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P02748

- CO9_HUMAN

UniProt

P02748 - CO9_HUMAN

Protein

Complement component C9

Gene

C9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C9 is the pore-forming subunit of the MAC.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei265 – 2662Cleavage; by thrombin

    GO - Biological processi

    1. complement activation, alternative pathway Source: UniProtKB-KW
    2. complement activation, classical pathway Source: UniProtKB-KW
    3. hemolysis by symbiont of host erythrocytes Source: ProtInc
    4. innate immune response Source: Reactome
    5. regulation of complement activation Source: Reactome

    Keywords - Biological processi

    Complement alternate pathway, Complement pathway, Cytolysis, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_118707. Regulation of Complement cascade.
    REACT_8028. Terminal pathway of complement.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement component C9
    Cleaved into the following 2 chains:
    Gene namesi
    Name:C9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:1358. C9.

    Subcellular locationi

    Secreted. Cell membrane; Multi-pass membrane protein
    Note: Secreted as soluble monomer. Oligomerizes at target membranes, forming a pre-pore. A conformation change then leads to the formation of a 100 Angstrom diameter pore.

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cytoplasm Source: HPA
    3. extracellular region Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. integral component of plasma membrane Source: ProtInc
    6. membrane attack complex Source: UniProtKB-KW
    7. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cell membrane, Membrane, Membrane attack complex, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Complement component 9 deficiency (C9D) [MIM:613825]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Some patients may develop dermatomyositis.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti119 – 1191C → G in C9D. 1 Publication
    VAR_012648
    Macular degeneration, age-related, 15 (ARMD15) [MIM:615591]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671P → S in ARMD15. 1 Publication
    VAR_070940

    Keywords - Diseasei

    Age-related macular degeneration, Disease mutation

    Organism-specific databases

    MIMi613825. phenotype.
    615591. phenotype.
    Orphaneti279. Age-related macular degeneration.
    169150. Immunodeficiency due to a late component of complements deficiency.
    PharmGKBiPA25968.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21211 PublicationAdd
    BLAST
    Chaini22 – 559538Complement component C9PRO_0000023602Add
    BLAST
    Chaini22 – 265244Complement component C9aPRO_0000023603Add
    BLAST
    Chaini266 – 559294Complement component C9bPRO_0000023604Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi43 ↔ 781 Publication
    Glycosylationi48 – 481C-linked (Man)
    Glycosylationi51 – 511C-linked (Man); partial
    Disulfide bondi54 ↔ 571 Publication
    Disulfide bondi88 ↔ 941 Publication
    Disulfide bondi101 ↔ 1121 Publication
    Disulfide bondi107 ↔ 1251 Publication
    Disulfide bondi119 ↔ 1341 Publication
    Disulfide bondi142 ↔ 1811 Publication
    Disulfide bondi254 ↔ 2551 Publication
    Glycosylationi277 – 2771N-linked (GlcNAc...)3 Publications
    Disulfide bondi380 ↔ 4051 Publication
    Glycosylationi415 – 4151N-linked (GlcNAc...) (complex)6 Publications
    Disulfide bondi510 ↔ 5261 Publication
    Disulfide bondi513 ↔ 5281 Publication
    Disulfide bondi530 ↔ 5391 Publication

    Post-translational modificationi

    Thrombin cleaves factor C9 to produce C9a and C9b.
    Phosphorylation sites are present in the extracellular medium.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP02748.
    PaxDbiP02748.
    PeptideAtlasiP02748.
    PRIDEiP02748.

    PTM databases

    PhosphoSiteiP02748.

    Expressioni

    Tissue specificityi

    Plasma.

    Gene expression databases

    ArrayExpressiP02748.
    BgeeiP02748.
    CleanExiHS_C9.
    GenevestigatoriP02748.

    Organism-specific databases

    HPAiCAB002151.
    HPA029577.

    Interactioni

    Subunit structurei

    Component of the membrane attack complex (MAC). MAC assembly is initiated by protelytic cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple copies of the pore-forming subunit C9.

    Protein-protein interaction databases

    BioGridi107196. 3 interactions.
    DIPiDIP-1124N.
    MINTiMINT-2800316.
    STRINGi9606.ENSP00000263408.

    Structurei

    3D structure databases

    ProteinModelPortaliP02748.
    SMRiP02748. Positions 36-540.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei314 – 33017Beta strandedSequence AnalysisAdd
    BLAST
    Transmembranei335 – 35420Beta strandedSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 9554TSP type-1PROSITE-ProRule annotationAdd
    BLAST
    Domaini99 – 13638LDL-receptor class APROSITE-ProRule annotationAdd
    BLAST
    Domaini138 – 509372MACPFPROSITE-ProRule annotationAdd
    BLAST
    Domaini510 – 54031EGF-likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the complement C6/C7/C8/C9 family.Curated
    Contains 1 EGF-like domain.Curated
    Contains 1 LDL-receptor class A domain.PROSITE-ProRule annotation
    Contains 1 MACPF domain.PROSITE-ProRule annotation
    Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Signal, Transmembrane, Transmembrane beta strand

    Phylogenomic databases

    eggNOGiNOG46204.
    HOGENOMiHOG000111869.
    HOVERGENiHBG106792.
    InParanoidiP02748.
    KOiK04000.
    OMAiPWNVASL.
    OrthoDBiEOG7D85W9.
    PhylomeDBiP02748.
    TreeFamiTF330498.

    Family and domain databases

    Gene3Di4.10.400.10. 1 hit.
    InterProiIPR009030. Growth_fac_rcpt_N_dom.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001862. MAC_perforin.
    IPR020864. MACPF.
    IPR020863. MACPF_CS.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF00057. Ldl_recept_a. 1 hit.
    PF01823. MACPF. 1 hit.
    PF00090. TSP_1. 1 hit.
    [Graphical view]
    PRINTSiPR00764. COMPLEMENTC9.
    SMARTiSM00192. LDLa. 1 hit.
    SM00457. MACPF. 1 hit.
    SM00209. TSP1. 1 hit.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 2 hits.
    SSF57424. SSF57424. 1 hit.
    SSF82895. SSF82895. 1 hit.
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS01209. LDLRA_1. 1 hit.
    PS50068. LDLRA_2. 1 hit.
    PS00279. MACPF_1. 1 hit.
    PS51412. MACPF_2. 1 hit.
    PS50092. TSP1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P02748-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSACRSFAVA ICILEISILT AQYTTSYDPE LTESSGSASH IDCRMSPWSE    50
    WSQCDPCLRQ MFRSRSIEVF GQFNGKRCTD AVGDRRQCVP TEPCEDAEDD 100
    CGNDFQCSTG RCIKMRLRCN GDNDCGDFSD EDDCESEPRP PCRDRVVEES 150
    ELARTAGYGI NILGMDPLST PFDNEFYNGL CNRDRDGNTL TYYRRPWNVA 200
    SLIYETKGEK NFRTEHYEEQ IEAFKSIIQE KTSNFNAAIS LKFTPTETNK 250
    AEQCCEETAS SISLHGKGSF RFSYSKNETY QLFLSYSSKK EKMFLHVKGE 300
    IHLGRFVMRN RDVVLTTTFV DDIKALPTTY EKGEYFAFLE TYGTHYSSSG 350
    SLGGLYELIY VLDKASMKRK GVELKDIKRC LGYHLDVSLA FSEISVGAEF 400
    NKDDCVKRGE GRAVNITSEN LIDDVVSLIR GGTRKYAFEL KEKLLRGTVI 450
    DVTDFVNWAS SINDAPVLIS QKLSPIYNLV PVKMKNAHLK KQNLERAIED 500
    YINEFSVRKC HTCQNGGTVI LMDGKCLCAC PFKFEGIACE ISKQKISEGL 550
    PALEFPNEK 559
    Length:559
    Mass (Da):63,173
    Last modified:February 1, 1996 - v2
    Checksum:i7403F6AD77B3ECE1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431C → R in AAA51889. (PubMed:6095282)Curated
    Sequence conflicti314 – 3141Missing in AAA51889. (PubMed:6095282)Curated
    Sequence conflicti417 – 4171T → P in AAA51889. (PubMed:6095282)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51R → W.
    Corresponds to variant rs700233 [ dbSNP | Ensembl ].
    VAR_022024
    Natural varianti119 – 1191C → G in C9D. 1 Publication
    VAR_012648
    Natural varianti127 – 1271D → Y.
    Corresponds to variant rs696763 [ dbSNP | Ensembl ].
    VAR_050481
    Natural varianti167 – 1671P → S in ARMD15. 1 Publication
    VAR_070940
    Natural varianti203 – 2031I → V.
    Corresponds to variant rs13361416 [ dbSNP | Ensembl ].
    VAR_027651
    Natural varianti279 – 2791T → S.
    Corresponds to variant rs34625111 [ dbSNP | Ensembl ].
    VAR_033802
    Natural varianti427 – 4271S → T.
    Corresponds to variant rs34421659 [ dbSNP | Ensembl ].
    VAR_061503

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02176 mRNA. Translation: CAA26117.1.
    BC020721 mRNA. Translation: AAH20721.1.
    K02766 mRNA. Translation: AAA51889.1.
    J02833 Genomic DNA. Translation: AAA51890.1.
    Y08545
    , Y08546, Y08547, Y08548, Y08549, Y08550, Y08551, Y08552, Y08553, Y08554 Genomic DNA. Translation: CAA69849.1.
    CCDSiCCDS3929.1.
    PIRiA59363. C9HU.
    RefSeqiNP_001728.1. NM_001737.3.
    UniGeneiHs.654443.

    Genome annotation databases

    EnsembliENST00000263408; ENSP00000263408; ENSG00000113600.
    GeneIDi735.
    KEGGihsa:735.
    UCSCiuc003jlv.4. human.

    Polymorphism databases

    DMDMi1352108.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    C9base

    C9 mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02176 mRNA. Translation: CAA26117.1 .
    BC020721 mRNA. Translation: AAH20721.1 .
    K02766 mRNA. Translation: AAA51889.1 .
    J02833 Genomic DNA. Translation: AAA51890.1 .
    Y08545
    , Y08546 , Y08547 , Y08548 , Y08549 , Y08550 , Y08551 , Y08552 , Y08553 , Y08554 Genomic DNA. Translation: CAA69849.1 .
    CCDSi CCDS3929.1.
    PIRi A59363. C9HU.
    RefSeqi NP_001728.1. NM_001737.3.
    UniGenei Hs.654443.

    3D structure databases

    ProteinModelPortali P02748.
    SMRi P02748. Positions 36-540.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107196. 3 interactions.
    DIPi DIP-1124N.
    MINTi MINT-2800316.
    STRINGi 9606.ENSP00000263408.

    PTM databases

    PhosphoSitei P02748.

    Polymorphism databases

    DMDMi 1352108.

    Proteomic databases

    MaxQBi P02748.
    PaxDbi P02748.
    PeptideAtlasi P02748.
    PRIDEi P02748.

    Protocols and materials databases

    DNASUi 735.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263408 ; ENSP00000263408 ; ENSG00000113600 .
    GeneIDi 735.
    KEGGi hsa:735.
    UCSCi uc003jlv.4. human.

    Organism-specific databases

    CTDi 735.
    GeneCardsi GC05M039320.
    HGNCi HGNC:1358. C9.
    HPAi CAB002151.
    HPA029577.
    MIMi 120940. gene.
    613825. phenotype.
    615591. phenotype.
    neXtProti NX_P02748.
    Orphaneti 279. Age-related macular degeneration.
    169150. Immunodeficiency due to a late component of complements deficiency.
    PharmGKBi PA25968.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46204.
    HOGENOMi HOG000111869.
    HOVERGENi HBG106792.
    InParanoidi P02748.
    KOi K04000.
    OMAi PWNVASL.
    OrthoDBi EOG7D85W9.
    PhylomeDBi P02748.
    TreeFami TF330498.

    Enzyme and pathway databases

    Reactomei REACT_118707. Regulation of Complement cascade.
    REACT_8028. Terminal pathway of complement.

    Miscellaneous databases

    GenomeRNAii 735.
    NextBioi 2992.
    PROi P02748.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02748.
    Bgeei P02748.
    CleanExi HS_C9.
    Genevestigatori P02748.

    Family and domain databases

    Gene3Di 4.10.400.10. 1 hit.
    InterProi IPR009030. Growth_fac_rcpt_N_dom.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001862. MAC_perforin.
    IPR020864. MACPF.
    IPR020863. MACPF_CS.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF00057. Ldl_recept_a. 1 hit.
    PF01823. MACPF. 1 hit.
    PF00090. TSP_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00764. COMPLEMENTC9.
    SMARTi SM00192. LDLa. 1 hit.
    SM00457. MACPF. 1 hit.
    SM00209. TSP1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 2 hits.
    SSF57424. SSF57424. 1 hit.
    SSF82895. SSF82895. 1 hit.
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS01209. LDLRA_1. 1 hit.
    PS50068. LDLRA_2. 1 hit.
    PS00279. MACPF_1. 1 hit.
    PS51412. MACPF_2. 1 hit.
    PS50092. TSP1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence and topology of human complement component C9."
      Stanley K.K., Kocher H.-P., Luzio J.P., Jackson P., Tschopp J.
      EMBO J. 4:375-382(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Liver.
    3. "Nucleotide sequence of cDNA and derived amino acid sequence of human complement component C9."
      Discipio R.G., Gehring M.R., Podack E.R., Kan C.C., Hugli T.E., Fey G.H.
      Proc. Natl. Acad. Sci. U.S.A. 81:7298-7302(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-559, PROTEIN SEQUENCE OF N-TERMINUS.
    4. "Relationships between the gene and protein structure in human complement component C9."
      Marazziti D., Eggertsen G., Fey G.H., Stanley K.K.
      Biochemistry 27:6529-6534(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-159.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-559, VARIANT C9D GLY-119.
    6. "The architecture of complement component C9 and poly(C9)."
      DiScipio R.G., Hugli T.E.
      J. Biol. Chem. 260:14802-14809(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, ELECTRON MICROSCOPY, GLYCOSYLATION AT ASN-277 AND ASN-415.
    7. "Identification of disulfide bonds in the ninth component (C9) of human complement."
      Lengweiler S., Schaller J., Rickli E.E.
      FEBS Lett. 380:8-12(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    8. "The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues."
      Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.
      J. Biol. Chem. 274:32786-32794(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT TRP-48 AND TRP-51.
    9. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415.
      Tissue: Plasma.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-415.
      Tissue: Plasma.
    11. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
      Lewandrowski U., Moebius J., Walter U., Sickmann A.
      Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415.
      Tissue: Platelet.
    12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-415.
      Tissue: Liver.
    13. Cited for: GLYCOSYLATION AT ASN-415.
    14. "Localization and molecular modelling of the membrane-inserted domain of the ninth component of human complement and perforin."
      Peitsch M.C., Amiguet P., Guy R., Brunner J., Maizel J.V. Jr., Tschopp J.
      Mol. Immunol. 27:589-602(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF MEMBRANE-SPANNING DOMAIN (MSB).
    15. Cited for: VARIANT ARMD15 SER-167.

    Entry informationi

    Entry nameiCO9_HUMAN
    AccessioniPrimary (citable) accession number: P02748
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 156 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 5
      Human chromosome 5: 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