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P09382 (LEG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Galectin-1

Short name=Gal-1
Alternative name(s):
14 kDa laminin-binding protein
Short name=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 names
Name:LGALS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Strong inducer of T-cell apoptosis. Ref.24 Ref.26 Ref.32

Subunit structure

Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD7, CD43 and CD45. Interacts with laminin (via poly-N-acetyllactosamine). Ref.18 Ref.23 Ref.31 Ref.32

Subcellular location

Secretedextracellular spaceextracellular matrix Ref.24.

Tissue specificity

Expressed in placenta, maternal decidua and fetal membranes. Within placenta, expressed in trophoblasts, stromal cells, villous endothelium, syncytiotrophoblast apical membrane and villous stroma. Within fetal membranes, expressed in amnion, chorioamniotic mesenchyma and chorion (at protein level). Expressed in cardiac, smooth, and skeletal muscle, neurons, thymus, kidney and hematopoietic cells. Ref.4 Ref.26

Sequence similarities

Contains 1 galectin domain.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentExtracellular matrix
Secreted
   LigandLectin
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell costimulation

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement PubMed 1713454. Source: ProtInc

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

multicellular organismal response to stress

Inferred from electronic annotation. Source: Ensembl

myoblast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

plasma cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of erythrocyte aggregation

Inferred from electronic annotation. Source: Ensembl

regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from mutant phenotype Ref.6. Source: GOC

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

intracellular

Inferred from direct assay. Source: LIFEdb

nucleus

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiongalactoside binding

Inferred from electronic annotation. Source: InterPro

lactose binding

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.21. Source: IntAct

signal transducer activity

Inferred from mutant phenotype Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTPRCP085752EBI-1048875,EBI-1341

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13 Ref.14 Ref.15 Ref.29
Chain2 – 135134Galectin-1
PRO_0000076917

Regions

Domain4 – 135132Galectin
Region45 – 495Beta-galactoside binding
Region69 – 724Beta-galactoside binding

Sites

Binding site531Beta-galactoside
Binding site621Beta-galactoside

Amino acid modifications

Modified residue21N-acetylalanine Ref.29 Ref.30
Modified residue131N6-acetyllysine By similarity
Modified residue291N6-acetyllysine Ref.27
Modified residue1081N6-acetyllysine; alternate By similarity
Modified residue1081N6-succinyllysine; alternate By similarity
Modified residue1281N6-acetyllysine By similarity

Secondary structure

...................... 135
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09382 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2FBB8D7A1FC0F1F9

FASTA13514,716
        10         20         30         40         50         60 
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV 

        70         80         90        100        110        120 
CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY 

       130 
MAADGDFKIK CVAFD 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of a full-length cDNA for human 14 kDa beta-galactoside-binding lectin."
Hirabayashi J., Ayaki K., Soma G., Kasai K.
Biochim. Biophys. Acta 1008:85-91(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[2]"Molecular cloning, characterization, and expression of a human 14-kDa lectin."
Couraud P.-O., Casentini-Borocz D., Bringman T.S., Griffith J., McGrogan M., Nedwin G.E.
J. Biol. Chem. 264:1310-1316(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta and Promyelocytic leukemia.
[3]"Evidence that the 14 kDa soluble beta-galactoside-binding lectin in man is encoded by a single gene."
Abbott W.M., Feizi T.
Biochem. J. 259:291-294(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hepatoma.
[4]"Emergence of hormonal and redox regulation of galectin-1 in placental mammals: implication in maternal-fetal immune tolerance."
Than N.G., Romero R., Erez O., Weckle A., Tarca A.L., Hotra J., Abbas A., Han Y.M., Kim S.S., Kusanovic J.P., Gotsch F., Hou Z., Santolaya-Forgas J., Benirschke K., Papp Z., Grossman L.I., Goodman M., Wildman D.E.
Proc. Natl. Acad. Sci. U.S.A. 105:15819-15824(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Placenta.
[5]"Genomic sequence and organization of two members of a human lectin gene family."
Gitt M.A., Barondes S.H.
Biochemistry 30:82-89(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lymphocyte.
[6]"Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung fibroblast.
[7]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thalamus.
[9]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Skin.
[13]"Complete amino acid sequence of a beta-galactoside-binding lectin from human placenta."
Hirabayashi J., Kasai K.
J. Biochem. 104:1-4(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-135.
Tissue: Placenta.
[14]"Beta-galactosidase soluble lectin from human brain: complete amino acid sequence."
Bladier D., le Caer J.-P., Joubert R., Caron M., Rossier J.
Neurochem. Int. 18:275-281(1991)
Cited for: PROTEIN SEQUENCE OF 2-135.
Tissue: Brain.
[15]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19.
Tissue: Platelet.
[16]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 38-49; 101-108 AND 113-128, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[17]"Further characterization and structural studies on human placenta lectin."
Hirabayashi J., Kawasaki H., Suzuki K., Kasai K.
J. Biochem. 101:987-995(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 70-87 AND 122-133.
Tissue: Placenta.
[18]"Identification of a 14-kDa laminin binding protein (HLBP14) in human melanoma cells that is identical to the 14-kDa galactoside binding lectin."
Castronovo V., Luyten F., van den Brule F., Sobel M.E.
Arch. Biochem. Biophys. 297:132-138(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-29; 50-74 AND 132-135, INTERACTION WITH LAMININ.
Tissue: Melanoma.
[19]"Human splenic galaptin: physicochemical characterization."
Sharma A., Chemelli R., Allen H.J.
Biochemistry 29:5309-5314(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Spleen.
[20]"Apoptosis of T cells mediated by galectin-1."
Perillo N.L., Pace K.E., Seilhamer J.J., Baum L.G.
Nature 378:736-739(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[21]"Galectin-1, a natural ligand for the receptor-type protein tyrosine phosphatase CD45."
Walzel H., Schulz U., Neels P., Brock J.
Immunol. Lett. 67:193-202(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Placenta.
[22]"Regulation of CD45-induced signaling by galectin-1 in Burkitt lymphoma B cells."
Fouillit M., Joubert-Caron R., Poirier F., Bourin P., Monostori E., Levi-Strauss M., Raphael M., Bladier D., Caron M.
Glycobiology 10:413-419(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[23]"Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation."
Tinari N., Kuwabara I., Huflejt M.E., Shen P.F., Iacobelli S., Liu F.-T.
Int. J. Cancer 91:167-172(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LGALS3BP.
[24]"Presentation of galectin-1 by extracellular matrix triggers T cell death."
He J., Baum L.G.
J. Biol. Chem. 279:4705-4712(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[25]"Abnormal proteins in primary breast cancer tissues from 25 Sudanese patients."
Ahamed M.E., Ahmed M.E., Eltoum A.M., Altahir G.O., Ahmed K.M., Harbi S.O., Stansalas J., Mohamed A.O.
Eur. J. Inflamm. 6:115-121(2008)
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Mammary cancer.
[26]"A primate subfamily of galectins expressed at the maternal-fetal interface that promote immune cell death."
Than N.G., Romero R., Goodman M., Weckle A., Xing J., Dong Z., Xu Y., Tarquini F., Szilagyi A., Gal P., Hou Z., Tarca A.L., Kim C.J., Kim J.S., Haidarian S., Uddin M., Bohn H., Benirschke K. expand/collapse author list , Santolaya-Forgas J., Grossman L.I., Erez O., Hassan S.S., Zavodszky P., Papp Z., Wildman D.E.
Proc. Natl. Acad. Sci. U.S.A. 106:9731-9736(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[27]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[30]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding."
Lopez-Lucendo M.F., Solis D., Andre S., Hirabayashi J., Kasai K., Kaltner H., Gabius H.-J., Romero A.
J. Mol. Biol. 343:957-970(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE, SUBUNIT.
[32]"Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1."
Nishi N., Abe A., Iwaki J., Yoshida H., Itoh A., Shoji H., Kamitori S., Hirabayashi J., Nakamura T.
Glycobiology 18:1065-1073(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-135 IN COMPLEX WITH LACTOSE, INTERACTION WITH CD2; CD3; CD7; CD43 AND CD45, SUBUNIT, FUNCTION.
[33]"Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose."
Di Lella S., Ma L., Ricci J.C., Rabinovich G.A., Asher S.A., Alvarez R.M.S.
Biochemistry 48:786-791(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14829 mRNA. Translation: CAA32938.1.
J04456 mRNA. Translation: AAA36170.1.
X15256 mRNA. Translation: CAA33328.1.
EU363770 mRNA. Translation: ACA58297.1.
M57678 Genomic DNA. Translation: AAB00777.1.
AB097036 mRNA. Translation: BAC77389.1.
CR456511 mRNA. Translation: CAG30397.1.
AK312161 mRNA. Translation: BAG35095.1.
BT006775 mRNA. Translation: AAP35421.1.
Z83844 Genomic DNA. Translation: CAB42897.1.
CH471095 Genomic DNA. Translation: EAW60178.1.
BC001693 mRNA. Translation: AAH01693.1.
BC020675 mRNA. Translation: AAH20675.1.
CCDSCCDS13954.1.
PIRLNHUGB. A37134.
RefSeqNP_002296.1. NM_002305.3.
UniGeneHs.445351.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZWX-ray1.70A/B2-135[»]
1W6MX-ray2.30A/B2-135[»]
1W6NX-ray1.65A/B2-135[»]
1W6OX-ray1.90A/B2-135[»]
1W6PX-ray1.80A/B2-135[»]
1W6QX-ray2.10A/B2-135[»]
2KM2NMR-A/B2-135[»]
2ZKNX-ray1.86A/B2-135[»]
3OY8X-ray2.19A/B2-135[»]
3OYWX-ray2.50A/B2-135[»]
3T2TX-ray1.90A/B1-135[»]
3W58X-ray1.58A/B/C/D2-135[»]
3W59X-ray2.10A/B/C/D2-135[»]
ProteinModelPortalP09382.
SMRP09382. Positions 2-135.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110147. 38 interactions.
DIPDIP-46153N.
IntActP09382. 7 interactions.
MINTMINT-3306493.
STRING9606.ENSP00000215909.

Chemistry

BindingDBP09382.
ChEMBLCHEMBL4915.

PTM databases

PhosphoSiteP09382.

Polymorphism databases

DMDM126155.

2D gel databases

DOSAC-COBS-2DPAGEP09382.
REPRODUCTION-2DPAGEIPI00219219.
P09382.
SWISS-2DPAGEP09382.
UCD-2DPAGEP09382.

Proteomic databases

MaxQBP09382.
PaxDbP09382.
PeptideAtlasP09382.
PRIDEP09382.

Protocols and materials databases

DNASU3956.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215909; ENSP00000215909; ENSG00000100097.
GeneID3956.
KEGGhsa:3956.
UCSCuc003atn.3. human.

Organism-specific databases

CTD3956.
GeneCardsGC22P038071.
HGNCHGNC:6561. LGALS1.
HPACAB002157.
HPA000646.
HPA000687.
HPA001130.
MIM150570. gene.
neXtProtNX_P09382.
PharmGKBPA30337.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279327.
HOGENOMHOG000059539.
HOVERGENHBG006255.
InParanoidP09382.
KOK06830.
OMAGHEFKFP.
OrthoDBEOG7NKKN0.
PhylomeDBP09382.
TreeFamTF315551.

Gene expression databases

ArrayExpressP09382.
BgeeP09382.
CleanExHS_LGALS1.
GenevestigatorP09382.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR015535. Galectin_1.
IPR001079. Galectin_CRD.
[Graphical view]
PANTHERPTHR11346:SF30. PTHR11346:SF30. 1 hit.
PfamPF00337. Gal-bind_lectin. 1 hit.
[Graphical view]
SMARTSM00908. Gal-bind_lectin. 1 hit.
SM00276. GLECT. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS51304. GALECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLGALS1. human.
EvolutionaryTraceP09382.
GeneWikiGalectin-1.
LGALS1.
GenomeRNAi3956.
NextBio15523.
PMAP-CutDBP09382.
PROP09382.
SOURCESearch...

Entry information

Entry nameLEG1_HUMAN
AccessionPrimary (citable) accession number: P09382
Secondary accession number(s): B2R5E8, Q9UDK5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM