CO2_HUMAN - dbPTM
CO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CO2_HUMAN
UniProt AC P06681
Protein Name Complement C2
Gene Name C2
Organism Homo sapiens (Human).
Sequence Length 752
Subcellular Localization Secreted.
Protein Description 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 C4b to generate the C3 or C5 convertase..
Protein Sequence MGPLMVLFCLLFLYPGLADSAPSCPQNVNISGGTFTLSHGWAPGSLLTYSCPQGLYPSPASRLCKSSGQWQTPGATRSLSKAVCKPVRCPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGETAVCDNGAGHCPNPGISLGAVRTGFRFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGTEPICRQPYSYDFPEDVAPALGTSFSHMLGATNPTQKTKESLGRKIQIQRSGHLNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTNTYAALNSVYLMMNNQMRLLGMETMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQKRNDYLDIYAIGVGKLDVDWRELNELGSKKDGERHAFILQDTKALHQVFEHMLDVSKLTDTICGVGNMSANASDQERTPWHVTIKPKSQETCRGALISDQWVLTAAHCFRDGNDHSLWRVNVGDPKSQWGKEFLIEKAVISPGFDVFAKKNQGILEFYGDDIALLKLAQKVKMSTHARPICLPCTMEANLALRRPQGSTCRDHENELLNKQSVPAHFVALNGSKLNINLKMGVEWTSCAEVVSQEKTMFPNLTDVREVVTDQFLCSGTQEDESPCKGESGGAVFLERRFRFFQVGLVSWGLYNPCLGSADKNSRKRAPRSKVPPPRDFHINLFRMQPWLRQHLGDVLNFLPL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
21 (in isoform 2)Phosphorylation-10.6924719451
29N-linked_GlycosylationPSCPQNVNISGGTFT
CCCCCCEEECCCEEE		30.20UniProtKB CARBOHYD
72O-linked_GlycosylationKSSGQWQTPGATRSL
CCCCCCCCCCCCCCC		22.26OGP
111 (in isoform 2)Phosphorylation-31.44-
112N-linked_GlycosylationGSYPVGGNVSFECED
CCCCCCCCEEEEECC		21.9616335952
126PhosphorylationDGFILRGSPVRQCRP
CCEEECCCCCCCCCC		17.4926329039
178PhosphorylationDKVRYRCSSNLVLTG
CCEEEEECCCEEEEC		17.17-
179PhosphorylationKVRYRCSSNLVLTGS
CEEEEECCCEEEECC		37.50-
186PhosphorylationSNLVLTGSSERECQG
CCEEEECCCCEECCC		24.64-
208PhosphorylationEPICRQPYSYDFPED
CCCCCCCCCCCCCCC		16.1224275569
222PhosphorylationDVAPALGTSFSHMLG
CHHHHHCCHHHHHHC		27.7024275569
225PhosphorylationPALGTSFSHMLGATN
HHHCCHHHHHHCCCC		14.0424275569
231PhosphorylationFSHMLGATNPTQKTK
HHHHHCCCCCCHHHH		39.6724275569
290N-linked_GlycosylationRIFSFEINVSVAIIT
EEEECEEEEEEEEEE		16.89UniProtKB CARBOHYD
313 (in isoform 2)Phosphorylation-32.3024719451
317PhosphorylationNDNSRDMTEVISSLE
CCCCCCHHHHHHHHH		31.2425072903
321PhosphorylationRDMTEVISSLENANY
CCHHHHHHHHHHCCC		33.7625072903
322PhosphorylationDMTEVISSLENANYK
CHHHHHHHHHHCCCC		28.6925072903
328PhosphorylationSSLENANYKDHENGT
HHHHHCCCCCCCCCC		18.5125072903
333N-linked_GlycosylationANYKDHENGTGTNTY
CCCCCCCCCCCCCHH		50.3217027507
361PhosphorylationMRLLGMETMAWQEIR
HHHHCCHHHHHHHHH		11.8724719451
442PhosphorylationHAFILQDTKALHQVF
EEEEECCHHHHHHHH		12.7823403867
456PhosphorylationFEHMLDVSKLTDTIC
HHHHHCHHHHHHCCC		22.9326714015
467N-linked_GlycosylationDTICGVGNMSANASD
HCCCCCCCCCCCCCC		20.8716335952
471N-linked_GlycosylationGVGNMSANASDQERT
CCCCCCCCCCCCCCC		32.4416335952
516PhosphorylationFRDGNDHSLWRVNVG
EECCCCCEEEEEECC		32.2724719451
527PhosphorylationVNVGDPKSQWGKEFL
EECCCCHHHCCHHHH		36.2324719451
612PhosphorylationNELLNKQSVPAHFVA
HHHHCCCCCCEEEEE		31.51-
621N-linked_GlycosylationPAHFVALNGSKLNIN
CEEEEEECCCEEEEE		42.8517623646
621N-linked_GlycosylationPAHFVALNGSKLNIN
CEEEEEECCCEEEEE		42.8516335952
651N-linked_GlycosylationQEKTMFPNLTDVREV
CCCCCCCCCCCHHHH		44.2916335952
651N-linked_GlycosylationQEKTMFPNLTDVREV
CCCCCCCCCCCHHHH		44.2918638581
660PhosphorylationTDVREVVTDQFLCSG
CCHHHHHHHHHCCCC		29.29-
666PhosphorylationVTDQFLCSGTQEDES
HHHHHCCCCCCCCCC		47.20-
668PhosphorylationDQFLCSGTQEDESPC
HHHCCCCCCCCCCCC		16.70-
673PhosphorylationSGTQEDESPCKGESG
CCCCCCCCCCCCCCC		48.17-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CO2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CO2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CO2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAF_HUMANCD55physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
217000Complement component 2 deficiency (C2D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CO2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.
"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.

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