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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MACGLVASN ------CCCCCEEEC | 8.97 | 22223895 | |
3 | S-palmitoylation | -----MACGLVASNL -----CCCCCEEECC | 4.12 | 29575903 | |
8 | Phosphorylation | MACGLVASNLNLKPG CCCCCEEECCCCCCC | 34.08 | 27050516 | |
13 | Ubiquitination | VASNLNLKPGECLRV EEECCCCCCCCEEEE | 50.32 | - | |
13 | Succinylation | VASNLNLKPGECLRV EEECCCCCCCCEEEE | 50.32 | 23954790 | |
13 | 2-Hydroxyisobutyrylation | VASNLNLKPGECLRV EEECCCCCCCCEEEE | 50.32 | - | |
13 | Acetylation | VASNLNLKPGECLRV EEECCCCCCCCEEEE | 50.32 | 21339330 | |
17 | S-palmitoylation | LNLKPGECLRVRGEV CCCCCCCEEEEEEEE | 3.49 | 29575903 | |
29 | Acetylation | GEVAPDAKSFVLNLG EEECCCCCEEEEEEC | 52.38 | 19608861 | |
29 | Ubiquitination | GEVAPDAKSFVLNLG EEECCCCCEEEEEEC | 52.38 | 21890473 | |
29 | Malonylation | GEVAPDAKSFVLNLG EEECCCCCEEEEEEC | 52.38 | 26320211 | |
29 | Ubiquitination | GEVAPDAKSFVLNLG EEECCCCCEEEEEEC | 52.38 | 21890473 | |
29 | 2-Hydroxyisobutyrylation | GEVAPDAKSFVLNLG EEECCCCCEEEEEEC | 52.38 | - | |
30 | Phosphorylation | EVAPDAKSFVLNLGK EECCCCCEEEEEECC | 23.47 | 29255136 | |
37 | Ubiquitination | SFVLNLGKDSNNLCL EEEEEECCCCCCEEE | 62.24 | 21906983 | |
37 | 2-Hydroxyisobutyrylation | SFVLNLGKDSNNLCL EEEEEECCCCCCEEE | 62.24 | - | |
37 | Acetylation | SFVLNLGKDSNNLCL EEEEEECCCCCCEEE | 62.24 | 21466224 | |
39 | Phosphorylation | VLNLGKDSNNLCLHF EEEECCCCCCEEEEE | 30.98 | 26657352 | |
43 | S-nitrosocysteine | GKDSNNLCLHFNPRF CCCCCCEEEEECCCC | 2.78 | - | |
43 | S-palmitoylation | GKDSNNLCLHFNPRF CCCCCCEEEEECCCC | 2.78 | 29575903 | |
43 | S-nitrosylation | GKDSNNLCLHFNPRF CCCCCCEEEEECCCC | 2.78 | 22178444 | |
58 | Phosphorylation | NAHGDANTIVCNSKD CCCCCCCEEEEECCC | 19.26 | 23322592 | |
61 | S-nitrosocysteine | GDANTIVCNSKDGGA CCCCEEEEECCCCCC | 4.15 | - | |
61 | S-palmitoylation | GDANTIVCNSKDGGA CCCCEEEEECCCCCC | 4.15 | 26865113 | |
61 | S-nitrosylation | GDANTIVCNSKDGGA CCCCEEEEECCCCCC | 4.15 | 18335467 | |
63 | Phosphorylation | ANTIVCNSKDGGAWG CCEEEEECCCCCCCC | 27.31 | 23322592 | |
64 | 2-Hydroxyisobutyrylation | NTIVCNSKDGGAWGT CEEEEECCCCCCCCC | 46.53 | - | |
64 | Acetylation | NTIVCNSKDGGAWGT CEEEEECCCCCCCCC | 46.53 | 23236377 | |
64 | Malonylation | NTIVCNSKDGGAWGT CEEEEECCCCCCCCC | 46.53 | 26320211 | |
64 | Ubiquitination | NTIVCNSKDGGAWGT CEEEEECCCCCCCCC | 46.53 | - | |
71 | Phosphorylation | KDGGAWGTEQREAVF CCCCCCCCCEEEEEE | 20.46 | 21712546 | |
105 | Phosphorylation | TVKLPDGYEFKFPNR EEECCCCCEEECCCC | 26.10 | 21082442 | |
108 | Malonylation | LPDGYEFKFPNRLNL CCCCCEEECCCCCCC | 48.23 | 26320211 | |
108 | Ubiquitination | LPDGYEFKFPNRLNL CCCCCEEECCCCCCC | 48.23 | 21890473 | |
108 | Succinylation | LPDGYEFKFPNRLNL CCCCCEEECCCCCCC | 48.23 | - | |
108 | 2-Hydroxyisobutyrylation | LPDGYEFKFPNRLNL CCCCCEEECCCCCCC | 48.23 | - | |
108 | Acetylation | LPDGYEFKFPNRLNL CCCCCEEECCCCCCC | 48.23 | 23954790 | |
108 | Succinylation | LPDGYEFKFPNRLNL CCCCCEEECCCCCCC | 48.23 | - | |
108 | Ubiquitination | LPDGYEFKFPNRLNL CCCCCEEECCCCCCC | 48.23 | 21890473 | |
108 | Sumoylation | LPDGYEFKFPNRLNL CCCCCEEECCCCCCC | 48.23 | - | |
120 | Phosphorylation | LNLEAINYMAADGDF CCCEEEEEEECCCCC | 5.09 | 22817900 | |
121 | Sulfoxidation | NLEAINYMAADGDFK CCEEEEEEECCCCCE | 1.83 | 30846556 | |
128 | Malonylation | MAADGDFKIKCVAFD EECCCCCEEEEEEEC | 46.10 | 26320211 | |
128 | Ubiquitination | MAADGDFKIKCVAFD EECCCCCEEEEEEEC | 46.10 | 2190698 | |
128 | Acetylation | MAADGDFKIKCVAFD EECCCCCEEEEEEEC | 46.10 | 26051181 | |
130 | Malonylation | ADGDFKIKCVAFD-- CCCCCEEEEEEEC-- | 24.21 | 32601280 | |
130 | 2-Hydroxyisobutyrylation | ADGDFKIKCVAFD-- CCCCCEEEEEEEC-- | 24.21 | - | |
130 | Ubiquitination | ADGDFKIKCVAFD-- CCCCCEEEEEEEC-- | 24.21 | - | |
130 | Acetylation | ADGDFKIKCVAFD-- CCCCCEEEEEEEC-- | 24.21 | 27178108 | |
131 | S-nitrosylation | DGDFKIKCVAFD--- CCCCEEEEEEEC--- | 2.80 | 22126794 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
30 | S | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LEG1_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MUC16_HUMAN | MUC16 | physical | 12615972 | |
GEMI4_HUMAN | GEMIN4 | physical | 11522829 | |
LEG3_HUMAN | LGALS3 | physical | 11522829 | |
SMN_HUMAN | SMN1 | physical | 11522829 | |
RSMB_HUMAN | SNRPB | physical | 11522829 | |
GEMI2_HUMAN | GEMIN2 | physical | 11522829 | |
PTPRC_HUMAN | PTPRC | physical | 10490978 | |
LEUK_HUMAN | SPN | physical | 10490978 | |
CD7_HUMAN | CD7 | physical | 10490978 | |
CD4_HUMAN | CD4 | physical | 10490978 | |
GTF2I_HUMAN | GTF2I | physical | 18662664 | |
ACOC_HUMAN | ACO1 | physical | 22863883 | |
APEX1_HUMAN | APEX1 | physical | 22863883 | |
PSMG1_HUMAN | PSMG1 | physical | 22863883 | |
RASH_HUMAN | HRAS | physical | 22696230 | |
ANX11_HUMAN | ANXA11 | physical | 26344197 | |
ANXA2_HUMAN | ANXA2 | physical | 26344197 | |
CHRD1_HUMAN | CHORDC1 | physical | 26344197 | |
HNRPL_HUMAN | HNRNPL | physical | 26344197 | |
PCBP1_HUMAN | PCBP1 | physical | 26344197 | |
PCBP2_HUMAN | PCBP2 | physical | 26344197 | |
PLIN3_HUMAN | PLIN3 | physical | 26344197 | |
RAB5C_HUMAN | RAB5C | physical | 26344197 | |
RAC1_HUMAN | RAC1 | physical | 26344197 | |
SERPH_HUMAN | SERPINH1 | physical | 26344197 | |
TALDO_HUMAN | TALDO1 | physical | 26344197 | |
UBE2N_HUMAN | UBE2N | physical | 26344197 |
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. |
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Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |