LOX15_RAT - dbPTM
LOX15_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LOX15_RAT
UniProt AC Q02759
Protein Name Arachidonate 15-lipoxygenase
Gene Name Alox15
Organism Rattus norvegicus (Rat).
Sequence Length 663
Subcellular Localization Cytoplasm, cytosol . Cell membrane
Peripheral membrane protein. Lipid droplet. Predominantly cytosolic
becomes enriched at membranes upon calcium binding. Translocates from the cytosol to the plasma membrane when stimulated by IL13/interleukin-13 a
Protein Description Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. In addition to its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass..
Protein Sequence MGVYRIRVSTGDSKYAGSNNEVYLWLVGQHGEASLGKLLRPCRDSEAEFKVDVSEYLGPLLFVRVQKWHYLTDDAWFCNWISVKGPGDQGSEYMFPCYRWVQGRSILSLPEGTGCTVVEDSQGLFRKHREEELEERRSLYRWGNWKDGSILNVAAASISDLPVDQRFREDKRIEFEASQVIGVMDTVVNFPINTVTCWKSLDDFNCVFKSGHTKMAERVRNSWKEDAFFGYQFLNGANPMVLKRSTCLPARLVFPPGMEKLQAQLNKELQKGTLFEADFFLLDGIKANVILCSQQYLAAPLVMLKLMPDGQLLPIAIQLELPKTGSTPPPIFTPSDPPMDWLLAKCWVRSSDLQLHELQAHLLRGHLMAEVFAVATMRCLPSVHPVFKLLVPHLLYTMEINVRARSDLISERGFFDKAMSTGGGGHLDLLKQAGAFLTYCSLCPPDDLAERGLLDIETCFYAKDALRLWQIMNRYVVGMFNLHYKTDKAVQDDYELQSWCREITDIGLQGAQDRGFPTSLQSRAQACYFITMCIFTCTAQHSSVHLGQLDWFYWVPNAPCTMRLPPPTTKEATMEKLMATLPNPNQSTLQINVVWLLGRRQAVMVPLGQHSEEHFPNPEAKAVLKKFREELAALDKEIEIRNKSLDIPYEYLRPSMVENSVAI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
149PhosphorylationWGNWKDGSILNVAAA
CCCCCCCCCEEEEEE
22673903
410PhosphorylationRARSDLISERGFFDK
CCCHHHHHCCCCHHH
30181290

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 LOX15_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LOX15_RAT !!

Disease-associated PTM Sites based on SAP

* 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 LOX15_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LOX15_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LOX15_RAT

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Related Literatures of Post-Translational Modification

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