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Q9HCD5

- NCOA5_HUMAN

UniProt

Q9HCD5 - NCOA5_HUMAN

Protein

Nuclear receptor coactivator 5

Gene

NCOA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (12 Feb 2003)
      Previous versions | rss
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    Functioni

    Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2).1 Publication

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor coactivator 5
    Short name:
    NCoA-5
    Alternative name(s):
    Coactivator independent of AF-2
    Short name:
    CIA
    Gene namesi
    Name:NCOA5
    Synonyms:KIAA1637
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15909. NCOA5.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. extracellular space Source: UniProt
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi342 – 3421I → A: Abolishes E2-inducible strong interaction with ESR1, but not basal interaction. 1 Publication
    Mutagenesisi348 – 3492LL → AA: Abolishes interaction with ESR1.

    Organism-specific databases

    PharmGKBiPA31474.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 579579Nuclear receptor coactivator 5PRO_0000094411Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei3 – 31Phosphothreonine1 Publication
    Modified residuei9 – 91Phosphoserine2 Publications
    Modified residuei29 – 291Phosphoserine1 Publication
    Modified residuei34 – 341Phosphoserine1 Publication
    Modified residuei126 – 1261Phosphoserine1 Publication
    Modified residuei151 – 1511Phosphoserine1 Publication
    Modified residuei378 – 3781Phosphoserine1 Publication
    Modified residuei381 – 3811Phosphoserine4 Publications
    Modified residuei394 – 3941Phosphothreonine1 Publication
    Modified residuei395 – 3951Phosphoserine1 Publication
    Modified residuei398 – 3981Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9HCD5.
    PaxDbiQ9HCD5.
    PRIDEiQ9HCD5.

    PTM databases

    PhosphoSiteiQ9HCD5.

    Miscellaneous databases

    PMAP-CutDBQ9HCD5.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiQ9HCD5.
    BgeeiQ9HCD5.
    CleanExiHS_NCOA5.
    GenevestigatoriQ9HCD5.

    Organism-specific databases

    HPAiHPA050231.

    Interactioni

    Subunit structurei

    Binds HTATIP2/TIP30. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and PPP1CA.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Nr1d2Q606742EBI-2863498,EBI-5326205From a different organism.

    Protein-protein interaction databases

    BioGridi121747. 14 interactions.
    IntActiQ9HCD5. 7 interactions.
    STRINGi9606.ENSP00000290231.

    Structurei

    Secondary structure

    1
    579
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi200 – 2078
    Helixi208 – 2103
    Helixi211 – 22111
    Turni222 – 2243
    Beta strandi227 – 2315
    Helixi238 – 24811
    Beta strandi251 – 2566
    Helixi258 – 2636
    Beta strandi265 – 2706
    Beta strandi272 – 2743
    Beta strandi277 – 2826
    Helixi283 – 30220
    Beta strandi304 – 3063
    Helixi345 – 3506

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V95NMR-A197-313[»]
    2J7XX-ray2.10B338-354[»]
    2J7YX-ray1.80B338-354[»]
    ProteinModelPortaliQ9HCD5.
    SMRiQ9HCD5. Positions 197-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HCD5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 158158Transcription repressionAdd
    BLAST
    Regioni458 – 579122Transcription activationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi345 – 3495LXXLL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi7 – 150144Arg/Asp-rich (mixed charge)Add
    BLAST

    Domaini

    Contains one Leu-Xaa-Xaa-Leu-Leu (LxxLL) motif that is essential for the association with nuclear receptors.

    Phylogenomic databases

    eggNOGiNOG147049.
    HOVERGENiHBG052585.
    InParanoidiQ9HCD5.
    OMAiGSARNMG.
    OrthoDBiEOG7GTT6B.
    PhylomeDBiQ9HCD5.
    TreeFamiTF324704.

    Family and domain databases

    Gene3Di3.40.50.800. 1 hit.
    InterProiIPR004154. Anticodon-bd.
    [Graphical view]
    SUPFAMiSSF52954. SSF52954. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9HCD5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTAPSRPSP TRRDPYGFGD SRDSRRDRSP IRGSPRREPR DGRNGRDARD    50
    SRDIRDPRDL RDHRHSRDLR DHRDSRSVRD VRDVRDLRDF RDLRDSRDFR 100
    DQRDPMYDRY RDMRDSRDPM YRREGSYDRY LRMDDYCRRK DDSYFDRYRD 150
    SFDGRGPPGP ESQSRAKERL KREERRREEL YRQYFEEIQR RFDAERPVDC 200
    SVIVVNKQTK DYAESVGRKV RDLGMVVDLI FLNTEVSLSQ ALEDVSRGGS 250
    PFAIVITQQH QIHRSCTVNI MFGTPQEHRN MPQADAMVLV ARNYERYKNE 300
    CREKEREEIA RQAAKMADEA ILQERERGGP EEGVRGGHPP AIQSLINLLA 350
    DNRYLTAEET DKIINYLRER KERLMRSSTD SLPGPISRQP LGATSGASLK 400
    TQPSSQPLQS GQVLPSATPT PSAPPTSQQE LQAKILSLFN SGTVTANSSS 450
    ASPSVAAGNT PNQNFSTAAN SQPQQRSQAS GNQPPSILGQ GGSAQNMGPR 500
    PGAPSQGLFG QPSSRLAPAS NMTSQRPVSS TGINFDNPSV QKALDTLIQS 550
    GPALSHLVSQ TTAQMGQPQA PMGSYQRHY 579
    Length:579
    Mass (Da):65,536
    Last modified:February 12, 2003 - v2
    Checksum:iD2ADCCEBEE566A91
    GO

    Sequence cautioni

    The sequence AAG36793.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti326 – 3261E → G.
    Corresponds to variant rs11549557 [ dbSNP | Ensembl ].
    VAR_053530

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF230533 mRNA. Translation: AAG36793.1. Different initiation.
    AF470686 mRNA. Translation: AAO33457.1.
    AL035662, AL162458 Genomic DNA. Translation: CAI42972.1.
    AL162458, AL035662 Genomic DNA. Translation: CAH74052.1.
    CH471077 Genomic DNA. Translation: EAW75765.1.
    CH471077 Genomic DNA. Translation: EAW75769.1.
    BC140836 mRNA. Translation: AAI40837.1.
    BC151133 mRNA. Translation: AAI51134.1.
    AB046857 mRNA. Translation: BAB13463.1.
    CCDSiCCDS13392.1.
    RefSeqiNP_066018.1. NM_020967.2.
    UniGeneiHs.654991.

    Genome annotation databases

    EnsembliENST00000290231; ENSP00000290231; ENSG00000124160.
    GeneIDi57727.
    KEGGihsa:57727.
    UCSCiuc002xrd.3. human.

    Polymorphism databases

    DMDMi28380083.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF230533 mRNA. Translation: AAG36793.1 . Different initiation.
    AF470686 mRNA. Translation: AAO33457.1 .
    AL035662 , AL162458 Genomic DNA. Translation: CAI42972.1 .
    AL162458 , AL035662 Genomic DNA. Translation: CAH74052.1 .
    CH471077 Genomic DNA. Translation: EAW75765.1 .
    CH471077 Genomic DNA. Translation: EAW75769.1 .
    BC140836 mRNA. Translation: AAI40837.1 .
    BC151133 mRNA. Translation: AAI51134.1 .
    AB046857 mRNA. Translation: BAB13463.1 .
    CCDSi CCDS13392.1.
    RefSeqi NP_066018.1. NM_020967.2.
    UniGenei Hs.654991.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V95 NMR - A 197-313 [» ]
    2J7X X-ray 2.10 B 338-354 [» ]
    2J7Y X-ray 1.80 B 338-354 [» ]
    ProteinModelPortali Q9HCD5.
    SMRi Q9HCD5. Positions 197-314.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121747. 14 interactions.
    IntActi Q9HCD5. 7 interactions.
    STRINGi 9606.ENSP00000290231.

    PTM databases

    PhosphoSitei Q9HCD5.

    Polymorphism databases

    DMDMi 28380083.

    Proteomic databases

    MaxQBi Q9HCD5.
    PaxDbi Q9HCD5.
    PRIDEi Q9HCD5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290231 ; ENSP00000290231 ; ENSG00000124160 .
    GeneIDi 57727.
    KEGGi hsa:57727.
    UCSCi uc002xrd.3. human.

    Organism-specific databases

    CTDi 57727.
    GeneCardsi GC20M044690.
    HGNCi HGNC:15909. NCOA5.
    HPAi HPA050231.
    neXtProti NX_Q9HCD5.
    PharmGKBi PA31474.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG147049.
    HOVERGENi HBG052585.
    InParanoidi Q9HCD5.
    OMAi GSARNMG.
    OrthoDBi EOG7GTT6B.
    PhylomeDBi Q9HCD5.
    TreeFami TF324704.

    Miscellaneous databases

    ChiTaRSi NCOA5. human.
    EvolutionaryTracei Q9HCD5.
    GeneWikii NCOA5.
    GenomeRNAii 57727.
    NextBioi 64672.
    PMAP-CutDB Q9HCD5.
    PROi Q9HCD5.

    Gene expression databases

    ArrayExpressi Q9HCD5.
    Bgeei Q9HCD5.
    CleanExi HS_NCOA5.
    Genevestigatori Q9HCD5.

    Family and domain databases

    Gene3Di 3.40.50.800. 1 hit.
    InterProi IPR004154. Anticodon-bd.
    [Graphical view ]
    SUPFAMi SSF52954. SSF52954. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant."
      Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.
      Mol. Cell. Biol. 21:343-353(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ESR1; ESR2 AND NR1D2, MUTAGENESIS OF ILE-342 AND 348-LEU-LEU-349.
      Tissue: Fetal kidney.
    2. "TIP30 interacts with an estrogen receptor alpha-interacting coactivator CIA and regulates c-myc transcription."
      Jiang C., Ito M., Piening V., Bruck K., Roeder R.G., Xiao H.
      J. Biol. Chem. 279:27781-27789(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 86-91 AND 280-292, FUNCTION, INTERACTION WITH HTATIP2.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Brain.
    6. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
      DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-579.
      Tissue: Brain.
    7. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."
      Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.
      Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; RBMX AND PPP1CA, INTERACTION WITH YLPM1.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-9; SER-29; SER-34; SER-378 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-126; SER-381; THR-394; SER-395 AND SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Solution structure of anticodon binding domain from nuclear receptor coactivator 5 (human KIAA1637 protein)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 197-313.

    Entry informationi

    Entry nameiNCOA5_HUMAN
    AccessioniPrimary (citable) accession number: Q9HCD5
    Secondary accession number(s): B2RTV9
    , E1P5R0, Q6HA99, Q9H1F2, Q9H2T2, Q9H4Y9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 12, 2003
    Last sequence update: February 12, 2003
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3