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Protein

Galectin-1

Gene

LGALS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Beta-galactoside
Binding sitei62 – 621Beta-galactoside

GO - Molecular functioni

  • lactose binding Source: Ensembl
  • poly(A) RNA binding Source: UniProtKB
  • signal transducer activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
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 namesi
Name:LGALS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:6561. LGALS1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: Ensembl
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular space Source: BHF-UCL
  • intracellular Source: LIFEdb
  • nucleus Source: Ensembl
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30337.

Chemistry

ChEMBLiCHEMBL4915.

Polymorphism and mutation databases

BioMutaiLGALS1.
DMDMi126155.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources3 Publications
Chaini2 – 135134Galectin-1PRO_0000076917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei13 – 131N6-acetyllysineBy similarity
Modified residuei29 – 291N6-acetyllysineCombined sources
Modified residuei30 – 301Phosphoserine; by FAM20C1 Publication
Modified residuei108 – 1081N6-acetyllysine; alternateBy similarity
Modified residuei108 – 1081N6-succinyllysine; alternateBy similarity
Modified residuei128 – 1281N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP09382.
MaxQBiP09382.
PaxDbiP09382.
PeptideAtlasiP09382.
PRIDEiP09382.
TopDownProteomicsiP09382.

2D gel databases

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

PTM databases

iPTMnetiP09382.
PhosphoSiteiP09382.
SwissPalmiP09382.

Miscellaneous databases

PMAP-CutDBP09382.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiENSG00000100097.
CleanExiHS_LGALS1.
ExpressionAtlasiP09382. baseline and differential.
GenevisibleiP09382. HS.

Organism-specific databases

HPAiCAB002157.
HPA000646.
HPA000687.
HPA001130.

Interactioni

Subunit structurei

Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6, CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-N-acetyllactosamine). Interacts with SUSD2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ALCAMQ137403EBI-1048875,EBI-1188108
CD6P302032EBI-1048875,EBI-2873748
KDRP359683EBI-1048875,EBI-1005487
PTPRCP085752EBI-1048875,EBI-1341

Protein-protein interaction databases

BioGridi110147. 95 interactions.
DIPiDIP-46153N.
IntActiP09382. 21 interactions.
MINTiMINT-3306493.
STRINGi9606.ENSP00000215909.

Chemistry

BindingDBiP09382.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210Combined sources
Beta strandi18 – 247Combined sources
Beta strandi30 – 389Combined sources
Beta strandi41 – 5212Combined sources
Beta strandi55 – 6511Combined sources
Beta strandi73 – 764Combined sources
Beta strandi84 – 929Combined sources
Beta strandi94 – 1007Combined sources
Helixi102 – 1043Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi116 – 13318Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4Q1PX-ray1.46A/B1-135[»]
4Q1RX-ray1.47A/B1-135[»]
4Q26X-ray1.40A/B/G/H1-135[»]
4Q27X-ray1.20A/B1-135[»]
4Q2FX-ray1.40A/B1-135[»]
4XBLX-ray1.93A/B1-135[»]
4Y1UX-ray1.76A/B3-135[»]
4Y1VX-ray2.32A/B3-135[»]
4Y1XX-ray2.45A/B3-135[»]
4Y1YX-ray1.86A/B4-135[»]
4Y1ZX-ray2.23A/B3-135[»]
4Y20X-ray2.20A/B3-135[»]
4Y22X-ray2.50A/B3-135[»]
4Y24X-ray2.32A/B3-135[»]
ProteinModelPortaliP09382.
SMRiP09382. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09382.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 135132GalectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 495Beta-galactoside binding
Regioni69 – 724Beta-galactoside binding

Sequence similaritiesi

Contains 1 galectin domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00440000034263.
HOGENOMiHOG000059539.
HOVERGENiHBG006255.
InParanoidiP09382.
KOiK06830.
OMAiCNSKEDG.
OrthoDBiEOG091G0S7H.
PhylomeDBiP09382.
TreeFamiTF315551.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 1 hit.
[Graphical view]
SMARTiSM00908. Gal-bind_lectin. 1 hit.
SM00276. GLECT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51304. GALECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF
60 70 80 90 100
NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK
110 120 130
LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD
Length:135
Mass (Da):14,716
Last modified:January 23, 2007 - v2
Checksum:i2FBB8D7A1FC0F1F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13954.1.
PIRiA37134. LNHUGB.
RefSeqiNP_002296.1. NM_002305.3.
UniGeneiHs.445351.

Genome annotation databases

EnsembliENST00000215909; ENSP00000215909; ENSG00000100097.
GeneIDi3956.
KEGGihsa:3956.
UCSCiuc003atn.4. human.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Galectin-1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13954.1.
PIRiA37134. LNHUGB.
RefSeqiNP_002296.1. NM_002305.3.
UniGeneiHs.445351.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4Q1PX-ray1.46A/B1-135[»]
4Q1RX-ray1.47A/B1-135[»]
4Q26X-ray1.40A/B/G/H1-135[»]
4Q27X-ray1.20A/B1-135[»]
4Q2FX-ray1.40A/B1-135[»]
4XBLX-ray1.93A/B1-135[»]
4Y1UX-ray1.76A/B3-135[»]
4Y1VX-ray2.32A/B3-135[»]
4Y1XX-ray2.45A/B3-135[»]
4Y1YX-ray1.86A/B4-135[»]
4Y1ZX-ray2.23A/B3-135[»]
4Y20X-ray2.20A/B3-135[»]
4Y22X-ray2.50A/B3-135[»]
4Y24X-ray2.32A/B3-135[»]
ProteinModelPortaliP09382.
SMRiP09382. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110147. 95 interactions.
DIPiDIP-46153N.
IntActiP09382. 21 interactions.
MINTiMINT-3306493.
STRINGi9606.ENSP00000215909.

Chemistry

BindingDBiP09382.
ChEMBLiCHEMBL4915.

PTM databases

iPTMnetiP09382.
PhosphoSiteiP09382.
SwissPalmiP09382.

Polymorphism and mutation databases

BioMutaiLGALS1.
DMDMi126155.

2D gel databases

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

Proteomic databases

EPDiP09382.
MaxQBiP09382.
PaxDbiP09382.
PeptideAtlasiP09382.
PRIDEiP09382.
TopDownProteomicsiP09382.

Protocols and materials databases

DNASUi3956.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215909; ENSP00000215909; ENSG00000100097.
GeneIDi3956.
KEGGihsa:3956.
UCSCiuc003atn.4. human.

Organism-specific databases

CTDi3956.
GeneCardsiLGALS1.
HGNCiHGNC:6561. LGALS1.
HPAiCAB002157.
HPA000646.
HPA000687.
HPA001130.
MIMi150570. gene.
neXtProtiNX_P09382.
PharmGKBiPA30337.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00440000034263.
HOGENOMiHOG000059539.
HOVERGENiHBG006255.
InParanoidiP09382.
KOiK06830.
OMAiCNSKEDG.
OrthoDBiEOG091G0S7H.
PhylomeDBiP09382.
TreeFamiTF315551.

Miscellaneous databases

ChiTaRSiLGALS1. human.
EvolutionaryTraceiP09382.
GeneWikiiGalectin-1.
LGALS1.
GenomeRNAii3956.
PMAP-CutDBP09382.
PROiP09382.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100097.
CleanExiHS_LGALS1.
ExpressionAtlasiP09382. baseline and differential.
GenevisibleiP09382. HS.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 1 hit.
[Graphical view]
SMARTiSM00908. Gal-bind_lectin. 1 hit.
SM00276. GLECT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51304. GALECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLEG1_HUMAN
AccessioniPrimary (citable) accession number: P09382
Secondary accession number(s): B2R5E8, Q9UDK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 201 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.