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P13671

- CO6_HUMAN

UniProt

P13671 - CO6_HUMAN

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Protein

Complement component C6

Gene

C6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 - 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. regulation of complement activation Source: Reactome
Complete GO annotation...

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. extracellular vesicular exosome Source: UniProtKB
  3. membrane attack complex Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiP13671.
CleanExiHS_C6.
ExpressionAtlasiP13671. baseline and differential.
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 – 263Combined sources
Beta strandi38 – 403Combined sources
Beta strandi42 – 487Combined sources
Helixi54 – 585Combined sources
Helixi61 – 644Combined sources
Beta strandi68 – 736Combined sources
Beta strandi95 – 973Combined sources
Beta strandi100 – 1045Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi151 – 1533Combined sources
Helixi154 – 1563Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi164 – 1674Combined sources
Helixi168 – 1703Combined sources
Beta strandi179 – 1824Combined sources
Helixi190 – 1945Combined sources
Beta strandi195 – 1984Combined sources
Turni199 – 2024Combined sources
Beta strandi203 – 2075Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi236 – 2405Combined sources
Helixi247 – 2493Combined sources
Beta strandi250 – 2567Combined sources
Helixi258 – 2625Combined sources
Beta strandi279 – 2824Combined sources
Turni287 – 2893Combined sources
Helixi298 – 30710Combined sources
Beta strandi309 – 32719Combined sources
Beta strandi329 – 3313Combined sources
Helixi336 – 3416Combined sources
Helixi351 – 36111Combined sources
Beta strandi363 – 3653Combined sources
Beta strandi367 – 38216Combined sources
Helixi383 – 3897Combined sources
Helixi393 – 40715Combined sources
Helixi418 – 4203Combined sources
Helixi426 – 4294Combined sources
Helixi434 – 4363Combined sources
Beta strandi437 – 4426Combined sources
Beta strandi445 – 4473Combined sources
Helixi449 – 4557Combined sources
Beta strandi461 – 4655Combined sources
Helixi466 – 47813Combined sources
Beta strandi481 – 4866Combined sources
Beta strandi487 – 4893Combined sources
Helixi490 – 4934Combined sources
Helixi500 – 51617Combined sources
Helixi520 – 5223Combined sources
Turni527 – 5293Combined sources
Beta strandi530 – 5356Combined sources
Beta strandi538 – 5425Combined sources
Beta strandi547 – 5493Combined sources
Helixi550 – 5523Combined sources
Beta strandi579 – 5868Combined sources
Beta strandi595 – 5973Combined sources
Beta strandi605 – 6106Combined sources
Beta strandi643 – 6453Combined sources
Beta strandi653 – 6564Combined sources
Beta strandi660 – 6634Combined sources
Beta strandi667 – 6726Combined sources
Beta strandi676 – 6805Combined sources
Beta strandi683 – 6864Combined sources
Beta strandi688 – 6925Combined sources
Beta strandi698 – 7014Combined sources
Beta strandi703 – 7053Combined sources
Beta strandi711 – 7144Combined sources
Beta strandi715 – 7173Combined sources
Beta strandi720 – 7234Combined sources
Beta strandi727 – 7293Combined sources
Beta strandi734 – 7363Combined sources
Beta strandi737 – 7404Combined sources
Beta strandi742 – 7454Combined sources
Beta strandi747 – 7493Combined sources
Beta strandi755 – 7573Combined sources
Turni772 – 7765Combined sources
Beta strandi778 – 7836Combined sources
Helixi789 – 7924Combined sources
Beta strandi798 – 8047Combined sources
Turni805 – 8084Combined sources
Beta strandi809 – 8146Combined sources
Helixi815 – 8228Combined sources
Helixi825 – 8273Combined sources
Beta strandi829 – 8368Combined sources
Helixi841 – 85111Combined sources
Beta strandi853 – 8575Combined sources
Beta strandi862 – 8643Combined sources
Beta strandi875 – 8773Combined sources
Beta strandi879 – 8813Combined sources
Helixi885 – 8917Combined sources
Beta strandi897 – 8993Combined sources
Beta strandi901 – 9033Combined sources
Beta strandi905 – 9073Combined sources
Helixi911 – 92010Combined sources
Beta strandi925 – 9306Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074478.
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

        10         20         30         40         50
MARRSVLYFI LLNALINKGQ ACFCDHYAWT QWTSCSKTCN SGTQSRHRQI
60 70 80 90 100
VVDKYYQENF CEQICSKQET RECNWQRCPI NCLLGDFGPW SDCDPCIEKQ
110 120 130 140 150
SKVRSVLRPS QFGGQPCTAP LVAFQPCIPS KLCKIEEADC KNKFRCDSGR
160 170 180 190 200
CIARKLECNG ENDCGDNSDE RDCGRTKAVC TRKYNPIPSV QLMGNGFHFL
210 220 230 240 250
AGEPRGEVLD NSFTGGICKT VKSSRTSNPY RVPANLENVG FEVQTAEDDL
260 270 280 290 300
KTDFYKDLTS LGHNENQQGS FSSQGGSSFS VPIFYSSKRS ENINHNSAFK
310 320 330 340 350
QAIQASHKKD SSFIRIHKVM KVLNFTTKAK DLHLSDVFLK ALNHLPLEYN
360 370 380 390 400
SALYSRIFDD FGTHYFTSGS LGGVYDLLYQ FSSEELKNSG LTEEEAKHCV
410 420 430 440 450
RIETKKRVLF AKKTKVEHRC TTNKLSEKHE GSFIQGAEKS ISLIRGGRSE
460 470 480 490 500
YGAALAWEKG SSGLEEKTFS EWLESVKENP AVIDFELAPI VDLVRNIPCA
510 520 530 540 550
VTKRNNLRKA LQEYAAKFDP CQCAPCPNNG RPTLSGTECL CVCQSGTYGE
560 570 580 590 600
NCEKQSPDYK SNAVDGQWGC WSSWSTCDAT YKRSRTRECN NPAPQRGGKR
610 620 630 640 650
CEGEKRQEED CTFSIMENNG QPCINDDEEM KEVDLPEIEA DSGCPQPVPP
660 670 680 690 700
ENGFIRNEKQ LYLVGEDVEI SCLTGFETVG YQYFRCLPDG TWRQGDVECQ
710 720 730 740 750
RTECIKPVVQ EVLTITPFQR LYRIGESIEL TCPKGFVVAG PSRYTCQGNS
760 770 780 790 800
WTPPISNSLT CEKDTLTKLK GHCQLGQKQS GSECICMSPE EDCSHHSEDL
810 820 830 840 850
CVFDTDSNDY FTSPACKFLA EKCLNNQQLH FLHIGSCQDG RQLEWGLERT
860 870 880 890 900
RLSSNSTKKE SCGYDTCYDW EKCSASTSKC VCLLPPQCFK GGNQLYCVKM
910 920 930
GSSTSEKTLN ICEVGTIRCA NRKMEILHPG KCLA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 GC05M041142.
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.
GeneTreei ENSGT00550000074478.
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

Bgeei P13671.
CleanExi HS_C6.
ExpressionAtlasi P13671. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 161 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

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