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Q16774

- KGUA_HUMAN

UniProt

Q16774 - KGUA_HUMAN

Protein

Guanylate kinase

Gene

GUK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Essential for recycling GMP and indirectly, cGMP.

    Catalytic activityi

    ATP + GMP = ADP + GDP.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei44 – 441By similarity
    Active sitei137 – 1371By similarity
    Active sitei148 – 1481By similarity
    Binding sitei171 – 1711ATPBy similarity
    Binding sitei172 – 1721ATP; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 188ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. guanylate kinase activity Source: UniProtKB

    GO - Biological processi

    1. ATP metabolic process Source: Ensembl
    2. dATP metabolic process Source: Ensembl
    3. dGDP biosynthetic process Source: Ensembl
    4. dGMP metabolic process Source: Ensembl
    5. drug metabolic process Source: Reactome
    6. GDP biosynthetic process Source: Ensembl
    7. GDP-mannose metabolic process Source: Ensembl
    8. glycoprotein transport Source: Ensembl
    9. GMP metabolic process Source: Ensembl
    10. nucleobase-containing small molecule interconversion Source: Reactome
    11. nucleobase-containing small molecule metabolic process Source: Reactome
    12. purine nucleotide metabolic process Source: UniProtKB
    13. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07104-MONOMER.
    ReactomeiREACT_121388. Abacavir metabolism.
    REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    SABIO-RKQ16774.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanylate kinase (EC:2.7.4.8)
    Alternative name(s):
    GMP kinase
    Gene namesi
    Name:GUK1
    Synonyms:GMK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4693. GUK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29072.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 197196Guanylate kinasePRO_0000170651Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ16774.
    PaxDbiQ16774.
    PRIDEiQ16774.

    PTM databases

    PhosphoSiteiQ16774.

    Expressioni

    Gene expression databases

    ArrayExpressiQ16774.
    BgeeiQ16774.
    CleanExiHS_GUK1.
    GenevestigatoriQ16774.

    Organism-specific databases

    HPAiHPA028118.
    HPA048587.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi109242. 3 interactions.
    IntActiQ16774. 2 interactions.
    STRINGi9606.ENSP00000317659.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16774.
    SMRiQ16774. Positions 5-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 186183Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the guanylate kinase family.Curated
    Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0194.
    HOGENOMiHOG000037640.
    HOVERGENiHBG003344.
    KOiK00942.
    OrthoDBiEOG7J1814.
    PhylomeDBiQ16774.
    TreeFamiTF314473.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    InterProiIPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR017665. Guanylate_kinase.
    IPR020590. Guanylate_kinase_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00625. Guanylate_kin. 1 hit.
    [Graphical view]
    SMARTiSM00072. GuKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
    PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
    PS50052. GUANYLATE_KINASE_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16774-1) [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

    MSGPRPVVLS GPSGAGKSTL LKRLLQEHSG IFGFSVSHTT RNPRPGEENG    50
    KDYYFVTREV MQRDIAAGDF IEHAEFSGNL YGTSKVAVQA VQAMNRICVL 100
    DVDLQGVRNI KATDLRPIYI SVQPPSLHVL EQRLRQRNTE TEESLVKRLA 150
    AAQADMESSK EPGLFDVVII NDSLDQAYAE LKEALSEEIK KAQRTGA 197
    Length:197
    Mass (Da):21,726
    Last modified:January 23, 2007 - v2
    Checksum:iC49573212A0DA825
    GO
    Isoform 2 (identifier: Q16774-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MLRRPLAGLAAAALGRAPPDGM

    Show »
    Length:218
    Mass (Da):23,782
    Checksum:i6972858284006BB2
    GO
    Isoform 3 (identifier: Q16774-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MLRRPLAGLAAAALGRAPPDGM
         159-197: SKEPGLFDVV...EIKKAQRTGA → RNQESSKDRR...CCPCGWNILG

    Note: Gene prediction based on EST data.

    Show »
    Length:241
    Mass (Da):26,596
    Checksum:i418604D9B391F864
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MLRRPLAGLAAAALGRAPPD GM in isoform 2 and isoform 3. 1 PublicationVSP_043778
    Alternative sequencei159 – 19739SKEPG…QRTGA → RNQESSKDRRLRLAVCSRHP GPIQDQGSSIEPPPWQAIRQ LCALGQHVEWRRCCPCGWNI LG in isoform 3. CuratedVSP_047372Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L76200 mRNA. Translation: AAC37598.1.
    U66895 mRNA. Translation: AAC50659.1.
    AK303845 mRNA. Translation: BAG64788.1.
    AL359510 Genomic DNA. No translation available.
    CH471098 Genomic DNA. Translation: EAW69856.1.
    BC006249 mRNA. Translation: AAH06249.1.
    BC009914 mRNA. Translation: AAH09914.1.
    CCDSiCCDS1568.1. [Q16774-1]
    CCDS53481.1. [Q16774-2]
    CCDS55689.1. [Q16774-3]
    PIRiS68864.
    RefSeqiNP_000849.1. NM_000858.5. [Q16774-1]
    NP_001152862.1. NM_001159390.1. [Q16774-2]
    NP_001152863.1. NM_001159391.1. [Q16774-1]
    NP_001229768.1. NM_001242839.1. [Q16774-1]
    NP_001229769.1. NM_001242840.1. [Q16774-3]
    UniGeneiHs.376933.

    Genome annotation databases

    EnsembliENST00000312726; ENSP00000317659; ENSG00000143774. [Q16774-1]
    ENST00000366716; ENSP00000355677; ENSG00000143774. [Q16774-1]
    ENST00000366718; ENSP00000355679; ENSG00000143774. [Q16774-1]
    ENST00000366726; ENSP00000355687; ENSG00000143774. [Q16774-1]
    ENST00000366728; ENSP00000355689; ENSG00000143774. [Q16774-3]
    ENST00000366730; ENSP00000355691; ENSG00000143774. [Q16774-1]
    ENST00000391865; ENSP00000375738; ENSG00000143774. [Q16774-2]
    GeneIDi2987.
    KEGGihsa:2987.
    UCSCiuc001hsh.3. human. [Q16774-1]
    uc001hsi.3. human. [Q16774-2]

    Polymorphism databases

    DMDMi2497498.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L76200 mRNA. Translation: AAC37598.1 .
    U66895 mRNA. Translation: AAC50659.1 .
    AK303845 mRNA. Translation: BAG64788.1 .
    AL359510 Genomic DNA. No translation available.
    CH471098 Genomic DNA. Translation: EAW69856.1 .
    BC006249 mRNA. Translation: AAH06249.1 .
    BC009914 mRNA. Translation: AAH09914.1 .
    CCDSi CCDS1568.1. [Q16774-1 ]
    CCDS53481.1. [Q16774-2 ]
    CCDS55689.1. [Q16774-3 ]
    PIRi S68864.
    RefSeqi NP_000849.1. NM_000858.5. [Q16774-1 ]
    NP_001152862.1. NM_001159390.1. [Q16774-2 ]
    NP_001152863.1. NM_001159391.1. [Q16774-1 ]
    NP_001229768.1. NM_001242839.1. [Q16774-1 ]
    NP_001229769.1. NM_001242840.1. [Q16774-3 ]
    UniGenei Hs.376933.

    3D structure databases

    ProteinModelPortali Q16774.
    SMRi Q16774. Positions 5-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109242. 3 interactions.
    IntActi Q16774. 2 interactions.
    STRINGi 9606.ENSP00000317659.

    Chemistry

    ChEMBLi CHEMBL4989.

    PTM databases

    PhosphoSitei Q16774.

    Polymorphism databases

    DMDMi 2497498.

    Proteomic databases

    MaxQBi Q16774.
    PaxDbi Q16774.
    PRIDEi Q16774.

    Protocols and materials databases

    DNASUi 2987.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312726 ; ENSP00000317659 ; ENSG00000143774 . [Q16774-1 ]
    ENST00000366716 ; ENSP00000355677 ; ENSG00000143774 . [Q16774-1 ]
    ENST00000366718 ; ENSP00000355679 ; ENSG00000143774 . [Q16774-1 ]
    ENST00000366726 ; ENSP00000355687 ; ENSG00000143774 . [Q16774-1 ]
    ENST00000366728 ; ENSP00000355689 ; ENSG00000143774 . [Q16774-3 ]
    ENST00000366730 ; ENSP00000355691 ; ENSG00000143774 . [Q16774-1 ]
    ENST00000391865 ; ENSP00000375738 ; ENSG00000143774 . [Q16774-2 ]
    GeneIDi 2987.
    KEGGi hsa:2987.
    UCSCi uc001hsh.3. human. [Q16774-1 ]
    uc001hsi.3. human. [Q16774-2 ]

    Organism-specific databases

    CTDi 2987.
    GeneCardsi GC01P228327.
    HGNCi HGNC:4693. GUK1.
    HPAi HPA028118.
    HPA048587.
    MIMi 139270. gene.
    neXtProti NX_Q16774.
    PharmGKBi PA29072.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0194.
    HOGENOMi HOG000037640.
    HOVERGENi HBG003344.
    KOi K00942.
    OrthoDBi EOG7J1814.
    PhylomeDBi Q16774.
    TreeFami TF314473.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07104-MONOMER.
    Reactomei REACT_121388. Abacavir metabolism.
    REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    SABIO-RK Q16774.

    Miscellaneous databases

    ChiTaRSi GUK1. human.
    GeneWikii GUK1.
    GenomeRNAii 2987.
    NextBioi 11844.
    PROi Q16774.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16774.
    Bgeei Q16774.
    CleanExi HS_GUK1.
    Genevestigatori Q16774.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    InterProi IPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR017665. Guanylate_kinase.
    IPR020590. Guanylate_kinase_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00625. Guanylate_kin. 1 hit.
    [Graphical view ]
    SMARTi SM00072. GuKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR03263. guanyl_kin. 1 hit.
    PROSITEi PS00856. GUANYLATE_KINASE_1. 1 hit.
    PS50052. GUANYLATE_KINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human guanylate kinase (GUK1): cDNA sequence, expression and chromosomal localisation."
      Fitzgibbon J., Katsanis N., Wells D., Delhanty J., Vallins W., Hunt D.M.
      FEBS Lett. 385:185-188(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retina.
    2. "Cloning, characterization, and modeling of mouse and human guanylate kinases."
      Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E.
      J. Biol. Chem. 271:16734-16740(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 2).
      Tissue: Ovary.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Lung.
    7. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKGUA_HUMAN
    AccessioniPrimary (citable) accession number: Q16774
    Secondary accession number(s): B1ANH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 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

    Miscellaneous

    In addition to phosphorylating GMP, antiviral prodrugs such as acyclovir, ganciclovir, and carbovir and anticancer prodrugs such as the thiopurines are dependent on GMPK for their activation.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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