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P09382

- LEG1_HUMAN

UniProt

P09382 - LEG1_HUMAN

Protein

Galectin-1

Gene

LGALS1

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

    May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis.3 Publications

    Sites

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

    GO - Molecular functioni

    1. galactoside binding Source: InterPro
    2. lactose binding Source: Ensembl
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. cellular response to glucose stimulus Source: Ensembl
    3. cellular response to organic cyclic compound Source: Ensembl
    4. multicellular organismal response to stress Source: Ensembl
    5. myoblast differentiation Source: Ensembl
    6. negative regulation of cell-substrate adhesion Source: Ensembl
    7. negative regulation of neuron projection development Source: Ensembl
    8. plasma cell differentiation Source: Ensembl
    9. positive regulation of erythrocyte aggregation Source: Ensembl
    10. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    11. regulation of apoptotic process Source: UniProtKB
    12. response to axon injury Source: Ensembl
    13. response to drug Source: Ensembl
    14. signal transduction Source: GOC
    15. T cell costimulation Source: Ensembl

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    Lectin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Galectin-1
    Short name:
    Gal-1
    Alternative name(s):
    14 kDa laminin-binding protein
    Short name:
    HLBP14
    14 kDa lectin
    Beta-galactoside-binding lectin L-14-I
    Galaptin
    HBL
    HPL
    Lactose-binding lectin 1
    Lectin galactoside-binding soluble 1
    Putative MAPK-activating protein PM12
    S-Lac lectin 1
    Gene namesi
    Name:LGALS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:6561. LGALS1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix 1 Publication

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. intracellular Source: LIFEdb
    6. nucleus Source: Ensembl
    7. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30337.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 135134Galectin-1PRO_0000076917Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei13 – 131N6-acetyllysineBy similarity
    Modified residuei29 – 291N6-acetyllysine1 Publication
    Modified residuei108 – 1081N6-acetyllysine; alternateBy similarity
    Modified residuei108 – 1081N6-succinyllysine; alternateBy similarity
    Modified residuei128 – 1281N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP09382.
    PaxDbiP09382.
    PeptideAtlasiP09382.
    PRIDEiP09382.

    2D gel databases

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

    PTM databases

    PhosphoSiteiP09382.

    Miscellaneous databases

    PMAP-CutDBP09382.

    Expressioni

    Tissue specificityi

    Expressed in placenta, maternal decidua and fetal membranes. Within placenta, expressed in trophoblasts, stromal cells, villous endothelium, syncytiotrophoblast apical membrane and villous stroma. Within fetal membranes, expressed in amnion, chorioamniotic mesenchyma and chorion (at protein level). Expressed in cardiac, smooth, and skeletal muscle, neurons, thymus, kidney and hematopoietic cells.2 Publications

    Gene expression databases

    ArrayExpressiP09382.
    BgeeiP09382.
    CleanExiHS_LGALS1.
    GenevestigatoriP09382.

    Organism-specific databases

    HPAiCAB002157.
    HPA000646.
    HPA000687.
    HPA001130.

    Interactioni

    Subunit structurei

    Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD7, CD43 and CD45. Interacts with laminin (via poly-N-acetyllactosamine).4 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi110147. 39 interactions.
    DIPiDIP-46153N.
    IntActiP09382. 9 interactions.
    MINTiMINT-3306493.
    STRINGi9606.ENSP00000215909.

    Structurei

    Secondary structure

    1
    135
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 127
    Beta strandi17 – 248
    Beta strandi30 – 389
    Beta strandi41 – 5212
    Beta strandi55 – 6511
    Beta strandi73 – 764
    Beta strandi82 – 9211
    Beta strandi94 – 1007
    Helixi102 – 1043
    Beta strandi106 – 1105
    Beta strandi118 – 13518

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GZWX-ray1.70A/B2-135[»]
    1W6MX-ray2.30A/B2-135[»]
    1W6NX-ray1.65A/B2-135[»]
    1W6OX-ray1.90A/B2-135[»]
    1W6PX-ray1.80A/B2-135[»]
    1W6QX-ray2.10A/B2-135[»]
    2KM2NMR-A/B2-135[»]
    2ZKNX-ray1.86A/B2-135[»]
    3OY8X-ray2.19A/B2-135[»]
    3OYWX-ray2.50A/B2-135[»]
    3T2TX-ray1.90A/B1-135[»]
    3W58X-ray1.58A/B/C/D2-135[»]
    3W59X-ray2.10A/B/C/D2-135[»]
    ProteinModelPortaliP09382.
    SMRiP09382. Positions 2-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09382.

    Family & Domainsi

    Domains and Repeats

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

    Region

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

    Sequence similaritiesi

    Contains 1 galectin domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG279327.
    HOGENOMiHOG000059539.
    HOVERGENiHBG006255.
    InParanoidiP09382.
    KOiK06830.
    OMAiGHEFKFP.
    OrthoDBiEOG7NKKN0.
    PhylomeDBiP09382.
    TreeFamiTF315551.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR015535. Galectin_1.
    IPR001079. Galectin_CRD.
    [Graphical view]
    PANTHERiPTHR11346:SF30. PTHR11346:SF30. 1 hit.
    PfamiPF00337. Gal-bind_lectin. 1 hit.
    [Graphical view]
    SMARTiSM00908. Gal-bind_lectin. 1 hit.
    SM00276. GLECT. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS51304. GALECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P09382-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF    50
    NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK 100
    LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD 135
    Length:135
    Mass (Da):14,716
    Last modified:January 23, 2007 - v2
    Checksum:i2FBB8D7A1FC0F1F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14829 mRNA. Translation: CAA32938.1.
    J04456 mRNA. Translation: AAA36170.1.
    X15256 mRNA. Translation: CAA33328.1.
    EU363770 mRNA. Translation: ACA58297.1.
    M57678 Genomic DNA. Translation: AAB00777.1.
    AB097036 mRNA. Translation: BAC77389.1.
    CR456511 mRNA. Translation: CAG30397.1.
    AK312161 mRNA. Translation: BAG35095.1.
    BT006775 mRNA. Translation: AAP35421.1.
    Z83844 Genomic DNA. Translation: CAB42897.1.
    CH471095 Genomic DNA. Translation: EAW60178.1.
    BC001693 mRNA. Translation: AAH01693.1.
    BC020675 mRNA. Translation: AAH20675.1.
    CCDSiCCDS13954.1.
    PIRiA37134. LNHUGB.
    RefSeqiNP_002296.1. NM_002305.3.
    UniGeneiHs.445351.

    Genome annotation databases

    EnsembliENST00000215909; ENSP00000215909; ENSG00000100097.
    GeneIDi3956.
    KEGGihsa:3956.
    UCSCiuc003atn.3. human.

    Polymorphism databases

    DMDMi126155.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    Galectin-1

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14829 mRNA. Translation: CAA32938.1 .
    J04456 mRNA. Translation: AAA36170.1 .
    X15256 mRNA. Translation: CAA33328.1 .
    EU363770 mRNA. Translation: ACA58297.1 .
    M57678 Genomic DNA. Translation: AAB00777.1 .
    AB097036 mRNA. Translation: BAC77389.1 .
    CR456511 mRNA. Translation: CAG30397.1 .
    AK312161 mRNA. Translation: BAG35095.1 .
    BT006775 mRNA. Translation: AAP35421.1 .
    Z83844 Genomic DNA. Translation: CAB42897.1 .
    CH471095 Genomic DNA. Translation: EAW60178.1 .
    BC001693 mRNA. Translation: AAH01693.1 .
    BC020675 mRNA. Translation: AAH20675.1 .
    CCDSi CCDS13954.1.
    PIRi A37134. LNHUGB.
    RefSeqi NP_002296.1. NM_002305.3.
    UniGenei Hs.445351.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GZW X-ray 1.70 A/B 2-135 [» ]
    1W6M X-ray 2.30 A/B 2-135 [» ]
    1W6N X-ray 1.65 A/B 2-135 [» ]
    1W6O X-ray 1.90 A/B 2-135 [» ]
    1W6P X-ray 1.80 A/B 2-135 [» ]
    1W6Q X-ray 2.10 A/B 2-135 [» ]
    2KM2 NMR - A/B 2-135 [» ]
    2ZKN X-ray 1.86 A/B 2-135 [» ]
    3OY8 X-ray 2.19 A/B 2-135 [» ]
    3OYW X-ray 2.50 A/B 2-135 [» ]
    3T2T X-ray 1.90 A/B 1-135 [» ]
    3W58 X-ray 1.58 A/B/C/D 2-135 [» ]
    3W59 X-ray 2.10 A/B/C/D 2-135 [» ]
    ProteinModelPortali P09382.
    SMRi P09382. Positions 2-135.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110147. 39 interactions.
    DIPi DIP-46153N.
    IntActi P09382. 9 interactions.
    MINTi MINT-3306493.
    STRINGi 9606.ENSP00000215909.

    Chemistry

    BindingDBi P09382.
    ChEMBLi CHEMBL4915.

    PTM databases

    PhosphoSitei P09382.

    Polymorphism databases

    DMDMi 126155.

    2D gel databases

    DOSAC-COBS-2DPAGE P09382.
    REPRODUCTION-2DPAGE IPI00219219.
    P09382.
    SWISS-2DPAGE P09382.
    UCD-2DPAGE P09382.

    Proteomic databases

    MaxQBi P09382.
    PaxDbi P09382.
    PeptideAtlasi P09382.
    PRIDEi P09382.

    Protocols and materials databases

    DNASUi 3956.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215909 ; ENSP00000215909 ; ENSG00000100097 .
    GeneIDi 3956.
    KEGGi hsa:3956.
    UCSCi uc003atn.3. human.

    Organism-specific databases

    CTDi 3956.
    GeneCardsi GC22P038071.
    HGNCi HGNC:6561. LGALS1.
    HPAi CAB002157.
    HPA000646.
    HPA000687.
    HPA001130.
    MIMi 150570. gene.
    neXtProti NX_P09382.
    PharmGKBi PA30337.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG279327.
    HOGENOMi HOG000059539.
    HOVERGENi HBG006255.
    InParanoidi P09382.
    KOi K06830.
    OMAi GHEFKFP.
    OrthoDBi EOG7NKKN0.
    PhylomeDBi P09382.
    TreeFami TF315551.

    Miscellaneous databases

    ChiTaRSi LGALS1. human.
    EvolutionaryTracei P09382.
    GeneWikii Galectin-1.
    LGALS1.
    GenomeRNAii 3956.
    NextBioi 15523.
    PMAP-CutDB P09382.
    PROi P09382.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09382.
    Bgeei P09382.
    CleanExi HS_LGALS1.
    Genevestigatori P09382.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR015535. Galectin_1.
    IPR001079. Galectin_CRD.
    [Graphical view ]
    PANTHERi PTHR11346:SF30. PTHR11346:SF30. 1 hit.
    Pfami PF00337. Gal-bind_lectin. 1 hit.
    [Graphical view ]
    SMARTi SM00908. Gal-bind_lectin. 1 hit.
    SM00276. GLECT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS51304. GALECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and nucleotide sequence of a full-length cDNA for human 14 kDa beta-galactoside-binding lectin."
      Hirabayashi J., Ayaki K., Soma G., Kasai K.
      Biochim. Biophys. Acta 1008:85-91(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    2. "Molecular cloning, characterization, and expression of a human 14-kDa lectin."
      Couraud P.-O., Casentini-Borocz D., Bringman T.S., Griffith J., McGrogan M., Nedwin G.E.
      J. Biol. Chem. 264:1310-1316(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta and Promyelocytic leukemia.
    3. "Evidence that the 14 kDa soluble beta-galactoside-binding lectin in man is encoded by a single gene."
      Abbott W.M., Feizi T.
      Biochem. J. 259:291-294(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Hepatoma.
    4. "Emergence of hormonal and redox regulation of galectin-1 in placental mammals: implication in maternal-fetal immune tolerance."
      Than N.G., Romero R., Erez O., Weckle A., Tarca A.L., Hotra J., Abbas A., Han Y.M., Kim S.S., Kusanovic J.P., Gotsch F., Hou Z., Santolaya-Forgas J., Benirschke K., Papp Z., Grossman L.I., Goodman M., Wildman D.E.
      Proc. Natl. Acad. Sci. U.S.A. 105:15819-15824(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Placenta.
    5. "Genomic sequence and organization of two members of a human lectin gene family."
      Gitt M.A., Barondes S.H.
      Biochemistry 30:82-89(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Lymphocyte.
    6. "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
      Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
      Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung fibroblast.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thalamus.
    9. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    10. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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].
      Tissue: Placenta and Skin.
    13. "Complete amino acid sequence of a beta-galactoside-binding lectin from human placenta."
      Hirabayashi J., Kasai K.
      J. Biochem. 104:1-4(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-135.
      Tissue: Placenta.
    14. "Beta-galactosidase soluble lectin from human brain: complete amino acid sequence."
      Bladier D., le Caer J.-P., Joubert R., Caron M., Rossier J.
      Neurochem. Int. 18:275-281(1991)
      Cited for: PROTEIN SEQUENCE OF 2-135.
      Tissue: Brain.
    15. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-19.
      Tissue: Platelet.
    16. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 38-49; 101-108 AND 113-128, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    17. "Further characterization and structural studies on human placenta lectin."
      Hirabayashi J., Kawasaki H., Suzuki K., Kasai K.
      J. Biochem. 101:987-995(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 70-87 AND 122-133.
      Tissue: Placenta.
    18. "Identification of a 14-kDa laminin binding protein (HLBP14) in human melanoma cells that is identical to the 14-kDa galactoside binding lectin."
      Castronovo V., Luyten F., van den Brule F., Sobel M.E.
      Arch. Biochem. Biophys. 297:132-138(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-29; 50-74 AND 132-135, INTERACTION WITH LAMININ.
      Tissue: Melanoma.
    19. "Human splenic galaptin: physicochemical characterization."
      Sharma A., Chemelli R., Allen H.J.
      Biochemistry 29:5309-5314(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Spleen.
    20. Cited for: CHARACTERIZATION.
    21. "Galectin-1, a natural ligand for the receptor-type protein tyrosine phosphatase CD45."
      Walzel H., Schulz U., Neels P., Brock J.
      Immunol. Lett. 67:193-202(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Tissue: Placenta.
    22. "Regulation of CD45-induced signaling by galectin-1 in Burkitt lymphoma B cells."
      Fouillit M., Joubert-Caron R., Poirier F., Bourin P., Monostori E., Levi-Strauss M., Raphael M., Bladier D., Caron M.
      Glycobiology 10:413-419(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    23. "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation."
      Tinari N., Kuwabara I., Huflejt M.E., Shen P.F., Iacobelli S., Liu F.-T.
      Int. J. Cancer 91:167-172(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LGALS3BP.
    24. "Presentation of galectin-1 by extracellular matrix triggers T cell death."
      He J., Baum L.G.
      J. Biol. Chem. 279:4705-4712(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.
    25. "Abnormal proteins in primary breast cancer tissues from 25 Sudanese patients."
      Ahamed M.E., Ahmed M.E., Eltoum A.M., Altahir G.O., Ahmed K.M., Harbi S.O., Stansalas J., Mohamed A.O.
      Eur. J. Inflamm. 6:115-121(2008)
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    26. Cited for: FUNCTION, TISSUE SPECIFICITY.
    27. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding."
      Lopez-Lucendo M.F., Solis D., Andre S., Hirabayashi J., Kasai K., Kaltner H., Gabius H.-J., Romero A.
      J. Mol. Biol. 343:957-970(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE, SUBUNIT.
    32. "Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1."
      Nishi N., Abe A., Iwaki J., Yoshida H., Itoh A., Shoji H., Kamitori S., Hirabayashi J., Nakamura T.
      Glycobiology 18:1065-1073(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-135 IN COMPLEX WITH LACTOSE, INTERACTION WITH CD2; CD3; CD7; CD43 AND CD45, SUBUNIT, FUNCTION.
    33. "Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose."
      Di Lella S., Ma L., Ricci J.C., Rabinovich G.A., Asher S.A., Alvarez R.M.S.
      Biochemistry 48:786-791(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

    Entry informationi

    Entry nameiLEG1_HUMAN
    AccessioniPrimary (citable) accession number: P09382
    Secondary accession number(s): B2R5E8, Q9UDK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 181 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3