AGER
entrez
177
canonical
uniprot
Q15109
canonical
ensembl
ENSG00000204305
resolver
ensembl
ENSG00000206320
resolver
ensembl
ENSG00000229058
resolver
ensembl
ENSG00000230514
resolver
ensembl
ENSG00000231268
resolver
ensembl
ENSG00000234729
resolver
ensembl
ENSG00000237405
resolver
ensp
ENSP00000364195
resolver
ensp
ENSP00000364208
resolver
ensp
ENSP00000364210
resolver
ensp
ENSP00000364217
resolver
ensp
ENSP00000387887
resolver
ensp
ENSP00000415144
resolver
ensp
ENSP00000416042
resolver
ensp
ENSP00000521524
resolver
ensp
ENSP00000645073
resolver
ensp
ENSP00000645074
resolver
ensp
ENSP00000645076
resolver
enst
ENST00000426138
resolver
enst
ENST00000427822
resolver
genesymbol
AGER
resolver
genesymbol_syn
RAGE
resolver
hgnc
HGNC:320
resolver
uniprot
A2BFI7
resolver
uniprot
A6NKF0
resolver
uniprot
A7Y2U9
resolver
uniprot
B0V176
resolver
uniprot
B4DNX3
resolver
uniprot
Q101R3
resolver
uniprot
Q15279
resolver
uniprot
Q3L1R4
resolver
uniprot
Q3L1R5
resolver
uniprot
Q3L1R6
resolver
uniprot
Q3L1R7
resolver
uniprot
Q3L1R8
resolver
uniprot
Q3L1S0
resolver
uniprot
Q86SN1
resolver
uniprot
Q9H2X7
resolver
uniprot
Q9Y3R3
resolver
uniprot
V5R6A3
resolver
uniprot_entry
B4DNX3_HUMAN
resolver
uniprot_entry
Q101R3_HUMAN
resolver
uniprot_entry
RAGE_HUMAN
resolver
uniprot_sec
A2BFI7
resolver
uniprot_sec
A6NKF0
resolver
uniprot_sec
A7Y2U9
resolver
uniprot_sec
B0V176
resolver
uniprot_sec
Q15279
resolver
uniprot_sec
Q3L1R4
resolver
uniprot_sec
Q3L1R5
resolver
uniprot_sec
Q3L1R6
resolver
uniprot_sec
Q3L1R7
resolver
uniprot_sec
Q3L1R8
resolver
uniprot_sec
Q3L1S0
resolver
uniprot_sec
Q86SN1
resolver
uniprot_sec
Q9H2X7
resolver
uniprot_sec
Q9Y3R3
resolver
uniprot_sec
V5R6A3
resolver
amino_acid_sequence
MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP
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:27572515, PubMed:28515150, PubMed:34743181, PubMed:35974093, PubMed:24081950). Advanced glycation end products (AGEs) are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes (PubMed:21565706). 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 (PubMed:21829704, PubMed:33436632). Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key pro-inflammatory mediators (PubMed:19386136). 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:19906677). 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 (PubMed:27572515). 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 (PubMed:34743181). Binds to DNA and promotes extracellular hypomethylated DNA (CpG DNA) uptake by cells via the endosomal route to activate inflammatory responses (PubMed:24081950, PubMed:28515150). Mediates phagocytosis by non-professional phagocytes (NPP) and this is enhanced by binding to ligands including RNA, DNA, HMGB1 and histones (PubMed:35974093). 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 (PubMed:35974093). 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 (By similarity). Enhances the endonuclease activity of MRE11, promoting the end resection of damaged DNA (By similarity). Promotes DNA damage repair in trophoblasts which enhances trophoblast invasion and contributes to placental development and maintenance (PubMed:33918759). 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 (PubMed:36807739). Mediates the production of reactive oxygen species (ROS) in human endothelial cells (PubMed:25401185). {ECO:0000250|UniProtKB:Q62151, ECO:0000269|PubMed:19906677, ECO:0000269|PubMed:20943659, ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:21565706, ECO:0000269|PubMed:21829704, ECO:0000269|PubMed:24081950, ECO:0000269|PubMed:25401185, ECO:0000269|PubMed:27572515, ECO:0000269|PubMed:28515150, ECO:0000269|PubMed:33436632, ECO:0000269|PubMed:33918759, ECO:0000269|PubMed:34743181, ECO:0000269|PubMed:35974093, ECO:0000269|PubMed:36807739}.
uniprot
proteins
mass_dalton
42803
uniprot
proteins
mutagenesis
MUTAGEN 374; /note="K->R: Less monoubiquitinated product and resistant to degradation."; /evidence="ECO:0000269|PubMed:28515150"; MUTAGEN 391; /note="S->A: Complete loss of phosphorylation by PKC/PRKCZ and by ATM."; /evidence="ECO:0000269|PubMed:21829704, ECO:0000269|PubMed:28977635
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on its cytoplasmic domain by PKCzeta/PRKCZ upon ligand binding (PubMed:21829704). Phosphorylated by ATM following DNA damage (By similarity). {ECO:0000250|UniProtKB:Q62151, ECO:0000269|PubMed:21829704}.; PTM: Targeted by the ubiquitin E3 ligase subunit FBXO10 to mediate its ubiquitination and degradation. {ECO:0000269|PubMed:28515150}.
uniprot
proteins
pubmed
11375354
uniprot
proteins
pubmed
12495433
uniprot
proteins
pubmed
1378843
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14656967
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18089847
uniprot
proteins
pubmed
19386136
uniprot
proteins
pubmed
19906677
uniprot
proteins
pubmed
20943659
uniprot
proteins
pubmed
20947022
uniprot
proteins
pubmed
21559403
uniprot
proteins
pubmed
21565706
uniprot
proteins
pubmed
21829704
uniprot
proteins
pubmed
22509345
uniprot
proteins
pubmed
23284645
uniprot
proteins
pubmed
24081950
uniprot
proteins
pubmed
24260107
uniprot
proteins
pubmed
25401185
uniprot
proteins
pubmed
27572515
uniprot
proteins
pubmed
28515150
uniprot
proteins
pubmed
28977635
uniprot
proteins
pubmed
33436632
uniprot
proteins
pubmed
33918759
uniprot
proteins
pubmed
34743181
uniprot
proteins
pubmed
35974093
uniprot
proteins
pubmed
36807739
uniprot
proteins
pubmed
7835890
uniprot
proteins
sequence_length
404
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22509345}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, phagocytic cup {ECO:0000269|PubMed:35974093}. Early endosome {ECO:0000269|PubMed:22509345}. Nucleus {ECO:0000269|PubMed:33918759, ECO:0000269|PubMed:36807739}. Note=Detected on the surface of CD11c+ peripheral blood mononuclear cells under basal conditions and after activation (PubMed:22509345). No surface expression is observed on resting T cells (PubMed:22509345). Localizes intracellularly in early endosomes in activated T cells of healthy controls and in resting T cells of patients with type I diabetes (PubMed:22509345). Nuclear translocation is enhanced by irradiation, hypoxia and reperfusion injury to brain or kidney (By similarity). Nuclear localization is enhanced by DNA damage in trophoblasts and increases in pre-term labor and preeclampsia placentas compared to control placentas (PubMed:33918759). {ECO:0000250|UniProtKB:Q62151, ECO:0000269|PubMed:22509345, ECO:0000269|PubMed:33918759}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:24081950, ECO:0000269|PubMed:27572515, ECO:0000269|PubMed:33436632}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.; SUBCELLULAR LOCATION: [Isoform 10]: Cell membrane {ECO:0000269|PubMed:24260107}; Single-pass type I membrane protein {ECO:0000269|PubMed:24260107}.
uniprot
proteins
transmembrane_region
TRANSMEM 343..363; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins