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P01589

- IL2RA_HUMAN

UniProt

P01589 - IL2RA_HUMAN

Protein

Interleukin-2 receptor subunit alpha

Gene

IL2RA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Receptor for interleukin-2.

    GO - Molecular functioni

    1. drug binding Source: Ensembl
    2. interleukin-2 receptor activity Source: ProtInc

    GO - Biological processi

    1. activation-induced cell death of T cells Source: Ensembl
    2. apoptotic process Source: ProtInc
    3. cell proliferation Source: ProtInc
    4. cell surface receptor signaling pathway Source: ProtInc
    5. immune response Source: ProtInc
    6. inflammatory response to antigenic stimulus Source: Ensembl
    7. negative regulation of defense response to virus Source: Ensembl
    8. negative regulation of immune response Source: Ensembl
    9. negative regulation of inflammatory response Source: Ensembl
    10. negative regulation of T cell proliferation Source: Ensembl
    11. Notch signaling pathway Source: Ensembl
    12. positive regulation of activated T cell proliferation Source: Ensembl
    13. positive regulation of T cell differentiation Source: Ensembl
    14. regulation of T cell homeostatic proliferation Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_23891. Interleukin receptor SHC signaling.
    REACT_27283. Interleukin-2 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interleukin-2 receptor subunit alpha
    Short name:
    IL-2 receptor subunit alpha
    Short name:
    IL-2-RA
    Short name:
    IL-2R subunit alpha
    Short name:
    IL2-RA
    Alternative name(s):
    TAC antigen
    p55
    CD_antigen: CD25
    Gene namesi
    Name:IL2RA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:6008. IL2RA.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Diabetes mellitus, insulin-dependent, 10 (IDDM10) [MIM:601942]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Keywords - Diseasei

    Diabetes mellitus

    Organism-specific databases

    MIMi601942. phenotype.
    606367. phenotype.
    Orphaneti169100. Immunodeficiency due to CD25 deficiency.
    85408. Juvenile rheumatoid factor-negative polyarthritis.
    85410. Oligoarticular juvenile arthritis.
    PharmGKBiPA29828.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 272251Interleukin-2 receptor subunit alphaPRO_0000011024Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 168
    Disulfide bondi49 ↔ 80
    Disulfide bondi51 ↔ 82
    Disulfide bondi67 ↔ 125
    Glycosylationi70 – 701N-linked (GlcNAc...)1 Publication
    Glycosylationi89 – 891N-linked (GlcNAc...)1 Publication
    Disulfide bondi152 ↔ 184
    Glycosylationi218 – 2181O-linked (GalNAc...)1 Publication
    Glycosylationi224 – 2241O-linked (GalNAc...)1 Publication
    Glycosylationi229 – 2291O-linked (GalNAc...)1 Publication
    Glycosylationi237 – 2371O-linked (GalNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP01589.
    PRIDEiP01589.

    PTM databases

    PhosphoSiteiP01589.

    Expressioni

    Gene expression databases

    ArrayExpressiP01589.
    BgeeiP01589.
    CleanExiHS_IL2RA.
    GenevestigatoriP01589.

    Organism-specific databases

    HPAiCAB002419.

    Interactioni

    Subunit structurei

    Non-covalent dimer of an alpha and a beta subunit. IL2R exists in 3 different forms: a high affinity dimer, an intermediate affinity monomer (beta subunit), and a low affinity monomer (alpha subunit). The high and intermediate affinity forms also associate with a gamma subunit.2 Publications

    Protein-protein interaction databases

    BioGridi109774. 4 interactions.
    DIPiDIP-1080N.
    IntActiP01589. 1 interaction.
    MINTiMINT-8146732.
    STRINGi9606.ENSP00000369293.

    Structurei

    Secondary structure

    1
    272
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 374
    Beta strandi39 – 413
    Beta strandi46 – 483
    Beta strandi55 – 573
    Beta strandi63 – 675
    Beta strandi74 – 774
    Beta strandi82 – 843
    Beta strandi135 – 1373
    Beta strandi143 – 1453
    Beta strandi147 – 1526
    Beta strandi157 – 1626
    Beta strandi164 – 1707
    Beta strandi172 – 1743
    Beta strandi175 – 1773
    Beta strandi182 – 1854

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ILMmodel-A23-83[»]
    1ILNmodel-A23-83[»]
    1Z92X-ray2.80B22-238[»]
    2B5IX-ray2.30D22-238[»]
    2ERJX-ray3.00A/E22-233[»]
    3IU3X-ray2.90I/J/K22-238[»]
    3NFPX-ray2.86I/K22-238[»]
    ProteinModelPortaliP01589.
    SMRiP01589. Positions 22-186.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01589.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 240219ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini260 – 27213CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei241 – 25919HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 8463Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini123 – 18664Sushi 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG47154.
    HOGENOMiHOG000113044.
    HOVERGENiHBG052109.
    InParanoidiP01589.
    KOiK05068.
    OMAiSIFTTEY.
    OrthoDBiEOG7S21ZH.
    PhylomeDBiP01589.
    TreeFamiTF337408.

    Family and domain databases

    InterProiIPR015486. IL-2_rcpt_alpha.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PANTHERiPTHR10573. PTHR10573. 1 hit.
    PfamiPF00084. Sushi. 2 hits.
    [Graphical view]
    SMARTiSM00032. CCP. 2 hits.
    [Graphical view]
    SUPFAMiSSF57535. SSF57535. 2 hits.
    PROSITEiPS50923. SUSHI. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01589-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSYLLMWGL LTFIMVPGCQ AELCDDDPPE IPHATFKAMA YKEGTMLNCE    50
    CKRGFRRIKS GSLYMLCTGN SSHSSWDNQC QCTSSATRNT TKQVTPQPEE 100
    QKERKTTEMQ SPMQPVDQAS LPGHCREPPP WENEATERIY HFVVGQMVYY 150
    QCVQGYRALH RGPAESVCKM THGKTRWTQP QLICTGEMET SQFPGEEKPQ 200
    ASPEGRPESE TSCLVTTTDF QIQTEMAATM ETSIFTTEYQ VAVAGCVFLL 250
    ISVLLLSGLT WQRRQRKSRR TI 272
    Length:272
    Mass (Da):30,819
    Last modified:July 21, 1986 - v1
    Checksum:i83D907C8C81D2C0E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti272 – 2721I → T.1 Publication
    Corresponds to variant rs12722712 [ dbSNP | Ensembl ].
    VAR_019280

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01057 mRNA. Translation: CAA25525.1.
    X03131
    , X03132, X03133, X03134, X03135, X03136, X03137, X03138 Genomic DNA. Translation: CAA26906.1.
    K03122 mRNA. Translation: AAB59535.1. Sequence problems.
    M11066
    , M10322, M11060, M11061, M11062, M11063, M11064, M11065 Genomic DNA. Translation: AAA67527.1.
    AY563103 Genomic DNA. Translation: AAS55572.1.
    AL157395, AL137186 Genomic DNA. Translation: CAH73595.1.
    AL137186, AL157395 Genomic DNA. Translation: CAI41069.1.
    CH471072 Genomic DNA. Translation: EAW86414.1.
    M15864 Genomic DNA. Translation: AAA59162.1.
    BN000945 Genomic DNA. Translation: CAK26553.1.
    CCDSiCCDS7076.1.
    PIRiA44186. UHHU2.
    RefSeqiNP_000408.1. NM_000417.2.
    UniGeneiHs.231367.

    Genome annotation databases

    EnsembliENST00000379959; ENSP00000369293; ENSG00000134460.
    GeneIDi3559.
    KEGGihsa:3559.
    UCSCiuc001iiz.2. human.

    Polymorphism databases

    DMDMi124317.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    IL2RAbase

    IL2RA mutation db

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01057 mRNA. Translation: CAA25525.1 .
    X03131
    , X03132 , X03133 , X03134 , X03135 , X03136 , X03137 , X03138 Genomic DNA. Translation: CAA26906.1 .
    K03122 mRNA. Translation: AAB59535.1 . Sequence problems.
    M11066
    , M10322 , M11060 , M11061 , M11062 , M11063 , M11064 , M11065 Genomic DNA. Translation: AAA67527.1 .
    AY563103 Genomic DNA. Translation: AAS55572.1 .
    AL157395 , AL137186 Genomic DNA. Translation: CAH73595.1 .
    AL137186 , AL157395 Genomic DNA. Translation: CAI41069.1 .
    CH471072 Genomic DNA. Translation: EAW86414.1 .
    M15864 Genomic DNA. Translation: AAA59162.1 .
    BN000945 Genomic DNA. Translation: CAK26553.1 .
    CCDSi CCDS7076.1.
    PIRi A44186. UHHU2.
    RefSeqi NP_000408.1. NM_000417.2.
    UniGenei Hs.231367.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ILM model - A 23-83 [» ]
    1ILN model - A 23-83 [» ]
    1Z92 X-ray 2.80 B 22-238 [» ]
    2B5I X-ray 2.30 D 22-238 [» ]
    2ERJ X-ray 3.00 A/E 22-233 [» ]
    3IU3 X-ray 2.90 I/J/K 22-238 [» ]
    3NFP X-ray 2.86 I/K 22-238 [» ]
    ProteinModelPortali P01589.
    SMRi P01589. Positions 22-186.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109774. 4 interactions.
    DIPi DIP-1080N.
    IntActi P01589. 1 interaction.
    MINTi MINT-8146732.
    STRINGi 9606.ENSP00000369293.

    Chemistry

    BindingDBi P01589.
    ChEMBLi CHEMBL2364167.
    DrugBanki DB00041. Aldesleukin.
    DB00074. Basiliximab.
    DB00111. Daclizumab.
    DB00004. Denileukin diftitox.
    GuidetoPHARMACOLOGYi 1695.

    PTM databases

    PhosphoSitei P01589.

    Polymorphism databases

    DMDMi 124317.

    Proteomic databases

    PaxDbi P01589.
    PRIDEi P01589.

    Protocols and materials databases

    DNASUi 3559.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379959 ; ENSP00000369293 ; ENSG00000134460 .
    GeneIDi 3559.
    KEGGi hsa:3559.
    UCSCi uc001iiz.2. human.

    Organism-specific databases

    CTDi 3559.
    GeneCardsi GC10M006041.
    HGNCi HGNC:6008. IL2RA.
    HPAi CAB002419.
    MIMi 147730. gene.
    601942. phenotype.
    606367. phenotype.
    neXtProti NX_P01589.
    Orphaneti 169100. Immunodeficiency due to CD25 deficiency.
    85408. Juvenile rheumatoid factor-negative polyarthritis.
    85410. Oligoarticular juvenile arthritis.
    PharmGKBi PA29828.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47154.
    HOGENOMi HOG000113044.
    HOVERGENi HBG052109.
    InParanoidi P01589.
    KOi K05068.
    OMAi SIFTTEY.
    OrthoDBi EOG7S21ZH.
    PhylomeDBi P01589.
    TreeFami TF337408.

    Enzyme and pathway databases

    Reactomei REACT_23891. Interleukin receptor SHC signaling.
    REACT_27283. Interleukin-2 signaling.

    Miscellaneous databases

    EvolutionaryTracei P01589.
    GeneWikii IL2RA.
    GenomeRNAii 3559.
    NextBioi 13900.
    PROi P01589.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01589.
    Bgeei P01589.
    CleanExi HS_IL2RA.
    Genevestigatori P01589.

    Family and domain databases

    InterProi IPR015486. IL-2_rcpt_alpha.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    PANTHERi PTHR10573. PTHR10573. 1 hit.
    Pfami PF00084. Sushi. 2 hits.
    [Graphical view ]
    SMARTi SM00032. CCP. 2 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 2 hits.
    PROSITEi PS50923. SUSHI. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of cDNA encoding human interleukin-2 receptor."
      Nikaido T., Shimizu A., Ishida N., Sabe H., Teshigawara K., Maeda M., Uchiyama T., Yodoi J., Honjo T.
      Nature 311:631-635(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Molecular cloning and structure of the human interleukin 2 receptor gene."
      Ishida N., Kanamori H., Noma T., Nikaido T., Sabe H., Suzuki N., Shimizu A., Honjo T.
      Nucleic Acids Res. 13:7579-7589(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. SeattleSNPs variation discovery resource
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-272.
    6. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "Regulation of the human interleukin-2 receptor alpha chain promoter: activation of a nonfunctional promoter by the transactivator gene of HTLV-I."
      Cross S.L., Feinberg M.B., Wolf J.B., Holbrook N.J., Wong-Stall F., Leonard W.J.
      Cell 49:47-56(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
    9. "Structural analysis of recombinant soluble human interleukin-2 receptor. Primary structure, assignment of disulfide bonds and core IL-2 binding structure."
      Miedel M.C., Hulmes J.D., Weber D.V., Bailon P., Pan Y.C.
      Biochem. Biophys. Res. Commun. 154:372-379(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS, GLYCOSYLATION AT ASN-70; ASN-89; THR-218; THR-224; THR-229 AND THR-237.
    10. "The interleukin-2 and interleukin-4 receptors studied by molecular modelling."
      Bamborough P., Hedgecock C.J., Richards W.G.
      Structure 2:839-851(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 23-83.
    11. "Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors."
      Wang X., Rickert M., Garcia K.C.
      Science 310:1159-1163(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-238 IN COMPLEX WITH IL2; IL2RB AND IL2RC, DISULFIDE BONDS.
    12. "Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor."
      Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.
      Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-233 IN COMPLEX WITH IL2; IL2RB AND IL2RC, DISULFIDE BONDS.
    13. "Large-scale genetic fine mapping and genotype-phenotype associations implicate polymorphism in the IL2RA region in type 1 diabetes."
      Lowe C.E., Cooper J.D., Brusko T., Walker N.M., Smyth D.J., Bailey R., Bourget K., Plagnol V., Field S., Atkinson M., Clayton D.G., Wicker L.S., Todd J.A.
      Nat. Genet. 39:1074-1082(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN IDDM10.

    Entry informationi

    Entry nameiIL2RA_HUMAN
    AccessioniPrimary (citable) accession number: P01589
    Secondary accession number(s): Q5W007
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 162 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 cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3