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. Author manuscript; available in PMC: 2021 Nov 17.
Published in final edited form as: J Carbohydr Chem. 2012 Jan 19;31(1):10–30. doi: 10.1080/07328303.2011.626544

Table 4:

N-linked and O-linked glycosylation site mappings of CA215

Accession number Peptide detecteda Peptide sequence homology of proteins (%)
I. CAC12842.1 1. EEQFNSTFR Immunoglobulin heavy chain (Fc) (100%)
II. CAA04843.1 2. EEQFNSTYR Immunoglobulin heavy chain (Fc) (100%)
III. AAB60643.2 3. LSVPTSEWQR Cathepsin S (100%)
IV AAK68690.1 4. FTCLATNDAGDSSK Hemicentin (100%)
Titin (100%)
Palladin isoform 4 (92%)
LRN4 (78%) (IgSF proteins)
V AAD38158.1 5. DTLMISR Immunoglobulin heavy chain (Fc) (100%)
VI. AAC39746.2 6. GYLPEPVTVTWNSGTLTNGVR Immunoglobulin heavy chain (Fab) (90%)
VII. AAN76042.1 7. SVSLTCMINGFYPSDISVEWEK Immunoglobulin heavy chain (Fc) (90%)
VIII. CAJ75462.1 8. QSSGLYSLSSVVSVTSSSQPVTCNV Immunoglobulin heavy chain (Fab and Fc) (100%)
IX. ABY48864.2 9. VYTMGPPREELSSR Immunoglobulin heavy chain (Fc) (98%)
IgA variable region (89%)
IgM (98%)
X. NP_001139647.1 10. TFPSVR Zinc finger protein 414 isoform I (100%)
Forkhead box protein C2 (100%)
Immunoglobulin heavy chain variable region (83%)
a

Bold letters indicate glycosylation sites.

Fc, constant region of immunoglobulins; Fab, variable region of immunoglobulins.

Lot CA215C (urea-eluted) was used for this analysis.

Source Protein BLAST Service: http://blast.ncbi.nlm.nih.gov/Blast.cgi.