Ager
entrez
11596
canonical
uniprot
Q62151
canonical
ensembl
ENSMUSG00000015452
resolver
ensp
ENSMUSP00000015596
resolver
ensp
ENSMUSP00000134401
resolver
ensp
ENSMUSP00000134579
resolver
genesymbol
Ager
resolver
genesymbol_syn
Rage
resolver
uniprot
C5H3H4
resolver
uniprot
C5H3H5
resolver
uniprot
C5H3H7
resolver
uniprot
C5H3I0
resolver
uniprot
C5H7W3
resolver
uniprot
C5H7W4
resolver
uniprot
C5H7W5
resolver
uniprot
C5H7W6
resolver
uniprot
C5H7W7
resolver
uniprot
C5H7W8
resolver
uniprot
C5H7W9
resolver
uniprot
O35444
resolver
uniprot
Q2PGG1
resolver
uniprot
V5R4Y0
resolver
uniprot_entry
RAGE_MOUSE
resolver
uniprot_sec
C5H3H4
resolver
uniprot_sec
C5H3H5
resolver
uniprot_sec
C5H3H7
resolver
uniprot_sec
C5H3I0
resolver
uniprot_sec
C5H7W3
resolver
uniprot_sec
C5H7W4
resolver
uniprot_sec
C5H7W5
resolver
uniprot_sec
C5H7W6
resolver
uniprot_sec
C5H7W7
resolver
uniprot_sec
C5H7W8
resolver
uniprot_sec
C5H7W9
resolver
uniprot_sec
O35444
resolver
uniprot_sec
Q2PGG1
resolver
uniprot_sec
V5R4Y0
resolver
amino_acid_sequence
MPAGTAARAWVLVLALWGAVAGGQNITARIGEPLVLSCKGAPKKPPQQLEWKLNTGRTEAWKVLSPQGGPWDSVARILPNGSLLLPATGIVDEGTFRCRATNRRGKEVKSNYRVRVYQIPGKPEIVDPASELTASVPNKVGTCVSEGSYPAGTLSWHLDGKLLIPDGKETLVKEETRRHPETGLFTLRSELTVIPTQGGTHPTFSCSFSLGLPRRRPLNTAPIQLRVREPGPPEGIQLLVEPEGGIVAPGGTVTLTCAISAQPPPQVHWIKDGAPLPLAPSPVLLLPEVGHEDEGTYSCVATHPSHGPQESPPVSIRVTETGDEGPAEGSVGESGLGTLALALGILGGLGVVALLVGAILWRKRQPRREERKAPESQEDEEERAELNQSEEAEMPENGAGGP
uniprot
proteins
function
FUNCTION: Cell surface pattern recognition receptor that senses endogenous stress signals with a broad ligand repertoire including advanced glycation end products, S100 proteins, high-mobility group box 1 protein/HMGB1, amyloid beta/APP oligomers, nucleic acids, histones, phospholipids and glycosaminoglycans (PubMed:21270403, PubMed:32670276). Advanced glycation end products (AGEs) are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. These ligands accumulate at inflammatory sites during the pathogenesis of various diseases including diabetes, vascular complications, neurodegenerative disorders and cancers, and RAGE transduces their binding into pro-inflammatory responses. Upon ligand binding, uses TIRAP and MYD88 as adapters to transduce the signal ultimately leading to the induction of inflammatory cytokines IL6, IL8 and TNFalpha through activation of NF-kappa-B. Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key pro-inflammatory mediators (By similarity). Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons (PubMed:19901339). ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Participates in endothelial albumin transcytosis together with HMGB1 through the RAGE/SRC/Caveolin-1 pathway, leading to endothelial hyperpermeability (By similarity). Mediates the loading of HMGB1 in extracellular vesicles (EVs) that shuttle HMGB1 to hepatocytes by transferrin-mediated endocytosis and subsequently promote hepatocyte pyroptosis by activating the NLRP3 inflammasome (By similarity). Binds to DNA and promotes extracellular hypomethylated DNA (CpG DNA) uptake by cells via the endosomal route to activate inflammatory responses (By similarity). Mediates phagocytosis by non-professional phagocytes (NPP) and this is enhanced by binding to ligands including RNA, DNA, HMGB1 and histones (By similarity). Promotes NPP-mediated phagocytosis of Saccharomyces cerevisiae spores by binding to RNA attached to the spore wall (PubMed:35974093). Also promotes NPP-mediated phagocytosis of apoptotic cells (By similarity). Following DNA damage, recruited to DNA double-strand break sites where it colocalizes with the MRN repair complex via interaction with double-strand break repair protein MRE11 (PubMed:28977635). Enhances the endonuclease activity of MRE11, promoting the end resection of damaged DNA (PubMed:28977635). Promotes DNA damage repair in trophoblasts which enhances trophoblast invasion and contributes to placental development and maintenance (By similarity). Protects cells from DNA replication stress by localizing to damaged replication forks where it stabilizes the MCM2-7 complex and promotes faithful progression of the replication fork (By similarity). {ECO:0000250|UniProtKB:Q15109, ECO:0000250|UniProtKB:Q63495, ECO:0000269|PubMed:10399917, ECO:0000269|PubMed:18539754, ECO:0000269|PubMed:19901339, ECO:0000269|PubMed:19906677, ECO:0000269|PubMed:21270403, ECO:0000269|PubMed:28977635, ECO:0000269|PubMed:32670276, ECO:0000269|PubMed:35974093}.; FUNCTION: [Isoform 2]: Is able to inhibit advanced glycation end product (AGE)-induced nuclear factor NF-kappa-B activation. {ECO:0000269|PubMed:16503878}.; FUNCTION: [Isoform 10]: Down-regulates receptor for advanced glycation end products (RAGE)-ligand induced signaling through various MAPK pathways including ERK1/2, p38 and SAPK/JNK. Significantly affects tumor cell properties through decreasing cell migration, invasion, adhesion and proliferation, and increasing cellular apoptosis. Exhibits drastic inhibition on tumorigenesis in vitro. {ECO:0000269|PubMed:24260107}.
uniprot
proteins
mass_dalton
42654
uniprot
proteins
mutagenesis
MUTAGEN 376; /note="S->A: Reduces phosphorylation. Abolishes phosphorylation and ability to reduce DNA damage; when associated with A-389."; /evidence="ECO:0000269|PubMed:28977635"; MUTAGEN 376; /note="S->E: Phosphomimetic mutant which does not lose the ability to reduce DNA damage; when associated with E-389."; /evidence="ECO:0000269|PubMed:28977635"; MUTAGEN 389; /note="S->A: Reduces phosphorylation. Abolishes phosphorylation and ability to reduce DNA damage; when associated with A-376."; /evidence="ECO:0000269|PubMed:28977635"; MUTAGEN 389; /note="S->E: Phosphomimetic mutant which does not lose the ability to reduce DNA damage; when associated with E-389."; /evidence="ECO:0000269|PubMed:28977635
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on its cytoplasmic domain by PKCzeta/PRKCZ upon ligand binding (By similarity). Phosphorylated by ATM following DNA damage (PubMed:28977635). {ECO:0000250|UniProtKB:Q15109, ECO:0000269|PubMed:28977635}.; PTM: Targeted by the ubiquitin E3 ligase subunit FBXO10 to mediate its ubiquitination and degradation. {ECO:0000250|UniProtKB:Q15109}.
uniprot
proteins
pubmed
10399917
uniprot
proteins
pubmed
14656967
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16503878
uniprot
proteins
pubmed
18539754
uniprot
proteins
pubmed
19164451
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19901339
uniprot
proteins
pubmed
19906677
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21270403
uniprot
proteins
pubmed
23679870
uniprot
proteins
pubmed
24260107
uniprot
proteins
pubmed
28977635
uniprot
proteins
pubmed
32338774
uniprot
proteins
pubmed
32670276
uniprot
proteins
pubmed
35974093
uniprot
proteins
pubmed
36807739
uniprot
proteins
pubmed
9224812
uniprot
proteins
sequence_length
402
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15109}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q15109}. Early endosome {ECO:0000250|UniProtKB:Q15109}. Nucleus {ECO:0000269|PubMed:28977635}. Note=Nuclear translocation is enhanced by irradiation, hypoxia and reperfusion injury to brain or kidney. {ECO:0000269|PubMed:28977635}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:Q15109}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:16503878}.; SUBCELLULAR LOCATION: [Isoform 10]: Cell membrane {ECO:0000269|PubMed:24260107}; Single-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 341..361; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins