taxonomy (2)
protein (6)
source (2)
structure (76)
composition (52)
disease (0)
reference (13)
site (8)
peptide (0)
- Coagulation factor VII / Homo sapiens P08709
- Erythropoietin / Homo sapiens P01588
- Interleukin-2 / Homo sapiens P60568
- L-selectin / Homo sapiens P14151
- Lactotransferrin / Homo sapiens P02788
- Phosphatidylcholine-sterol acyltransferase / Homo sapiens P04180
Protein
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914) Plasma Membrane (GO_0005886)
Source
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)Man(a1-?)[GalNAc(b1-4)GlcNAc(b1-2)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-?)[Gal(b1-4)GlcNAc(b1-2)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / Complex / Fuc(a1-2)Gal(b1-4)GlcNAc(b1-2)Man(a1-?)[Gal(b1-4)GlcNAc(b1-2)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / HSO3(-6)GlcNAc(b1-4)[GlcNAc(b1-2)]Man(a1-3)[GlcNAc(b1-2)[GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)Man(a1-3)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-3)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)Man(a1-3)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-?)[Gal(b1-4)GlcNAc(b1-2)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-3)GlcNAc(b1-4)[Gal(b1-4)GlcNAc(b1-2)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-3)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)Man(a1-?)[GalNAc(b1-4)GlcNAc(b1-2)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ Gal(b1-4)GlcNAc(b1-4)"
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-3)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / Complex / Fuc(a1-2)Gal(b1-4)GlcNAc(b1-2)Man(a1-?)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ Fuc(a1-2)"
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-3)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc+"+ Gal(b1-4)GlcNAc(b1-3)"
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc+"Gal(b1-4)GlcNAc(b1-3)"
- N-Linked / Complex / Gal(b1-3)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-3)GlcNAc(b1-4)[Gal(b1-4)GlcNAc(b1-2)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-3)GlcNAc(b1-?)[Gal(b1-4)GlcNAc(b1-?)]Man(a1-?)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-?)]Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ Gal(b1-4)GlcNAc(b1-3)"
- N-Linked / Complex / Fuc(a1-2)Gal(b1-4)GlcNAc(b1-4)[Gal(b1-4)GlcNAc(b1-2)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ NeuAc(a2-3)"
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-3)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ NeuAc"
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ Fuc(a1-2)"
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-?)]Man(a1-?)[Gal(b1-4)GlcNAc(b1-?)[GalNAc(b1-4)GlcNAc(b1-?)]Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ NeuAc(a2-3)"
- N-Linked / Complex / Fuc(a1-2)Gal(b1-4)GlcNAc(b1-4)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)]Man(a1-3)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ Gal(b1-4)GlcNAc(b1-3)"
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-?)]Man(a1-?)[Gal(b1-4)GlcNAc(b1-2)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ 2 x Gal(b1-4)GlcNAc(b1-3)"
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-?)[Gal(b1-4)GlcNAc(b1-?)]Man(a1-?)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-?)]Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ 2 x NeuAc(a2-3)"
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-?)]Man(a1-?)[Gal(b1-4)GlcNAc(b1-?)[GalNAc(b1-4)GlcNAc(b1-?)]Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ 2 x NeuAc(a2-3)"
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ 2 x Gal(b1-4)GlcNAc(b1-3)"
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)Man(a1-?)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-?)]Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ 3 x Gal(b1-4)GlcNAc(b1-3) "
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-?)]Man(a1-?)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-?)[GalNAc(b1-4)GlcNAc(b1-?)]Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ 3 x Gal(b1-4)GlcNAc(b1-3)"
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)Man(a1-?)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-?)]Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ 4 x Gal(b1-4)GlcNAc(b1-3)"
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ 3 x NeuAc(a2-3)"
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)]Man(a1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-4)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / High-Mannose / Man(a1-2)Man(a1-2)Man(a1-3)[Man(a1-6)]Man(b1-4)GlcNAc
- N-Linked / High-Mannose / Man(a1-3)[Man(a1-6)]Man(a1-6)[Man(a1-3)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / High-Mannose / Man(a1-3)[Man(a1-6)]Man(a1-6)[Man(a1-3)]Man(b1-4)GlcNAc(b1-4)GlcNAc+"+ Man(a1-2)"
- N-Linked / High-Mannose / Man(a1-3)[Man(a1-6)]Man(a1-6)[Man(a1-3)]Man(b1-4)GlcNAc(b1-4)GlcNAc+"+ 2 x Man(a1-2)"
- N-Linked / High-Mannose / Man(a1-3)[Man(a1-6)]Man(a1-6)[Man(a1-3)]Man(b1-4)GlcNAc(b1-4)GlcNAc+"+ 3 x Man(a1-2)"
- N-Linked / High-Mannose / Man(a1-3)[Man(a1-6)]Man(a1-6)[Man(a1-3)]Man(b1-4)GlcNAc(b1-4)GlcNAc+"+ 4 x Man(a1-2)"
- N-Linked / Hybrid / GlcNAc(a1-P-6)Man(a1-2)Man(a1-3)[Man(a1-3)[Man(a1-6)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / Hybrid / Gal(b1-4)GlcNAc(b1-2)Man(a1-?)[Man(a1-3)[Man(a1-6)]Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- O-Linked / Core 1 / Gal(b1-3)GalNAc
- O-Linked / Core 1 / NeuAc(a2-3)Gal(b1-3)GalNAc
- O-Linked / Core 1 / NeuAc(a2-3)Gal(b1-3)[NeuAc(a2-6)]GalNAc
- O-Linked / No-core / Xyl(?1-?)Glc+"+ Xyl"
- O-Linked / O-Fuc / Fuc
- O-Linked / O-Glc / Glc
- O-Linked / O-Glc / Xyl(?1-?)Glc
Reported structure
- dHex:1 (avg mass : 164.1583 )
- Hex:1 (avg mass : 180.1577 )
- Hex:1 Pent:1 (avg mass : 312.2738 )
- Hex:1 Pent:2 (avg mass : 444.3899 )
- Hex:1 HexNAc:1 (avg mass : 383.3527 )
- Hex:1 HexNAc:1 NeuAc:1 (avg mass : 674.6106 )
- Hex:1 HexNAc:1 NeuAc:2 (avg mass : 965.8685 )
- Hex:3 HexNAc:6 dHex:1 Su:1 (avg mass : 1949.8197 )
- Hex:4 HexNAc:5 dHex:1 (avg mass : 1828.7029 )
- Hex:5 HexNAc:1 (avg mass : 1031.9223 )
- Hex:5 HexNAc:2 (avg mass : 1235.1173 )
- Hex:5 HexNAc:4 (avg mass : 1641.5073 )
- Hex:5 HexNAc:4 NeuAc:1 (avg mass : 1932.7652 )
- Hex:5 HexNAc:4 NeuAc:2 (avg mass : 2224.0231 )
- Hex:5 HexNAc:4 dHex:1 (avg mass : 1787.6503 )
- Hex:5 HexNAc:4 dHex:1 NeuAc:1 (avg mass : 2078.9082 )
- Hex:5 HexNAc:4 dHex:1 NeuAc:2 (avg mass : 2370.1661 )
- Hex:5 HexNAc:4 dHex:1 NeuAc:3 (avg mass : 2661.424 )
- Hex:5 HexNAc:4 dHex:2 (avg mass : 1933.7933 )
- Hex:5 HexNAc:4 dHex:2 NeuAc:1 (avg mass : 2225.0512 )
- Hex:5 HexNAc:6 dHex:1 (avg mass : 2194.0403 )
- Hex:6 HexNAc:2 (avg mass : 1397.2597 )
- Hex:6 HexNAc:3 Ph:1 (avg mass : 1680.4346 )
- Hex:6 HexNAc:3 dHex:1 (avg mass : 1746.5977 )
- Hex:6 HexNAc:5 (avg mass : 2006.8447 )
- Hex:6 HexNAc:5 dHex:1 (avg mass : 2152.9877 )
- Hex:6 HexNAc:5 dHex:1 NeuAc:2 (avg mass : 2735.5035 )
- Hex:6 HexNAc:5 dHex:1 NeuAc:3 (avg mass : 3026.7614 )
- Hex:6 HexNAc:5 dHex:2 (avg mass : 2299.1307 )
- Hex:6 HexNAc:5 dHex:2 NeuAc:1 (avg mass : 2590.3886 )
- Hex:6 HexNAc:5 dHex:2 NeuAc:2 (avg mass : 2881.6465 )
- Hex:6 HexNAc:7 dHex:1 NeuAc:1 (avg mass : 2850.6356 )
- Hex:6 HexNAc:7 dHex:1 NeuAc:2 (avg mass : 3141.8935 )
- Hex:6 HexNAc:7 dHex:1 NeuAc:3 (avg mass : 3433.1514 )
- Hex:7 HexNAc:2 (avg mass : 1559.4021 )
- Hex:7 HexNAc:6 (avg mass : 2372.1821 )
- Hex:7 HexNAc:6 dHex:1 (avg mass : 2518.3251 )
- Hex:7 HexNAc:6 dHex:1 NeuAc:2 (avg mass : 3100.8409 )
- Hex:7 HexNAc:6 dHex:1 NeuAc:3 (avg mass : 3392.0988 )
- Hex:7 HexNAc:6 dHex:1 NeuAc:4 (avg mass : 3683.3567 )
- Hex:7 HexNAc:6 dHex:2 (avg mass : 2664.4681 )
- Hex:8 HexNAc:2 (avg mass : 1721.5445 )
- Hex:8 HexNAc:7 dHex:1 (avg mass : 2883.6625 )
- Hex:8 HexNAc:7 dHex:1 NeuAc:2 (avg mass : 3466.1783 )
- Hex:8 HexNAc:7 dHex:1 NeuAc:3 (avg mass : 3757.4362 )
- Hex:8 HexNAc:7 dHex:1 NeuAc:4 (avg mass : 4048.6941 )
- Hex:9 HexNAc:2 (avg mass : 1883.6869 )
- Hex:9 HexNAc:8 dHex:1 (avg mass : 3248.9999 )
- Hex:9 HexNAc:8 dHex:1 NeuAc:3 (avg mass : 4122.7736 )
- Hex:9 HexNAc:8 dHex:1 NeuAc:4 (avg mass : 4414.0315 )
- Hex:10 HexNAc:9 dHex:1 (avg mass : 3614.3373 )
- Hex:10 HexNAc:9 dHex:1 NeuAc:4 (avg mass : 4779.3689 )
Composition
Disease
- Structural analysis of sulfated N-linked oligosaccharides in erythropoietin (2001 - Kawasaki, Haishima, Ohta, Itoh, Hyuga, Hayakawa) / Status : Reviewed
- Carbohydrate structures of soluble human L-selectin recombinantly expressed in baby-hamster kidney cells. (2000 - Gohlke M, Mach U, Nuck R, Zimmermann-Kordmann M, Grunow D, Fieger C, Volz B, Tauber R, Petri T, Debus N, Reutter W) / Status : Reviewed
- Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties. (1998 - Lacko A, Reason A, Nuckolls C, Kudchodkar B, Nair M, Sundarrajan G, Pritchard P, Morris H, Dell A) / Status : Reviewed
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Structural determination of two N-linked glycans isolated from recombinant human lactoferrin expressed in BHK cells. (1995 - Legrand D, Salmon V, Coddeville B, Benaissa M, Plancke Y, Spik G) / Status : Reviewed
- Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells. (1995 - Nimtz M, Wray V, Rdiger A, Conradt H) / Status : Reviewed
- A strategy for the mapping of N-glycans by high-performance capillary electrophoresis. (1994 - Hermentin P, Doenges R, Witzel R, Hokke C, Vliegenthart J, Kamerling J, Conradt H, Nimtz M, Brazel D) / Status : Reviewed
- Accumulation of pentamannose oligosaccharides in human mononuclear leukocytes by action of swainsonine, an inhibitor of glycoprotein processing. (1993 - Kang M, Bowlin T, Vijay I, Sunkara S) / Status : Reviewed
- Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells. (1993 - Nimtz M, Martin W, Wray V, Klppel K, Augustin J, Conradt H) / Status : Reviewed
- Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine. (1991 - Bjoern S, Foster D, Thim L, Wiberg F, Christensen M, Komiyama Y, Pedersen A, Kisiel W) / Status : Reviewed
- Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells. Structure of O-linked carbohydrate chains and their location within the polypeptide. (1989 - Conradt H, Nimtz M, Dittmar K, Lindenmaier W, Hoppe J, Hauser H) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
- Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. (1984 - Yamashita K, Ohkura T, Tachibana Y, Takasaki S, Kobata A) / Status : Reviewed
Reference
- Coagulation factor VII / Homo sapiens
-
Erythropoietin / Homo sapiens
- Undefined site
- Asn-51
- Interleukin-2 / Homo sapiens
-
L-selectin / Homo sapiens
- Undefined site
-
Lactotransferrin / Homo sapiens
- Undefined site
-
Phosphatidylcholine-sterol acyltransferase / Homo sapiens
- Undefined site
Reported glycosite
Mass spectrometry observed peptide
-
- N-Linked / Complex
(avg mass : 1641.5073)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914) Plasma Membrane (GO_0005886)
- Carbohydrate structures of soluble human L-selectin recombinantly expressed in baby-hamster kidney cells. (2000 - Gohlke M, Mach U, Nuck R, Zimmermann-Kordmann M, Grunow D, Fieger C, Volz B, Tauber R, Petri T, Debus N, Reutter W) / Status : Reviewed
- Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties. (1998 - Lacko A, Reason A, Nuckolls C, Kudchodkar B, Nair M, Sundarrajan G, Pritchard P, Morris H, Dell A) / Status : Reviewed
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
- Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. (1984 - Yamashita K, Ohkura T, Tachibana Y, Takasaki S, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
L-selectin / Homo sapiens
- Undefined site
-
Phosphatidylcholine-sterol acyltransferase / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 1787.6503)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914) Plasma Membrane (GO_0005886)
- Carbohydrate structures of soluble human L-selectin recombinantly expressed in baby-hamster kidney cells. (2000 - Gohlke M, Mach U, Nuck R, Zimmermann-Kordmann M, Grunow D, Fieger C, Volz B, Tauber R, Petri T, Debus N, Reutter W) / Status : Reviewed
- Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties. (1998 - Lacko A, Reason A, Nuckolls C, Kudchodkar B, Nair M, Sundarrajan G, Pritchard P, Morris H, Dell A) / Status : Reviewed
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
- Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. (1984 - Yamashita K, Ohkura T, Tachibana Y, Takasaki S, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
L-selectin / Homo sapiens
- Undefined site
-
Phosphatidylcholine-sterol acyltransferase / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 1828.7029)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 1932.7652)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Lactotransferrin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 1933.7933)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 1949.8197)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2006.8447)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914) Plasma Membrane (GO_0005886)
- Carbohydrate structures of soluble human L-selectin recombinantly expressed in baby-hamster kidney cells. (2000 - Gohlke M, Mach U, Nuck R, Zimmermann-Kordmann M, Grunow D, Fieger C, Volz B, Tauber R, Petri T, Debus N, Reutter W) / Status : Reviewed
- Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties. (1998 - Lacko A, Reason A, Nuckolls C, Kudchodkar B, Nair M, Sundarrajan G, Pritchard P, Morris H, Dell A) / Status : Reviewed
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
- Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. (1984 - Yamashita K, Ohkura T, Tachibana Y, Takasaki S, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
L-selectin / Homo sapiens
- Undefined site
-
Phosphatidylcholine-sterol acyltransferase / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2006.8447)
-
- N-Linked / Complex
(avg mass : 2006.8447)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Phosphatidylcholine-sterol acyltransferase / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2078.9082)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Carbohydrate structures of soluble human L-selectin recombinantly expressed in baby-hamster kidney cells. (2000 - Gohlke M, Mach U, Nuck R, Zimmermann-Kordmann M, Grunow D, Fieger C, Volz B, Tauber R, Petri T, Debus N, Reutter W) / Status : Reviewed
- Structural determination of two N-linked glycans isolated from recombinant human lactoferrin expressed in BHK cells. (1995 - Legrand D, Salmon V, Coddeville B, Benaissa M, Plancke Y, Spik G) / Status : Reviewed
-
L-selectin / Homo sapiens
- Undefined site
-
Lactotransferrin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2152.9877)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Carbohydrate structures of soluble human L-selectin recombinantly expressed in baby-hamster kidney cells. (2000 - Gohlke M, Mach U, Nuck R, Zimmermann-Kordmann M, Grunow D, Fieger C, Volz B, Tauber R, Petri T, Debus N, Reutter W) / Status : Reviewed
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2152.9877)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914) Plasma Membrane (GO_0005886)
- Carbohydrate structures of soluble human L-selectin recombinantly expressed in baby-hamster kidney cells. (2000 - Gohlke M, Mach U, Nuck R, Zimmermann-Kordmann M, Grunow D, Fieger C, Volz B, Tauber R, Petri T, Debus N, Reutter W) / Status : Reviewed
- Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties. (1998 - Lacko A, Reason A, Nuckolls C, Kudchodkar B, Nair M, Sundarrajan G, Pritchard P, Morris H, Dell A) / Status : Reviewed
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
- Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. (1984 - Yamashita K, Ohkura T, Tachibana Y, Takasaki S, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
L-selectin / Homo sapiens
- Undefined site
-
Phosphatidylcholine-sterol acyltransferase / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2152.9877)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914) Plasma Membrane (GO_0005886)
- Carbohydrate structures of soluble human L-selectin recombinantly expressed in baby-hamster kidney cells. (2000 - Gohlke M, Mach U, Nuck R, Zimmermann-Kordmann M, Grunow D, Fieger C, Volz B, Tauber R, Petri T, Debus N, Reutter W) / Status : Reviewed
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
- Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. (1984 - Yamashita K, Ohkura T, Tachibana Y, Takasaki S, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2152.9877)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Phosphatidylcholine-sterol acyltransferase / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2194.0403)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2224.0231)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Lactotransferrin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2225.0512)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2299.1307)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2370.1661)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Carbohydrate structures of soluble human L-selectin recombinantly expressed in baby-hamster kidney cells. (2000 - Gohlke M, Mach U, Nuck R, Zimmermann-Kordmann M, Grunow D, Fieger C, Volz B, Tauber R, Petri T, Debus N, Reutter W) / Status : Reviewed
- Structural determination of two N-linked glycans isolated from recombinant human lactoferrin expressed in BHK cells. (1995 - Legrand D, Salmon V, Coddeville B, Benaissa M, Plancke Y, Spik G) / Status : Reviewed
- Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells. (1993 - Nimtz M, Martin W, Wray V, Klppel K, Augustin J, Conradt H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
L-selectin / Homo sapiens
- Undefined site
-
Lactotransferrin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2372.1821)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914) Plasma Membrane (GO_0005886)
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
- Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. (1984 - Yamashita K, Ohkura T, Tachibana Y, Takasaki S, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2372.1821)
-
- N-Linked / Complex
(avg mass : 2372.1821)
-
- N-Linked / Complex
(avg mass : 2518.3251)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2518.3251)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2518.3251)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2518.3251)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914) Plasma Membrane (GO_0005886)
- Carbohydrate structures of soluble human L-selectin recombinantly expressed in baby-hamster kidney cells. (2000 - Gohlke M, Mach U, Nuck R, Zimmermann-Kordmann M, Grunow D, Fieger C, Volz B, Tauber R, Petri T, Debus N, Reutter W) / Status : Reviewed
- Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties. (1998 - Lacko A, Reason A, Nuckolls C, Kudchodkar B, Nair M, Sundarrajan G, Pritchard P, Morris H, Dell A) / Status : Reviewed
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
- Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. (1984 - Yamashita K, Ohkura T, Tachibana Y, Takasaki S, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
L-selectin / Homo sapiens
- Undefined site
-
Phosphatidylcholine-sterol acyltransferase / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2518.3251)
-
- N-Linked / Complex
(avg mass : 2590.3886)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2661.424)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2664.4681)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2735.5035)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2735.5035)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2850.6356)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2881.6465)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2883.6625)
-
- N-Linked / Complex
(avg mass : 2883.6625)
-
- N-Linked / Complex
(avg mass : 2883.6625)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2883.6625)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 2883.6625)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3026.7614)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- A strategy for the mapping of N-glycans by high-performance capillary electrophoresis. (1994 - Hermentin P, Doenges R, Witzel R, Hokke C, Vliegenthart J, Kamerling J, Conradt H, Nimtz M, Brazel D) / Status : Reviewed
- Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells. (1993 - Nimtz M, Martin W, Wray V, Klppel K, Augustin J, Conradt H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3026.7614)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- A strategy for the mapping of N-glycans by high-performance capillary electrophoresis. (1994 - Hermentin P, Doenges R, Witzel R, Hokke C, Vliegenthart J, Kamerling J, Conradt H, Nimtz M, Brazel D) / Status : Reviewed
- Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells. (1993 - Nimtz M, Martin W, Wray V, Klppel K, Augustin J, Conradt H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3100.8409)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3100.8409)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3141.8935)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3248.9999)
-
- N-Linked / Complex
(avg mass : 3248.9999)
-
- N-Linked / Complex
(avg mass : 3248.9999)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3392.0988)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3392.0988)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3433.1514)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3466.1783)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3614.3373)
-
- N-Linked / Complex
(avg mass : 3614.3373)
-
- N-Linked / Complex
(avg mass : 3614.3373)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Biological and physicochemical characterization of recombinant human erythropoietins fractionated by Mono Q column chromatography and their modification with sialyltransferase. (1996 - Morimoto K, Tsuda E, Said A, Uchida E, Hatakeyama S, Ueda M, Hayakawa T) / Status : Reviewed
- Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins. (1988 - Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3683.3567)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- A strategy for the mapping of N-glycans by high-performance capillary electrophoresis. (1994 - Hermentin P, Doenges R, Witzel R, Hokke C, Vliegenthart J, Kamerling J, Conradt H, Nimtz M, Brazel D) / Status : Reviewed
- Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells. (1993 - Nimtz M, Martin W, Wray V, Klppel K, Augustin J, Conradt H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3757.4362)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 3757.4362)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 4048.6941)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- A strategy for the mapping of N-glycans by high-performance capillary electrophoresis. (1994 - Hermentin P, Doenges R, Witzel R, Hokke C, Vliegenthart J, Kamerling J, Conradt H, Nimtz M, Brazel D) / Status : Reviewed
- Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells. (1993 - Nimtz M, Martin W, Wray V, Klppel K, Augustin J, Conradt H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 4122.7736)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 4414.0315)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- A strategy for the mapping of N-glycans by high-performance capillary electrophoresis. (1994 - Hermentin P, Doenges R, Witzel R, Hokke C, Vliegenthart J, Kamerling J, Conradt H, Nimtz M, Brazel D) / Status : Reviewed
- Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells. (1993 - Nimtz M, Martin W, Wray V, Klppel K, Augustin J, Conradt H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex
(avg mass : 4779.3689)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / High-Mannose
(avg mass : 1031.9223)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
- N-Linked / High-Mannose
(avg mass : 1235.1173)
-
- N-Linked / High-Mannose
(avg mass : 1397.2597)
-
- N-Linked / High-Mannose
(avg mass : 1559.4021)
-
- N-Linked / High-Mannose
(avg mass : 1721.5445)
-
- N-Linked / High-Mannose
(avg mass : 1883.6869)
-
- N-Linked / Hybrid
(avg mass : 1680.4346)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Erythropoietin / Homo sapiens
-
- N-Linked / Hybrid
(avg mass : 1746.5977)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
L-selectin / Homo sapiens
- Undefined site
-
- O-Linked / Core 1
(avg mass : 383.3527)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- O-Linked / Core 1
(avg mass : 674.6106)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells. (1993 - Nimtz M, Martin W, Wray V, Klppel K, Augustin J, Conradt H) / Status : Reviewed
- Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells. Structure of O-linked carbohydrate chains and their location within the polypeptide. (1989 - Conradt H, Nimtz M, Dittmar K, Lindenmaier W, Hoppe J, Hauser H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
- Interleukin-2 / Homo sapiens
-
- O-Linked / Core 1
(avg mass : 965.8685)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells. (1993 - Nimtz M, Martin W, Wray V, Klppel K, Augustin J, Conradt H) / Status : Reviewed
- Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells. Structure of O-linked carbohydrate chains and their location within the polypeptide. (1989 - Conradt H, Nimtz M, Dittmar K, Lindenmaier W, Hoppe J, Hauser H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
- Interleukin-2 / Homo sapiens
-
- O-Linked / No-core
(avg mass : 444.3899)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Coagulation factor VII / Homo sapiens
-
- O-Linked / O-Fuc
(avg mass : 164.1583)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Coagulation factor VII / Homo sapiens
-
- O-Linked / O-Glc
(avg mass : 180.1577)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Coagulation factor VII / Homo sapiens
-
- O-Linked / O-Glc
(avg mass : 312.2738)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Coagulation factor VII / Homo sapiens
Source
Reported glycosite
- O-Linked / O-Glc
(avg mass : 312.2738)
Source
Reported glycosite
- O-Linked / O-Glc
(avg mass : 180.1577)
Source
Reported glycosite
- O-Linked / O-Fuc
(avg mass : 164.1583)
Source
Reported glycosite
- O-Linked / No-core
(avg mass : 444.3899)
Source
Reference
Reported glycosite
- O-Linked / Core 1
(avg mass : 965.8685)
Source
Reference
Reported glycosite
- O-Linked / Core 1
(avg mass : 674.6106)
Source
Reported glycosite
- O-Linked / Core 1
(avg mass : 383.3527)
Source
Reported glycosite
- N-Linked / Hybrid
(avg mass : 1746.5977)
Source
Reported glycosite
- N-Linked / Hybrid
(avg mass : 1680.4346)
Reported glycosite
- N-Linked / High-Mannose
(avg mass : 1883.6869)
Reported glycosite
- N-Linked / High-Mannose
(avg mass : 1721.5445)
Reported glycosite
- N-Linked / High-Mannose
(avg mass : 1559.4021)
Reported glycosite
- N-Linked / High-Mannose
(avg mass : 1397.2597)
Reported glycosite
- N-Linked / High-Mannose
(avg mass : 1235.1173)
Source
Reported glycosite
- N-Linked / High-Mannose
(avg mass : 1031.9223)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 4779.3689)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 4414.0315)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 4122.7736)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 4048.6941)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 3757.4362)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 3757.4362)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 3683.3567)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 3614.3373)
Reported glycosite
- N-Linked / Complex
(avg mass : 3614.3373)
Reported glycosite
- N-Linked / Complex
(avg mass : 3614.3373)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 3466.1783)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 3433.1514)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 3392.0988)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 3392.0988)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 3248.9999)
Reported glycosite
- N-Linked / Complex
(avg mass : 3248.9999)
Reported glycosite
- N-Linked / Complex
(avg mass : 3248.9999)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 3141.8935)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 3100.8409)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 3100.8409)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 3026.7614)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 3026.7614)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2883.6625)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 2883.6625)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 2883.6625)
Reported glycosite
- N-Linked / Complex
(avg mass : 2883.6625)
Reported glycosite
- N-Linked / Complex
(avg mass : 2883.6625)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2881.6465)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2850.6356)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2735.5035)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2735.5035)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2664.4681)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2661.424)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2590.3886)
Reported glycosite
- N-Linked / Complex
(avg mass : 2518.3251)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 2518.3251)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2518.3251)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2518.3251)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2518.3251)
Reported glycosite
- N-Linked / Complex
(avg mass : 2372.1821)
Reported glycosite
- N-Linked / Complex
(avg mass : 2372.1821)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 2372.1821)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 2370.1661)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2299.1307)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2225.0512)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2224.0231)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2194.0403)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2152.9877)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 2152.9877)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 2152.9877)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 2152.9877)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 2078.9082)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 2006.8447)
Reported glycosite
- N-Linked / Complex
(avg mass : 2006.8447)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 2006.8447)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 1949.8197)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 1933.7933)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 1932.7652)
Source
Reported glycosite
- N-Linked / Complex
(avg mass : 1828.7029)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 1787.6503)
Source
Reference
Reported glycosite
- N-Linked / Complex
(avg mass : 1641.5073)
