Q15109 (RAGE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Advanced glycosylation end product-specific receptor

Alternative name(s):
Receptor for advanced glycosylation end products

Gene names

Name:	AGER
Synonyms:	RAGE

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.13 Ref.14 Ref.16 Ref.18
Subunit structure	Interacts with S100A1 and APP By similarity. Interacts with S100B, S100A12 and S100A14. Ref.12 Ref.14 Ref.16 Ref.17
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 process	Inflammatory response
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell surface receptor signaling pathway Traceable author statement PubMed 10835680. Source: ProtInc induction of positive chemotaxis Inferred from electronic annotation. Source: Compara 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
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	transmembrane signaling receptor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	2	EBI-1646426,EBI-401755
NCK1	P16333	2	EBI-1646426,EBI-389883
S100P	P25815	2	EBI-1646426,EBI-743700

Alternative products

This entry describes 4 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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Chain

23 – 404

382

Advanced glycosylation end product-specific receptor

PRO_0000014923

Regions

Topological domain

23 – 342

320

Extracellular Potential

Transmembrane

343 – 363

21

Helical; Potential

Topological domain

364 – 404

41

Cytoplasmic Potential

Domain

23 – 116

94

Ig-like V-type

Domain

124 – 221

98

Ig-like C2-type 1

Domain

227 – 317

91

Ig-like C2-type 2

Compositional bias

380 – 384

5

Poly-Glu

Amino acid modifications

Glycosylation

25

1

N-linked (GlcNAc...) Potential

Glycosylation

81

1

N-linked (GlcNAc...) Potential

Disulfide bond

38 ↔ 99

Ref.17 Ref.18

Disulfide bond

144 ↔ 208

Ref.17 Ref.18

Disulfide bond

259 ↔ 301

Potential

Natural variations

Alternative sequence

54 – 67

14

Missing in isoform 2.

VSP_002551

Alternative sequence

140

1

K → KVVEESRRSRKRPCEQE in isoform 4.

VSP_043528

Alternative sequence

275 – 404

130

GVPLP…STGGP → VSDLERGAGRTRRGGANCRL CGRIRAGNSSPGPGDPGRPG DSRPAHWGHLVAKAATPRRG EEGPRKPGGRGGACRTESVG GT in isoform 2.

VSP_002552

Alternative sequence

332 – 404

73

SVGGS…STGGP → EGFDKVREAEDSPQHM in isoform 3 and isoform 4.

VSP_042011

Natural variant

82

1

G → S. Ref.8
Corresponds to variant rs2070600 [ dbSNP | Ensembl ].

VAR_024500

Natural variant

100

1

Q → R. Ref.3

VAR_011338

Experimental info

Sequence conflict

1

1

M → G in AAA03574. Ref.1

Secondary structure

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404

Helix Strand Turn

Details...

Beta strand

24 – 29

6

Beta strand

34 – 36

3

Beta strand

43 – 46

4

Beta strand

48 – 55

8

Beta strand

58 – 60

3

Beta strand

62 – 64

3

Helix

71 – 74

4

Beta strand

76 – 78

3

Turn

80 – 82

3

Beta strand

84 – 88

5

Helix

91 – 93

3

Beta strand

95 – 102

8

Beta strand

108 – 119

12

Beta strand

125 – 128

4

Beta strand

131 – 133

3

Beta strand

139 – 151

13

Beta strand

154 – 159

6

Beta strand

171 – 179

9

Turn

181 – 183

3

Beta strand

186 – 194

9

Beta strand

206 – 211

6

Beta strand

213 – 216

4

Beta strand

228 – 230

3

Beta strand

241 – 244

4

Beta strand

247 – 249

3

Beta strand

254 – 258

5

Beta strand

262 – 264

3

Beta strand

272 – 277

6

Beta strand

284 – 290

7

Turn

293 – 295

3

Beta strand

297 – 300

4

Beta strand

309 – 311

3

Beta strand

316 – 320

5

Beta strand

322 – 324

3

Beta strand

364 – 366

3

Turn

367 – 369

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 0D584C436C30CCE7	FASTA	404	42,803
	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
	Isoform 2 (RAGESEC) [UniParc]. Checksum: 35DDF66A13E39B38	FASTA	342	36,193
	10 20 30 40 50 60 MAAGTAVGAW VLVLSLWGAV VGAQNITARI GEPLVLKCKG APKKPPQRLE WKLGGGPWDS 70 80 90 100 110 120 VARVLPNGSL FLPAVGIQDE GIFRCQAMNR NGKETKSNYR VRVYQIPGKP EIVDSASELT 130 140 150 160 170 180 AGVPNKVGTC VSEGSYPAGT LSWHLDGKPL VPNEKGVSVK EQTRRHPETG LFTLQSELMV 190 200 210 220 230 240 TPARGGDPRP TFSCSFSPGL PRHRALRTAP IQPRVWEPVP LEEVQLVVEP EGGAVAPGGT 250 260 270 280 290 300 VTLTCEVPAQ PSPQIHWMKD VSDLERGAGR TRRGGANCRL CGRIRAGNSS PGPGDPGRPG 310 320 330 340 DSRPAHWGHL VAKAATPRRG EEGPRKPGGR GGACRTESVG GT
	Isoform 3 [UniParc]. Checksum: 519E377C4D6AC62C	FASTA	347	37,050
	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 CVATHSSHGP QESRAVSISI IEPGEEGPTA GEGFDKVREA EDSPQHM
	Isoform 4 [UniParc]. Checksum: 82CC2FB0B9F209EA	FASTA	363	39,020
	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 VVEESRRSRK RPCEQEVGTC VSEGSYPAGT LSWHLDGKPL 190 200 210 220 230 240 VPNEKGVSVK EQTRRHPETG LFTLQSELMV TPARGGDPRP TFSCSFSPGL PRHRALRTAP 250 260 270 280 290 300 IQPRVWEPVP LEEVQLVVEP EGGAVAPGGT VTLTCEVPAQ PSPQIHWMKD GVPLPLPPSP 310 320 330 340 350 360 VLILPEIGPQ DQGTYSCVAT HSSHGPQESR AVSISIIEPG EEGPTAGEGF DKVREAEDSP QHM

References

	« Hide 'large scale' referencesShow '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 3 AND 4), ALTERNATIVE SPLICING. Tissue: Lung.
[8]	"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.
[9]	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. , 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].
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
AY755620 mRNA. Translation: AAX07273.1.
AY755622 mRNA. Translation: AAX07275.1.
AY755628 mRNA. Translation: AAX07281.1.
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.
BC020669 mRNA. Translation: AAH20669.1.
AF208289 Genomic DNA. Translation: AAG35728.1.

IPI

IPI00014810.
IPI00220335.
IPI00431197.

PIR

I61596.

RefSeq

NP_001127.1. NM_001136.4.
NP_001193863.1. NM_001206934.1.
NP_001193869.1. NM_001206940.1.
NP_001193895.1. NM_001206966.1.
NP_751947.1. NM_172197.2.

UniGene

Hs.534342.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3S58	X-ray	3.10	A/B	23-237	[»]
3S59	X-ray	2.80	A/B	23-237	[»]

ProteinModelPortal

Q15109.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15109. 5 interactions.

MINT

MINT-2635420.

STRING

9606.ENSP00000396679.

PTM databases

PhosphoSite

Q15109.

Polymorphism databases

DMDM

2497317.

Proteomic databases

PaxDb

Q15109.

PRIDE

Q15109.

Protocols and materials databases

DNASU

177.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375055; ENSP00000364195; ENSG00000204305.
ENST00000375067; ENSP00000364208; ENSG00000204305.
ENST00000375076; ENSP00000364217; ENSG00000204305.
ENST00000383275; ENSP00000372762; ENSG00000206320.
ENST00000383279; ENSP00000372766; ENSG00000206320.
ENST00000412470; ENSP00000387853; ENSG00000229058.
ENST00000426138; ENSP00000415144; ENSG00000230514.
ENST00000427822; ENSP00000416042; ENSG00000231268.
ENST00000432831; ENSP00000413391; ENSG00000237405.
ENST00000436456; ENSP00000397227; ENSG00000234729.
ENST00000438221; ENSP00000387887; ENSG00000204305.
ENST00000441180; ENSP00000388462; ENSG00000234729.
ENST00000441804; ENSP00000391743; ENSG00000237405.
ENST00000447921; ENSP00000395812; ENSG00000237405.
ENST00000449037; ENSP00000400667; ENSG00000229058.
ENST00000451115; ENSP00000401068; ENSG00000206320.
ENST00000453588; ENSP00000399686; ENSG00000234729.
ENST00000456918; ENSP00000409457; ENSG00000229058.
ENST00000547651; ENSP00000449708; ENSG00000229058.
ENST00000550562; ENSP00000446835; ENSG00000234729.
ENST00000551254; ENSP00000449226; ENSG00000206320.
ENST00000551827; ENSP00000449042; ENSG00000237405.

GeneID

177.

KEGG

hsa:177.

UCSC

uc003oal.2. human.
uc003oan.2. human.

Organism-specific databases

CTD

177.

GeneCards

GC06M032148.

HGNC

HGNC:320. AGER.

HPA

CAB011682.

MIM

600214. gene.

neXtProt

NX_Q15109.

PharmGKB

PA24617.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG80687.

HOGENOM

HOG000232122.

HOVERGEN

HBG004350.

InParanoid

Q15109.

OrthoDB

EOG451DR2.

PhylomeDB

Q15109.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q15109.

Bgee

Q15109.

CleanEx

HS_AGER.
HS_RAGE.

Genevestigator

Q15109.

GermOnline

ENSG00000204305. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

IPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]

Pfam

PF08205. C2-set_2. 1 hit.
[Graphical view]

SMART

SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

AGER. human.

EvolutionaryTrace

Q15109.

GenomeRNAi

177.

NextBio

716.

SOURCE

Search...

Entry information

Entry name

RAGE_HUMAN

Accession

Primary (citable) accession number: Q15109
Secondary accession number(s): A2BFI7 , A6NKF0, B0V176, Q15279, Q3L1R7, Q86SN1, Q9H2X7, Q9Y3R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.