Sequence of TRYD_HUMAN
EC Number:3.4.21.59
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Preferential cleavage: Arg-/-, Lys-/-, but with more restricted specificity than trypsin
Other sequences found for EC No. 3.4.21.59
General information:
Sequence
0 MLLLAPQMLS LLLLALPVLA SPAYVAPAPG QALQQTGIVG GQEAPRSKWP WQVSLRVRGP
60 YWMHFCGGSL IHPQWVLTAA HCVEPDIKDL AALRVQLREQ HLYYQDQLLP VSRIIVHPQF
120 YIIQTGADIA LLELEEPVNI SSHIHTVTLP PASETFPPGM PCWVTGWGDV DNNVHLPPPY
180 PLKEVEVPVV ENHLCNAEYH TGLHTGHSFQ IVRDDMLCAG SENHDSCQGD SGGPLVCKVN
240 GT
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
112437
Pallaoro M.,Fejzo M.S.,Shayesteh L.,Blount J.L.,Caughey G.H.
Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3.
J. Biol. Chem.
274
3355-3362
1999
112438
Min H.-K.,Kambe N.,Schwartz L.B.
Human mouse mast cell protease 7-like tryptase genes are pseudogenes.
J. Allergy Clin. Immunol.
107
315-321
2001
112439
Daniels R.J.,Peden J.F.,Lloyd C.,Horsley S.W.,Clark K.,Tufarelli C.,Kearney L.,Buckle V.J.,Doggett N.A.,Flint J.,Higgs D.R.
Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16.
Hum. Mol. Genet.
10
339-352
2001
112440
Martin J.,Han C.,Gordon L.A.,Terry A.,Prabhakar S.,She X.,Xie G.,Hellsten U.,Chan Y.M.,Altherr M.,Couronne O.,Aerts A.,Bajorek E.,Black S.,Blumer H.,Branscomb E.,Brown N.C.,Bruno W.J.,Buckingham J.M.,Callen D.F.,Campbell C.S.,Campbell M.L.,Campbell E.W.,Caoile C.,Challacombe J.F.,Chasteen L.A.,Chertkov O.,Chi H.C.,Christensen M.,Clark L.M.,Cohn J.D.,Denys M.,Detter J.C.,Dickson M.,Dimitrijevic-Bussod M.,Escobar J.,Fawcett J.J.,Flowers D.,Fotopulos D.,Glavina T.,Gomez M.,Gonzales E.,Goodstein D.,Goodwin L.A.,Grady D.L.,Grigoriev I.,Groza M.,Hammon N.,Hawkins T.,Haydu L.,Hildebrand C.E.,Huang W.,Israni S.,Jett J.,Jewett P.B.,Kadner K.,Kimball H.,Kobayashi A.,Krawczyk M.-C.,Leyba T.,Longmire J.L.,Lopez F.,Lou Y.,Lowry S.,Ludeman T.,Manohar C.F.,Mark G.A.,McMurray K.L.,Meincke L.J.,Morgan J.,Moyzis R.K.,Mundt M.O.,Munk A.C.,Nandkeshwar R.D.,Pitluck S.,Pollard M.,Predki P.,Parson-Quintana B.,Ramirez L.,Rash S.,Retterer J.,Ricke D.O.,Robinson D.L.,Rodriguez A.,Salamov A.,Saunders E.H.,Scott D.,Shough T.,Stallings R.L.,Stalvey M.,Sutherland R.D.,Tapia R.,Tesmer J.G.,Thayer N.,Thompson L.S.,Tice H.,Torney D.C.,Tran-Gyamfi M.,Tsai M.,Ulanovsky L.E.,Ustaszewska A.,Vo N.,White P.S.,Williams A.L.,Wills P.L.,Wu J.-R.,Wu K.,Yang J.,DeJong P.,Bruce D.,Doggett N.A.,Deaven L.,Schmutz J.,Grimwood J.,Richardson P.,Rokhsar D.S.,Eichler E.E.,Gilna P.,Lucas S.M.,Myers R.M.,Rubin E.M.,Pennacchio L.A.
The sequence and analysis of duplication-rich human chromosome 16.
Nature
432
988-994
2004
112441
Jackson N.E.,Wang H.W.,Bryant K.J.,McNeil H.P.,Husain A.,Liu K.,Tedla N.,Thomas P.S.,King G.C.,Hettiaratchi A.,Cairns J.,Hunt J.E.
Alternate mRNA splicing in multiple human tryptase genes is predicted to regulate tetramer formation.
J. Biol. Chem.
283
34178-34187
2008
112442
Wang H.-W.,McNeil H.P.,Husain A.,Liu K.,Tedla N.,Thomas P.S.,Raftery M.,King G.C.,Cai Z.Y.,Hunt J.E.
Delta tryptase is expressed in multiple human tissues, and a recombinant form has proteolytic activity.
J. Immunol.
169
5145-5152
2002
