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Protein

Galectin-9

Gene

LGALS9

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

Functioni

Binds galactosides (PubMed:18005988). Has high affinity for the Forssman pentasaccharide (PubMed:18005988). Ligand for HAVCR2/TIM3 (PubMed:16286920). Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death (PubMed:16286920). Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth (By similarity). Ligand for P4HB; the interaction retains P4HB at the cell surface of Th2 T-helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). Ligand for CD44; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (By similarity). Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation (PubMed:23817958). Expands regulatory T-cells and induces cytotoxic T-cell apoptosis following virus infection (PubMed:20209097). Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells (PubMed:24465902, PubMed:16116184). Inhibits degranulation and induces apoptosis of mast cells (PubMed:24465902). Induces maturation and migration of dendritic cells (PubMed:25754930, PubMed:16116184). Inhibits natural killer (NK) cell function (PubMed:23408620). Can transform NK cell phenotype from peripheral to decidual during pregnancy (PubMed:25578313). Astrocyte derived galectin-9 enhances microglial TNF production (By similarity). May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion (By similarity). Highly selective to the anion urate (By similarity).By similarity11 Publications
Isoform 2: Acts as an eosinophil chemoattractant (PubMed:9642261). It also inhibits angiogenesis (PubMed:24333696). Suppresses IFNG production by natural killer cells (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei48 – 481Beta-galactoside 1
Binding sitei61 – 611Beta-galactoside 1
Binding sitei65 – 651Beta-galactoside 1
Binding sitei75 – 751Beta-galactoside 1
Binding sitei267 – 2671Beta-galactoside 2
Binding sitei271 – 2711Beta-galactoside 2
Binding sitei281 – 2811Beta-galactoside 2By similarity

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • disaccharide binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • galactose binding Source: ProtInc
  • signal transducer activity Source: UniProtKB

GO - Biological processi

  • cellular response to interferon-gamma Source: UniProtKB
  • cellular response to virus Source: UniProtKB
  • chemotaxis Source: UniProtKB-KW
  • ERK1 and ERK2 cascade Source: UniProtKB
  • female pregnancy Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • maternal process involved in female pregnancy Source: UniProtKB
  • natural killer cell tolerance induction Source: UniProtKB
  • negative regulation of activated T cell proliferation Source: UniProtKB
  • negative regulation of CD4-positive, alpha-beta T cell proliferation Source: UniProtKB
  • negative regulation of chemokine production Source: UniProtKB
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of interferon-gamma production Source: UniProtKB
  • negative regulation of mast cell degranulation Source: UniProtKB
  • negative regulation of natural killer cell mediated cytotoxicity Source: UniProtKB
  • negative regulation of tumor necrosis factor production Source: UniProtKB
  • p38MAPK cascade Source: UniProtKB
  • positive regulation of activated T cell autonomous cell death Source: UniProtKB
  • positive regulation of CD4-positive, alpha-beta T cell proliferation Source: UniProtKB
  • positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: UniProtKB
  • positive regulation of dendritic cell apoptotic process Source: UniProtKB
  • positive regulation of dendritic cell chemotaxis Source: UniProtKB
  • positive regulation of dendritic cell differentiation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of interferon-gamma secretion Source: UniProtKB
  • positive regulation of interleukin-10 secretion Source: UniProtKB
  • positive regulation of interleukin-12 secretion Source: UniProtKB
  • positive regulation of interleukin-13 secretion Source: UniProtKB
  • positive regulation of interleukin-1 beta secretion Source: UniProtKB
  • positive regulation of interleukin-4 production Source: UniProtKB
  • positive regulation of interleukin-6 secretion Source: UniProtKB
  • positive regulation of interleukin-8 secretion Source: UniProtKB
  • positive regulation of monocyte chemotactic protein-1 production Source: UniProtKB
  • positive regulation of NF-kappaB import into nucleus Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Source: UniProtKB
  • positive regulation of transforming growth factor beta production Source: UniProtKB
  • positive regulation of tumor necrosis factor secretion Source: UniProtKB
  • positive regulation of viral entry into host cell Source: UniProtKB
  • response to interleukin-1 Source: UniProtKB
  • response to lipopolysaccharide Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Immunity

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiR-HSA-451927. Interleukin-2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Galectin-9
Short name:
Gal-9
Alternative name(s):
Ecalectin
Tumor antigen HOM-HD-21
Gene namesi
Name:LGALS9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:6570. LGALS9.

Subcellular locationi

Isoform 2 :
Isoform 3 :

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • intracellular Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30347.

Chemistry

ChEMBLiCHEMBL5474.

Polymorphism and mutation databases

BioMutaiLGALS9.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Galectin-9PRO_0000076946Add
BLAST

Proteomic databases

EPDiO00182.
MaxQBiO00182.
PaxDbiO00182.
PeptideAtlasiO00182.
PRIDEiO00182.

PTM databases

iPTMnetiO00182.
PhosphoSiteiO00182.

Expressioni

Tissue specificityi

Peripheral blood leukocytes and lymphatic tissues. Expressed in lung, liver, breast and kidney with higher levels in tumor endothelial cells than normal endothelium (at protein level) (PubMed:24333696). Expressed in trophoblast cells in decidua and placenta in pregnancy (at protein level) (PubMed:23242525, PubMed:25578313). Isoform 2 is the most abundant isoform expressed in endothelial cells (PubMed:24333696). Upon endothelial cell activation isoform 2 expression decreases while expression of isoform 3 and isoform 5 increases (PubMed:24333696). Isoform 4 decreases in pathological pregnancy (PubMed:23242525).3 Publications

Inductioni

By toll-like receptor ligands zymosan (TLR2 ligand), polyinosinic:polycytidylic acid (poly I:C) (TLR3 ligand) and lipopolysaccharides (LPS) (TLR4 ligand) and by proinflammatory cytokines INFG, TNFA, IL1A and IL1B in mesenchymal stromal cells (PubMed:23817958). By INFG in macrophages (PubMed:20209097). Up-regulated in dendritic cells following infection with dengue virus (PubMed:25754930). Up-regulated in Kupffer cells following infection with hepatitis C virus (PubMed:20209097). Up-regulated in plasma following infection with HIV-1 (PubMed:24786365).4 Publications

Gene expression databases

BgeeiO00182.
CleanExiHS_LGALS9.
ExpressionAtlasiO00182. baseline and differential.
GenevisibleiO00182. HS.

Organism-specific databases

HPAiHPA046876.
HPA047218.

Interactioni

Subunit structurei

Monomer.2 Publications

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110156. 78 interactions.
IntActiO00182. 12 interactions.
STRINGi9606.ENSP00000378856.

Chemistry

BindingDBiO00182.

Structurei

Secondary structure

1
355
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi10 – 123Combined sources
Beta strandi15 – 206Combined sources
Beta strandi30 – 378Combined sources
Beta strandi39 – 413Combined sources
Beta strandi43 – 5614Combined sources
Beta strandi58 – 658Combined sources
Beta strandi71 – 788Combined sources
Beta strandi86 – 894Combined sources
Beta strandi98 – 1058Combined sources
Beta strandi107 – 1148Combined sources
Beta strandi117 – 1237Combined sources
Helixi128 – 1303Combined sources
Beta strandi133 – 14614Combined sources
Beta strandi193 – 1975Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi240 – 2478Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi253 – 2608Combined sources
Beta strandi263 – 2719Combined sources
Turni272 – 2754Combined sources
Beta strandi276 – 2838Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi305 – 3128Combined sources
Beta strandi314 – 3218Combined sources
Beta strandi324 – 3307Combined sources
Helixi336 – 3383Combined sources
Beta strandi341 – 35414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EAKX-ray1.97A/B/C1-148[»]
2EALX-ray1.85A/B1-148[»]
2YY1X-ray2.17A1-147[»]
2ZHKX-ray1.80A/B1-148[»]
2ZHLX-ray1.75A/B/C/D1-148[»]
2ZHMX-ray1.84A/B/C/D1-148[»]
2ZHNX-ray1.30A1-148[»]
3LSDX-ray2.03A6-148[»]
3LSEX-ray2.69A6-148[»]
3NV1X-ray1.50A218-355[»]
3NV2X-ray2.34A218-355[»]
3NV3X-ray1.57A218-355[»]
3NV4X-ray1.99A218-355[»]
3WLUX-ray1.40A/B/C/D5-148[»]
3WV6X-ray1.95A/B1-148[»]
A/B178-355[»]
ProteinModelPortaliO00182.
SMRiO00182. Positions 3-355.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00182.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 148132Galectin 1PROSITE-ProRule annotationAdd
BLAST
Domaini227 – 355129Galectin 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 887Beta-galactoside binding 1
Regioni287 – 2937Beta-galactoside binding 2By similarity

Domaini

Contains two homologous but distinct carbohydrate-binding domains.

Sequence similaritiesi

Contains 2 galectin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00760000119105.
HOGENOMiHOG000290194.
HOVERGENiHBG002412.
InParanoidiO00182.
KOiK10093.
OMAiANEWGNE.
OrthoDBiEOG73Z2TM.
PhylomeDBiO00182.
TreeFamiTF315551.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 2 hits.
[Graphical view]
SMARTiSM00908. Gal-bind_lectin. 2 hits.
SM00276. GLECT. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS51304. GALECTIN. 2 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00182-1) [UniParc]FASTAAdd to basket

Also known as: Long, Gal-9FL1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAFSGSQAPY LSPAVPFSGT IQGGLQDGLQ ITVNGTVLSS SGTRFAVNFQ
60 70 80 90 100
TGFSGNDIAF HFNPRFEDGG YVVCNTRQNG SWGPEERKTH MPFQKGMPFD
110 120 130 140 150
LCFLVQSSDF KVMVNGILFV QYFHRVPFHR VDTISVNGSV QLSYISFQNP
160 170 180 190 200
RTVPVQPAFS TVPFSQPVCF PPRPRGRRQK PPGVWPANPA PITQTVIHTV
210 220 230 240 250
QSAPGQMFST PAIPPMMYPH PAYPMPFITT ILGGLYPSKS ILLSGTVLPS
260 270 280 290 300
AQRFHINLCS GNHIAFHLNP RFDENAVVRN TQIDNSWGSE ERSLPRKMPF
310 320 330 340 350
VRGQSFSVWI LCEAHCLKVA VDGQHLFEYY HRLRNLPTIN RLEVGGDIQL

THVQT
Length:355
Mass (Da):39,518
Last modified:July 15, 1998 - v2
Checksum:i4748C22FCAFA536A
GO
Isoform 2 (identifier: O00182-2) [UniParc]FASTAAdd to basket

Also known as: Medium, Gal-9delta51 Publication

, D51 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     149-180: Missing.

Show »
Length:323
Mass (Da):35,888
Checksum:i1A3EB2941FC7F377
GO
Isoform 3 (identifier: O00182-3) [UniParc]FASTAAdd to basket

Also known as: Short, Gal-9delta5/61 Publication

, D5/61 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     149-180: Missing.
     181-192: Missing.

Show »
Length:311
Mass (Da):34,691
Checksum:i3D00232FE39D776C
GO
Isoform 4 (identifier: O00182-4) [UniParc]FASTAAdd to basket

Also known as: Gal-9delta5/101 Publication

, D5/101 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     149-180: Missing.
     254-355: FHINLCSGNH...GDIQLTHVQT → CGSCVKLTASRWPWMVSTCLNTTIA

Show »
Length:246
Mass (Da):26,777
Checksum:i414EB1F6493EE81E
GO
Isoform 5 (identifier: O00182-5) [UniParc]FASTAAdd to basket

Also known as: Gal-9delta5/6/101 Publication

, D5/6/101 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     149-180: Missing.
     181-192: Missing.
     254-355: FHINLCSGNH...GDIQLTHVQT → CGSCVKLTASRWPWMVSTCLNTTIA

Show »
Length:234
Mass (Da):25,579
Checksum:i29B8BF54B3F32BC3
GO
Isoform 6 (identifier: O00182-6) [UniParc]FASTAAdd to basket

Also known as: D61 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     181-192: Missing.

Show »
Length:343
Mass (Da):38,321
Checksum:i79BEC0B506CFA9DF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481N → D in CAB93851 (Ref. 6) Curated
Sequence conflicti79 – 813NGS → KGR in CAB93851 (Ref. 6) Curated
Sequence conflicti88 – 881K → R in CAA88922 (PubMed:9045665).Curated
Sequence conflicti89 – 891T → M in CAB93851 (Ref. 6) Curated
Sequence conflicti93 – 931F → S in BAD96952 (Ref. 7) Curated
Sequence conflicti135 – 1351S → F in CAA88922 (PubMed:9045665).Curated
Sequence conflicti270 – 2701P → L in CAA88922 (PubMed:9045665).Curated
Sequence conflicti313 – 3131E → G in CAA88922 (PubMed:9045665).Curated
Sequence conflicti326 – 3261L → V in CAB93851 (Ref. 6) Curated
Sequence conflicti341 – 3411R → K in CAB93851 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51G → S.2 Publications
Corresponds to variant rs3751093 [ dbSNP | Ensembl ].
VAR_020453

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei149 – 18032Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 5 Publications1 PublicationVSP_003096Add
BLAST
Alternative sequencei181 – 19212Missing in isoform 3, isoform 5 and isoform 6. 2 PublicationsVSP_057842Add
BLAST
Alternative sequencei254 – 355102FHINL…THVQT → CGSCVKLTASRWPWMVSTCL NTTIA in isoform 4 and isoform 5. 1 PublicationVSP_057843Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49107 mRNA. Translation: CAA88922.1.
AB006782 mRNA. Translation: BAA22166.1.
AB005894 mRNA. Translation: BAA31542.1.
AB003517 mRNA. Translation: BAF76327.1.
AB008492 mRNA. Translation: BAF76328.1.
AB040130 Genomic DNA. Translation: BAB83623.1.
AB040130 Genomic DNA. Translation: BAB83625.1.
AB040130 Genomic DNA. Translation: BAB83624.1.
AJ288083
, AJ288084, AJ288085, AJ288086, AJ288087, AJ288088, AJ288089, AJ288090 Genomic DNA. Translation: CAB93851.1.
AK223232 mRNA. Translation: BAD96952.1.
AC015688 Genomic DNA. No translation available.
CH471159 Genomic DNA. Translation: EAW51037.1.
CH471159 Genomic DNA. Translation: EAW51038.1.
CH471159 Genomic DNA. Translation: EAW51039.1.
CH471159 Genomic DNA. Translation: EAW51044.1.
BC105942 mRNA. Translation: AAI05943.1.
BC105944 mRNA. Translation: AAI05945.1.
BC110340 mRNA. Translation: AAI10341.1.
CCDSiCCDS11222.1. [O00182-1]
CCDS32592.1. [O00182-2]
RefSeqiNP_002299.2. NM_002308.3. [O00182-2]
NP_033665.1. NM_009587.2. [O00182-1]
XP_006721955.1. XM_006721892.1. [O00182-3]
XP_006721957.1. XM_006721894.2. [O00182-4]
XP_006721958.1. XM_006721895.2. [O00182-5]
UniGeneiHs.81337.

Genome annotation databases

EnsembliENST00000302228; ENSP00000306228; ENSG00000168961. [O00182-2]
ENST00000313648; ENSP00000318214; ENSG00000168961. [O00182-4]
ENST00000395473; ENSP00000378856; ENSG00000168961. [O00182-1]
GeneIDi3965.
KEGGihsa:3965.
UCSCiuc002gzp.4. human. [O00182-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Galectin-9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49107 mRNA. Translation: CAA88922.1.
AB006782 mRNA. Translation: BAA22166.1.
AB005894 mRNA. Translation: BAA31542.1.
AB003517 mRNA. Translation: BAF76327.1.
AB008492 mRNA. Translation: BAF76328.1.
AB040130 Genomic DNA. Translation: BAB83623.1.
AB040130 Genomic DNA. Translation: BAB83625.1.
AB040130 Genomic DNA. Translation: BAB83624.1.
AJ288083
, AJ288084, AJ288085, AJ288086, AJ288087, AJ288088, AJ288089, AJ288090 Genomic DNA. Translation: CAB93851.1.
AK223232 mRNA. Translation: BAD96952.1.
AC015688 Genomic DNA. No translation available.
CH471159 Genomic DNA. Translation: EAW51037.1.
CH471159 Genomic DNA. Translation: EAW51038.1.
CH471159 Genomic DNA. Translation: EAW51039.1.
CH471159 Genomic DNA. Translation: EAW51044.1.
BC105942 mRNA. Translation: AAI05943.1.
BC105944 mRNA. Translation: AAI05945.1.
BC110340 mRNA. Translation: AAI10341.1.
CCDSiCCDS11222.1. [O00182-1]
CCDS32592.1. [O00182-2]
RefSeqiNP_002299.2. NM_002308.3. [O00182-2]
NP_033665.1. NM_009587.2. [O00182-1]
XP_006721955.1. XM_006721892.1. [O00182-3]
XP_006721957.1. XM_006721894.2. [O00182-4]
XP_006721958.1. XM_006721895.2. [O00182-5]
UniGeneiHs.81337.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EAKX-ray1.97A/B/C1-148[»]
2EALX-ray1.85A/B1-148[»]
2YY1X-ray2.17A1-147[»]
2ZHKX-ray1.80A/B1-148[»]
2ZHLX-ray1.75A/B/C/D1-148[»]
2ZHMX-ray1.84A/B/C/D1-148[»]
2ZHNX-ray1.30A1-148[»]
3LSDX-ray2.03A6-148[»]
3LSEX-ray2.69A6-148[»]
3NV1X-ray1.50A218-355[»]
3NV2X-ray2.34A218-355[»]
3NV3X-ray1.57A218-355[»]
3NV4X-ray1.99A218-355[»]
3WLUX-ray1.40A/B/C/D5-148[»]
3WV6X-ray1.95A/B1-148[»]
A/B178-355[»]
ProteinModelPortaliO00182.
SMRiO00182. Positions 3-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110156. 78 interactions.
IntActiO00182. 12 interactions.
STRINGi9606.ENSP00000378856.

Chemistry

BindingDBiO00182.
ChEMBLiCHEMBL5474.

PTM databases

iPTMnetiO00182.
PhosphoSiteiO00182.

Polymorphism and mutation databases

BioMutaiLGALS9.

Proteomic databases

EPDiO00182.
MaxQBiO00182.
PaxDbiO00182.
PeptideAtlasiO00182.
PRIDEiO00182.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302228; ENSP00000306228; ENSG00000168961. [O00182-2]
ENST00000313648; ENSP00000318214; ENSG00000168961. [O00182-4]
ENST00000395473; ENSP00000378856; ENSG00000168961. [O00182-1]
GeneIDi3965.
KEGGihsa:3965.
UCSCiuc002gzp.4. human. [O00182-1]

Organism-specific databases

CTDi3965.
GeneCardsiLGALS9.
HGNCiHGNC:6570. LGALS9.
HPAiHPA046876.
HPA047218.
MIMi601879. gene.
neXtProtiNX_O00182.
PharmGKBiPA30347.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00760000119105.
HOGENOMiHOG000290194.
HOVERGENiHBG002412.
InParanoidiO00182.
KOiK10093.
OMAiANEWGNE.
OrthoDBiEOG73Z2TM.
PhylomeDBiO00182.
TreeFamiTF315551.

Enzyme and pathway databases

ReactomeiR-HSA-451927. Interleukin-2 signaling.

Miscellaneous databases

ChiTaRSiLGALS9. human.
EvolutionaryTraceiO00182.
GeneWikiiLGALS9.
GenomeRNAii3965.
PROiO00182.
SOURCEiSearch...

Gene expression databases

BgeeiO00182.
CleanExiHS_LGALS9.
ExpressionAtlasiO00182. baseline and differential.
GenevisibleiO00182. HS.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 2 hits.
[Graphical view]
SMARTiSM00908. Gal-bind_lectin. 2 hits.
SM00276. GLECT. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS51304. GALECTIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular definition of a novel human galectin which is immunogenic in patients with Hodgkin's disease."
    Tuereci O., Schmitt H., Fadle N., Pfreundschuh M., Sahin U.
    J. Biol. Chem. 272:6416-6422(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Spleen.
  2. "Human galectin-9 isoform full-length cDNA from gastric adenocarcinoma."
    Kato S.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Gastric carcinoma.
  3. "Human ecalectin, a variant of human galectin-9, is a novel eosinophil chemoattractant produced by T lymphocytes."
    Matsumoto R., Matsumoto H., Seki M., Hata M., Asano Y., Kanegasaki S., Stevens R.L., Hirashima M.
    J. Biol. Chem. 273:16976-16984(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, VARIANT SER-5.
  4. "Cloning and expression of human urate transporter mRNA."
    Nakajima H., Shichiri M., Hamaguchi T.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Kidney and Stomach.
  5. "Homo sapiens galectin-9 (LGALS9) / ecalectin gene."
    Akiyama S.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 3).
  6. "Genomic organization of the human galectin-9 gene."
    Graessler J., Spitzenberger F., Schroeder H.E.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT SER-5.
    Tissue: Gastric mucosa.
  8. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] (ISOFORM 2).
    Tissue: Colon.
  11. Cited for: FUNCTION.
  12. "The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity."
    Zhu C., Anderson A.C., Schubart A., Xiong H., Imitola J., Khoury S.J., Zheng X.X., Strom T.B., Kuchroo V.K.
    Nat. Immunol. 6:1245-1252(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS LIGAND FOR HAVCR2/TIM3.
  13. Cited for: FUNCTION, INDUCTION.
  14. "Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry."
    Bi S., Hong P.W., Lee B., Baum L.G.
    Proc. Natl. Acad. Sci. U.S.A. 108:10650-10655(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS LIGAND FOR P4HB.
  15. "Profiling Lgals9 splice variant expression at the fetal-maternal interface: implications in normal and pathological human pregnancy."
    Heusschen R., Freitag N., Tirado-Gonzalez I., Barrientos G., Moschansky P., Munoz-Fernandez R., Leno-Duran E., Klapp B.F., Thijssen V.L., Blois S.M.
    Biol. Reprod. 88:22-22(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORM 6), TISSUE SPECIFICITY.
  16. "Proinflammatory stimuli induce galectin-9 in human mesenchymal stromal cells to suppress T-cell proliferation."
    Gieseke F., Kruchen A., Tzaribachev N., Bentzien F., Dominici M., Muller I.
    Eur. J. Immunol. 43:2741-2749(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
  17. Cited for: FUNCTION.
  18. "Galectin-9 is rapidly released during acute HIV-1 infection and remains sustained at high levels despite viral suppression even in elite controllers."
    Tandon R., Chew G.M., Byron M.M., Borrow P., Niki T., Hirashima M., Barbour J.D., Norris P.J., Lanteri M.C., Martin J.N., Deeks S.G., Ndhlovu L.C.
    AIDS Res. Hum. Retroviruses 30:654-664(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  19. "Endothelial LGALS9 splice variant expression in endothelial cell biology and angiogenesis."
    Heusschen R., Schulkens I.A., van Beijnum J., Griffioen A.W., Thijssen V.L.
    Biochim. Biophys. Acta 1842:284-292(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
  20. "Galectin-9 enhances cytokine secretion, but suppresses survival and degranulation, in human mast cell line."
    Kojima R., Ohno T., Iikura M., Niki T., Hirashima M., Iwaya K., Tsuda H., Nonoyama S., Matsuda A., Saito H., Matsumoto K., Nakae S.
    PLoS ONE 9:E86106-E86106(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "The Galectin-9/Tim-3 pathway is involved in the regulation of NK cell function at the maternal-fetal interface in early pregnancy."
    Li Y.H., Zhou W.H., Tao Y., Wang S.C., Jiang Y.L., Zhang D., Piao H.L., Fu Q., Li D.J., Du M.R.
    Cell. Mol. Immunol. 13:73-81(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  22. "Up-regulation of galectin-9 induces cell migration in human dendritic cells infected with dengue virus."
    Hsu Y.L., Wang M.Y., Ho L.J., Huang C.Y., Lai J.H.
    J. Cell. Mol. Med. 19:1065-1076(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  23. "Structural analysis of the human galectin-9 N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue."
    Nagae M., Nishi N., Nakamura-Tsuruta S., Hirabayashi J., Wakatsuki S., Kato R.
    J. Mol. Biol. 375:119-135(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-148 IN COMPLEXES WITH LACTOSE AND COMPLEX BETA-GALACTOSIDE, SUBUNIT, CARBOHYDRATE SPECIFICITY, FUNCTION.
  24. "Crystal structure of N-terminal domain of human galectin-9 containing L-acetyllactosamine."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 1-150 IN COMPLEX WITH L-ACETYLLACTOSAMINE.
  25. "Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain."
    Nagae M., Nishi N., Murata T., Usui T., Nakamura T., Wakatsuki S., Kato R.
    Glycobiology 19:112-117(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 1-148 IN COMPLEXES WITH N-ACETYLLACTOSAMINE OLIGOMERS, FUNCTION.
  26. "X-ray structures of human galectin-9 C-terminal domain in complexes with a biantennary oligosaccharide and sialyllactose."
    Yoshida H., Teraoka M., Nishi N., Nakakita S., Nakamura T., Hirashima M., Kamitori S.
    J. Biol. Chem. 285:36969-36976(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 186-323 IN COMPLEXES WITH OLIGOSACCHARIDES.

Entry informationi

Entry nameiLEG9_HUMAN
AccessioniPrimary (citable) accession number: O00182
Secondary accession number(s): A7VJG6
, F8W9W4, O14532, O75028, Q3B8N1, Q53FQ0, Q8WYQ7, Q9NQ58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: July 6, 2016
This is version 157 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, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.