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P11226

- MBL2_HUMAN

UniProt

P11226 - MBL2_HUMAN

Protein

Mannose-binding protein C

Gene

MBL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages. May bind DNA.1 Publication

    GO - Molecular functioni

    1. calcium-dependent protein binding Source: UniProtKB
    2. carbohydrate binding Source: InterPro
    3. mannose binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. receptor binding Source: UniProtKB

    GO - Biological processi

    1. acute-phase response Source: BHF-UCL
    2. complement activation Source: Reactome
    3. complement activation, classical pathway Source: UniProtKB-KW
    4. complement activation, lectin pathway Source: UniProtKB
    5. defense response to bacterium Source: BHF-UCL
    6. defense response to Gram-positive bacterium Source: MGI
    7. innate immune response Source: BHF-UCL
    8. killing by host of symbiont cells Source: Ensembl
    9. negative regulation of growth of symbiont in host Source: MGI
    10. negative regulation of viral process Source: BHF-UCL
    11. opsonization Source: BHF-UCL
    12. positive regulation of phagocytosis Source: Ensembl
    13. response to oxidative stress Source: UniProtKB

    Keywords - Biological processi

    Complement activation lectin pathway, Complement pathway, Immunity, Innate immunity

    Keywords - Ligandi

    Calcium, Lectin, Mannose-binding

    Enzyme and pathway databases

    ReactomeiREACT_7964. Lectin pathway of complement activation.
    REACT_8024. Initial triggering of complement.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannose-binding protein C
    Short name:
    MBP-C
    Alternative name(s):
    Collectin-1
    MBP1
    Mannan-binding protein
    Mannose-binding lectin
    Gene namesi
    Name:MBL2
    Synonyms:COLEC1, MBL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:6922. MBL2.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. collagen trimer Source: UniProtKB-KW
    3. extracellular region Source: Reactome
    4. extracellular space Source: BHF-UCL

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    MIMi610424. phenotype.
    614372. phenotype.
    PharmGKBiPA30665.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20201 PublicationAdd
    BLAST
    Chaini21 – 248228Mannose-binding protein CPRO_0000017401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei47 – 471Hydroxyproline1 Publication
    Modified residuei73 – 731Hydroxyproline1 Publication
    Modified residuei79 – 791Hydroxyproline1 Publication
    Modified residuei82 – 821Hydroxyproline1 Publication
    Modified residuei88 – 881Hydroxyproline1 Publication
    Disulfide bondi155 ↔ 244
    Disulfide bondi222 ↔ 236

    Keywords - PTMi

    Disulfide bond, Hydroxylation

    Proteomic databases

    MaxQBiP11226.
    PaxDbiP11226.
    PeptideAtlasiP11226.
    PRIDEiP11226.

    Miscellaneous databases

    PMAP-CutDBP11226.

    Expressioni

    Tissue specificityi

    Plasma protein produced mainly in the liver.1 Publication

    Gene expression databases

    ArrayExpressiP11226.
    BgeeiP11226.
    CleanExiHS_MBL2.
    GenevestigatoriP11226.

    Organism-specific databases

    HPAiCAB016782.
    HPA002027.

    Interactioni

    Subunit structurei

    Oligomeric complex of 3 or more homotrimers. Interacts with MASP1 and MASP2. Interacts with MEP1A and MEP1B and may inhibit their catalytic activity.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRP1Q079545EBI-5325353,EBI-1046087

    Protein-protein interaction databases

    BioGridi110323. 4 interactions.
    IntActiP11226. 3 interactions.
    MINTiMINT-6630459.
    STRINGi9606.ENSP00000363079.

    Structurei

    Secondary structure

    1
    248
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi110 – 12920
    Beta strandi131 – 1344
    Beta strandi137 – 14711
    Helixi148 – 15710
    Helixi168 – 17710
    Beta strandi182 – 1876
    Beta strandi189 – 1913
    Helixi216 – 2183
    Beta strandi222 – 2254
    Beta strandi231 – 2344
    Beta strandi238 – 24710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HUPX-ray2.50A108-248[»]
    ProteinModelPortaliP11226.
    SMRiP11226. Positions 108-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11226.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 9958Collagen-likeAdd
    BLAST
    Domaini134 – 245112C-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili112 – 130191 PublicationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi21 – 4121Cys-richAdd
    BLAST

    Domaini

    The coiled-coil domain mediates trimerization.

    Sequence similaritiesi

    Contains 1 C-type lectin domain.PROSITE-ProRule annotation
    Contains 1 collagen-like domain.Curated

    Keywords - Domaini

    Coiled coil, Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG265984.
    HOVERGENiHBG108270.
    InParanoidiP11226.
    KOiK03991.
    OMAiLCAQFQG.
    OrthoDBiEOG7VTDPW.
    PhylomeDBiP11226.
    TreeFamiTF330481.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    [Graphical view]
    PfamiPF01391. Collagen. 1 hit.
    PF00059. Lectin_C. 1 hit.
    [Graphical view]
    SMARTiSM00034. CLECT. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P11226-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLFPSLPLL LLSMVAASYS ETVTCEDAQK TCPAVIACSS PGINGFPGKD    50
    GRDGTKGEKG EPGQGLRGLQ GPPGKLGPPG NPGPSGSPGP KGQKGDPGKS 100
    PDGDSSLAAS ERKALQTEMA RIKKWLTFSL GKQVGNKFFL TNGEIMTFEK 150
    VKALCVKFQA SVATPRNAAE NGAIQNLIKE EAFLGITDEK TEGQFVDLTG 200
    NRLTYTNWNE GEPNNAGSDE DCVLLLKNGQ WNDVPCSTSH LAVCEFPI 248
    Length:248
    Mass (Da):26,144
    Last modified:April 1, 1990 - v2
    Checksum:iC1F2AAED46D0F774
    GO

    Polymorphismi

    Genetic variations in MBL2 influence susceptibility to hepatitis B virus (HBV) infection [MIMi:610424].
    Genetic variations in MBL2 are responsible for mannose-binding protein deficiency [MIMi:614372]. This condition is defined as MBL2 protein level of less than 100 ng/ml, is present in about 5% of people of European descent and in about 10% of sub-Saharan Africans. Most MBL2-deficient adults appear healthy, but low levels of MBL2 are associated with increased risk of infection in toddlers, in cancer patients undergoing chemotherapy, and in organ-transplant patients receiving immunosuppressive drugs, particularly recipients of liver transplants. There is an association between low levels of MBL2 and a defect of opsonization which results in susceptibility to frequent and chronic infections (PubMed:1675710). Functional MBL2 deficiency may be associated with protection against tuberculosis caused by Mycobacterium africanum but not by Mycobacterium tuberculosis, as observed in studies on Ghanaian patients with pulmonary tuberculosis (PubMed:21695215).2 Publications

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 241T → A in Chinese. 1 Publication
    VAR_013294
    Natural varianti52 – 521R → C in 0.05% of European and African populations. 3 Publications
    Corresponds to variant rs5030737 [ dbSNP | Ensembl ].
    VAR_008543
    Natural varianti54 – 541G → D Polymorphism associated with mannose-binding protein deficiency and recurrent infections. 8 Publications
    Corresponds to variant rs1800450 [ dbSNP | Ensembl ].
    VAR_004182
    Natural varianti57 – 571G → E Polymorphism associated with mannose-binding protein deficiency; associated with protection against tuberculosis caused by Mycobacterium africanum. 5 Publications
    Corresponds to variant rs1800451 [ dbSNP | Ensembl ].
    VAR_004183
    Natural varianti214 – 2141N → Y.
    Corresponds to variant rs12260094 [ dbSNP | Ensembl ].
    VAR_050119

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15422 mRNA. Translation: CAA33462.1.
    X15954
    , X15955, X15956, X15957 Genomic DNA. Translation: CAA34079.1.
    AF080510, AF080508, AF080509 Genomic DNA. Translation: AAC31937.1.
    Y16576 Genomic DNA. Translation: CAB56044.1.
    Y16577 Genomic DNA. Translation: CAB56120.1.
    Y16578 Genomic DNA. Translation: CAB56045.1.
    Y16579 Genomic DNA. Translation: CAB56121.1.
    Y16580 Genomic DNA. Translation: CAB56122.1.
    Y16581 Genomic DNA. Translation: CAB56123.1.
    Y16582 Genomic DNA. Translation: CAB56124.1.
    AF360991 mRNA. Translation: AAK52907.1.
    AY826184 mRNA. Translation: AAV80468.1.
    DQ217939 Genomic DNA. Translation: ABB01009.1.
    EU596574 Genomic DNA. Translation: ACC62880.1.
    CH471083 Genomic DNA. Translation: EAW54148.1.
    CH471083 Genomic DNA. Translation: EAW54149.1.
    BC096179 mRNA. Translation: AAH96179.1.
    BC096180 mRNA. Translation: AAH96180.3.
    BC069338 mRNA. Translation: AAH69338.1.
    BC096181 mRNA. Translation: AAH96181.3.
    BC096182 mRNA. Translation: AAH96182.3.
    AF482699 Genomic DNA. Translation: AAN39274.1.
    AF482700 Genomic DNA. Translation: AAN39275.1.
    CCDSiCCDS7247.1.
    PIRiJL0115. LNHUMC.
    RefSeqiNP_000233.1. NM_000242.2.
    XP_006717924.1. XM_006717861.1.
    UniGeneiHs.499674.

    Genome annotation databases

    EnsembliENST00000373968; ENSP00000363079; ENSG00000165471.
    GeneIDi4153.
    KEGGihsa:4153.
    UCSCiuc001jjt.3. human.

    Polymorphism databases

    DMDMi126676.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    Mannose-binding protein

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15422 mRNA. Translation: CAA33462.1 .
    X15954
    , X15955 , X15956 , X15957 Genomic DNA. Translation: CAA34079.1 .
    AF080510 , AF080508 , AF080509 Genomic DNA. Translation: AAC31937.1 .
    Y16576 Genomic DNA. Translation: CAB56044.1 .
    Y16577 Genomic DNA. Translation: CAB56120.1 .
    Y16578 Genomic DNA. Translation: CAB56045.1 .
    Y16579 Genomic DNA. Translation: CAB56121.1 .
    Y16580 Genomic DNA. Translation: CAB56122.1 .
    Y16581 Genomic DNA. Translation: CAB56123.1 .
    Y16582 Genomic DNA. Translation: CAB56124.1 .
    AF360991 mRNA. Translation: AAK52907.1 .
    AY826184 mRNA. Translation: AAV80468.1 .
    DQ217939 Genomic DNA. Translation: ABB01009.1 .
    EU596574 Genomic DNA. Translation: ACC62880.1 .
    CH471083 Genomic DNA. Translation: EAW54148.1 .
    CH471083 Genomic DNA. Translation: EAW54149.1 .
    BC096179 mRNA. Translation: AAH96179.1 .
    BC096180 mRNA. Translation: AAH96180.3 .
    BC069338 mRNA. Translation: AAH69338.1 .
    BC096181 mRNA. Translation: AAH96181.3 .
    BC096182 mRNA. Translation: AAH96182.3 .
    AF482699 Genomic DNA. Translation: AAN39274.1 .
    AF482700 Genomic DNA. Translation: AAN39275.1 .
    CCDSi CCDS7247.1.
    PIRi JL0115. LNHUMC.
    RefSeqi NP_000233.1. NM_000242.2.
    XP_006717924.1. XM_006717861.1.
    UniGenei Hs.499674.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HUP X-ray 2.50 A 108-248 [» ]
    ProteinModelPortali P11226.
    SMRi P11226. Positions 108-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110323. 4 interactions.
    IntActi P11226. 3 interactions.
    MINTi MINT-6630459.
    STRINGi 9606.ENSP00000363079.

    Chemistry

    ChEMBLi CHEMBL1795113.

    Polymorphism databases

    DMDMi 126676.

    Proteomic databases

    MaxQBi P11226.
    PaxDbi P11226.
    PeptideAtlasi P11226.
    PRIDEi P11226.

    Protocols and materials databases

    DNASUi 4153.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373968 ; ENSP00000363079 ; ENSG00000165471 .
    GeneIDi 4153.
    KEGGi hsa:4153.
    UCSCi uc001jjt.3. human.

    Organism-specific databases

    CTDi 4153.
    GeneCardsi GC10M054525.
    HGNCi HGNC:6922. MBL2.
    HPAi CAB016782.
    HPA002027.
    MIMi 154545. gene.
    610424. phenotype.
    614372. phenotype.
    neXtProti NX_P11226.
    PharmGKBi PA30665.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265984.
    HOVERGENi HBG108270.
    InParanoidi P11226.
    KOi K03991.
    OMAi LCAQFQG.
    OrthoDBi EOG7VTDPW.
    PhylomeDBi P11226.
    TreeFami TF330481.

    Enzyme and pathway databases

    Reactomei REACT_7964. Lectin pathway of complement activation.
    REACT_8024. Initial triggering of complement.

    Miscellaneous databases

    EvolutionaryTracei P11226.
    GeneWikii Mannan-binding_lectin.
    GenomeRNAii 4153.
    NextBioi 16342.
    PMAP-CutDB P11226.
    PROi P11226.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11226.
    Bgeei P11226.
    CleanExi HS_MBL2.
    Genevestigatori P11226.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    [Graphical view ]
    Pfami PF01391. Collagen. 1 hit.
    PF00059. Lectin_C. 1 hit.
    [Graphical view ]
    SMARTi SM00034. CLECT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human mannose-binding protein is an acute-phase reactant that shares sequence homology with other vertebrate lectins."
      Ezekowitz R.A.B., Day L.E., Herman G.A.
      J. Exp. Med. 167:1034-1046(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Erratum
      Ezekowitz R.A.B., Day L.E., Herman G.A.
      J. Exp. Med. 174:753-753(1991)
    3. "The human mannose-binding protein gene. Exon structure reveals its evolutionary relationship to a human pulmonary surfactant gene and localization to chromosome 10."
      Sastry K., Herman G.A., Day L.E., Deignan E., Bruns G., Morton C.C., Ezekowitz R.A.B.
      J. Exp. Med. 170:1175-1189(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
      Tissue: Liver.
    4. "Structure and evolutionary origin of the gene encoding a human serum mannose-binding protein."
      Taylor M.E., Brickell P.M., Craig R.K., Summerfield J.A.
      Biochem. J. 262:763-771(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Different molecular events result in low protein levels of mannan-binding lectin in populations from South-East Africa and South America."
      Madsen H.O., Satz M.L., Hogh B., Svejgaard A., Garred P.
      J. Immunol. 161:3169-3175(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-52; ASP-54 AND GLU-57.
    6. "Cloning and sequencing of mannan-binding lectin cDNA of Chinese."
      Chen Z., Zhu X., Xie P.
      Mian Yi Xue Za Zhi 15:83-86(1999)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-24.
      Tissue: Liver.
    7. "Prokaryotic expression of human mbl."
      Wu Z., Zhang S., Wang Y.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    8. "Genetic variation in immune response genes."
      Tan J., Ong R., Hibberd M.L., Seielstad M.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    9. "Cloning and sequencing of mannan-binding lectin gene from chinese Han people."
      Lai Q., Zuo D., Chen Z.
      Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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], VARIANT ASP-54.
    12. "Restricted polymorphisms of the mannose-binding lectin gene in a population of Papua New Guinea."
      Jueliger S., Kremsner P.G., Alpers M.P., Reeder J.C., Kun J.F.J.
      Mutat. Res. 505:87-91(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59, VARIANT ASP-54.
    13. "Structure and function of mannan-binding proteins isolated from human liver and serum."
      Kurata H., Sannoh T., Kozutsumi Y., Yokota Y., Kawasaki T.
      J. Biochem. 115:1148-1154(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-248, SUBCELLULAR LOCATION, HYDROXYLATION AT PRO-47; PRO-73; PRO-79; PRO-82 AND PRO-88.
      Tissue: Liver and Plasma.
    14. Cited for: INTERACTION WITH MASP1 AND MASP2.
    15. Cited for: FUNCTION.
    16. "Nucleic acid is a novel ligand for innate, immune pattern recognition collectins surfactant proteins A and D and mannose-binding lectin."
      Palaniyar N., Nadesalingam J., Clark H., Shih M.J., Dodds A.W., Reid K.B.M.
      J. Biol. Chem. 279:32728-32736(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING.
    17. "Mannan-binding protein blocks the activation of metalloproteases meprin alpha and beta."
      Hirano M., Ma B.Y., Kawasaki N., Okimura K., Baba M., Nakagawa T., Miwa K., Kawasaki N., Oka S., Kawasaki T.
      J. Immunol. 175:3177-3185(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEP1A AND MEP1B.
    18. "Comparative study of the human ficolins reveals unique features of Ficolin-3 (Hakata antigen)."
      Hummelshoej T., Fog L.M., Madsen H.O., Sim R.B., Garred P.
      Mol. Immunol. 45:1623-1632(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    19. "Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil."
      Sheriff S., Chang C.Y., Ezekowitz R.A.
      Nat. Struct. Biol. 1:789-794(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 108-248, SUBUNIT, COILED-COIL.
    20. "Molecular basis of opsonic defect in immunodeficient children."
      Sumiya M., Super M., Tabona P., Levinsky R.J., Arai T., Turner M.W., Summerfield J.A.
      Lancet 337:1569-1570(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASP-54, ASSOCIATION WITH MANNOSE-BINDING PROTEIN DEFICIENCY AND SUSCEPTIBILITY TO CHRONIC INFECTIONS.
    21. "High frequencies in African and non-African populations of independent mutations in the mannose binding protein gene."
      Lipscombe R.J., Sumiya M., Hill A.V.S., Lau Y.L., Levinsky R.J., Summerfield J.A., Turner M.W.
      Hum. Mol. Genet. 1:709-715(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ASP-54 AND GLU-57, ASSOCIATION WITH MANNOSE-BINDING PROTEIN DEFICIENCY.
    22. "Distinct and overlapping functions of allelic forms of human mannose binding protein."
      Super M., Gillies S.D., Foley S., Sastry K., Schweinle J.E., Silverman V.J., Ezekowitz R.A.
      Nat. Genet. 2:50-55(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASP-54.
    23. "Genotyping of the three major allelic variants of the human mannose-binding lectin gene by denaturing gradient gel electrophoresis."
      Gabolde M., Muralitharan S., Besmond C.
      Hum. Mutat. 14:80-83(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CYS-52; ASP-54 AND GLU-57.
    24. "Mannose binding lectin genotypes influence recovery from hepatitis B virus infection."
      Thio C.L., Mosbruger T., Astemborski J., Greer S., Kirk G.D., O'Brien S.J., Thomas D.L.
      J. Virol. 79:9192-9196(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO HBV INFECTION, VARIANTS CYS-52; ASP-54 AND GLU-57.
    25. "Variant G57E of mannose binding lectin associated with protection against tuberculosis caused by Mycobacterium africanum but not by M. tuberculosis."
      Thye T., Niemann S., Walter K., Homolka S., Intemann C.D., Chinbuah M.A., Enimil A., Gyapong J., Osei I., Owusu-Dabo E., Rusch-Gerdes S., Horstmann R.D., Ehlers S., Meyer C.G.
      PLoS ONE 6:E20908-E20908(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLU-57, ASSOCIATION WITH PROTECTION AGAINST TUBERCULOSIS.

    Entry informationi

    Entry nameiMBL2_HUMAN
    AccessioniPrimary (citable) accession number: P11226
    Secondary accession number(s): Q4VB12
    , Q4VB13, Q4VB14, Q5SQS3, Q86SI4, Q96KE4, Q96TF7, Q96TF8, Q96TF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 177 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 10
      Human chromosome 10: 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