LMBL3_HUMAN - dbPTM
LMBL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMBL3_HUMAN
UniProt AC Q96JM7
Protein Name Lethal(3)malignant brain tumor-like protein 3
Gene Name L3MBTL3
Organism Homo sapiens (Human).
Sequence Length 780
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. Required for normal maturation of myeloid progenitor cells (By similarity)..
Protein Sequence MTESASSTSGQEFDVFSVMDWKDGVGTLPGSDLKFRVNEFGALEVITDENEMENVKKATATTTWMVPTAQEAPTSPPSSRPVFPPAYWTSPPGCPTVFSEKTGMPFRLKDPVKVEGLQFCENCCQYGNVDECLSGGNYCSQNCARHIKDKDQKEERDVEEDNEEEDPKCSRKKKPKLSLKADTKEDGEERDDEMENKQDVRILRGSQRARRKRRGDSAVLKQGLPPKGKKAWCWASYLEEEKAVAVPAKLFKEHQSFPYNKNGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKGYKEEEFNWQTYLKTCKAQAAPKSLFENQNITVIPSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPNVKHFSWDKYLEETNSLPAPARAFKVKPPHGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPPLSPLELMEASEHGGCSTPGCKGIGHFKRARHLGPHSAANCPYSEINLNKDRIFPDRLSGEMPPASPSFPRNKRTDANESSSSPEIRDQHADDVKEDFEERTESEMRTSHEARGAREEPTVQQAQRRSAVFLSFKSPIPCLPLRWEQQSKLLPTVAGIPASKVSKWSTDEVSEFIQSLPGCEEHGKVFKDEQIDGEAFLLMTQTDIVKIMSIKLGPALKIFNSILMFKAAEKNSHNEL
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
59PhosphorylationMENVKKATATTTWMV
HHHHHHCCEEEEEEC		33.1630576142
62 (in isoform 2)Phosphorylation-18.9225332170
68 (in isoform 2)Phosphorylation-29.5725332170
68PhosphorylationTTTWMVPTAQEAPTS
EEEEECCCCCCCCCC		29.5726074081
74 (in isoform 2)Phosphorylation-62.0025332170
74PhosphorylationPTAQEAPTSPPSSRP
CCCCCCCCCCCCCCC		62.0026074081
75PhosphorylationTAQEAPTSPPSSRPV
CCCCCCCCCCCCCCC		33.4826074081
78PhosphorylationEAPTSPPSSRPVFPP
CCCCCCCCCCCCCCC		42.2226074081
79PhosphorylationAPTSPPSSRPVFPPA
CCCCCCCCCCCCCCH		46.5126074081
87PhosphorylationRPVFPPAYWTSPPGC
CCCCCCHHCCCCCCC		18.2626074081
170PhosphorylationEEEDPKCSRKKKPKL
CCCCCCCCCCCCCCC		53.9421712546
180SumoylationKKPKLSLKADTKEDG
CCCCCCCCCCCCCCC		40.62-
180SumoylationKKPKLSLKADTKEDG
CCCCCCCCCCCCCCC		40.62-
197SumoylationRDDEMENKQDVRILR
CCHHHHHHHHHHHHH		34.27-
197SumoylationRDDEMENKQDVRILR
CCHHHHHHHHHHHHH		34.27-
206PhosphorylationDVRILRGSQRARRKR
HHHHHHHHHHHHHHH		15.2827251275
217PhosphorylationRRKRRGDSAVLKQGL
HHHHCCCHHHHHCCC		24.0929496963
249AcetylationKAVAVPAKLFKEHQS
HCCCCCHHHHHHHCC		48.6825953088
325PhosphorylationPVGWCEKTGHKLHPP
CCCHHCCCCCCCCCC		23.4024260401
336SumoylationLHPPKGYKEEEFNWQ
CCCCCCCCCHHCCHH		68.28-
336SumoylationLHPPKGYKEEEFNWQ
CCCCCCCCCHHCCHH		68.28-
376SumoylationSGFRVGMKLEAVDKK
CCCCCCCEEEECCCC		36.93-
376SumoylationSGFRVGMKLEAVDKK
CCCCCCCEEEECCCC		36.93-
435PhosphorylationWCKEHRRTLITPPGY
CHHHHCCCEECCCCC		23.5928555341
438PhosphorylationEHRRTLITPPGYPNV
HHCCCEECCCCCCCC		26.9226270265
442PhosphorylationTLITPPGYPNVKHFS
CEECCCCCCCCCCCC		9.4526270265
453PhosphorylationKHFSWDKYLEETNSL
CCCCHHHHHHHHCCC		19.5120049867
457PhosphorylationWDKYLEETNSLPAPA
HHHHHHHHCCCCCCC		22.2620049867
459PhosphorylationKYLEETNSLPAPARA
HHHHHHCCCCCCCHH		43.0520049867
480SumoylationHGFQKKMKLEVVDKR
CCCCCCCEEEEECCC		50.83-
480SumoylationHGFQKKMKLEVVDKR
CCCCCCCEEEEECCC		50.83-
486AcetylationMKLEVVDKRNPMFIR
CEEEEECCCCCCEEE		42.3318585307
560PhosphorylationSEHGGCSTPGCKGIG
HHCCCCCCCCCCCCC		27.9825627689
583PhosphorylationGPHSAANCPYSEINL
CCCCCCCCCHHHCCC		2.6132142685
583 (in isoform 2)Phosphorylation-2.61-
585PhosphorylationHSAANCPYSEINLNK
CCCCCCCHHHCCCCC		22.5727642862
599PhosphorylationKDRIFPDRLSGEMPP
CCCCCCCCCCCCCCC		30.8733259812
601PhosphorylationRIFPDRLSGEMPPAS
CCCCCCCCCCCCCCC		33.3325159151
608PhosphorylationSGEMPPASPSFPRNK
CCCCCCCCCCCCCCC		27.1829255136
610PhosphorylationEMPPASPSFPRNKRT
CCCCCCCCCCCCCCC		45.4430266825
612UbiquitinationPPASPSFPRNKRTDA
CCCCCCCCCCCCCCC		43.1822817900
612 (in isoform 2)Ubiquitination-43.1821890473
617PhosphorylationSFPRNKRTDANESSS
CCCCCCCCCCCCCCC		40.8623663014
622PhosphorylationKRTDANESSSSPEIR
CCCCCCCCCCCHHHH		35.0123927012
623PhosphorylationRTDANESSSSPEIRD
CCCCCCCCCCHHHHH		28.7623927012
624PhosphorylationTDANESSSSPEIRDQ
CCCCCCCCCHHHHHH		60.2223401153
625PhosphorylationDANESSSSPEIRDQH
CCCCCCCCHHHHHHC		28.6223401153
637 (in isoform 1)Ubiquitination-59.5721890473
637SumoylationDQHADDVKEDFEERT
HHCHHHHHHHHHHHH		59.5728112733
637UbiquitinationDQHADDVKEDFEERT
HHCHHHHHHHHHHHH		59.5722817900
667 (in isoform 2)Ubiquitination-36.6621890473
667UbiquitinationEPTVQQAQRRSAVFL
CCHHHHHHHHCCEEE		36.6621890473
670PhosphorylationVQQAQRRSAVFLSFK
HHHHHHHCCEEEEEC		30.8530266825
672UbiquitinationQAQRRSAVFLSFKSP
HHHHHCCEEEEECCC		5.3822817900
675PhosphorylationRRSAVFLSFKSPIPC
HHCCEEEEECCCCCC		21.1130266825
678PhosphorylationAVFLSFKSPIPCLPL
CEEEEECCCCCCCCC		26.5021815630
679UbiquitinationVFLSFKSPIPCLPLR
EEEEECCCCCCCCCC		34.8233845483
682UbiquitinationSFKSPIPCLPLRWEQ
EECCCCCCCCCCHHH		6.7329967540
691PhosphorylationPLRWEQQSKLLPTVA
CCCHHHHHCCCCCCC		25.6022199227
692UbiquitinationLRWEQQSKLLPTVAG
CCHHHHHCCCCCCCC		50.1022817900
692 (in isoform 1)Ubiquitination-50.1021890473
704SumoylationVAGIPASKVSKWSTD
CCCCCHHHCCCCCHH		53.2728112733
704SumoylationVAGIPASKVSKWSTD
CCCCCHHHCCCCCHH		53.27-
704UbiquitinationVAGIPASKVSKWSTD
CCCCCHHHCCCCCHH		53.2733845483
707UbiquitinationIPASKVSKWSTDEVS
CCHHHCCCCCHHHHH		48.4229967540
727UbiquitinationLPGCEEHGKVFKDEQ
CCCHHHHCCEEECCC		30.9721890473
739UbiquitinationDEQIDGEAFLLMTQT
CCCCCCCEEEEEEHH		13.1027667366
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 LMBL3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMBL3_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 LMBL3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
23455924
LMBL3_HUMANL3MBTL3physical
25416956
ASB6_HUMANASB6physical
25416956
LMBL3_HUMANL3MBTL3physical
21516116
TOP2A_HUMANTOP2Aphysical
26496610
XPO1_HUMANXPO1physical
26496610
NDUAD_HUMANNDUFA13physical
26496610
SAMD1_HUMANSAMD1physical
26496610
SAM13_HUMANSAMD13physical
28514442
SAMD1_HUMANSAMD1physical
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 LMBL3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-608, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, AND MASSSPECTROMETRY.

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