LEGL_HUMAN - dbPTM
LEGL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LEGL_HUMAN
UniProt AC Q3ZCW2
Protein Name Galectin-related protein
Gene Name LGALSL
Organism Homo sapiens (Human).
Sequence Length 172
Subcellular Localization
Protein Description Does not bind lactose, and may not bind carbohydrates..
Protein Sequence MAGSVADSDAVVKLDDGHLNNSLSSPVQADVYFPRLIVPFCGHIKGGMRPGKKVLVMGIVDLNPESFAISLTCGDSEDPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAIPYFPFIPDQPFRVEILCEHPRFRVFVDGHQLFDFYHRIQTLSAIDTIKINGDLQITKLG
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------MAGSVADSD
------CCCCCCCCC
20.9719413330
4Phosphorylation----MAGSVADSDAV
----CCCCCCCCCCE
12.4727732954
8PhosphorylationMAGSVADSDAVVKLD
CCCCCCCCCCEEECC
20.1028450419
22PhosphorylationDDGHLNNSLSSPVQA
CCCCCCCCCCCCCCC
28.6730266825
24PhosphorylationGHLNNSLSSPVQADV
CCCCCCCCCCCCCCE
32.2030266825
25PhosphorylationHLNNSLSSPVQADVY
CCCCCCCCCCCCCEE
34.0929255136
32PhosphorylationSPVQADVYFPRLIVP
CCCCCCEEECCEECC
14.3822199227

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 LEGL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LEGL_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 LEGL_HUMAN !!

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

Oops, there are no PPI records of LEGL_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 LEGL_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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-22 AND SER-25, AND MASSSPECTROMETRY.

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