Prothrombin

Taxonomy

• Homo sapiens (Human)

Protein

• Prothrombin / Homo sapiens    P00734

Source

• Blood Plasma (UBERON_0001969)  
• Blood Serum (UBERON_0001977)  
• Cerebrospinal Fluid (UBERON_0001359)  
• Mammary Gland (UBERON_0001911)  
• Milk (UBERON_0001913)  
• Urine (UBERON_0001088)  

Reported structure

• N-Linked / Complex / Gal(?1-?)GlcNAc(?1-?)Man(a1-3)[Gal(?1-?)GlcNAc(?1-?)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc
• N-Linked / Complex / NeuAc(a2-6)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 / NeuAc(a2-6)Gal(b1-4)GlcNAc(b1-2)Man(a1-6)[Gal(b1-4)GlcNAc(b1-2)Man(a1-3)]Man(b1-4)GlcNAc(b1-4)GlcNAc
• N-Linked / Complex / Structure 3507
• N-Linked / Complex / NeuAc(?2-?)Gal(?1-?)GlcNAc(?1-?)Man(a1-3)[NeuAc(?2-?)Gal(?1-?)GlcNAc(?1-?)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc
• N-Linked / Complex / NeuAc(a2-6)Gal(b1-4)GlcNAc(b1-2)Man(a1-3)[NeuAc(a2-6)Gal(b1-4)GlcNAc(b1-2)Man(a1-6)]Man(b1-4)GlcNAc(b1-4)GlcNAc
• N-Linked / Undefined core / HexNAc(??-?)HexNAc(??-?)[Hex(??-?)HexNAc(??-?)]Hex(??-?)[HexNAc(??-?)HexNAc(??-?)[HexNAc(??-?)HexNAc(??-?)]Hex(??-?)]Hex(??-?)HexNAc(??-?)HexNAc

Composition

• Hex:3 HexNAc:6 dHex:1 NeuAc:1 (avg mass : 2161.0134 )
• Hex:3 HexNAc:6 dHex:1 NeuAc:2 (avg mass : 2452.2713 )
• Hex:3 HexNAc:6 dHex:3 (avg mass : 2162.0415 )
• Hex:3 HexNAc:7 (avg mass : 1926.8075 )
• Hex:3 HexNAc:9 dHex:1 (avg mass : 2479.3405 )
• Hex:4 HexNAc:3 NeuAc:1 (avg mass : 1567.4278 )
• Hex:4 HexNAc:4 NeuAc:1 (avg mass : 1770.6228 )
• Hex:4 HexNAc:5 NeuAc:1 NeuGc:1 (avg mass : 2281.0751 )
• Hex:4 HexNAc:9 (avg mass : 2495.3399 )
• Hex:5 HexNAc:3 NeuAc:1 (avg mass : 1729.5702 )
• Hex:5 HexNAc:4 (avg mass : 1641.5073 )
• Hex:5 HexNAc:4 NeuAc:1 (avg mass : 1932.7652 )
• Hex:5 HexNAc:4 NeuAc:2 (avg mass : 2224.0231 )
• Hex:5 HexNAc:4 dHex:1 NeuAc:1 (avg mass : 2078.9082 )
• Hex:5 HexNAc:4 dHex:1 NeuAc:2 (avg mass : 2370.1661 )
• Hex:5 HexNAc:4 dHex:2 NeuAc:1 (avg mass : 2225.0512 )
• Hex:5 HexNAc:4 dHex:2 NeuAc:2 (avg mass : 2516.3091 )
• Hex:5 HexNAc:4 dHex:3 NeuAc:1 (avg mass : 2371.1942 )
• Hex:5 HexNAc:5 dHex:1 NeuAc:1 (avg mass : 2282.1032 )
• Hex:5 HexNAc:6 dHex:1 NeuAc:1 (avg mass : 2485.2982 )
• Hex:6 HexNAc:4 dHex:1 (avg mass : 1949.7927 )
• Hex:6 HexNAc:5 NeuAc:2 (avg mass : 2589.3605 )
• Hex:6 HexNAc:5 NeuAc:3 (avg mass : 2880.6184 )
• Hex:6 HexNAc:5 dHex:1 NeuAc:2 (avg mass : 2735.5035 )
• Hex:6 HexNAc:5 dHex:1 NeuAc:3 (avg mass : 3026.7614 )
• Hex:6 HexNAc:5 dHex:2 (avg mass : 2299.1307 )
• Hex:6 HexNAc:6 (avg mass : 2210.0397 )
• Hex:6 HexNAc:6 NeuAc:2 (avg mass : 2792.5555 )
• Hex:6 HexNAc:6 dHex:1 (avg mass : 2356.1827 )
• Hex:6 HexNAc:6 dHex:1 NeuAc:2 (avg mass : 2938.6985 )
• Hex:6 HexNAc:6 dHex:2 NeuAc:2 (avg mass : 3084.8415 )
• Hex:7 HexNAc:6 NeuAc:3 (avg mass : 3245.9558 )
• Hex:7 HexNAc:6 dHex:1 (avg mass : 2518.3251 )

Disease

• Cancer, breast (DOID:1612)
• Esophageal cancer (DOID:5041)
• Oral squamous cell carcinoma (DOID:0050866)
• Prostate cancer (DOID:10283)

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
• 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
• 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
• Large-scale intact glycopeptide identification by Mascot database search (2018 - Ravi Chand Bollineni, Christian Jeffrey Koehler, Randi Elin Gislefoss, Jan Haug Anonsen, Bernd Thiede) / 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
• Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls (2014 - Kontro H, Joenväärä S, Haglund C, Renkonen R) / Status : Reviewed
• Selective glycopeptide profiling by acetone enrichment and LC/MS (2014 - Takakura D, Harazono A, Hashii N, Kawasaki N) / Status : Reviewed
• Computational framework for identification of intact glycopeptides in complex samples (2014 - Mayampurath A, Yu CY, Song E, Balan J, Mechref Y, Tang H.) / Status : Reviewed
• Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD (2012 - Halim A, Nilsson J, Rüetschi U, Hesse C, Larson G) / Status : Reviewed
• Enrichment of glycopeptides for glycan structure and attachment site identification (2009 - Nilsson J, Rüetschi U, Halim A, Hesse C, Carlsohn E, Brinkmalm G, Larson G.) / Status : Reviewed
• Studies on the structures of the carbohydrate moiety of human prothrombin. (1981 - Mizuochi T, Fujii J, Kisiel W, Kobata A) / Status : Reviewed

Reported glycosite

• Prothrombin / Homo sapiens
  •        Undefined site
  •        Asn-121
  •        Asn-143
  •        Asn-260
  •        Asn-416

Mass spectrometry observed peptide

• DKLAACLEGNCAEGLGTNYRGHVNITR (27aa)
  •    P00734    Asn-121     Prothrombin / Homo sapiens
• GHVNITR (7aa)
  •    P00734    Asn-121     Prothrombin / Homo sapiens
• GHVNITRSGIECQLWR (16aa)
  •    P00734    Asn-121     Prothrombin / Homo sapiens
• YPHKPEINSTTHPGADIQENFCR (23aa)
  •    P00734    Asn-143     Prothrombin / Homo sapiens
• YPHKPEINSTTHPGADLQENFCR (23aa)
  •    P00734    Asn-143     Prothrombin / Homo sapiens
• HKPEINSTTHPGADLQENFCR (21aa)
  •    P00734    Asn-143     Prothrombin / Homo sapiens
• SRYPHKPEINSTTHPGADLQENFCR (25aa)
  •    P00734    Asn-143     Prothrombin / Homo sapiens
• YPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVR (42aa)
  •    P00734    Asn-143     Prothrombin / Homo sapiens
• HQDFNSAVQLVENFCR (16aa)
  •    P00734    Asn-260     Prothrombin / Homo sapiens
• NFTENDLLVR (10aa)
  •    P00734    Asn-416     Prothrombin / Homo sapiens
• KNFTENDLLVRI (12aa)
  •    P00734    Asn-416     Prothrombin / Homo sapiens
• CLLYPPWDKNFTENDLLVR (19aa)
  •    P00734    Asn-416     Prothrombin / Homo sapiens