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Q15109 (RAGE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Advanced glycosylation end product-specific receptor
Alternative name(s):
Receptor for advanced glycosylation end products
Gene names
Name:AGER
Synonyms:RAGE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.14 Ref.15 Ref.18 Ref.20

Subunit structure

Interacts with S100A1 and APP By similarity. Interacts with S100B, S100A12 and S100A14. Constitutive homodimer; disulfide-linked. Ref.13 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein.

Isoform 2: Secreted.

Tissue specificity

Endothelial cells.

Sequence similarities

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Biological processInflammatory response
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell surface receptor signaling pathway

Traceable author statement PubMed 10835680. Source: ProtInc

induction of positive chemotaxis

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement PubMed 10399917. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

neuron projection development

Inferred from genetic interaction PubMed 10391939. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 10391939. Source: UniProtKB

response to wounding

Traceable author statement PubMed 10399917. Source: ProtInc

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionS100 protein binding

Inferred from physical interaction PubMed 15033494. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 24119142. Source: IntAct

receptor activity

Traceable author statement PubMed 8751438. Source: ProtInc

transmembrane signaling receptor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15109-1)

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.
Isoform 2 (identifier: Q15109-2)

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
Isoform 3 (identifier: Q15109-3)

The sequence of this isoform differs from the canonical sequence as follows:
     332-404: SVGGSGLGTL...EAGESSTGGP → EGFDKVREAEDSPQHM
Isoform 4 (identifier: Q15109-4)

The sequence of this isoform differs from the canonical sequence as follows:
     140-140: K → KVVEESRRSRKRPCEQE
     332-404: SVGGSGLGTL...EAGESSTGGP → EGFDKVREAEDSPQHM
Isoform 5 (identifier: Q15109-5)

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.
Isoform 6 (identifier: Q15109-6)

The sequence of this isoform differs from the canonical sequence as follows:
     140-140: K → KVVEESRRSRKRPCEQE
Isoform 7 (identifier: Q15109-7)

Also known as: del exon3;

The sequence of this isoform differs from the canonical sequence as follows:
     54-67: Missing.
Isoform 8 (identifier: Q15109-8)

The sequence of this isoform differs from the canonical sequence as follows:
     275-325: GVPLPLPPSP...VSISIIEPGE → NQARRGQLQV...TRRKRRSVQN
     326-404: Missing.
Isoform 9 (identifier: Q15109-9)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 404382Advanced glycosylation end product-specific receptor
PRO_0000014923

Regions

Topological domain23 – 342320Extracellular Potential
Transmembrane343 – 36321Helical; Potential
Topological domain364 – 40441Cytoplasmic Potential
Domain23 – 11694Ig-like V-type
Domain124 – 22198Ig-like C2-type 1
Domain227 – 31791Ig-like C2-type 2
Compositional bias380 – 3845Poly-Glu

Amino acid modifications

Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Disulfide bond38 ↔ 99 Ref.16 Ref.19 Ref.20
Disulfide bond144 ↔ 208 Ref.16 Ref.19 Ref.20
Disulfide bond259Interchain Ref.16 Ref.19 Ref.20
Disulfide bond301Interchain Ref.16 Ref.19 Ref.20

Natural variations

Alternative sequence54 – 6714Missing in isoform 2 and isoform 7.
VSP_002551
Alternative sequence113 – 1219YRVRVYQIP → WWWSQKVEQ in isoform 5.
VSP_047884
Alternative sequence122 – 404283Missing in isoform 5.
VSP_047885
Alternative sequence1401K → KVVEESRRSRKRPCEQE in isoform 4 and isoform 6.
VSP_043528
Alternative sequence275 – 404130GVPLP…STGGP → VSDLERGAGRTRRGGANCRL CGRIRAGNSSPGPGDPGRPG DSRPAHWGHLVAKAATPRRG EEGPRKPGGRGGACRTESVG GT in isoform 2.
VSP_002552
Alternative sequence275 – 32551GVPLP…IEPGE → NQARRGQLQVRGLIKSGKQK IAPNTCDWGDGQQERNGRPQ KTRRKRRSVQN in isoform 8.
VSP_047886
Alternative sequence276 – 35580VPLPL…LGTAA → LRTREPTAVWPPIPATGPRK AVLSASASSNQARRGQLQVR GLIKSGKQKIAPNTCDWGDG QQERNGRPQKTRRKRRSVQN in isoform 9.
VSP_047887
Alternative sequence326 – 40479Missing in isoform 8.
VSP_047888
Alternative sequence332 – 40473SVGGS…STGGP → EGFDKVREAEDSPQHM in isoform 3 and isoform 4.
VSP_042011
Alternative sequence356 – 40449Missing in isoform 9.
VSP_047889
Natural variant821G → S. Ref.9
Corresponds to variant rs2070600 [ dbSNP | Ensembl ].
VAR_024500
Natural variant1001Q → R. Ref.3
VAR_011338

Experimental info

Sequence conflict11M → G in AAA03574. Ref.1

Secondary structure

.......................................................................... 404
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 0D584C436C30CCE7

FASTA40442,803
        10         20         30         40         50         60 
MAAGTAVGAW VLVLSLWGAV VGAQNITARI GEPLVLKCKG APKKPPQRLE WKLNTGRTEA 

        70         80         90        100        110        120 
WKVLSPQGGG PWDSVARVLP NGSLFLPAVG IQDEGIFRCQ AMNRNGKETK SNYRVRVYQI 

       130        140        150        160        170        180 
PGKPEIVDSA SELTAGVPNK VGTCVSEGSY PAGTLSWHLD GKPLVPNEKG VSVKEQTRRH 

       190        200        210        220        230        240 
PETGLFTLQS ELMVTPARGG DPRPTFSCSF SPGLPRHRAL RTAPIQPRVW EPVPLEEVQL 

       250        260        270        280        290        300 
VVEPEGGAVA PGGTVTLTCE VPAQPSPQIH WMKDGVPLPL PPSPVLILPE IGPQDQGTYS 

       310        320        330        340        350        360 
CVATHSSHGP QESRAVSISI IEPGEEGPTA GSVGGSGLGT LALALGILGG LGTAALLIGV 

       370        380        390        400 
ILWQRRQRRG EERKAPENQE EEEERAELNQ SEEPEAGESS TGGP 

« Hide

Isoform 2 (RAGESEC) [UniParc].

Checksum: 35DDF66A13E39B38
Show »

FASTA34236,193
Isoform 3 [UniParc].

Checksum: 519E377C4D6AC62C
Show »

FASTA34737,050
Isoform 4 [UniParc].

Checksum: 82CC2FB0B9F209EA
Show »

FASTA36339,020
Isoform 5 (del exon3-7) [UniParc].

Checksum: E97FC3AF05656A12
Show »

FASTA12113,192
Isoform 6 [UniParc].

Checksum: 5C7E88B8E689D4E5
Show »

FASTA42044,773
Isoform 7 (del exon3) [UniParc].

Checksum: 45A848CAF877F023
Show »

FASTA39041,234
Isoform 8 [UniParc].

Checksum: F69D13970D2A81B6
Show »

FASTA32535,322
Isoform 9 (del exon8-9) [UniParc].

Checksum: 728DA303F36B4175
Show »

FASTA35538,379

References

« Hide 'large scale' references
[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]"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. expand/collapse author list , 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.
[9]"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. expand/collapse author list , 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.
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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.
[12]"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.
[13]"Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization and function."
Moroz O.V., Burkitt W., Wittkowski H., He W., Ianoul A., Novitskaya V., Xie J., Polyakova O., Lednev I.K., Shekhtman A., Derrick P.J., Bjoerk P., Foell D., Bronstein I.B.
BMC Biochem. 10:11-11(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH S100A12.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"Advanced glycation end product recognition by the receptor for AGEs."
Xue J., Rai V., Singer D., Chabierski S., Xie J., Reverdatto S., Burz D.S., Schmidt A.M., Hoffmann R., Shekhtman A.
Structure 19:722-732(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 23-125, FUNCTION, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
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.
PIRI61596.
RefSeqNP_001127.1. NM_001136.4.
NP_001193858.1. NM_001206929.1.
NP_001193861.1. NM_001206932.1.
NP_001193863.1. NM_001206934.1.
NP_001193865.1. NM_001206936.1.
NP_001193869.1. NM_001206940.1.
NP_001193883.1. NM_001206954.1.
NP_001193895.1. NM_001206966.1.
NP_751947.1. NM_172197.2.
UniGeneHs.534342.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
3S58X-ray3.10A/B23-237[»]
3S59X-ray2.80A/B23-237[»]
4LP4X-ray2.40A/B23-231[»]
4LP5X-ray3.80A/B23-323[»]
ProteinModelPortalQ15109.
SMRQ15109. Positions 23-321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106685. 5 interactions.
IntActQ15109. 7 interactions.
MINTMINT-2635420.
STRING9606.ENSP00000396679.

Chemistry

ChEMBLCHEMBL2176846.

PTM databases

PhosphoSiteQ15109.

Polymorphism databases

DMDM2497317.

Proteomic databases

PaxDbQ15109.
PRIDEQ15109.

Protocols and materials databases

DNASU177.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375055; 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]
GeneID177.
KEGGhsa:177.
UCSCuc003oal.2. human. [Q15109-1]
uc003oan.2. human. [Q15109-2]
uc003oat.2. human. [Q15109-4]
uc003oau.2. human. [Q15109-3]

Organism-specific databases

CTD177.
GeneCardsGC06M032148.
GC06Mi32160.
GC06Mj32097.
GC06Ml32188.
GC06Mm32225.
GC06Mn32106.
GC06Mo32155.
HGNCHGNC:320. AGER.
HPACAB011682.
MIM600214. gene.
neXtProtNX_Q15109.
PharmGKBPA24617.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80687.
HOGENOMHOG000232122.
HOVERGENHBG004350.
InParanoidQ15109.
PhylomeDBQ15109.
TreeFamTF337155.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ15109.
BgeeQ15109.
CleanExHS_AGER.
HS_RAGE.
GenevestigatorQ15109.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamPF08205. C2-set_2. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAGER. human.
EvolutionaryTraceQ15109.
GeneWikiRAGE_(receptor).
GenomeRNAi177.
NextBio716.
PROQ15109.
SOURCESearch...

Entry information

Entry nameRAGE_HUMAN
AccessionPrimary (citable) accession number: Q15109
Secondary accession number(s): A2BFI7 expand/collapse secondary AC list , A6NKF0, A7Y2U9, B0V176, Q15279, Q3L1R4, Q3L1R5, Q3L1R6, Q3L1R7, Q3L1R8, Q3L1S0, Q86SN1, Q9H2X7, Q9Y3R3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM