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
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

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
30	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

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.

Oops, there are no SNP-PTM records of LEG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
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

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.

Related Literatures of Post-Translational Modification

Acetylation

"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.
PubMed: 19413330

"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.
PubMed: 19608861

Phosphorylation

"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.
PubMed: 19534553