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Q15109

- RAGE_HUMAN

UniProt

Q15109 - RAGE_HUMAN

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Protein
Advanced glycosylation end product-specific receptor
Gene
AGER, RAGE
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mediates interactions of advanced glycosylation end products (AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE/RAGE signaling plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling By similarity. Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. 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. Can also bind oligonucleotides.4 Publications

GO - Molecular functioni

  1. S100 protein binding Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. protein binding Source: UniProtKB
  4. receptor activity Source: ProtInc
  5. transmembrane signaling receptor activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. cell surface receptor signaling pathway Source: ProtInc
  2. induction of positive chemotaxis Source: Ensembl
  3. inflammatory response Source: ProtInc
  4. innate immune response Source: Reactome
  5. neuron projection development Source: UniProtKB
  6. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  7. response to wounding Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Inflammatory response

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_25195. Advanced glycosylation endproduct receptor signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Advanced glycosylation end product-specific receptor
Alternative name(s):
Receptor for advanced glycosylation end products
Gene namesi
Name:AGER
Synonyms:RAGE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:320. AGER.

Subcellular locationi

Isoform 1 : Cell membrane; Single-pass type I membrane protein 1 Publication
Isoform 2 : Secreted 1 Publication
Isoform 10 : Cell membrane; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 342320Extracellular Reviewed prediction
Add
BLAST
Transmembranei343 – 36321Helical; Reviewed prediction
Add
BLAST
Topological domaini364 – 40441Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. integral component of plasma membrane Source: ProtInc
  3. membrane Source: UniProtKB-KW
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24617.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 404382Advanced glycosylation end product-specific receptor
PRO_0000014923Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi38 ↔ 993 Publications
Glycosylationi81 – 811N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi144 ↔ 2083 Publications
Disulfide bondi259 – 259Interchain3 Publications
Disulfide bondi301 – 301Interchain3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ15109.
PRIDEiQ15109.

PTM databases

PhosphoSiteiQ15109.

Expressioni

Tissue specificityi

Endothelial cells.

Gene expression databases

ArrayExpressiQ15109.
BgeeiQ15109.
CleanExiHS_AGER.
HS_RAGE.
GenevestigatoriQ15109.

Organism-specific databases

HPAiCAB011682.

Interactioni

Subunit structurei

Interacts with S100A1 and APP By similarity. Interacts with S100B, S100A12 and S100A14. Constitutive homodimer; disulfide-linked.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1646426,EBI-1646426
GRB2P629932EBI-1646426,EBI-401755
NCK1P163332EBI-1646426,EBI-389883
RHOAP615862EBI-1646426,EBI-446668
S100BP042715EBI-1646426,EBI-458391
S100PP258152EBI-1646426,EBI-743700
TTRP027662EBI-1646426,EBI-711909

Protein-protein interaction databases

BioGridi106685. 5 interactions.
IntActiQ15109. 7 interactions.
MINTiMINT-2635420.
STRINGi9606.ENSP00000396679.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 296
Beta strandi34 – 363
Beta strandi43 – 464
Beta strandi48 – 558
Beta strandi58 – 603
Beta strandi62 – 643
Helixi71 – 744
Beta strandi76 – 783
Turni80 – 823
Beta strandi84 – 885
Helixi91 – 933
Beta strandi95 – 1028
Turni104 – 1063
Beta strandi108 – 11912
Beta strandi125 – 1284
Beta strandi131 – 1333
Beta strandi139 – 15113
Beta strandi154 – 1596
Beta strandi162 – 1643
Beta strandi171 – 1799
Turni181 – 1833
Beta strandi186 – 1949
Beta strandi206 – 2116
Beta strandi213 – 2164
Beta strandi228 – 2303
Beta strandi241 – 2444
Beta strandi247 – 2493
Beta strandi254 – 2585
Beta strandi262 – 2643
Beta strandi272 – 2776
Beta strandi284 – 2907
Turni293 – 2953
Beta strandi297 – 3004
Beta strandi309 – 3113
Beta strandi316 – 3205
Beta strandi322 – 3243
Beta strandi364 – 3663
Turni367 – 3693

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PWImodel-A1-404[»]
2BJPmodel-A1-404[»]
2E5ENMR-A23-121[»]
2ENSNMR-A235-323[»]
2L7UNMR-A23-125[»]
2LE9NMR-A/D235-327[»]
2LMBNMR-A363-376[»]
3CJJX-ray1.85A23-240[»]
3O3UX-ray1.50N23-231[»]
4LP4X-ray2.40A/B23-231[»]
4LP5X-ray3.80A/B23-323[»]
4OF5X-ray2.80A/B23-237[»]
4OFVX-ray3.10A/B23-235[»]
4OI7X-ray3.10A/B23-237[»]
4OI8X-ray3.10A/B23-237[»]
ProteinModelPortaliQ15109.
SMRiQ15109. Positions 23-321.

Miscellaneous databases

EvolutionaryTraceiQ15109.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 11694Ig-like V-type
Add
BLAST
Domaini124 – 22198Ig-like C2-type 1
Add
BLAST
Domaini227 – 31791Ig-like C2-type 2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi380 – 3845Poly-Glu

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG80687.
HOGENOMiHOG000232122.
HOVERGENiHBG004350.
InParanoidiQ15109.
PhylomeDBiQ15109.
TreeFamiTF337155.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequences (10)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 10 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15109-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAAGTAVGAW VLVLSLWGAV VGAQNITARI GEPLVLKCKG APKKPPQRLE    50
WKLNTGRTEA WKVLSPQGGG PWDSVARVLP NGSLFLPAVG IQDEGIFRCQ 100
AMNRNGKETK SNYRVRVYQI PGKPEIVDSA SELTAGVPNK VGTCVSEGSY 150
PAGTLSWHLD GKPLVPNEKG VSVKEQTRRH PETGLFTLQS ELMVTPARGG 200
DPRPTFSCSF SPGLPRHRAL RTAPIQPRVW EPVPLEEVQL VVEPEGGAVA 250
PGGTVTLTCE VPAQPSPQIH WMKDGVPLPL PPSPVLILPE IGPQDQGTYS 300
CVATHSSHGP QESRAVSISI IEPGEEGPTA GSVGGSGLGT LALALGILGG 350
LGTAALLIGV ILWQRRQRRG EERKAPENQE EEEERAELNQ SEEPEAGESS 400
TGGP 404
Length:404
Mass (Da):42,803
Last modified:November 1, 1997 - v1
Checksum:i0D584C436C30CCE7
GO
Isoform 2 (identifier: Q15109-2) [UniParc]FASTAAdd to Basket

Also known as: RAGESEC

The sequence of this isoform differs from the canonical sequence as follows:
     54-67: Missing.
     275-404: GVPLPLPPSP...EAGESSTGGP → VSDLERGAGR...ACRTESVGGT

Show »
Length:342
Mass (Da):36,193
Checksum:i35DDF66A13E39B38
GO
Isoform 3 (identifier: Q15109-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     332-404: SVGGSGLGTL...EAGESSTGGP → EGFDKVREAEDSPQHM

Show »
Length:347
Mass (Da):37,050
Checksum:i519E377C4D6AC62C
GO
Isoform 4 (identifier: Q15109-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     140-140: K → KVVEESRRSRKRPCEQE
     332-404: SVGGSGLGTL...EAGESSTGGP → EGFDKVREAEDSPQHM

Show »
Length:363
Mass (Da):39,020
Checksum:i82CC2FB0B9F209EA
GO
Isoform 5 (identifier: Q15109-5) [UniParc]FASTAAdd to Basket

Also known as: del exon3-7

The sequence of this isoform differs from the canonical sequence as follows:
     113-121: YRVRVYQIP → WWWSQKVEQ
     122-404: Missing.

Show »
Length:121
Mass (Da):13,192
Checksum:iE97FC3AF05656A12
GO
Isoform 6 (identifier: Q15109-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     140-140: K → KVVEESRRSRKRPCEQE

Show »
Length:420
Mass (Da):44,773
Checksum:i5C7E88B8E689D4E5
GO
Isoform 7 (identifier: Q15109-7) [UniParc]FASTAAdd to Basket

Also known as: del exon3

The sequence of this isoform differs from the canonical sequence as follows:
     54-67: Missing.

Show »
Length:390
Mass (Da):41,234
Checksum:i45A848CAF877F023
GO
Isoform 8 (identifier: Q15109-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     275-325: GVPLPLPPSP...VSISIIEPGE → NQARRGQLQV...TRRKRRSVQN
     326-404: Missing.

Show »
Length:325
Mass (Da):35,322
Checksum:iF69D13970D2A81B6
GO
Isoform 9 (identifier: Q15109-9) [UniParc]FASTAAdd to Basket

Also known as: del exon8-9

The sequence of this isoform differs from the canonical sequence as follows:
     276-355: VPLPLPPSPV...GILGGLGTAA → LRTREPTAVW...TRRKRRSVQN
     356-404: Missing.

Show »
Length:355
Mass (Da):38,379
Checksum:i728DA303F36B4175
GO
Isoform 10 (identifier: Q15109-10) [UniParc]FASTAAdd to Basket

Also known as: delta-ICD, variant 20

The sequence of this isoform differs from the canonical sequence as follows:
     374-404: KAPENQEEEEERAELNQSEEPEAGESSTGGP → PQKTRRKRRSVQN

Note: Detected in lung, brain, heart and kidney.

Show »
Length:386
Mass (Da):41,098
Checksum:i4D3BCF036D55A052
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821G → S.1 Publication
Corresponds to variant rs2070600 [ dbSNP | Ensembl ].
VAR_024500
Natural varianti100 – 1001Q → R.1 Publication
VAR_011338

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei54 – 6714Missing in isoform 2 and isoform 7.
VSP_002551Add
BLAST
Alternative sequencei113 – 1219YRVRVYQIP → WWWSQKVEQ in isoform 5.
VSP_047884
Alternative sequencei122 – 404283Missing in isoform 5.
VSP_047885Add
BLAST
Alternative sequencei140 – 1401K → KVVEESRRSRKRPCEQE in isoform 4 and isoform 6.
VSP_043528
Alternative sequencei275 – 404130GVPLP…STGGP → VSDLERGAGRTRRGGANCRL CGRIRAGNSSPGPGDPGRPG DSRPAHWGHLVAKAATPRRG EEGPRKPGGRGGACRTESVG GT in isoform 2.
VSP_002552Add
BLAST
Alternative sequencei275 – 32551GVPLP…IEPGE → NQARRGQLQVRGLIKSGKQK IAPNTCDWGDGQQERNGRPQ KTRRKRRSVQN in isoform 8.
VSP_047886Add
BLAST
Alternative sequencei276 – 35580VPLPL…LGTAA → LRTREPTAVWPPIPATGPRK AVLSASASSNQARRGQLQVR GLIKSGKQKIAPNTCDWGDG QQERNGRPQKTRRKRRSVQN in isoform 9.
VSP_047887Add
BLAST
Alternative sequencei326 – 40479Missing in isoform 8.
VSP_047888Add
BLAST
Alternative sequencei332 – 40473SVGGS…STGGP → EGFDKVREAEDSPQHM in isoform 3 and isoform 4.
VSP_042011Add
BLAST
Alternative sequencei356 – 40449Missing in isoform 9.
VSP_047889Add
BLAST
Alternative sequencei374 – 40431KAPEN…STGGP → PQKTRRKRRSVQN in isoform 10.
VSP_055321Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → G in AAA03574. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M91211 mRNA. Translation: AAA03574.1.
D28769 Genomic DNA. Translation: BAA05958.1.
AB036432 mRNA. Translation: BAA89369.1.
AJ133822 mRNA. Translation: CAB43108.1.
AB061668 mRNA. Translation: BAC65465.1.
U89336 Genomic DNA. Translation: AAB47491.1.
AY755619 mRNA. Translation: AAX07272.1.
AY755620 mRNA. Translation: AAX07273.1.
AY755621 mRNA. Translation: AAX07274.1.
AY755622 mRNA. Translation: AAX07275.1.
AY755623 mRNA. Translation: AAX07276.1.
AY755624 mRNA. Translation: AAX07277.1.
AY755625 mRNA. Translation: AAX07278.1.
AY755628 mRNA. Translation: AAX07281.1.
DQ104252 mRNA. Translation: AAZ32413.1.
EU117141 mRNA. Translation: ABV03807.1.
KC692917 mRNA. Translation: AHB30241.1.
AK313178 mRNA. Translation: BAG35995.1.
AL662830 Genomic DNA. Translation: CAI17535.1.
AL662830 Genomic DNA. Translation: CAI17536.1.
AL662830 Genomic DNA. Translation: CAM24893.1.
AL662884 Genomic DNA. Translation: CAI18354.1.
AL662884 Genomic DNA. Translation: CAI18355.1.
AL662884 Genomic DNA. Translation: CAM25647.1.
AL845464 Genomic DNA. Translation: CAI41809.1.
AL845464 Genomic DNA. Translation: CAI41810.1.
AL845464 Genomic DNA. Translation: CAM25716.1.
BX284686 Genomic DNA. Translation: CAM26223.1.
BX284686 Genomic DNA. Translation: CAM26225.1.
BX927239 Genomic DNA. Translation: CAQ06596.1.
BX927239 Genomic DNA. Translation: CAQ06597.1.
CR933878 Genomic DNA. Translation: CAQ09624.1.
CR812478 Genomic DNA. Translation: CAQ10699.1.
CH471081 Genomic DNA. Translation: EAX03610.1.
CH471081 Genomic DNA. Translation: EAX03611.1.
BC020669 mRNA. Translation: AAH20669.1.
AF208289 Genomic DNA. Translation: AAG35728.1.
CCDSiCCDS4746.1. [Q15109-1]
CCDS4747.1. [Q15109-2]
CCDS56417.1. [Q15109-4]
CCDS56418.1. [Q15109-3]
PIRiI61596.
RefSeqiNP_001127.1. NM_001136.4. [Q15109-1]
NP_001193858.1. NM_001206929.1. [Q15109-6]
NP_001193861.1. NM_001206932.1. [Q15109-7]
NP_001193863.1. NM_001206934.1. [Q15109-4]
NP_001193865.1. NM_001206936.1. [Q15109-9]
NP_001193869.1. NM_001206940.1. [Q15109-3]
NP_001193883.1. NM_001206954.1. [Q15109-8]
NP_001193895.1. NM_001206966.1. [Q15109-3]
NP_751947.1. NM_172197.2. [Q15109-2]
UniGeneiHs.534342.

Genome annotation databases

EnsembliENST00000375055; ENSP00000364195; ENSG00000204305. [Q15109-3]
ENST00000375065; ENSP00000364206; ENSG00000204305. [Q15109-5]
ENST00000375067; ENSP00000364208; ENSG00000204305. [Q15109-2]
ENST00000375076; ENSP00000364217; ENSG00000204305. [Q15109-1]
ENST00000383275; ENSP00000372762; ENSG00000206320. [Q15109-3]
ENST00000383279; ENSP00000372766; ENSG00000206320. [Q15109-2]
ENST00000412470; ENSP00000387853; ENSG00000229058. [Q15109-2]
ENST00000426138; ENSP00000415144; ENSG00000230514.
ENST00000427822; ENSP00000416042; ENSG00000231268.
ENST00000432831; ENSP00000413391; ENSG00000237405. [Q15109-3]
ENST00000436456; ENSP00000397227; ENSG00000234729. [Q15109-1]
ENST00000438221; ENSP00000387887; ENSG00000204305. [Q15109-4]
ENST00000441180; ENSP00000388462; ENSG00000234729. [Q15109-2]
ENST00000441804; ENSP00000391743; ENSG00000237405. [Q15109-2]
ENST00000447921; ENSP00000395812; ENSG00000237405. [Q15109-1]
ENST00000449037; ENSP00000400667; ENSG00000229058. [Q15109-3]
ENST00000451115; ENSP00000401068; ENSG00000206320. [Q15109-1]
ENST00000453588; ENSP00000399686; ENSG00000234729. [Q15109-3]
ENST00000456918; ENSP00000409457; ENSG00000229058. [Q15109-1]
ENST00000547328; ENSP00000448579; ENSG00000206320. [Q15109-5]
ENST00000547651; ENSP00000449708; ENSG00000229058. [Q15109-4]
ENST00000548464; ENSP00000450134; ENSG00000234729. [Q15109-5]
ENST00000549758; ENSP00000447301; ENSG00000229058. [Q15109-5]
ENST00000550562; ENSP00000446835; ENSG00000234729. [Q15109-4]
ENST00000551254; ENSP00000449226; ENSG00000206320. [Q15109-4]
ENST00000551381; ENSP00000448979; ENSG00000237405. [Q15109-5]
ENST00000551827; ENSP00000449042; ENSG00000237405. [Q15109-4]
GeneIDi177.
KEGGihsa:177.
UCSCiuc003oal.2. human. [Q15109-1]
uc003oan.2. human. [Q15109-2]
uc003oat.2. human. [Q15109-4]
uc003oau.2. human. [Q15109-3]

Polymorphism databases

DMDMi2497317.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M91211 mRNA. Translation: AAA03574.1 .
D28769 Genomic DNA. Translation: BAA05958.1 .
AB036432 mRNA. Translation: BAA89369.1 .
AJ133822 mRNA. Translation: CAB43108.1 .
AB061668 mRNA. Translation: BAC65465.1 .
U89336 Genomic DNA. Translation: AAB47491.1 .
AY755619 mRNA. Translation: AAX07272.1 .
AY755620 mRNA. Translation: AAX07273.1 .
AY755621 mRNA. Translation: AAX07274.1 .
AY755622 mRNA. Translation: AAX07275.1 .
AY755623 mRNA. Translation: AAX07276.1 .
AY755624 mRNA. Translation: AAX07277.1 .
AY755625 mRNA. Translation: AAX07278.1 .
AY755628 mRNA. Translation: AAX07281.1 .
DQ104252 mRNA. Translation: AAZ32413.1 .
EU117141 mRNA. Translation: ABV03807.1 .
KC692917 mRNA. Translation: AHB30241.1 .
AK313178 mRNA. Translation: BAG35995.1 .
AL662830 Genomic DNA. Translation: CAI17535.1 .
AL662830 Genomic DNA. Translation: CAI17536.1 .
AL662830 Genomic DNA. Translation: CAM24893.1 .
AL662884 Genomic DNA. Translation: CAI18354.1 .
AL662884 Genomic DNA. Translation: CAI18355.1 .
AL662884 Genomic DNA. Translation: CAM25647.1 .
AL845464 Genomic DNA. Translation: CAI41809.1 .
AL845464 Genomic DNA. Translation: CAI41810.1 .
AL845464 Genomic DNA. Translation: CAM25716.1 .
BX284686 Genomic DNA. Translation: CAM26223.1 .
BX284686 Genomic DNA. Translation: CAM26225.1 .
BX927239 Genomic DNA. Translation: CAQ06596.1 .
BX927239 Genomic DNA. Translation: CAQ06597.1 .
CR933878 Genomic DNA. Translation: CAQ09624.1 .
CR812478 Genomic DNA. Translation: CAQ10699.1 .
CH471081 Genomic DNA. Translation: EAX03610.1 .
CH471081 Genomic DNA. Translation: EAX03611.1 .
BC020669 mRNA. Translation: AAH20669.1 .
AF208289 Genomic DNA. Translation: AAG35728.1 .
CCDSi CCDS4746.1. [Q15109-1 ]
CCDS4747.1. [Q15109-2 ]
CCDS56417.1. [Q15109-4 ]
CCDS56418.1. [Q15109-3 ]
PIRi I61596.
RefSeqi NP_001127.1. NM_001136.4. [Q15109-1 ]
NP_001193858.1. NM_001206929.1. [Q15109-6 ]
NP_001193861.1. NM_001206932.1. [Q15109-7 ]
NP_001193863.1. NM_001206934.1. [Q15109-4 ]
NP_001193865.1. NM_001206936.1. [Q15109-9 ]
NP_001193869.1. NM_001206940.1. [Q15109-3 ]
NP_001193883.1. NM_001206954.1. [Q15109-8 ]
NP_001193895.1. NM_001206966.1. [Q15109-3 ]
NP_751947.1. NM_172197.2. [Q15109-2 ]
UniGenei Hs.534342.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PWI model - A 1-404 [» ]
2BJP model - A 1-404 [» ]
2E5E NMR - A 23-121 [» ]
2ENS NMR - A 235-323 [» ]
2L7U NMR - A 23-125 [» ]
2LE9 NMR - A/D 235-327 [» ]
2LMB NMR - A 363-376 [» ]
3CJJ X-ray 1.85 A 23-240 [» ]
3O3U X-ray 1.50 N 23-231 [» ]
4LP4 X-ray 2.40 A/B 23-231 [» ]
4LP5 X-ray 3.80 A/B 23-323 [» ]
4OF5 X-ray 2.80 A/B 23-237 [» ]
4OFV X-ray 3.10 A/B 23-235 [» ]
4OI7 X-ray 3.10 A/B 23-237 [» ]
4OI8 X-ray 3.10 A/B 23-237 [» ]
ProteinModelPortali Q15109.
SMRi Q15109. Positions 23-321.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106685. 5 interactions.
IntActi Q15109. 7 interactions.
MINTi MINT-2635420.
STRINGi 9606.ENSP00000396679.

Chemistry

ChEMBLi CHEMBL2176846.

PTM databases

PhosphoSitei Q15109.

Polymorphism databases

DMDMi 2497317.

Proteomic databases

PaxDbi Q15109.
PRIDEi Q15109.

Protocols and materials databases

DNASUi 177.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375055 ; ENSP00000364195 ; ENSG00000204305 . [Q15109-3 ]
ENST00000375065 ; ENSP00000364206 ; ENSG00000204305 . [Q15109-5 ]
ENST00000375067 ; ENSP00000364208 ; ENSG00000204305 . [Q15109-2 ]
ENST00000375076 ; ENSP00000364217 ; ENSG00000204305 . [Q15109-1 ]
ENST00000383275 ; ENSP00000372762 ; ENSG00000206320 . [Q15109-3 ]
ENST00000383279 ; ENSP00000372766 ; ENSG00000206320 . [Q15109-2 ]
ENST00000412470 ; ENSP00000387853 ; ENSG00000229058 . [Q15109-2 ]
ENST00000426138 ; ENSP00000415144 ; ENSG00000230514 .
ENST00000427822 ; ENSP00000416042 ; ENSG00000231268 .
ENST00000432831 ; ENSP00000413391 ; ENSG00000237405 . [Q15109-3 ]
ENST00000436456 ; ENSP00000397227 ; ENSG00000234729 . [Q15109-1 ]
ENST00000438221 ; ENSP00000387887 ; ENSG00000204305 . [Q15109-4 ]
ENST00000441180 ; ENSP00000388462 ; ENSG00000234729 . [Q15109-2 ]
ENST00000441804 ; ENSP00000391743 ; ENSG00000237405 . [Q15109-2 ]
ENST00000447921 ; ENSP00000395812 ; ENSG00000237405 . [Q15109-1 ]
ENST00000449037 ; ENSP00000400667 ; ENSG00000229058 . [Q15109-3 ]
ENST00000451115 ; ENSP00000401068 ; ENSG00000206320 . [Q15109-1 ]
ENST00000453588 ; ENSP00000399686 ; ENSG00000234729 . [Q15109-3 ]
ENST00000456918 ; ENSP00000409457 ; ENSG00000229058 . [Q15109-1 ]
ENST00000547328 ; ENSP00000448579 ; ENSG00000206320 . [Q15109-5 ]
ENST00000547651 ; ENSP00000449708 ; ENSG00000229058 . [Q15109-4 ]
ENST00000548464 ; ENSP00000450134 ; ENSG00000234729 . [Q15109-5 ]
ENST00000549758 ; ENSP00000447301 ; ENSG00000229058 . [Q15109-5 ]
ENST00000550562 ; ENSP00000446835 ; ENSG00000234729 . [Q15109-4 ]
ENST00000551254 ; ENSP00000449226 ; ENSG00000206320 . [Q15109-4 ]
ENST00000551381 ; ENSP00000448979 ; ENSG00000237405 . [Q15109-5 ]
ENST00000551827 ; ENSP00000449042 ; ENSG00000237405 . [Q15109-4 ]
GeneIDi 177.
KEGGi hsa:177.
UCSCi uc003oal.2. human. [Q15109-1 ]
uc003oan.2. human. [Q15109-2 ]
uc003oat.2. human. [Q15109-4 ]
uc003oau.2. human. [Q15109-3 ]

Organism-specific databases

CTDi 177.
GeneCardsi GC06M032148.
GC06Mi32160.
GC06Mj32097.
GC06Ml32188.
GC06Mm32225.
GC06Mn32106.
GC06Mo32155.
HGNCi HGNC:320. AGER.
HPAi CAB011682.
MIMi 600214. gene.
neXtProti NX_Q15109.
PharmGKBi PA24617.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG80687.
HOGENOMi HOG000232122.
HOVERGENi HBG004350.
InParanoidi Q15109.
PhylomeDBi Q15109.
TreeFami TF337155.

Enzyme and pathway databases

Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_25195. Advanced glycosylation endproduct receptor signaling.

Miscellaneous databases

ChiTaRSi AGER. human.
EvolutionaryTracei Q15109.
GeneWikii RAGE_(receptor).
GenomeRNAii 177.
NextBioi 716.
PROi Q15109.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15109.
Bgeei Q15109.
CleanExi HS_AGER.
HS_RAGE.
Genevestigatori Q15109.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
InterProi IPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view ]
Pfami PF08205. C2-set_2. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins."
    Neeper M., Schmidt A.M., Brett J., Yan S.D., Wang F., Pan Y.C., Elliston K., Stern D., Shaw A.
    J. Biol. Chem. 267:14998-15004(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lung.
  2. "Three genes in the human MHC class III region near the junction with the class II: gene for receptor of advanced glycosylation end products, PBX2 homeobox gene and a notch homolog, human counterpart of mouse mammary tumor gene int-3."
    Sugaya K., Fukagawa T., Matsumoto K., Mita K., Takahashi E., Ando A., Inoko H., Ikemura T.
    Genomics 23:408-419(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  3. "Molecular heterogeneity of the receptor for advanced glycation endproducts."
    Abedin M.J., Yonekura H., Migita H., Karasawa J., Yamamoto Y., Yamamoto H.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-100.
  4. "cDNA cloning of a novel secreted isoform of the human receptor for advanced glycation end products (RAGE) and characterization of cells co-expressing cell-surface scavenger receptors and Swedish mutant amyloid precursor protein."
    Malherbe P., Richards J., Gaillard H., Thompson A., Diener C., Schuler A., Huber G.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  5. "Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury."
    Yonekura H., Yamamoto Y., Sakurai S., Petrova R.G., Abedin J., Li H., Yasui K., Takeuchi M., Makita Z., Takasawa S., Okamoto H., Watanabe T., Yamamoto H.
    Biochem. J. 370:1097-1109(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING.
    Tissue: Skin.
  6. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
    Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
    Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Identification, classification, and expression of RAGE gene splice variants."
    Hudson B.I., Carter A.M., Harja E., Kalea A.Z., Arriero M., Yang H., Grant P.J., Schmidt A.M.
    FASEB J. 22:1572-1580(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6; 7; 8 AND 9), ALTERNATIVE SPLICING.
    Tissue: Aortic smooth muscle and Lung.
  8. "Alternative splicing of the RAGE cytoplasmic domain regulates cell signaling and function."
    Jules J., Maiguel D., Hudson B.I.
    PLoS ONE 8:E78267-E78267(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), SUBCELLULAR LOCATION (ISOFORM 10).
    Tissue: Lung.
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  10. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-82.
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  13. "Effects of novel polymorphisms in the RAGE gene on transcriptional regulation and their association with diabetic retinopathy."
    Hudson B.I., Stickland M.H., Futers T.S., Grant P.J.
    Diabetes 50:1505-1511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
  14. Cited for: INTERACTION WITH S100A12.
  15. "RAGE-dependent signaling in microglia contributes to neuroinflammation, Abeta accumulation, and impaired learning/memory in a mouse model of Alzheimer's disease."
    Fang F., Lue L.-F., Yan S., Xu H., Luddy J.S., Chen D., Walker D.G., Stern D.M., Yan S., Schmidt A.M., Chen J.X., Yan S.S.
    FASEB J. 24:1043-1055(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "S100A14 stimulates cell proliferation and induces cell apoptosis at different concentrations via receptor for advanced glycation end products (RAGE)."
    Jin Q., Chen H., Luo A., Ding F., Liu Z.
    PLoS ONE 6:E19375-E19375(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH S100A14, FUNCTION.
  17. "Disulfide bonds within the C2 domain of RAGE play key roles in its dimerization and biogenesis."
    Wei W., Lampe L., Park S., Vangara B.S., Waldo G.S., Cabantous S., Subaran S.S., Yang D., Lakatta E.G., Lin L.
    PLoS ONE 7:E50736-E50736(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERCHAIN DISULFIDE BONDS.
  18. "Solution structure of the third Ig-like domain from human advanced glycosylation end product-specific receptor."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 235-323.
  19. "The 1.5 A crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding."
    Park H., Adsit F.G., Boyington J.C.
    J. Biol. Chem. 285:40762-40770(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 23-231, FUNCTION, DNA-BINDING, INTERACTION WITH S100B.
  20. "Structural basis for ligand recognition and activation of RAGE."
    Koch M., Chitayat S., Dattilo B.M., Schiefner A., Diez J., Chazin W.J., Fritz G.
    Structure 18:1342-1352(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 23-240, INTERACTION WITH S100B, DISULFIDE BONDS.
  21. Cited for: STRUCTURE BY NMR OF 23-125, FUNCTION, DISULFIDE BONDS.

Entry informationi

Entry nameiRAGE_HUMAN
AccessioniPrimary (citable) accession number: Q15109
Secondary accession number(s): A2BFI7
, A6NKF0, A7Y2U9, B0V176, Q15279, Q3L1R4, Q3L1R5, Q3L1R6, Q3L1R7, Q3L1R8, Q3L1S0, Q86SN1, Q9H2X7, Q9Y3R3, V5R6A3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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