Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs.

true 1988-08-01 2008-07-22 109 CATB_HUMAN Cathepsin B Cathepsin B1 APP secretase APPS Cathepsin B light chain Cathepsin B heavy chain Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. Chan S.J. San Segundo B. McCormick M.B. Steiner D.F. 1986 Proc. Natl. Acad. Sci. U.S.A. 83 7721-7725 NUCLEOTIDE SEQUENCE [MRNA] VARIANT VAL-26 Human gastric adenocarcinoma cathepsin B: isolation and sequencing of full-length cDNAs and polymorphisms of the gene. Cao L. Taggart R.T. Berquin I.M. Moin K. Fong D. Sloane B.F. doi:10.1016/0378-1119(94)90750-1 1994 Gene 139 163-169 NUCLEOTIDE SEQUENCE [MRNA] Gastric carcinoma The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). The MGC Project Team doi:10.1101/gr.2596504 2004 Genome Res. 14 2121-2127 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT VAL-26 Brain Placenta Amino acid sequence of human liver cathepsin B. Ritonja A. Popovic T. Turk V. Wiedenmann K. Machleidt W. doi:10.1016/0014-5793(85)81136-4 1985 FEBS Lett. 181 169-172 PROTEIN SEQUENCE OF 80-126 AND 129-333 Liver Human tumour cathepsin B. Comparison with normal liver cathepsin B. Moin K. Day N.A. Sameni M. Hasnain S. Hirama T. Sloane B.F. 1992 Biochem. J. 285 427-434 PROTEIN SEQUENCE OF 80-91 AND 129-139 Liver Isolation of a cDNA clone for the human lysosomal proteinase cathepsin B. Fong D. Calhoun D.H. Hsieh W.-T. Lee B. Wells R.D. 1986 Proc. Natl. Acad. Sci. U.S.A. 83 2909-2913 NUCLEOTIDE SEQUENCE [MRNA] OF 131-339 Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. Basrur V. Yang F. Kushimoto T. Higashimoto Y. Yasumoto K. Valencia J. Muller J. Vieira W.D. Watabe H. Shabanowitz J. Hearing V.J. Hunt D.F. Appella E. doi:10.1021/pr025562r 2003 J. Proteome Res. 2 69-79 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] MASS SPECTROMETRY Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. Chi A. Valencia J.C. Hu Z.-Z. Watabe H. Yamaguchi H. Mangini N.J. Huang H. Canfield V.A. Cheng K.C. Yang F. Abe R. Yamagishi S. Shabanowitz J. Hearing V.J. Wu C. Appella E. Hunt D.F. doi:10.1021/pr060363j 2006 J. Proteome Res. 5 3135-3144 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] MASS SPECTROMETRY The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. Musil D. Zucic D. Turk D. Engh R.A. Mayr I. Huber R. Popovic T. Turk V. Towatari T. Katunuma N. Bode W. 1991 EMBO J. 10 2321-2330 X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) Crystal structures of human procathepsin B at 3.2- and 3.3-A resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. Turk D. Podobnik M. Kuhelj R. Dolinar M. Turk V. doi:10.1016/0014-5793(96)00309-2 1996 FEBS Lett. 384 211-214 X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) Crystal structure of the wild-type human procathepsin B at 2.5-A resolution reveals the native active site of a papain-like cysteine protease zymogen. Podobnik M. Kuhelj R. Turk V. Turk D. doi:10.1006/jmbi.1997.1218 1997 J. Mol. Biol. 271 774-788 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) CTSB CPSB Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. Dimer of a heavy chain and a light chain cross-linked by a disulfide bond. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Belongs to the peptidase C1 family. 1 17 Activation peptide 18 79 Cathepsin B 80 333 Cathepsin B light chain 80 126 Cathepsin B heavy chain 129 333 334 339 108 108 278 278 298 298 N-linked (GlcNAc...) 192 192 93 93 122 122 105 105 150 150 141 141 207 207 142 142 146 146 179 179 211 211 187 187 198 198 V 26 26 N 235 235 G 53 53 AA sequence D 228 228 86 89 94 96 104 106 108 123 135 141 144 146 155 164 178 180 188 191 219 222 226 231 236 246 249 256 257 260 264 267 274 288 291 297 309 313 318 320 321 324 326 330 EMBL EMBL EMBL EMBL EMBL PIR A26498 RefSeq RefSeq RefSeq RefSeq RefSeq UniGene PDB 2.00 A/D=80-126 B/E=129-333 PDB 1.90 A/B/C=79-339 PDB 2.10 A/C=80-126 B/D=129-333 PDB 3.20 A=18-333 PDB 2.15 A=80-126 B=129-333 PDB 3.30 A=18-333 PDB 2.50 A=18-333 PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum SMR 18-333 MEROPS PhosphoSite SWISS-2DPAGE PeptideAtlas Ensembl Homo sapiens GeneID KEGG H-InvDB HGNC CTSB HPA MIM gene PharmGKB HOGENOM HOVERGEN LinkHub ArrayExpress CleanEx GermOnline Homo sapiens InterPro Pept_cys_AS InterPro Peptidase_C1A InterPro Peptidase_C1A_C InterPro Peptidase_C1A_cathepsin-B InterPro Propeptide_C1A PANTHER CathepsinB_like 1 PANTHER Peptidase_C1A 1 Pfam Peptidase_C1 1 Pfam Propeptide_C1 1 PRINTS PAPAIN ProDom Peptidase_C1 1 SMART Pept_C1 1 PROSITE THIOL_PROTEASE_ASN 1 PROSITE THIOL_PROTEASE_CYS 1 PROSITE THIOL_PROTEASE_HIS 1 ProtInc ProtInc UniProtKB ProtInc UniProtKB 2005-06-21 3 true 37822 MWQLWASLCC LLVLANARSR PSFHPLSDEL VNYVNKRNTT WQAGHNFYNV DMSYLKRLCG TFLGGPKPPQ RVMFTEDLKL PASFDAREQW PQCPTIKEIR DQGSCGSCWA FGAVEAISDR ICIHTNAHVS VEVSAEDLLT CCGSMCGDGC NGGYPAEAWN FWTRKGLVSG GLYESHVGCR PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSEKDIM AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI