Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15109

- RAGE_HUMAN

UniProt

Q15109 - RAGE_HUMAN

Protein

Advanced glycosylation end product-specific receptor

Gene

AGER

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.By similarity4 Publications

    GO - Molecular functioni

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

    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

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

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: Reactome

    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 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 404382Advanced glycosylation end product-specific receptorPRO_0000014923Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi38 ↔ 99
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi144 ↔ 208
    Disulfide bondi259 – 259Interchain
    Disulfide bondi301 – 301Interchain

    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.By similarity6 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

    1
    404
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15109.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 342320ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini364 – 40441CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei343 – 36321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → G in AAA03574. (PubMed:1378843)Curated

    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. 2 PublicationsVSP_002551Add
    BLAST
    Alternative sequencei113 – 1219YRVRVYQIP → WWWSQKVEQ in isoform 5. 1 PublicationVSP_047884
    Alternative sequencei122 – 404283Missing in isoform 5. 1 PublicationVSP_047885Add
    BLAST
    Alternative sequencei140 – 1401K → KVVEESRRSRKRPCEQE in isoform 4 and isoform 6. 1 PublicationVSP_043528
    Alternative sequencei275 – 404130GVPLP…STGGP → VSDLERGAGRTRRGGANCRL CGRIRAGNSSPGPGDPGRPG DSRPAHWGHLVAKAATPRRG EEGPRKPGGRGGACRTESVG GT in isoform 2. 1 PublicationVSP_002552Add
    BLAST
    Alternative sequencei275 – 32551GVPLP…IEPGE → NQARRGQLQVRGLIKSGKQK IAPNTCDWGDGQQERNGRPQ KTRRKRRSVQN in isoform 8. 1 PublicationVSP_047886Add
    BLAST
    Alternative sequencei276 – 35580VPLPL…LGTAA → LRTREPTAVWPPIPATGPRK AVLSASASSNQARRGQLQVR GLIKSGKQKIAPNTCDWGDG QQERNGRPQKTRRKRRSVQN in isoform 9. 1 PublicationVSP_047887Add
    BLAST
    Alternative sequencei326 – 40479Missing in isoform 8. 1 PublicationVSP_047888Add
    BLAST
    Alternative sequencei332 – 40473SVGGS…STGGP → EGFDKVREAEDSPQHM in isoform 3 and isoform 4. 2 PublicationsVSP_042011Add
    BLAST
    Alternative sequencei356 – 40449Missing in isoform 9. 1 PublicationVSP_047889Add
    BLAST
    Alternative sequencei374 – 40431KAPEN…STGGP → PQKTRRKRRSVQN in isoform 10. 1 PublicationVSP_055321Add
    BLAST

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 154 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