Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Complement C1q subcomponent subunit A  

UniProtKB / Swiss-Prot ID :  C1QA_HUMAN

Gene Name (Synonyms) : 
C1QA  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein Function :  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 Ca(2+)-dependent C1r(2)C1s(2) 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. 

Protein Sequence MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIRTGIQGLKGDQ...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
23E -> K (in dbSNP:rs17887074). VAR_021090
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
335-hydroxylysine.PDGKKGEAG
CCCCCCCCC
68.46UniProtKB
Link-
33O-linked (Gal...).PDGKKGEAG
CCCCCCCCC
68.46UniProtKB
Link-
394-hydroxyproline.EAGRPGRRG
CCCCCCCCC
39.46UniProtKB
Link-
454-hydroxyproline.RRGRPGLKG
CCCCCCCCC
56.12UniProtKB
Link-
485-hydroxylysine.RPGLKGEQG
CCCCCCCCC
67.33UniProtKB
Link-
48O-linked (Gal...).RPGLKGEQG
CCCCCCCCC
67.33UniProtKB
Link-
544-hydroxyproline.EQGEPGAPG
CCCCCCCCC
51.58UniProtKB
Link-
574-hydroxyproline.EPGAPGIRT
CCCCCCCCC
44.66UniProtKB
Link-
675-hydroxylysine.IQGLKGDQG
CCCCCCCCC
68.23UniProtKB
Link-
67O-linked (Gal...).IQGLKGDQG
CCCCCCCCC
68.23UniProtKB
Link-
734-hydroxyproline.DQGEPGPSG
CCCCCCCCC
67.81UniProtKB
Link-
854-hydroxyproline.KVGYPGPSG
CCCCCCCCC
42.14UniProtKB
Link-
974-hydroxyproline.ARGIPGIKG
CCCCCCCCC
41.08UniProtKB
Link-
1005-hydroxylysine.IPGIKGTKG
CCCCCCCCC
67.45UniProtKB
Link-
100O-linked (Gal...).IPGIKGTKG
CCCCCCCCC
67.45UniProtKB
Link-
1035-hydroxylysine.IKGTKGSPG
CCCCCCCCC
67.09UniProtKB
Link-
103O-linked (Gal...).IKGTKGSPG
CCCCCCCCC
67.09UniProtKB
Link-
146N-linked (Glc...)EPYQNHSGR
CCCCCCCCE
26.00HPRD
Link
146N-linked (GlcNAc...).EPYQNHSGR
CCCCCCCCE
26.00UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SAMP_HUMANin vitroHPRD:00393HPRD8417122
CO2A1_HUMANin vitroHPRD:00393HPRD8778019
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Disease Reference
Kegg disease
OMIM disease
613652Complement component C1q deficiency (C1QD)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures