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P10643

- CO7_HUMAN

UniProt

P10643 - CO7_HUMAN

Protein

Complement component C7

Gene

C7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (15 Mar 2005)
      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. C7 serves as a membrane anchor.

    GO - Biological processi

    1. cellular sodium ion homeostasis Source: Ensembl
    2. complement activation Source: ProtInc
    3. complement activation, alternative pathway Source: UniProtKB-KW
    4. complement activation, classical pathway Source: UniProtKB-KW
    5. cytolysis Source: UniProtKB-KW
    6. innate immune response Source: Reactome
    7. 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 C7
    Gene namesi
    Name:C7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:1346. C7.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. membrane attack complex Source: ProtInc

    Keywords - Cellular componenti

    Membrane attack complex, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Complement component 7 deficiency (C7D) [MIM:610102]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis.3 Publications
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti220 – 2201R → Q in C7D. 1 Publication
    VAR_012643
    Natural varianti379 – 3791G → R in C7D. 1 Publication
    VAR_012644
    Natural varianti521 – 5211R → S in C7D. 1 Publication
    Corresponds to variant rs121964920 [ dbSNP | Ensembl ].
    VAR_012645
    Natural varianti682 – 6821E → Q in C7D. 1 Publication
    VAR_012646
    Natural varianti687 – 6871R → H in C7D. 1 Publication
    VAR_012647

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi610102. phenotype.
    Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
    PharmGKBiPA25941.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Add
    BLAST
    Chaini23 – 843821Complement component C7PRO_0000023583Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361C-linked (Man)
    Disulfide bondi85 ↔ 96By similarity
    Disulfide bondi91 ↔ 109By similarity
    Disulfide bondi103 ↔ 119By similarity
    Disulfide bondi128 ↔ 165By similarity
    Glycosylationi202 – 2021N-linked (GlcNAc...)2 Publications
    Disulfide bondi337 ↔ 3531 Publication
    Glycosylationi503 – 5031C-linked (Man); partial
    Glycosylationi506 – 5061C-linked (Man); partial
    Glycosylationi509 – 5091C-linked (Man); partial
    Disulfide bondi571 ↔ 613By similarity
    Disulfide bondi599 ↔ 626By similarity
    Disulfide bondi631 ↔ 673By similarity
    Disulfide bondi659 ↔ 688By similarity
    Glycosylationi696 – 6961O-linked (GalNAc...)1 Publication
    Disulfide bondi702 ↔ 7131 Publication
    Disulfide bondi715 ↔ 7501 Publication
    Disulfide bondi721 ↔ 7431 Publication
    Disulfide bondi728 ↔ 7631 Publication
    Glycosylationi754 – 7541N-linked (GlcNAc...) (complex)2 Publications
    Disulfide bondi773 ↔ 7821 Publication
    Disulfide bondi776 ↔ 7891 Publication
    Disulfide bondi791 ↔ 8251 Publication
    Disulfide bondi797 ↔ 8181 Publication
    Disulfide bondi805 ↔ 8381 Publication

    Post-translational modificationi

    C7 has 28 disulfide bridges.
    O- and C-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.5 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP10643.
    PaxDbiP10643.
    PRIDEiP10643.

    PTM databases

    PhosphoSiteiP10643.

    Expressioni

    Gene expression databases

    BgeeiP10643.
    CleanExiHS_C7.
    GenevestigatoriP10643.

    Organism-specific databases

    HPAiHPA001465.

    Interactioni

    Subunit structurei

    Monomer or dimer; as a C5b-7 complex it can also form multimeric rosettes. 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

    BioGridi107191. 3 interactions.
    IntActiP10643. 2 interactions.
    MINTiMINT-7032139.
    STRINGi9606.ENSP00000322061.

    Structurei

    Secondary structure

    1
    843
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi706 – 7094
    Beta strandi712 – 7154
    Helixi718 – 7203
    Beta strandi726 – 7316
    Turni732 – 7343
    Beta strandi737 – 7415
    Helixi742 – 7509
    Beta strandi755 – 7573
    Beta strandi766 – 7694
    Beta strandi778 – 7825
    Beta strandi784 – 7918
    Helixi794 – 7963
    Beta strandi803 – 8086
    Beta strandi811 – 8166
    Helixi817 – 82610
    Beta strandi831 – 8366

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WCYNMR-A693-843[»]
    ProteinModelPortaliP10643.
    SMRiP10643. Positions 25-843.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10643.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 8054TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini83 – 12139LDL-receptor class APROSITE-ProRule annotationAdd
    BLAST
    Domaini124 – 456333MACPFPROSITE-ProRule annotationAdd
    BLAST
    Domaini457 – 48731EGF-likeAdd
    BLAST
    Domaini500 – 54950TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini569 – 62860Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini629 – 69062Sushi 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni545 – 61571CCP 1Add
    BLAST
    Regioni616 – 69378CCP 2Add
    BLAST
    Regioni695 – 77076Factor I module (FIM) 1Add
    BLAST
    Regioni771 – 84373Factor I module (FIM) 2Add
    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 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation
    Contains 2 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiNOG145238.
    HOGENOMiHOG000111868.
    HOVERGENiHBG005367.
    InParanoidiP10643.
    KOiK03996.
    OMAiLLEPHCF.
    OrthoDBiEOG7ZSHS9.
    PhylomeDBiP10643.
    TreeFamiTF330498.

    Family and domain databases

    Gene3Di4.10.400.10. 1 hit.
    InterProiIPR003884. FacI_MAC.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001862. MAC_perforin.
    IPR020864. MACPF.
    IPR020863. MACPF_CS.
    IPR000436. Sushi_SCR_CCP.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF00057. Ldl_recept_a. 1 hit.
    PF01823. MACPF. 1 hit.
    PF00084. Sushi. 2 hits.
    PF00090. TSP_1. 2 hits.
    [Graphical view]
    PRINTSiPR00764. COMPLEMENTC9.
    SMARTiSM00032. CCP. 2 hits.
    SM00057. FIMAC. 2 hits.
    SM00192. LDLa. 1 hit.
    SM00457. MACPF. 1 hit.
    SM00209. TSP1. 2 hits.
    [Graphical view]
    SUPFAMiSSF57535. SSF57535. 2 hits.
    SSF82895. SSF82895. 2 hits.
    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.
    PS50923. SUSHI. 2 hits.
    PS50092. TSP1. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10643-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVISLFILV GFIGEFQSFS SASSPVNCQW DFYAPWSECN GCTKTQTRRR    50
    SVAVYGQYGG QPCVGNAFET QSCEPTRGCP TEEGCGERFR CFSGQCISKS 100
    LVCNGDSDCD EDSADEDRCE DSERRPSCDI DKPPPNIELT GNGYNELTGQ 150
    FRNRVINTKS FGGQCRKVFS GDGKDFYRLS GNVLSYTFQV KINNDFNYEF 200
    YNSTWSYVKH TSTEHTSSSR KRSFFRSSSS SSRSYTSHTN EIHKGKSYQL 250
    LVVENTVEVA QFINNNPEFL QLAEPFWKEL SHLPSLYDYS AYRRLIDQYG 300
    THYLQSGSLG GEYRVLFYVD SEKLKQNDFN SVEEKKCKSS GWHFVVKFSS 350
    HGCKELENAL KAASGTQNNV LRGEPFIRGG GAGFISGLSY LELDNPAGNK 400
    RRYSAWAESV TNLPQVIKQK LTPLYELVKE VPCASVKKLY LKWALEEYLD 450
    EFDPCHCRPC QNGGLATVEG THCLCHCKPY TFGAACEQGV LVGNQAGGVD 500
    GGWSCWSSWS PCVQGKKTRS RECNNPPPSG GGRSCVGETT ESTQCEDEEL 550
    EHLRLLEPHC FPLSLVPTEF CPSPPALKDG FVQDEGTMFP VGKNVVYTCN 600
    EGYSLIGNPV ARCGEDLRWL VGEMHCQKIA CVLPVLMDGI QSHPQKPFYT 650
    VGEKVTVSCS GGMSLEGPSA FLCGSSLKWS PEMKNARCVQ KENPLTQAVP 700
    KCQRWEKLQN SRCVCKMPYE CGPSLDVCAQ DERSKRILPL TVCKMHVLHC 750
    QGRNYTLTGR DSCTLPASAE KACGACPLWG KCDAESSKCV CREASECEEE 800
    GFSICVEVNG KEQTMSECEA GALRCRGQSI SVTSIRPCAA ETQ 843
    Length:843
    Mass (Da):93,518
    Last modified:March 15, 2005 - v2
    Checksum:iDBD5D7C92DF71FA5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti152 – 1521R → V in CAA60121. (PubMed:7730625)Curated
    Sequence conflicti821 – 8222GA → AL(PubMed:7730625)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281C → R.
    Corresponds to variant rs2271708 [ dbSNP | Ensembl ].
    VAR_050480
    Natural varianti220 – 2201R → Q in C7D. 1 Publication
    VAR_012643
    Natural varianti379 – 3791G → R in C7D. 1 Publication
    VAR_012644
    Natural varianti389 – 3891S → T Polymorphism confirmed at protein level. 2 Publications
    Corresponds to variant rs1063499 [ dbSNP | Ensembl ].
    VAR_033798
    Natural varianti420 – 4201K → Q.
    Corresponds to variant rs3792646 [ dbSNP | Ensembl ].
    VAR_022023
    Natural varianti521 – 5211R → S in C7D. 1 Publication
    Corresponds to variant rs121964920 [ dbSNP | Ensembl ].
    VAR_012645
    Natural varianti587 – 5871T → P Polymorphism confirmed at protein level. 2 Publications
    Corresponds to variant rs13157656 [ dbSNP | Ensembl ].
    VAR_033799
    Natural varianti682 – 6821E → Q in C7D. 1 Publication
    VAR_012646
    Natural varianti687 – 6871R → H in C7D. 1 Publication
    VAR_012647

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03507 mRNA. Translation: AAA51861.1.
    BC063851 mRNA. Translation: AAH63851.1.
    X86328
    , X86329, X86330, X86331, X86332, X86333, X86334, X86335, X86336, X86337, X86338, X86339, X86340, X86341, X86342, X86343, X86344 Genomic DNA. Translation: CAA60121.1.
    CCDSiCCDS47201.1.
    PIRiA27340.
    RefSeqiNP_000578.2. NM_000587.2.
    UniGeneiHs.78065.

    Genome annotation databases

    EnsembliENST00000313164; ENSP00000322061; ENSG00000112936.
    GeneIDi730.
    KEGGihsa:730.
    UCSCiuc003jmh.3. human.

    Polymorphism databases

    DMDMi61252057.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    C7base

    C7 mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03507 mRNA. Translation: AAA51861.1 .
    BC063851 mRNA. Translation: AAH63851.1 .
    X86328
    , X86329 , X86330 , X86331 , X86332 , X86333 , X86334 , X86335 , X86336 , X86337 , X86338 , X86339 , X86340 , X86341 , X86342 , X86343 , X86344 Genomic DNA. Translation: CAA60121.1 .
    CCDSi CCDS47201.1.
    PIRi A27340.
    RefSeqi NP_000578.2. NM_000587.2.
    UniGenei Hs.78065.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WCY NMR - A 693-843 [» ]
    ProteinModelPortali P10643.
    SMRi P10643. Positions 25-843.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107191. 3 interactions.
    IntActi P10643. 2 interactions.
    MINTi MINT-7032139.
    STRINGi 9606.ENSP00000322061.

    PTM databases

    PhosphoSitei P10643.

    Polymorphism databases

    DMDMi 61252057.

    Proteomic databases

    MaxQBi P10643.
    PaxDbi P10643.
    PRIDEi P10643.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313164 ; ENSP00000322061 ; ENSG00000112936 .
    GeneIDi 730.
    KEGGi hsa:730.
    UCSCi uc003jmh.3. human.

    Organism-specific databases

    CTDi 730.
    GeneCardsi GC05P040909.
    HGNCi HGNC:1346. C7.
    HPAi HPA001465.
    MIMi 217070. gene.
    610102. phenotype.
    neXtProti NX_P10643.
    Orphaneti 169150. Immunodeficiency due to a late component of complements deficiency.
    PharmGKBi PA25941.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145238.
    HOGENOMi HOG000111868.
    HOVERGENi HBG005367.
    InParanoidi P10643.
    KOi K03996.
    OMAi LLEPHCF.
    OrthoDBi EOG7ZSHS9.
    PhylomeDBi P10643.
    TreeFami TF330498.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi C7. human.
    EvolutionaryTracei P10643.
    GenomeRNAii 730.
    NextBioi 2972.
    PROi P10643.
    SOURCEi Search...

    Gene expression databases

    Bgeei P10643.
    CleanExi HS_C7.
    Genevestigatori P10643.

    Family and domain databases

    Gene3Di 4.10.400.10. 1 hit.
    InterProi IPR003884. FacI_MAC.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001862. MAC_perforin.
    IPR020864. MACPF.
    IPR020863. MACPF_CS.
    IPR000436. Sushi_SCR_CCP.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF00057. Ldl_recept_a. 1 hit.
    PF01823. MACPF. 1 hit.
    PF00084. Sushi. 2 hits.
    PF00090. TSP_1. 2 hits.
    [Graphical view ]
    PRINTSi PR00764. COMPLEMENTC9.
    SMARTi SM00032. CCP. 2 hits.
    SM00057. FIMAC. 2 hits.
    SM00192. LDLa. 1 hit.
    SM00457. MACPF. 1 hit.
    SM00209. TSP1. 2 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 2 hits.
    SSF82895. SSF82895. 2 hits.
    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.
    PS50923. SUSHI. 2 hits.
    PS50092. TSP1. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The structure of human complement component C7 and the C5b-7 complex."
      Discipio R.G., Chakravari D.N., Mueller-Eberhard H.J., Fey G.H.
      J. Biol. Chem. 263:549-560(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT PRO-587.
    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: PNS.
    3. "Structure of the human C7 gene and comparison with the C6, C8A, C8B and C9 genes."
      Hobart M.J., Fernie B.A., DiScipio R.G.
      J. Immunol. 154:5188-5194(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-822, VARIANT THR-389.
    4. "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-36; TRP-503; TRP-506 AND TRP-509.
    5. "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-202.
      Tissue: Plasma.
    6. "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-202 AND ASN-754.
      Tissue: Plasma.
    7. Cited for: GLYCOSYLATION AT ASN-754.
    8. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-696, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Solution structure of factor I-like modules from complement C7 reveals a pair of follistatin domains in compact pseudosymmetric arrangement."
      Phelan M.M., Thai C.-T., Soares D.C., Ogata R.T., Barlow P.N., Bramham J.
      J. Biol. Chem. 284:19637-19649(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 693-843, DISULFIDE BONDS.
    10. "Molecular bases of combined subtotal deficiencies of C6 and C7: their effects in combination with other C6 and C7 deficiencies."
      Fernie B.A., Wurzner R., Orren A., Morgan B.P., Potter P.C., Platonov A.E., Vershinina I.V., Shipulin G.A., Lachmann P.J., Hobart M.J.
      J. Immunol. 157:3648-3657(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT C7D SER-521.
    11. "Molecular bases of C7 deficiency: three different defects."
      Fernie B.A., Orren A., Sheehan G., Schlesinger M., Hobart M.J.
      J. Immunol. 159:1019-1026(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT C7D ARG-379.
    12. "Complement C7 deficiency: seven further molecular defects and their associated marker haplotypes."
      Fernie B.A., Hobart M.J.
      Hum. Genet. 103:513-519(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS C7D GLN-220; GLN-682 AND HIS-687.
    13. "Quantitative detection of single amino acid polymorphisms by targeted proteomics."
      Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
      J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS THR-389 AND PRO-587, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCO7_HUMAN
    AccessioniPrimary (citable) accession number: P10643
    Secondary accession number(s): Q6P3T5, Q92489
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 158 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3