LOX5_HUMAN - dbPTM
LOX5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LOX5_HUMAN
UniProt AC P09917
Protein Name Arachidonate 5-lipoxygenase
Gene Name ALOX5
Organism Homo sapiens (Human).
Sequence Length 674
Subcellular Localization Cytoplasm. Nucleus matrix. Nucleus membrane
Peripheral membrane protein. Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-272. Calcium binding promotes translocation from the cytosol and the nuclea
Protein Description Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes..
Protein Sequence MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGCNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECGLFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWEAIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLTVVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPYYYLSPDRIPNSVAI
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
21PhosphorylationWFAGTDDYIYLSLVG
EECCCCCEEEEEECC		8.3567340431
23PhosphorylationAGTDDYIYLSLVGSA
CCCCCEEEEEECCCC		5.5267340433
43PhosphorylationHLLDKPFYNDFERGA
HHCCCCCCCCCCCCC		23.5067340429
54PhosphorylationERGAVDSYDVTVDEE
CCCCCCEEEEECCHH		15.2367340425
75PhosphorylationVRIEKRKYWLNDDWY
EEEEECCEECCCCEE		21.1146155867
87PhosphorylationDWYLKYITLKTPHGD
CEEEEEEEEECCCCC		21.0746155855
95PhosphorylationLKTPHGDYIEFPCYR
EECCCCCCEEECEEE		13.6228064214
101PhosphorylationDYIEFPCYRWITGDV
CCEEECEEEEECCCE		14.827443033
105PhosphorylationFPCYRWITGDVEVVL
ECEEEEECCCEEEEE		21.9946155849
182PhosphorylationGVDFVLNYSKAMENL
CCCHHHCHHHHHHHH		13.8546155861
183PhosphorylationVDFVLNYSKAMENLF
CCHHHCHHHHHHHHH		16.9246155837
250PhosphorylationPVLIRRCTELPEKLP
HHHHHHCCCCCCCCC		38.4567340409
259PhosphorylationLPEKLPVTTEMVECS
CCCCCCCCHHHHHHH		18.3367340421
260PhosphorylationPEKLPVTTEMVECSL
CCCCCCCHHHHHHHH		23.4767340423
266PhosphorylationTTEMVECSLERQLSL
CHHHHHHHHHHHHCH		21.5467340411
272PhosphorylationCSLERQLSLEQEVQQ
HHHHHHHCHHHHHHC		22.8610779545
311UbiquitinationQFLAAPICLLYKNLA
HHHHHHHHHHHHHHH		1.7729901268
318UbiquitinationCLLYKNLANKIVPIA
HHHHHHHHCCHHHEE		25.3529901268
431UbiquitinationKANATGGGGHVQMVQ
CCCCCCCCHHHHHHH		25.1229901268
434UbiquitinationATGGGGHVQMVQRAM
CCCCCHHHHHHHHHH		4.4329901268
435UbiquitinationTGGGGHVQMVQRAMK
CCCCHHHHHHHHHHC		22.2129901268
445PhosphorylationQRAMKDLTYASLCFP
HHHHCCCCHHHHHCH		27.4667340417
446PhosphorylationRAMKDLTYASLCFPE
HHHCCCCHHHHHCHH		11.0767340427
448PhosphorylationMKDLTYASLCFPEAI
HCCCCHHHHHCHHHH		18.4367340413
456UbiquitinationLCFPEAIKARGMESK
HHCHHHHHHCCCCCC		38.7929901268
463UbiquitinationKARGMESKEDIPYYF
HHCCCCCCCCCCEEE		46.2129901268
486PhosphorylationWEAIRTFTAEVVDIY
HHHHHHHEEEEEEEE		22.6967340419
524PhosphorylationGMRGRKSSGFPKSVK
CCCCCCCCCCCCCCC		47.7021098726
528AcetylationRKSSGFPKSVKSREQ
CCCCCCCCCCCCHHH		66.677704161
532PhosphorylationGFPKSVKSREQLSEY
CCCCCCCCHHHHHHH		38.6046155843
548UbiquitinationTVVIFTASAQHAAVN
CEEEEECCCCCHHHH		25.9629901268
551UbiquitinationIFTASAQHAAVNFGQ
EEECCCCCHHHHCCC		18.5129901268
580UbiquitinationRAPPPTAKGVVTIEQ
CCCCCCCCCEEEHHH		55.5029901268
664PhosphorylationQLPYYYLSPDRIPNS
CCCEEECCCCCCCCC		14.5012205041
671PhosphorylationSPDRIPNSVAI----
CCCCCCCCCCC----		13.9467340415
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
43YPhosphorylationKinaseFGRP09769
PSP
43YPhosphorylationKinaseHCKP08631
PSP
43YPhosphorylationKinaseYESP07947
PSP
54YPhosphorylationKinaseFGRP09769
PSP
54YPhosphorylationKinaseHCKP08631
PSP
54YPhosphorylationKinaseYESP07947
PSP
95YPhosphorylationKinaseHCKP08631
PSP
272SPhosphorylationKinasePKA_GROUP-PhosphoELM
272SPhosphorylationKinasePKA-FAMILY-GPS
272SPhosphorylationKinaseMAPK2P49137
PhosphoELM
272SPhosphorylationKinaseKCC2AQ9UQM7
PhosphoELM
272SPhosphorylationKinasePRKACAP17612
GPS
446YPhosphorylationKinaseYESP07947
PSP
446YPhosphorylationKinaseFGRP09769
PSP
448SPhosphorylationKinasePKACAP17612
PSP
524SPhosphorylationKinasePRKACAP05132
GPS
524SPhosphorylationKinasePKA-FAMILY-GPS
524SPhosphorylationKinasePKACAP17612
PSP
524SPhosphorylationKinasePKA-Uniprot
524SPhosphorylationKinasePKA_GROUP-PhosphoELM
664SPhosphorylationKinaseMAPK1P28482
GPS
671SPhosphorylationKinasePKACAP17612
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
272SPhosphorylation

11844797
524SPhosphorylation

15280375
524SPhosphorylation

15280375
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 LOX5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COTL1_HUMANCOTL1physical
11297527
TGFA1_HUMANTGFBRAP1physical
10051563
A4_HUMANAPPphysical
21832049
AL5AP_HUMANALOX5APphysical
19233132
COTL1_HUMANCOTL1physical
10051563
DICER_HUMANDICER1physical
10051563
DICER_HUMANDICER1physical
19022417
P85A_HUMANPIK3R1physical
21200133
MEOX1_HUMANMEOX1physical
25416956
REL_HUMANRELphysical
25416956
MD1L1_HUMANMAD1L1physical
25416956
HIPL2_HUMANHHIPL2physical
25416956
CEP63_HUMANCEP63physical
25416956
SYCE1_HUMANSYCE1physical
25416956
NUTM1_HUMANNUTM1physical
25416956
CE57L_HUMANCEP57L1physical
25416956
AL5AP_HUMANALOX5APphysical
26396238
AL5AP_HUMANALOX5APphysical
26327594
COTL1_HUMANCOTL1physical
25034252
RUND1_HUMANRUNDC1physical
28514442
SLAI1_HUMANSLAIN1physical
28514442
TBD2B_HUMANTBC1D2Bphysical
28514442
ERG7_HUMANLSSphysical
28514442
KDM3B_HUMANKDM3Bphysical
28514442
TPP2_HUMANTPP2physical
28514442
MPP5_HUMANMPP5physical
28514442
OSB11_HUMANOSBPL11physical
28514442
CKAP5_HUMANCKAP5physical
28514442
KKCC2_HUMANCAMKK2physical
28514442
PLPL2_HUMANPNPLA2physical
28514442
MND1_HUMANMND1physical
28514442
MTMR4_HUMANMTMR4physical
28514442
DDHD2_HUMANDDHD2physical
28514442
RB3GP_HUMANRAB3GAP1physical
28514442
KI16B_HUMANKIF16Bphysical
28514442
PSMF1_HUMANPSMF1physical
28514442
AMOT_HUMANAMOTphysical
28514442
DMWD_HUMANDMWDphysical
28514442
TRI65_HUMANTRIM65physical
28514442
ERC6L_HUMANERCC6Lphysical
28514442
PMF1_HUMANPMF1physical
28514442
ITSN1_HUMANITSN1physical
28514442
MTMR3_HUMANMTMR3physical
28514442
CN080_HUMANC14orf80physical
28514442
PUR8_HUMANADSLphysical
28514442
COG2_HUMANCOG2physical
28514442
CDC16_HUMANCDC16physical
28514442
AMOL1_HUMANAMOTL1physical
28514442
NFKB2_HUMANNFKB2physical
28514442
ERMP1_HUMANERMP1physical
28514442
MADD_HUMANMADDphysical
28514442
ARMX5_HUMANARMCX5physical
28514442
KS6A2_HUMANRPS6KA2physical
28514442
NEUR3_HUMANNEU3physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D00414 Zileuton (USP/INN); Zyflo (TN)
D01773 Oxatomide (JAN/USAN/INN); Celtect (TN)
D03010 Atreleuton (USAN/INN)
D03080 Benoxaprofen (USAN/INN); Oraflex (TN)
D03652 Darbufelone mesylate (USAN)
D03882 Docebenone (USAN/INN)
D03990 Enazadrem phosphate (USAN)
D04151 Fenleuton (USAN/INN); Lofrin (TN)
D04770 Lonapalene (USAN)
D09667 Setileuton (USAN/INN)
DrugBank
DB00233Aminosalicylic Acid
DB01014Balsalazide
DB00586Diclofenac
DB00711Diethylcarbamazine
DB00179Masoprocol
DB00939Meclofenamic acid
DB00244Mesalazine
DB01017Minocycline
DB00471Montelukast
DB00795Sulfasalazine
DB00163Vitamin E
DB00744Zileuton
Regulatory Network of LOX5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation of serine 271 on 5-lipoxygenase and its role innuclear export.";
Flamand N., Luo M., Peters-Golden M., Brock T.G.;
J. Biol. Chem. 284:306-313(2009).
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-272, AND MUTAGENESIS OFSER-272.
"Protein kinase A inhibits leukotriene synthesis by phosphorylation of5-lipoxygenase on serine 523.";
Luo M., Jones S.M., Phare S.M., Coffey M.J., Peters-Golden M.,Brock T.G.;
J. Biol. Chem. 279:41512-41520(2004).
Cited for: PHOSPHORYLATION AT SER-524, AND MUTAGENESIS OF SER-524.
"Arachidonic acid promotes phosphorylation of 5-lipoxygenase at Ser-271 by MAPK-activated protein kinase 2 (MK2).";
Werz O., Szellas D., Steinhilber D., Radmark O.;
J. Biol. Chem. 277:14793-14800(2002).
Cited for: PHOSPHORYLATION AT SER-272.

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