Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
5-LO (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
5-LO arachidonate 5-lipoxygenase. Arachidonic acid promotes its phosphorylation by p38 MAPK-regulated MAPKAP kinases. Upregulated in glioblastoma multiforme and colon, pancreatic and bladder cancer. Note: This description may include information from UniProtKB.
Protein type: Lipid Metabolism - arachidonic acid; Oxidoreductase; Nuclear envelope; Lipid Metabolism - linoleic acid; EC 1.13.11.34
Cellular Component: extracellular space; nuclear membrane; nuclear matrix; nuclear envelope lumen; nuclear envelope; cytosol
Molecular Function: protein binding; iron ion binding; arachidonate 5-lipoxygenase activity
Biological Process: leukotriene biosynthetic process; leukotriene production during acute inflammatory response; lipoxygenase pathway; arachidonic acid metabolic process; leukotriene metabolic process
Reference #:  P09917 (UniProtKB)
Alt. Names/Synonyms: 5-lipoxygenase; 5-LO; 5-LOX; 5LPG; ALOX5; Arachidonate 5-lipoxygenase; arachidonic acid 5-lipoxygenase; leukotriene A4 synthase; LOG5; LOX5; MGC163204
Gene Symbols: ALOX5
Molecular weight: 77,983 Da
Basal Isoelectric point: 5.51  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

5-LO

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
enzymatic activity, induced: S272‑p, S664‑p
enzymatic activity, inhibited: S524‑p
intracellular localization: S272‑p, S524‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
6 2 S272-p CSLERQLsLEQEVQQ
0 1 K456 LCFPEAIKARGMESK
3 0 S524-p GMRGRKSsGFPKSVK
2 0 S664-p QLPYYYLsPDRIPNS
3748 : Phospho-5-Lipoxygenase (Ser271) Antibody
3749 : Phospho-5-Lipoxygenase (Ser663) Antibody
  mouse

 
S272-p CSLERQLsLEQEVQE
K456-u LCFPEAIkARGMDST
S524 GMRGKKASGFPKSIK
S664 KLPYYYLSPDRIPNS
3748 : Phospho-5-Lipoxygenase (Ser271) Antibody
3749 : Phospho-5-Lipoxygenase (Ser663) Antibody
  rat

 
S271 CSLERQLSLEQEVQE
K455 LCFPEAIKARGMDNT
S523-p GMRGRKAsGFPKSIK
S663 KLPYYYLSPDRIPNS
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.