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P07357

- CO8A_HUMAN

UniProt

P07357 - CO8A_HUMAN

Protein

Complement component C8 alpha chain

Gene

C8A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      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. C8A inserts into the target membrane, but does not form pores by itself.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei43 – 431Not glycosylated

    GO - Biological processi

    1. complement activation Source: MGI
    2. complement activation, alternative pathway Source: UniProtKB-KW
    3. complement activation, classical pathway Source: UniProtKB-KW
    4. cytolysis Source: UniProtKB-KW
    5. immune response Source: ProtInc
    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.

    Protein family/group databases

    TCDBi1.C.39.3.1. the membrane attack complex/perforin (macpf) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement component C8 alpha chain
    Alternative name(s):
    Complement component 8 subunit alpha
    Gene namesi
    Name:C8A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1352. C8A.

    Subcellular locationi

    Secreted. Cell membrane; Multi-pass membrane protein
    Note: Secreted as soluble protein. Inserts into the cell membrane of target cells.

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: Reactome
    3. extracellular space Source: ProtInc
    4. membrane Source: ProtInc
    5. membrane attack complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Membrane attack complex, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Complement component 8 deficiency, 1 (C8D1) [MIM:613790]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi613790. phenotype.
    Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
    PharmGKBiPA25951.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 3010Sequence AnalysisPRO_0000023585
    Chaini31 – 584554Complement component C8 alpha chainPRO_0000023586Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi39 ↔ 74By similarity
    Glycosylationi44 – 441C-linked (Man)
    Disulfide bondi50 ↔ 53By similarity
    Disulfide bondi84 ↔ 90By similarity
    Disulfide bondi96 ↔ 108By similarity
    Disulfide bondi102 ↔ 121By similarity
    Disulfide bondi115 ↔ 130By similarity
    Disulfide bondi140 ↔ 177
    Disulfide bondi194 – 194Interchain (with C-60 in C8-gamma chain)
    Disulfide bondi375 ↔ 399
    Glycosylationi437 – 4371N-linked (GlcNAc...)2 Publications
    Glycosylationi542 – 5421C-linked (Man)
    Glycosylationi545 – 5451C-linked (Man)
    Glycosylationi548 – 5481C-linked (Man)

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP07357.
    PaxDbiP07357.
    PRIDEiP07357.

    PTM databases

    PhosphoSiteiP07357.

    Expressioni

    Gene expression databases

    BgeeiP07357.
    CleanExiHS_C8A.
    GenevestigatoriP07357.

    Interactioni

    Subunit structurei

    Heterotrimer of 3 chains: alpha, beta and gamma. The alpha and gamma chains are disulfide bonded. 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 C9.3 Publications

    Protein-protein interaction databases

    BioGridi107192. 2 interactions.
    DIPiDIP-1125N.
    STRINGi9606.ENSP00000354458.

    Structurei

    Secondary structure

    1
    584
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni52 – 543
    Beta strandi56 – 605
    Beta strandi63 – 653
    Beta strandi78 – 836
    Beta strandi97 – 1015
    Beta strandi103 – 1053
    Helixi111 – 1133
    Beta strandi116 – 1183
    Beta strandi121 – 1233
    Beta strandi127 – 1293
    Beta strandi140 – 1434
    Helixi149 – 1524
    Beta strandi154 – 1574
    Turni158 – 1614
    Beta strandi162 – 1687
    Beta strandi179 – 1824
    Turni183 – 1864
    Beta strandi189 – 1913
    Turni192 – 1954
    Beta strandi196 – 1983
    Helixi201 – 2033
    Beta strandi204 – 2074
    Beta strandi212 – 2176
    Beta strandi226 – 2327
    Helixi233 – 24311
    Beta strandi246 – 2527
    Beta strandi260 – 2667
    Helixi273 – 2808
    Beta strandi287 – 30317
    Beta strandi305 – 3084
    Helixi312 – 3198
    Helixi327 – 33711
    Beta strandi339 – 35820
    Helixi359 – 3657
    Helixi369 – 37911
    Helixi398 – 4025
    Helixi408 – 4136
    Beta strandi416 – 4216
    Helixi443 – 4497
    Turni450 – 4523
    Beta strandi455 – 4639
    Helixi464 – 4707
    Helixi477 – 49115
    Helixi496 – 4983
    Turni503 – 5053
    Beta strandi508 – 5114
    Beta strandi514 – 5174
    Beta strandi525 – 5273
    Beta strandi552 – 5543
    Beta strandi556 – 5594
    Beta strandi578 – 5825

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QOSX-ray1.81A188-198[»]
    2QQHX-ray2.50A133-366[»]
    A410-492[»]
    2RD7X-ray2.15A133-492[»]
    3OJYX-ray2.51A31-584[»]
    ProteinModelPortaliP07357.
    SMRiP07357. Positions 32-582.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07357.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 9154TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini94 – 13239LDL-receptor class APROSITE-ProRule annotationAdd
    BLAST
    Domaini135 – 498364MACPFPROSITE-ProRule annotationAdd
    BLAST
    Domaini499 – 52931EGF-likeAdd
    BLAST
    Domaini539 – 58345TSP type-1 2PROSITE-ProRule annotationAdd
    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 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiNOG48024.
    HOGENOMiHOG000231146.
    HOVERGENiHBG005368.
    InParanoidiP07357.
    KOiK03997.
    OMAiFMRIFTK.
    OrthoDBiEOG7CRTPG.
    PhylomeDBiP07357.
    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. 2 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 3 hits.
    SSF82895. SSF82895. 2 hits.
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01209. LDLRA_1. 1 hit.
    PS50068. LDLRA_2. 1 hit.
    PS00279. MACPF_1. 1 hit.
    PS51412. MACPF_2. 1 hit.
    PS50092. TSP1. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07357-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFAVVFFILS LMTCQPGVTA QEKVNQRVRR AATPAAVTCQ LSNWSEWTDC    50
    FPCQDKKYRH RSLLQPNKFG GTICSGDIWD QASCSSSTTC VRQAQCGQDF 100
    QCKETGRCLK RHLVCNGDQD CLDGSDEDDC EDVRAIDEDC SQYEPIPGSQ 150
    KAALGYNILT QEDAQSVYDA SYYGGQCETV YNGEWRELRY DSTCERLYYG 200
    DDEKYFRKPY NFLKYHFEAL ADTGISSEFY DNANDLLSKV KKDKSDSFGV 250
    TIGIGPAGSP LLVGVGVSHS QDTSFLNELN KYNEKKFIFT RIFTKVQTAH 300
    FKMRKDDIML DEGMLQSLME LPDQYNYGMY AKFINDYGTH YITSGSMGGI 350
    YEYILVIDKA KMESLGITSR DITTCFGGSL GIQYEDKINV GGGLSGDHCK 400
    KFGGGKTERA RKAMAVEDII SRVRGGSSGW SGGLAQNRST ITYRSWGRSL 450
    KYNPVVIDFE MQPIHEVLRH TSLGPLEAKR QNLRRALDQY LMEFNACRCG 500
    PCFNNGVPIL EGTSCRCQCR LGSLGAACEQ TQTEGAKADG SWSCWSSWSV 550
    CRAGIQERRR ECDNPAPQNG GASCPGRKVQ TQAC 584
    Length:584
    Mass (Da):65,163
    Last modified:February 1, 1995 - v2
    Checksum:i9F61DDA51D2F3BBA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti575 – 5751P → S in AAA82124. (PubMed:7759071)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti93 – 931Q → K in allele C8A*B. 2 Publications
    Corresponds to variant rs652785 [ dbSNP | Ensembl ].
    VAR_011889
    Natural varianti407 – 4071T → I.
    Corresponds to variant rs706479 [ dbSNP | Ensembl ].
    VAR_011890
    Natural varianti458 – 4581D → N.
    Corresponds to variant rs17114555 [ dbSNP | Ensembl ].
    VAR_033800
    Natural varianti485 – 4851R → L.
    Corresponds to variant rs1620075 [ dbSNP | Ensembl ].
    VAR_011891
    Natural varianti561 – 5611E → Q.
    Corresponds to variant rs1342440 [ dbSNP | Ensembl ].
    VAR_011892
    Natural varianti575 – 5751P → L.
    Corresponds to variant rs17300936 [ dbSNP | Ensembl ].
    VAR_033801

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16974 mRNA. Translation: AAA52200.1.
    U08006
    , U07996, U07997, U07998, U07999, U08000, U08001, U08002, U08003, U08004, U08005 Genomic DNA. Translation: AAA82124.1.
    AL121998 Genomic DNA. Translation: CAI19172.1.
    BC132911 mRNA. Translation: AAI32912.1.
    BC132913 mRNA. Translation: AAI32914.1.
    CCDSiCCDS606.1.
    PIRiI37213. C8HUA.
    RefSeqiNP_000553.1. NM_000562.2.
    UniGeneiHs.93210.

    Genome annotation databases

    EnsembliENST00000361249; ENSP00000354458; ENSG00000157131.
    GeneIDi731.
    KEGGihsa:731.
    UCSCiuc001cyo.2. human.

    Polymorphism databases

    DMDMi729167.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16974 mRNA. Translation: AAA52200.1 .
    U08006
    , U07996 , U07997 , U07998 , U07999 , U08000 , U08001 , U08002 , U08003 , U08004 , U08005 Genomic DNA. Translation: AAA82124.1 .
    AL121998 Genomic DNA. Translation: CAI19172.1 .
    BC132911 mRNA. Translation: AAI32912.1 .
    BC132913 mRNA. Translation: AAI32914.1 .
    CCDSi CCDS606.1.
    PIRi I37213. C8HUA.
    RefSeqi NP_000553.1. NM_000562.2.
    UniGenei Hs.93210.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QOS X-ray 1.81 A 188-198 [» ]
    2QQH X-ray 2.50 A 133-366 [» ]
    A 410-492 [» ]
    2RD7 X-ray 2.15 A 133-492 [» ]
    3OJY X-ray 2.51 A 31-584 [» ]
    ProteinModelPortali P07357.
    SMRi P07357. Positions 32-582.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107192. 2 interactions.
    DIPi DIP-1125N.
    STRINGi 9606.ENSP00000354458.

    Protein family/group databases

    TCDBi 1.C.39.3.1. the membrane attack complex/perforin (macpf) family.

    PTM databases

    PhosphoSitei P07357.

    Polymorphism databases

    DMDMi 729167.

    Proteomic databases

    MaxQBi P07357.
    PaxDbi P07357.
    PRIDEi P07357.

    Protocols and materials databases

    DNASUi 731.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361249 ; ENSP00000354458 ; ENSG00000157131 .
    GeneIDi 731.
    KEGGi hsa:731.
    UCSCi uc001cyo.2. human.

    Organism-specific databases

    CTDi 731.
    GeneCardsi GC01P057237.
    HGNCi HGNC:1352. C8A.
    MIMi 120950. gene.
    613790. phenotype.
    neXtProti NX_P07357.
    Orphaneti 169150. Immunodeficiency due to a late component of complements deficiency.
    PharmGKBi PA25951.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG48024.
    HOGENOMi HOG000231146.
    HOVERGENi HBG005368.
    InParanoidi P07357.
    KOi K03997.
    OMAi FMRIFTK.
    OrthoDBi EOG7CRTPG.
    PhylomeDBi P07357.
    TreeFami TF330498.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi C8A. human.
    EvolutionaryTracei P07357.
    GenomeRNAii 731.
    NextBioi 2976.
    PROi P07357.
    SOURCEi Search...

    Gene expression databases

    Bgeei P07357.
    CleanExi HS_C8A.
    Genevestigatori P07357.

    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. 2 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 3 hits.
    SSF82895. SSF82895. 2 hits.
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01209. LDLRA_1. 1 hit.
    PS50068. LDLRA_2. 1 hit.
    PS00279. MACPF_1. 1 hit.
    PS51412. MACPF_2. 1 hit.
    PS50092. TSP1. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complementary DNA and derived amino acid sequence of the alpha subunit of human complement protein C8: evidence for the existence of a separate alpha subunit messenger RNA."
      Rao A.G., Howard O.M.Z., Ng S.C., Whitehead A.S., Colten H.R., Sodetz J.M.
      Biochemistry 26:3556-3564(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    2. Sodetz J.M.
      Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 467-479.
    3. "Genomic organization of human complement protein C8 alpha and further examination of its linkage to C8 beta."
      Michelotti G.A., Snider J.V., Sodetz J.M.
      Hum. Genet. 95:513-518(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Blood.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 LYS-93.
    6. "The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure."
      Steckel E.W., York R.G., Monahan J.B., Sodetz J.M.
      J. Biol. Chem. 255:11997-12005(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT.
    7. "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-44; TRP-542; TRP-545 AND TRP-548.
    8. "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-437.
      Tissue: Plasma.
    9. "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-437.
      Tissue: Liver.
    10. "Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense."
      Hadders M.A., Beringer D.X., Gros P.
      Science 317:1552-1554(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-492, FUNCTION.
    11. "Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit."
      Slade D.J., Lovelace L.L., Chruszcz M., Minor W., Lebioda L., Sodetz J.M.
      J. Mol. Biol. 379:331-342(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 133-492 IN COMPLEX WITH C8G, INTERCHAIN DISULFIDE BOND.
    12. "Crystal structure of complement protein C8gamma in complex with a peptide containing the C8gamma binding site on C8alpha: implications for C8gamma ligand binding."
      Lovelace L.L., Chiswell B., Slade D.J., Sodetz J.M., Lebioda L.
      Mol. Immunol. 45:750-756(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 188-198 IN COMPLEX WITH C8G.
    13. "The eighth component of human complement: molecular basis of C8A (C81) polymorphism."
      Zhang L., Rittner C., Sodetz J.M., Schneider P.M., Kaufmann T.
      Hum. Genet. 96:281-284(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT C8A*B LYS-93.

    Entry informationi

    Entry nameiCO8A_HUMAN
    AccessioniPrimary (citable) accession number: P07357
    Secondary accession number(s): A2RUI4
    , A2RUI5, Q13668, Q9H130
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 160 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 1
      Human chromosome 1: 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