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Q9R207

- NBN_MOUSE

UniProt

Q9R207 - NBN_MOUSE

Protein

Nibrin

Gene

Nbn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability. Forms a complex with RBBP8 to link DNA double-strand break sensing to resection. Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex By similarity.By similarity

    GO - Molecular functioni

    1. ATP-dependent DNA helicase activity Source: Ensembl
    2. damaged DNA binding Source: MGI
    3. protein N-terminus binding Source: UniProtKB
    4. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. blastocyst growth Source: UniProtKB
    2. cell proliferation Source: MGI
    3. DNA damage checkpoint Source: MGI
    4. double-strand break repair Source: UniProtKB
    5. intrinsic apoptotic signaling pathway Source: MGI
    6. in utero embryonic development Source: UniProtKB
    7. isotype switching Source: UniProtKB
    8. meiotic nuclear division Source: UniProtKB-KW
    9. mitotic cell cycle checkpoint Source: UniProtKB
    10. mitotic G2 DNA damage checkpoint Source: UniProtKB
    11. neuromuscular process controlling balance Source: MGI
    12. positive regulation of kinase activity Source: Ensembl
    13. positive regulation of protein autophosphorylation Source: Ensembl
    14. regulation of fibroblast proliferation Source: UniProtKB
    15. telomere maintenance Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA repair, Meiosis

    Enzyme and pathway databases

    ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nibrin
    Alternative name(s):
    Cell cycle regulatory protein p95
    Nijmegen breakage syndrome protein 1 homolog
    Gene namesi
    Name:Nbn
    Synonyms:Nbs1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1351625. Nbn.

    Subcellular locationi

    Nucleus. NucleusPML body By similarity. Chromosometelomere By similarity
    Note: Localizes to discrete nuclear foci after treatment with genotoxic agents.By similarity

    GO - Cellular componenti

    1. Mre11 complex Source: UniProtKB
    2. nuclear chromosome, telomeric region Source: Ensembl
    3. nuclear inclusion body Source: UniProtKB
    4. nucleolus Source: Ensembl
    5. nucleus Source: MGI
    6. PML body Source: UniProtKB-SubCell
    7. replication fork Source: MGI
    8. site of double-strand break Source: Ensembl

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 751751NibrinPRO_0000231044Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei343 – 3431Phosphoserine; by ATM1 Publication
    Modified residuei398 – 3981PhosphoserineBy similarity
    Modified residuei433 – 4331PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by ATM in response of ionizing radiation, and such phosphorylation is responsible intra-S phase checkpoint control and telomere maintenance.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9R207.
    PRIDEiQ9R207.

    PTM databases

    PhosphoSiteiQ9R207.

    Expressioni

    Tissue specificityi

    High expression in the liver, heart and testis. Low expression in all other tissues analyzed. In the cerebellum the postmitotic Purkinje cells are marked specifically.1 Publication

    Developmental stagei

    A low level of expression is observed in all tissues. Highly specific expression was observed in organs with physiologic DNA double strand breakage (DSB), such as testis, thymus and spleen. Enhanced expression is also found at sites of high proliferative activity. These are the subventricular layer of the telencephalon and the diencephalon, the liver, lung, kidney and gut, as well as striated and smooth muscle cells in various organs.1 Publication

    Gene expression databases

    ArrayExpressiQ9R207.
    BgeeiQ9R207.
    CleanExiMM_NBN.
    GenevestigatoriQ9R207.

    Interactioni

    Subunit structurei

    Component of the MRN complex composed of two heterodimers RAD50/MRE11A associated with a single NBN. Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50 and MRE11A. Interacts with histone H2AFX this requires phosphorylation of H2AFX on 'Ser-139'. Interacts with HJURP, INTS3, KPNA2 and TERF2. Interacts with RBBP8; the interaction links the role of the MRN complex in DNA double-strand break sensing to resection. Interacts with SP100; recruits NBN to PML bodies. Interacts with ATF2. Interacts with MTOR, MAPKAP1 isoform 2 and RICTOR; indicative for an association with the mTORC2 complex.1 Publication

    Protein-protein interaction databases

    BioGridi205163. 7 interactions.
    DIPiDIP-46804N.
    IntActiQ9R207. 1 interaction.
    MINTiMINT-4084511.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R207.
    SMRiQ9R207. Positions 217-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 8360FHAPROSITE-ProRule annotationAdd
    BLAST
    Domaini105 – 18177BRCTAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni111 – 328218Mediates interaction with SP100Add
    BLAST
    Regioni221 – 403183Interaction with MTOR, MAPKAP1 and RICTORBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi461 – 4677Nuclear localization signalBy similarity
    Motifi734 – 7418EEXXXDDL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi449 – 4524Poly-Gln

    Domaini

    The FHA and BRCT domains are likely to have a crucial role for both binding to histone H2AFX and for relocalization of MRE11/RAD50 complex to the vicinity of DNA damage.By similarity
    The C-terminal domain contains a MRE11-binding site, and this interaction is required for the nuclear localization of the MRN complex.By similarity
    The EEXXXDDL motif at the C-terminus is required for the interaction with ATM and its recruitment to sites of DNA damage and promote the phosphorylation of ATM substrates, leading to the events of DNA damage response.By similarity

    Sequence similaritiesi

    Contains 1 BRCT domain.Curated
    Contains 1 FHA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG84999.
    GeneTreeiENSGT00390000000521.
    HOGENOMiHOG000231654.
    HOVERGENiHBG053070.
    InParanoidiQ9R207.
    KOiK10867.
    OMAiKLPHIIG.
    OrthoDBiEOG7B5WV7.
    PhylomeDBiQ9R207.
    TreeFamiTF101103.

    Family and domain databases

    Gene3Di2.60.200.20. 1 hit.
    3.40.50.10190. 1 hit.
    InterProiIPR001357. BRCT_dom.
    IPR013908. DNA-repair_Nbs1_C.
    IPR000253. FHA_dom.
    IPR016592. Nibrin_met.
    IPR008984. SMAD_FHA_domain.
    [Graphical view]
    PfamiPF00498. FHA. 1 hit.
    PF08599. Nbs1_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF011869. Nibrin_animal. 1 hit.
    SMARTiSM00292. BRCT. 1 hit.
    SM00240. FHA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    SSF52113. SSF52113. 1 hit.
    PROSITEiPS50006. FHA_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9R207-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWKLLPAAGA APGEPYRLLA GVEYVVGRKN CGILIENDQS ISRNHAVLTV    50
    NFPVTSLSQT DEIPTLTIKD NSKYGTFVNE EKMQTGLSCT LKTGDRVTFG 100
    VFESKFRVEY EPLVVCSSCL DVSGKTVLNQ AILQLGGLTA NNWTEECTHL 150
    VMSAVKVTIK TICALICGRP IIKPEYFSEF LKAVESKKQP PDIESFYPPI 200
    DEPAIGSKSV DLSGRHERKQ IFKGKTFVFL NAKQHKKLSS AVAFGGGEAR 250
    LMAEDDEEEQ SFFSAPGTCV VDVGITNTQL IISHSQKKWI HLIMDTLQRN 300
    GLRPIPEAEI GLAVIFMTTE NYCNPQGQPC TELKTTTPGP SLSQVLSANG 350
    KIIPSAPVNM TTYVADTESE PADTCMPLSE RPEEVKIPGL EQSSRKLSQE 400
    TFNIKEAPKP SSKANNVASD TLVRGKTPSY QLSPMKFPVA NKNKDWTSQQ 450
    QQNSIKNYFQ PCTRKRERDE DNPELSSCKS SRMELSCSLL EQTQPAGPSL 500
    WKSKEHQSQN ATLDREADTS SVGGMDIELN RKSPDRKPLP TETLRPRKRK 550
    DVDLATEEEV LEELLRSTKP ELAVQVKVEK QEADDTIRKK PRMDAERNRP 600
    LNGGSEPESN SALQEDEREK KDELQTESWS TKHEIANSDG LQDSSEELPR 650
    KLLLTEFRSL VVSNHNSTSR NLCVNECGPL KNFKKFKKAT FPGAGKLPHI 700
    IGGSDLVGHH ARKNTELEEW LKQEMEVQKQ QAKEESLADD LFRYNPNVKR 750
    R 751
    Length:751
    Mass (Da):83,795
    Last modified:May 1, 2000 - v1
    Checksum:iC9F597CC08227B2C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91G → S in AAH44773. (PubMed:15489334)Curated
    Sequence conflicti11 – 122AP → SL in AAC62113. 1 PublicationCurated
    Sequence conflicti325 – 3251P → Q in BAE22356. (PubMed:16141072)Curated
    Sequence conflicti366 – 3661D → E in BAA76298. 1 PublicationCurated
    Sequence conflicti455 – 4551I → F in BAA76298. 1 PublicationCurated
    Sequence conflicti513 – 5131L → Q in AAH44773. (PubMed:15489334)Curated
    Sequence conflicti664 – 6641N → K in AAH44773. (PubMed:15489334)Curated
    Sequence conflicti676 – 6761E → D in AAH44773. (PubMed:15489334)Curated
    Sequence conflicti679 – 6791P → S in AAH44773. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076687 mRNA. Translation: AAD20943.1.
    AB016988 mRNA. Translation: BAA76298.1.
    AF092840 mRNA. Translation: AAC62113.1.
    BC044773 mRNA. Translation: AAH44773.1.
    BC055061 mRNA. Translation: AAH55061.1.
    AK134960 mRNA. Translation: BAE22356.1.
    AK031933 mRNA. Translation: BAC27610.1.
    CCDSiCCDS17986.1.
    RefSeqiNP_038780.3. NM_013752.3.
    UniGeneiMm.20866.

    Genome annotation databases

    EnsembliENSMUST00000029879; ENSMUSP00000029879; ENSMUSG00000028224.
    GeneIDi27354.
    KEGGimmu:27354.
    UCSCiuc008sbn.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076687 mRNA. Translation: AAD20943.1 .
    AB016988 mRNA. Translation: BAA76298.1 .
    AF092840 mRNA. Translation: AAC62113.1 .
    BC044773 mRNA. Translation: AAH44773.1 .
    BC055061 mRNA. Translation: AAH55061.1 .
    AK134960 mRNA. Translation: BAE22356.1 .
    AK031933 mRNA. Translation: BAC27610.1 .
    CCDSi CCDS17986.1.
    RefSeqi NP_038780.3. NM_013752.3.
    UniGenei Mm.20866.

    3D structure databases

    ProteinModelPortali Q9R207.
    SMRi Q9R207. Positions 217-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 205163. 7 interactions.
    DIPi DIP-46804N.
    IntActi Q9R207. 1 interaction.
    MINTi MINT-4084511.

    PTM databases

    PhosphoSitei Q9R207.

    Proteomic databases

    PaxDbi Q9R207.
    PRIDEi Q9R207.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029879 ; ENSMUSP00000029879 ; ENSMUSG00000028224 .
    GeneIDi 27354.
    KEGGi mmu:27354.
    UCSCi uc008sbn.1. mouse.

    Organism-specific databases

    CTDi 4683.
    MGIi MGI:1351625. Nbn.

    Phylogenomic databases

    eggNOGi NOG84999.
    GeneTreei ENSGT00390000000521.
    HOGENOMi HOG000231654.
    HOVERGENi HBG053070.
    InParanoidi Q9R207.
    KOi K10867.
    OMAi KLPHIIG.
    OrthoDBi EOG7B5WV7.
    PhylomeDBi Q9R207.
    TreeFami TF101103.

    Enzyme and pathway databases

    Reactomei REACT_188819. DNA Damage/Telomere Stress Induced Senescence.

    Miscellaneous databases

    NextBioi 305208.
    PROi Q9R207.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9R207.
    Bgeei Q9R207.
    CleanExi MM_NBN.
    Genevestigatori Q9R207.

    Family and domain databases

    Gene3Di 2.60.200.20. 1 hit.
    3.40.50.10190. 1 hit.
    InterProi IPR001357. BRCT_dom.
    IPR013908. DNA-repair_Nbs1_C.
    IPR000253. FHA_dom.
    IPR016592. Nibrin_met.
    IPR008984. SMAD_FHA_domain.
    [Graphical view ]
    Pfami PF00498. FHA. 1 hit.
    PF08599. Nbs1_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF011869. Nibrin_animal. 1 hit.
    SMARTi SM00292. BRCT. 1 hit.
    SM00240. FHA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    SSF52113. SSF52113. 1 hit.
    PROSITEi PS50006. FHA_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification, characterization, and mapping of a mouse homolog of the gene mutated in Nijmegen breakage syndrome."
      Vissinga C.S., Yeo T.C., Woessner J., Massa H.F., Wilson R.K., Trask B.J., Concannon P.
      Cytogenet. Cell Genet. 87:80-84(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structure of the mouse Nijmegen breakage syndrome (Nibrin/Nbs1) protein."
      Saito T.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain and Testis.
    3. "Isolation of 50 cDNAs differentially expressed in embryonic forebrain as compared to mid and hindbrain: a strategy to identify candidate genes involved in human neurodevelopmental diseases."
      Mas C., Bourgeois F., Simonneau M.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain stem.
    4. "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].
      Strain: Czech II and FVB/N.
      Tissue: Colon and Mammary gland.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-613.
      Strain: C57BL/6J.
      Tissue: Medulla oblongata.
    6. "Expression pattern of the Nijmegen breakage syndrome gene, Nbs1, during murine development."
      Wilda M., Demuth I., Concannon P., Sperling K., Hameister H.
      Hum. Mol. Genet. 9:1739-1744(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. "Recruitment of NBS1 into PML oncogenic domains via interaction with SP100 protein."
      Naka K., Ikeda K., Motoyama N.
      Biochem. Biophys. Res. Commun. 299:863-871(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SP100.
    8. "Mice lacking protein phosphatase 5 are defective in ataxia telangiectasia mutated (ATM)-mediated cell cycle arrest."
      Yong W., Bao S., Chen H., Li D., Sanchez E.R., Shou W.
      J. Biol. Chem. 282:14690-14694(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-343.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiNBN_MOUSE
    AccessioniPrimary (citable) accession number: Q9R207
    Secondary accession number(s): O88981
    , Q3UY57, Q811I6, Q8CCY0, Q9R1X1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3