P09382 (LEG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	135 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.24 Ref.29
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.28 Ref.29
Subcellular location	Secreted › extracellular space › extracellular 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
Sequence similarities	Contains 1 galectin domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Ligand	Lectin
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell costimulation Inferred from electronic annotation. Source: Compara apoptotic process Traceable author statement PubMed 1713454. Source: ProtInc cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara cellular response to organic cyclic compound Inferred from electronic annotation. Source: Compara multicellular organismal response to stress Inferred from electronic annotation. Source: Compara myoblast differentiation Inferred from electronic annotation. Source: Compara negative regulation of cell-substrate adhesion Inferred from electronic annotation. Source: Compara negative regulation of neuron projection development Inferred from electronic annotation. Source: Compara plasma cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of erythrocyte aggregation Inferred from electronic annotation. Source: Compara regulation of apoptotic process Traceable author statement PubMed 16130169. Source: UniProtKB response to axon injury Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara cytoplasm Traceable author statement PubMed 16130169. Source: UniProtKB extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL nucleus Inferred from electronic annotation. Source: Compara proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	galactoside binding Inferred from electronic annotation. Source: InterPro lactose binding Inferred from electronic annotation. Source: Compara signal transducer activity Inferred from mutant phenotype Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.13 Ref.14 Ref.15

Chain

2 – 135

134

Galectin-1

PRO_0000076917

Regions

Domain

4 – 135

132

Galectin

Region

45 – 49

5

Beta-galactoside binding

Region

69 – 72

4

Beta-galactoside binding

Sites

Binding site

53

1

Beta-galactoside

Binding site

62

1

Beta-galactoside

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

29

1

N6-acetyllysine Ref.26

Secondary structure

1

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135

Helix Strand Turn

Details...

Beta strand

6 – 9

4

Beta strand

18 – 24

7

Beta strand

29 – 31

3

Beta strand

33 – 38

6

Beta strand

41 – 52

12

Beta strand

55 – 65

11

Beta strand

73 – 76

4

Beta strand

84 – 92

9

Beta strand

94 – 100

7

Helix

102 – 104

3

Beta strand

106 – 110

5

Beta strand

120 – 124

5

Beta strand

127 – 134

8

Sequences

	Sequence		Length	Mass (Da)
	P09382 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 2FBB8D7A1FC0F1F9	FASTA	135	14,716
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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]	"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, MASS SPECTROMETRY.
[27]	"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].
[28]	"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.
[29]	"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.
[30]	"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.

Web resources

Functional Glycomics Gateway - Glycan Binding

Galectin-1

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.

IPI

IPI00219219.

PIR

LNHUGB. A37134.

RefSeq

NP_002296.1. NM_002305.3.

UniGene

Hs.445351.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GZW	X-ray	1.70	A/B	2-134	[»]
1W6M	X-ray	2.30	A/B	4-135	[»]
1W6N	X-ray	1.65	A/B	4-134	[»]
1W6O	X-ray	1.90	A/B	4-134	[»]
1W6P	X-ray	1.80	A/B	4-134	[»]
1W6Q	X-ray	2.10	A/B	2-134	[»]
2KM2	NMR	-	A/B	2-135	[»]
2ZKN	X-ray	1.86	A/B	4-135	[»]
3OY8	X-ray	2.19	A/B	2-135	[»]
3OYW	X-ray	2.50	A/B	2-135	[»]
3T2T	X-ray	1.90	A/B	1-135	[»]

ProteinModelPortal

P09382.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46153N.

IntAct

P09382. 5 interactions.

MINT

MINT-3306493.

STRING

9606.ENSP00000215909.

PTM databases

PhosphoSite

P09382.

Polymorphism databases

DMDM

126155.

2D gel databases

DOSAC-COBS-2DPAGE

P09382.

REPRODUCTION-2DPAGE

IPI00219219.
P09382.

SWISS-2DPAGE

P09382.

UCD-2DPAGE

P09382.

Proteomic databases

PaxDb

P09382.

PeptideAtlas

P09382.

PRIDE

P09382.

Protocols and materials databases

DNASU

3956.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000215909; ENSP00000215909; ENSG00000100097.

GeneID

3956.

KEGG

hsa:3956.

UCSC

uc003atn.3. human.

Organism-specific databases

CTD

3956.

GeneCards

GC22P038071.

HGNC

HGNC:6561. LGALS1.

HPA

CAB002157.
HPA000646.

MIM

150570. gene.

neXtProt

NX_P09382.

PharmGKB

PA30337.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG279327.

HOGENOM

HOG000059539.

HOVERGEN

HBG006255.

InParanoid

P09382.

KO

K06830.

OMA

GGAWGAE.

OrthoDB

EOG4GXFP7.

PhylomeDB

P09382.

Gene expression databases

ArrayExpress

P09382.

Bgee

P09382.

CleanEx

HS_LGALS1.

Genevestigator

P09382.

GermOnline

ENSG00000100097. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.200. 1 hit.

InterPro

IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR015535. Galectin_1.
IPR001079. Galectin_CRD.
[Graphical view]

PANTHER

PTHR11346:SF30. PTHR11346:SF30. 1 hit.

Pfam

PF00337. Gal-bind_lectin. 1 hit.
[Graphical view]

SMART

SM00908. Gal-bind_lectin. 1 hit.
SM00276. GLECT. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS51304. GALECTIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P09382.

ChEMBL

CHEMBL4915.

ChiTaRS

LGALS1. human.

EvolutionaryTrace

P09382.

GenomeRNAi

3956.

NextBio

15523.

PMAP-CutDB

P09382.

SOURCE

Search...

Entry information

Entry name

LEG1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 165 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.