UniProt ID | PLBL1_MOUSE | |
---|---|---|
UniProt AC | Q8VCI0 | |
Protein Name | Phospholipase B-like 1 | |
Gene Name | Plbd1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 550 | |
Subcellular Localization | Lysosome. | |
Protein Description | Exhibits weak phospholipase activity, acting on various phospholipids, including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids. However, in view of the small size of the putative binding pocket, it has been proposed that it may act rather as an amidase or a peptidase (By similarity).. | |
Protein Sequence | MCHRSPGRSLRPPSPLLLLLPLLLQPPWAAGAASQSDPTGVHCATAYWSPESKKVEIKTVLDKNGDAYGYYNDSIKTTGWGILEIRAGYGSQVLSNEIIMFLAGYLEGYLTALHMYDHFTNLYPQLIKNPSIVKKVQDFMEKQEMWTRQNIKAQKDDPFWRHTGYVVTQLDGLYLGAQKRASEEKIKPMTMFQIQFLNAVGDLLDLIPSLSPTKSSSMMKFKIWEMGHCSALIKVLPGFENIYFAHSSWYTYAAMLRIYKHWDFNIKDKYTLSKRLSFSSYPGFLESLDDFYILSSGLILLQTTNSVYNKTLLKQVVPKTLLAWQRVRVANMMAEGGKEWAQIFSKHNSGTYNNQYMVLDLKKVTINRSLDKGTLYIVEQIPTYVEYSDQTNVLRKGYWASYNIPFHKTIYNWSGYPLLVHKLGLDYSYDLAPRAKIFRRDQGNVTDMASMKYIMRYNNYKEDPYSKGDPCSTICCREDLNGASPSPGGCYDTKVADIFLASQYKAYAISGPTVQDGLPPFNWNRFNETLHRGMPEVFDFNFVTMKPILS | |
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 |
---|---|---|---|---|---|
72 | N-linked_Glycosylation | GDAYGYYNDSIKTTG CCCCCEECCCCCCCC | 28.24 | 16170054 | |
309 | N-linked_Glycosylation | QTTNSVYNKTLLKQV ECCCCCCCHHHHHHH | 28.78 | - | |
367 | N-linked_Glycosylation | DLKKVTINRSLDKGT EEEEEEEECCCCCCE | 20.37 | - | |
412 | N-linked_Glycosylation | PFHKTIYNWSGYPLL CCCCEECCCCCCCEE | 23.68 | - | |
457 | Phosphorylation | SMKYIMRYNNYKEDP HHHHHHHHCCCCCCC | 7.15 | 22817900 | |
527 | N-linked_Glycosylation | PFNWNRFNETLHRGM CCCHHHHHHHHHCCC | 37.80 | - | |
529 | Phosphorylation | NWNRFNETLHRGMPE CHHHHHHHHHCCCCC | 29.03 | 30635358 | |
544 | Phosphorylation | VFDFNFVTMKPILS- EECCEEEEECCCCC- | 18.49 | 30635358 | |
550 | Phosphorylation | VTMKPILS------- EEECCCCC------- | 38.61 | 30635358 |
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 PLBL1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PLBL1_MOUSE !! |
* 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 PLBL1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PLBL1_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"High throughput quantitative glycomics and glycoform-focusedproteomics of murine dermis and epidermis."; Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K.,Monde K., Nishimura S.; Mol. Cell. Proteomics 4:1977-1989(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-72, AND MASS SPECTROMETRY. |