CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002770
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Galectin-1 
Protein Synonyms/Alias
 Gal-1; 14 kDa laminin-binding protein; HLBP14; 14 kDa lectin; Beta-galactoside-binding lectin L-14-I; Galaptin; HBL; HPL; Lactose-binding lectin 1; Lectin galactoside-binding soluble 1; Putative MAPK-activating protein PM12; S-Lac lectin 1 
Gene Name
 LGALS1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
13VASNLNLKPGECLRVacetylation[1]
13VASNLNLKPGECLRVubiquitination[2]
29GEVAPDAKSFVLNLGacetylation[3, 4, 5]
29GEVAPDAKSFVLNLGubiquitination[2, 6, 7, 8, 9]
37SFVLNLGKDSNNLCLacetylation[10]
37SFVLNLGKDSNNLCLubiquitination[2, 7]
64NTIVCNSKDGGAWGTacetylation[5]
64NTIVCNSKDGGAWGTubiquitination[2, 7, 11]
108LPDGYEFKFPNRLNLacetylation[4, 5]
108LPDGYEFKFPNRLNLubiquitination[2, 6, 7, 8, 9]
128MAADGDFKIKCVAFDacetylation[4]
128MAADGDFKIKCVAFDubiquitination[7, 8]
Reference
 [1] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [10] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [11] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 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. 
Sequence Annotation
 DOMAIN 4 135 Galectin.
 REGION 45 49 Beta-galactoside binding.
 REGION 69 72 Beta-galactoside binding.
 BINDING 53 53 Beta-galactoside.
 BINDING 62 62 Beta-galactoside.
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 29 29 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Extracellular matrix; Lectin; Reference proteome; Secreted. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 135 AA 
Protein Sequence
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV 60
CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY 120
MAADGDFKIK CVAFD 135 
Gene Ontology
 GO:0009986; C:cell surface; IEA:Compara.
 GO:0005737; C:cytoplasm; TAS:UniProtKB.
 GO:0005615; C:extracellular space; IDA:BHF-UCL.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
 GO:0016936; F:galactoside binding; IEA:InterPro.
 GO:0030395; F:lactose binding; IEA:Compara.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0006915; P:apoptotic process; TAS:ProtInc.
 GO:0071333; P:cellular response to glucose stimulus; IEA:Compara.
 GO:0071407; P:cellular response to organic cyclic compound; IEA:Compara.
 GO:0033555; P:multicellular organismal response to stress; IEA:Compara.
 GO:0045445; P:myoblast differentiation; IEA:Compara.
 GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Compara.
 GO:0010977; P:negative regulation of neuron projection development; IEA:Compara.
 GO:0002317; P:plasma cell differentiation; IEA:Compara.
 GO:0034120; P:positive regulation of erythrocyte aggregation; IEA:Compara.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
 GO:0048678; P:response to axon injury; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0031295; P:T cell costimulation; IEA:Compara. 
Interpro
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR015535; Galectin_1.
 IPR001079; Galectin_CRD. 
Pfam
 PF00337; Gal-bind_lectin 
SMART
 SM00908; Gal-bind_lectin
 SM00276; GLECT 
PROSITE
 PS51304; GALECTIN 
PRINTS