LEG1_HUMAN - dbPTM
LEG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LEG1_HUMAN
UniProt AC P09382
Protein Name Galectin-1
Gene Name LGALS1
Organism Homo sapiens (Human).
Sequence Length 135
Subcellular Localization Secreted, extracellular space, extracellular matrix .
Protein Description Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis..
Protein Sequence MACGLVASNLNLKPGECLRVRGEVAPDAKSFVLNLGKDSNNLCLHFNPRFNAHGDANTIVCNSKDGGAWGTEQREAVFPFQPGSVAEVCITFDQANLTVKLPDGYEFKFPNRLNLEAINYMAADGDFKIKCVAFD
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------MACGLVASN
------CCCCCEEEC
8.9722223895
3S-palmitoylation-----MACGLVASNL
-----CCCCCEEECC
4.1229575903
8PhosphorylationMACGLVASNLNLKPG
CCCCCEEECCCCCCC
34.0827050516
13UbiquitinationVASNLNLKPGECLRV
EEECCCCCCCCEEEE
50.32-
13SuccinylationVASNLNLKPGECLRV
EEECCCCCCCCEEEE
50.3223954790
132-HydroxyisobutyrylationVASNLNLKPGECLRV
EEECCCCCCCCEEEE
50.32-
13AcetylationVASNLNLKPGECLRV
EEECCCCCCCCEEEE
50.3221339330
17S-palmitoylationLNLKPGECLRVRGEV
CCCCCCCEEEEEEEE
3.4929575903
29AcetylationGEVAPDAKSFVLNLG
EEECCCCCEEEEEEC
52.3819608861
29UbiquitinationGEVAPDAKSFVLNLG
EEECCCCCEEEEEEC
52.3821890473
29MalonylationGEVAPDAKSFVLNLG
EEECCCCCEEEEEEC
52.3826320211
29UbiquitinationGEVAPDAKSFVLNLG
EEECCCCCEEEEEEC
52.3821890473
292-HydroxyisobutyrylationGEVAPDAKSFVLNLG
EEECCCCCEEEEEEC
52.38-
30PhosphorylationEVAPDAKSFVLNLGK
EECCCCCEEEEEECC
23.4729255136
37UbiquitinationSFVLNLGKDSNNLCL
EEEEEECCCCCCEEE
62.2421906983
372-HydroxyisobutyrylationSFVLNLGKDSNNLCL
EEEEEECCCCCCEEE
62.24-
37AcetylationSFVLNLGKDSNNLCL
EEEEEECCCCCCEEE
62.2421466224
39PhosphorylationVLNLGKDSNNLCLHF
EEEECCCCCCEEEEE
30.9826657352
43S-nitrosocysteineGKDSNNLCLHFNPRF
CCCCCCEEEEECCCC
2.78-
43S-palmitoylationGKDSNNLCLHFNPRF
CCCCCCEEEEECCCC
2.7829575903
43S-nitrosylationGKDSNNLCLHFNPRF
CCCCCCEEEEECCCC
2.7822178444
58PhosphorylationNAHGDANTIVCNSKD
CCCCCCCEEEEECCC
19.2623322592
61S-nitrosocysteineGDANTIVCNSKDGGA
CCCCEEEEECCCCCC
4.15-
61S-palmitoylationGDANTIVCNSKDGGA
CCCCEEEEECCCCCC
4.1526865113
61S-nitrosylationGDANTIVCNSKDGGA
CCCCEEEEECCCCCC
4.1518335467
63PhosphorylationANTIVCNSKDGGAWG
CCEEEEECCCCCCCC
27.3123322592
642-HydroxyisobutyrylationNTIVCNSKDGGAWGT
CEEEEECCCCCCCCC
46.53-
64AcetylationNTIVCNSKDGGAWGT
CEEEEECCCCCCCCC
46.5323236377
64MalonylationNTIVCNSKDGGAWGT
CEEEEECCCCCCCCC
46.5326320211
64UbiquitinationNTIVCNSKDGGAWGT
CEEEEECCCCCCCCC
46.53-
71PhosphorylationKDGGAWGTEQREAVF
CCCCCCCCCEEEEEE
20.4621712546
105PhosphorylationTVKLPDGYEFKFPNR
EEECCCCCEEECCCC
26.1021082442
108MalonylationLPDGYEFKFPNRLNL
CCCCCEEECCCCCCC
48.2326320211
108UbiquitinationLPDGYEFKFPNRLNL
CCCCCEEECCCCCCC
48.2321890473
108SuccinylationLPDGYEFKFPNRLNL
CCCCCEEECCCCCCC
48.23-
1082-HydroxyisobutyrylationLPDGYEFKFPNRLNL
CCCCCEEECCCCCCC
48.23-
108AcetylationLPDGYEFKFPNRLNL
CCCCCEEECCCCCCC
48.2323954790
108SuccinylationLPDGYEFKFPNRLNL
CCCCCEEECCCCCCC
48.23-
108UbiquitinationLPDGYEFKFPNRLNL
CCCCCEEECCCCCCC
48.2321890473
108SumoylationLPDGYEFKFPNRLNL
CCCCCEEECCCCCCC
48.23-
120PhosphorylationLNLEAINYMAADGDF
CCCEEEEEEECCCCC
5.0922817900
121SulfoxidationNLEAINYMAADGDFK
CCEEEEEEECCCCCE
1.8330846556
128MalonylationMAADGDFKIKCVAFD
EECCCCCEEEEEEEC
46.1026320211
128UbiquitinationMAADGDFKIKCVAFD
EECCCCCEEEEEEEC
46.102190698
128AcetylationMAADGDFKIKCVAFD
EECCCCCEEEEEEEC
46.1026051181
130MalonylationADGDFKIKCVAFD--
CCCCCEEEEEEEC--
24.2132601280
1302-HydroxyisobutyrylationADGDFKIKCVAFD--
CCCCCEEEEEEEC--
24.21-
130UbiquitinationADGDFKIKCVAFD--
CCCCCEEEEEEEC--
24.21-
130AcetylationADGDFKIKCVAFD--
CCCCCEEEEEEEC--
24.2127178108
131S-nitrosylationDGDFKIKCVAFD---
CCCCEEEEEEEC---
2.8022126794

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
30SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LEG1_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 LEG1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUC16_HUMANMUC16physical
12615972
GEMI4_HUMANGEMIN4physical
11522829
LEG3_HUMANLGALS3physical
11522829
SMN_HUMANSMN1physical
11522829
RSMB_HUMANSNRPBphysical
11522829
GEMI2_HUMANGEMIN2physical
11522829
PTPRC_HUMANPTPRCphysical
10490978
LEUK_HUMANSPNphysical
10490978
CD7_HUMANCD7physical
10490978
CD4_HUMANCD4physical
10490978
GTF2I_HUMANGTF2Iphysical
18662664
ACOC_HUMANACO1physical
22863883
APEX1_HUMANAPEX1physical
22863883
PSMG1_HUMANPSMG1physical
22863883
RASH_HUMANHRASphysical
22696230
ANX11_HUMANANXA11physical
26344197
ANXA2_HUMANANXA2physical
26344197
CHRD1_HUMANCHORDC1physical
26344197
HNRPL_HUMANHNRNPLphysical
26344197
PCBP1_HUMANPCBP1physical
26344197
PCBP2_HUMANPCBP2physical
26344197
PLIN3_HUMANPLIN3physical
26344197
RAB5C_HUMANRAB5Cphysical
26344197
RAC1_HUMANRAC1physical
26344197
SERPH_HUMANSERPINH1physical
26344197
TALDO_HUMANTALDO1physical
26344197
UBE2N_HUMANUBE2Nphysical
26344197

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 LEG1_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.
"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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