LOXE3_HUMAN - dbPTM
LOXE3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LOXE3_HUMAN
UniProt AC Q9BYJ1
Protein Name Hydroperoxide isomerase ALOXE3
Gene Name ALOXE3
Organism Homo sapiens (Human).
Sequence Length 711
Subcellular Localization Cytoplasm .
Protein Description Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced dioxygenase activity compared to other lipoxygenases. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols. The dioxygenase activity requires a step of activation of the enzyme by molecular oxygen. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites. Plays also a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG. Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia..
Protein Sequence MAVYRLCVTTGPYLRAGTLDNISVTLVGTCGESPKQRLDRMGRDFAPGSVQKYKVRCTAELGELLLLRVHKERYAFFRKDSWYCSRICVTEPDGSVSHFPCYQWIEGYCTVELRPGTARTICQDSLPLLLDHRTRELRARQECYRWKIYAPGFPCMVDVNSFQEMESDKKFALTKTTTCVDQGDSSGNRYLPGFPMKIDIPSLMYMEPNVRYSATKTISLLFNAIPASLGMKLRGLLDRKGSWKKLDDMQNIFWCHKTFTTKYVTEHWCEDHFFGYQYLNGVNPVMLHCISSLPSKLPVTNDMVAPLLGQDTCLQTELERGNIFLADYWILAEAPTHCLNGRQQYVAAPLCLLWLSPQGALVPLAIQLSQTPGPDSPIFLPTDSEWDWLLAKTWVRNSEFLVHENNTHFLCTHLLCEAFAMATLRQLPLCHPIYKLLLPHTRYTLQVNTIARATLLNPEGLVDQVTSIGRQGLIYLMSTGLAHFTYTNFCLPDSLRARGVLAIPNYHYRDDGLKIWAAIESFVSEIVGYYYPSDASVQQDSELQAWTGEIFAQAFLGRESSGFPSRLCTPGEMVKFLTAIIFNCSAQHAAVNSGQHDFGAWMPNAPSSMRQPPPQTKGTTTLKTYLDTLPEVNISCNNLLLFWLVSQEPKDQRPLGTYPDEHFTEEAPRRSIAAFQSRLAQISRDIQERNQGLALPYTYLDPPLIENSVSI
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
44 (in isoform 2)Phosphorylation-38.03-
44PhosphorylationRLDRMGRDFAPGSVQ
HHHHCCCCCCCCCCC
38.03-
52UbiquitinationFAPGSVQKYKVRCTA
CCCCCCCCEEEEEEE
44.9029967540
117PhosphorylationTVELRPGTARTICQD
EEEECCCCHHHHHHC
18.6910394743
134PhosphorylationPLLLDHRTRELRARQ
HHHHCHHHHHHHHHH
25.6910394753
169UbiquitinationFQEMESDKKFALTKT
HHHHHCCCCEEEEEE
60.1023000965
170UbiquitinationQEMESDKKFALTKTT
HHHHCCCCEEEEEEE
40.6423000965
175UbiquitinationDKKFALTKTTTCVDQ
CCCEEEEEEEEEEEC
44.7323000965
176PhosphorylationKKFALTKTTTCVDQG
CCEEEEEEEEEEECC
23.3150564823
184UbiquitinationTTCVDQGDSSGNRYL
EEEEECCCCCCCCCC
33.7229967540
295PhosphorylationHCISSLPSKLPVTND
HHHHCCCCCCCCCCC
52.7124719451
300PhosphorylationLPSKLPVTNDMVAPL
CCCCCCCCCCCHHHH
24.4624719451
301UbiquitinationPSKLPVTNDMVAPLL
CCCCCCCCCCHHHHH
35.3023000965
302UbiquitinationSKLPVTNDMVAPLLG
CCCCCCCCCHHHHHC
24.4623000965
307UbiquitinationTNDMVAPLLGQDTCL
CCCCHHHHHCCCCHH
6.3923000965
316PhosphorylationGQDTCLQTELERGNI
CCCCHHHHHHHHCCE
29.5924719451
407PhosphorylationFLVHENNTHFLCTHL
EEEECCCCHHHHHHH
26.1122468782
423PhosphorylationCEAFAMATLRQLPLC
HHHHHHHHHHCCCCC
14.9122468782
434PhosphorylationLPLCHPIYKLLLPHT
CCCCCHHHHHHCCCC
10.4746106903
578PhosphorylationGEMVKFLTAIIFNCS
HHHHHHHHHHHHHCC
20.9527251275
593PhosphorylationAQHAAVNSGQHDFGA
HHCHHHHCCCCCCCC
32.9827251275
607PhosphorylationAWMPNAPSSMRQPPP
CCCCCCCCCCCCCCC
34.0627251275
608PhosphorylationWMPNAPSSMRQPPPQ
CCCCCCCCCCCCCCC
19.5427251275
616PhosphorylationMRQPPPQTKGTTTLK
CCCCCCCCCCCCCHH
36.9027251275
617UbiquitinationRQPPPQTKGTTTLKT
CCCCCCCCCCCCHHH
49.3527667366
677PhosphorylationRSIAAFQSRLAQISR
HHHHHHHHHHHHHHH
23.8646106909
739Phosphorylation-----------------------------------
-----------------------------------
27251275
749Ubiquitination---------------------------------------------
---------------------------------------------
27667366

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 LOXE3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LOXE3_HUMAN !!

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 LOXE3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NBEA_HUMANNBEAphysical
28514442
ZFHX4_HUMANZFHX4physical
28514442
KTU_HUMANDNAAF2physical
28514442
SRC_HUMANSRCphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
EDEM3_HUMANEDEM3physical
28514442
HOOK1_HUMANHOOK1physical
28514442
HERC4_HUMANHERC4physical
28514442
CH60_HUMANHSPD1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LOXE3_HUMAN

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Related Literatures of Post-Translational Modification

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