UniProt ID | MAL2_HUMAN | |
---|---|---|
UniProt AC | Q969L2 | |
Protein Name | Protein MAL2 | |
Gene Name | MAL2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 176 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein. Apical cell membrane Multi-pass membrane protein. Endomembrane system. Cytoplasm, perinuclear region. Associated with lipid rafts. In polarized epithelial cells, restricted to the apical surface. In hepato |
|
Protein Description | Member of the machinery of polarized transport. Required for the indirect transcytotic route at the step of the egress of the transcytosing cargo from perinuclear endosomes in order for it to travel to the apical surface via a raft-dependent pathway.. | |
Protein Sequence | MSAGGASVPPPPNPAVSFPPPRVTLPAGPDILRTYSGAFVCLEILFGGLVWILVASSNVPLPLLQGWVMFVSVTAFFFSLLFLGMFLSGMVAQIDANWNFLDFAYHFTVFVFYFGAFLLEAAATSLHDLHCNTTITGQPLLSDNQYNINVAASIFAFMTTACYGCSLGLALRRWRP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSAGGASVP ------CCCCCCCCC | 35.30 | 25849741 | |
7 | Phosphorylation | -MSAGGASVPPPPNP -CCCCCCCCCCCCCC | 38.13 | 25841592 | |
17 | Phosphorylation | PPPNPAVSFPPPRVT CCCCCCCCCCCCCEE | 33.86 | 27251275 | |
132 | N-linked_Glycosylation | SLHDLHCNTTITGQP HHHHCCCCCEECCCC | 29.52 | 12370246 |
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 MAL2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MAL2_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 MAL2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TBB5_HUMAN | TUBB | physical | 25416956 | |
RAB37_HUMAN | RAB37 | physical | 25416956 |
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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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-132, AND MASSSPECTROMETRY. | |
"MAL2, a novel raft protein of the MAL family, is an essentialcomponent of the machinery for transcytosis in hepatoma HepG2 cells."; de Marco M.C., Martin-Belmonte F., Kremer L., Albar J.P., Correas I.,Vaerman J.P., Marazuela M., Byrne J.A., Alonso M.A.; J. Cell Biol. 159:37-44(2002). Cited for: FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-132. |