ASpdb: an integrative knowledgebase of human protein isoforms from experimental and AI-predicted structures

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	Protein Summary
	AS Summary
	Protein Functional Features
	Gene Isoform Structures and Expression Levels
	Protein Structures
	pLDDT Score Distribution
	Ramachandran Plot of Protein Structures
	Potential Active Site Information
	Protein Structure and Feature Comparision
	Protein-Protein Interaction
	Related Drugs
	Related Diseases
	Clinically Important Variants

Protein:AGER

Protein Summary

Gene summary

Gene name: AGER
ASpdb.0 ID: 177
	Gene
Gene symbol	AGER
Gene ID	177
Gene name	advanced glycosylation end-product specific receptor
Synonyms	RAGE\|SCARJ1\|sRAGE
Cytomap	6p21.32
Type of gene	protein-coding
Description	advanced glycosylation end product-specific receptorreceptor for advanced glycation end-products
Modification date	20240411
UniProtAcc	Q15109

Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez

Partner	Gene	GO ID	GO term	PubMed ID
Gene	AGER	GO:0001540	amyloid-beta binding	29518356
Gene	AGER	GO:0001650	fibrillar center	-
Gene	AGER	GO:0001914	regulation of T cell mediated cytotoxicity	22473704
Gene	AGER	GO:0005886	plasma membrane	-
Gene	AGER	GO:0010255	glucose mediated signaling pathway	25689357
Gene	AGER	GO:0016324	apical plasma membrane	26005850
Gene	AGER	GO:0030054	cell junction	-
Gene	AGER	GO:0032693	negative regulation of interleukin-10 production	22473704
Gene	AGER	GO:0051092	positive regulation of NF-kappaB transcription factor activity	10391939
Gene	AGER	GO:0150104	transport across blood-brain barrier	23973487
Gene	AGER	GO:2000514	regulation of CD4-positive, alpha-beta T cell activation	22473704

AS Summary

Information of the canonical protein with experimentally identified structure from PDB (2023).

UniProt Acc	File name	PDB ID	Method	Resolution	Chain	Start	End
Q15109-1	Q15109-1_4ybh_A.pdb	4YBH	X-ray	2.4	A	23	322

ASpdb's canonical and alternatively spliced isoform information.

accession_id	gene_name	canonical_id	alternative_id	canonical_length	alternative_length	canonical_start	canonical_end	type	originalSEQ	variationSEQ	alternative_start	alternative_end
Q15109	AGER	Q15109-1	Q15109-10	404	386	374	404	Substitution	KAPENQEEEEERAELNQSEEPEAGESSTGGP	PQKTRRKRRSVQN	374	386
Q15109	AGER	Q15109-1	Q15109-2	404	342	54	67	Deletion	none	none	53	53
Q15109	AGER	Q15109-1	Q15109-2	404	342	275	404	Substitution	GVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP	VSDLERGAGRTRRGGANCRLCGRIRAGNSSPGPGDPGRPGDSRPAHWGHLVAKAATPRRGEEGPRKPGGRGGACRTESVGGT	261	342
Q15109	AGER	Q15109-1	Q15109-3	404	347	332	404	Substitution	SVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP	EGFDKVREAEDSPQHM	332	347
Q15109	AGER	Q15109-1	Q15109-4	404	363	140	140	Substitution	K	KVVEESRRSRKRPCEQE	140	156
Q15109	AGER	Q15109-1	Q15109-4	404	363	332	404	Substitution	SVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP	EGFDKVREAEDSPQHM	348	363
Q15109	AGER	Q15109-1	Q15109-5	404	121	113	121	Substitution	YRVRVYQIP	WWWSQKVEQ	113	121
Q15109	AGER	Q15109-1	Q15109-5	404	121	122	404	Deletion	none	none	121	121
Q15109	AGER	Q15109-1	Q15109-6	404	420	140	140	Substitution	K	KVVEESRRSRKRPCEQE	140	156
Q15109	AGER	Q15109-1	Q15109-7	404	390	54	67	Deletion	none	none	53	53
Q15109	AGER	Q15109-1	Q15109-8	404	325	275	325	Substitution	GVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGE	NQARRGQLQVRGLIKSGKQKIAPNTCDWGDGQQERNGRPQKTRRKRRSVQN	275	325
Q15109	AGER	Q15109-1	Q15109-8	404	325	326	404	Deletion	none	none	325	325
Q15109	AGER	Q15109-1	Q15109-9	404	355	276	355	Substitution	VPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAA	LRTREPTAVWPPIPATGPRKAVLSASASSNQARRGQLQVRGLIKSGKQKIAPNTCDWGDGQQERNGRPQKTRRKRRSVQN	276	355
Q15109	AGER	Q15109-1	Q15109-9	404	355	356	404	Deletion	none	none	355	355

Multiple sequence alignment of our canonical and alternatively spliced AGER

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of AGER

UniProt-id	ENSG	ENST	ENSP
Q15109-1	ENSG00000204305.16	ENST00000375076.9	ENSP00000364217.4
Q15109-1	ENSG00000234729.9	ENST00000436456.6	ENSP00000397227.2
Q15109-1	ENSG00000237405.10	ENST00000447921.6	ENSP00000395812.2
Q15109-1	ENSG00000206320.12	ENST00000451115.6	ENSP00000401068.2
Q15109-1	ENSG00000229058.10	ENST00000456918.6	ENSP00000409457.2
Q15109-2	ENSG00000204305.16	ENST00000375067.7	ENSP00000364208.3
Q15109-2	ENSG00000206320.12	ENST00000383279.8	ENSP00000372766.4
Q15109-2	ENSG00000229058.10	ENST00000412470.6	ENSP00000387853.2
Q15109-2	ENSG00000234729.9	ENST00000441180.6	ENSP00000388462.2
Q15109-2	ENSG00000237405.10	ENST00000441804.6	ENSP00000391743.2
Q15109-3	ENSG00000204305.16	ENST00000375055.6	ENSP00000364195.2
Q15109-3	ENSG00000206320.12	ENST00000383275.6	ENSP00000372762.2
Q15109-3	ENSG00000237405.10	ENST00000432831.5	ENSP00000413391.1
Q15109-3	ENSG00000229058.10	ENST00000449037.5	ENSP00000400667.1
Q15109-3	ENSG00000234729.9	ENST00000453588.5	ENSP00000399686.1
Q15109-4	ENSG00000204305.16	ENST00000438221.6	ENSP00000387887.2
Q15109-4	ENSG00000229058.10	ENST00000547651.2	ENSP00000449708.1
Q15109-4	ENSG00000234729.9	ENST00000550562.5	ENSP00000446835.1
Q15109-4	ENSG00000206320.12	ENST00000551254.5	ENSP00000449226.1
Q15109-4	ENSG00000237405.10	ENST00000551827.4	ENSP00000449042.1
Q15109-6	ENSG00000204305.16	ENST00000375069.7	ENSP00000364210.4
Q15109-6	ENSG00000206320.12	ENST00000547328.5	ENSP00000448579.2
Q15109-6	ENSG00000234729.9	ENST00000548464.3	ENSP00000450134.2
Q15109-6	ENSG00000229058.10	ENST00000549758.5	ENSP00000447301.2
Q15109-6	ENSG00000237405.10	ENST00000551381.5	ENSP00000448979.2

UniProt-id	NM ID	NP ID
Q15109-1	NM_001136.4	NP_001127.1
Q15109-2	NM_172197.2	NP_751947.1
Q15109-3	NM_001206940.1	NP_001193869.1
Q15109-3	NM_001206966.1	NP_001193895.1
Q15109-4	NM_001206934.1	NP_001193863.1
Q15109-6	NM_001206929.1	NP_001193858.1
Q15109-7	NM_001206932.1	NP_001193861.1
Q15109-8	NM_001206954.1	NP_001193883.1
Q15109-9	NM_001206936.1	NP_001193865.1

Amino acid sequences of our canonical and alternatively spliced AGER

accession_id	Protein sequence
Q15109-1	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVG IQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRH PETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIH WMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGV
Q15109-10	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVG IQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRH PETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIH WMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGV
Q15109-2	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNR NGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMV TPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDVSDLERGAGR
Q15109-3	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVG IQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRH PETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIH
Q15109-4	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVG IQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVVEESRRSRKRPCEQEVGTCVSEGSYPAGTLSWHLDGKPL VPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGT VTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGEGFDKVREAEDSP
Q15109-5	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVG
Q15109-6	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVG IQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVVEESRRSRKRPCEQEVGTCVSEGSYPAGTLSWHLDGKPL VPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGT VTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALA
Q15109-7	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNR NGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMV TPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSP VLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERK
Q15109-8	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVG IQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRH PETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIH
Q15109-9	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVG IQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRH PETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIH

Protein Functional Features

Main function of this protein. (from UniProt)

AGER (go to UniProt):Q15109

Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at
download page
* Minus value of BPloci means that the break pointn is located before the CDS.

- Retained protein feature among the 13 regional features.

Accession_id	Subsection	Start	End	Funcitonal feature	Splicing information
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=54;End=67
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=275;End=404
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=332;End=404
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=140;End=140
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=332;End=404
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=113;End=121
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=122;End=404
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=140;End=140
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=54;End=67
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=275;End=325
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=326;End=404
Q15109	Topological domain	23	342	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=276;End=355
Q15109	Transmembrane	343	363	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=275;End=404
Q15109	Transmembrane	343	363	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=332;End=404
Q15109	Transmembrane	343	363	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=332;End=404
Q15109	Transmembrane	343	363	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=122;End=404
Q15109	Transmembrane	343	363	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=326;End=404
Q15109	Transmembrane	343	363	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=276;End=355
Q15109	Transmembrane	343	363	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=356;End=404
Q15109	Topological domain	364	404	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=374;End=404
Q15109	Topological domain	364	404	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=275;End=404
Q15109	Topological domain	364	404	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=332;End=404
Q15109	Topological domain	364	404	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Substitution;Start=332;End=404
Q15109	Topological domain	364	404	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=122;End=404
Q15109	Topological domain	364	404	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=326;End=404
Q15109	Topological domain	364	404	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	Type=Deletion;Start=356;End=404
Q15109	Domain	23	116	Note=Ig-like V-type	Type=Deletion;Start=54;End=67
Q15109	Domain	23	116	Note=Ig-like V-type	Type=Substitution;Start=113;End=121
Q15109	Domain	23	116	Note=Ig-like V-type	Type=Deletion;Start=54;End=67
Q15109	Domain	124	221	Note=Ig-like C2-type 1	Type=Substitution;Start=140;End=140
Q15109	Domain	124	221	Note=Ig-like C2-type 1	Type=Deletion;Start=122;End=404
Q15109	Domain	124	221	Note=Ig-like C2-type 1	Type=Substitution;Start=140;End=140
Q15109	Domain	227	317	Note=Ig-like C2-type 2	Type=Substitution;Start=275;End=404
Q15109	Domain	227	317	Note=Ig-like C2-type 2	Type=Deletion;Start=122;End=404
Q15109	Domain	227	317	Note=Ig-like C2-type 2	Type=Substitution;Start=275;End=325
Q15109	Domain	227	317	Note=Ig-like C2-type 2	Type=Substitution;Start=276;End=355
Q15109	Region	367	404	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=374;End=404
Q15109	Region	367	404	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=275;End=404
Q15109	Region	367	404	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=332;End=404
Q15109	Region	367	404	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=332;End=404
Q15109	Region	367	404	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=122;End=404
Q15109	Region	367	404	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=326;End=404
Q15109	Region	367	404	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=356;End=404
Q15109	Compositional bias	367	381	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=374;End=404
Q15109	Compositional bias	367	381	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=275;End=404
Q15109	Compositional bias	367	381	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=332;End=404
Q15109	Compositional bias	367	381	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=332;End=404
Q15109	Compositional bias	367	381	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=122;End=404
Q15109	Compositional bias	367	381	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=326;End=404
Q15109	Compositional bias	367	381	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=356;End=404

Gene Isoform Structures and Expression Levels for AGER

Gene structures of our canonical and alternative spliced genes of AGER
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.

Expression levels of gene isoforms across GTEx.

Expression levels of gene isoforms across TCGA.

Protein Structures

PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.

3D view using mol* of Q15109-1

3D view using mol* of Q15109-10

3D view using mol* of Q15109-2

3D view using mol* of Q15109-3

3D view using mol* of Q15109-4

3D view using mol* of Q15109-5

3D view using mol* of Q15109-6

3D view using mol* of Q15109-7

3D view using mol* of Q15109-8

3D view using mol* of Q15109-9

pLDDT Score Distribution

pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.

pLDDT distribution across the protein length of Q15109-1

pLDDT distribution across the protein length of Q15109-10

pLDDT distribution across the protein length of Q15109-2

pLDDT distribution across the protein length of Q15109-3

pLDDT distribution across the protein length of Q15109-4

pLDDT distribution across the protein length of Q15109-5

pLDDT distribution across the protein length of Q15109-6

pLDDT distribution across the protein length of Q15109-7

pLDDT distribution across the protein length of Q15109-8

pLDDT distribution across the protein length of Q15109-9

Ramachandran Plot of Protein Structures

Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.

Ramachandran plot of Q15109-1

Ramachandran plot of Q15109-2

Ramachandran plot of Q15109-4

Ramachandran plot of Q15109-5

Ramachandran plot of Q15109-7

Ramachandran plot of Q15109-9

Potential Active Site Information

The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.

UniProt-id	Site score	Size	D score	Volume	Exposure	Enclosure	Contact	Phobic	Philic	Balance	Don/Acc	Residues
Q15109-1	0.793	64	0.724	148.862	0.682	0.607	0.872	0.153	1.203	0.128	1.443	45,46,47,49,62,63,64,65,66,67,68,70,71,72,73,76,77 ,78,79,80
Q15109-10	0.792	45	0.793	119.707	0.664	0.647	0.775	1.02	0.692	1.474	1.311	133,159,160,164,170,171,194,195,196,197,200,201,20 4,206,229
Q15109-2	0.893	68	0.918	200.655	0.618	0.649	0.851	1.033	0.757	1.365	1.614	145,146,148,149,150,151,154,155,157,180,181,182,18 3,186,187,190,192,215
Q15109-3	0.807	54	0.803	197.911	0.693	0.64	0.808	0.909	0.833	1.092	1.852	159,160,162,163,164,165,168,169,170,171,194,195,19 6,197,200,201,202,204,206,229,231
Q15109-4	0.81	41	0.785	127.939	0.523	0.737	0.991	1.74	0.797	2.184	1.683	133,175,176,180,186,187,210,211,212,213,216,217,22 0,222,245
Q15109-5	0.711	48	0.676	138.229	0.746	0.598	0.854	0.206	1.024	0.201	1.42	45,46,47,49,62,63,64,65,66,68,69,70,71,72,73,76,77 ,78,82
Q15109-6	0.812	42	0.808	129.311	0.592	0.699	0.885	1.484	0.678	2.19	1.738	133,175,176,180,186,187,210,211,212,213,216,217,22 0,222,245
Q15109-7	0.78	42	0.78	124.852	0.644	0.647	0.805	1.356	0.667	2.032	0.909	119,145,146,150,156,157,180,181,182,183,186,187,19 0,192,215
Q15109-8	1.002	116	1.034	259.651	0.523	0.676	0.976	0.679	0.954	0.713	1.214	236,237,239,258,259,260,261,262,263,264,265,266,26 7,269,271,284,286,287,288,289,290,291,292,293
Q15109-9	0.826	59	0.808	142.688	0.624	0.674	0.97	0.203	0.977	0.208	1.014	247,248,249,250,251,252,253,255,287,288,289,290,29 4,295,296,317,318,319,320,321,322,323

Protein Structure and Feature Comparision

Protein Structure Comparision Using Template Modeling Scores (TM-score).

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)

3D view using mol* of Q15109-1_Q15109-1_4ybh_A.pdb

Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of Q15109-1_4ybh_A_Q15109-10.pdb

3D view using mol* of Q15109-1_4ybh_A_Q15109-2.pdb

3D view using mol* of Q15109-1_4ybh_A_Q15109-3.pdb

3D view using mol* of Q15109-1_4ybh_A_Q15109-4.pdb

3D view using mol* of Q15109-1_4ybh_A_Q15109-5.pdb

3D view using mol* of Q15109-1_4ybh_A_Q15109-6.pdb

3D view using mol* of Q15109-1_4ybh_A_Q15109-7.pdb

3D view using mol* of Q15109-1_4ybh_A_Q15109-8.pdb

3D view using mol* of Q15109-1_4ybh_A_Q15109-9.pdb

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of Q15109-1_Q15109-10.pdb

3D view using mol* of Q15109-1_Q15109-2.pdb

3D view using mol* of Q15109-1_Q15109-3.pdb

3D view using mol* of Q15109-1_Q15109-4.pdb

3D view using mol* of Q15109-1_Q15109-5.pdb

3D view using mol* of Q15109-1_Q15109-6.pdb

3D view using mol* of Q15109-1_Q15109-7.pdb

3D view using mol* of Q15109-1_Q15109-8.pdb

3D view using mol* of Q15109-1_Q15109-9.pdb

Protein Feature Comparison of the protein sequendary structures among the protiens.

./stats/secondary_structure/figure/Q15109-1_vs_Q15109-10.png

./stats/secondary_structure/figure/Q15109-1_vs_Q15109-2.png

./stats/secondary_structure/figure/Q15109-1_vs_Q15109-3.png

./stats/secondary_structure/figure/Q15109-1_vs_Q15109-4.png

./stats/secondary_structure/figure/Q15109-1_vs_Q15109-5.png

./stats/secondary_structure/figure/Q15109-1_vs_Q15109-6.png

./stats/secondary_structure/figure/Q15109-1_vs_Q15109-7.png

./stats/secondary_structure/figure/Q15109-1_vs_Q15109-8.png

./stats/secondary_structure/figure/Q15109-1_vs_Q15109-9.png

Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.

./stats/relative_asa/Q15109-1_vs_Q15109-10.png

./stats/relative_asa/Q15109-1_vs_Q15109-2.png

./stats/relative_asa/Q15109-1_vs_Q15109-3.png

./stats/relative_asa/Q15109-1_vs_Q15109-4.png

./stats/relative_asa/Q15109-1_vs_Q15109-5.png

./stats/relative_asa/Q15109-1_vs_Q15109-6.png

./stats/relative_asa/Q15109-1_vs_Q15109-7.png

./stats/relative_asa/Q15109-1_vs_Q15109-8.png

./stats/relative_asa/Q15109-1_vs_Q15109-9.png

Protein-Protein Interaction

Interactors from UniProt.

Accession_id

Subsection

Start

End

Funcitonal feature

Splicing information

Interactors from STRING.

Gene name

Interactors

Related Drugs to AGER

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession

Gene name

DrugBank ID

Drug name

Drug group

Actions

Related Diseases to AGER

Previous studies relating to the alternative splicing of AGER and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
AGER	18550199	Increased serum endogenous secretory receptor for advanced glycation end-product (esRAGE) levels in type 2 diabetic patients with decreased renal function.	The binding of advanced glycation end-products (AGEs) to their receptor for AGEs (RAGE) may play an important role in the development of diabetic vascular complications. Recently, soluble RAGE (sRAGE) has been identified as an alternative splicing form of RAGE. Furthermore, administration of sRAGE improved atherosclerosis in type 2 diabetic mice.	D003924	Diabetes Mellitus, Type 2
AGER	18550199	Increased serum endogenous secretory receptor for advanced glycation end-product (esRAGE) levels in type 2 diabetic patients with decreased renal function.	The binding of advanced glycation end-products (AGEs) to their receptor for AGEs (RAGE) may play an important role in the development of diabetic vascular complications. Recently, soluble RAGE (sRAGE) has been identified as an alternative splicing form of RAGE. Furthermore, administration of sRAGE improved atherosclerosis in type 2 diabetic mice.	D003928	Diabetic Nephropathies
AGER	18593464	Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis.	Despite the advent of biological therapies for the treatment of rheumatoid arthritis, there is a compelling need to develop alternative therapeutic targets for nonresponders to existing treatments. Soluble receptors occur naturally in vivo, such as the splice variant of the cell surface receptor for vascular endothelial growth factor (VEGF)--a key regulator of angiogenesis in rheumatoid arthritis. Bioinformatics analyses predict that the majority of human genes undergo alternative splicing, generating proteins--many of which may have regulatory functions. The objective of the present study was to identify alternative splice variants (ASV) from cell surface receptor genes, and to determine whether the novel proteins encoded exert therapeutic activity in an in vivo model of arthritis.	D001172	Arthritis, Rheumatoid
AGER	18593464	Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis.	Despite the advent of biological therapies for the treatment of rheumatoid arthritis, there is a compelling need to develop alternative therapeutic targets for nonresponders to existing treatments. Soluble receptors occur naturally in vivo, such as the splice variant of the cell surface receptor for vascular endothelial growth factor (VEGF)--a key regulator of angiogenesis in rheumatoid arthritis. Bioinformatics analyses predict that the majority of human genes undergo alternative splicing, generating proteins--many of which may have regulatory functions. The objective of the present study was to identify alternative splice variants (ASV) from cell surface receptor genes, and to determine whether the novel proteins encoded exert therapeutic activity in an in vivo model of arthritis.	D004195	Disease Models, Animal
AGER	18952609	Receptor for advanced glycation end products is subjected to protein ectodomain shedding by metalloproteinases.	The receptor for advanced glycation end products (RAGE) is a 55-kDa type I membrane glycoprotein of the immunoglobulin superfamily. Ligand-induced up-regulation of RAGE is involved in various pathophysiological processes, including late diabetic complications and Alzheimer disease. Application of recombinant soluble RAGE has been shown to block RAGE-mediated pathophysiological conditions. After expression of full-length RAGE in HEK cells we identified a 48-kDa soluble RAGE form (sRAGE) in the culture medium. This variant of RAGE is smaller than a 51-kDa soluble version derived from alternative splicing. The release of sRAGE can be induced by the phorbol ester PMA and the calcium ionophore calcimycin via calcium-dependent protein kinase C subtypes. Hydroxamic acid-based metalloproteinase inhibitors block the release of sRAGE, and by RNA interference experiments we identified ADAM10 and MMP9 to be involved in RAGE shedding. In protein biotinylation experiments we show that membrane-anchored full-length RAGE is the precursor of sRAGE and that sRAGE is efficiently released from the cell surface. We identified cleavage of RAGE to occur close to the cell membrane. Ectodomain shedding of RAGE simultaneously generates sRAGE and a membrane-anchored C-terminal RAGE fragment (RAGE-CTF). The amount of RAGE-CTF increases when RAGE-expressing cells are treated with a gamma-secretase inhibitor, suggesting that RAGE-CTF is normally further processed by gamma-secretase. Identification of these novel mechanisms involved in regulating the availability of cell surface-located RAGE and its soluble ectodomain may influence further research in RAGE-mediated processes in cell biology and pathophysiology.	D000544	Alzheimer Disease
AGER	18952609	Receptor for advanced glycation end products is subjected to protein ectodomain shedding by metalloproteinases.	The receptor for advanced glycation end products (RAGE) is a 55-kDa type I membrane glycoprotein of the immunoglobulin superfamily. Ligand-induced up-regulation of RAGE is involved in various pathophysiological processes, including late diabetic complications and Alzheimer disease. Application of recombinant soluble RAGE has been shown to block RAGE-mediated pathophysiological conditions. After expression of full-length RAGE in HEK cells we identified a 48-kDa soluble RAGE form (sRAGE) in the culture medium. This variant of RAGE is smaller than a 51-kDa soluble version derived from alternative splicing. The release of sRAGE can be induced by the phorbol ester PMA and the calcium ionophore calcimycin via calcium-dependent protein kinase C subtypes. Hydroxamic acid-based metalloproteinase inhibitors block the release of sRAGE, and by RNA interference experiments we identified ADAM10 and MMP9 to be involved in RAGE shedding. In protein biotinylation experiments we show that membrane-anchored full-length RAGE is the precursor of sRAGE and that sRAGE is efficiently released from the cell surface. We identified cleavage of RAGE to occur close to the cell membrane. Ectodomain shedding of RAGE simultaneously generates sRAGE and a membrane-anchored C-terminal RAGE fragment (RAGE-CTF). The amount of RAGE-CTF increases when RAGE-expressing cells are treated with a gamma-secretase inhibitor, suggesting that RAGE-CTF is normally further processed by gamma-secretase. Identification of these novel mechanisms involved in regulating the availability of cell surface-located RAGE and its soluble ectodomain may influence further research in RAGE-mediated processes in cell biology and pathophysiology.	D048909	Diabetes Complications

Clinically important variants in AGER

(ClinVar, 04/20/2024)

accession_id

uniprot_id

gene_name

Type

Variant

Clinical_significance