Hex:4 HexNAc:4

Taxonomy

• Homo sapiens (Human)

Protein

• Immunoglobulin alpha (non secretory) / Homo sapiens    P01877    P01876
• Immunoglobulin alpha-2 heavy chain (secretory) - heavy chain 1 / Homo sapiens    P0DOX2
• Immunoglobulin alpha-2 heavy chain (secretory) - heavy chain 2 / Homo sapiens    P0DOX2
• Immunoglobulin alpha-2 heavy chain (secretory) - heavy chain 3 / Homo sapiens    P0DOX2
• Immunoglobulin epsilon chain c region / Homo sapiens    P01854
• Immunoglobulin gamma / Homo sapiens    P01859    P01861    P01857    P01860
• Immunoglobulin gamma-1 heavy chain / Homo sapiens    P0DOX5
• Immunoglobulin gamma-3 (anti-nip antibody) / Homo sapiens    
• Immunoglobulin gamma-3-[fa243] (anti-nip antibody) / Homo sapiens    P01860
• Immunoglobulin gamma-3-[ya296] (anti-nip antibody) / Homo sapiens    
• Immunoglobulin heavy constant alpha 1 / Homo sapiens    P01876
• Immunoglobulin heavy constant alpha 1 - heavy chain 1 / Homo sapiens    P01876
• Immunoglobulin heavy constant alpha 1 - heavy chain 2 / Homo sapiens    P01876
• Immunoglobulin heavy constant alpha 2 / Homo sapiens    P01877
• Immunoglobulin heavy constant alpha 2 - heavy chain 1 / Homo sapiens    P01877
• Immunoglobulin heavy constant delta / Homo sapiens    P01880
• Immunoglobulin heavy constant gamma 1 / Homo sapiens    P01857
• Immunoglobulin heavy constant gamma 2 / Homo sapiens    P01859
• Immunoglobulin heavy constant gamma 2 - heavy chain 2 / Homo sapiens    P01859
• Immunoglobulin heavy constant gamma 2 - heavy chain 1 / Homo sapiens    P01859
• Immunoglobulin heavy constant gamma 3 / Homo sapiens    P01860
• Immunoglobulin heavy constant gamma 4 / Homo sapiens    P01861
• Immunoglobulin heavy constant mu / Homo sapiens    P01871
• Immunoglobulin J chain / Homo sapiens    P01591

Source

• Blood Plasma (UBERON_0001969)  
• Blood Serum (UBERON_0001977)  
• Bone Marrow (UBERON_0002371)  
• Mammary Gland (UBERON_0001911)  
• Milk (UBERON_0001913)  
• Ovary (UBERON_0000992)   CHO-K1 (CVCL_0214)  
• Urine (UBERON_0001088)  

Reported structure

• N-Linked / Complex / Structure 2011
• N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)Man(a1-3)[GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc
• N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)Man(a1-6)[GlcNAc(b1-2)Man(a1-3)]Man(b1-4)GlcNAc(b1-4)GlcNAc
• N-Linked / Complex / Gal(b1-4)GlcNAc(b1-2)Man(a1-?)[GlcNAc(b1-2)Man(a1-?)]Man(b1-4)GlcNAc(b1-4)GlcNAc
• N-Linked / Complex / Structure 9500
• N-Linked / Complex / Structure 10889
• N-Linked / Undefined core / Hex(??-?)HexNAc(??-?)Hex(??-?)[HexNAc(??-?)Hex(??-?)]Hex(??-?)HexNAc(??-?)HexNAc
• O-Linked / Core 2 / Gal(b1-3)GlcNAc(b1-3)[Gal(b1-4)GlcNAc(b1-6)]Gal(b1-3)[Gal(b1-4)GlcNAc(b1-6)]GalNAc
• O-Linked / Core 2 / Gal(b1-4)GlcNAc(b1-3)[Gal(b1-4)GlcNAc(b1-6)]Gal(b1-3)[Gal(b1-4)GlcNAc(b1-6)]GalNAc

Composition

• Hex:4 HexNAc:4 (avg mass : 1479.3649 )

Disease

• Arthritis, Rheumatoid (DOID:7148)
• Asymptomatic myositis (DOID:633)
• Cancer, breast (DOID:1612)
• Control/Healthy
• Gastritis (DOID:4029)
• Heavy Chain Disease (DOID:0060125)
• Hypersensitivity reaction disease (DOID:0060056)
• Multiple myeloma (DOID:9538)
• Myeloma (DOID:0070004)
• Myeloma, Multiple with an accompanying Hypogammaglobulinaemia
• Myositis (DOID:633)
• Oral squamous cell carcinoma (DOID:0050866)
• Prostate cancer (DOID:10283)
• Sjogren's Syndrome (DOID:12894)
• Systemic lupus erythematosus (DOID:9074)

Reference

• Community evaluation of glycoproteomics informatics solutions reveals high-performance search strategies for serum glycopeptide analysis (2021 - Rebeca Kawahara, Anastasia Chernykh, Kathirvel Alagesan, Marshall Bern, Weiqian Cao, Robert J. Chalkley, Kai Cheng, Matthew S. Choo, Nathan Edwards, Radoslav Goldman, Marcus Hoffmann, Yingwei Hu, Yifan Huang, Jin Young Kim, Doron Kletter, Benoit Liquet, Mingqi Liu, Yehia Mechref, Bo Meng, Sriram Neelamegham, Terry Nguyen-Khuong, Jonas Nilsson, Adam Pap, Gun Wook Park, Benjamin L. Parker, Cassandra L. Pegg, Josef M. Penninger, Toan K. Phung, Markus Pioch, Erdmann Rapp, Enes Sakalli, Miloslav Sanda, Benjamin L. Schulz, Nichollas E. Scott, Georgy Sofronov, Johannes Stadlmann, Sergey Y. Vakhrushev, Christina M. Woo, Hung-Yi Wu, Pengyuan Yang, Wantao Ying, Hui Zhang, Yong Zhang, Jingfu Zhao, Joseph Zaia, Stuart M. Haslam, Giuseppe Palmisano, Jong Shin Yoo, Göran Larson, Kai-Hooi Khoo, Katalin F. Medzihradszky, Daniel Kolarich, Nicolle H. Packer, Morten Thaysen-Andersen) / Status : Reviewed
• Quantitative Longitudinal Inventory of the N-Glycoproteome of Human Milk from a Single Donor Reveals the Highly Variable Repertoire and Dynamic Site-Specific Changes (2020 - Jing Zhu, Yu-Hsien Lin, Kelly A Dingess, Marko Mank, Bernd Stahl, Albert J R Heck) / Status : Reviewed
• A novel, ultrasensitive approach for quantitative carbohydrate composition and linkage analysis using LC-ESI ion trap tandem mass spectrometry (2019 - Kathirvel Alagesan, Daniel Varon Silva, Peter H Seeberger, Daniel Kolarich) / Status : Reviewed
• Reanalysis of global proteomic and phosphoproteomic data identified a large number of glycopeptides (2018 - Yingwei Hu, Punit Shah, David J. Clark, Minghui Ao, Hui Zhang) / Status : Unreviewed
• Distinct urinary glycoprotein signatures in prostate cancer patients (2018 - Rebeca Kawahara, Fabio Ortega, Livia Rosa-Fernandes, Vanessa Guimarães, Daniel Quina, Willian Nahas, Veit Schwämmle, Miguel Srougi, Katia R.M. Leite, Morten Thaysen-Andersen, Martin R. Larsen and Giuseppe Palmisano) / Status : Unreviewed
• Site-Specific Profiling of Serum Glycoproteins Using N-Linked Glycan and Glycosite Analysis Revealing Atypical N-Glycosylation Sites on Albumin and α-1B-Glycoprotein (2018 - Shisheng Sun, Yingwei Hu, Li Jia, Shadi Toghi Eshghi, Yang Liu, Punit Shah, Hui Zhang) / Status : Unreviewed
• Tongue Cancer Patients Can be Distinguished from Healthy Controls by Specific N-Glycopeptides Found in Serum. (2018 - Mayank Saraswat, Antti Mäkitie, Tiialotta Tohmola, Amy Dickinson, Shruti Saraswat, Sakari Joenväärä, Suvi Renkonen) / Status : Reviewed
• Hinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3) (2015 - Rosina Plomp, Gillian Dekkers, Yoann Rombouts, Remco Visser, Carolien A.M.Koeleman, Guinevere S.M.Kammeijer, Bas C.Jansen, Theo Rispens, Paul J.Hensbergen, Gestur Vidarsson, Manfred Wuhrer) / Status : Reviewed
• The serum immunoglobulin G glycosylation signature of gastric cancer (2015 - L. Renee Ruhaak, Donald A. Barkauskas, Javier Torres, Cara L. Cooke, Lauren D. Wu, Carol Stroble, Sureyya Ozcan, Cynthia C. Williams, Margarita Camorlinga, David M. Rocke, Carlito B. Lebrilla, Jay V. Solnick,) / Status : Reviewed
• Immunoglobulin G (IgG) Fab Glycosylation Analysis Using a New Mass Spectrometric High-throughput Profiling Method Reveals Pregnancy-associated Changes (2014 - Albert Bondt, Yoann Rombouts, Maurice H.J.Selman, Paul J.Hensbergen, Karli R.Reiding, Johanna M.W.Hazes, Radboud J.E.M.Dolhain, Manfred Wuhrer) / Status : Reviewed
• Efficient and accurate glycopeptide identification pipeline for high-throughput site-specific N-glycosylation analysis (2014 - Liu M, Zhang Y, Chen Y, Yan G, Shen C, Cao J, Zhou X, Liu X, Zhang L, Shen H, Lu H, He F, Yang P) / Status : Reviewed
• Selective glycopeptide profiling by acetone enrichment and LC/MS (2014 - Takakura D, Harazono A, Hashii N, Kawasaki N) / Status : Reviewed
• Absolute Quantitation of Immunoglobulin G and Its Glycoforms Using Multiple Reaction Monitoring (2013 - Qiuting Hong, Carlito B. Lebrilla, Suzanne Miyamoto, L. Renee Ruhaak) / Status : Reviewed
• Loci Associated with N-Glycosylation of Human Immunoglobulin G Show Pleiotropy with Autoimmune Diseases and Haematological Cancers (2013 - Gordan Lauc, Jennifer E. Huffman, Maja Pučić, Lina Zgaga, Barbara Adamczyk, Ana Mužinić, Mislav Novokmet, Ozren Polašek, Olga Gornik, Jasminka Krištić, Toma Keser, Veronique Vitart, Blanca Scheijen, Hae-Won Uh, Mariam Molokhia, Alan Leslie Patrick, Paul McKeigue,Ivana Kolčić, Ivan Krešimir Lukić, Olivia Swann, Frank N. van Leeuwen, L. Renee Ruhaak, Jeanine J. Houwing-Duistermaat, P. Eline Slagboom, Marian Beekman, Anton J. M. de Craen, André M. Deelder, Qiang Zeng, Wei Wang, Nicholas D. Hastie, Ulf Gyllensten, James F. Wilson, Manfred Wuhrer, Alan F. Wright, Pauline M. Rudd, Caroline Hayward, Yurii Aulchenko, Harry Campbell, Igor Rudan) / Status : Reviewed
• Mass Spectrometric Determination of IgG Subclass-Specific Glycosylation Profiles in Siblings Discordant for Myositis Syndromes (2011 - Irina Perdivara, Shyamal D. Peddada, Frederick W. Miller, Kenneth B. Tomer, Leesa J. Deterding) / Status : Reviewed
• Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry (2008 - Harazono A, Kawasaki N, Itoh S, Hashii N, Matsuishi-Nakajima Y, Kawanishi T, Yamaguchi T) / Status : Reviewed
• Differential Glycosylation of Polymeric and Monomeric IgA: A Possible Role in Glomerular Inflammation in IgA Nephropathy (2006 - Beatrijs D. Oortwijn, Anja Roos, Louise Royle, Daniëlle J. van Gijlswijk-Janssen, Maria C. Faber-Krol, Jan-Willem Eijgenraam, Raymond A. Dwek, Mohamed R. Daha, Pauline M. Rudd, Cees van Kooten) / Status : Reviewed
• Human Serum IgM Glycosylation: IDENTIFICATION OF GLYCOFORMS THAT CAN BIND TO MANNAN-BINDING LECTIN (2005 - James N.Arnold, Mark R.Wormald, David M.Suter, Catherine M.Radcliffe, David J.Harvey, Raymond A.Dwek, Pauline M.Rudd, Robert B.Sim) / Status : Reviewed
• The Glycosylation of Human Serum IgD and IgE and the Accessibility of Identified Oligomannose Structures for Interaction with Mannan-Binding Lectin (2004 - James N. Arnold, Catherine M. Radcliffe, Mark R. Wormald, Louise Royle, David J. Harvey, Max Crispin, Raymond A. Dwek, Robert B. Sim and Pauline M. Rudd) / Status : Reviewed
• Structural studies on IgG oligosaccharides of patients with primary Sjogren's syndrome. (2002 - Kuroda Y, Nakata M, Makino A, Matsumoto A, Ohashi K, Itahashi K, Takeuchi F, Goto M, Kojima N, Mizuochi T) / Status : Reviewed
• Sialylation of human IgG-Fc carbohydrate by transfected rat alpha2,6-sialyltransferase (2001 - Jassal, Jenkins, Charlwood, Camilleri, Jefferis, Lund) / Status : Reviewed
• Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fc gamma recpetor I and influence the synthesis of its oligosaccharide chains (1996 - Lund, Takahashi, Pound, Goodall, Jefferis) / Status : Reviewed
• The resolution of the neutral N-linked oligosaccharides of IgG by high pH anion-exchange chromatography. (1996 - McGuire J, Douglas M, Smith K) / Status : Reviewed
• Structural heterogeneity of sugar chains in immunoglobulin G. Conformation of immunoglobulin G molecule and substrate specificities of glycosyltransferases. (1990 - Fujii S, Nishiura T, Nishikawa A, Miura R, Taniguchi N) / Status : Reviewed
• A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins. (1990 - Jefferis R, Lund J, Mizutani H, Nakagawa H, Kawazoe Y, Arata Y, Takahashi N) / Status : Reviewed
• Primary structure of twenty three neutral and monosialylated oligosaccharides O-glycosidically linked to the human secretory immunoglobulin A hinge region determined by a combination of permethylation analysis and 400-MHz 1H-NMR spectroscopy. (1989 - Pierce-Cretel A, Decottignies J, Wieruszeski J, Strecker G, Montreuil J, Spik G) / Status : Reviewed
• Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G. (1987 - Takahashi N, Ishii I, Ishihara H, Mori M, Tejima S, Jefferis R, Endo S, Arata Y) / Status : Reviewed
• Structures of the oligosaccharides present at the three asparagine-linked glycosylation sites of human IgD. (1983 - S J Mellis, J U Baenziger) / Status : Reviewed

Reported glycosite

• Immunoglobulin alpha (non secretory) / Homo sapiens
  •        Undefined site
• Immunoglobulin alpha-2 heavy chain (secretory) - heavy chain 1 / Homo sapiens
  •        Undefined site
• Immunoglobulin alpha-2 heavy chain (secretory) - heavy chain 2 / Homo sapiens
  •        Undefined site
• Immunoglobulin alpha-2 heavy chain (secretory) - heavy chain 3 / Homo sapiens
  •        Undefined site
• Immunoglobulin epsilon chain c region / Homo sapiens
  •        Undefined site
• Immunoglobulin gamma / Homo sapiens
  •        Undefined site
• Immunoglobulin gamma-1 heavy chain / Homo sapiens
  •        Undefined site
• Immunoglobulin gamma-3 (anti-nip antibody) / Homo sapiens
  •        Undefined site
• Immunoglobulin gamma-3-[fa243] (anti-nip antibody) / Homo sapiens
  •        Undefined site
• Immunoglobulin gamma-3-[ya296] (anti-nip antibody) / Homo sapiens
  •        Undefined site
• Immunoglobulin heavy constant alpha 1 / Homo sapiens
  •        Undefined site
  •        Thr-106
  •        Asn-144
• Immunoglobulin heavy constant alpha 1 - heavy chain 1 / Homo sapiens
  •        Undefined site
• Immunoglobulin heavy constant alpha 1 - heavy chain 2 / Homo sapiens
  •        Undefined site
• Immunoglobulin heavy constant alpha 2 / Homo sapiens
  •        Undefined site
  •        Asn-131
• Immunoglobulin heavy constant alpha 2 - heavy chain 1 / Homo sapiens
  •        Undefined site
• Immunoglobulin heavy constant delta / Homo sapiens
  •        Undefined site
  •        Asn-316
• Immunoglobulin heavy constant gamma 1 / Homo sapiens
  •        Undefined site
  •        Asn-227
  •        Asn-180
• Immunoglobulin heavy constant gamma 2 / Homo sapiens
  •        Undefined site
  •        Asn-227
  •        Asn-176
• Immunoglobulin heavy constant gamma 2 - heavy chain 2 / Homo sapiens
  •        Undefined site
• Immunoglobulin heavy constant gamma 2 - heavy chain 1 / Homo sapiens
  •        Undefined site
• Immunoglobulin heavy constant gamma 3 / Homo sapiens
  •        Undefined site
  •        Asn-227
• Immunoglobulin heavy constant gamma 4 / Homo sapiens
  •        Asn-177
• Immunoglobulin heavy constant mu / Homo sapiens
  •        Undefined site
  •        Asn-46
• Immunoglobulin J chain / Homo sapiens
  •        Asn-71

Mass spectrometry observed peptide

• RENISDPTSPLRT (13aa)
  •    P01591    Asn-71     Immunoglobulin J chain / Homo sapiens
• HYTNPSQDVTVPCPVPSTPPTPSPSTPPTPSPSCCHPR (38aa)
  •    P01876    Thr-106     Immunoglobulin heavy constant alpha 1 / Homo sapiens
• LSLHRPALEDLLLGSEANLTCTLTGLR (27aa)
  •    P01876    Asn-144     Immunoglobulin heavy constant alpha 1 / Homo sapiens
  •    P01877    Asn-131     Immunoglobulin heavy constant alpha 2 / Homo sapiens
• RLSLHRPALEDLLLGSEANLTCTLTGLRD (29aa)
  •    P01876    Asn-144     Immunoglobulin heavy constant alpha 1 / Homo sapiens
• PALEDLLLGSEANLTCTLTGLR (22aa)
  •    P01876    Asn-144     Immunoglobulin heavy constant alpha 1 / Homo sapiens
• EEQFNSTFR (9aa)
  •    P01860    Asn-227     Immunoglobulin heavy constant gamma 3 / Homo sapiens
  •    VAR_003892   226:Y→F
  •    P01859    Asn-227     Immunoglobulin heavy constant gamma 2 / Homo sapiens
  •    P01859    Asn-176     Immunoglobulin heavy constant gamma 2 / Homo sapiens
• EEQYNSTYR (9aa)
  •    P01857    Asn-227     Immunoglobulin heavy constant gamma 1 / Homo sapiens
  •    P01857    Asn-180     Immunoglobulin heavy constant gamma 1 / Homo sapiens
• REEQYNSTYRV (11aa)
  •    P01857    Asn-180     Immunoglobulin heavy constant gamma 1 / Homo sapiens
• EEQYNSTY (8aa)
  •    P01857    Asn-180     Immunoglobulin heavy constant gamma 1 / Homo sapiens
• KTKPREEQYNSTYRV (15aa)
  •    P01857    Asn-180     Immunoglobulin heavy constant gamma 1 / Homo sapiens
• EEQYNSTYR  (10aa)
  •    P01857    Asn-180     Immunoglobulin heavy constant gamma 1 / Homo sapiens
• EEQYNSTFR (9aa)
  •    P01860    Asn-227     Immunoglobulin heavy constant gamma 3 / Homo sapiens