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
- O-Linked / Core 0 / GalNAc
- O-Linked / Core 1 / Gal(b1-3)GalNAc
- O-Linked / Undefined core / GlcNAc(?1-?)GalNAc
- O-Linked / Core 0 / NeuAc(a2-6)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 2 / GlcNAc(?1-?)Gal(b1-3)[GlcNAc(b1-6)]GalNAc(a1-
- O-Linked / Core 1 / NeuAc(a2-3)Gal(b1-3)[NeuAc(a2-6)]GalNAc
- 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 / 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 / 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)[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(b1-3)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)[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(b1-6)[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 / 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 / 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(?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 / 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 / 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+"+ 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
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 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
- 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
- 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
-
- O-Linked / Core 0 (avg mass : 221.2103)
- Urine (UBERON_0001088)
- Anemia, Aplastic (DOID:12449)
- Determination of site-specific glycan heterogeneity on glycoproteins (2012 - Kolarich D1, Jensen PH, Altmann F, Packer NH.) / 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
-
Erythropoietin / Homo sapiens
- Undefined site
- Ser-153
-
- O-Linked / Core 1 (avg mass : 383.3527)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Determination of site-specific glycan heterogeneity on glycoproteins (2012 - Kolarich D1, Jensen PH, Altmann F, Packer NH.) / 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
- Ser-153
-
- O-Linked / Undefined core (avg mass : 424.4053)
- Erythropoietin / Homo sapiens
-
- O-Linked / Core 0 (avg mass : 512.4682)
- Urine (UBERON_0001088)
- Anemia, Aplastic (DOID:12449)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- O-Linked / Core 1 (avg mass : 674.6106)
- Ovary (UBERON_0000992) CHO (CVCL_0213)
-
Erythropoietin / Homo sapiens
- Undefined site
-
- O-Linked / Core 1 (avg mass : 674.6106)
- Erythropoietin / Homo sapiens
-
- O-Linked / Core 1 (avg mass : 674.6106)
- 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
- 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
-
Erythropoietin / Homo sapiens
- Undefined site
-
- O-Linked / Core 2 (avg mass : 789.7427)
- Erythropoietin / Homo sapiens
-
- O-Linked / Core 1 (avg mass : 965.8685)
- 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
- 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
-
Erythropoietin / Homo sapiens
- Undefined site
-
- 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 / Hybrid (avg mass : 1680.4346)
- Kidney (UBERON_0002113) BHK-21 (CVCL_1914)
- Erythropoietin / Homo sapiens
-
- 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)
- 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 : 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)
- 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 : 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)
- 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
- 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
- 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 : 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
- 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
- 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 : 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
- 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
- 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)
- 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)
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Reported glycosite
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Reported glycosite
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Reported glycosite
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Reported glycosite
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Reported glycosite
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Reported glycosite
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Reported glycosite
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Reported glycosite
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Disease
Reported glycosite
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Reported glycosite
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Disease
Reported glycosite
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Reported glycosite
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Reported glycosite
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Reported glycosite
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Reference
Reported glycosite
Suggested 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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Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
Suggested glycosite
Disease
Reported glycosite
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Disease
Reported glycosite
Suggested glycosite
Disease
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Reported glycosite
Suggested glycosite
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Reported glycosite
Suggested glycosite
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
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Reported glycosite
Suggested glycosite
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Reported glycosite
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Reported glycosite
Suggested glycosite
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Reported glycosite
Suggested glycosite