UniProt ID | MZB1_HUMAN | |
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UniProt AC | Q8WU39 | |
Protein Name | Marginal zone B- and B1-cell-specific protein | |
Gene Name | MZB1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 189 | |
Subcellular Localization |
Isoform 1: Endoplasmic reticulum lumen . Secreted . Isoform 2: Cytoplasm . Diffuse granular localization in the cytoplasm surrounding the nucleus (PubMed:11350957). |
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Protein Description | Associates with immunoglobulin M (IgM) heavy and light chains and promotes IgM assembly and secretion. May exert its effect by acting as a molecular chaperone or as an oxidoreductase as it displays a low level of oxidoreductase activity (By similarity). Isoform 2 may be involved in regulation of apoptosis. Helps to diversify peripheral B-cell functions by regulating Ca(2+) stores, antibody secretion and integrin activation.; Acts as a hormone-regulated adipokine/proinflammatory cytokine that is implicated in causing chronic inflammation, affecting cellular expansion and blunting insulin response in adipocytes. May have a role in the onset of insulin resistance.. | |
Protein Sequence | MRLSLPLLLLLLGAWAIPGGLGDRAPLTATAPQLDDEEMYSAHMPAHLRCDACRAVAYQMWQNLAKAETKLHTSNSGGRRELSELVYTDVLDRSCSRNWQDYGVREVDQVKRLTGPGLSEGPEPSISVMVTGGPWPTRLSRTCLHYLGEFGEDQIYEAHQQGRGALEALLCGGPQGACSEKVSATREEL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
28 | O-linked_Glycosylation | LGDRAPLTATAPQLD CCCCCCCEEECCCCC | OGP | ||
30 | O-linked_Glycosylation | DRAPLTATAPQLDDE CCCCCEEECCCCCHH | OGP | ||
41 | O-linked_Glycosylation | LDDEEMYSAHMPAHL CCHHHHHHCCCCHHH | OGP | ||
66 | Ubiquitination | QMWQNLAKAETKLHT HHHHHHHHHHHHCCC | 22817900 | ||
70 | Ubiquitination | NLAKAETKLHTSNSG HHHHHHHHCCCCCCC | 22817900 | ||
70 | Acetylation | NLAKAETKLHTSNSG HHHHHHHHCCCCCCC | 25953088 | ||
70 (in isoform 1) | Ubiquitination | - | 21906983 | ||
125 | O-linked_Glycosylation | LSEGPEPSISVMVTG CCCCCCCCEEEEEEC | OGP | ||
181 | Ubiquitination | PQGACSEKVSATREE CCCCCCHHHCCHHHC | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of MZB1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of MZB1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of MZB1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MZB1_HUMAN !! |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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