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O00767

- ACOD_HUMAN

UniProt

O00767 - ACOD_HUMAN

Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (06 Jun 2002)
      Previous versions | rss
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    Functioni

    Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O2 and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA.

    Catalytic activityi

    Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.

    Cofactori

    Iron.

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. stearoyl-CoA 9-desaturase activity Source: ProtInc

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    Iron

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-CoA desaturase (EC:1.14.19.1)
    Alternative name(s):
    Delta(9)-desaturase
    Short name:
    Delta-9 desaturase
    Fatty acid desaturase
    Stearoyl-CoA desaturase
    Gene namesi
    Name:SCD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:10571. SCD.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: HPA
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34984.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Acyl-CoA desaturasePRO_0000185395Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO00767.
    PaxDbiO00767.
    PRIDEiO00767.

    PTM databases

    PhosphoSiteiO00767.

    Expressioni

    Gene expression databases

    BgeeiO00767.
    GenevestigatoriO00767.

    Organism-specific databases

    HPAiHPA012107.

    Interactioni

    Protein-protein interaction databases

    BioGridi112225. 5 interactions.
    IntActiO00767. 2 interactions.
    MINTiMINT-2997962.

    Structurei

    3D structure databases

    ProteinModelPortaliO00767.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 7171CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini94 – 1029LumenalSequence Analysis
    Topological domaini120 – 21697CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini236 – 25015LumenalSequence AnalysisAdd
    BLAST
    Topological domaini274 – 35986CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei72 – 9322HelicalSequence AnalysisAdd
    BLAST
    Transmembranei103 – 11917HelicalSequence AnalysisAdd
    BLAST
    Transmembranei217 – 23519HelicalSequence AnalysisAdd
    BLAST
    Transmembranei251 – 27323HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi120 – 1256Histidine box-1
    Motifi157 – 1615Histidine box-2
    Motifi298 – 3025Histidine box-3

    Domaini

    The histidine box domains may contain the active site and/or be involved in metal ion binding.

    Sequence similaritiesi

    Belongs to the fatty acid desaturase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1398.
    HOVERGENiHBG003367.
    InParanoidiO00767.
    KOiK00507.
    OMAiYLLAYCA.
    OrthoDBiEOG7ZPNKS.
    PhylomeDBiO00767.
    TreeFamiTF313251.

    Family and domain databases

    InterProiIPR005804. Fatty_acid_desaturase-1.
    IPR001522. Fatty_acid_desaturase-1_C.
    IPR015876. Fatty_acid_desaturase-1_core.
    [Graphical view]
    PfamiPF00487. FA_desaturase. 1 hit.
    [Graphical view]
    PRINTSiPR00075. FACDDSATRASE.
    PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O00767-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAHLLQDDI SSSYTTTTTI TAPPSRVLQN GGDKLETMPL YLEDDIRPDI    50
    KDDIYDPTYK DKEGPSPKVE YVWRNIILMS LLHLGALYGI TLIPTCKFYT 100
    WLWGVFYYFV SALGITAGAH RLWSHRSYKA RLPLRLFLII ANTMAFQNDV 150
    YEWARDHRAH HKFSETHADP HNSRRGFFFS HVGWLLVRKH PAVKEKGSTL 200
    DLSDLEAEKL VMFQRRYYKP GLLMMCFILP TLVPWYFWGE TFQNSVFVAT 250
    FLRYAVVLNA TWLVNSAAHL FGYRPYDKNI SPRENILVSL GAVGEGFHNY 300
    HHSFPYDYSA SEYRWHINFT TFFIDCMAAL GLAYDRKKVS KAAILARIKR 350
    TGDGNYKSG 359
    Length:359
    Mass (Da):41,523
    Last modified:June 6, 2002 - v2
    Checksum:iED56A63DBD850F05
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51L → M in AAB30631. (PubMed:7909540)Curated
    Sequence conflicti8 – 81D → E in AAB30631. (PubMed:7909540)Curated
    Sequence conflicti25 – 262SR → PG in CAA73998. 1 PublicationCurated
    Sequence conflicti25 – 262SR → PG in AAB30631. (PubMed:7909540)Curated
    Sequence conflicti237 – 2371F → C in AAB30631. (PubMed:7909540)Curated
    Sequence conflicti269 – 2691H → L in BAD96582. 1 PublicationCurated
    Sequence conflicti320 – 3201T → N in CAA73998. 1 PublicationCurated
    Sequence conflicti326 – 3261C → W in CAA73998. 1 PublicationCurated
    Sequence conflicti333 – 3331A → T in CAA73998. 1 PublicationCurated
    Sequence conflicti356 – 3594Missing in AAH05807. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti224 – 2241M → L.4 Publications
    Corresponds to variant rs2234970 [ dbSNP | Ensembl ].
    VAR_025994

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13647 mRNA. Translation: CAA73998.1.
    AF097514 mRNA. Translation: AAD29870.1.
    AB032261 mRNA. Translation: BAA93510.1.
    AK312312 mRNA. Translation: BAG35237.1.
    AK222862 mRNA. Translation: BAD96582.1.
    AL139819 Genomic DNA. Translation: CAH72823.1.
    AL139819 Genomic DNA. Translation: CAH72824.1.
    CH471066 Genomic DNA. Translation: EAW49829.1.
    CH471066 Genomic DNA. Translation: EAW49830.1.
    BC005807 mRNA. Translation: AAH05807.1.
    BC062303 mRNA. Translation: AAH62303.1.
    AF320307 Genomic DNA. Translation: AAK54510.1.
    S70284 mRNA. Translation: AAB30631.1.
    CCDSiCCDS7493.1.
    PIRiI54779.
    RefSeqiNP_005054.3. NM_005063.4.
    UniGeneiHs.558396.

    Genome annotation databases

    EnsembliENST00000370355; ENSP00000359380; ENSG00000099194.
    GeneIDi6319.
    KEGGihsa:6319.
    UCSCiuc001kqy.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13647 mRNA. Translation: CAA73998.1 .
    AF097514 mRNA. Translation: AAD29870.1 .
    AB032261 mRNA. Translation: BAA93510.1 .
    AK312312 mRNA. Translation: BAG35237.1 .
    AK222862 mRNA. Translation: BAD96582.1 .
    AL139819 Genomic DNA. Translation: CAH72823.1 .
    AL139819 Genomic DNA. Translation: CAH72824.1 .
    CH471066 Genomic DNA. Translation: EAW49829.1 .
    CH471066 Genomic DNA. Translation: EAW49830.1 .
    BC005807 mRNA. Translation: AAH05807.1 .
    BC062303 mRNA. Translation: AAH62303.1 .
    AF320307 Genomic DNA. Translation: AAK54510.1 .
    S70284 mRNA. Translation: AAB30631.1 .
    CCDSi CCDS7493.1.
    PIRi I54779.
    RefSeqi NP_005054.3. NM_005063.4.
    UniGenei Hs.558396.

    3D structure databases

    ProteinModelPortali O00767.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112225. 5 interactions.
    IntActi O00767. 2 interactions.
    MINTi MINT-2997962.

    Chemistry

    BindingDBi O00767.
    ChEMBLi CHEMBL5555.

    PTM databases

    PhosphoSitei O00767.

    Proteomic databases

    MaxQBi O00767.
    PaxDbi O00767.
    PRIDEi O00767.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370355 ; ENSP00000359380 ; ENSG00000099194 .
    GeneIDi 6319.
    KEGGi hsa:6319.
    UCSCi uc001kqy.3. human.

    Organism-specific databases

    CTDi 6319.
    GeneCardsi GC10P102096.
    H-InvDB HIX0009123.
    HGNCi HGNC:10571. SCD.
    HPAi HPA012107.
    MIMi 604031. gene.
    neXtProti NX_O00767.
    PharmGKBi PA34984.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1398.
    HOVERGENi HBG003367.
    InParanoidi O00767.
    KOi K00507.
    OMAi YLLAYCA.
    OrthoDBi EOG7ZPNKS.
    PhylomeDBi O00767.
    TreeFami TF313251.

    Miscellaneous databases

    ChiTaRSi SCD. human.
    GeneWikii Stearoyl-CoA_desaturase-1.
    GenomeRNAii 6319.
    NextBioi 24520.
    PROi O00767.
    SOURCEi Search...

    Gene expression databases

    Bgeei O00767.
    Genevestigatori O00767.

    Family and domain databases

    InterProi IPR005804. Fatty_acid_desaturase-1.
    IPR001522. Fatty_acid_desaturase-1_C.
    IPR015876. Fatty_acid_desaturase-1_core.
    [Graphical view ]
    Pfami PF00487. FA_desaturase. 1 hit.
    [Graphical view ]
    PRINTSi PR00075. FACDDSATRASE.
    PROSITEi PS00476. FATTY_ACID_DESATUR_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and expression of a stearoyl CoA desaturase from human liver."
      Al-Jeryan L., McCord A., Pierotti A.R., Craft J.A.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Human stearoyl-CoA desaturase: alternative transcripts generated from a single gene by usage of tandem polyadenylation sites."
      Zhang L., Ge L., Parimoo S., Stenn K., Prouty S.M.
      Biochem. J. 340:255-264(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-224.
      Tissue: Brain, Liver and Skin.
    3. "Cloning, sequencing and expression of human stearoyl-CoA desaturase."
      Hoshino T., Ohtsu K.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-224.
    4. "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: Cerebellum.
    5. Suzuki Y., Sugano S., 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: Liver.
    6. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-224.
    8. "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], VARIANT LEU-224.
      Tissue: Mammary gland and Placenta.
    9. "Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: requirement of a conserved CCAAT cis-element."
      Zhang L., Ge L., Tran T., Stenn K., Prouty S.M.
      Biochem. J. 357:183-193(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
    10. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
      Xu G., Shin S.B., Jaffrey S.R.
      Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-27.
      Tissue: Leukemic T-cell.
    11. "Partial characterization of a cDNA for human stearoyl-CoA desaturase and changes in its mRNA expression in some normal and malignant tissues."
      Li J., Ding S.-F., Habib N.A., Fermor B.F., Wood C.B., Gilmour R.S.
      Int. J. Cancer 57:348-352(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-239.
      Tissue: Adipose tissue.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiACOD_HUMAN
    AccessioniPrimary (citable) accession number: O00767
    Secondary accession number(s): B2R5U0
    , D3DR68, Q16150, Q53GR9, Q5W037, Q5W038, Q6GSS4, Q96KF6, Q9BS07, Q9Y695
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 143 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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