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMBL2_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 LMBL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_HUMANRB1physical
17540172
CBX3_HUMANCBX3physical
17540172
HDAC3_HUMANHDAC3physical
20385135
E2F6_HUMANE2F6physical
21596310
CBX3_HUMANCBX3physical
21596310
RING2_HUMANRNF2physical
21596310
H31T_HUMANHIST3H3physical
21596310
PCGF6_HUMANPCGF6physical
21596310
MPP3_HUMANMPP3physical
21988832
STAC3_HUMANSTAC3physical
25416956
TRI42_HUMANTRIM42physical
25416956
SSFA2_HUMANSSFA2physical
28514442
TFDP1_HUMANTFDP1physical
28514442
TFDP2_HUMANTFDP2physical
28514442
CIZ1_HUMANCIZ1physical
28514442
MGAP_HUMANMGAphysical
28514442
LIN54_HUMANLIN54physical
28514442
ITPR2_HUMANITPR2physical
28514442
RING2_HUMANRNF2physical
28514442
RING1_HUMANRING1physical
28514442
ZN296_HUMANZNF296physical
28514442
ITPR3_HUMANITPR3physical
28514442
MTA1_HUMANMTA1physical
28514442
MTA2_HUMANMTA2physical
28514442
MBD3_HUMANMBD3physical
28514442
UBE2O_HUMANUBE2Ophysical
28514442
P66B_HUMANGATAD2Bphysical
28514442
HDAC2_HUMANHDAC2physical
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 LMBL2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, AND MASSSPECTROMETRY.
"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-12; SER-13; SER-683;SER-688 AND SER-689, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66 AND THR-76, AND MASSSPECTROMETRY.

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