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O00214

- LEG8_HUMAN

UniProt

O00214 - LEG8_HUMAN

Protein

Galectin-8

Gene

LGALS8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (23 Mar 2010)
      Previous versions | rss
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    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
    2. protein binding Source: IntAct

    GO - Biological processi

    1. plasma cell differentiation Source: Ensembl
    2. T cell costimulation Source: Ensembl

    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: 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: UniProt
    4. membrane Source: UniProtKB

    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

    ArrayExpressiO00214.
    BgeeiO00214.
    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. 10 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 – 63
    Beta strandi8 – 147
    Beta strandi17 – 226
    Beta strandi32 – 387
    Beta strandi44 – 5310
    Turni56 – 594
    Beta strandi61 – 699
    Beta strandi71 – 733
    Beta strandi75 – 828
    Beta strandi90 – 923
    Beta strandi102 – 1098
    Beta strandi111 – 1188
    Beta strandi121 – 1277
    Helixi132 – 1343
    Beta strandi137 – 1437
    Beta strandi145 – 1528
    Beta strandi186 – 1905
    Beta strandi200 – 2078
    Beta strandi213 – 2208
    Turni221 – 2244
    Beta strandi225 – 2339
    Turni234 – 2374
    Beta strandi238 – 2458
    Beta strandi246 – 2494
    Beta strandi256 – 2583
    Beta strandi266 – 2738
    Beta strandi275 – 2828
    Beta strandi285 – 2917
    Helixi297 – 2993
    Beta strandi302 – 31716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOVERGENiHBG002412.
    KOiK06832.
    OMAiVNIHSVG.
    PhylomeDBiO00214.
    TreeFamiTF315551.

    Family and domain databases

    Gene3Di2.60.120.200. 2 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

    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

    MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL    50
    QNGSSMKPRA DVAFHFNPRF KRAGCIVCNT LINEKWGREE ITYDTPFKRE 100
    KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG 150
    FSFSSDLQST QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT 200
    VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG 250
    EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI 300
    DTLEINGDIH LLEVRSW 317
    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 AAD45404.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAB51605.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAD45402.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAD45403.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAD45404.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH15818.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH16486.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141N → S in AAL77076. 1 PublicationCurated
    Sequence conflicti98 – 1003KRE → QKEK in CAA62904. 1 PublicationCurated
    Sequence conflicti112 – 1121D → A in CAA62904. 1 PublicationCurated
    Sequence conflicti171 – 1711S → V in AAB51605. (PubMed:8692978)Curated
    Sequence conflicti199 – 1991R → G in AAL77076. 1 PublicationCurated
    Sequence conflicti204 – 2041K → Q in AAB51605. (PubMed:8692978)Curated
    Sequence conflicti225 – 2251D → H in AAL77076. 1 PublicationCurated
    Sequence conflicti259 – 2591F → L in AAK16736. 1 PublicationCurated
    Isoform 2 (identifier: O00214-2)
    Sequence conflicti220 – 2201M → T in AAL77076. 1 PublicationCurated

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS1611.1. [O00214-2 ]
    CCDS1612.1. [O00214-1 ]
    PIRi JC6147.
    RefSeqi NP_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 ]
    UniGenei Hs.4082.
    Hs.708114.
    Hs.735982.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YRO NMR - A 176-317 [» ]
    2YV8 X-ray 1.92 A 1-152 [» ]
    2YXS X-ray 2.13 A 1-152 [» ]
    3AP4 X-ray 2.33 A/B/C/D 1-154 [» ]
    3AP5 X-ray 1.92 A 1-154 [» ]
    3AP6 X-ray 1.58 A/B/C/D 1-154 [» ]
    3AP7 X-ray 1.53 A 1-154 [» ]
    3AP9 X-ray 1.33 A 1-154 [» ]
    3APB X-ray 1.95 A/B 1-154 [» ]
    3OJB X-ray 3.01 A/B/C/D 186-315 [» ]
    3VKL X-ray 2.55 A/B 1-155 [» ]
    A/B 184-317 [» ]
    3VKM X-ray 2.98 A/B 1-155 [» ]
    A/B 184-317 [» ]
    3VKN X-ray 1.98 A/B 1-153 [» ]
    3VKO X-ray 2.08 A/B 1-153 [» ]
    4BMB X-ray 1.35 A 4-153 [» ]
    4BME X-ray 2.00 A/B 4-155 [» ]
    4FQZ X-ray 2.80 A 1-155 [» ]
    A 184-317 [» ]
    4GXL X-ray 2.02 A 186-317 [» ]
    4HAN X-ray 2.55 A/B 1-155 [» ]
    A/B 184-317 [» ]
    ProteinModelPortali O00214.
    SMRi O00214. Positions 1-317.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110155. 10 interactions.
    IntActi O00214. 3 interactions.
    MINTi MINT-1458207.

    Chemistry

    BindingDBi O00214.
    ChEMBLi CHEMBL5475.

    PTM databases

    PhosphoSitei O00214.

    Proteomic databases

    MaxQBi O00214.
    PaxDbi O00214.
    PRIDEi O00214.

    Protocols and materials databases

    DNASUi 3964.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341872 ; 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 ]
    GeneIDi 3964.
    KEGGi hsa:3964.
    UCSCi uc001hxw.2. human. [O00214-2 ]
    uc001hxz.2. human. [O00214-1 ]

    Organism-specific databases

    CTDi 3964.
    GeneCardsi GC01P236681.
    HGNCi HGNC:6569. LGALS8.
    HPAi HPA030491.
    MIMi 606099. gene.
    neXtProti NX_O00214.
    PharmGKBi PA30346.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264430.
    HOVERGENi HBG002412.
    KOi K06832.
    OMAi VNIHSVG.
    PhylomeDBi O00214.
    TreeFami TF315551.

    Miscellaneous databases

    ChiTaRSi LGALS8. human.
    EvolutionaryTracei O00214.
    GeneWikii Galectin-8.
    LGALS8.
    GenomeRNAii 3964.
    NextBioi 15552.
    PROi O00214.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00214.
    Bgeei O00214.
    Genevestigatori O00214.

    Family and domain databases

    Gene3Di 2.60.120.200. 2 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

    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(1996) [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(1997)
      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 (JUN-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 (OCT-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(2000) [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 (JAN-2001) 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 (JAN-2001) 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 (JAN-2002) 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(2006) [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(2004) [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 (FEB-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 (MAY-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(2011) [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: October 1, 2014
    This is version 142 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