Plasminogen

Details

Name
Plasminogen
Kind
protein
Synonyms
  • 3.4.21.7
Gene Name
PLG
UniProtKB Entry
P00747Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0016037|Plasminogen
MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFT
CRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKN
GITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILE
CEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRE
LRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWS
AQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTE
QLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAG
LTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEED
CMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGG
PWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRT
RFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLE
PTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQ
LPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSW
GLGCARPNKPGVYVRVSRFVTWIEGVMRNN
Number of residues
810
Molecular Weight
90568.415
Theoretical pI
7.25
GO Classification
Functions
endopeptidase activity / enzyme binding / kinase binding / protease binding / protein antigen binding / protein-folding chaperone binding / signaling receptor binding
Processes
biological process involved in interaction with symbiont / labyrinthine layer blood vessel development / mononuclear cell migration / muscle cell cellular homeostasis / myoblast differentiation / negative regulation of cell population proliferation / positive regulation of blood vessel endothelial cell migration / tissue regeneration / trans-synaptic signaling by BDNF, modulating synaptic transmission / trophoblast giant cell differentiation
Components
collagen-containing extracellular matrix / external side of plasma membrane / glutamatergic synapse / Schaffer collateral - CA1 synapse
General Function
Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells
Specific Function
apolipoprotein binding
Pfam Domain Function
Signal Regions
1-19
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0016038|Plasminogen (PLG)
ATGGAACATAAGGAAGTGGTTCTTCTACTTCTTTTATTTCTGAAATCAGGTCAAGGAGAG
CCTCTGGATGACTATGTGAATACCCAGGGGGCTTCACTGTTCAGTGTCACTAAGAAGCAG
CTGGGAGCAGGAAGTATAGAAGAATGTGCAGCAAAATGTGAGGAGGACGAAGAATTCACC
TGCAGGGCATTCCAATATCACAGTAAAGAGCAACAATGTGTGATAATGGCTGAAAACAGG
AAGTCCTCCATAATCATTAGGATGAGAGATGTAGTTTTATTTGAAAAGAAAGTGTATCTC
TCAGAGTGCAAGACTGGGAATGGAAAGAACTACAGAGGGACGATGTCCAAAACAAAAAAT
GGCATCACCTGTCAAAAATGGAGTTCCACTTCTCCCCACAGACCTAGATTCTCACCTGCT
ACACACCCCTCAGAGGGACTGGAGGAGAACTACTGCAGGAATCCAGACAACGATCCGCAG
GGGCCCTGGTGCTATACTACTGATCCAGAAAAGAGATATGACTACTGCGACATTCTTGAG
TGTGAAGAGGAATGTATGCATTGCAGTGGAGAAAACTATGACGGCAAAATTTCCAAGACC
ATGTCTGGACTGGAATGCCAGGCCTGGGACTCTCAGAGCCCACACGCTCATGGATACATT
CCTTCCAAATTTCCAAACAAGAACCTGAAGAAGAATTACTGTCGTAACCCCGATAGGGAG
CTGCGGCCTTGGTGTTTCACCACCGACCCCAACAAGCGCTGGGAACTTTGTGACATCCCC
CGCTGCACAACACCTCCACCATCTTCTGGTCCCACCTACCAGTGTCTGAAGGGAACAGGT
GAAAACTATCGCGGGAATGTGGCTGTTACCGTGTCCGGGCACACCTGTCAGCACTGGAGT
GCACAGACCCCTCACACACATAACAGGACACCAGAAAACTTCCCCTGCAAAAATTTGGAT
GAAAACTACTGCCGCAATCCTGACGGAAAAAGGGCCCCATGGTGCCATACAACCAACAGC
CAAGTGCGGTGGGAGTACTGTAAGATACCGTCCTGTGACTCCTCCCCAGTATCCACGGAA
CAATTGGCTCCCACAGCACCACCTGAGCTAACCCCTGTGGTCCAGGACTGCTACCATGGT
GATGGACAGAGCTACCGAGGCACATCCTCCACCACCACCACAGGAAAGAAGTGTCAGTCT
TGGTCATCTATGACACCACACCGGCACCAGAAGACCCCAGAAAACTACCCAAATGCTGGC
CTGACAATGAACTACTGCAGGAATCCAGATGCCGATAAAGGCCCCTGGTGTTTTACCACA
GACCCCAGCGTCAGGTGGGAGTACTGCAACCTGAAAAAATGCTCAGGAACAGAAGCGAGT
GTTGTAGCACCTCCGCCTGTTGTCCTGCTTCCAGATGTAGAGACTCCTTCCGAAGAAGAC
TGTATGTTTGGGAATGGGAAAGGATACCGAGGCAAGAGGGCGACCACTGTTACTGGGACG
CCATGCCAGGACTGGGCTGCCCAGGAGCCCCATAGACACAGCATTTTCACTCCAGAGACA
AATCCACGGGCGGGTCTGGAAAAAAATTACTGCCGTAACCCTGATGGTGATGTAGGTGGT
CCCTGGTGCTACACGACAAATCCAAGAAAACTTTACGACTACTGTGATGTCCCTCAGTGT
GCGGCCCCTTCATTTGATTGTGGGAAGCCTCAAGTGGAGCCGAAGAAATGTCCTGGAAGG
GTTGTAGGGGGGTGTGTGGCCCACCCACATTCCTGGCCCTGGCAAGTCAGTCTTAGAACA
AGGTTTGGAATGCACTTCTGTGGAGGCACCTTGATATCCCCAGAGTGGGTGTTGACTGCT
GCCCACTGCTTGGAGAAGTCCCCAAGGCCTTCATCCTACAAGGTCATCCTGGGTGCACAC
CAAGAAGTGAATCTCGAACCGCATGTTCAGGAAATAGAAGTGTCTAGGCTGTTCTTGGAG
CCCACACGAAAAGATATTGCCTTGCTAAAGCTAAGCAGTCCTGCCGTCATCACTGACAAA
GTAATCCCAGCTTGTCTGCCATCCCCAAATTATGTGGTCGCTGACCGGACCGAATGTTTC
ATCACTGGCTGGGGAGAAACCCAAGGTACTTTTGGAGCTGGCCTTCTCAAGGAAGCCCAG
CTCCCTGTGATTGAGAATAAAGTGTGCAATCGCTATGAGTTTCTGAATGGAAGAGTCCAA
TCCACCGAACTCTGTGCTGGGCATTTGGCCGGAGGCACTGACAGTTGCCAGGGTGACAGT
GGAGGTCCTCTGGTTTGCTTCGAGAAGGACAAATACATTTTACAAGGAGTCACTTCTTGG
GGTCTTGGCTGTGCACGCCCCAATAAGCCTGGTGTCTATGTTCGTGTTTCAAGGTTTGTT
ACTTGGATTGAGGGAGTGATGAGAAATAATTAA
Chromosome Location
6
Locus
6q26
External Identifiers
ResourceLink
UniProtKB IDP00747
UniProtKB Entry NamePLMN_HUMAN
GenBank Protein ID387026
GenBank Gene IDX05199
GeneCard IDPLG
GenAtlas IDPLG
HGNC IDHGNC:9071
PDB ID(s)1B2I, 1BML, 1BUI, 1CEA, 1CEB, 1DDJ, 1HPJ, 1HPK, 1I5K, 1KI0, 1KRN, 1L4D, 1L4Z, 1PK4, 1PKR, 1PMK, 1QRZ, 1RJX, 2DOH, 2DOI, 2KNF, 2L0S, 2PK4, 3UIR, 4A5T, 4CIK, 4DCB, 4DUR, 4DUU, 5HPG, 5UGD, 5UGG, 6D3X, 6D3Y, 6D3Z, 6D40, 6OG4, 6OQJ, 6OQK, 6Q1U, 6UZ4, 6UZ5, 7E50, 7THS, 7UAH, 8F7U, 8F7V, 8UQ6
KEGG IDhsa:5340
IUPHAR/Guide To Pharmacology ID2394
NCBI Gene ID5340
General References
  1. Petersen TE, Martzen MR, Ichinose A, Davie EW: Characterization of the gene for human plasminogen, a key proenzyme in the fibrinolytic system. J Biol Chem. 1990 Apr 15;265(11):6104-11. [Article]
  2. Forsgren M, Raden B, Israelsson M, Larsson K, Heden LO: Molecular cloning and characterization of a full-length cDNA clone for human plasminogen. FEBS Lett. 1987 Mar 23;213(2):254-60. [Article]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [Article]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. Wiman B, Wallen P: Structural relationship between "glutamic acid" and "lysine" forms of human plasminogen and their interaction with the NH2-terminal activation peptide as studied by affinity chromatography. Eur J Biochem. 1975 Jan 15;50(3):489-94. [Article]
  6. Malinowski DP, Sadler JE, Davie EW: Characterization of a complementary deoxyribonucleic acid coding for human and bovine plasminogen. Biochemistry. 1984 Aug 28;23(18):4243-50. [Article]
  7. Wiman B, Wallen P: Amino-acid sequence of the cyanogen-bromide fragment from human plasminogen that forms the linkage between the plasmin chains. Eur J Biochem. 1975 Oct 15;58(2):539-47. [Article]
  8. Wiman B: Primary structure of the B-chain of human plasmin. Eur J Biochem. 1977 Jun 1;76(1):129-37. [Article]
  9. Robbins KC, Bernabe P, Arzadon L, Summaria L: The primary structure of human plasminogen. II. The histidine loop of human plasmin: light (B) chain active center histidine sequence. J Biol Chem. 1973 Mar 10;248(5):1631-3. [Article]
  10. Groskopf WR, Summaria L, Robbins KC: Studies on the active center of human plasmin. Partial amino acid sequence of a peptide containing the active center serine residue. J Biol Chem. 1969 Jul 10;244(13):3590-7. [Article]
  11. Trexler M, Vali Z, Patthy L: Structure of the omega-aminocarboxylic acid-binding sites of human plasminogen. Arginine 70 and aspartic acid 56 are essential for binding of ligand by kringle 4. J Biol Chem. 1982 Jul 10;257(13):7401-6. [Article]
  12. Vali Z, Patthy L: The fibrin-binding site of human plasminogen. Arginines 32 and 34 are essential for fibrin affinity of the kringle 1 domain. J Biol Chem. 1984 Nov 25;259(22):13690-4. [Article]
  13. Wang H, Prorok M, Bretthauer RK, Castellino FJ: Serine-578 is a major phosphorylation locus in human plasma plasminogen. Biochemistry. 1997 Jul 1;36(26):8100-6. [Article]
  14. Marti T, Schaller J, Rickli EE, Schmid K, Kamerling JP, Gerwig GJ, van Halbeek H, Vliegenthart JF: The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen. Species specificity in relation to sialylation and fucosylation patterns. Eur J Biochem. 1988 Apr 5;173(1):57-63. [Article]
  15. Borza DB, Morgan WT: Acceleration of plasminogen activation by tissue plasminogen activator on surface-bound histidine-proline-rich glycoprotein. J Biol Chem. 1997 Feb 28;272(9):5718-26. [Article]
  16. Pirie-Shepherd SR, Stevens RD, Andon NL, Enghild JJ, Pizzo SV: Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2. J Biol Chem. 1997 Mar 14;272(11):7408-11. [Article]
  17. O'Reilly MS, Holmgren L, Shing Y, Chen C, Rosenthal RA, Moses M, Lane WS, Cao Y, Sage EH, Folkman J: Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma. Cell. 1994 Oct 21;79(2):315-28. [Article]
  18. Sim BK, O'Reilly MS, Liang H, Fortier AH, He W, Madsen JW, Lapcevich R, Nacy CA: A recombinant human angiostatin protein inhibits experimental primary and metastatic cancer. Cancer Res. 1997 Apr 1;57(7):1329-34. [Article]
  19. Lijnen HR, Ugwu F, Bini A, Collen D: Generation of an angiostatin-like fragment from plasminogen by stromelysin-1 (MMP-3). Biochemistry. 1998 Apr 7;37(14):4699-702. [Article]
  20. Moser TL, Stack MS, Asplin I, Enghild JJ, Hojrup P, Everitt L, Hubchak S, Schnaper HW, Pizzo SV: Angiostatin binds ATP synthase on the surface of human endothelial cells. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):2811-6. [Article]
  21. Goretzki L, Lombardo CR, Stallcup WB: Binding of the NG2 proteoglycan to kringle domains modulates the functional properties of angiostatin and plasmin(ogen). J Biol Chem. 2000 Sep 15;275(37):28625-33. [Article]
  22. Rossignol P, Ho-Tin-Noe B, Vranckx R, Bouton MC, Meilhac O, Lijnen HR, Guillin MC, Michel JB, Angles-Cano E: Protease nexin-1 inhibits plasminogen activation-induced apoptosis of adherent cells. J Biol Chem. 2004 Mar 12;279(11):10346-56. Epub 2003 Dec 29. [Article]
  23. Bratt A, Birot O, Sinha I, Veitonmaki N, Aase K, Ernkvist M, Holmgren L: Angiomotin regulates endothelial cell-cell junctions and cell motility. J Biol Chem. 2005 Oct 14;280(41):34859-69. Epub 2005 Jul 25. [Article]
  24. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. doi: 10.1002/pmic.200701057. [Article]
  25. Kirschbaum NE, Budzynski AZ: A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule. J Biol Chem. 1990 Aug 15;265(23):13669-76. [Article]
  26. Poon IK, Olsson AK, Hulett MD, Parish CR: Regulation of histidine-rich glycoprotein (HRG) function via plasmin-mediated proteolytic cleavage. Biochem J. 2009 Oct 23;424(1):27-37. doi: 10.1042/BJ20090794. [Article]
  27. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  28. Mulichak AM, Tulinsky A, Ravichandran KG: Crystal and molecular structure of human plasminogen kringle 4 refined at 1.9-A resolution. Biochemistry. 1991 Oct 29;30(43):10576-88. [Article]
  29. Wu TP, Padmanabhan K, Tulinsky A, Mulichak AM: The refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4. Biochemistry. 1991 Oct 29;30(43):10589-94. [Article]
  30. Wu TP, Padmanabhan KP, Tulinsky A: The structure of recombinant plasminogen kringle 1 and the fibrin binding site. Blood Coagul Fibrinolysis. 1994 Apr;5(2):157-66. [Article]
  31. Mathews II, Vanderhoff-Hanaver P, Castellino FJ, Tulinsky A: Crystal structures of the recombinant kringle 1 domain of human plasminogen in complexes with the ligands epsilon-aminocaproic acid and trans-4-(aminomethyl)cyclohexane-1-carboxylic Acid. Biochemistry. 1996 Feb 27;35(8):2567-76. [Article]
  32. Stec B, Yamano A, Whitlow M, Teeter MM: Structure of human plasminogen kringle 4 at 1.68 a and 277 K. A possible structural role of disordered residues. Acta Crystallogr D Biol Crystallogr. 1997 Mar 1;53(Pt 2):169-78. [Article]
  33. Parry MA, Fernandez-Catalan C, Bergner A, Huber R, Hopfner KP, Schlott B, Guhrs KH, Bode W: The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action. Nat Struct Biol. 1998 Oct;5(10):917-23. [Article]
  34. Chang Y, Mochalkin I, McCance SG, Cheng B, Tulinsky A, Castellino FJ: Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen. Biochemistry. 1998 Mar 10;37(10):3258-71. [Article]
  35. Wang X, Terzyan S, Tang J, Loy JA, Lin X, Zhang XC: Human plasminogen catalytic domain undergoes an unusual conformational change upon activation. J Mol Biol. 2000 Jan 28;295(4):903-14. [Article]
  36. Rios-Steiner JL, Schenone M, Mochalkin I, Tulinsky A, Castellino FJ: Structure and binding determinants of the recombinant kringle-2 domain of human plasminogen to an internal peptide from a group A Streptococcal surface protein. J Mol Biol. 2001 May 11;308(4):705-19. [Article]
  37. Abad MC, Arni RK, Grella DK, Castellino FJ, Tulinsky A, Geiger JH: The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin. J Mol Biol. 2002 May 10;318(4):1009-17. [Article]
  38. Wakeham N, Terzyan S, Zhai P, Loy JA, Tang J, Zhang XC: Effects of deletion of streptokinase residues 48-59 on plasminogen activation. Protein Eng. 2002 Sep;15(9):753-61. [Article]
  39. Terzyan S, Wakeham N, Zhai P, Rodgers K, Zhang XC: Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain. Proteins. 2004 Aug 1;56(2):277-84. [Article]
  40. Millers EK, Johnson LA, Birrell GW, Masci PP, Lavin MF, de Jersey J, Guddat LW: The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake. PLoS One. 2013;8(1):e54104. doi: 10.1371/journal.pone.0054104. Epub 2013 Jan 15. [Article]
  41. Atkinson RA, Williams RJ: Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry. J Mol Biol. 1990 Apr 5;212(3):541-52. [Article]
  42. Rejante MR, Llinas M: 1H-NMR assignments and secondary structure of human plasminogen kringle 1. Eur J Biochem. 1994 May 1;221(3):927-37. [Article]
  43. Rejante MR, Llinas M: Solution structure of the epsilon-aminohexanoic acid complex of human plasminogen kringle 1. Eur J Biochem. 1994 May 1;221(3):939-49. [Article]
  44. Sohndel S, Hu CK, Marti D, Affolter M, Schaller J, Llinas M, Rickli EE: Recombinant gene expression and 1H NMR characteristics of the kringle (2 + 3) supermodule: spectroscopic/functional individuality of plasminogen kringle domains. Biochemistry. 1996 Feb 20;35(7):2357-64. [Article]
  45. Marti DN, Hu CK, An SS, von Haller P, Schaller J, Llinas M: Ligand preferences of kringle 2 and homologous domains of human plasminogen: canvassing weak, intermediate, and high-affinity binding sites by 1H-NMR. Biochemistry. 1997 Sep 30;36(39):11591-604. [Article]
  46. Ichinose A, Espling ES, Takamatsu J, Saito H, Shinmyozu K, Maruyama I, Petersen TE, Davie EW: Two types of abnormal genes for plasminogen in families with a predisposition for thrombosis. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):115-9. [Article]
  47. Azuma H, Uno Y, Shigekiyo T, Saito S: Congenital plasminogen deficiency caused by a Ser572 to Pro mutation. Blood. 1993 Jul 15;82(2):475-80. [Article]
  48. Miyata T, Iwanaga S, Sakata Y, Aoki N: Plasminogen Tochigi: inactive plasmin resulting from replacement of alanine-600 by threonine in the active site. Proc Natl Acad Sci U S A. 1982 Oct;79(20):6132-6. [Article]
  49. Miyata T, Iwanaga S, Sakata Y, Aoki N, Takamatsu J, Kamiya T: Plasminogens Tochigi II and Nagoya: two additional molecular defects with Ala-600----Thr replacement found in plasmin light chain variants. J Biochem. 1984 Aug;96(2):277-87. [Article]
  50. Kikuchi S, Yamanouchi Y, Li L, Kobayashi K, Ijima H, Miyazaki R, Tsuchiya S, Hamaguchi H: Plasminogen with type-I mutation is polymorphic in the Japanese population. Hum Genet. 1992 Sep-Oct;90(1-2):7-11. [Article]
  51. Schuster V, Mingers AM, Seidenspinner S, Nussgens Z, Pukrop T, Kreth HW: Homozygous mutations in the plasminogen gene of two unrelated girls with ligneous conjunctivitis. Blood. 1997 Aug 1;90(3):958-66. [Article]
  52. Higuchi Y, Furihata K, Ueno I, Ishikawa S, Okumura N, Tozuka M, Sakurai N: Plasminogen Kanagawa-I, a novel missense mutation, is caused by the amino acid substitution G732R. Br J Haematol. 1998 Dec;103(3):867-70. [Article]
  53. Schuster V, Seidenspinner S, Zeitler P, Escher C, Pleyer U, Bernauer W, Stiehm ER, Isenberg S, Seregard S, Olsson T, Mingers AM, Schambeck C, Kreth HW: Compound-heterozygous mutations in the plasminogen gene predispose to the development of ligneous conjunctivitis. Blood. 1999 May 15;93(10):3457-66. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Tranexamic acidapprovedyestargetinhibitorDetails
Aminocaproic acidapproved, investigationalyestargetinhibitorDetails
Urokinaseapproved, investigational, withdrawnyestargetactivatorDetails
BicineexperimentalyestargetinhibitorDetails
Streptokinaseapproved, investigationalyestargetactivatorDetails
DesmoteplaseinvestigationalunknowntargetDetails
Aprotininapproved, investigational, withdrawnyestargetDetails
TenecteplaseapprovedyestargetactivatorDetails
Alteplaseapproved, investigationalyestargetactivatorDetails
AnistreplaseapprovedyestargetactivatorDetails
Reteplaseapproved, investigationalyestargetactivatorDetails
GabexateinvestigationalyestargetinhibitorDetails
Copperapproved, investigationalunknowntargetDetails
2-(2-Hydroxy-Phenyl)-1h-Indole-5-CarboxamidineexperimentalyestargetinhibitorDetails
Ranolazineapproved, investigationalyestargetmodulatorDetails
MelagatranexperimentalyestargetinhibitorDetails