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Protein

Galectin-8

Gene

LGALS8

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

Functioni

Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei59 – 591Critical for binding to sialylated and sulfated oligosaccharides
Binding sitei69 – 691Carbohydrate
Binding sitei79 – 791Carbohydrate
Binding sitei89 – 891Carbohydrate

GO - Molecular functioni

  1. carbohydrate binding Source: ProtInc

GO - Biological processi

  1. plasma cell differentiation Source: Ensembl
  2. T cell costimulation Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Galectin-8
Short name:
Gal-8
Alternative name(s):
Po66 carbohydrate-binding protein
Short name:
Po66-CBP
Prostate carcinoma tumor antigen 1
Short name:
PCTA-1
Gene namesi
Name:LGALS8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6569. LGALS8.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular space Source: ProtInc
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30346.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Galectin-8PRO_0000076943Add
BLAST

Proteomic databases

MaxQBiO00214.
PaxDbiO00214.
PRIDEiO00214.

PTM databases

PhosphoSiteiO00214.

Expressioni

Tissue specificityi

Ubiquitous. Selective expression by prostate carcinomas versus normal prostate and benign prostatic hypertrophy.

Gene expression databases

BgeeiO00214.
ExpressionAtlasiO00214. baseline and differential.
GenevestigatoriO00214.

Organism-specific databases

HPAiHPA030491.

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TGIF1Q1558310EBI-740058,EBI-714215

Protein-protein interaction databases

BioGridi110155. 105 interactions.
IntActiO00214. 3 interactions.
MINTiMINT-1458207.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi8 – 147Combined sources
Beta strandi17 – 226Combined sources
Beta strandi32 – 387Combined sources
Beta strandi44 – 5310Combined sources
Turni56 – 594Combined sources
Beta strandi61 – 699Combined sources
Beta strandi71 – 733Combined sources
Beta strandi75 – 828Combined sources
Beta strandi90 – 923Combined sources
Beta strandi102 – 1098Combined sources
Beta strandi111 – 1188Combined sources
Beta strandi121 – 1277Combined sources
Helixi132 – 1343Combined sources
Beta strandi137 – 1437Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi186 – 1905Combined sources
Beta strandi200 – 2078Combined sources
Beta strandi213 – 2208Combined sources
Turni221 – 2244Combined sources
Beta strandi225 – 2339Combined sources
Turni234 – 2374Combined sources
Beta strandi238 – 2458Combined sources
Beta strandi246 – 2494Combined sources
Beta strandi256 – 2583Combined sources
Beta strandi266 – 2738Combined sources
Beta strandi275 – 2828Combined sources
Beta strandi285 – 2917Combined sources
Helixi297 – 2993Combined sources
Beta strandi302 – 31716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YRONMR-A176-317[»]
2YV8X-ray1.92A1-152[»]
2YXSX-ray2.13A1-152[»]
3AP4X-ray2.33A/B/C/D1-154[»]
3AP5X-ray1.92A1-154[»]
3AP6X-ray1.58A/B/C/D1-154[»]
3AP7X-ray1.53A1-154[»]
3AP9X-ray1.33A1-154[»]
3APBX-ray1.95A/B1-154[»]
3OJBX-ray3.01A/B/C/D186-315[»]
3VKLX-ray2.55A/B1-155[»]
A/B184-317[»]
3VKMX-ray2.98A/B1-155[»]
A/B184-317[»]
3VKNX-ray1.98A/B1-153[»]
3VKOX-ray2.08A/B1-153[»]
4BMBX-ray1.35A4-153[»]
4BMEX-ray2.00A/B4-155[»]
4FQZX-ray2.80A1-155[»]
A184-317[»]
4GXLX-ray2.02A186-317[»]
4HANX-ray2.55A/B1-155[»]
A/B184-317[»]
ProteinModelPortaliO00214.
SMRiO00214. Positions 1-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00214.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 152134Galectin 1PROSITE-ProRule annotationAdd
BLAST
Domaini187 – 317131Galectin 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni249 – 2557Beta-galactoside bindingBy similarity

Domaini

Contains two homologous but distinct carbohydrate-binding domains.

Sequence similaritiesi

Contains 2 galectin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG264430.
GeneTreeiENSGT00760000119105.
HOVERGENiHBG002412.
InParanoidiO00214.
KOiK06832.
OMAiAWGEEER.
PhylomeDBiO00214.
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. AlignAdd to basket

Isoform 1 (identifier: O00214-1) [UniParc]FASTAAdd to basket

Also known as: I

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
MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL
60 70 80 90 100
QNGSSMKPRA DVAFHFNPRF KRAGCIVCNT LINEKWGREE ITYDTPFKRE
110 120 130 140 150
KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG
160 170 180 190 200
FSFSSDLQST QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT
210 220 230 240 250
VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
260 270 280 290 300
EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI
310
DTLEINGDIH LLEVRSW
Length:317
Mass (Da):35,808
Last modified:March 23, 2010 - v4
Checksum:iAA13116AC5C0D69A
GO
Isoform 2 (identifier: O00214-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     183-183: L → LPSNRGGDISKIAPRTVYTKSKDSTVNHTLTCTKIPPMNYVSK

Show »
Length:359
Mass (Da):40,397
Checksum:i39BED76B4115A798
GO

Sequence cautioni

The sequence AAB51605.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAD45402.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAD45403.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAD45404.1 differs from that shown.Probable cloning artifact.Curated
The sequence AAD45404.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH15818.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH16486.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141N → S in AAL77076 (Ref. 8) Curated
Sequence conflicti98 – 1003KRE → QKEK in CAA62904 (Ref. 2) Curated
Sequence conflicti112 – 1121D → A in CAA62904 (Ref. 2) Curated
Sequence conflicti171 – 1711S → V in AAB51605 (PubMed:8692978).Curated
Sequence conflicti199 – 1991R → G in AAL77076 (Ref. 8) Curated
Sequence conflicti204 – 2041K → Q in AAB51605 (PubMed:8692978).Curated
Sequence conflicti225 – 2251D → H in AAL77076 (Ref. 8) Curated
Sequence conflicti259 – 2591F → L in AAK16736 (Ref. 7) Curated
Isoform 2 (identifier: O00214-2)
Sequence conflicti220 – 2201M → T in AAL77076 (Ref. 8) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191F → Y.4 Publications
Corresponds to variant rs2737713 [ dbSNP | Ensembl ].
VAR_012990
Natural varianti36 – 361R → C.4 Publications
Corresponds to variant rs1041935 [ dbSNP | Ensembl ].
VAR_009710
Natural varianti56 – 561M → V.5 Publications
Corresponds to variant rs1041937 [ dbSNP | Ensembl ].
VAR_012991
Natural varianti184 – 1841R → S.4 Publications
Corresponds to variant rs2243525 [ dbSNP | Ensembl ].
VAR_063506

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei183 – 1831L → LPSNRGGDISKIAPRTVYTK SKDSTVNHTLTCTKIPPMNY VSK in isoform 2. 4 PublicationsVSP_003094

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L78132 mRNA. Translation: AAB51605.1. Different initiation.
X91790 mRNA. Translation: CAA62904.1.
AF074000 mRNA. Translation: AAD45402.1. Different initiation.
AF074001 mRNA. Translation: AAD45403.1. Different initiation.
AF074002 mRNA. Translation: AAD45404.1. Sequence problems.
AF193806, AF193805 Genomic DNA. Translation: AAF19370.1.
AF342815 mRNA. Translation: AAK16735.1.
AF342816 mRNA. Translation: AAK16736.1.
AF468213 mRNA. Translation: AAL77076.1.
AL359921 Genomic DNA. Translation: CAI13773.1.
AL359921 Genomic DNA. Translation: CAI13774.1.
BC015818 mRNA. Translation: AAH15818.1. Different initiation.
BC016486 mRNA. Translation: AAH16486.2. Different initiation.
CCDSiCCDS1611.1. [O00214-2]
CCDS1612.1. [O00214-1]
PIRiJC6147.
RefSeqiNP_006490.3. NM_006499.4. [O00214-2]
NP_963837.1. NM_201543.2. [O00214-1]
NP_963838.1. NM_201544.2. [O00214-1]
NP_963839.1. NM_201545.2. [O00214-2]
UniGeneiHs.4082.
Hs.708114.
Hs.735982.

Genome annotation databases

EnsembliENST00000341872; ENSP00000342139; ENSG00000116977. [O00214-1]
ENST00000352231; ENSP00000309576; ENSG00000116977. [O00214-2]
ENST00000366584; ENSP00000355543; ENSG00000116977. [O00214-1]
ENST00000450372; ENSP00000408657; ENSG00000116977. [O00214-2]
ENST00000526589; ENSP00000435460; ENSG00000116977. [O00214-2]
ENST00000526634; ENSP00000437040; ENSG00000116977. [O00214-1]
ENST00000527974; ENSP00000431398; ENSG00000116977. [O00214-2]
GeneIDi3964.
KEGGihsa:3964.
UCSCiuc001hxw.2. human. [O00214-2]
uc001hxz.2. human. [O00214-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Galectin-8 C-terminal CRD

Functional Glycomics Gateway - Glycan Binding

Galectin-8 long isoform

Functional Glycomics Gateway - Glycan Binding

Galectin-8 long isoform

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L78132 mRNA. Translation: AAB51605.1. Different initiation.
X91790 mRNA. Translation: CAA62904.1.
AF074000 mRNA. Translation: AAD45402.1. Different initiation.
AF074001 mRNA. Translation: AAD45403.1. Different initiation.
AF074002 mRNA. Translation: AAD45404.1. Sequence problems.
AF193806, AF193805 Genomic DNA. Translation: AAF19370.1.
AF342815 mRNA. Translation: AAK16735.1.
AF342816 mRNA. Translation: AAK16736.1.
AF468213 mRNA. Translation: AAL77076.1.
AL359921 Genomic DNA. Translation: CAI13773.1.
AL359921 Genomic DNA. Translation: CAI13774.1.
BC015818 mRNA. Translation: AAH15818.1. Different initiation.
BC016486 mRNA. Translation: AAH16486.2. Different initiation.
CCDSiCCDS1611.1. [O00214-2]
CCDS1612.1. [O00214-1]
PIRiJC6147.
RefSeqiNP_006490.3. NM_006499.4. [O00214-2]
NP_963837.1. NM_201543.2. [O00214-1]
NP_963838.1. NM_201544.2. [O00214-1]
NP_963839.1. NM_201545.2. [O00214-2]
UniGeneiHs.4082.
Hs.708114.
Hs.735982.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YRONMR-A176-317[»]
2YV8X-ray1.92A1-152[»]
2YXSX-ray2.13A1-152[»]
3AP4X-ray2.33A/B/C/D1-154[»]
3AP5X-ray1.92A1-154[»]
3AP6X-ray1.58A/B/C/D1-154[»]
3AP7X-ray1.53A1-154[»]
3AP9X-ray1.33A1-154[»]
3APBX-ray1.95A/B1-154[»]
3OJBX-ray3.01A/B/C/D186-315[»]
3VKLX-ray2.55A/B1-155[»]
A/B184-317[»]
3VKMX-ray2.98A/B1-155[»]
A/B184-317[»]
3VKNX-ray1.98A/B1-153[»]
3VKOX-ray2.08A/B1-153[»]
4BMBX-ray1.35A4-153[»]
4BMEX-ray2.00A/B4-155[»]
4FQZX-ray2.80A1-155[»]
A184-317[»]
4GXLX-ray2.02A186-317[»]
4HANX-ray2.55A/B1-155[»]
A/B184-317[»]
ProteinModelPortaliO00214.
SMRiO00214. Positions 1-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110155. 105 interactions.
IntActiO00214. 3 interactions.
MINTiMINT-1458207.

Chemistry

BindingDBiO00214.
ChEMBLiCHEMBL5475.

PTM databases

PhosphoSiteiO00214.

Proteomic databases

MaxQBiO00214.
PaxDbiO00214.
PRIDEiO00214.

Protocols and materials databases

DNASUi3964.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341872; ENSP00000342139; ENSG00000116977. [O00214-1]
ENST00000352231; ENSP00000309576; ENSG00000116977. [O00214-2]
ENST00000366584; ENSP00000355543; ENSG00000116977. [O00214-1]
ENST00000450372; ENSP00000408657; ENSG00000116977. [O00214-2]
ENST00000526589; ENSP00000435460; ENSG00000116977. [O00214-2]
ENST00000526634; ENSP00000437040; ENSG00000116977. [O00214-1]
ENST00000527974; ENSP00000431398; ENSG00000116977. [O00214-2]
GeneIDi3964.
KEGGihsa:3964.
UCSCiuc001hxw.2. human. [O00214-2]
uc001hxz.2. human. [O00214-1]

Organism-specific databases

CTDi3964.
GeneCardsiGC01P236681.
HGNCiHGNC:6569. LGALS8.
HPAiHPA030491.
MIMi606099. gene.
neXtProtiNX_O00214.
PharmGKBiPA30346.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264430.
GeneTreeiENSGT00760000119105.
HOVERGENiHBG002412.
InParanoidiO00214.
KOiK06832.
OMAiAWGEEER.
PhylomeDBiO00214.
TreeFamiTF315551.

Miscellaneous databases

ChiTaRSiLGALS8. human.
EvolutionaryTraceiO00214.
GeneWikiiGalectin-8.
LGALS8.
GenomeRNAii3964.
NextBioi15552.
PROiO00214.
SOURCEiSearch...

Gene expression databases

BgeeiO00214.
ExpressionAtlasiO00214. baseline and differential.
GenevestigatoriO00214.

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. "Surface-epitope masking and expression cloning identifies the human prostate carcinoma tumor antigen gene PCTA-1 a member of the galectin gene family."
    Su Z.-Z., Lin J., Shen R., Fisher P.E., Goldstein N.I., Fisher P.B.
    Proc. Natl. Acad. Sci. U.S.A. 93:7252-7257(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-56 AND SER-184.
    Tissue: Prostate.
  2. "Galectin-8: on the road from structure to function."
    Hadari Y.R., Eisenstein M., Zakut R., Zick Y.
    Trends Glycosci. Glycotechnol. 9:103-112(1996)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Hippocampus.
  3. "Molecular cloning of a beta-galactoside-binding lectin related to galectin-8 and identified in human lung carcinoma."
    Brichory F., Bidon N., Desrues B., Bourguet P., Le Pennec J.-P., Dazord L.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, VARIANTS TYR-19; CYS-36; VAL-56 AND SER-184.
    Tissue: Lung carcinoma.
  4. "Genomic organization and expression of the human galectin-8 gene."
    Maier C., Haeussler J., Roesch K., Moschgath E., Vogel W.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TYR-19; CYS-36; VAL-56 AND SER-184.
  5. "Molecular characterization of prostate carcinoma tumor antigen-1, PCTA-1, a human galectin-8 related gene."
    Gopalkrishnan R.V., Roberts T., Tuli S., Kang D., Christiansen K.A., Fisher P.B.
    Oncogene 19:4405-4416(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "Coca (colorectal carcinoma-derived) galectin-8 variant I full-length cDNA from a human colorectal carcinoma cell line."
    Lahm H., Siebert H.-C., Andre S., Hoeflich A., Diehl D., Sordat B., Kaltner H., Wolf E., Gabius H.-J.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon carcinoma.
  7. "Coca (Colorectal carcinoma-derived) galectin-8 variant II."
    Lahm H., Siebert H.-C., Andre S., Hoeflich A., Diehl D., Sordat B., Kaltner H., Wolf E., Gabius H.-J.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Colon carcinoma.
  8. "Galectins in murine and human non-Hodgkin's lymphomas."
    Moisan S., Mercier J., Demers M., Belanger S.D., Alain T., Kossakowska A.E., Potworowski E.F., St-Pierre Y.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS TYR-19; CYS-36 AND VAL-56.
  9. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS TYR-19; CYS-36; VAL-56 AND SER-184.
    Tissue: Brain and Skin.
  11. "Solution structure of the C-terminal Gal-bind lectin protein from human galectin-8."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JAN-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 176-317.
  12. "Crystal structure of N-terminal domain of human galectin-8."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 1-152 IN COMPLEX WITH LACTOSE.
  13. "Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans."
    Ideo H., Matsuzaka T., Nonaka T., Seko A., Yamashita K.
    J. Biol. Chem. 286:11346-11355(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1-154 ALONE AND IN COMPLEX WITH CARBOHYDRATES, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiLEG8_HUMAN
AccessioniPrimary (citable) accession number: O00214
Secondary accession number(s): O15215
, Q5T3P5, Q5T3Q4, Q8TEV1, Q96B92, Q9BXC8, Q9H584, Q9H585, Q9UEZ6, Q9UP32, Q9UP33, Q9UP34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 23, 2010
Last modified: February 4, 2015
This is version 145 of the entry and version 4 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 1
    Human chromosome 1: 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

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 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.