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Q9BW71

- HIRP3_HUMAN

UniProt

Q9BW71 - HIRP3_HUMAN

Protein

HIRA-interacting protein 3

Gene

HIRIP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    May play a role in chromatin function and histone metabolism via its interaction with HIRA and histones.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin assembly or disassembly Source: ProtInc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    HIRA-interacting protein 3
    Gene namesi
    Name:HIRIP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:4917. HIRIP3.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Nuclear throughout the cell cycle and is excluded from condensed chromatin during mitosis.

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29294.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 556556HIRA-interacting protein 3PRO_0000083989Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271Phosphoserine2 Publications
    Modified residuei84 – 841Phosphothreonine2 Publications
    Modified residuei87 – 871Phosphoserine2 Publications
    Modified residuei98 – 981Phosphoserine2 Publications
    Modified residuei100 – 1001Phosphoserine2 Publications
    Modified residuei125 – 1251Phosphoserine5 Publications
    Modified residuei142 – 1421Phosphoserine3 Publications
    Modified residuei143 – 1431Phosphoserine3 Publications
    Modified residuei159 – 1591Phosphoserine5 Publications
    Modified residuei160 – 1601Phosphoserine5 Publications
    Modified residuei196 – 1961Phosphoserine6 Publications
    Modified residuei199 – 1991Phosphoserine5 Publications
    Modified residuei223 – 2231Phosphoserine5 Publications
    Modified residuei227 – 2271Phosphoserine7 Publications
    Modified residuei289 – 2891Phosphoserine4 Publications
    Modified residuei291 – 2911Phosphoserine4 Publications
    Modified residuei330 – 3301Phosphoserine4 Publications
    Modified residuei332 – 3321Phosphoserine4 Publications
    Modified residuei333 – 3331Phosphoserine4 Publications
    Modified residuei357 – 3571Phosphoserine3 Publications
    Modified residuei358 – 3581Phosphothreonine3 Publications
    Modified residuei359 – 3591Phosphoserine3 Publications
    Modified residuei363 – 3631Phosphoserine4 Publications
    Modified residuei370 – 3701Phosphoserine4 Publications
    Modified residuei372 – 3721Phosphoserine3 Publications
    Modified residuei550 – 5501Phosphoserine2 Publications
    Modified residuei551 – 5511Phosphoserine2 Publications
    Modified residuei555 – 5551Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by CK2.7 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BW71.
    PaxDbiQ9BW71.
    PRIDEiQ9BW71.

    PTM databases

    PhosphoSiteiQ9BW71.

    Expressioni

    Tissue specificityi

    Widely expressed. Isoform 1 is predominant in skeletal muscle. Isoform 2 is predominant in liver and heart.1 Publication

    Gene expression databases

    ArrayExpressiQ9BW71.
    BgeeiQ9BW71.
    CleanExiHS_HIRIP3.
    GenevestigatoriQ9BW71.

    Interactioni

    Subunit structurei

    Interacts with HIRA. Weak interaction with histones H2B and H3. Interacts with CK2.2 Publications

    Protein-protein interaction databases

    BioGridi114053. 30 interactions.
    IntActiQ9BW71. 6 interactions.
    MINTiMINT-1411245.
    STRINGi9606.ENSP00000279392.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BW71.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi129 – 253125Glu-richAdd
    BLAST
    Compositional biasi398 – 4036Poly-Ser

    Phylogenomic databases

    eggNOGiNOG25729.
    HOGENOMiHOG000112903.
    HOVERGENiHBG066199.
    InParanoidiQ9BW71.
    OMAiDPERKRF.
    OrthoDBiEOG790G1V.
    PhylomeDBiQ9BW71.
    TreeFamiTF331753.

    Family and domain databases

    InterProiIPR019098. Histone_chaperone_domain_CHZ.
    [Graphical view]
    PfamiPF09649. CHZ. 1 hit.
    [Graphical view]
    SMARTiSM01082. CHZ. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BW71-1) [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

    MAREKEMQEF TRSFFRGRPD LSTLTHSIVR RRYLAHSGRS HLEPEEKQAL    50
    KRLVEEELLK MQVDEAASRE DKLDLTKKGK RPPTPCSDPE RKRFRFNSES 100
    ESGSEASSPD YFGPPAKNGV AAEVSPAKEE NPRRASKAVE ESSDEERQRD 150
    LPAQRGEESS EEEEKGYKGK TRKKPVVKKQ APGKASVSRK QAREESEESE 200
    AEPVQRTAKK VEGNKGTKSL KESEQESEEE ILAQKKEQRE EEVEEEEKEE 250
    DEEKGDWKPR TRSNGRRKSA REERSCKQKS QAKRLLGDSD SEEEQKEAAS 300
    SGDDSGRDRE PPVQRKSEDR TQLKGGKRLS GSSEDEEDSG KGEPTAKGSR 350
    KMARLGSTSG EESDLEREVS DSEAGGGPQG ERKNRSSKKS SRKGRTRSSS 400
    SSSDGSPEAK GGKAGSGRRG EDHPAVMRLK RYIRACGAHR NYKKLLGSCC 450
    SHKERLSILR AELEALGMKG TPSLGKCRAL KEQREEAAEV ASLDVANIIS 500
    GSGRPRRRTA WNPLGEAAPP GELYRRTLDS DEERPRPAPP DWSHMRGIIS 550
    SDGESN 556
    Length:556
    Mass (Da):61,957
    Last modified:October 17, 2006 - v3
    Checksum:iACABE2E0032B8C13
    GO
    Isoform 2 (identifier: Q9BW71-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         101-413: Missing.

    Show »
    Length:243
    Mass (Da):27,612
    Checksum:i6DE219CC60F3BAB8
    GO
    Isoform 3 (identifier: Q9BW71-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         101-175: ESGSEASSPD...GYKGKTRKKP → GWLRSPWRGP...GPEGAEGGGS
         176-556: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:175
    Mass (Da):19,709
    Checksum:i8E6D1E89AC91F6BF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581L → P in CAA11273. (PubMed:9710638)Curated
    Sequence conflicti58 – 581L → P in CAA11274. (PubMed:9710638)Curated
    Sequence conflicti58 – 581L → P in CAA11275. (PubMed:9710638)Curated
    Sequence conflicti58 – 581L → P(PubMed:17391060)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti496 – 4961A → V.
    Corresponds to variant rs35431046 [ dbSNP | Ensembl ].
    VAR_051033
    Natural varianti521 – 5211G → W.
    Corresponds to variant rs11643314 [ dbSNP | Ensembl ].
    VAR_028115

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei101 – 413313Missing in isoform 2. 1 PublicationVSP_003877Add
    BLAST
    Alternative sequencei101 – 17575ESGSE…TRKKP → GWLRSPWRGPPGCDEAEALH SGLWCPSKLQEAVGLLLLTQ GAPEYPPGRTGSARHEGYPF PREVSGPEGAEGGGS in isoform 3. 1 PublicationVSP_046024Add
    BLAST
    Alternative sequencei176 – 556381Missing in isoform 3. 1 PublicationVSP_046025Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ223349 mRNA. Translation: CAA11273.1.
    AJ223350 mRNA. Translation: CAA11274.1.
    AJ223351 mRNA. Translation: CAA11275.2.
    BX393533 mRNA. No translation available.
    AC093512 Genomic DNA. No translation available.
    BC000588 mRNA. Translation: AAH00588.1.
    CCDSiCCDS10664.1. [Q9BW71-1]
    CCDS58449.1. [Q9BW71-3]
    RefSeqiNP_001184252.1. NM_001197323.1. [Q9BW71-3]
    NP_003600.2. NM_003609.4. [Q9BW71-1]
    UniGeneiHs.567370.

    Genome annotation databases

    EnsembliENST00000279392; ENSP00000279392; ENSG00000149929. [Q9BW71-1]
    ENST00000564026; ENSP00000456824; ENSG00000149929. [Q9BW71-3]
    GeneIDi8479.
    KEGGihsa:8479.
    UCSCiuc002dve.3. human. [Q9BW71-1]

    Polymorphism databases

    DMDMi116242511.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ223349 mRNA. Translation: CAA11273.1 .
    AJ223350 mRNA. Translation: CAA11274.1 .
    AJ223351 mRNA. Translation: CAA11275.2 .
    BX393533 mRNA. No translation available.
    AC093512 Genomic DNA. No translation available.
    BC000588 mRNA. Translation: AAH00588.1 .
    CCDSi CCDS10664.1. [Q9BW71-1 ]
    CCDS58449.1. [Q9BW71-3 ]
    RefSeqi NP_001184252.1. NM_001197323.1. [Q9BW71-3 ]
    NP_003600.2. NM_003609.4. [Q9BW71-1 ]
    UniGenei Hs.567370.

    3D structure databases

    ProteinModelPortali Q9BW71.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114053. 30 interactions.
    IntActi Q9BW71. 6 interactions.
    MINTi MINT-1411245.
    STRINGi 9606.ENSP00000279392.

    PTM databases

    PhosphoSitei Q9BW71.

    Polymorphism databases

    DMDMi 116242511.

    Proteomic databases

    MaxQBi Q9BW71.
    PaxDbi Q9BW71.
    PRIDEi Q9BW71.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000279392 ; ENSP00000279392 ; ENSG00000149929 . [Q9BW71-1 ]
    ENST00000564026 ; ENSP00000456824 ; ENSG00000149929 . [Q9BW71-3 ]
    GeneIDi 8479.
    KEGGi hsa:8479.
    UCSCi uc002dve.3. human. [Q9BW71-1 ]

    Organism-specific databases

    CTDi 8479.
    GeneCardsi GC16M030005.
    HGNCi HGNC:4917. HIRIP3.
    MIMi 603365. gene.
    neXtProti NX_Q9BW71.
    PharmGKBi PA29294.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG25729.
    HOGENOMi HOG000112903.
    HOVERGENi HBG066199.
    InParanoidi Q9BW71.
    OMAi DPERKRF.
    OrthoDBi EOG790G1V.
    PhylomeDBi Q9BW71.
    TreeFami TF331753.

    Miscellaneous databases

    GeneWikii HIRIP3.
    GenomeRNAii 8479.
    NextBioi 31725.
    PROi Q9BW71.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BW71.
    Bgeei Q9BW71.
    CleanExi HS_HIRIP3.
    Genevestigatori Q9BW71.

    Family and domain databases

    InterProi IPR019098. Histone_chaperone_domain_CHZ.
    [Graphical view ]
    Pfami PF09649. CHZ. 1 hit.
    [Graphical view ]
    SMARTi SM01082. CHZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA."
      Lorain S., Quivy J.-P., Monier-Gavelle F., Scamps C., Lecluse Y., Almouzni G., Lipinski M.
      Mol. Cell. Biol. 18:5546-5556(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH HIRA, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    2. "HIRIP3 is a nuclear phosphoprotein interacting with and phosphorylated by the serine-threonine kinase CK2."
      Assrir N., Filhol O., Galisson F., Lipinski M.
      Biol. Chem. 388:391-398(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CK2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    3. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Neuroblastoma.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Skin.
    6. "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-125; SER-142; SER-143; SER-159; SER-160; SER-196; SER-199; SER-223; SER-227; SER-289 AND SER-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84; SER-87; SER-196; SER-227 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-100; SER-159; SER-160; SER-223; SER-227; SER-330; SER-332; SER-333; SER-357; THR-358; SER-359; SER-363 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-27; SER-125; SER-196; SER-199; SER-223; SER-227; SER-363; SER-370 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-159; SER-160; SER-196; SER-199; SER-227; SER-289; SER-291; SER-330; SER-332; SER-333; SER-550; SER-551 AND SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-142; SER-143; SER-159; SER-160; SER-196; SER-199; SER-223; SER-227; SER-289; SER-291; SER-330; SER-332; SER-333; SER-357; THR-358; SER-359; SER-363 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHIRP3_HUMAN
    AccessioniPrimary (citable) accession number: Q9BW71
    Secondary accession number(s): H3BSR3, O75707, O75708
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 110 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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

    External Data

    Dasty 3