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P25685

- DNJB1_HUMAN

UniProt

P25685 - DNJB1_HUMAN

Protein

DnaJ homolog subfamily B member 1

Gene

DNAJB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.

    GO - Molecular functioni

    1. ATPase activator activity Source: BHF-UCL
    2. ATPase binding Source: BHF-UCL
    3. chaperone binding Source: UniProt
    4. Hsp70 protein binding Source: BHF-UCL
    5. protein binding Source: IntAct
    6. unfolded protein binding Source: UniProt

    GO - Biological processi

    1. chaperone cofactor-dependent protein refolding Source: UniProtKB
    2. chaperone mediated protein folding requiring cofactor Source: Ensembl
    3. negative regulation of inclusion body assembly Source: UniProt
    4. positive regulation of ATPase activity Source: BHF-UCL
    5. response to unfolded protein Source: ProtInc

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    ReactomeiREACT_200624. Attenuation phase.
    REACT_200775. HSF1-dependent transactivation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DnaJ homolog subfamily B member 1
    Alternative name(s):
    DnaJ protein homolog 1
    Heat shock 40 kDa protein 1
    Short name:
    HSP40
    Short name:
    Heat shock protein 40
    Human DnaJ protein 1
    Short name:
    hDj-1
    Gene namesi
    Name:DNAJB1
    Synonyms:DNAJ1, HDJ1, HSPF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:5270. DNAJB1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. Nucleusnucleolus 1 Publication
    Note: Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock.

    GO - Cellular componenti

    1. cytosol Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. nucleolus Source: UniProtKB-SubCell
    4. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27412.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 340339DnaJ homolog subfamily B member 1PRO_0000071016Add
    BLAST

    Proteomic databases

    MaxQBiP25685.
    PaxDbiP25685.
    PeptideAtlasiP25685.
    PRIDEiP25685.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00015947.

    PTM databases

    PhosphoSiteiP25685.

    Expressioni

    Inductioni

    By heat shock.1 Publication

    Gene expression databases

    ArrayExpressiP25685.
    BgeeiP25685.
    CleanExiHS_DNAJB1.
    GenevestigatoriP25685.

    Organism-specific databases

    HPAiCAB017450.

    Interactioni

    Subunit structurei

    Interacts with DNAJC3. Interacts with SRPK1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Phlda1Q623922EBI-357034,EBI-309727From a different organism.

    Protein-protein interaction databases

    BioGridi109569. 55 interactions.
    DIPiDIP-41180N.
    IntActiP25685. 30 interactions.
    MINTiMINT-204558.
    STRINGi9606.ENSP00000254322.

    Structurei

    Secondary structure

    1
    340
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 94
    Helixi17 – 2913
    Turni33 – 353
    Helixi41 – 5414
    Helixi58 – 669
    Helixi69 – 713
    Beta strandi166 – 1705
    Helixi172 – 1776
    Beta strandi179 – 19012
    Turni191 – 1933
    Beta strandi197 – 20812
    Beta strandi217 – 2204
    Beta strandi228 – 2303
    Beta strandi235 – 2417
    Beta strandi248 – 2503
    Beta strandi253 – 2619
    Helixi262 – 2676
    Beta strandi269 – 2746
    Beta strandi280 – 2856
    Beta strandi294 – 2974
    Beta strandi305 – 3073
    Beta strandi314 – 3218
    Helixi328 – 33710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HDJNMR-A1-76[»]
    2QLDX-ray2.70A158-340[»]
    3AGXX-ray1.85A/B161-340[»]
    3AGYX-ray1.85A/B161-340[»]
    3AGZX-ray2.51A/B151-340[»]
    ProteinModelPortaliP25685.
    SMRiP25685. Positions 1-340.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25685.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7069JPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 J domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2214.
    HOGENOMiHOG000226718.
    HOVERGENiHBG066727.
    InParanoidiP25685.
    KOiK09507.
    OMAiNPFDNFF.
    OrthoDBiEOG7TF79F.
    PhylomeDBiP25685.
    TreeFamiTF105141.

    Family and domain databases

    Gene3Di1.10.287.110. 1 hit.
    InterProiIPR002939. DnaJ_C.
    IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR008971. HSP40/DnaJ_pept-bd.
    [Graphical view]
    PfamiPF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    [Graphical view]
    PRINTSiPR00625. JDOMAIN.
    SMARTiSM00271. DnaJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 2 hits.
    PROSITEiPS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P25685-1) [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

    MGKDYYQTLG LARGASDEEI KRAYRRQALR YHPDKNKEPG AEEKFKEIAE    50
    AYDVLSDPRK REIFDRYGEE GLKGSGPSGG SGGGANGTSF SYTFHGDPHA 100
    MFAEFFGGRN PFDTFFGQRN GEEGMDIDDP FSGFPMGMGG FTNVNFGRSR 150
    SAQEPARKKQ DPPVTHDLRV SLEEIYSGCT KKMKISHKRL NPDGKSIRNE 200
    DKILTIEVKK GWKEGTKITF PKEGDQTSNN IPADIVFVLK DKPHNIFKRD 250
    GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE 300
    GLPLPKTPEK RGDLIIEFEV IFPERIPQTS RTVLEQVLPI 340
    Length:340
    Mass (Da):38,044
    Last modified:January 23, 2007 - v4
    Checksum:i17545098B0C196DF
    GO
    Isoform 2 (identifier: P25685-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:240
    Mass (Da):27,016
    Checksum:i760FFA819B48174B
    GO

    Sequence cautioni

    The sequence CAA44287.1 differs from that shown. Reason: Frameshift at positions 11, 28, 81 and 136.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681G → L in CAA44287. (PubMed:1754405)Curated
    Sequence conflicti150 – 1501R → C in CAA44287. (PubMed:1754405)Curated
    Sequence conflicti183 – 1831M → T in CAA44287. (PubMed:1754405)Curated
    Sequence conflicti320 – 3201V → A in CAA44287. (PubMed:1754405)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_056414Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62421 mRNA. Translation: CAA44287.1. Frameshift.
    D49547 mRNA. Translation: BAA08495.1.
    D85429 Genomic DNA. Translation: BAA12819.1.
    AK301817 mRNA. Translation: BAG63264.1.
    AC009004 Genomic DNA. No translation available.
    AC012318 Genomic DNA. No translation available.
    BC002352 mRNA. Translation: AAH02352.1.
    BC019827 mRNA. Translation: AAH19827.1.
    CCDSiCCDS12312.1.
    PIRiJN0912.
    S20062.
    RefSeqiNP_006136.1. NM_006145.1.
    XP_006722796.1. XM_006722733.1.
    UniGeneiHs.515210.

    Genome annotation databases

    EnsembliENST00000254322; ENSP00000254322; ENSG00000132002.
    ENST00000396969; ENSP00000444212; ENSG00000132002.
    GeneIDi3337.
    KEGGihsa:3337.
    UCSCiuc002myz.1. human.

    Polymorphism databases

    DMDMi1706473.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62421 mRNA. Translation: CAA44287.1 . Frameshift.
    D49547 mRNA. Translation: BAA08495.1 .
    D85429 Genomic DNA. Translation: BAA12819.1 .
    AK301817 mRNA. Translation: BAG63264.1 .
    AC009004 Genomic DNA. No translation available.
    AC012318 Genomic DNA. No translation available.
    BC002352 mRNA. Translation: AAH02352.1 .
    BC019827 mRNA. Translation: AAH19827.1 .
    CCDSi CCDS12312.1.
    PIRi JN0912.
    S20062.
    RefSeqi NP_006136.1. NM_006145.1.
    XP_006722796.1. XM_006722733.1.
    UniGenei Hs.515210.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HDJ NMR - A 1-76 [» ]
    2QLD X-ray 2.70 A 158-340 [» ]
    3AGX X-ray 1.85 A/B 161-340 [» ]
    3AGY X-ray 1.85 A/B 161-340 [» ]
    3AGZ X-ray 2.51 A/B 151-340 [» ]
    ProteinModelPortali P25685.
    SMRi P25685. Positions 1-340.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109569. 55 interactions.
    DIPi DIP-41180N.
    IntActi P25685. 30 interactions.
    MINTi MINT-204558.
    STRINGi 9606.ENSP00000254322.

    PTM databases

    PhosphoSitei P25685.

    Polymorphism databases

    DMDMi 1706473.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00015947.

    Proteomic databases

    MaxQBi P25685.
    PaxDbi P25685.
    PeptideAtlasi P25685.
    PRIDEi P25685.

    Protocols and materials databases

    DNASUi 3337.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254322 ; ENSP00000254322 ; ENSG00000132002 .
    ENST00000396969 ; ENSP00000444212 ; ENSG00000132002 .
    GeneIDi 3337.
    KEGGi hsa:3337.
    UCSCi uc002myz.1. human.

    Organism-specific databases

    CTDi 3337.
    GeneCardsi GC19M014625.
    H-InvDB HIX0014838.
    HGNCi HGNC:5270. DNAJB1.
    HPAi CAB017450.
    MIMi 604572. gene.
    neXtProti NX_P25685.
    PharmGKBi PA27412.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2214.
    HOGENOMi HOG000226718.
    HOVERGENi HBG066727.
    InParanoidi P25685.
    KOi K09507.
    OMAi NPFDNFF.
    OrthoDBi EOG7TF79F.
    PhylomeDBi P25685.
    TreeFami TF105141.

    Enzyme and pathway databases

    Reactomei REACT_200624. Attenuation phase.
    REACT_200775. HSF1-dependent transactivation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.

    Miscellaneous databases

    ChiTaRSi DNAJB1. human.
    EvolutionaryTracei P25685.
    GeneWikii DNAJB1.
    GenomeRNAii 3337.
    NextBioi 13208.
    PROi P25685.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25685.
    Bgeei P25685.
    CleanExi HS_DNAJB1.
    Genevestigatori P25685.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    InterProi IPR002939. DnaJ_C.
    IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR008971. HSP40/DnaJ_pept-bd.
    [Graphical view ]
    Pfami PF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    [Graphical view ]
    PRINTSi PR00625. JDOMAIN.
    SMARTi SM00271. DnaJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 2 hits.
    PROSITEi PS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human homologue of the Escherichia coli DnaJ heat-shock protein."
      Raabe T., Manley J.L.
      Nucleic Acids Res. 19:6645-6645(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ."
      Ohtsuka K.
      Biochem. Biophys. Res. Commun. 197:235-240(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-48.
      Tissue: Placenta.
    3. "Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2."
      Hata M., Okumura K., Seto M., Ohtsuka K.
      Genomics 38:446-449(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    4. "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 2).
      Tissue: Testis.
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain and Lung.
    7. "Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells."
      Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T., Tanabe K., Ohtsuka K.
      Cell Struct. Funct. 17:77-86(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-49, INDUCTION, SUBCELLULAR LOCATION.
    8. "The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity."
      Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I., Katze M.G.
      J. Biol. Chem. 274:3797-3803(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAJC3.
    9. "Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones."
      Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.
      Genes Dev. 23:482-495(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRPK1.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain."
      Qian Y.Q., Patel D., Hartl F.-U., McColl D.J.
      J. Mol. Biol. 260:224-235(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-76.

    Entry informationi

    Entry nameiDNJB1_HUMAN
    AccessioniPrimary (citable) accession number: P25685
    Secondary accession number(s): B4DX52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 154 of the entry and version 4 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3