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P11226

- MBL2_HUMAN

UniProt

P11226 - MBL2_HUMAN

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Protein

Mannose-binding protein C

Gene

MBL2

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

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. mannose binding Source: UniProtKB
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP11226.
CleanExiHS_MBL2.
ExpressionAtlasiP11226. baseline and differential.
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 – 12920Combined sources
Beta strandi131 – 1344Combined sources
Beta strandi137 – 14711Combined sources
Helixi148 – 15710Combined sources
Helixi168 – 17710Combined sources
Beta strandi182 – 1876Combined sources
Beta strandi189 – 1913Combined sources
Helixi216 – 2183Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi238 – 24710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HUPX-ray2.50A108-248[»]
ProteinModelPortaliP11226.
SMRiP11226. Positions 67-92, 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.
GeneTreeiENSGT00700000104102.
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

        10         20         30         40         50
MSLFPSLPLL LLSMVAASYS ETVTCEDAQK TCPAVIACSS PGINGFPGKD
60 70 80 90 100
GRDGTKGEKG EPGQGLRGLQ GPPGKLGPPG NPGPSGSPGP KGQKGDPGKS
110 120 130 140 150
PDGDSSLAAS ERKALQTEMA RIKKWLTFSL GKQVGNKFFL TNGEIMTFEK
160 170 180 190 200
VKALCVKFQA SVATPRNAAE NGAIQNLIKE EAFLGITDEK TEGQFVDLTG
210 220 230 240
NRLTYTNWNE GEPNNAGSDE DCVLLLKNGQ WNDVPCSTSH LAVCEFPI
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HUP X-ray 2.50 A 108-248 [» ]
ProteinModelPortali P11226.
SMRi P11226. Positions 67-92, 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.
GeneTreei ENSGT00700000104102.
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

Bgeei P11226.
CleanExi HS_MBL2.
ExpressionAtlasi P11226. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 179 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

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