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MBL2 (human)

Overview MBL2 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. Note: This description may include information from UniProtKB. Protein type: Secreted, signal peptide; Secreted Cellular Component: extracellular space; collagen; extracellular region Molecular Function: mannose binding; protein binding; eukaryotic cell surface binding; bacterial cell surface binding; calcium-dependent protein binding; receptor binding Biological Process: defense response to Gram-positive bacterium; killing by host of symbiont cells; positive regulation of phagocytosis; acute-phase response; innate immune response; response to oxidative stress; opsonization; complement activation, lectin pathway; complement activation, classical pathway; complement activation Reference #:  P11226 (UniProtKB) Gene Symbols: MBL2 Molecular weight: 26,144 Da Basal Isoelectric point: 5.39  Predict pI for various phosphorylation states

Select Structure to View Below MBL2 1HUP - A=108-248 (human)

STRING  |  Scansite  |  Phospho.ELM  |  Pfam  |  RCSB PDB  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein

	Modification Sites and Domains

	Modification Sites in Parent Protein, Orthologs, and Isoforms

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		S100-p	QKGDPGKsPDGDSSL
0	1		S110-p	GDSSLAAsERKALQT

	mouse
-	under review
-	under review

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