CO8B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CO8B_HUMAN
• UniProt AC: P07358
• Protein Name: Complement component C8 beta chain
• Gene Name: C8B
• Organism: Homo sapiens (Human).
• Sequence Length: 591
• 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: MKNSRTWAWRAPVELFLLCAALGCLSLPGSRGERPHSFGSNAVNKSFAKSRQMRSVDVTLMPIDCELSSWSSWTTCDPCQKKRYRYAYLLQPSQFHGEPCNFSDKEVEDCVTNRPCRSQVRCEGFVCAQTGRCVNRRLLCNGDNDCGDQSDEANCRRIYKKCQHEMDQYWGIGSLASGINLFTNSFEGPVLDHRYYAGGCSPHYILNTRFRKPYNVESYTPQTQGKYEFILKEYESYSDFERNVTEKMASKSGFSFGFKIPGIFELGISSQSDRGKHYIRRTKRFSHTKSVFLHARSDLEVAHYKLKPRSLMLHYEFLQRVKRLPLEYSYGEYRDLFRDFGTHYITEAVLGGIYEYTLVMNKEAMERGDYTLNNVHACAKNDFKIGGAIEEVYVSLGVSVGKCRGILNEIKDRNKRDTMVEDLVVLVRGGASEHITTLAYQELPTADLMQEWGDAVQYNPAIIKVKVEPLYELVTATDFAYSSTVRQNMKQALEEFQKEVSSCHCAPCQGNGVPVLKGSRCDCICPVGSQGLACEVSYRKNTPIDGKWNCWSNWSSCSGRRKTRQRQCNNPPPQNGGSPCSGPASETLDCS

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
46	Phosphorylation	GSNAVNKSFAKSRQM CCCCCCHHHHHHHCC	25.82	28188228
70	C-linked_Glycosylation	IDCELSSWSSWTTCD ECEECCCCCCCCCCC	7.94	10551839
73	C-linked_Glycosylation	ELSSWSSWTTCDPCQ ECCCCCCCCCCCHHH	7.10	10551839
101	N-linked_Glycosylation	QFHGEPCNFSDKEVE HCCCCCCCCCCCCHH	50.61	UniProtKB CARBOHYD
105	Acetylation	EPCNFSDKEVEDCVT CCCCCCCCCHHHHHC	63.56	30587353
144	N-linked_Glycosylation	RLLCNGDNDCGDQSD EEEECCCCCCCCCCH	48.12	17623646
144	N-linked_Glycosylation	RLLCNGDNDCGDQSD EEEECCCCCCCCCCH	48.12	-
150	Phosphorylation	DNDCGDQSDEANCRR CCCCCCCCHHHHHHH	42.00	24505115
214	Phosphorylation	NTRFRKPYNVESYTP CCCCCCCCCCCCCCC	34.57	-
227	Phosphorylation	TPQTQGKYEFILKEY CCCCCCEEEEEHHEH	23.93	-
234	Phosphorylation	YEFILKEYESYSDFE EEEEHHEHHCCHHHH	14.48	-
243	N-linked_Glycosylation	SYSDFERNVTEKMAS CCHHHHHHHHHHHHH	37.55	16335952
278	Phosphorylation	QSDRGKHYIRRTKRF CCHHCHHHHHHCCCC	10.29	23403867
346	Phosphorylation	DFGTHYITEAVLGGI HHCCHHHHHHHHCHH	15.66	22817900
371	Phosphorylation	AMERGDYTLNNVHAC HHHHCCCCCCCHHHH	27.96	22817900
418	Phosphorylation	KDRNKRDTMVEDLVV HHCCCCCCCEEEEEE	27.44	16335952
501	Phosphorylation	EEFQKEVSSCHCAPC HHHHHHHHHCCCCCC	28.48	-
551	C-linked_Glycosylation	IDGKWNCWSNWSSCS CCCCCCCCCCCHHCC	7.47	10551839
554	C-linked_Glycosylation	KWNCWSNWSSCSGRR CCCCCCCCHHCCCCC	6.01	10551839

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CO8B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CO8B_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CO8B_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CO8B_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 613789: Complement component 8 deficiency, 2 (C8D2)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

C-linked Glycosylation

"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-70; TRP-73; TRP-551 AND TRP-554.
PubMed: 10551839

N-linked Glycosylation

"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-243, AND MASSSPECTROMETRY.
PubMed: 19159218

"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-243, AND MASSSPECTROMETRY.
PubMed: 16335952

Phosphorylation

"Structure of human C8 protein provides mechanistic insight intomembrane pore formation by complement.";
Lovelace L.L., Cooper C.L., Sodetz J.M., Lebioda L.;
J. Biol. Chem. 286:17585-17592(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 55-591, PHOSPHORYLATION ATTHR-418, SUBUNIT, AND DISULFIDE BONDS.
PubMed: 21454577

"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418, AND MASSSPECTROMETRY.
PubMed: 17693683