LEMD2_MOUSE - dbPTM
LEMD2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LEMD2_MOUSE
UniProt AC Q6DVA0
Protein Name LEM domain-containing protein 2
Gene Name Lemd2
Organism Mus musculus (Mouse).
Sequence Length 511
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 (By similarity; Required for embryonic development and is involved in regulation of several signaling pathways such as MAPK and AKT]
Protein Sequence MAGLSDLELRRELQALGFQPGPITDTTRNVYRNKLRRLRGEARLRDDERLREDAGPREDAGPRGPERQREEARLREEAPLRARPAASVLRSEPWPLSPSPPAPSAASDASGPYGNFGASASPWAASRGLSYPPHAGPGPLRRRASVRGSSEDDEDTRTPDRHAPGRGRHWWAPPSASARPHSALLGADARPGLKGSRTGSAGAGRTRPEVGRWLERCLSRLLLWASLGLLLGFLAILWVKMGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPEKLKSKCIPVLEAQEYIANVTSSPSSRFKAALTWILSSNKDVGIWLKGEDPSELATTVDKVVCLESARPRMGIGCRLSRALLTAVTHVLIFFWCLAFLWGLLILLKYRWRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNESRIQTESHRVAGEDMLVWRWTKPSSFSDSER
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
27.86-
5Phosphorylation---MAGLSDLELRRE
---CCCCCHHHHHHH
38.9530352176
87PhosphorylationLRARPAASVLRSEPW
CCCCCHHHHHHCCCC
24.6429176673
99PhosphorylationEPWPLSPSPPAPSAA
CCCCCCCCCCCCCCC
39.89-
113PhosphorylationASDASGPYGNFGASA
CCCCCCCCCCCCCCC
28.38-
130PhosphorylationWAASRGLSYPPHAGP
HHHHCCCCCCCCCCC
38.1228833060
131PhosphorylationAASRGLSYPPHAGPG
HHHCCCCCCCCCCCC
26.3128833060
145PhosphorylationGPLRRRASVRGSSED
CCCCCCCCCCCCCCC
15.5525521595
149PhosphorylationRRASVRGSSEDDEDT
CCCCCCCCCCCCCCC
21.7125521595
150PhosphorylationRASVRGSSEDDEDTR
CCCCCCCCCCCCCCC
48.1225521595
156PhosphorylationSSEDDEDTRTPDRHA
CCCCCCCCCCCCCCC
34.1027087446
158PhosphorylationEDDEDTRTPDRHAPG
CCCCCCCCCCCCCCC
31.4725159016
182PhosphorylationSASARPHSALLGADA
CCCCCCCHHHCCCCC
24.2426824392
196PhosphorylationARPGLKGSRTGSAGA
CCCCCCCCCCCCCCC
25.6926824392
366PhosphorylationDKVVCLESARPRMGI
CEEEEHHCCCCCCCC
19.34-
444PhosphorylationWEQDMERYPYVGILH
HHHHHHHCCEEEEEE
5.89-
501PhosphorylationDMLVWRWTKPSSFSD
CEEEEEECCCCCCCC
25.2225619855
504PhosphorylationVWRWTKPSSFSDSER
EEEECCCCCCCCCCC
45.6427742792
505PhosphorylationWRWTKPSSFSDSER-
EEECCCCCCCCCCC-
36.9827742792
507PhosphorylationWTKPSSFSDSER---
ECCCCCCCCCCC---
42.0226824392
509PhosphorylationKPSSFSDSER-----
CCCCCCCCCC-----
33.7927742792

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LEMD2_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LEMD2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LEMD2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507 AND SER-509, ANDMASS SPECTROMETRY.

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