dbPTM

CO7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CO7_HUMAN
UniProt AC	P10643
Protein Name	Complement component C7
Gene Name	C7
Organism	Homo sapiens (Human).
Sequence Length	843
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. C7 serves as a membrane anchor..
Protein Sequence	MKVISLFILVGFIGEFQSFSSASSPVNCQWDFYAPWSECNGCTKTQTRRRSVAVYGQYGGQPCVGNAFETQSCEPTRGCPTEEGCGERFRCFSGQCISKSLVCNGDSDCDEDSADEDRCEDSERRPSCDIDKPPPNIELTGNGYNELTGQFRNRVINTKSFGGQCRKVFSGDGKDFYRLSGNVLSYTFQVKINNDFNYEFYNSTWSYVKHTSTEHTSSSRKRSFFRSSSSSSRSYTSHTNEIHKGKSYQLLVVENTVEVAQFINNNPEFLQLAEPFWKELSHLPSLYDYSAYRRLIDQYGTHYLQSGSLGGEYRVLFYVDSEKLKQNDFNSVEEKKCKSSGWHFVVKFSSHGCKELENALKAASGTQNNVLRGEPFIRGGGAGFISGLSYLELDNPAGNKRRYSAWAESVTNLPQVIKQKLTPLYELVKEVPCASVKKLYLKWALEEYLDEFDPCHCRPCQNGGLATVEGTHCLCHCKPYTFGAACEQGVLVGNQAGGVDGGWSCWSSWSPCVQGKKTRSRECNNPPPSGGGRSCVGETTESTQCEDEELEHLRLLEPHCFPLSLVPTEFCPSPPALKDGFVQDEGTMFPVGKNVVYTCNEGYSLIGNPVARCGEDLRWLVGEMHCQKIACVLPVLMDGIQSHPQKPFYTVGEKVTVSCSGGMSLEGPSAFLCGSSLKWSPEMKNARCVQKENPLTQAVPKCQRWEKLQNSRCVCKMPYECGPSLDVCAQDERSKRILPLTVCKMHVLHCQGRNYTLTGRDSCTLPASAEKACGACPLWGKCDAESSKCVCREASECEEEGFSICVEVNGKEQTMSECEAGALRCRGQSISVTSIRPCAAETQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	C-linked_Glycosylation	QWDFYAPWSECNGCT CEEEECCHHHCCCCC	9.89	10551839
36	C-linked_Glycosylation	QWDFYAPWSECNGCT CEEEECCHHHCCCCC	9.89	10551839
202	N-linked_Glycosylation	DFNYEFYNSTWSYVK CCCEEEEEECEEEEE	37.98	14760718
202	N-linked_Glycosylation	DFNYEFYNSTWSYVK CCCEEEEEECEEEEE	37.98	16335952
223	Phosphorylation	TSSSRKRSFFRSSSS CCCCCCHHHCCCCCC	31.60	24719451
228	Phosphorylation	KRSFFRSSSSSSRSY CHHHCCCCCCCCCCE	29.95	-
229	Phosphorylation	RSFFRSSSSSSRSYT HHHCCCCCCCCCCEE	35.17	24425749
230	Phosphorylation	SFFRSSSSSSRSYTS HHCCCCCCCCCCEEC	33.99	24425749
231	Phosphorylation	FFRSSSSSSRSYTSH HCCCCCCCCCCEECC	31.55	24425749
234	Phosphorylation	SSSSSSRSYTSHTNE CCCCCCCCEECCCCE	34.41	24425749
331	Phosphorylation	LKQNDFNSVEEKKCK HCCCCCCCCHHHHHH	30.79	27130503
422	Phosphorylation	QVIKQKLTPLYELVK HHHHHHCCHHHHHHH	20.48	29083192
425	Phosphorylation	KQKLTPLYELVKEVP HHHCCHHHHHHHHCC	14.39	29083192
467	Phosphorylation	CQNGGLATVEGTHCL CCCCCEEEEECCEEE	24.92	29507054
503	C-linked_Glycosylation	AGGVDGGWSCWSSWS CCCCCCCCCCHHCCC	8.88	10551839
503	C-linked_Glycosylation	AGGVDGGWSCWSSWS CCCCCCCCCCHHCCC	8.88	10551839
506	C-linked_Glycosylation	VDGGWSCWSSWSPCV CCCCCCCHHCCCCCC	7.00	10551839
506	C-linked_Glycosylation	VDGGWSCWSSWSPCV CCCCCCCHHCCCCCC	7.00	10551839
509	C-linked_Glycosylation	GWSCWSSWSPCVQGK CCCCHHCCCCCCCCC	10.77	10551839
509	C-linked_Glycosylation	GWSCWSSWSPCVQGK CCCCHHCCCCCCCCC	10.77	10551839
598	Phosphorylation	VGKNVVYTCNEGYSL CCCCEEEECCCCCCC	9.39	24505115
696	O-linked_Glycosylation	VQKENPLTQAVPKCQ EECCCCHHHCCHHHH	18.75	22171320
754	N-linked_Glycosylation	VLHCQGRNYTLTGRD EEEECCCCEEECCCC	40.75	16335952
754	N-linked_Glycosylation	VLHCQGRNYTLTGRD EEEECCCCEEECCCC	40.75	17623646
834	Phosphorylation	GQSISVTSIRPCAAE CCCEEEEEEEECCCC	17.91	-

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 CO7_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CO7_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 CO7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CO7_HUMAN !!

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610102	Complement component 7 deficiency (C7D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CO7_HUMAN

Related Literatures of Post-Translational Modification

C-linked Glycosylation
Reference	PubMed
"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-36; TRP-503; TRP-506 AND TRP-509.	10551839 [Abstract]
N-linked Glycosylation
Reference	PubMed
"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-202 AND ASN-754, AND MASSSPECTROMETRY.	16335952 [Abstract]
"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-202, AND MASSSPECTROMETRY.	14760718 [Abstract]
O-linked Glycosylation
Reference	PubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT THR-696, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.	22171320 [Abstract]