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O15540

- FABP7_HUMAN

UniProt

O15540 - FABP7_HUMAN

Protein

Fatty acid-binding protein, brain

Gene

FABP7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers By similarity.By similarity

    GO - Molecular functioni

    1. lipid binding Source: ProtInc
    2. transporter activity Source: InterPro

    GO - Biological processi

    1. cell proliferation in forebrain Source: Ensembl
    2. epithelial cell proliferation Source: Ensembl
    3. negative regulation of cell proliferation Source: ProtInc
    4. nervous system development Source: ProtInc
    5. neurogenesis Source: Ensembl
    6. prepulse inhibition Source: Ensembl

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid-binding protein, brain
    Alternative name(s):
    Brain lipid-binding protein
    Short name:
    BLBP
    Brain-type fatty acid-binding protein
    Short name:
    B-FABP
    Fatty acid-binding protein 7
    Mammary-derived growth inhibitor related
    Gene namesi
    Name:FABP7
    Synonyms:BLBP, FABPB, MRG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:3562. FABP7.

    Subcellular locationi

    GO - Cellular componenti

    1. cell projection Source: Ensembl
    2. cytoplasm Source: UniProtKB-SubCell
    3. neuronal cell body Source: Ensembl
    4. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27963.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 132131Fatty acid-binding protein, brainPRO_0000067373Add
    BLAST

    Proteomic databases

    PaxDbiO15540.
    PRIDEiO15540.

    2D gel databases

    DOSAC-COBS-2DPAGEO15540.

    PTM databases

    PhosphoSiteiO15540.

    Expressioni

    Tissue specificityi

    Expressed in brain and other neural tissues.

    Gene expression databases

    ArrayExpressiO15540.
    BgeeiO15540.
    CleanExiHS_FABP7.
    GenevestigatoriO15540.

    Organism-specific databases

    HPAiCAB025488.
    CAB058697.
    HPA028825.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000357429.

    Structurei

    Secondary structure

    1
    132
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53
    Beta strandi7 – 1610
    Helixi17 – 237
    Helixi28 – 369
    Beta strandi40 – 467
    Beta strandi49 – 557
    Beta strandi63 – 653
    Beta strandi71 – 744
    Turni76 – 783
    Beta strandi80 – 889
    Beta strandi91 – 988
    Beta strandi101 – 11010
    Beta strandi113 – 1208
    Beta strandi123 – 1319

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FDQX-ray2.10A/B2-132[»]
    1FE3X-ray2.80A2-132[»]
    1JJXNMR-A2-132[»]
    ProteinModelPortaliO15540.
    SMRiO15540. Positions 2-132.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15540.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni127 – 1293Fatty acid binding

    Domaini

    Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG241430.
    HOGENOMiHOG000004829.
    HOVERGENiHBG005633.
    KOiK08756.
    OMAiPTIVISH.
    OrthoDBiEOG7NW6BZ.
    PhylomeDBiO15540.
    TreeFamiTF316894.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view]
    PfamiPF00061. Lipocalin. 1 hit.
    [Graphical view]
    PRINTSiPR00178. FATTYACIDBP.
    SUPFAMiSSF50814. SSF50814. 1 hit.
    PROSITEiPS00214. FABP. 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: O15540-1) [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

    MVEAFCATWK LTNSQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGDKV    50
    VIRTLSTFKN TEISFQLGEE FDETTADDRN CKSVVSLDGD KLVHIQKWDG 100
    KETNFVREIK DGKMVMTLTF GDVVAVRHYE KA 132
    Length:132
    Mass (Da):14,889
    Last modified:January 23, 2007 - v3
    Checksum:iF1E8EE12B9474B97
    GO
    Isoform 2 (identifier: O15540-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         117-132: TLTFGDVVAVRHYEKA → VSNDNSPFFLVFFSSPHTSHLLPSSSLLLPFFLLPSFFNNTSLARFFNYM

    Show »
    Length:166
    Mass (Da):18,829
    Checksum:i4E88C1139530F07A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601N → D in BAA23324. 1 PublicationCurated
    Sequence conflicti110 – 1101K → R in CAG33338. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti61 – 611T → M.
    Corresponds to variant rs2279381 [ dbSNP | Ensembl ].
    VAR_049012

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei117 – 13216TLTFG…HYEKA → VSNDNSPFFLVFFSSPHTSH LLPSSSLLLPFFLLPSFFNN TSLARFFNYM in isoform 2. 2 PublicationsVSP_055490Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002962 mRNA. Translation: CAA05773.1.
    D88648 mRNA. Translation: BAA23645.1.
    U51338 mRNA. Translation: AAB87141.1.
    D50373 mRNA. Translation: BAA23324.1.
    U81235 mRNA. Translation: AAD00507.1.
    CR457057 mRNA. Translation: CAG33338.1.
    AK289836 mRNA. Translation: BAF82525.1.
    AK311867 mRNA. Translation: BAG34808.1.
    AL512688 mRNA. Translation: CAC21646.1.
    AL645811 Genomic DNA. Translation: CAI15449.1.
    CH471051 Genomic DNA. Translation: EAW48166.1.
    CH471051 Genomic DNA. Translation: EAW48167.1.
    BC012299 mRNA. Translation: AAH12299.1.
    CCDSiCCDS5127.1.
    RefSeqiNP_001437.1. NM_001446.3.
    UniGeneiHs.26770.

    Genome annotation databases

    EnsembliENST00000356535; ENSP00000348931; ENSG00000164434. [O15540-2]
    ENST00000368444; ENSP00000357429; ENSG00000164434. [O15540-1]
    GeneIDi2173.
    KEGGihsa:2173.
    UCSCiuc003pzf.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002962 mRNA. Translation: CAA05773.1 .
    D88648 mRNA. Translation: BAA23645.1 .
    U51338 mRNA. Translation: AAB87141.1 .
    D50373 mRNA. Translation: BAA23324.1 .
    U81235 mRNA. Translation: AAD00507.1 .
    CR457057 mRNA. Translation: CAG33338.1 .
    AK289836 mRNA. Translation: BAF82525.1 .
    AK311867 mRNA. Translation: BAG34808.1 .
    AL512688 mRNA. Translation: CAC21646.1 .
    AL645811 Genomic DNA. Translation: CAI15449.1 .
    CH471051 Genomic DNA. Translation: EAW48166.1 .
    CH471051 Genomic DNA. Translation: EAW48167.1 .
    BC012299 mRNA. Translation: AAH12299.1 .
    CCDSi CCDS5127.1.
    RefSeqi NP_001437.1. NM_001446.3.
    UniGenei Hs.26770.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FDQ X-ray 2.10 A/B 2-132 [» ]
    1FE3 X-ray 2.80 A 2-132 [» ]
    1JJX NMR - A 2-132 [» ]
    ProteinModelPortali O15540.
    SMRi O15540. Positions 2-132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000357429.

    Chemistry

    DrugBanki DB00132. Alpha-Linolenic Acid.
    DB00154. gamma-Homolinolenic acid.
    DB00159. Icosapent.

    PTM databases

    PhosphoSitei O15540.

    2D gel databases

    DOSAC-COBS-2DPAGE O15540.

    Proteomic databases

    PaxDbi O15540.
    PRIDEi O15540.

    Protocols and materials databases

    DNASUi 2173.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356535 ; ENSP00000348931 ; ENSG00000164434 . [O15540-2 ]
    ENST00000368444 ; ENSP00000357429 ; ENSG00000164434 . [O15540-1 ]
    GeneIDi 2173.
    KEGGi hsa:2173.
    UCSCi uc003pzf.3. human.

    Organism-specific databases

    CTDi 2173.
    GeneCardsi GC06P123142.
    HGNCi HGNC:3562. FABP7.
    HPAi CAB025488.
    CAB058697.
    HPA028825.
    MIMi 602965. gene.
    neXtProti NX_O15540.
    PharmGKBi PA27963.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG241430.
    HOGENOMi HOG000004829.
    HOVERGENi HBG005633.
    KOi K08756.
    OMAi PTIVISH.
    OrthoDBi EOG7NW6BZ.
    PhylomeDBi O15540.
    TreeFami TF316894.

    Miscellaneous databases

    EvolutionaryTracei O15540.
    GeneWikii FABP7.
    GenomeRNAii 2173.
    NextBioi 8777.
    PROi O15540.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15540.
    Bgeei O15540.
    CleanExi HS_FABP7.
    Genevestigatori O15540.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR00178. FATTYACIDBP.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00214. FABP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human brain-type fatty acid binding protein shows high affinity for omega-3 fatty acids but not for omega-6 fatty acids."
      Schnuetgen F., Boerchers T., Xhong N., Godbout R., Sacchettini J.C., Spener F.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Isolation and expression of a cDNA for human brain fatty acid-binding protein (B-FABP)."
      Shimizu F., Watanabe T.K., Shinomiya H., Nakamura Y., Fujiwara T.
      Biochim. Biophys. Acta 1354:24-28(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Correlation of B-FABP and GFAP expression in malignant glioma."
      Godbout R., Bisgrove D.A., Shkolny D., Day R.S. III
      Oncogene 16:1955-1962(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retina.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    5. "Identification and characterization of a novel human tumor suppressor gene with homology to mammary derived growth inhibitor."
      Shi Y.E., Ni J.
      Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    9. "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].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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: Mammary gland.
    12. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 11-53; 60-79; 83-97 AND 114-127, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    13. "Crystal structure and thermodynamic analysis of human brain fatty acid-binding protein."
      Balendiran G.K., Schnuetgen F., Scapin G., Boerchers T., Xhong N., Lim K., Godbout R., Spener F., Sacchettini J.C.
      J. Biol. Chem. 275:27045-27054(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
    14. "Solution structure of fatty acid-binding protein from human brain."
      Rademacher M., Zimmerman A.W., Rueterjans H., Veerkamp J.H., Luecke C.
      Mol. Cell. Biochem. 239:61-68(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiFABP7_HUMAN
    AccessioniPrimary (citable) accession number: O15540
    Secondary accession number(s): B2R4L1
    , O14951, Q6IAU7, Q9H047
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 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

    3D-structure, Complete proteome, Direct protein sequencing, 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