Protein knowledgebaseSequence archiveHelp pages, FAQs, UniProtKB manual, documents, news archive and Biocuration projects.Sequence clustersProtein sets from fully sequenced genomesAnnotation systemsSystems used to automatically annotate proteins with high accuracy:Supporting dataSelect one of the options below to target your search:You are using a version of browser that may not display all the features of this website. Please consider upgrading . Complement C1q subcomponent subunit CC1QCHomo sapiens (Human)-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveliFunctioniC1q 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 - Molecular functioniGO - Biological processiNon-traceable author statementiInferred from direct assayiInferred from direct assayiKeywordsiBiological process, , Enzyme and pathway databasesReactomei Initial triggering of complement.
Classical antibody-mediated complement activation.
Regulation of Complement cascade. Names & TaxonomyiProtein namesiRecommended name:Complement C1q subcomponent subunit CGene namesiName:Synonyms:C1QGOrganismiTaxonomic identifieri
[]Taxonomic lineagei >
Proteomesi Componenti: Chromosome 1 Organism-specific databasesEuPathDBi HGNCi C1QC. Subcellular locationi
Extracellular region or secreted
Plasma membrane
Cytoskeleton
Peroxisome
Golgi apparatus
Mitochondrion
Manual annotation
Automatic computational assertionGraphics by Christian S Source: Keywords - Cellular componentiPathology & BiotechiInvolvement in diseaseiThe disease is caused by mutations affecting the gene represented in this entry.Disease descriptionA 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.Feature keyPosition(s)DescriptionActionsGraphical viewLengthNatural variantiVAR_008542 in C1QD. Manual assertion based on experiment ini"Homozygous hereditary C1q deficiency and systemic lupus erythematosus. A new family and the molecular basis of C1q deficiency in three families.", , , , , ,
[] [] []Cited for: VARIANT C1QD ARG-34.Corresponds to variant .1Keywords - DiseaseiOrganism-specific databasesDisGeNETi MalaCardsi MIMi phenotype. OpenTargetsi Orphaneti Immunodeficiency due to an early component of complement deficiency. PharmGKBi Chemistry databasesDrugBanki Abciximab.
Adalimumab.
Alefacept.
Alemtuzumab.
Basiliximab.
Bevacizumab.
Cetuximab.
Daclizumab.
Efalizumab.
Etanercept.
Gemtuzumab ozogamicin.
Ibritumomab tiuxetan.
Muromonab.
Natalizumab.
Palivizumab.
Rituximab.
Tositumomab.
Trastuzumab. Polymorphism and mutation databasesBioMutai DMDMi PTM / ProcessingiMolecule processingFeature keyPosition(s)DescriptionActionsGraphical viewLengthSignal peptideiManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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. 28ChainiPRO_Complement C1q subcomponent subunit C 217Amino acid modificationsFeature keyPosition(s)DescriptionActionsGraphical viewLengthDisulfide bondiInterchainModified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Modified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Modified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Modified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Modified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Modified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Modified residuei5-hydroxylysineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1GlycosylationiO-linked (Gal...) hydroxylysine1Modified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Modified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Modified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Modified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Modified residuei4-hydroxyprolineManual assertion based on experiment ini"Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
[] [] []Cited for: PROTEIN SEQUENCE OF , 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-105.1Post-translational modificationiO-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.Keywords - PTMi, , Proteomic databasesPaxDbi PeptideAtlasi PRIDEi PTM databasesPhosphoSitePlusi Miscellaneous databasesPMAP-CutDBi ExpressioniGene expression databasesBgeei CleanExi ExpressionAtlasi baseline and differential. Genevisiblei HS. Organism-specific databasesHPAi
InteractioniSubunit structureiC1 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 databasesBioGridi 2 interactors.CORUMi IntActi 6 interactors.MINTi STRINGi StructureiSecondary structure1245Legend: HelixTurnBeta strandPDB Structure known for this areaFeature keyPosition(s)DescriptionActionsGraphical viewLengthHelixiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei5Beta strandiManual assertion inferred from combination of experimental and computational evidencei4TurniManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei13Beta strandiManual assertion inferred from combination of experimental and computational evidencei7Beta strandiManual assertion inferred from combination of experimental and computational evidencei8Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei11Beta strandiManual assertion inferred from combination of experimental and computational evidencei10Beta strandiManual assertion inferred from combination of experimental and computational evidencei93D structure databasesSelect the link destinations:PDBeiRCSB PDBiPDBjiPDB entryMethodResolution (?)ChainPositionsPDBsumX-ray1.85C[]X-ray2.05C/F[]X-ray1.90C/F[]X-ray2.30C/F[]X-ray1.25C/F[]X-ray1.35A[]X-ray1.55A[]ProteinModelPortali SMRi ModBaseiMobiDBiMiscellaneous databasesEvolutionaryTracei Family & DomainsiDomains and RepeatsFeature keyPosition(s)DescriptionActionsGraphical viewLengthDomainiCollagen-like 82DomainiC1qManual assertion according to rulesi 131Keywords - Domaini, , Phylogenomic databaseseggNOGi Eukaryota.
LUCA. GeneTreei HOGENOMi HOVERGENi InParanoidi KOi OMAi OrthoDBi PhylomeDBi TreeFami Family and domain databasesGene3Di 1 hit. InterProi C1q_dom.
Tumour_necrosis_fac-like_dom. Pfami C1q. 1 hit.
Collagen. 1 hit. PRINTSi COMPLEMNTC1Q. SMARTi C1Q. 1 hit. SUPFAMi SSF49842. 1 hit. PROSITEi C1Q. 1 hit. SequenceiSequence statusi: Complete.Sequence processingi: The displayed sequence is further processed into a mature form.P02747-1 []
50MDVGPSSLPH LGLKLLLLLL LLPLRGQANT GCYGIPGMPG LPGAPGKDGY
100DGLPGPKGEP GIPAIPGIRG PKGQKGEPGL PGHPGKNGPM GPPGMPGVPG
150PMGIPGEPGE EGRYKQKFQS VFTVTRQTHQ PPAPNSLIRF NAVLTNPQGD
200YDTSTGKFTC KVPGLYYFVY HASHTANLCV LLYRSGVKVV TFCGHTSKTN
240 QVNSGGVLLR LQVGEEVWLA VNDYYDMVGI QGSDSVFSGF LLFPD 24525,774April 16, 2002 - v3Checksum:iFA17117EB7ABFC12BLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutterExperimental InfoFeature keyPosition(s)DescriptionActionsGraphical viewLengthSequence conflictiK → R in
(PubMed:).1Sequence conflictiP → A no nucleotide entry
(PubMed:).1Sequence conflictiGQ → AK in
() 2Sequence conflictiK → P AA sequence
(PubMed:).1Sequence conflictiP → K AA sequence
(PubMed:).1Sequence conflictiK → P AA sequence
(PubMed:).1Sequence conflictiP → K AA sequence
(PubMed:).1Sequence conflictiN → D AA sequence
(PubMed:).1Sequence conflictiM → N AA sequence
(PubMed:).1Sequence conflictiI → F in
() 1Sequence conflictiG → E in
() 1Sequence conflictiE → G in
(PubMed:).1Natural variantFeature keyPosition(s)DescriptionActionsGraphical viewLengthNatural variantiVAR_008542 in C1QD. Manual assertion based on experiment ini"Homozygous hereditary C1q deficiency and systemic lupus erythematosus. A new family and the molecular basis of C1q deficiency in three families.", , , , , ,
[] [] []Cited for: VARIANT C1QD ARG-34.Corresponds to variant .1Sequence databasesSelect the link destinations:EMBLiGenBankiDDBJi mRNA. Translation: . mRNA. Translation: . Genomic DNA. No translation available. mRNA. Translation: .CCDSi PIRi C1HUQC. RefSeqi
UniGenei Genome annotation databasesEnsembli; ; . ; ; . ; ; . GeneIDi KEGGi UCSCi human. Similar proteinsi mRNA. Translation: . mRNA. Translation: . Genomic DNA. No translation available. mRNA. Translation: .CCDSi PIRi C1HUQC. RefSeqi
UniGenei 3D structure databasesSelect the link destinations:PDBeiRCSB PDBiPDBjiPDB entryMethodResolution (?)ChainPositionsPDBsumX-ray1.85C[]X-ray2.05C/F[]X-ray1.90C/F[]X-ray2.30C/F[]X-ray1.25C/F[]X-ray1.35A[]X-ray1.55A[]ProteinModelPortali SMRi ModBaseiMobiDBiProtein-protein interaction databasesBioGridi 2 interactors.CORUMi IntActi 6 interactors.MINTi STRINGi Chemistry databasesDrugBanki Abciximab.
Adalimumab.
Alefacept.
Alemtuzumab.
Basiliximab.
Bevacizumab.
Cetuximab.
Daclizumab.
Efalizumab.
Etanercept.
Gemtuzumab ozogamicin.
Ibritumomab tiuxetan.
Muromonab.
Natalizumab.
Palivizumab.
Rituximab.
Tositumomab.
Trastuzumab. PTM databasesPhosphoSitePlusi Polymorphism and mutation databasesBioMutai DMDMi Proteomic databasesPaxDbi PeptideAtlasi PRIDEi Protocols and materials databasesDNASUi Structural Biology KnowledgebaseGenome annotation databasesEnsembli; ; . ; ; . ; ; . GeneIDi KEGGi UCSCi human. Organism-specific databasesCTDi DisGeNETi EuPathDBi GeneCardsi HGNCi C1QC. HPAi
MalaCardsi MIMi gene.
phenotype. neXtProti OpenTargetsi Orphaneti Immunodeficiency due to an early component of complement deficiency. PharmGKBi GenAtlasiPhylogenomic databaseseggNOGi Eukaryota.
LUCA. GeneTreei HOGENOMi HOVERGENi InParanoidi KOi OMAi OrthoDBi PhylomeDBi TreeFami Enzyme and pathway databasesReactomei Initial triggering of complement.
Classical antibody-mediated complement activation.
Regulation of Complement cascade. Miscellaneous databasesChiTaRSi human. EvolutionaryTracei GenomeRNAii PMAP-CutDBi PROi SOURCEiGene expression databasesBgeei CleanExi ExpressionAtlasi baseline and differential. Genevisiblei HS. Family and domain databasesGene3Di 1 hit. InterProi C1q_dom.
Tumour_necrosis_fac-like_dom. Pfami C1q. 1 hit.
Collagen. 1 hit. PRINTSi COMPLEMNTC1Q. SMARTi C1Q. 1 hit. SUPFAMi SSF49842. 1 hit. PROSITEi C1Q. 1 hit. ProtoNetiMiscellaneousiKeywords - Technical termi, , , Documents
Human chromosome 1: entries, gene names and cross-references to MIM
List of human entries with polymorphisms or disease mutations
Index of human polymorphisms and disease mutations
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Index of Protein Data Bank (PDB) cross-references索尼EA47EC/P（粉）
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