LEMD2_HUMAN - dbPTM
LEMD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LEMD2_HUMAN
UniProt AC Q8NC56
Protein Name LEM domain-containing protein 2
Gene Name LEMD2
Organism Homo sapiens (Human).
Sequence Length 503
Subcellular Localization Nucleus inner membrane
Multi-pass membrane protein . Lamina-associated protein residing in the inner nuclear membrane (INM). Localized exclusively to the nuclear envelope, giving rise to a typical rim-like staining of the nuclear periphery.
Protein Description Involved in nuclear structure organization. [PubMed: 16339967 Required for maintaining the integrity of the nuclear envelope]
Protein Sequence MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGEARLRDEERLREEARPRGEERLREEARLREDAPLRARPAAASPRAEPWLSQPASGSAYATPGAYGDIRPSAASWVGSRGLAYPARPAQLRRRASVRGSSEEDEDARTPDRATQGPGLAARRWWAASPAPARLPSSLLGPDPRPGLRATRAGPAGAARARPEVGRRLERWLSRLLLWASLGLLLVFLGILWVKMGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPENLKSKCIPVMEAQEYIANVTSSSSAKFEAALTWILSSNKDVGIWLKGEDQSELVTTVDKVVCLESAHPRMGVGCRLSRALLTAVTNVLIFFWCLAFLWGLLILLKYRWRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNESRIQTESHRVAGEDMLVWRWTKPSSFSDSER
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
2Acetylation------MAGLSDLEL
------CCCCCHHHH		27.8622814378
5Phosphorylation---MAGLSDLELRRE
---CCCCCHHHHHHH		38.9523401153
10MethylationGLSDLELRRELQALG
CCCHHHHHHHHHHCC		22.20115482009
26PhosphorylationQPGPITDTTRDVYRN
CCCCCCCHHHHHHHH		18.3228555341
27PhosphorylationPGPITDTTRDVYRNK
CCCCCCHHHHHHHHH		27.9025627689
82PhosphorylationRARPAAASPRAEPWL
CCCCCCCCCCCCCCC		15.3622115753
90PhosphorylationPRAEPWLSQPASGSA
CCCCCCCCCCCCCCC		30.1926074081
94PhosphorylationPWLSQPASGSAYATP
CCCCCCCCCCCCCCC		39.7129978859
96PhosphorylationLSQPASGSAYATPGA
CCCCCCCCCCCCCCC		18.6628796482
98PhosphorylationQPASGSAYATPGAYG
CCCCCCCCCCCCCCC		16.8328796482
100PhosphorylationASGSAYATPGAYGDI
CCCCCCCCCCCCCCC		15.0228796482
104PhosphorylationAYATPGAYGDIRPSA
CCCCCCCCCCCCHHH		22.6528796482
108MethylationPGAYGDIRPSAASWV
CCCCCCCCHHHHHHH		24.7082797205
110PhosphorylationAYGDIRPSAASWVGS
CCCCCCHHHHHHHCC		26.9824173317
113PhosphorylationDIRPSAASWVGSRGL
CCCHHHHHHHCCCCC		23.2424173317
117PhosphorylationSAASWVGSRGLAYPA
HHHHHHCCCCCCCCC		17.3524173317
122PhosphorylationVGSRGLAYPARPAQL
HCCCCCCCCCCHHHH		11.5028152594
134PhosphorylationAQLRRRASVRGSSEE
HHHHHHHHCCCCCCC		15.5522167270
138PhosphorylationRRASVRGSSEEDEDA
HHHHCCCCCCCCCCC		24.8229255136
139PhosphorylationRASVRGSSEEDEDAR
HHHCCCCCCCCCCCC		48.0729255136
147PhosphorylationEEDEDARTPDRATQG
CCCCCCCCCCCCCCC		31.1222167270
152PhosphorylationARTPDRATQGPGLAA
CCCCCCCCCCCCHHH		34.65-
166PhosphorylationARRWWAASPAPARLP
HHHHHHCCCCCCCCC		17.5323927012
174PhosphorylationPAPARLPSSLLGPDP
CCCCCCCHHHHCCCC		37.9029255136
175PhosphorylationAPARLPSSLLGPDPR
CCCCCCHHHHCCCCC		26.1829255136
188PhosphorylationPRPGLRATRAGPAGA
CCCCCCCCCCCCCCH		18.0223403867
192UbiquitinationLRATRAGPAGAARAR
CCCCCCCCCCHHHCC		26.9121890473
264UbiquitinationTDEFCQAKQKAALLE
CHHHHHHHHHHHHHH		26.84-
264MethylationTDEFCQAKQKAALLE
CHHHHHHHHHHHHHH		26.84-
266MethylationEFCQAKQKAALLELL
HHHHHHHHHHHHHHH		34.61-
319AcetylationVTSSSSAKFEAALTW
CCCCCCHHHHHHHHH		45.767710437
352AcetylationELVTTVDKVVCLESA
HEEEEECEEEECCCC		32.0326051181
436PhosphorylationWEQDMERYPYVGILH
HHHHHHHCCEEEEEE		5.8922817900
438PhosphorylationQDMERYPYVGILHVR
HHHHHCCEEEEEEEC		11.45-
453PhosphorylationDSLIPPQSRRRMKRV
HHCCCHHHHHHHHHH		33.2626462736
470PhosphorylationRAVEFLASNESRIQT
HHHHHHHCCCHHCCC		43.1923312004
473PhosphorylationEFLASNESRIQTESH
HHHHCCCHHCCCCHH		38.6423312004
477PhosphorylationSNESRIQTESHRVAG
CCCHHCCCCHHHCCC		36.76-
479PhosphorylationESRIQTESHRVAGED
CHHCCCCHHHCCCCC		21.71-
493PhosphorylationDMLVWRWTKPSSFSD
CEEEEEECCCCCCCC		25.2222167270
494UbiquitinationMLVWRWTKPSSFSDS
EEEEEECCCCCCCCC		35.6221890473
496PhosphorylationVWRWTKPSSFSDSER
EEEECCCCCCCCCCC		45.6422167270
497PhosphorylationWRWTKPSSFSDSER-
EEECCCCCCCCCCC-		36.9822167270
499PhosphorylationWTKPSSFSDSER---
ECCCCCCCCCCC---		42.0229255136
501PhosphorylationKPSSFSDSER-----
CCCCCCCCCC-----		33.7929255136
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 LEMD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LEMD2_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 LEMD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LEMD2_HUMAN !!
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 LEMD2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-139, ANDMASS SPECTROMETRY.
"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-134; SER-138; SER-139;SER-166 AND SER-499, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, 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-499, AND MASSSPECTROMETRY.

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