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O43681

- ASNA_HUMAN

UniProt

O43681 - ASNA_HUMAN

Protein

ATPase ASNA1

Gene

ASNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting By similarity. May be involved in insulin signaling.2 PublicationsUniRule annotation

    Kineticsi

    1. KM=0.22 mM for ATP1 Publication

    Vmax=16.6 nmol/min/mg enzyme for ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei74 – 741UniRule annotation
    Binding sitei251 – 2511ATPUniRule annotation
    Binding sitei278 – 2781ATPUniRule annotation
    Metal bindingi289 – 2891Zinc; shared with dimeric partnerUniRule annotation
    Metal bindingi292 – 2921Zinc; shared with dimeric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi45 – 528ATPUniRule annotation

    GO - Molecular functioni

    1. arsenite transmembrane transporter activity Source: ProtInc
    2. ATPase activity Source: InterPro
    3. ATP binding Source: UniProtKB-HAMAP
    4. metal ion binding Source: UniProtKB-KW
    5. transporter activity Source: ProtInc

    GO - Biological processi

    1. inorganic anion transport Source: GOC
    2. protein insertion into ER membrane Source: UniProtKB-HAMAP
    3. transport Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Protein family/group databases

    TCDBi3.A.19.1.1. the tms recognition/insertion complex (trc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATPase ASNA1UniRule annotation (EC:3.6.-.-UniRule annotation)
    Alternative name(s):
    Arsenical pump-driving ATPaseUniRule annotation
    Arsenite-stimulated ATPaseUniRule annotation
    Transmembrane domain recognition complex 40 kDa ATPase subunit
    hARSA-I
    hASNA-I
    Gene namesi
    Name:ASNA1UniRule annotation
    Synonyms:ARSA, TRC40
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:752. ASNA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. endoplasmic reticulum Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt
    4. nucleolus Source: HPA
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 461G → R: Abolishes ATPase activity, dominantly inhibits the TA protein insertion pathway. 1 Publication

    Organism-specific databases

    PharmGKBiPA25051.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 348347ATPase ASNA1PRO_0000152253Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO43681.
    PaxDbiO43681.
    PRIDEiO43681.

    2D gel databases

    OGPiO43681.

    PTM databases

    PhosphoSiteiO43681.

    Expressioni

    Tissue specificityi

    Expressed in the epithelial cells of the liver, kidney, and stomach wall, in the adrenal medulla, in the islet cells of the pancreas, in the red pulp of the spleen, and in cardiac and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiO43681.
    BgeeiO43681.
    CleanExiHS_ARSA.
    HS_ASNA1.
    GenevestigatoriO43681.

    Organism-specific databases

    HPAiHPA045951.
    HPA048087.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Component of a transmembrane domain recognition complex (TRC) By similarity. Interacts with SERP1 and SEC61B By similarity. Interacts with WRB.3 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi106931. 18 interactions.
    IntActiO43681. 9 interactions.
    MINTiMINT-4656878.
    STRINGi9606.ENSP00000349887.

    Structurei

    3D structure databases

    ProteinModelPortaliO43681.
    SMRiO43681. Positions 27-342.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the arsA ATPase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0003.
    HOGENOMiHOG000197637.
    InParanoidiO43681.
    KOiK01551.
    OMAiMYRYLTV.
    OrthoDBiEOG79W95W.
    PhylomeDBiO43681.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    HAMAPiMF_03112. Asna1_Get3.
    InterProiIPR025723. Anion-transp_ATPase-like_dom.
    IPR016300. ATPase_ArsA/GET3.
    IPR027542. ATPase_ArsA/GET3_euk.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10803. PTHR10803. 1 hit.
    PfamiPF02374. ArsA_ATPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00345. GET3_arsA_TRC40. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    O43681-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAGVAGWGV EAEEFEDAPD VEPLEPTLSN IIEQRSLKWI FVGGKGGVGK    50
    TTCSCSLAVQ LSKGRESVLI ISTDPAHNIS DAFDQKFSKV PTKVKGYDNL 100
    FAMEIDPSLG VAELPDEFFE EDNMLSMGKK MMQEAMSAFP GIDEAMSYAE 150
    VMRLVKGMNF SVVVFDTAPT GHTLRLLNFP TIVERGLGRL MQIKNQISPF 200
    ISQMCNMLGL GDMNADQLAS KLEETLPVIR SVSEQFKDPE QTTFICVCIA 250
    EFLSLYETER LIQELAKCKI DTHNIIVNQL VFPDPEKPCK MCEARHKIQA 300
    KYLDQMEDLY EDFHIVKLPL LPHEVRGADK VNTFSALLLE PYKPPSAQ 348
    Length:348
    Mass (Da):38,793
    Last modified:May 30, 2000 - v2
    Checksum:iDA52C4ACC35C7A36
    GO

    Sequence cautioni

    The sequence AAC50731.1 differs from that shown. Reason: Frameshift at position 19.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti113 – 1142EL → DV in AAC50731. (PubMed:8884272)Curated
    Sequence conflicti205 – 2051C → F in AAC03551. 1 PublicationCurated
    Sequence conflicti303 – 3031L → P in BAD97083. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti332 – 3321N → S.1 Publication
    Corresponds to variant rs8177499 [ dbSNP | Ensembl ].
    VAR_018844

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047469 mRNA. Translation: AAC03551.1.
    AK291855 mRNA. Translation: BAF84544.1.
    AK223363 mRNA. Translation: BAD97083.1.
    AY304483 Genomic DNA. Translation: AAP45050.1.
    AC018761 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84303.1.
    BC002651 mRNA. Translation: AAH02651.1.
    U60276 mRNA. Translation: AAC50731.1. Frameshift.
    CCDSiCCDS32920.1.
    RefSeqiNP_004308.2. NM_004317.2.
    UniGeneiHs.465985.

    Genome annotation databases

    EnsembliENST00000357332; ENSP00000349887; ENSG00000198356.
    ENST00000591090; ENSP00000466379; ENSG00000198356.
    GeneIDi439.
    KEGGihsa:439.
    UCSCiuc002muv.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047469 mRNA. Translation: AAC03551.1 .
    AK291855 mRNA. Translation: BAF84544.1 .
    AK223363 mRNA. Translation: BAD97083.1 .
    AY304483 Genomic DNA. Translation: AAP45050.1 .
    AC018761 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84303.1 .
    BC002651 mRNA. Translation: AAH02651.1 .
    U60276 mRNA. Translation: AAC50731.1 . Frameshift.
    CCDSi CCDS32920.1.
    RefSeqi NP_004308.2. NM_004317.2.
    UniGenei Hs.465985.

    3D structure databases

    ProteinModelPortali O43681.
    SMRi O43681. Positions 27-342.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106931. 18 interactions.
    IntActi O43681. 9 interactions.
    MINTi MINT-4656878.
    STRINGi 9606.ENSP00000349887.

    Chemistry

    DrugBanki DB00171. Adenosine triphosphate.

    Protein family/group databases

    TCDBi 3.A.19.1.1. the tms recognition/insertion complex (trc) family.

    PTM databases

    PhosphoSitei O43681.

    2D gel databases

    OGPi O43681.

    Proteomic databases

    MaxQBi O43681.
    PaxDbi O43681.
    PRIDEi O43681.

    Protocols and materials databases

    DNASUi 439.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357332 ; ENSP00000349887 ; ENSG00000198356 .
    ENST00000591090 ; ENSP00000466379 ; ENSG00000198356 .
    GeneIDi 439.
    KEGGi hsa:439.
    UCSCi uc002muv.3. human.

    Organism-specific databases

    CTDi 439.
    GeneCardsi GC19P012848.
    HGNCi HGNC:752. ASNA1.
    HPAi HPA045951.
    HPA048087.
    MIMi 601913. gene.
    neXtProti NX_O43681.
    PharmGKBi PA25051.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0003.
    HOGENOMi HOG000197637.
    InParanoidi O43681.
    KOi K01551.
    OMAi MYRYLTV.
    OrthoDBi EOG79W95W.
    PhylomeDBi O43681.

    Miscellaneous databases

    ChiTaRSi ASNA1. human.
    GeneWikii ASNA1.
    GenomeRNAii 439.
    NextBioi 1839.
    PROi O43681.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43681.
    Bgeei O43681.
    CleanExi HS_ARSA.
    HS_ASNA1.
    Genevestigatori O43681.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    HAMAPi MF_03112. Asna1_Get3.
    InterProi IPR025723. Anion-transp_ATPase-like_dom.
    IPR016300. ATPase_ArsA/GET3.
    IPR027542. ATPase_ArsA/GET3_euk.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10803. PTHR10803. 1 hit.
    Pfami PF02374. ArsA_ATPase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00345. GET3_arsA_TRC40. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human homolog of bacterial and mouse arsenite translocating ATPase gene, ArsA."
      Hu G.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Salivary gland.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    4. NIEHS SNPs program
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-332.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Uterus.
    8. "Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter."
      Kurdi-Haidar B., Aebi S., Heath D., Enns R.E., Naredi P., Hom D.K., Howell S.B.
      Genomics 36:486-491(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-348.
    9. "Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I)."
      Kurdi-Haidar B., Heath D., Aebi S., Howell S.B.
      J. Biol. Chem. 273:22173-22176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    10. "Dual cytoplasmic and nuclear distribution of the novel arsenite-stimulated human ATPase (hASNA-I)."
      Kurdi-Haidar B., Hom D.K., Flittner D.E., Heath D., Fink L., Naredi P., Howell S.B.
      J. Cell. Biochem. 71:1-10(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Immunohistochemical analysis of the distribution of the human ATPase (hASNA-I) in normal tissues and its overexpression in breast adenomas and carcinomas."
      Kurdi-Haidar B., Heath D., Naredi P., Varki N., Howell S.B.
      J. Histochem. Cytochem. 46:1243-1248(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "Identification of a targeting factor for posttranslational membrane protein insertion into the ER."
      Stefanovic S., Hegde R.S.
      Cell 128:1147-1159(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE TRC COMPLEX, MUTAGENESIS OF GLY-46, SUBCELLULAR LOCATION, INTERACTION WITH SEC61B.
    13. "Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins."
      Favaloro V., Spasic M., Schwappach B., Dobberstein B.
      J. Cell Sci. 121:1832-1840(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SERP1 AND SEC61B.
    14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "WRB is the receptor for TRC40/Asna1-mediated insertion of tail-anchored proteins into the ER membrane."
      Vilardi F., Lorenz H., Dobberstein B.
      J. Cell Sci. 124:1301-1307(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WRB, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiASNA_HUMAN
    AccessioniPrimary (citable) accession number: O43681
    Secondary accession number(s): A6NHP8
    , A8K740, Q53FC6, Q92849
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 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 19
      Human chromosome 19: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3