Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Galectin-1  

UniProtKB / Swiss-Prot ID :  LEG1_HUMAN

Gene Name (Synonyms) : 
LGALS1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted, extracellular space, extracellular matrix. 

Protein Function :  May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. 

Protein Sequence MACGLVASNLNLKPGECLRVRGEVAPDAKSFVLNLGKDSNNLCLHFNPRFNAHGDANTIVCNSKDGGAWG...
Predicted Secondary Structure CCCCCEEEECCCCCCCEEEEEEEECCCCCEEEEEECCCCCCEEEEEEEEECCCCCCCEEEEECCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MACGLV
---CCCCCE
8.97UniProtKB
Link
29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)APDAKSFVL
CCCCCEEEE
52.38Phosphositeplus
Link
29N6-acetyllysineAPDAKSFVL
CCCCCEEEE
52.38HPRD
Link
29N6-acetyllysineAPDAKSFVL
CCCCCEEEE
52.38Phosphositeplus
Link
29N6-acetyllysine.APDAKSFVL
CCCCCEEEE
52.38UniProtKB
Link
30PhosphoserinePDAKSFVLN
CCCCEEEEE
23.47HPRD
Link
30PhosphoserinePDAKSFVLN
CCCCEEEEE
23.47Phosphositeplus
Link
37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LNLGKDSNN
EEECCCCCC
62.24Phosphositeplus
Link
43S-nitrosocysteineSNNLCLHFN
CCCEEEEEE
2.78dbSNO
Link
61S-nitrosocysteineNTIVCNSKD
CEEEEECCC
4.15dbSNO
Link
61S-nitrosocysteineNTIVCNSKD
CEEEEECCC
4.15HPRD
Link
61S-nitrosocysteineNTIVCNSKD
CEEEEECCC
4.15SysPTM
Link
64Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VCNSKDGGA
EEECCCCCC
46.53Phosphositeplus
Link
105PhosphotyrosineLPDGYEFKF
ECCCEEEEE
26.10Phosphositeplus
Link
105Phosphotyrosine.LPDGYEFKF
ECCCEEEEE
26.10UniProtKB
Link
108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GYEFKFPNR
CEEEEECCC
48.23Phosphositeplus
Link
120PhosphotyrosineEAINYMAAD
HHCCEEEEE
5.09Phosphositeplus
Link
128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DGDFKIKCV
EEEEEEEEE
46.10Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ITB1_HUMANin vitroHPRD:01040HPRD14550305
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures