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Q13636

- RAB31_HUMAN

UniProt

Q13636 - RAB31_HUMAN

Protein

Ras-related protein Rab-31

Gene

RAB31

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Required for the integrity and for normal function of the Golgi apparatus and the trans-Golgi network. Plays a role in insulin-stimulated translocation of GLUT4 to the cell membrane. Plays a role in M6PR transport from the trans-Golgi network to endosomes. Plays a role in the internalization of EGFR from the cell membrane into endosomes. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 198GTP
    Nucleotide bindingi60 – 645GTP
    Nucleotide bindingi118 – 1214GTP

    GO - Molecular functioni

    1. GDP binding Source: UniProtKB
    2. GTPase activity Source: ProtInc
    3. GTP binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to insulin stimulus Source: UniProtKB
    2. Golgi to plasma membrane protein transport Source: UniProtKB
    3. GTP catabolic process Source: GOC
    4. phagosome maturation Source: UniProtKB
    5. receptor internalization Source: UniProtKB
    6. regulated secretory pathway Source: UniProtKB
    7. small GTPase mediated signal transduction Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-31
    Alternative name(s):
    Ras-related protein Rab-22B
    Gene namesi
    Name:RAB31
    Synonyms:RAB22B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:9771. RAB31.

    Subcellular locationi

    Golgi apparatustrans-Golgi network. Golgi apparatustrans-Golgi network membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Early endosome. Cytoplasmic vesiclephagosome. Cytoplasmic vesiclephagosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
    Note: Rapidly recruited to phagosomes containing S.aureus or M.tuberculosis.

    GO - Cellular componenti

    1. early endosome Source: UniProtKB
    2. phagocytic vesicle Source: UniProtKB
    3. phagocytic vesicle membrane Source: UniProtKB-SubCell
    4. trans-Golgi network membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641Q → L: No change in GTPase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34122.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 194194Ras-related protein Rab-31PRO_0000121232Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei35 – 351Phosphoserine1 Publication
    Lipidationi193 – 1931S-geranylgeranyl cysteineBy similarity
    Lipidationi194 – 1941S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Lipoprotein, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiQ13636.
    PaxDbiQ13636.
    PRIDEiQ13636.

    PTM databases

    PhosphoSiteiQ13636.

    Expressioni

    Tissue specificityi

    Highest expression in placenta and brain with lower levels in heart and lung. Not detected in liver, skeletal muscle, kidney or pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ13636.
    BgeeiQ13636.
    CleanExiHS_RAB31.
    GenevestigatoriQ13636.

    Organism-specific databases

    HPAiHPA019717.

    Interactioni

    Subunit structurei

    Interacts with OCRL. Interacts with NGFR By similarity. Interacts (in GDP-bound form) with RIN3 and GAPVD1, which function as guanine exchange factors (GEF). Interacts (in GTP-bound form) with EEA1. Interacts with EGFR.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi116221. 18 interactions.
    IntActiQ13636. 3 interactions.
    MINTiMINT-1404598.
    STRINGi9606.ENSP00000304565.

    Structurei

    Secondary structure

    1
    194
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 129
    Helixi18 – 2710
    Beta strandi38 – 4811
    Beta strandi50 – 6112
    Helixi65 – 717
    Helixi72 – 754
    Beta strandi79 – 868
    Helixi91 – 10616
    Beta strandi112 – 1187
    Helixi120 – 1256
    Helixi130 – 1389
    Turni139 – 1413
    Beta strandi143 – 1464
    Turni149 – 1524
    Helixi155 – 16410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FG5X-ray2.80A2-174[»]
    ProteinModelPortaliQ13636.
    SMRiQ13636. Positions 3-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13636.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi34 – 429Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOVERGENiHBG009351.
    InParanoidiQ13636.
    KOiK07891.
    OMAiIKLGKQT.
    OrthoDBiEOG77DJ7M.
    PhylomeDBiQ13636.
    TreeFamiTF331262.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view]
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00175. RAB. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51419. RAB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q13636-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIRELKVCL LGDTGVGKSS IVCRFVQDHF DHNISPTIGA SFMTKTVPCG    50
    NELHKFLIWD TAGQERFHSL APMYYRGSAA AVIVYDITKQ DSFYTLKKWV 100
    KELKEHGPEN IVMAIAGNKC DLSDIREVPL KDAKEYAESI GAIVVETSAK 150
    NAINIEELFQ GISRQIPPLD PHENGNNGTI KVEKPTMQAS RRCC 194
    Length:194
    Mass (Da):21,569
    Last modified:November 1, 1997 - v1
    Checksum:i19825648A9C214B9
    GO

    Sequence cautioni

    The sequence AAG09690.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH01148.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti189 – 1891A → S in AAC50773. (PubMed:8863739)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U57091 mRNA. Translation: AAC50773.1.
    U59877 mRNA. Translation: AAB02832.1.
    AF234995 mRNA. Translation: AAG13847.1.
    AF183421 mRNA. Translation: AAG09690.1. Different initiation.
    AF498957 mRNA. Translation: AAM21105.1.
    AK314809 mRNA. Translation: BAG37334.1.
    BT020027 mRNA. Translation: AAV38830.1.
    BT020028 mRNA. Translation: AAV38831.1.
    CR407659 mRNA. Translation: CAG28587.1.
    AC006238 Genomic DNA. No translation available.
    AP000902 Genomic DNA. No translation available.
    BC001148 mRNA. Translation: AAH01148.1. Different initiation.
    PIRiJC4961.
    RefSeqiNP_006859.2. NM_006868.3.
    UniGeneiHs.744887.
    Hs.99528.

    Genome annotation databases

    EnsembliENST00000578921; ENSP00000461945; ENSG00000168461.
    GeneIDi11031.
    KEGGihsa:11031.
    UCSCiuc002kog.2. human.

    Polymorphism databases

    DMDMi2500069.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U57091 mRNA. Translation: AAC50773.1 .
    U59877 mRNA. Translation: AAB02832.1 .
    AF234995 mRNA. Translation: AAG13847.1 .
    AF183421 mRNA. Translation: AAG09690.1 . Different initiation.
    AF498957 mRNA. Translation: AAM21105.1 .
    AK314809 mRNA. Translation: BAG37334.1 .
    BT020027 mRNA. Translation: AAV38830.1 .
    BT020028 mRNA. Translation: AAV38831.1 .
    CR407659 mRNA. Translation: CAG28587.1 .
    AC006238 Genomic DNA. No translation available.
    AP000902 Genomic DNA. No translation available.
    BC001148 mRNA. Translation: AAH01148.1 . Different initiation.
    PIRi JC4961.
    RefSeqi NP_006859.2. NM_006868.3.
    UniGenei Hs.744887.
    Hs.99528.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FG5 X-ray 2.80 A 2-174 [» ]
    ProteinModelPortali Q13636.
    SMRi Q13636. Positions 3-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116221. 18 interactions.
    IntActi Q13636. 3 interactions.
    MINTi MINT-1404598.
    STRINGi 9606.ENSP00000304565.

    PTM databases

    PhosphoSitei Q13636.

    Polymorphism databases

    DMDMi 2500069.

    Proteomic databases

    MaxQBi Q13636.
    PaxDbi Q13636.
    PRIDEi Q13636.

    Protocols and materials databases

    DNASUi 11031.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000578921 ; ENSP00000461945 ; ENSG00000168461 .
    GeneIDi 11031.
    KEGGi hsa:11031.
    UCSCi uc002kog.2. human.

    Organism-specific databases

    CTDi 11031.
    GeneCardsi GC18P009701.
    HGNCi HGNC:9771. RAB31.
    HPAi HPA019717.
    MIMi 605694. gene.
    neXtProti NX_Q13636.
    PharmGKBi PA34122.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOVERGENi HBG009351.
    InParanoidi Q13636.
    KOi K07891.
    OMAi IKLGKQT.
    OrthoDBi EOG77DJ7M.
    PhylomeDBi Q13636.
    TreeFami TF331262.

    Miscellaneous databases

    ChiTaRSi RAB31. human.
    EvolutionaryTracei Q13636.
    GeneWikii RAB31.
    GenomeRNAii 11031.
    NextBioi 41922.
    PROi Q13636.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13636.
    Bgeei Q13636.
    CleanExi HS_RAB31.
    Genevestigatori Q13636.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00175. RAB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of two novel rab genes from human melanocytes."
      Chen D., Guo J., Miki T., Tachibana M., Gahl W.A.
      Gene 174:129-134(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Melanocyte.
    2. "Molecular cloning, bacterial expression and properties of Rab31 and Rab32."
      Bao X., Faris A.E., Jang E.K., Haslam R.J.
      Eur. J. Biochem. 269:259-271(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, MUTAGENESIS OF GLN-64.
      Tissue: Platelet.
    3. "Small GTPase Rab22B is expressed in intestinal epithelial Caco-2 cells."
      Opdam F.J.M., van den Vorstenbosch R., Booltink E., Fransen J.A.M.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "A novel gene expressed in human pheochromocytoma."
      Peng Y., Gu Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pheochromocytoma.
    5. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. "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].
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: Lung.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Rab22B's role in trans-Golgi network membrane dynamics."
      Ng E.L., Wang Y., Tang B.L.
      Biochem. Biophys. Res. Commun. 361:751-757(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates Glut4 trafficking in adipocytes."
      Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T., Inoue M., Pessin J.E., Saltiel A.R.
      Cell Metab. 5:59-72(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GAPVD1 AND EEA1, SUBCELLULAR LOCATION.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Rab22B is expressed in the CNS astroglia lineage and plays a role in epidermal growth factor receptor trafficking in A431 cells."
      Ng E.L., Ng J.J., Liang F., Tang B.L.
      J. Cell. Physiol. 221:716-728(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EGFR AND EEA1.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Characterization of RIN3 as a guanine nucleotide exchange factor for the Rab5 subfamily GTPase Rab31."
      Kajiho H., Sakurai K., Minoda T., Yoshikawa M., Nakagawa S., Fukushima S., Kontani K., Katada T.
      J. Biol. Chem. 286:24364-24373(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RIN3.
    18. "Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes."
      Seto S., Tsujimura K., Koide Y.
      Traffic 12:407-420(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    19. "Crystal structure of human RAB31 in complex with a GTP analogue."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-174 IN COMPLEX WITH GTP ANALOG.

    Entry informationi

    Entry nameiRAB31_HUMAN
    AccessioniPrimary (citable) accession number: Q13636
    Secondary accession number(s): B2RBT7, Q15770, Q9HC00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 136 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, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: 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