dbPTM

CO6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CO6_HUMAN
UniProt AC	P13671
Protein Name	Complement component C6
Gene Name	C6
Organism	Homo sapiens (Human).
Sequence Length	934
Subcellular Localization	Secreted.
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..
Protein Sequence	MARRSVLYFILLNALINKGQACFCDHYAWTQWTSCSKTCNSGTQSRHRQIVVDKYYQENFCEQICSKQETRECNWQRCPINCLLGDFGPWSDCDPCIEKQSKVRSVLRPSQFGGQPCTAPLVAFQPCIPSKLCKIEEADCKNKFRCDSGRCIARKLECNGENDCGDNSDERDCGRTKAVCTRKYNPIPSVQLMGNGFHFLAGEPRGEVLDNSFTGGICKTVKSSRTSNPYRVPANLENVGFEVQTAEDDLKTDFYKDLTSLGHNENQQGSFSSQGGSSFSVPIFYSSKRSENINHNSAFKQAIQASHKKDSSFIRIHKVMKVLNFTTKAKDLHLSDVFLKALNHLPLEYNSALYSRIFDDFGTHYFTSGSLGGVYDLLYQFSSEELKNSGLTEEEAKHCVRIETKKRVLFAKKTKVEHRCTTNKLSEKHEGSFIQGAEKSISLIRGGRSEYGAALAWEKGSSGLEEKTFSEWLESVKENPAVIDFELAPIVDLVRNIPCAVTKRNNLRKALQEYAAKFDPCQCAPCPNNGRPTLSGTECLCVCQSGTYGENCEKQSPDYKSNAVDGQWGCWSSWSTCDATYKRSRTRECNNPAPQRGGKRCEGEKRQEEDCTFSIMENNGQPCINDDEEMKEVDLPEIEADSGCPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVECQRTECIKPVVQEVLTITPFQRLYRIGESIELTCPKGFVVAGPSRYTCQGNSWTPPISNSLTCEKDTLTKLKGHCQLGQKQSGSECICMSPEEDCSHHSEDLCVFDTDSNDYFTSPACKFLAEKCLNNQQLHFLHIGSCQDGRQLEWGLERTRLSSNSTKKESCGYDTCYDWEKCSASTSKCVCLLPPQCFKGGNQLYCVKMGSSTSEKTLNICEVGTIRCANRKMEILHPGKCLA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	C-linked_Glycosylation	CFCDHYAWTQWTSCS CCCCCCEEECCEECC	5.07	10551839
29	C-linked_Glycosylation	CFCDHYAWTQWTSCS CCCCCCEEECCEECC	5.07	10551839
32	C-linked_Glycosylation	DHYAWTQWTSCSKTC CCCEEECCEECCCCC	5.27	10551839
32	C-linked_Glycosylation	DHYAWTQWTSCSKTC CCCEEECCEECCCCC	5.27	10551839
38	O-linked_Glycosylation	QWTSCSKTCNSGTQS CCEECCCCCCCCCCC	10.71	22267737
41	Phosphorylation	SCSKTCNSGTQSRHR ECCCCCCCCCCCHHE	45.42	18452278
45	Phosphorylation	TCNSGTQSRHRQIVV CCCCCCCCHHEEEEH	29.86	18452278
90	C-linked_Glycosylation	LLGDFGPWSDCDPCI EECCCCCHHHCHHHH	13.74	10551839
90	C-linked_Glycosylation	LLGDFGPWSDCDPCI EECCCCCHHHCHHHH	13.74	10551839
130	Phosphorylation	AFQPCIPSKLCKIEE EECCCCCHHHCCCCC	20.53	24719451
162	N-linked_Glycosylation	KLECNGENDCGDNSD EEEECCCCCCCCCCC	51.80	-
162	N-linked_Glycosylation	KLECNGENDCGDNSD EEEECCCCCCCCCCC	51.80	17623646
278	Phosphorylation	FSSQGGSSFSVPIFY CCCCCCCCCEEEEEE	25.47	19007248
311	Phosphorylation	QASHKKDSSFIRIHK HHHHCCCCCHHHHHH	35.71	25003641
312	Phosphorylation	ASHKKDSSFIRIHKV HHHCCCCCHHHHHHH	34.52	24719451
324	N-linked_Glycosylation	HKVMKVLNFTTKAKD HHHHHHHCCCCCCHH	34.89	17623646
324	N-linked_Glycosylation	HKVMKVLNFTTKAKD HHHHHHHCCCCCCHH	34.89	17623646
355	Phosphorylation	EYNSALYSRIFDDFG CCCHHHHHHHCCCCC	21.54	24719451
392	O-linked_Glycosylation	ELKNSGLTEEEAKHC HHHHCCCCHHHHHHH	44.89	22267737
561	Phosphorylation	KQSPDYKSNAVDGQW CCCCCCCCCCCCCCC	24.64	-
568	C-linked_Glycosylation	SNAVDGQWGCWSSWS CCCCCCCCCCCCCHH	14.94	10551839
568	C-linked_Glycosylation	SNAVDGQWGCWSSWS CCCCCCCCCCCCCHH	14.94	10551839
571	C-linked_Glycosylation	VDGQWGCWSSWSTCD CCCCCCCCCCHHCCC	7.46	10551839
571	C-linked_Glycosylation	VDGQWGCWSSWSTCD CCCCCCCCCCHHCCC	7.46	10551839
574	C-linked_Glycosylation	QWGCWSSWSTCDATY CCCCCCCHHCCCCCC	7.67	10551839
574	C-linked_Glycosylation	QWGCWSSWSTCDATY CCCCCCCHHCCCCCC	7.67	10551839
727	Phosphorylation	RLYRIGESIELTCPK HHHCCCCCEEEECCC	19.02	24505115
731	Phosphorylation	IGESIELTCPKGFVV CCCCEEEECCCCEEE	17.61	24505115
742	Phosphorylation	GFVVAGPSRYTCQGN CEEEECCCCEECCCC	36.68	-
767	Phosphorylation	TCEKDTLTKLKGHCQ EECCCHHHHHCCCCC	36.10	-
855	N-linked_Glycosylation	ERTRLSSNSTKKESC HHHCCCCCCCCCHHC	50.77	16335952
855	N-linked_Glycosylation	ERTRLSSNSTKKESC HHHCCCCCCCCCHHC	50.77	16335952

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 CO6_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CO6_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 CO6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CO5_HUMAN	C5	physical	2808363
SART3_HUMAN	SART3	physical	21988832
D19L3_HUMAN	DPY19L3	physical	28514442
ACOT9_HUMAN	ACOT9	physical	28514442
B3GLT_HUMAN	B3GALTL	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612446	Complement component 6 deficiency (C6D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CO6_HUMAN

Related Literatures of Post-Translational Modification

C-linked Glycosylation
Reference	PubMed
"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.	22267737 [Abstract]
"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.	10551839 [Abstract]
N-linked Glycosylation
Reference	PubMed
"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.	22267737 [Abstract]
"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.	16335952 [Abstract]
Phosphorylation
Reference	PubMed
"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.	19007248 [Abstract]