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O00182

- LEG9_HUMAN

UniProt

O00182 - LEG9_HUMAN

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Protein

Galectin-9

Gene

LGALS9

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

Functioni

Binds galactosides. Has high affinity for the Forssman pentasaccharide. May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. Inhibits cell proliferation. It is a ligand for HAVCR2/TIM3. Induces T-helper type 1 lymphocyte (Th1) death. Isoform Short acts as an eosinophil chemoattractant.3 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

  1. carbohydrate binding Source: UniProtKB
  2. galactose binding Source: ProtInc
  3. signal transducer activity Source: UniProtKB

GO - Biological processi

  1. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  2. signal transduction Source: GOC
Complete GO annotation...

Keywords - Ligandi

Lectin

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
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:6570. LGALS9.

Subcellular locationi

Cytoplasm By similarity. Secreted By similarity
Note: May also be secreted by a non-classical secretory pathway.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30347.

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiO00182.
PRIDEiO00182.

PTM databases

PhosphoSiteiO00182.

Expressioni

Tissue specificityi

Peripheral blood leukocytes and lymphatic tissues. Overexpressed in Hodgkin disease tissue.

Gene expression databases

BgeeiO00182.
CleanExiHS_LGALS9.
ExpressionAtlasiO00182. baseline and differential.
GenevestigatoriO00182.

Organism-specific databases

HPAiHPA046876.
HPA047218.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi110156. 68 interactions.
IntActiO00182. 12 interactions.
STRINGi9606.ENSP00000378856.

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 strandi225 – 2306Combined sources
Beta strandi240 – 2478Combined 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[»]
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

GeneTreeiENSGT00760000119105.
HOGENOMiHOG000290194.
HOVERGENiHBG002412.
InParanoidiO00182.
KOiK10093.
OMAiVCNTRQN.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

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

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 Short (identifier: O00182-2) [UniParc]FASTAAdd to Basket

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481N → D in CAB93851. 1 PublicationCurated
Sequence conflicti79 – 813NGS → KGR in CAB93851. 1 PublicationCurated
Sequence conflicti88 – 881K → R in CAA88922. (PubMed:9045665)Curated
Sequence conflicti89 – 891T → M in CAB93851. 1 PublicationCurated
Sequence conflicti93 – 931F → S in BAD96952. 1 PublicationCurated
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. 1 PublicationCurated
Sequence conflicti341 – 3411R → K in CAB93851. 1 PublicationCurated

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 Short. 5 PublicationsVSP_003096Add
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: 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.
CH471159 Genomic DNA. Translation: EAW51037.1.
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]
UniGeneiHs.81337.

Genome annotation databases

EnsembliENST00000302228; ENSP00000306228; ENSG00000168961. [O00182-2]
ENST00000395473; ENSP00000378856; ENSG00000168961. [O00182-1]
GeneIDi3965.
KEGGihsa:3965.
UCSCiuc002gzp.3. human. [O00182-1]
uc002gzq.3. human. [O00182-2]

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: 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 .
CH471159 Genomic DNA. Translation: EAW51037.1 .
CH471159 Genomic DNA. Translation: EAW51044.1 .
BC105942 mRNA. Translation: AAI05943.1 .
BC105944 mRNA. Translation: AAI05945.1 .
BC110340 mRNA. Translation: AAI10341.1 .
CCDSi CCDS11222.1. [O00182-1 ]
CCDS32592.1. [O00182-2 ]
RefSeqi NP_002299.2. NM_002308.3. [O00182-2 ]
NP_033665.1. NM_009587.2. [O00182-1 ]
UniGenei Hs.81337.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EAK X-ray 1.97 A/B/C 1-148 [» ]
2EAL X-ray 1.85 A/B 1-148 [» ]
2YY1 X-ray 2.17 A 1-147 [» ]
2ZHK X-ray 1.80 A/B 1-148 [» ]
2ZHL X-ray 1.75 A/B/C/D 1-148 [» ]
2ZHM X-ray 1.84 A/B/C/D 1-148 [» ]
2ZHN X-ray 1.30 A 1-148 [» ]
3LSD X-ray 2.03 A 6-148 [» ]
3LSE X-ray 2.69 A 6-148 [» ]
3NV1 X-ray 1.50 A 218-355 [» ]
3NV2 X-ray 2.34 A 218-355 [» ]
3NV3 X-ray 1.57 A 218-355 [» ]
3NV4 X-ray 1.99 A 218-355 [» ]
ProteinModelPortali O00182.
SMRi O00182. Positions 3-355.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110156. 68 interactions.
IntActi O00182. 12 interactions.
STRINGi 9606.ENSP00000378856.

Chemistry

BindingDBi O00182.
ChEMBLi CHEMBL5474.

PTM databases

PhosphoSitei O00182.

Proteomic databases

MaxQBi O00182.
PRIDEi O00182.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302228 ; ENSP00000306228 ; ENSG00000168961 . [O00182-2 ]
ENST00000395473 ; ENSP00000378856 ; ENSG00000168961 . [O00182-1 ]
GeneIDi 3965.
KEGGi hsa:3965.
UCSCi uc002gzp.3. human. [O00182-1 ]
uc002gzq.3. human. [O00182-2 ]

Organism-specific databases

CTDi 3965.
GeneCardsi GC17P025956.
HGNCi HGNC:6570. LGALS9.
HPAi HPA046876.
HPA047218.
MIMi 601879. gene.
neXtProti NX_O00182.
PharmGKBi PA30347.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00760000119105.
HOGENOMi HOG000290194.
HOVERGENi HBG002412.
InParanoidi O00182.
KOi K10093.
OMAi VCNTRQN.
OrthoDBi EOG73Z2TM.
PhylomeDBi O00182.
TreeFami TF315551.

Miscellaneous databases

ChiTaRSi LGALS9. human.
EvolutionaryTracei O00182.
GeneWikii LGALS9.
GenomeRNAii 3965.
NextBioi 15562.
PROi O00182.
SOURCEi Search...

Gene expression databases

Bgeei O00182.
CleanExi HS_LGALS9.
ExpressionAtlasi O00182. baseline and differential.
Genevestigatori O00182.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
InterProi IPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view ]
Pfami PF00337. Gal-bind_lectin. 2 hits.
[Graphical view ]
SMARTi SM00908. Gal-bind_lectin. 2 hits.
SM00276. GLECT. 2 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 2 hits.
PROSITEi PS51304. GALECTIN. 2 hits.
[Graphical view ]
ProtoNeti Search...

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 SHORT).
    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 LONG).
    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 SHORT), 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 LONG AND SHORT).
    Tissue: Kidney and Stomach.
  5. "Homo sapiens galectin-9 (LGALS9) / ecalectin gene, exon 2 through 11."
    Akiyama S.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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 SHORT), VARIANT SER-5.
    Tissue: Gastric mucosa.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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 SHORT).
    Tissue: Colon.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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
, O14532, O75028, Q3B8N1, Q53FQ0, Q9NQ58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: November 26, 2014
This is version 141 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

External Data

Dasty 3