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Q9NR19

- ACSA_HUMAN

UniProt

Q9NR19 - ACSA_HUMAN

Protein

Acetyl-coenzyme A synthetase, cytoplasmic

Gene

ACSS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Activates acetate so that it can be used for lipid synthesis or for energy generation.

    Catalytic activityi

    ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei363 – 3631Coenzyme ABy similarity
    Binding sitei552 – 5521ATPBy similarity
    Binding sitei567 – 5671ATPBy similarity
    Binding sitei575 – 5751Coenzyme A; via carbonyl oxygenBy similarity
    Binding sitei636 – 6361Coenzyme ABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi439 – 4413ATPBy similarity
    Nucleotide bindingi463 – 4686ATPBy similarity

    GO - Molecular functioni

    1. acetate-CoA ligase activity Source: UniProtKB
    2. AMP binding Source: UniProtKB
    3. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. acetate biosynthetic process Source: Ensembl
    2. acetyl-CoA biosynthetic process from acetate Source: InterPro
    3. ethanol oxidation Source: Reactome
    4. lipid biosynthetic process Source: UniProtKB
    5. propionate biosynthetic process Source: Ensembl
    6. small molecule metabolic process Source: Reactome
    7. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05484-MONOMER.
    BRENDAi6.2.1.1. 2681.
    ReactomeiREACT_34. Ethanol oxidation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-coenzyme A synthetase, cytoplasmic (EC:6.2.1.1)
    Alternative name(s):
    Acetate--CoA ligase
    Acetyl-CoA synthetase
    Short name:
    ACS
    Short name:
    AceCS
    Acyl-CoA synthetase short-chain family member 2
    Acyl-activating enzyme
    Gene namesi
    Name:ACSS2
    Synonyms:ACAS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15814. ACSS2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. intracellular membrane-bounded organelle Source: HPA
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24429.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 701701Acetyl-coenzyme A synthetase, cytoplasmicPRO_0000208423Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei30 – 301Phosphoserine1 Publication
    Modified residuei263 – 2631PhosphoserineBy similarity
    Modified residuei267 – 2671Phosphoserine2 Publications
    Modified residuei418 – 4181N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NR19.
    PaxDbiQ9NR19.
    PRIDEiQ9NR19.

    PTM databases

    PhosphoSiteiQ9NR19.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NR19.
    BgeeiQ9NR19.
    CleanExiHS_ACSS2.
    GenevestigatoriQ9NR19.

    Organism-specific databases

    HPAiHPA004141.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UPF1Q929001EBI-372879,EBI-373471

    Protein-protein interaction databases

    BioGridi120989. 2 interactions.
    IntActiQ9NR19. 3 interactions.
    STRINGi9606.ENSP00000353804.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NR19.
    SMRiQ9NR19. Positions 45-696.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni219 – 2224Coenzyme A bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    HOVERGENiHBG014401.
    KOiK01895.
    OMAiAWIWYRD.
    OrthoDBiEOG77T140.
    PhylomeDBiQ9NR19.
    TreeFamiTF300417.

    Family and domain databases

    InterProiIPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NR19-1) [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

    MGLPEERVRS GSGSRGQEEA GAGGRARSWS PPPEVSRSAH VPSLQRYREL    50
    HRRSVEEPRE FWGDIAKEFY WKTPCPGPFL RYNFDVTKGK IFIEWMKGAT 100
    TNICYNVLDR NVHEKKLGDK VAFYWEGNEP GETTQITYHQ LLVQVCQFSN 150
    VLRKQGIQKG DRVAIYMPMI PELVVAMLAC ARIGALHSIV FAGFSSESLC 200
    ERILDSSCSL LITTDAFYRG EKLVNLKELA DEALQKCQEK GFPVRCCIVV 250
    KHLGRAELGM GDSTSQSPPI KRSCPDVQIS WNQGIDLWWH ELMQEAGDEC 300
    EPEWCDAEDP LFILYTSGST GKPKGVVHTV GGYMLYVATT FKYVFDFHAE 350
    DVFWCTADIG WITGHSYVTY GPLANGATSV LFEGIPTYPD VNRLWSIVDK 400
    YKVTKFYTAP TAIRLLMKFG DEPVTKHSRA SLQVLGTVGE PINPEAWLWY 450
    HRVVGAQRCP IVDTFWQTET GGHMLTPLPG ATPMKPGSAT FPFFGVAPAI 500
    LNESGEELEG EAEGYLVFKQ PWPGIMRTVY GNHERFETTY FKKFPGYYVT 550
    GDGCQRDQDG YYWITGRIDD MLNVSGHLLS TAEVESALVE HEAVAEAAVV 600
    GHPHPVKGEC LYCFVTLCDG HTFSPKLTEE LKKQIREKIG PIATPDYIQN 650
    APGLPKTRSG KIMRRVLRKI AQNDHDLGDM STVADPSVIS HLFSHRCLTI 700
    Q 701
    Length:701
    Mass (Da):78,580
    Last modified:October 1, 2000 - v1
    Checksum:i833580B41B73A8B4
    GO
    Isoform 2 (identifier: Q9NR19-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         277-277: V → VQGKLKEKSKRVQP

    Note: No experimental confirmation available.

    Show »
    Length:714
    Mass (Da):80,087
    Checksum:i820E84E62A72E214
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 791F → L in BAC03849. (PubMed:14702039)Curated
    Sequence conflicti615 – 6151V → F in AAH12172. (PubMed:15489334)Curated
    Sequence conflicti680 – 6801M → L in BAC03849. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei277 – 2771V → VQGKLKEKSKRVQP in isoform 2. 1 PublicationVSP_046376

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263614 mRNA. Translation: AAF75064.1.
    AK092281 mRNA. Translation: BAC03849.1.
    AL133324, AL049709 Genomic DNA. Translation: CAI19311.1.
    AL133324, AL049709 Genomic DNA. Translation: CAI19312.1.
    AL049709, AL133324 Genomic DNA. Translation: CAI19725.1.
    AL049709, AL133324 Genomic DNA. Translation: CAI19726.1.
    CH471077 Genomic DNA. Translation: EAW76248.1.
    BC012172 mRNA. Translation: AAH12172.1.
    CCDSiCCDS13243.1. [Q9NR19-1]
    CCDS42868.2. [Q9NR19-2]
    RefSeqiNP_001070020.2. NM_001076552.2. [Q9NR19-2]
    NP_061147.1. NM_018677.3. [Q9NR19-1]
    UniGeneiHs.517034.

    Genome annotation databases

    EnsembliENST00000253382; ENSP00000253382; ENSG00000131069. [Q9NR19-2]
    ENST00000360596; ENSP00000353804; ENSG00000131069. [Q9NR19-1]
    GeneIDi55902.
    KEGGihsa:55902.
    UCSCiuc002xbc.2. human. [Q9NR19-1]
    uc010gey.2. human.

    Polymorphism databases

    DMDMi20137525.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263614 mRNA. Translation: AAF75064.1 .
    AK092281 mRNA. Translation: BAC03849.1 .
    AL133324 , AL049709 Genomic DNA. Translation: CAI19311.1 .
    AL133324 , AL049709 Genomic DNA. Translation: CAI19312.1 .
    AL049709 , AL133324 Genomic DNA. Translation: CAI19725.1 .
    AL049709 , AL133324 Genomic DNA. Translation: CAI19726.1 .
    CH471077 Genomic DNA. Translation: EAW76248.1 .
    BC012172 mRNA. Translation: AAH12172.1 .
    CCDSi CCDS13243.1. [Q9NR19-1 ]
    CCDS42868.2. [Q9NR19-2 ]
    RefSeqi NP_001070020.2. NM_001076552.2. [Q9NR19-2 ]
    NP_061147.1. NM_018677.3. [Q9NR19-1 ]
    UniGenei Hs.517034.

    3D structure databases

    ProteinModelPortali Q9NR19.
    SMRi Q9NR19. Positions 45-696.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120989. 2 interactions.
    IntActi Q9NR19. 3 interactions.
    STRINGi 9606.ENSP00000353804.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.
    DB00171. Adenosine triphosphate.

    PTM databases

    PhosphoSitei Q9NR19.

    Polymorphism databases

    DMDMi 20137525.

    Proteomic databases

    MaxQBi Q9NR19.
    PaxDbi Q9NR19.
    PRIDEi Q9NR19.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253382 ; ENSP00000253382 ; ENSG00000131069 . [Q9NR19-2 ]
    ENST00000360596 ; ENSP00000353804 ; ENSG00000131069 . [Q9NR19-1 ]
    GeneIDi 55902.
    KEGGi hsa:55902.
    UCSCi uc002xbc.2. human. [Q9NR19-1 ]
    uc010gey.2. human.

    Organism-specific databases

    CTDi 55902.
    GeneCardsi GC20P033459.
    HGNCi HGNC:15814. ACSS2.
    HPAi HPA004141.
    MIMi 605832. gene.
    neXtProti NX_Q9NR19.
    PharmGKBi PA24429.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0365.
    HOGENOMi HOG000229981.
    HOVERGENi HBG014401.
    KOi K01895.
    OMAi AWIWYRD.
    OrthoDBi EOG77T140.
    PhylomeDBi Q9NR19.
    TreeFami TF300417.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS05484-MONOMER.
    BRENDAi 6.2.1.1. 2681.
    Reactomei REACT_34. Ethanol oxidation.

    Miscellaneous databases

    GeneWikii ACSS2.
    GenomeRNAii 55902.
    NextBioi 61271.
    PROi Q9NR19.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NR19.
    Bgeei Q9NR19.
    CleanExi HS_ACSS2.
    Genevestigatori Q9NR19.

    Family and domain databases

    InterProi IPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins."
      Luong A., Hannah V.C., Brown M.S., Goldstein J.L.
      J. Biol. Chem. 275:26458-26466(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    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] (ISOFORM 2).
      Tissue: Tongue.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Skin.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiACSA_HUMAN
    AccessioniPrimary (citable) accession number: Q9NR19
    Secondary accession number(s): A6NE90
    , Q5QPH2, Q5QPH3, Q8N238, Q96EL0, Q9NQP7, Q9UJ15
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 123 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3