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P02747

- C1QC_HUMAN

UniProt

P02747 - C1QC_HUMAN

Protein

Complement C1q subcomponent subunit C

Gene

C1QC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (16 Apr 2002)
      Previous versions | rss
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    Functioni

    C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca2+-dependent C1r2C1s2 proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.

    GO - Biological processi

    1. complement activation Source: Reactome
    2. complement activation, classical pathway Source: Reactome
    3. immune response Source: UniProtKB
    4. innate immune response Source: Reactome
    5. negative regulation of granulocyte differentiation Source: BHF-UCL
    6. negative regulation of macrophage differentiation Source: BHF-UCL

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement C1q subcomponent subunit C
    Gene namesi
    Name:C1QC
    Synonyms:C1QG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1245. C1QC.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. collagen trimer Source: UniProtKB-KW
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Complement component C1q deficiency (C1QD) [MIM:613652]: A disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti34 – 341G → R in C1QD. 1 Publication
    VAR_008542

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi613652. phenotype.
    Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBiPA25626.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28281 PublicationAdd
    BLAST
    Chaini29 – 245217Complement C1q subcomponent subunit CPRO_0000003524Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 – 32Interchain
    Modified residuei36 – 3614-hydroxyproline1 Publication
    Modified residuei39 – 3914-hydroxyproline1 Publication
    Modified residuei42 – 4214-hydroxyproline1 Publication
    Modified residuei45 – 4514-hydroxyproline1 Publication
    Modified residuei54 – 5414-hydroxyproline1 Publication
    Modified residuei63 – 6314-hydroxyproline1 Publication
    Modified residuei75 – 7515-hydroxylysine1 Publication
    Glycosylationi75 – 751O-linked (Gal...)
    Modified residuei81 – 8114-hydroxyproline1 Publication
    Modified residuei93 – 9314-hydroxyproline1 Publication
    Modified residuei96 – 9614-hydroxyproline1 Publication
    Modified residuei99 – 9914-hydroxyproline1 Publication
    Modified residuei105 – 10514-hydroxyproline1 Publication

    Post-translational modificationi

    O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiP02747.
    PeptideAtlasiP02747.
    PRIDEiP02747.

    Miscellaneous databases

    PMAP-CutDBP02747.

    Expressioni

    Gene expression databases

    BgeeiP02747.
    CleanExiHS_C1QC.
    GenevestigatoriP02747.

    Organism-specific databases

    HPAiCAB009828.
    HPA001471.

    Interactioni

    Subunit structurei

    C1 is a calcium-dependent trimolecular complex of C1q, R and S in the molar ration of 1:2:2. C1q subcomponent is composed of nine subunits, six of which are disulfide-linked dimers of the A and B chains, and three of which are disulfide-linked dimers of the C chain.

    Protein-protein interaction databases

    BioGridi107175. 2 interactions.
    IntActiP02747. 2 interactions.
    MINTiMINT-6630018.
    STRINGi9606.ENSP00000363768.

    Structurei

    Secondary structure

    1
    245
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi116 – 1183
    Beta strandi121 – 1255
    Beta strandi142 – 1454
    Turni153 – 1553
    Beta strandi157 – 1593
    Beta strandi164 – 17613
    Beta strandi178 – 1847
    Beta strandi187 – 1948
    Beta strandi197 – 1993
    Beta strandi201 – 21111
    Beta strandi216 – 22510
    Beta strandi236 – 2449

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PK6X-ray1.85C117-245[»]
    2JG8X-ray2.05C/F115-245[»]
    2JG9X-ray1.90C/F115-245[»]
    2WNUX-ray2.30C/F115-245[»]
    2WNVX-ray1.25C/F115-245[»]
    ProteinModelPortaliP02747.
    SMRiP02747. Positions 34-113, 117-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02747.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 11282Collagen-likeAdd
    BLAST
    Domaini115 – 245131C1qPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C1q domain.PROSITE-ProRule annotation
    Contains 1 collagen-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG115796.
    HOGENOMiHOG000085653.
    HOVERGENiHBG108220.
    InParanoidiP02747.
    KOiK03988.
    OMAiQTANLCV.
    OrthoDBiEOG70ZZPW.
    PhylomeDBiP02747.
    TreeFamiTF329591.

    Family and domain databases

    Gene3Di2.60.120.40. 1 hit.
    InterProiIPR001073. C1q.
    IPR008160. Collagen.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view]
    PfamiPF00386. C1q. 1 hit.
    PF01391. Collagen. 2 hits.
    [Graphical view]
    PRINTSiPR00007. COMPLEMNTC1Q.
    SMARTiSM00110. C1Q. 1 hit.
    [Graphical view]
    SUPFAMiSSF49842. SSF49842. 1 hit.
    PROSITEiPS50871. C1Q. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P02747-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDVGPSSLPH LGLKLLLLLL LLPLRGQANT GCYGIPGMPG LPGAPGKDGY    50
    DGLPGPKGEP GIPAIPGIRG PKGQKGEPGL PGHPGKNGPM GPPGMPGVPG 100
    PMGIPGEPGE EGRYKQKFQS VFTVTRQTHQ PPAPNSLIRF NAVLTNPQGD 150
    YDTSTGKFTC KVPGLYYFVY HASHTANLCV LLYRSGVKVV TFCGHTSKTN 200
    QVNSGGVLLR LQVGEEVWLA VNDYYDMVGI QGSDSVFSGF LLFPD 245
    Length:245
    Mass (Da):25,774
    Last modified:April 16, 2002 - v3
    Checksum:iFA17117EB7ABFC12
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141K → R in BAB71575. (PubMed:14702039)Curated
    Sequence conflicti23 – 231P → A no nucleotide entry (PubMed:1706597)Curated
    Sequence conflicti26 – 272GQ → AK in AAP97191. 1 PublicationCurated
    Sequence conflicti57 – 571K → P AA sequence (PubMed:486087)Curated
    Sequence conflicti66 – 661P → K AA sequence (PubMed:486087)Curated
    Sequence conflicti72 – 721K → P AA sequence (PubMed:486087)Curated
    Sequence conflicti84 – 841P → K AA sequence (PubMed:486087)Curated
    Sequence conflicti87 – 871N → D AA sequence (PubMed:486087)Curated
    Sequence conflicti90 – 901M → N AA sequence (PubMed:486087)Curated
    Sequence conflicti104 – 1041I → F in AAP97191. 1 PublicationCurated
    Sequence conflicti149 – 1491G → E in AAP97191. 1 PublicationCurated
    Sequence conflicti215 – 2151E → G in BAB71575. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti34 – 341G → R in C1QD. 1 Publication
    VAR_008542

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087892 mRNA. Translation: AAP97191.1.
    AK057792 mRNA. Translation: BAB71575.1.
    AL158086 Genomic DNA. Translation: CAI22894.1.
    BC009016 mRNA. Translation: AAH09016.1.
    CCDSiCCDS227.1.
    PIRiS14351. C1HUQC.
    RefSeqiNP_001107573.1. NM_001114101.1.
    NP_758957.2. NM_172369.3.
    UniGeneiHs.467753.

    Genome annotation databases

    EnsembliENST00000374637; ENSP00000363768; ENSG00000159189.
    ENST00000374639; ENSP00000363770; ENSG00000159189.
    ENST00000374640; ENSP00000363771; ENSG00000159189.
    GeneIDi714.
    KEGGihsa:714.
    UCSCiuc001bga.4. human.

    Polymorphism databases

    DMDMi20178281.

    Cross-referencesi

    Web resourcesi

    C1QGbase

    C1QC mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087892 mRNA. Translation: AAP97191.1 .
    AK057792 mRNA. Translation: BAB71575.1 .
    AL158086 Genomic DNA. Translation: CAI22894.1 .
    BC009016 mRNA. Translation: AAH09016.1 .
    CCDSi CCDS227.1.
    PIRi S14351. C1HUQC.
    RefSeqi NP_001107573.1. NM_001114101.1.
    NP_758957.2. NM_172369.3.
    UniGenei Hs.467753.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PK6 X-ray 1.85 C 117-245 [» ]
    2JG8 X-ray 2.05 C/F 115-245 [» ]
    2JG9 X-ray 1.90 C/F 115-245 [» ]
    2WNU X-ray 2.30 C/F 115-245 [» ]
    2WNV X-ray 1.25 C/F 115-245 [» ]
    ProteinModelPortali P02747.
    SMRi P02747. Positions 34-113, 117-245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107175. 2 interactions.
    IntActi P02747. 2 interactions.
    MINTi MINT-6630018.
    STRINGi 9606.ENSP00000363768.

    Chemistry

    DrugBanki DB00054. Abciximab.
    DB00051. Adalimumab.
    DB00092. Alefacept.
    DB00087. Alemtuzumab.
    DB00074. Basiliximab.
    DB00112. Bevacizumab.
    DB00002. Cetuximab.
    DB00111. Daclizumab.
    DB00095. Efalizumab.
    DB00005. Etanercept.
    DB00056. Gemtuzumab ozogamicin.
    DB00078. Ibritumomab.
    DB00075. Muromonab.
    DB00108. Natalizumab.
    DB00110. Palivizumab.
    DB00073. Rituximab.
    DB00081. Tositumomab.
    DB00072. Trastuzumab.

    Polymorphism databases

    DMDMi 20178281.

    Proteomic databases

    PaxDbi P02747.
    PeptideAtlasi P02747.
    PRIDEi P02747.

    Protocols and materials databases

    DNASUi 714.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374637 ; ENSP00000363768 ; ENSG00000159189 .
    ENST00000374639 ; ENSP00000363770 ; ENSG00000159189 .
    ENST00000374640 ; ENSP00000363771 ; ENSG00000159189 .
    GeneIDi 714.
    KEGGi hsa:714.
    UCSCi uc001bga.4. human.

    Organism-specific databases

    CTDi 714.
    GeneCardsi GC01P022970.
    HGNCi HGNC:1245. C1QC.
    HPAi CAB009828.
    HPA001471.
    MIMi 120575. gene.
    613652. phenotype.
    neXtProti NX_P02747.
    Orphaneti 169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBi PA25626.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG115796.
    HOGENOMi HOG000085653.
    HOVERGENi HBG108220.
    InParanoidi P02747.
    KOi K03988.
    OMAi QTANLCV.
    OrthoDBi EOG70ZZPW.
    PhylomeDBi P02747.
    TreeFami TF329591.

    Enzyme and pathway databases

    Reactomei REACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.

    Miscellaneous databases

    ChiTaRSi C1QC. human.
    EvolutionaryTracei P02747.
    GenomeRNAii 714.
    NextBioi 2902.
    PMAP-CutDB P02747.
    PROi P02747.
    SOURCEi Search...

    Gene expression databases

    Bgeei P02747.
    CleanExi HS_C1QC.
    Genevestigatori P02747.

    Family and domain databases

    Gene3Di 2.60.120.40. 1 hit.
    InterProi IPR001073. C1q.
    IPR008160. Collagen.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view ]
    Pfami PF00386. C1q. 1 hit.
    PF01391. Collagen. 2 hits.
    [Graphical view ]
    PRINTSi PR00007. COMPLEMNTC1Q.
    SMARTi SM00110. C1Q. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49842. SSF49842. 1 hit.
    PROSITEi PS50871. C1Q. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q."
      Sellar G.C., Blake D.J., Reid K.B.M.
      Biochem. J. 274:481-490(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Monocyte.
    2. "Cloning and characterization of a novel human cDNA homology to murine C1q C-chain mRNA."
      Dai F.Y., Yu L., Wan Y.Z., Zhang H.L., Huang J., Zhao S.Y.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    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].
      Tissue: Brain.
    6. "Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
      Reid K.B.M.
      Biochem. J. 179:367-371(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-122, HYDROXYLATION AT PRO-36; PRO-39; PRO-42; PRO-45; PRO-54; PRO-63; LYS-75; PRO-81; PRO-93; PRO-96; PRO-99 AND PRO-105.
    7. "The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties."
      Gaboriaud C., Juanhuix J., Gruez A., Lacroix M., Darnault C., Pignol D., Verger D., Fontecilla-Camps J.-C., Arlaud G.J.
      J. Biol. Chem. 278:46974-46982(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 117-245.
    8. "Molecular basis of hereditary C1q deficiency."
      Petry F.
      Immunobiology 199:286-294(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON C1Q DEFICIENCY.
    9. "Homozygous hereditary C1q deficiency and systemic lupus erythematosus. A new family and the molecular basis of C1q deficiency in three families."
      Slingsby J.H., Norsworthy P., Pearce G., Vaishnaw A.K., Issler H., Morley B.J., Walport M.J.
      Arthritis Rheum. 39:663-670(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT C1QD ARG-34.

    Entry informationi

    Entry nameiC1QC_HUMAN
    AccessioniPrimary (citable) accession number: P02747
    Secondary accession number(s): Q7Z502, Q96DL2, Q96H05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 157 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 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