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P13671

- CO6_HUMAN

UniProt

P13671 - CO6_HUMAN

Protein

Complement component C6

Gene

C6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (01 May 2007)
      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.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. complement activation Source: ProtInc
    2. complement activation, classical pathway Source: UniProtKB-KW
    3. cytolysis Source: UniProtKB-KW
    4. innate immune response Source: Reactome
    5. in utero embryonic development Source: Ensembl
    6. positive regulation of activation of membrane attack complex Source: Ensembl
    7. positive regulation of angiogenesis Source: Ensembl
    8. regulation of complement activation Source: Reactome

    Keywords - Biological processi

    Complement pathway, Cytolysis, Immunity, Innate immunity

    Enzyme and pathway databases

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

    Protein family/group databases

    TCDBi1.C.39.3.3. the membrane attack complex/perforin (macpf) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement component C6
    Gene namesi
    Name:C6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:1339. C6.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. membrane attack complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane attack complex, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Complement component 6 deficiency (C6D) [MIM:612446]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi612446. phenotype.
    Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
    PharmGKBiPA25921.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21211 PublicationAdd
    BLAST
    Chaini22 – 934913Complement component C6PRO_0000023579Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi22 ↔ 61
    Disulfide bondi24 ↔ 65
    Glycosylationi29 – 291C-linked (Man)
    Glycosylationi32 – 321C-linked (Man); partial
    Disulfide bondi35 ↔ 73
    Glycosylationi38 – 381O-linked (Fuc...)1 Publication
    Disulfide bondi39 ↔ 78
    Disulfide bondi82 ↔ 117
    Glycosylationi90 – 901C-linked (Man); partial
    Disulfide bondi93 ↔ 127
    Disulfide bondi96 ↔ 133
    Disulfide bondi140 ↔ 151
    Disulfide bondi146 ↔ 164
    Disulfide bondi158 ↔ 173
    Disulfide bondi180 ↔ 218
    Glycosylationi324 – 3241N-linked (GlcNAc...)2 Publications
    Glycosylationi392 – 3921O-linked (Fuc...)1 Publication
    Disulfide bondi399 ↔ 420
    Disulfide bondi499 ↔ 623
    Disulfide bondi521 ↔ 570
    Disulfide bondi523 ↔ 539
    Disulfide bondi526 ↔ 541
    Disulfide bondi543 ↔ 552
    Glycosylationi568 – 5681C-linked (Man); partial
    Glycosylationi571 – 5711C-linked (Man); partial
    Glycosylationi574 – 5741C-linked (Man); partial
    Disulfide bondi577 ↔ 611
    Disulfide bondi589 ↔ 601
    Disulfide bondi644 ↔ 686
    Disulfide bondi672 ↔ 699
    Disulfide bondi704 ↔ 746
    Disulfide bondi732 ↔ 761
    Disulfide bondi773 ↔ 823
    Disulfide bondi784 ↔ 801
    Disulfide bondi786 ↔ 837
    Disulfide bondi793 ↔ 816
    Glycosylationi855 – 8551N-linked (GlcNAc...)1 Publication
    Disulfide bondi862 ↔ 873
    Disulfide bondi867 ↔ 919
    Disulfide bondi880 ↔ 897
    Disulfide bondi882 ↔ 932
    Disulfide bondi888 ↔ 912

    Post-translational modificationi

    All cysteine residues are assumed to be cross-linked to one another. Individual modules containing an even number of conserved cysteine residues are supposed to have disulfide linkages only within the same module.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP13671.
    PRIDEiP13671.

    PTM databases

    PhosphoSiteiP13671.

    Expressioni

    Gene expression databases

    ArrayExpressiP13671.
    BgeeiP13671.
    CleanExiHS_C6.
    GenevestigatoriP13671.

    Organism-specific databases

    HPAiHPA043823.

    Interactioni

    Subunit structurei

    Component of the membrane attack complex (MAC). MAC assembly is initiated by proteolytic cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and 12-14 copies of the pore-forming subunit C9.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163332EBI-1753221,EBI-389883

    Protein-protein interaction databases

    BioGridi107190. 3 interactions.
    IntActiP13671. 5 interactions.
    STRINGi9606.ENSP00000263413.

    Structurei

    Secondary structure

    1
    934
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 263
    Beta strandi38 – 403
    Beta strandi42 – 487
    Helixi54 – 585
    Helixi61 – 644
    Beta strandi68 – 736
    Beta strandi95 – 973
    Beta strandi100 – 1045
    Beta strandi106 – 1083
    Beta strandi121 – 1255
    Beta strandi130 – 1334
    Beta strandi141 – 1455
    Beta strandi151 – 1533
    Helixi154 – 1563
    Beta strandi157 – 1615
    Beta strandi164 – 1674
    Helixi168 – 1703
    Beta strandi179 – 1824
    Helixi190 – 1945
    Beta strandi195 – 1984
    Turni199 – 2024
    Beta strandi203 – 2075
    Beta strandi226 – 2283
    Beta strandi236 – 2405
    Helixi247 – 2493
    Beta strandi250 – 2567
    Helixi258 – 2625
    Beta strandi279 – 2824
    Turni287 – 2893
    Helixi298 – 30710
    Beta strandi309 – 32719
    Beta strandi329 – 3313
    Helixi336 – 3416
    Helixi351 – 36111
    Beta strandi363 – 3653
    Beta strandi367 – 38216
    Helixi383 – 3897
    Helixi393 – 40715
    Helixi418 – 4203
    Helixi426 – 4294
    Helixi434 – 4363
    Beta strandi437 – 4426
    Beta strandi445 – 4473
    Helixi449 – 4557
    Beta strandi461 – 4655
    Helixi466 – 47813
    Beta strandi481 – 4866
    Beta strandi487 – 4893
    Helixi490 – 4934
    Helixi500 – 51617
    Helixi520 – 5223
    Turni527 – 5293
    Beta strandi530 – 5356
    Beta strandi538 – 5425
    Beta strandi547 – 5493
    Helixi550 – 5523
    Beta strandi579 – 5868
    Beta strandi595 – 5973
    Beta strandi605 – 6106
    Beta strandi643 – 6453
    Beta strandi653 – 6564
    Beta strandi660 – 6634
    Beta strandi667 – 6726
    Beta strandi676 – 6805
    Beta strandi683 – 6864
    Beta strandi688 – 6925
    Beta strandi698 – 7014
    Beta strandi703 – 7053
    Beta strandi711 – 7144
    Beta strandi715 – 7173
    Beta strandi720 – 7234
    Beta strandi727 – 7293
    Beta strandi734 – 7363
    Beta strandi737 – 7404
    Beta strandi742 – 7454
    Beta strandi747 – 7493
    Beta strandi755 – 7573
    Turni772 – 7765
    Beta strandi778 – 7836
    Helixi789 – 7924
    Beta strandi798 – 8047
    Turni805 – 8084
    Beta strandi809 – 8146
    Helixi815 – 8228
    Helixi825 – 8273
    Beta strandi829 – 8368
    Helixi841 – 85111
    Beta strandi853 – 8575
    Beta strandi862 – 8643
    Beta strandi875 – 8773
    Beta strandi879 – 8813
    Helixi885 – 8917
    Beta strandi897 – 8993
    Beta strandi901 – 9033
    Beta strandi905 – 9073
    Helixi911 – 92010
    Beta strandi925 – 9306

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3T5OX-ray2.87A22-934[»]
    4A5WX-ray3.50B22-934[»]
    4E0SX-ray4.21B22-934[»]
    ProteinModelPortaliP13671.
    SMRiP13671. Positions 22-934.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 7958TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini81 – 13454TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini138 – 17538LDL-receptor class APROSITE-ProRule annotationAdd
    BLAST
    Domaini176 – 522347MACPFPROSITE-ProRule annotationAdd
    BLAST
    Domaini523 – 55331EGF-likeAdd
    BLAST
    Domaini565 – 61248TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini642 – 70160Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini702 – 76362Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini780 – 83960Kazal-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini876 – 93459Kazal-like 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni611 – 68878CCP 1Add
    BLAST
    Regioni642 – 934293C5b-binding domainAdd
    BLAST
    Regioni689 – 76577CCP 2Add
    BLAST
    Regioni766 – 84075Factor I module (FIM) 1Add
    BLAST
    Regioni858 – 93477Factor I module (FIM) 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the complement C6/C7/C8/C9 family.Curated
    Contains 1 EGF-like domain.Curated
    Contains 2 Kazal-like domains.PROSITE-ProRule annotation
    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 3 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiNOG145238.
    HOGENOMiHOG000111865.
    HOVERGENiHBG005366.
    InParanoidiP13671.
    KOiK03995.
    OMAiCVCQSGT.
    OrthoDBiEOG7NPFT9.
    PhylomeDBiP13671.
    TreeFamiTF330498.

    Family and domain databases

    InterProiIPR003884. FacI_MAC.
    IPR002350. Kazal_dom.
    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]
    PfamiPF07648. Kazal_2. 1 hit.
    PF00057. Ldl_recept_a. 1 hit.
    PF01823. MACPF. 1 hit.
    PF00084. Sushi. 2 hits.
    PF00090. TSP_1. 3 hits.
    [Graphical view]
    PRINTSiPR00764. COMPLEMENTC9.
    SMARTiSM00032. CCP. 2 hits.
    SM00057. FIMAC. 2 hits.
    SM00280. KAZAL. 1 hit.
    SM00192. LDLa. 1 hit.
    SM00457. MACPF. 1 hit.
    SM00209. TSP1. 3 hits.
    [Graphical view]
    SUPFAMiSSF57424. SSF57424. 1 hit.
    SSF57535. SSF57535. 2 hits.
    SSF82895. SSF82895. 3 hits.
    PROSITEiPS00022. EGF_1. 1 hit.
    PS51465. KAZAL_2. 2 hits.
    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. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P13671-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARRSVLYFI LLNALINKGQ ACFCDHYAWT QWTSCSKTCN SGTQSRHRQI    50
    VVDKYYQENF CEQICSKQET RECNWQRCPI NCLLGDFGPW SDCDPCIEKQ 100
    SKVRSVLRPS QFGGQPCTAP LVAFQPCIPS KLCKIEEADC KNKFRCDSGR 150
    CIARKLECNG ENDCGDNSDE RDCGRTKAVC TRKYNPIPSV QLMGNGFHFL 200
    AGEPRGEVLD NSFTGGICKT VKSSRTSNPY RVPANLENVG FEVQTAEDDL 250
    KTDFYKDLTS LGHNENQQGS FSSQGGSSFS VPIFYSSKRS ENINHNSAFK 300
    QAIQASHKKD SSFIRIHKVM KVLNFTTKAK DLHLSDVFLK ALNHLPLEYN 350
    SALYSRIFDD FGTHYFTSGS LGGVYDLLYQ FSSEELKNSG LTEEEAKHCV 400
    RIETKKRVLF AKKTKVEHRC TTNKLSEKHE GSFIQGAEKS ISLIRGGRSE 450
    YGAALAWEKG SSGLEEKTFS EWLESVKENP AVIDFELAPI VDLVRNIPCA 500
    VTKRNNLRKA LQEYAAKFDP CQCAPCPNNG RPTLSGTECL CVCQSGTYGE 550
    NCEKQSPDYK SNAVDGQWGC WSSWSTCDAT YKRSRTRECN NPAPQRGGKR 600
    CEGEKRQEED CTFSIMENNG QPCINDDEEM KEVDLPEIEA DSGCPQPVPP 650
    ENGFIRNEKQ LYLVGEDVEI SCLTGFETVG YQYFRCLPDG TWRQGDVECQ 700
    RTECIKPVVQ EVLTITPFQR LYRIGESIEL TCPKGFVVAG PSRYTCQGNS 750
    WTPPISNSLT CEKDTLTKLK GHCQLGQKQS GSECICMSPE EDCSHHSEDL 800
    CVFDTDSNDY FTSPACKFLA EKCLNNQQLH FLHIGSCQDG RQLEWGLERT 850
    RLSSNSTKKE SCGYDTCYDW EKCSASTSKC VCLLPPQCFK GGNQLYCVKM 900
    GSSTSEKTLN ICEVGTIRCA NRKMEILHPG KCLA 934
    Length:934
    Mass (Da):104,786
    Last modified:May 1, 2007 - v3
    Checksum:iA88F4BED7CC349D3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti567 – 5671Q → H in BAD02321. 1 PublicationCurated
    Sequence conflicti616 – 6161M → I in BAD02321. 1 PublicationCurated
    Sequence conflicti934 – 9341A → T in BAD02321. 1 PublicationCurated

    Polymorphismi

    The sequence shown is that of allotype C6 B.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti119 – 1191A → E in allotype C6 A. 5 Publications
    Corresponds to variant rs1801033 [ dbSNP | Ensembl ].
    VAR_006056
    Natural varianti397 – 3971K → E.
    Corresponds to variant rs6896011 [ dbSNP | Ensembl ].
    VAR_027647
    Natural varianti470 – 4701S → F.
    Corresponds to variant rs10462014 [ dbSNP | Ensembl ].
    VAR_027648

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05064 mRNA. Translation: AAA51860.1.
    J05024 mRNA. Translation: AAA59668.1.
    X72177 Genomic DNA. Translation: CAA50994.1.
    AB126592 mRNA. Translation: BAD02321.1.
    AC008863 Genomic DNA. No translation available.
    AC091871 Genomic DNA. No translation available.
    BC035723 mRNA. Translation: AAH35723.1.
    J04506 mRNA. Translation: AAB59433.1.
    CCDSiCCDS3936.1.
    PIRiA34372.
    RefSeqiNP_000056.2. NM_000065.3.
    NP_001108603.2. NM_001115131.2.
    UniGeneiHs.481992.

    Genome annotation databases

    EnsembliENST00000263413; ENSP00000263413; ENSG00000039537.
    ENST00000337836; ENSP00000338861; ENSG00000039537.
    GeneIDi729.
    KEGGihsa:729.
    UCSCiuc003jmk.3. human.

    Polymorphism databases

    DMDMi146345396.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    C6base

    C6 mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05064 mRNA. Translation: AAA51860.1 .
    J05024 mRNA. Translation: AAA59668.1 .
    X72177 Genomic DNA. Translation: CAA50994.1 .
    AB126592 mRNA. Translation: BAD02321.1 .
    AC008863 Genomic DNA. No translation available.
    AC091871 Genomic DNA. No translation available.
    BC035723 mRNA. Translation: AAH35723.1 .
    J04506 mRNA. Translation: AAB59433.1 .
    CCDSi CCDS3936.1.
    PIRi A34372.
    RefSeqi NP_000056.2. NM_000065.3.
    NP_001108603.2. NM_001115131.2.
    UniGenei Hs.481992.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3T5O X-ray 2.87 A 22-934 [» ]
    4A5W X-ray 3.50 B 22-934 [» ]
    4E0S X-ray 4.21 B 22-934 [» ]
    ProteinModelPortali P13671.
    SMRi P13671. Positions 22-934.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107190. 3 interactions.
    IntActi P13671. 5 interactions.
    STRINGi 9606.ENSP00000263413.

    Protein family/group databases

    TCDBi 1.C.39.3.3. the membrane attack complex/perforin (macpf) family.

    PTM databases

    PhosphoSitei P13671.

    Polymorphism databases

    DMDMi 146345396.

    Proteomic databases

    PaxDbi P13671.
    PRIDEi P13671.

    Protocols and materials databases

    DNASUi 729.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263413 ; ENSP00000263413 ; ENSG00000039537 .
    ENST00000337836 ; ENSP00000338861 ; ENSG00000039537 .
    GeneIDi 729.
    KEGGi hsa:729.
    UCSCi uc003jmk.3. human.

    Organism-specific databases

    CTDi 729.
    GeneCardsi GC05M041178.
    H-InvDB HIX0024838.
    HGNCi HGNC:1339. C6.
    HPAi HPA043823.
    MIMi 217050. gene.
    612446. phenotype.
    neXtProti NX_P13671.
    Orphaneti 169150. Immunodeficiency due to a late component of complements deficiency.
    PharmGKBi PA25921.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145238.
    HOGENOMi HOG000111865.
    HOVERGENi HBG005366.
    InParanoidi P13671.
    KOi K03995.
    OMAi CVCQSGT.
    OrthoDBi EOG7NPFT9.
    PhylomeDBi P13671.
    TreeFami TF330498.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi C6. human.
    GeneWikii Complement_component_6.
    GenomeRNAii 729.
    NextBioi 2968.
    PROi P13671.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13671.
    Bgeei P13671.
    CleanExi HS_C6.
    Genevestigatori P13671.

    Family and domain databases

    InterProi IPR003884. FacI_MAC.
    IPR002350. Kazal_dom.
    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 PF07648. Kazal_2. 1 hit.
    PF00057. Ldl_recept_a. 1 hit.
    PF01823. MACPF. 1 hit.
    PF00084. Sushi. 2 hits.
    PF00090. TSP_1. 3 hits.
    [Graphical view ]
    PRINTSi PR00764. COMPLEMENTC9.
    SMARTi SM00032. CCP. 2 hits.
    SM00057. FIMAC. 2 hits.
    SM00280. KAZAL. 1 hit.
    SM00192. LDLa. 1 hit.
    SM00457. MACPF. 1 hit.
    SM00209. TSP1. 3 hits.
    [Graphical view ]
    SUPFAMi SSF57424. SSF57424. 1 hit.
    SSF57535. SSF57535. 2 hits.
    SSF82895. SSF82895. 3 hits.
    PROSITEi PS00022. EGF_1. 1 hit.
    PS51465. KAZAL_2. 2 hits.
    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. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6."
      Haefliger J.-A., Tschopp J., Vial N., Jenne D.E.
      J. Biol. Chem. 264:18041-18051(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-31 AND 633-640.
    2. "The molecular architecture of human complement component C6."
      Discipio R.G., Hugli T.E.
      J. Biol. Chem. 264:16197-16206(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-119.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-119.
      Tissue: Blood.
    4. "Sequence variation in C6 locus."
      Soejima M., Koda Y.
      Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      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], VARIANT GLU-119.
      Tissue: Ovary.
    7. "Structural homology of complement protein C6 with other channel-forming proteins of complement."
      Chakravarti D.N., Chakravarti B., Parra C.A., Mueller-Eberhard H.J.
      Proc. Natl. Acad. Sci. U.S.A. 86:2799-2803(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-491, VARIANT GLU-119.
    8. "Elucidation of the disulfide-bonding pattern in the factor I modules of the sixth component (C6) of human complement."
      Lengweiler S., Schaller J., DiScipio R.G., Rickli E.E.
      Biochim. Biophys. Acta 1342:13-18(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS IN FACTOR I MODULE 1 REGION.
    9. "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-29; TRP-32; TRP-90; TRP-568; TRP-571 AND TRP-574.
    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-324 AND ASN-855.
      Tissue: Plasma.
    11. "Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC)."
      Aleshin A.E., Schraufstatter I.U., Stec B., Bankston L.A., Liddington R.C., DiScipio R.G.
      J. Biol. Chem. 287:10210-10222(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 22-934, GLYCOSYLATION AT TRP-29; TRP-32; THR-38; ASN-324; THR-392; TRP-568 AND TRP-571, SUBUNIT, DISULFIDE BONDS.
    12. "Polymorphism of human complement component C6: an amino acid substitution (Glu/Ala) within the second thrombospondin repeat differentiates between the two common allotypes C6 A and C6 B."
      Dewald G., Nothen M.M., Cichon S.
      Biochem. Biophys. Res. Commun. 194:458-464(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ALLOTYPE C6 A GLU-119.
    13. "Meningococccal meningitis and complement component 6 deficiency associated with oculocutaneous albinism."
      Ikinciogullari A., Tekin M., Dogu F., Reisli I., Tanir G., Yi Z., Garrison N., Brilliant M.H., Babacan E.
      Eur. J. Pediatr. 164:177-179(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN COMPLEMENT COMPONENT 6 DEFICIENCY.

    Entry informationi

    Entry nameiCO6_HUMAN
    AccessioniPrimary (citable) accession number: P13671
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 159 of the entry and version 3 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