Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Complement component C6  

UniProtKB / Swiss-Prot ID :  CO6_HUMAN

Gene Name (Synonyms) : 
C6  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein Function :  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. 

Protein Sequence MARRSVLYFILLNALINKGQACFCDHYAWTQWTSCSKTCNSGTQSRHRQIVVDKYYQENFCEQICSKQET...
Predicted Secondary Structure CCCEEEEEEEEEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCEEEEEEEEECCCCCCCCCCCCCCCCCCE...
Protein Variant
LocationDescription
119A -> E (in allotype C6 A;dbSNP:rs1801033).
397K -> E (in dbSNP:rs6896011). VAR_027647
470S -> F (in dbSNP:rs10462014). VAR_027648
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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
29C-linked (Man)DHYAWTQWT
CCCCCCCCC
5.07HPRD
Link
29C-linked (Man)DHYAWTQWT
CCCCCCCCC
5.07OGlycBase
Link
29C-linked (Man).DHYAWTQWT
CCCCCCCCC
5.07UniProtKB
Link
32C-linked (Man)AWTQWTSCS
CCCCCCCCC
5.27HPRD
Link
32C-linked (Man)AWTQWTSCS
CCCCCCCCC
5.27OGlycBase
Link
32C-linked (Man); partial.AWTQWTSCS
CCCCCCCCC
5.27UniProtKB
Link
41PhosphoserineKTCNSGTQS
CCCCCCEEE
45.42HPRD
Link
45PhosphoserineSGTQSRHRQ
CCEEEEEEE
29.86HPRD
Link
90C-linked (Man)DFGPWSDCD
CCCCCCCCC
13.74HPRD
Link
90C-linked (Man)DFGPWSDCD
CCCCCCCCC
13.74OGlycBase
Link
90C-linked (Man); partial.DFGPWSDCD
CCCCCCCCC
13.74UniProtKB
Link
162N-linked (Glc...)CNGENDCGD
CCCHHHCCC
51.80HPRD
Link
278PhosphoserineQGGSSFSVP
EEEECCCCC
25.47HPRD
Link-
278Phosphoserine.QGGSSFSVP
EEEECCCCC
25.47UniProtKB
Link-
324N-linked (Glc...)MKVLNFTTK
EEEEEEEEC
34.89HPRD
Link
324N-linked (GlcNAc...).MKVLNFTTK
EEEEEEEEC
34.89UniProtKB
Link
568C-linked (Man)VDGQWGCWS
CCCCEECCC
14.94HPRD
Link
568C-linked (Man)VDGQWGCWS
CCCCEECCC
14.94OGlycBase
Link
568C-linked (Man); partial.VDGQWGCWS
CCCCEECCC
14.94UniProtKB
Link
571C-linked (Man)QWGCWSSWS
CEECCCCCC
7.46HPRD
Link
571C-linked (Man)QWGCWSSWS
CEECCCCCC
7.46OGlycBase
Link
571C-linked (Man); partial.QWGCWSSWS
CEECCCCCC
7.46UniProtKB
Link
574C-linked (Man)CWSSWSTCD
CCCCCCCCC
7.67HPRD
Link
574C-linked (Man)CWSSWSTCD
CCCCCCCCC
7.67OGlycBase
Link
574C-linked (Man); partial.CWSSWSTCD
CCCCCCCCC
7.67UniProtKB
Link
773S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)LKGHCQLGQ
CCCCCCCCC
4.94HPRD
Link
784S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)SGSECICMS
CCCEEEEEC
2.88HPRD
Link
786S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)SECICMSPE
CEEEEECCC
3.14HPRD
Link
793S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)PEEDCSHHS
CCCCCCCCC
4.76HPRD
Link
801S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)SEDLCVFDT
CCEEECCCC
4.42HPRD
Link
816S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)TSPACKFLA
CCCCCCCCC
3.48HPRD
Link
823S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)LAEKCLNNQ
CCCCCCCCC
3.56HPRD
Link
837S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)HIGSCQDGR
EEEECCCCC
3.45HPRD
Link
855N-linked (Glc...)RLSSNSTKK
ECCCCCEEC
50.77HPRD
Link
855N-linked (GlcNAc...).RLSSNSTKK
ECCCCCEEC
50.77UniProtKB
Link
862S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)KKESCGYDT
ECCCCCCCC
6.50HPRD
Link
867S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GYDTCYDWE
CCCCCCCCC
2.37HPRD
Link
873S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)DWEKCSAST
CCCCCCCCC
2.52HPRD
Link
880S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)STSKCVCLL
CCCEEEEEC
2.34HPRD
Link
882S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)SKCVCLLPP
CEEEEECCC
4.53HPRD
Link
888S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)LPPQCFKGG
CCCCCCCCC
4.73HPRD
Link
897S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)NQLYCVKMG
CEEEEEEEC
3.01HPRD
Link
912S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)TLNICEVGT
EEEEEEEEE
3.18HPRD
Link
919S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)GTIRCANRK
EEHEECCCE
3.30HPRD
Link
932S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)HPGKCLA
CCCCCCC
4.88HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CO5_HUMANin vitroHPRD:01956HPRD1387399
2808363
THRB_HUMANin vitroHPRD:01956HPRD3192535
NCOAT_HUMANyeast 2-hybridHPRD:01956HPRD16169070
CO5_HUMANENSP00000263413STRING
CO5_HUMANENSP00000263413STRING
CO5_HUMANENSP00000263413STRING
CO8G_HUMANENSP00000263413STRING
CO9_HUMANENSP00000263413STRING
CO7_HUMANENSP00000263413STRING
CO8A_HUMANENSP00000263413STRING
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Disease Reference
Kegg disease
OMIM disease
612446Complement component 6 deficiency (C6D)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
C-linked Glycosylation
ReferencePubMed
"Structure of complement C6 suggests a mechanism for initiation andunidirectional, sequential assembly of membrane attack complex(MAC).";
Aleshin A.E., Schraufstatter I.U., Stec B., Bankston L.A.,Liddington R.C., DiScipio R.G.;
J. Biol. Chem. 287:10210-10222(2012).
Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 22-934, GLYCOSYLATION ATTRP-29; TRP-32; THR-38; ASN-324; THR-392; TRP-568 AND TRP-571,SUBUNIT, AND DISULFIDE BONDS.
"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).
Cited for: GLYCOSYLATION AT TRP-29; TRP-32; TRP-90; TRP-568; TRP-571 AND TRP-574.
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-324 AND ASN-855, AND MASSSPECTROMETRY.
"Structure of complement C6 suggests a mechanism for initiation andunidirectional, sequential assembly of membrane attack complex(MAC).";
Aleshin A.E., Schraufstatter I.U., Stec B., Bankston L.A.,Liddington R.C., DiScipio R.G.;
J. Biol. Chem. 287:10210-10222(2012).
Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 22-934, GLYCOSYLATION ATTRP-29; TRP-32; THR-38; ASN-324; THR-392; TRP-568 AND TRP-571,SUBUNIT, AND DISULFIDE BONDS.
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures