taxonomy (1)
protein (1)
source (5)
structure (114)
composition (65)
disease (2)
reference (16)
site (5)
peptide (0)
- Homo sapiens (Human)
Taxonomy
- Erythropoietin / Homo sapiens P01588
Protein
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Urine (UBERON_0001088)
- Namalwa (CVCL_0067) B-Lymphocyte (CL_0000236)
- RPMI-1788 (CVCL_2710) B-Lymphocyte (CL_0000236)
Source
- N-Linked / Complex / Man(a1-3)[Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ GlcNAc"
- N-Linked / Complex / Man(a1-3)[Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc+"+ 2 x GlcNAc"
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)Man(a1-?)[Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc
- N-Linked / Complex / Man(a1-3)[Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ 2 x GlcNAc"
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)Man(a1-?)[GlcNAc(?1-?)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / Complex / Fuc(?1-?)[Gal(?1-?)]GlcNAc(?1-?)Man(a1-?)[Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)Man(a1-?)[GlcNAc(?1-?)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]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)GlcNAc
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]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(?1-?)GlcNAc(?1-?)Man(a1-?)[GlcNAc(?1-?)Man(a1-?)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)GlcNAc
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ Fuc"
- 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(?1-?)GlcNAc(?1-?)Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]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 / NeuAc(a2-3)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 / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)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(?1-?)GlcNAc(?1-?)Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ Fuc"
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-?)[Gal(?1-?)GlcNAc(?1-?)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]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(?1-?)GlcNAc(?1-?)[GlcNAc(?1-?)]Man(a1-?)[Gal(?1-?)GlcNAc(?1-?)Man(a1-?)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-?)[Gal(?1-?)GlcNAc(?1-?)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ Fuc"
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-?)[Gal(?1-?)GlcNAc(?1-?)Man(a1-?)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc
- 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 / Structure 2271
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-?)[Gal(?1-?)GlcNAc(?1-?)Man(a1-?)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ Fuc"
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc
- 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(b1-4)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(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-?)[Gal(?1-?)GlcNAc(?1-?)Man(a1-?)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ GlcNAc"
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]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 / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)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 / Structure 867
- 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)[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 / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)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 / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-6)[Gal(b1-4)GlcNAc(b1-2)]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(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ Fuc"
- 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(b1-3)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(a1-6)[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)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- N-Linked / Complex / Structure 886
- 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(b1-6)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc+"+ Neu5,9Ac2(a2-3) + 2 x NeuAc(a2-3)"
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ Gal(?1-?)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 / Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-?)[Gal(b1-4)GlcNAc(b1-?)]Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)Man(a1-3)]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)[Gal(b1-4)GlcNAc(b1-6)]Man(a1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-4)[Gal(b1-4)GlcNAc(b1-2)]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(b1-6)]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 / Structure 1342
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)[NeuAc(a2-3)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(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ Gal(?1-?)GlcNAc(?1-?) + Fuc(?1-?)"
- 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(b1-3)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 / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ Gal(?1-?)GlcNAc(?1-?) + GlcNAc(?1-?)"
- 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 NeuAc(a2-3)"
- 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(b1-4)]Man(a1-3)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-6)[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)[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(b1-6)]Man(a1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-4)[Gal(b1-4)GlcNAc(b1-2)]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)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(b1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)]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 / Structure 3656
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ 2 x Gal(?1-?)GlcNAc(?1-?)"
- 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(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ 2 x Gal(?1-?)GlcNAc(?1-?) + Fuc(?1-?)"
- 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 / Structure 788
- 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(b1-2)[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+"+ Neu5,9Ac2(a2-3) + 3 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+"+ 3 x NeuAc(a2-3) + NeuGc(a2-3)"
- 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 / 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 / Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-6)[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+"+ 3 x NeuAc(a2-3)"
- N-Linked / Complex / NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)[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)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(b1-6)[Gal(b1-4)GlcNAc(b1-2)]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(b1-6)[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 / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ 3 x Gal(?1-?)GlcNAc(?1-?)"
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ 3 x Gal(?1-?)GlcNAc(?1-?) + Fuc(?1-?)"
- 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(b1-6)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)]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 / Structure 2165
- 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) + NeuGc(a2-3)"
- N-Linked / Complex / Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-6)[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+"+ 3 x NeuAc(a2-3) + NeuGc(a2-3)"
- N-Linked / Complex / NeuAc(a2-3)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)[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(b1-4)[Gal(b1-4)GlcNAc(b1-2)]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(b1-6)[Gal(b1-4)GlcNAc(b1-3)Gal(b1-4)GlcNAc(b1-2)]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 / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ 4 x Gal(?1-?)GlcNAc(?1-?)"
- N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ 4 x Gal(?1-?)GlcNAc(?1-?) + Fuc(?1-?)"
- 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 / Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)[Gal(?1-?)GlcNAc(?1-?)]Man(a1-6)][GlcNAc(?1-4)]Man(b1-4)GlcNAc(b1-4)[Fuc(?1-6)]GlcNAc+"+ 5 x Gal(?1-?)GlcNAc(?1-?)"
- 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 / 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(b1-4)[NeuAc(a2-3)Gal(b1-4)GlcNAc(b1-2)]Man(a1-3)]Man(b1-4)GlcNAc(b1-4)[Fuc(a1-6)]GlcNAc
- 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
- O-Linked / Core 0 / GalNAc
- O-Linked / Core 0 / NeuAc(a2-6)GalNAc
- O-Linked / Core 1 / Gal(b1-3)GalNAc
- O-Linked / Core 1 / Gal(b1-3)[NeuAc(a2-6)]GalNAc
- O-Linked / Core 1 / Gal(b1-3)GalNAc(a +"NeuAc"
- 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 / Core 2 / GlcNAc(?1-?)Gal(b1-3)[GlcNAc(b1-6)]GalNAc(a1-
- O-Linked / Undefined core / GlcNAc(?1-?)GalNAc
Reported structure
- HexNAc:1 (avg mass : 221.2103 )
- HexNAc:1 NeuAc:1 (avg mass : 512.4682 )
- HexNAc:2 (avg mass : 424.4053 )
- 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:1 HexNAc:3 (avg mass : 789.7427 )
- Hex:3 HexNAc:3 dHex:1 (avg mass : 1260.1705 )
- Hex:3 HexNAc:4 (avg mass : 1317.2225 )
- Hex:3 HexNAc:4 dHex:1 (avg mass : 1463.3655 )
- Hex:3 HexNAc:6 dHex:1 Su:1 (avg mass : 1949.8197 )
- Hex:4 HexNAc:3 dHex:1 (avg mass : 1422.3129 )
- Hex:4 HexNAc:3 dHex:2 (avg mass : 1568.4559 )
- Hex:4 HexNAc:4 (avg mass : 1479.3649 )
- Hex:4 HexNAc:4 dHex:1 (avg mass : 1625.5079 )
- Hex:4 HexNAc:5 dHex:1 (avg mass : 1828.7029 )
- Hex:5 HexNAc:4 (avg mass : 1641.5073 )
- 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:2 (avg mass : 1933.7933 )
- Hex:5 HexNAc:5 (avg mass : 1844.7023 )
- Hex:5 HexNAc:5 dHex:1 (avg mass : 1990.8453 )
- Hex:5 HexNAc:5 dHex:2 (avg mass : 2136.9883 )
- Hex:5 HexNAc:6 dHex:1 (avg mass : 2194.0403 )
- Hex:6 HexNAc:3 Ph:1 (avg mass : 1680.4346 )
- 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:1 (avg mass : 2444.2456 )
- 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:1 NeuAc:3 Ac:1 (avg mass : 3026.7614 )
- Hex:6 HexNAc:5 dHex:2 (avg mass : 2299.1307 )
- Hex:6 HexNAc:6 dHex:1 (avg mass : 2356.1827 )
- Hex:6 HexNAc:6 dHex:2 (avg mass : 2502.3257 )
- Hex:6 HexNAc:7 dHex:1 (avg mass : 2559.3777 )
- 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:3 NeuGc:1 (avg mass : 3699.3561 )
- Hex:7 HexNAc:6 dHex:1 NeuAc:4 (avg mass : 3683.3567 )
- Hex:7 HexNAc:6 dHex:1 NeuAc:4 Ac:1 (avg mass : 3683.3567 )
- Hex:7 HexNAc:7 dHex:1 (avg mass : 2721.5201 )
- Hex:7 HexNAc:7 dHex:2 (avg mass : 2867.6631 )
- 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:3 NeuGc:1 (avg mass : 4064.6935 )
- Hex:8 HexNAc:7 dHex:1 NeuAc:4 (avg mass : 4048.6941 )
- Hex:8 HexNAc:8 dHex:1 (avg mass : 3086.8575 )
- Hex:8 HexNAc:8 dHex:2 (avg mass : 3233.0005 )
- Hex:8 HexNAc:9 dHex:1 (avg mass : 3290.0525 )
- 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:9 HexNAc:9 dHex:1 (avg mass : 3452.1949 )
- Hex:9 HexNAc:9 dHex:2 (avg mass : 3598.3379 )
- Hex:10 HexNAc:9 dHex:1 (avg mass : 3614.3373 )
- Hex:10 HexNAc:9 dHex:1 NeuAc:4 (avg mass : 4779.3689 )
- Hex:10 HexNAc:10 dHex:1 (avg mass : 3817.5323 )
- Hex:10 HexNAc:10 dHex:2 (avg mass : 3963.6753 )
- Hex:11 HexNAc:11 dHex:1 (avg mass : 4182.8697 )
- Hex:11 HexNAc:11 dHex:2 (avg mass : 4329.0127 )
- Hex:12 HexNAc:12 dHex:1 (avg mass : 4548.2071 )
Composition
- Determination of site-specific glycan heterogeneity on glycoproteins (2012 - Kolarich D1, Jensen PH, Altmann F, Packer NH.) / Status : Reviewed
- Structural analysis of sulfated N-linked oligosaccharides in erythropoietin (2001 - Kawasaki, Haishima, Ohta, Itoh, Hyuga, Hayakawa) / Status : Reviewed
- Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties. (2000 - Cointe D, Bliard R, Jorieux S, Leroy Y, Glacet A, Verbert A, Bourel D, Chirat F) / 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 analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / 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
- Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. (1994 - Watson E, Bhide A, van Halbeek 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
- 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
- Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. (1993 - Inoue N, Takeuchi M, Asano K, Shimizu R, Takasaki S, Kobata A) / Status : Reviewed
- Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization. (1992 - Rice K, Takahashi N, Namiki Y, Tran A, Lisi P, Lee Y) / Status : Reviewed
- Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides. (1991 - Hokke C, Kamerling J, van Dedem G, Vliegenthart J) / Status : Reviewed
- Sialylated carbohydrate chains of recombinant human glycoproteins expressed in Chinese hamster ovary cells contain traces of N-glycolylneuraminic acid. (1990 - Hokke C, Bergwerff A, van Dedem G, van Oostrum J, Kamerling J, Vliegenthart J) / Status : Reviewed
- Recombinant human erythropoietin produced by Namalwa cells. (1989 - Yanagi H, Yoshima T, Ogawa I, Okamoto M) / 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 asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. (1988 - Takeuchi M, Takasaki S, Miyazaki H, Kato T, Hoshi S, Kochibe N, Kobata A) / Status : Reviewed
Reference
- Erythropoietin / Homo sapiens
Reported glycosite
Mass spectrometry observed peptide
-
- N-Linked / Complex (avg mass : 1260.1705)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1317.2225)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1422.3129)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1463.3655)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1479.3649)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1568.4559)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1625.5079)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1641.5073)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Urine (UBERON_0001088)
- Anemia, Aplastic (DOID:12449)
- 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 asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. (1988 - Takeuchi M, Takasaki S, Miyazaki H, Kato T, Hoshi S, Kochibe N, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 1787.6503)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1787.6503)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Urine (UBERON_0001088)
- Anemia, Aplastic (DOID:12449)
- 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 asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. (1988 - Takeuchi M, Takasaki S, Miyazaki H, Kato T, Hoshi S, Kochibe N, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 1828.7029)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1844.7023)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1933.7933)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 1949.8197)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 1990.8453)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2006.8447)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Urine (UBERON_0001088)
- Anemia, Aplastic (DOID:12449)
- 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 asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. (1988 - Takeuchi M, Takasaki S, Miyazaki H, Kato T, Hoshi S, Kochibe N, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2006.8447)
- Anemia, Aplastic (DOID:12449)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2078.9082)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2078.9082)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2136.9883)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2152.9877)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2152.9877)
- 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 : 2152.9877)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Urine (UBERON_0001088)
- Namalwa (CVCL_0067) B-Lymphocyte (CL_0000236)
- 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
- Recombinant human erythropoietin produced by Namalwa cells. (1989 - Yanagi H, Yoshima T, Ogawa I, Okamoto M) / 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 asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. (1988 - Takeuchi M, Takasaki S, Miyazaki H, Kato T, Hoshi S, Kochibe N, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2152.9877)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Urine (UBERON_0001088)
- Anemia, Aplastic (DOID:12449)
- 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 asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. (1988 - Takeuchi M, Takasaki S, Miyazaki H, Kato T, Hoshi S, Kochibe N, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2194.0403)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2299.1307)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2356.1827)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2370.1661)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / Status : Reviewed
- Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. (1994 - Watson E, Bhide A, van Halbeek H) / 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
- Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization. (1992 - Rice K, Takahashi N, Namiki Y, Tran A, Lisi P, Lee Y) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2372.1821)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Urine (UBERON_0001088)
- Anemia, Aplastic (DOID:12449)
- 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 asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. (1988 - Takeuchi M, Takasaki S, Miyazaki H, Kato T, Hoshi S, Kochibe N, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2444.2456)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2502.3257)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2518.3251)
- Erythropoietin / Homo sapiens
-
- 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)
- Anemia, Aplastic (DOID:12449)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2518.3251)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Urine (UBERON_0001088)
- Namalwa (CVCL_0067) B-Lymphocyte (CL_0000236)
- 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
- Recombinant human erythropoietin produced by Namalwa cells. (1989 - Yanagi H, Yoshima T, Ogawa I, Okamoto M) / 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 asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. (1988 - Takeuchi M, Takasaki S, Miyazaki H, Kato T, Hoshi S, Kochibe N, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2559.3777)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2721.5201)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2735.5035)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / 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 : 2735.5035)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2735.5035)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2735.5035)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / 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 : 2735.5035)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2735.5035)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2735.5035)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 2867.6631)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 2883.6625)
- Urine (UBERON_0001088)
- Anemia, Aplastic (DOID:12449)
-
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)
- 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)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3026.7614)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / Status : Reviewed
- Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. (1994 - Watson E, Bhide A, van Halbeek 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
- 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
- Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization. (1992 - Rice K, Takahashi N, Namiki Y, Tran A, Lisi P, Lee Y) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3026.7614)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 3026.7614)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / Status : Reviewed
- Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. (1994 - Watson E, Bhide A, van Halbeek 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
- 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
- Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization. (1992 - Rice K, Takahashi N, Namiki Y, Tran A, Lisi P, Lee Y) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3026.7614)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3086.8575)
- Erythropoietin / Homo sapiens
-
- 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)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3100.8409)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
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)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 3100.8409)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3233.0005)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 3248.9999)
- Urine (UBERON_0001088)
- Anemia, Aplastic (DOID:12449)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3248.9999)
- 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 asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. (1988 - Takeuchi M, Takasaki S, Miyazaki H, Kato T, Hoshi S, Kochibe N, Kobata A) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3290.0525)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 3392.0988)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3392.0988)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / Status : Reviewed
- Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. (1994 - Watson E, Bhide A, van Halbeek 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
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3392.0988)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / Status : Reviewed
- Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. (1994 - Watson E, Bhide A, van Halbeek H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3392.0988)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / Status : Reviewed
- Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. (1994 - Watson E, Bhide A, van Halbeek H) / 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 : 3392.0988)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / Status : Reviewed
- Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. (1994 - Watson E, Bhide A, van Halbeek H) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3392.0988)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3392.0988)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3392.0988)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 3452.1949)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 3466.1783)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3598.3379)
- Erythropoietin / Homo sapiens
-
- 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)
- Erythropoietin / Homo sapiens
-
- N-Linked / Complex (avg mass : 3683.3567)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / Status : Reviewed
- Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. (1994 - Watson E, Bhide A, van Halbeek 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
- 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
- Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization. (1992 - Rice K, Takahashi N, Namiki Y, Tran A, Lisi P, Lee Y) / Status : Reviewed
- Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides. (1991 - Hokke C, Kamerling J, van Dedem G, Vliegenthart J) / Status : Reviewed
- Sialylated carbohydrate chains of recombinant human glycoproteins expressed in Chinese hamster ovary cells contain traces of N-glycolylneuraminic acid. (1990 - Hokke C, Bergwerff A, van Dedem G, van Oostrum J, Kamerling J, Vliegenthart J) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3683.3567)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3699.3561)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
- Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. (1995 - Hokke C, Bergwerff A, Van Dedem G, Kamerling J, Vliegenthart J) / Status : Reviewed
- Sialylated carbohydrate chains of recombinant human glycoproteins expressed in Chinese hamster ovary cells contain traces of N-glycolylneuraminic acid. (1990 - Hokke C, Bergwerff A, van Dedem G, van Oostrum J, Kamerling J, Vliegenthart J) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3757.4362)
- 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
- Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization. (1992 - Rice K, Takahashi N, Namiki Y, Tran A, Lisi P, Lee Y) / Status : Reviewed
-
Erythropoietin / Homo sapiens
- Undefined site
-
- N-Linked / Complex (avg mass : 3757.4362)
Disease
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Reported glycosite
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Disease
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Reported glycosite
Suggested glycosite
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Reported glycosite
Suggested glycosite
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Reported glycosite
Suggested glycosite
Source
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Reported glycosite
Suggested glycosite
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Reported glycosite
Suggested glycosite
Source
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Reference
Reported glycosite
Suggested glycosite
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Disease
Reported glycosite
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Reported glycosite
Suggested glycosite
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Reported glycosite
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Reported glycosite
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Source
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Reported glycosite
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Disease
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Reported glycosite
Suggested glycosite
Source
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Reported glycosite
Suggested glycosite
Source
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Reported glycosite
Suggested glycosite
Disease
Reference
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
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Reference
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Source
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
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Disease
Reported glycosite
Suggested glycosite
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Reported glycosite
Suggested glycosite
Source
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Reported glycosite
Suggested glycosite
Disease
Reference
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
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Disease
Reported glycosite
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Reported glycosite
Suggested glycosite
Source
Reference
Reported glycosite
Suggested glycosite
Source
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Reference
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Source
Disease
Reported glycosite
Suggested glycosite
Source
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Source
Disease
Reference
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Source
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Source
Disease
Reference
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Source
Disease
Reference
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite