CO9_HUMAN - dbPTM
CO9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CO9_HUMAN
UniProt AC P02748
Protein Name Complement component C9
Gene Name C9
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization Secreted . Target cell membrane
Multi-pass membrane protein . Secreted as soluble monomer. Oligomerizes at target membranes, forming a pre-pore. A conformation change then leads to the formation of a 100 Angstrom diameter pore.
Protein Description 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. [PubMed: 9634479]
Protein Sequence MSACRSFAVAICILEISILTAQYTTSYDPELTESSGSASHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRCTDAVGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLRCNGDNDCGDFSDEDDCESEPRPPCRDRVVEESELARTAGYGINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWNVASLIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAAISLKFTPTETNKAEQCCEETASSISLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFLHVKGEIHLGRFVMRNRDVVLTTTFVDDIKALPTTYEKGEYFAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELKDIKRCLGYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVNITSENLIDDVVSLIRGGTRKYAFELKEKLLRGTVIDVTDFVNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLERAIEDYINEFSVRKCHTCQNGGTVILMDGKCLCACPFKFEGIACEISKQKISEGLPALEFPNEK
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
17PhosphorylationAICILEISILTAQYT
HHHHHHHHHHHHEEC		11.3624505115
20PhosphorylationILEISILTAQYTTSY
HHHHHHHHHEECCCC		15.2824505115
24PhosphorylationSILTAQYTTSYDPEL
HHHHHEECCCCCCHH		9.3724505115
24O-linked_GlycosylationSILTAQYTTSYDPEL
HHHHHEECCCCCCHH		9.37OGP
25PhosphorylationILTAQYTTSYDPELT
HHHHEECCCCCCHHH		21.9824505115
26PhosphorylationLTAQYTTSYDPELTE
HHHEECCCCCCHHHC		21.5324505115
26O-linked_GlycosylationLTAQYTTSYDPELTE
HHHEECCCCCCHHHC		21.53OGP
32O-linked_GlycosylationTSYDPELTESSGSAS
CCCCCHHHCCCCCCC		31.96OGP
34PhosphorylationYDPELTESSGSASHI
CCCHHHCCCCCCCCC		34.4624505115
48C-linked_GlycosylationIDCRMSPWSEWSQCD
CCCCCCCCHHHHCCC		11.1110551839
48C-linked_GlycosylationIDCRMSPWSEWSQCD
CCCCCCCCHHHHCCC		11.1110551839
51C-linked_GlycosylationRMSPWSEWSQCDPCL
CCCCCHHHHCCCHHH		6.5410551839
51C-linked_GlycosylationRMSPWSEWSQCDPCL
CCCCCHHHHCCCHHH		6.5410551839
66PhosphorylationRQMFRSRSIEVFGQF
HHHHHHHCEEEEEEE		25.09-
225UbiquitinationEEQIEAFKSIIQEKT
HHHHHHHHHHHHHHC		48.0329967540
244PhosphorylationAAISLKFTPTETNKA
EEEEEEECCCCCCHH		27.93-
248PhosphorylationLKFTPTETNKAEQCC
EEECCCCCCHHHHHH		44.49-
258PhosphorylationAEQCCEETASSISLH
HHHHHHHHHCCEEEC		15.0028857561
258O-linked_GlycosylationAEQCCEETASSISLH
HHHHHHHHHCCEEEC		15.00OGP
260PhosphorylationQCCEETASSISLHGK
HHHHHHHCCEEECCC		35.3126657352
261PhosphorylationCCEETASSISLHGKG
HHHHHHCCEEECCCC		17.4626657352
263PhosphorylationEETASSISLHGKGSF
HHHHCCEEECCCCEE		19.0924719451
277N-linked_GlycosylationFRFSYSKNETYQLFL
EEEEECCCCEEEEEE		40.684055801
279PhosphorylationFSYSKNETYQLFLSY
EEECCCCEEEEEEEE		26.4323663014
280PhosphorylationSYSKNETYQLFLSYS
EECCCCEEEEEEEEC		9.3123663014
285PhosphorylationETYQLFLSYSSKKEK
CEEEEEEEECCCCEE		18.6823663014
286PhosphorylationTYQLFLSYSSKKEKM
EEEEEEEECCCCEEE		21.0723663014
287PhosphorylationYQLFLSYSSKKEKMF
EEEEEEECCCCEEEE		32.1023663014
288PhosphorylationQLFLSYSSKKEKMFL
EEEEEECCCCEEEEE		39.2423663014
316PhosphorylationRNRDVVLTTTFVDDI
CCCCEEEEEEEHHHH		16.5123663014
317PhosphorylationNRDVVLTTTFVDDIK
CCCEEEEEEEHHHHH		17.6723663014
318PhosphorylationRDVVLTTTFVDDIKA
CCEEEEEEEHHHHHC		19.2023663014
378UbiquitinationGVELKDIKRCLGYHL
CCCHHHHHHHHCCCC		47.39-
383PhosphorylationDIKRCLGYHLDVSLA
HHHHHHCCCCEEEEE		6.0522461510
392PhosphorylationLDVSLAFSEISVGAE
CEEEEECEECCCCCE		28.5422461510
395PhosphorylationSLAFSEISVGAEFNK
EEECEECCCCCEECH		15.5022461510
415N-linked_GlycosylationRGEGRAVNITSENLI
CCCCCCEECCCCCHH		30.7318638581
415N-linked_GlycosylationRGEGRAVNITSENLI
CCCCCCEECCCCCHH		30.7316263699
435UbiquitinationLIRGGTRKYAFELKE
HHHCCCHHHHHHHHH		40.54-
436PhosphorylationIRGGTRKYAFELKEK
HHCCCHHHHHHHHHH		17.1530622161
483UbiquitinationIYNLVPVKMKNAHLK
CHHCCCCCCCCHHHH		37.78-
485UbiquitinationNLVPVKMKNAHLKKQ
HCCCCCCCCHHHHHH		45.31-
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 CO9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CO9_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 CO9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD59_HUMANCD59physical
1377690
APOE_HUMANAPOEphysical
28514442
CYTM_HUMANCST6physical
28514442
Drug and Disease Associations
Kegg Disease
H00103 Late complement pathway defects, including the following seven diseases: C5 deficiency; C6 deficienc
OMIM Disease
613825Complement component 9 deficiency (C9D)
615591Macular degeneration, age-related, 15 (ARMD15)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CO9_HUMAN

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Related Literatures of Post-Translational Modification
C-linked Glycosylation
ReferencePubMed
"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-48 AND TRP-51.
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-277 AND ASN-415, AND MASSSPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415, 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-277 AND ASN-415, AND MASSSPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415, AND MASSSPECTROMETRY.
"The architecture of complement component C9 and poly(C9).";
DiScipio R.G., Hugli T.E.;
J. Biol. Chem. 260:14802-14809(1985).
Cited for: PARTIAL PROTEIN SEQUENCE, ELECTRON MICROSCOPY, AND GLYCOSYLATION ATASN-277 AND ASN-415.
Phosphorylation
ReferencePubMed
"An initial characterization of the serum phosphoproteome.";
Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III;
J. Proteome Res. 8:5523-5531(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, TISSUE SPECIFICITY,AND MASS SPECTROMETRY.

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