Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Complement C2  

UniProtKB / Swiss-Prot ID :  CO2_HUMAN

Gene Name (Synonyms) : 
C2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein Function :  Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor 4b to generate the C3 or C5 convertase. 

Protein Sequence MGPLMVLFCLLFLYPGLADSAPSCPQNVNISGGTFTLSHGWAPGSLLTYSCPQGLYPSPASRLCKSSGQW...
Predicted Secondary Structure CCHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCEEEECCCCCCCCEEEEEECCCCEECCCEEEECCCCEE...
Protein Variant
LocationDescription
131C -> Y (in C2D). VAR_008544
209S -> F (in C2D; dbSNP:rs28934590). VAR_008545
318E -> D (in dbSNP:rs9332739). VAR_019158
464G -> R (in C2D). VAR_008546
533F -> L (in dbSNP:rs1042664). VAR_011772
734R -> C (in dbSNP:rs4151648). VAR_019159
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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
112N-linked (GlcNAc...).PVGGNVSFE
EECCEEEEE
21.96UniProtKB
Link-
333N-linked (GlcNAc...).KDHENGTGT
HHCCCCCCC
50.32UniProtKB
Link
467N-linked (GlcNAc...).CGVGNMSAN
CCCCCCEEE
20.87UniProtKB
Link
471N-linked (GlcNAc...).NMSANASDQ
CCEEEECCC
32.44UniProtKB
Link
621N-linked (Glc...)FVALNGSKL
EEECCCCEE
42.85HPRD
Link
621N-linked (GlcNAc...).FVALNGSKL
EEECCCCEE
42.85UniProtKB
Link
651N-linked (Glc...)TMFPNLTDV
HCCCCCCCC
44.29HPRD
Link
651N-linked (GlcNAc...)TMFPNLTDV
HCCCCCCCC
44.29SysPTM
Link
651N-linked (GlcNAc...).TMFPNLTDV
HCCCCCCCC
44.29UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CO3_HUMANin vitroHPRD:08939HPRD3546307
CO5_HUMANin vitroHPRD:08939HPRD12878586
8175701
MASP1_HUMANin vitroHPRD:08939HPRD10946292
CO5_HUMANENSP00000299367STRING
CO5_HUMANENSP00000299367STRING
CO5_HUMANENSP00000299367STRING
MASP2_HUMANENSP00000299367STRING
CO3_HUMANENSP00000299367STRING
CY1_HUMANENSP00000299367STRING
C1S_HUMANENSP00000299367STRING
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Disease Reference
Kegg disease
OMIM disease
217000Complement component 2 deficiency (C2D)
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-112; ASN-333; ASN-467;ASN-471; ASN-621 AND ASN-651, AND MASS SPECTROMETRY.
"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-112 AND ASN-333, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures