Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P62306

- RUXF_HUMAN

UniProt

P62306 - RUXF_HUMAN

Protein

Small nuclear ribonucleoprotein F

Gene

SNRPF

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

    Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. histone mRNA metabolic process Source: Reactome
    3. mRNA 3'-end processing Source: Reactome
    4. mRNA splicing, via spliceosome Source: UniProtKB
    5. ncRNA metabolic process Source: Reactome
    6. RNA metabolic process Source: Reactome
    7. RNA splicing Source: UniProtKB
    8. spliceosomal snRNP assembly Source: UniProtKB
    9. termination of RNA polymerase II transcription Source: Reactome
    10. transcription from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_11066. snRNP Assembly.
    REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Small nuclear ribonucleoprotein F
    Short name:
    snRNP-F
    Alternative name(s):
    Sm protein F
    Short name:
    Sm-F
    Short name:
    SmF
    Gene namesi
    Name:SNRPF
    Synonyms:PBSCF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:11162. SNRPF.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Nucleus 1 Publication
    Note: SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. methylosome Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. pICln-Sm protein complex Source: UniProtKB
    6. small nuclear ribonucleoprotein complex Source: UniProtKB
    7. SMN-Sm protein complex Source: UniProtKB
    8. spliceosomal complex Source: UniProtKB
    9. U12-type spliceosomal complex Source: UniProtKB
    10. U1 snRNP Source: UniProtKB
    11. U4 snRNP Source: UniProtKB
    12. U7 snRNP Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36003.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 8685Small nuclear ribonucleoprotein FPRO_0000125536Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP62306.
    PaxDbiP62306.
    PeptideAtlasiP62306.
    PRIDEiP62306.

    PTM databases

    PhosphoSiteiP62306.

    Miscellaneous databases

    PMAP-CutDBP62306.

    Expressioni

    Gene expression databases

    ArrayExpressiP62306.
    BgeeiP62306.
    CleanExiHS_SNRPF.
    GenevestigatoriP62306.

    Interactioni

    Subunit structurei

    U1 snRNP is for instance composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Component of the heptameric ring U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CLNS1AP541054EBI-356900,EBI-724693
    SNRPEP623044EBI-356900,EBI-348082

    Protein-protein interaction databases

    BioGridi112520. 67 interactions.
    DIPiDIP-31221N.
    IntActiP62306. 27 interactions.
    MINTiMINT-1137229.
    STRINGi9606.ENSP00000266735.

    Structurei

    Secondary structure

    1
    86
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 148
    Beta strandi17 – 237
    Beta strandi28 – 369
    Beta strandi42 – 5110
    Beta strandi54 – 6411
    Helixi66 – 683
    Beta strandi69 – 746

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VU2X-ray3.10D/L/T/b/j/r/z1-86[»]
    1VU3X-ray3.10D/L/T/b/j/r1-86[»]
    2Y9AX-ray3.60F/M/T1-86[»]
    2Y9BX-ray3.60F/M/T1-86[»]
    2Y9CX-ray3.60F/M/T1-86[»]
    2Y9DX-ray3.60F/M/T1-86[»]
    3CW1X-ray5.491/2/F/Z1-86[»]
    3PGWX-ray4.40F/I1-86[»]
    3S6NX-ray2.50F1-86[»]
    4F77X-ray3.10D/L/T/b/j/r/z1-86[»]
    4F7UX-ray1.90F/I1-86[»]
    ProteinModelPortaliP62306.
    SMRiP62306. Positions 3-76.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62306.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1958.
    HOVERGENiHBG052369.
    InParanoidiP62306.
    KOiK11098.
    OMAiSTDGYMN.
    OrthoDBiEOG7HXCTK.
    PhylomeDBiP62306.
    TreeFamiTF314481.

    Family and domain databases

    InterProiIPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    IPR016487. snRNP_SmF.
    [Graphical view]
    PfamiPF01423. LSM. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006609. snRNP_SmF. 1 hit.
    SMARTiSM00651. Sm. 1 hit.
    [Graphical view]
    SUPFAMiSSF50182. SSF50182. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P62306-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLPLNPKPF LNGLTGKPVM VKLKWGMEYK GYLVSVDGYM NMQLANTEEY   50
    IDGALSGHLG EVLIRCNNVL YIRGVEEEEE DGEMRE 86
    Length:86
    Mass (Da):9,725
    Last modified:July 5, 2004 - v1
    Checksum:i416B88D575DAE58A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti86 – 861E → D in CAG33032. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85372 mRNA. Translation: CAA59688.1.
    CR456751 mRNA. Translation: CAG33032.1.
    AK311752 mRNA. Translation: BAG34695.1.
    CH471054 Genomic DNA. Translation: EAW97548.1.
    BC002505 mRNA. Translation: AAH02505.3.
    BC063397 mRNA. Translation: AAH63397.2.
    BC128452 mRNA. Translation: AAI28453.1.
    BC128453 mRNA. Translation: AAI28454.1.
    CCDSiCCDS9055.1.
    PIRiS55053.
    RefSeqiNP_003086.1. NM_003095.2.
    UniGeneiHs.105465.

    Genome annotation databases

    EnsembliENST00000266735; ENSP00000266735; ENSG00000139343.
    GeneIDi6636.
    KEGGihsa:6636.
    UCSCiuc001tej.3. human.

    Polymorphism databases

    DMDMi61237391.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85372 mRNA. Translation: CAA59688.1 .
    CR456751 mRNA. Translation: CAG33032.1 .
    AK311752 mRNA. Translation: BAG34695.1 .
    CH471054 Genomic DNA. Translation: EAW97548.1 .
    BC002505 mRNA. Translation: AAH02505.3 .
    BC063397 mRNA. Translation: AAH63397.2 .
    BC128452 mRNA. Translation: AAI28453.1 .
    BC128453 mRNA. Translation: AAI28454.1 .
    CCDSi CCDS9055.1.
    PIRi S55053.
    RefSeqi NP_003086.1. NM_003095.2.
    UniGenei Hs.105465.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VU2 X-ray 3.10 D/L/T/b/j/r/z 1-86 [» ]
    1VU3 X-ray 3.10 D/L/T/b/j/r 1-86 [» ]
    2Y9A X-ray 3.60 F/M/T 1-86 [» ]
    2Y9B X-ray 3.60 F/M/T 1-86 [» ]
    2Y9C X-ray 3.60 F/M/T 1-86 [» ]
    2Y9D X-ray 3.60 F/M/T 1-86 [» ]
    3CW1 X-ray 5.49 1/2/F/Z 1-86 [» ]
    3PGW X-ray 4.40 F/I 1-86 [» ]
    3S6N X-ray 2.50 F 1-86 [» ]
    4F77 X-ray 3.10 D/L/T/b/j/r/z 1-86 [» ]
    4F7U X-ray 1.90 F/I 1-86 [» ]
    ProteinModelPortali P62306.
    SMRi P62306. Positions 3-76.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112520. 67 interactions.
    DIPi DIP-31221N.
    IntActi P62306. 27 interactions.
    MINTi MINT-1137229.
    STRINGi 9606.ENSP00000266735.

    PTM databases

    PhosphoSitei P62306.

    Polymorphism databases

    DMDMi 61237391.

    Proteomic databases

    MaxQBi P62306.
    PaxDbi P62306.
    PeptideAtlasi P62306.
    PRIDEi P62306.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266735 ; ENSP00000266735 ; ENSG00000139343 .
    GeneIDi 6636.
    KEGGi hsa:6636.
    UCSCi uc001tej.3. human.

    Organism-specific databases

    CTDi 6636.
    GeneCardsi GC12P096252.
    HGNCi HGNC:11162. SNRPF.
    MIMi 603541. gene.
    neXtProti NX_P62306.
    PharmGKBi PA36003.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1958.
    HOVERGENi HBG052369.
    InParanoidi P62306.
    KOi K11098.
    OMAi STDGYMN.
    OrthoDBi EOG7HXCTK.
    PhylomeDBi P62306.
    TreeFami TF314481.

    Enzyme and pathway databases

    Reactomei REACT_11066. snRNP Assembly.
    REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi SNRPF. human.
    EvolutionaryTracei P62306.
    GeneWikii Small_nuclear_ribonucleoprotein_polypeptide_F.
    GenomeRNAii 6636.
    NextBioi 25853.
    PMAP-CutDB P62306.
    PROi P62306.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62306.
    Bgeei P62306.
    CleanExi HS_SNRPF.
    Genevestigatori P62306.

    Family and domain databases

    InterProi IPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    IPR016487. snRNP_SmF.
    [Graphical view ]
    Pfami PF01423. LSM. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006609. snRNP_SmF. 1 hit.
    SMARTi SM00651. Sm. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50182. SSF50182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions."
      Hermann H., Fabrizio P., Raker V.A., Foulaki K., Hornig H., Brahms H., Luehrmann R.
      EMBO J. 14:2076-2088(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cervix carcinoma.
    2. "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].
    3. "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].
      Tissue: Amygdala.
    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: Colon.
    6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-22 AND 66-86, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    7. "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein."
      Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.
      EMBO J. 20:5470-5479(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE U7 SNRNP COMPLEX.
    8. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    9. "The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
      Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
      RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
      Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
      Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN SMN-SM COMPLEX, SUBCELLULAR LOCATION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."
      Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.
      Nature 458:475-480(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) IN SPLICEOSOMAL U1 SNRNP.
    13. "Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis."
      Leung A.K., Nagai K., Li J.
      Nature 473:536-539(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN SPLICEOSOMAL CORE U4 SNRNP.
    14. "Structural basis of assembly chaperone-mediated snRNP formation."
      Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K., Stark H., Schindelin H., Fischer U.
      Mol. Cell 49:692-703(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN 6S PICLN-SM COMPLEX, FUNCTION IN CORE U1 SNRNP BIOGENESIS.

    Entry informationi

    Entry nameiRUXF_HUMAN
    AccessioniPrimary (citable) accession number: P62306
    Secondary accession number(s): A2VCR2
    , B2R498, Q15356, Q6IBQ1, Q6P4I0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 104 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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