Resource Batimastat

Predicate	Value (sorted: default)
rdfs:label	"Batimastat"
rdf:type	drugbank:drugs
drugbank:description	" 130370-60-4 experimental An anticancer drug that belongs to the family of drugs called angiogenesis inhibitors. Batimastat is a matrix metalloproteinase inhibitor. This compound belongs to the n-acyl-alpha amino acids and derivatives. These are compounds containing an alpha amino acid (or a derivative thereof) which bears an acyl group at his terminal nitrogen atom. N-acyl-alpha Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Alpha Amino Acid Amides N-acyl Amines Phenylpropylamines Amphetamines and Derivatives Thiophenes Hydroxamic Acids Secondary Carboxylic Acid Amides Carboxylic Acids Enolates Polyamines Thioethers amphetamine or derivative phenylpropylamine benzene thiophene carboxamide group hydroxamic acid secondary carboxylic acid amide thioether polyamine carboxylic acid enolate amine organonitrogen compound BB94 Antineoplastic Agents Protease Inhibitors Humans and other mammals logP 3.23 ALOGPS logS -5.4 ALOGPS Water Solubility 1.73e-03 g/l ALOGPS logP 3.27 ChemAxon IUPAC Name (2R,3S)-N-hydroxy-N'-[(1S)-1-(methylcarbamoyl)-2-phenylethyl]-2-(2-methylpropyl)-3-[(thiophen-2-ylsulfanyl)methyl]butanediamide ChemAxon Traditional IUPAC Name (2R,3S)-N-hydroxy-N'-[(1S)-1-(methylcarbamoyl)-2-phenylethyl]-2-(2-methylpropyl)-3-[(thiophen-2-ylsulfanyl)methyl]butanediamide ChemAxon Molecular Weight 477.64 ChemAxon Monoisotopic Weight 477.175597875 ChemAxon SMILES [H][C@@](CC1=CC=CC=C1)(NC(=O)[C@]([H])(CC(C)C)[C@]([H])(CSC1=CC=CS1)C(=O)NO)C(=O)NC ChemAxon Molecular Formula C23H31N3O4S2 ChemAxon InChI InChI=1S/C23H31N3O4S2/c1-15(2)12-17(18(22(28)26-30)14-32-20-10-7-11-31-20)21(27)25-19(23(29)24-3)13-16-8-5-4-6-9-16/h4-11,15,17-19,30H,12-14H2,1-3H3,(H,24,29)(H,25,27)(H,26,28)/t17-,18+,19+/m1/s1 ChemAxon InChIKey InChIKey=XFILPEOLDIKJHX-QYZOEREBSA-N ChemAxon Polar Surface Area (PSA) 107.53 ChemAxon Refractivity 127.3 ChemAxon Polarizability 49.79 ChemAxon Rotatable Bond Count 12 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 8.86 ChemAxon pKa (strongest basic) -0.57 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5362422 PubChem Substance 46505727 KEGG Drug D03061 ChemSpider 4515033 PDB BAT BE0001182 Neutrophil collagenase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Neutrophil collagenase Involved in protease activity and collagen degradation Can degrade fibrillar type I, II, and III collagens MMP8 11q22.3 Cytoplasmic granule. Note=Stored in intracellular granules None 6.86 53413.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7175 GenAtlas MMP8 GeneCards MMP8 GenBank Gene Database J05556 GenBank Protein Database 180618 UniProtKB P22894 UniProt Accession MMP8_HUMAN EC 3.4.24.34 Matrix metalloproteinase-8 MMP-8 Neutrophil collagenase precursor PMNL collagenase PMNL-CL >Neutrophil collagenase precursor MFSLKTLPFLLLLHVQISKAFPVSSKEKNTKTVQDYLEKFYQLPSNQYQSTRKNGTNVIV EKLKEMQRFFGLNVTGKPNEETLDMMKKPRCGVPDSGGFMLTPGNPKWERTNLTYRIRNY TPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGIL AHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYA FRETSNYSLPQDDIDGIQAIYGLSSNPIQPTGPSTPKPCDPSLTFDAITTLRGEILFFKD RYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGYDILQG YPKDISNYGFPSSVQAIDAAVFYRSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGI ESKVDAVFQQEHFFHVFSGPRYYAFDLIAQRVTRVARGNKWLNCRYG >1404 bp ATGTTCTCCCTGAAGACGCTTCCATTTCTGCTCTTACTCCATGTGCAGATTTCCAAGGCC TTTCCTGTATCTTCTAAAGAGAAAAATACAAAAACTGTTCAGGACTACCTGGAAAAGTTC TACCAATTACCAAGCAACCAGTATCAGTCTACAAGGAAGAATGGCACTAATGTGATCGTT GAAAAGCTTAAAGAAATGCAGCGATTTTTTGGGTTGAATGTGACGGGGAAGCCAAATGAG GAAACTCTGGACATGATGAAAAAGCCTCGCTGTGGAGTGCCTGACAGTGGTGGTTTTATG TTAACCCCAGGAAACCCCAAGTGGGAACGCACTAACTTGACCTACAGGATTCGAAACTAT ACCCCACAGCTGTCAGAGGCTGAGGTAGAAAGAGCTATCAAGGATGCCTTTGAACTCTGG AGTGTTGCATCACCTCTCATCTTCACCAGGATCTCACAGGGAGAGGCAGATATCAACATT GCTTTTTACCAAAGAGATCACGGTGACAATTCTCCATTTGATGGACCCAATGGAATCCTT GCTCATGCCTTTCAGCCAGGCCAAGGTATTGGAGGAGATGCTCATTTTGATGCCGAAGAA ACATGGACCAACACCTCCGCAAATTACAACTTGTTTCTTGTTGCTGCTCATGAATTTGGC CATTCTTTGGGGCTCGCTCACTCCTCTGACCCTGGTGCCTTGATGTATCCCAACTATGCT TTCAGGGAAACCAGCAACTACTCACTCCCTCAAGATGACATCGATGGCATTCAGGCCATC TATGGACTTTCAAGCAACCCTATCCAACCTACTGGACCAAGCACACCCAAACCCTGTGAC CCCAGTTTGACATTTGATGCTATCACCACACTCCGTGGAGAAATACTTTTCTTTAAAGAC AGGTACTTCTGGAGAAGGCATCCTCAGCTACAAAGAGTCGAAATGAATTTTATTTCTCTA TTCTGGCCATCCCTTCCAACTGGTATACAGGCTGCTTATGAAGATTTTGACAGAGACCTC ATTTTCCTATTTAAAGGCAACCAATACTGGGCTCTGAGTGGCTATGATATTCTGCAAGGT TATCCCAAGGATATATCAAACTATGGCTTCCCCAGCAGCGTCCAAGCAATTGACGCAGCT GTTTTCTACAGAAGTAAAACATACTTCTTTGTAAATGACCAATTCTGGAGATATGATAAC CAAAGACAATTCATGGAGCCAGGTTATCCCAAAAGCATATCAGGTGCCTTTCCAGGAATA GAGAGTAAAGTTGATGCAGTTTTCCAGCAAGAACATTTCTTCCATGTCTTCAGTGGACCA AGATATTACGCATTTGATCTTATTGCTCAGAGAGTTACCAGAGTTGCAAGAGGCAATAAA TGGCTTAACTGTAGATATGGCTGA PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix (sensu Metazoa) component extracellular matrix function catalytic activity function hydrolase activity function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process BE0001198 Macrophage metalloelastase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Macrophage metalloelastase Involved in protease activity May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3 MMP12 11q22.3 Cytoplasmic None 8.98 54002.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7158 GenAtlas MMP12 GeneCards MMP12 GenBank Gene Database L23808 GenBank Protein Database 435970 UniProtKB P39900 UniProt Accession MMP12_HUMAN EC 3.4.24.65 HME Macrophage elastase Macrophage metalloelastase precursor Matrix metalloproteinase-12 ME MMP-12 >Macrophage metalloelastase precursor MKFLLILLLQATASGALPLNSSTSLEKNNVLFGERYLEKFYGLEINKLPVTKMKYSGNLM KEKIQEMQHFLGLKVTGQLDTSTLEMMHAPRCGVPDVHHFREMPGGPVWRKHYITYRINN YTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGI LAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTY KYVDINTFRLSADDIRGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFF FKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNLRP EPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITK NFQGIGPKIDAVFYSKNKYYYFFQGSNQFEYDFLLQRITKTLKSNSWFGC >1413 bp ATGAAGTTTCTTCTAATACTGCTCCTGCAGGCCACTGCTTCTGGAGCTCTTCCCCTGAAC AGCTCTACAAGCCTGGAAAAAAATAATGTGCTATTTGGTGAGAGATACTTAGAAAAATTT TATGGCCTTGAGATAAACAAACTTCCAGTGACAAAAATGAAATATAGTGGAAACTTAATG AAGGAAAAAATCCAAGAAATGCAGCACTTCTTGGGTCTGAAAGTGACCGGGCAACTGGAC ACATCTACCCTGGAGATGATGCACGCACCTCGATGTGGAGTCCCCGATCTCCATCATTTC AGGGAAATGCCAGGGGGGCCCGTATGGAGGAAACATTATATCACCTACAGAATCAATAAT TACACACCTGACATGAACCGTGAGGATGTTGACTACGCAATCCGGAAAGCTTTCCAAGTA TGGAGTAATGTTACCCCCTTGAAATTCAGCAAGATTAACACAGGCATGGCTGACATTTTG GTGGTTTTTGCCCGTGGAGCTCATGGAGACTTCCATGCTTTTGATGGCAAAGGTGGAATC CTAGCCCATGCTTTTGGACCTGGATCTGGCATTGGAGGGGATGCACATTTCGATGAGGAC GAATTCTGGACTACACATTCAGGAGGCACAAACTTGTTCCTCACTGCTGTTCACGAGATT GGCCATTCCTTAGGTCTTGGCCATTCTAGTGATCCAAAGGCTGTAATGTTCCCCACCTAC AAATATGTCGACATCAACACATTTCGCCTCTCTGCTGATGACATACGTGGCATTCAGTCC CTGTATGGAGACCCAAAAGAGAACCAACGCTTGCCAAATCCTGACAATTCAGAACCAGCT CTCTGTGACCCCAATTTGAGTTTTGATGCTGTCACTACCGTGGGAAATAAGATCTTTTTC TTCAAAGACAGGTTCTTCTGGCTGAAGGTTTCTGAGAGACCAAAGACCAGTGTTAATTTA ATTTCTTCCTTATGGCCAACCTTGCCATCTGGCATTGAAGCTGCTTATGAAATTGAAGCC AGAAATCAAGTTTTTCTTTTTAAAGATGACAAATACTGGTTAATTAGCAATTTAAGACCA GAGCCAAATTATCCCAAGAGCATACATTCTTTTGGTTTTCCTAACTTTGTGAAAAAAATT GATGCAGCTGTTTTTAACCCACGTTTTTATAGGACCTACTTCTTTGTAGATAACCAGTAT TGGAGGTATGATGAAAGGAGACAGATGATGGACCCTGGTTATCCCAAACTGATTACCAAG AACTTCCAAGGAATCGGGCCTAAAATTGATGCAGTCTTCTATTCTAAAAACAAATACTAC TATTTCTTCCAAGGATCTAACCAATTTGAATATGACTTCCTACTCCAACGTATCACCAAA ACACTGAAAAGCAATAGCTGGTTTGGTTGTTAG PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix component extracellular matrix (sensu Metazoa) function catalytic activity function hydrolase activity function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process BE0001637 Matrix metalloproteinase-16 Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Matrix metalloproteinase-16 Involved in protease activity Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. The short isoform cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells MMP16 8q21 Isoform Long:Cell membrane; single-pass type I membrane protein (Potential). Isoform Short:Secreted 565-585 8.74 69522.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7162 GenAtlas MMP16 GeneCards MMP16 GenBank Gene Database AB009303 GenBank Protein Database 2662306 UniProtKB P51512 UniProt Accession MMP16_HUMAN EC 3.4.24.- Matrix metalloproteinase-16 precursor Membrane-type matrix metalloproteinase 3 Membrane-type-3 matrix metalloproteinase MMP- X2 MMP-16 MT-MMP 3 MT3-MMP MT3MMP MTMMP3 >Matrix metalloproteinase-16 precursor MILLTFSTGRRLDFVHHSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRM SVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFHIRRKRY ALTGQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKR DVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDL FLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPT RPLPTVPPHRSIPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVF KDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQ PGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITVW KGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRVK EGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCK RSMQEWV >1824 bp ATGATCTTACTCACATTCAGCACTGGAAGACGGTTGGATTTCGTGCATCATTCGGGGGTG TTTTTCTTGCAAACCTTGCTTTGGATTTTATGTGCTACAGTCTGCGGAACGGAGCAGTAT TTCAATGTGGAGGTTTGGTTACAAAAGTACGGCTACCTTCCACCGACTGACCCCAGAATG TCAGTGCTGCGCTCTGCAGAGACCATGCAGTCTGCCCTAGCTGCCATGCAGCAGTTCTAT GGCATTAACATGACAGGAAAAGTGGACAGAAACACAATTGACTGGATGAAGAAGCCCCGA TGCGGTGTACCTGACCAGACAAGAGGTAGCTCCAAATTTCATATTCGTCGAAAGCGATAT GCATTGACAGGACAGAAATGGCAGCACAAGCACATCACTTACAGTATAAAGAACGTAACT CCAAAAGTAGGAGACCCTGAGACTCGTAAAGCTATTCGCCGTGCCTTTGATGTGTGGCAG AATGTAACTCCTCTGACATTTGAAGAAGTTCCCTACAGTGAATTAGAAAATGGCAAACGT GATGTGGATATAACCATTATTTTTGCATCTGGTTTCCATGGGGACAGCTCTCCCTTTGAT GGAGAGGGAGGATTTTTGGCACATGCCTACTTCCCTGGACCAGGAATTGGAGGAGATACC CATTTTGACTCAGATGAGCCATGGACACTAGGAAATCCTAATCATGATGGAAATGACTTA TTTCTTGTAGCAGTCCATGAACTGGGACATGCTCTGGGATTGGAGCATTCCAATGACCCC ACTGCCATCATGGCTCCATTTTACCAGTACATGGAAACAGACAACTTCAAACTACCTAAT GATGATTTACAGGGCATCCAGAAAATATATGGTCCACCTGACAAGATTCCTCCACCTACA AGACCTCTACCGACAGTGCCCCCACACCGCTCTATTCCTCCGGCTGACCCAAGGAAAAAT GACAGGCCAAAACCTCCTCGGCCTCCAACCGGCAGACCCTCCTATCCCGGAGCCAAACCC AACATCTGTGATGGGAACTTTAACACTCTAGCTATTCTTCGTCGTGAGATGTTTGTTTTC AAGGACCAGTGGTTTTGGCGAGTGAGAAACAACAGGGTGATGGATGGATACCCAATGCAA ATTACTTACTTCTGGCGGGGCTTGCCTCCTAGTATCGATGCAGTTTATGAAAATAGCGAC GGGAATTTTGTGTTCTTTAAAGGTAACAAATATTGGGTGTTCAAGGATACAACTCTTCAA CCTGGTTACCCTCATGACTTGATAACCCTTGGAAGTGGAATTCCCCCTCATGGTATTGAT TCAGCCATTTGGTGGGAGGACGTCGGGAAAACCTATTTCTTCAAGGGAGACAGATATTGG AGATATAGTGAAGAAATGAAAACAATGGACCCTGGCTATCCCAAGCCAATCACAGTCTGG AAAGGGATCCCTGAATCTCCTCAGGGAGCATTTGTACACAAAGAAAATGGCTTTACGTAT TTCTACAAAGGAAAGGAGTATTGGAAATTCAACAACCAGATACTCAAGGTAGAACCTGGA CATCCAAGATCCATCCTCAAGGATTTTATGGGCTGTGATGGACCAACAGACAGAGTTAAA GAAGGACACAGCCCACCAGATGATGTAGACATTGTCATCAAACTGGACAACACAGCCAGC ACTGTGAAAGCCATAGCTATTGTCATTCCCTGCATCTTGGCCTTATGCCTCCTTGTATTG GTTTACACTGTGTTCCAGTTCAAGAGGAAAGGAACACCCCGCCACATACTGTACTGTAAA CGCTCTATGCAAGAGTGGGTGTGA PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix component extracellular matrix (sensu Metazoa) function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding function catalytic activity function hydrolase activity process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism BE0003872 Disintegrin and metalloproteinase domain-containing protein 28 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Disintegrin and metalloproteinase domain-containing protein 28 Involved in metalloendopeptidase activity May play a role in the adhesive and proteolytic events that occur during lymphocyte emigration or may function in ectodomain shedding of lymphocyte surface target proteins, such as FASL and CD40L. May be involved in sperm maturation ADAM28 8p21.2 Isoform 2:Secreted 666-686 6.8 87180.0 Human HUGO Gene Nomenclature Committee (HGNC) GNC:206 GeneCards ADAM28 GenBank Gene Database AF137334 GenBank Protein Database 4583505 UniProtKB Q9UKQ2 UniProt Accession ADA28_HUMAN ADAM 28 eMDC II Epididymial metalloproteinase-like, disintegrin-like, and cysteine-rich protein II MDC-L Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L >Disintegrin and metalloproteinase domain-containing protein 28 MLQGLLPVSLLLSVAVSAIKELPGVKKYEVVYPIRLHPLHKREAKEPEQQEQFETELKYK MTINGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYYQGHILNEKVSDAS ISTCRGLRGYFSQGDQRYFIEPLSPIHRDGQEHALFKYNPDEKNYDSTCGMDGVLWAHDL QQNIALPATKLVKLKDRKVQEHEKYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNM LYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATE LAGTTVGLAFMSTMCSPYSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYSCKCPSTI CVMDKALSFYIPTDFSSCSRLSYDKFFEDKLSNCLFNAPLPTDIISTPICGNQLVEMGED CDCGTSEECTNICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNG KSGNCPDDRFQVNGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNRNEGGSK YGYCRRVDDTLIPCKANDTMCGKLFCQGGSDNLPWKGRIVTFLTCKTFDPEDTSQEIGMV ANGTKCGDNKVCINAECVDIEKAYKSTNCSSKCKGHAVCDHELQCQCEEGWIPPDCDDSS VVFHFSIVVGVLFPMAVIFVVVAMVIRHQSSREKQKKDQRPLSTTGTRPHKQKRKPQMVK AVQPQEMSQMKPHVYDLPVEGNEPPASFHKDTNALPPTVFKDNPMSTPKDSNPEA >2328 bp ATGTTGCAAGGTCTCCTGCCAGTCAGTCTCCTCCTCTCTGTTGCAGTAAGTGCTATAAAA GAACTCCCTGGGGTGAAGAAGTATGAAGTGGTTTATCCTATAAGACTTCATCCACTGCAT AAAAGAGAGGCCAAAGAGCCAGAGCAACAGGAACAATTTGAAACTGAATTAAAGTATAAA ATGACAATTAATGGAAAAATTGCAGTGCTTTATTTGAAAAAAAACAAGAACCTCCTTGCA CCAGGCTACACGGAAACATATTATAATTCCACTGGAAAGGAGATCACCACAAGCCCACAA ATTATGGATGATTGTTATTATCAAGGACATATTCTTAATGAAAAGGTTTCTGACGCTAGC ATCAGCACATGTAGGGGTCTAAGGGGCTACTTCAGTCAGGGGGATCAAAGATACTTTATT GAACCTTTAAGCCCCATACATCGGGATGGACAGGAGCATGCACTCTTCAAGTATAACCCT GATGAAAAGAATTATGACAGCACCTGTGGGATGGATGGTGTGTTGTGGGCCCACGATTTG CAGCAGAACATTGCCCTACCTGCCACCAAACTAGTAAAATTGAAAGACAGGAAGGTTCAG GAACATGAGAAATACATAGAATATTATCTGGTCCTGGATAATGGTGAGTTTAAAAGGTAC AATGAGAATCAAGATGAGATCAGAAAGAGGGTATTTGAGATGGCTAATTATGTCAACATG CTTTATAAAAAGCTCAATACTCATGTGGCCTTAGTTGGTATGGAAATCTGGACTGACAAG GATAAGATAAAGATAACCCCAAATGCAAGCTTCACCTTGGAGAATTTTTCTAAATGGAGG GGGAGTGTTCTCTCAAGAAGAAAGCGTCATGATATTGCTCAGTTAATCACAGCAACAGAA CTTGCTGGAACGACTGTGGGTCTTGCATTTATGTCTACAATGTGTTCTCCTTATTCTGTT GGCGTTGTTCAGGACCACAGCGATAATCTTCTTAGAGTTGCAGGGACAATGGCACATGAA ATGGGCCACAACTTTGGAATGTTTCATGACGACTATTCTTGCAAGTGTCCTTCTACAATA TGTGTGATGGACAAAGCACTGAGCTTCTATATACCCACAGACTTCAGTTCCTGCAGCCGT CTCAGCTATGACAAGTTTTTTGAAGATAAATTATCAAATTGCCTCTTTAATGCTCCATTG CCTACAGATATCATATCCACTCCAATTTGTGGGAACCAGTTGGTGGAAATGGGAGAGGAC TGTGATTGTGGGACATCTGAGGAATGTACCAATATTTGCTGTGATGCTAAGACATGTAAA ATCAAAGCAACTTTTCAATGTGCATTAGGAGAATGTTGTGAAAAATGCCAATTTAAAAAG GCTGGGATGGTGTGCAGACCAGCAAAAGATGAGTGCGACCTGCCTGAAATGTGTAATGGT AAATCTGGTAATTGTCCTGATGATAGATTCCAAGTCAATGGCTTCCCTTGCCATCACGGG AAGGGCCACTGCTTGATGGGCACATGCCCCACACTGCGGGAGCAGTGCACAGAGCTGTGG GGACCAGGAACTGAGGTTGCAGATAAGTCATGTTACAACAGGAATGAAGGTGGGTCAAAG TACGGGTACTGTCGCAGAGTGGATGACACACTCATTCCCTGCAAAGCAAATGATACCATG TGTGGGAAGTTGTTCTGTCAAGGTGGGTCGGATAATTTGCCCTGGAAAGGACGGATAGTG ACTTTCCTGACATGTAAAACATTTGATCCTGAAGACACAAGTCAAGAAATAGGCATGGTG GCCAATGGAACTAAGTGTGGCGATAACAAGGTTTGCATTAATGCAGAATGTGTGGATATT GAGAAAGCCTACAAATCAACCAATTGCTCATCCAAGTGCAAAGGACATGCTGTGTGTGAC CATGAGCTCCAGTGTCAATGTGAGGAAGGATGGATCCCTCCCGACTGCGATGACTCCTCA GTGGTCTTCCACTTCTCCATTGTGGTTGGGGTGCTGTTCCCAATGGCGGTCATTTTTGTG GTGGTTGCTATGGTAATCCGGCACCAGAGCTCCAGAGAAAAGCAGAAGAAAGATCAGAGG CCACTATCTACCACTGGCACCAGGCCACACAAACAGAAGAGGAAACCCCAGATGGTAAAG GCTGTTCAACCCCAAGAGATGAGTCAGATGAAGCCCCATGTGTATGATCTGCCAGTAGAA GGCAATGAGCCCCCAGCCTCTTTTCATAAAGACACAAACGCACTTCCCCCTACTGTTTTC AAGGATAATCCAATGTCTACACCTAAGGACTCAAATCCAGAAGCATGA PF01562 Pep_M12B_propep PF01421 Reprolysin PF00200 Disintegrin PF08516 ADAM_CR component extracellular matrix component extracellular matrix (sensu Metazoa) function catalytic activity function peptidase activity function hydrolase activity function endopeptidase activity function ion binding function metallopeptidase activity function cation binding function metalloendopeptidase activity function transition metal ion binding function zinc ion binding function binding process protein metabolism process cellular protein metabolism process metabolism process macromolecule metabolism process proteolysis process physiological process BE0003730 A disintegrin and metalloproteinase with thrombospondin motifs 5 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown A disintegrin and metalloproteinase with thrombospondin motifs 5 Involved in integrin binding Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period ADAMTS5 21q21.3 Secreted, extracellular space, extracellular matrix (By similarity) None 9.01 101714.9 Human HUGO Gene Nomenclature Committee (HGNC) GNC:221 GeneCards ADAMTS5 GenBank Gene Database AF142099 GenBank Protein Database 5733438 UniProtKB Q9UNA0 UniProt Accession ATS5_HUMAN A disintegrin and metalloproteinase with thrombospondin motifs 11 ADAM-TS 11 ADAM-TS 5 ADAM-TS5 ADAMTS-11 ADAMTS-5 ADMP-2 Aggrecanase-2 >A disintegrin and metalloproteinase with thrombospondin motifs 5 MLLGWASLLLCAFRLPLAAVGPAATPAQDKAGQPPTAAAAAQPRRRQGEEVQERAEPPGH PHPLAQRRRSKGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDGSVGIAGFVPAGGGT SAPWRHRSHCFYRGTVDASPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEKGR VYGDGSARILHVYTREGFSFEALPPRASCETPASTPEAHEHAPAHSNPSGRAALASQLLD QSALSPAGGSGPQTWWRRRRRSISRARQVELLLVADASMARLYGRGLQHYLLTLASIANR LYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYD AAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSH DDSKFCEETFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQI LGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGT PCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPR NNGRYCTGKRAIYRSCSLMPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVL PADVCKLTCRAKGTGYYVVFSPKVTDGTECRPYSNSVCVRGKCVRTGCDGIIGSKLQYDK CGVCGGDNSSCTKIVGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKK NGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPT KPLDVRYSFFVPKKSTPKVNSVTSHGSNKVGSHTSQPQWVTGPWLACSRTCDTGWHTRTV QCQDGNRKLAKGCPLSQRPSAFKQCLLKKC >2793 bp ATGCTGCTCGGGTGGGCGTCCCTGCTGCTGTGCGCGTTCCGCCTGCCCCTGGCCGCGGTC GGCCCCGCCGCGACACCTGCCCAGGATAAAGCCGGGCAGCCTCCGACTGCTGCAGCAGCC GCCCAGCCCCGCCGGCGGCAGGGGGAGGAGGTGCAGGAGCGAGCCGAGCCTCCCGGCCAC CCGCACCCCCTGGCGCAGCGGCGCAGGAGCAAGGGGCTGGTGCAGAACATCGACCAACTC TACTCCGGCGGCGGCAAGGTGGGCTACCTCGTCTACGCGGGCGGCCGGAGGTTCCTCTTG GACCTGGAGCGAGATGGTTCGGTGGGCATTGCTGGCTTCGTGCCCGCAGGAGGCGGGACG AGTGCGCCCTGGCGCCACCGGAGCCACTGCTTCTATCGGGGCACAGTGGACGCTAGTCCC CGCTCTCTGGCTGTCTTTGACCTCTGTGGGGGTCTCGACGGCTTCTTCGCGGTCAAGCAC GCGCGCTACACCCTAAAGCCACTGCTGCGCGGACCCTGGGCGGAGGAAGAAAAGGGGCGC GTGTACGGGGATGGGTCCGCACGGATCCTGCACGTCTACACCCGCGAGGGCTTCAGCTTC GAGGCCCTGCCGCCGCGCGCCAGCTGCGAAACCCCCGCGTCCACACCGGAGGCCCACGAG CATGCTCCGGCGCACAGCAACCCGAGCGGACGCGCAGCACTGGCCTCGCAGCTCTTGGAC CAGTCCGCTCTCTCGCCCGCTGGGGGCTCAGGACCGCAGACGTGGTGGCGGCGGCGGCGC CGCTCCATCTCCCGGGCCCGCCAGGTGGAGCTGCTTCTGGTGGCTGACGCGTCCATGGCG CGGTTGTATGGCCGGGGCCTGCAGCATTACCTGCTGACCCTGGCCTCCATCGCCAATAGG CTGTACAGCCATGCTAGCATCGAGAACCACATCCGCCTGGCCGTGGTGAAGGTGGTGGTG CTAGGCGACAAGGACAAGAGCCTGGAAGTGAGCAAGAACGCTGCCACCACACTCAAGAAC TTTTGCAAGTGGCAGCACCAACACAACCAGCTGGGAGATGACCATGAGGAGCACTACGAT GCAGCTATCCTGTTTACTCGGGAGGATTTATGTGGGCATCATTCATGTGACACCCTGGGA ATGGCAGACGTTGGGACCATATGTTCTCCAGAGCGCAGCTGTGCTGTGATTGAAGACGAT GGCCTCCACGCAGCCTTCACTGTGGCTCACGAAATCGGACATTTACTTGGCCTCTCCCAT GACGATTCCAAATTCTGTGAAGAGACCTTTGGTTCCACAGAAGATAAGCGCTTAATGTCT TCCATCCTTACCAGCATTGATGCATCTAAGCCCTGGTCCAAATGCACTTCAGCCACCATC ACAGAATTCCTGGATGATGGCCATGGTAACTGTTTGCTGGACCTACCACGAAAGCAGATC CTGGGCCCCGAAGAACTCCCAGGACAGACCTACGATGCCACCCAGCAGTGCAACCTGACA TTCGGGCCTGAGTACTCCGTGTGTCCCGGCATGGATGTCTGTGCTCGCCTGTGGTGTGCT GTGGTACGCCAGGGCCAGATGGTCTGTCTGACCAAGAAGCTGCCTGCGGTGGAAGGGACG CCTTGTGGAAAGGGGAGAATCTGCCTGCAGGGCAAATGTGTGGACAAAACCAAGAAAAAA TATTATTCAACGTCAAGCCATGGCAACTGGGGATCTTGGGGATCCTGGGGCCAGTGTTCT CGCTCATGTGGAGGAGGAGTGCAGTTTGCCTATCGTCACTGTAATAACCCTGCTCCCAGA AACAACGGACGCTACTGCACAGGGAAGAGGGCCATCTACCGCTCCTGCAGTCTCATGCCC TGCCCACCCAATGGTAAATCATTTCGTCATGAACAGTGTGAGGCCAAAAATGGCTATCAG TCTGATGCAAAAGGAGTCAAAACTTTTGTGGAATGGGTTCCCAAATATGCAGGTGTCCTG CCAGCGGATGTGTGCAAGCTGACCTGCAGAGCCAAGGGCACTGGCTACTATGTGGTATTT TCTCCAAAGGTGACCGATGGCACTGAATGTAGGCCGTACAGTAATTCCGTCTGCGTCCGG GGGAAGTGTGTGAGAACTGGCTGTGACGGCATCATTGGCTCAAAGCTGCAGTATGACAAG TGCGGAGTATGTGGAGGAGACAACTCCAGCTGTACAAAGATTGTTGGAACCTTTAATAAG AAAAGTAAGGGTTACACTGACGTGGTGAGGATTCCTGAAGGGGCAACCCACATAAAAGTT CGACAGTTCAAAGCCAAAGACCAGACTAGATTCACTGCCTATTTAGCCCTGAAAAAGAAA AACGGTGAGTACCTTATCAATGGAAAGTACATGATCTCCACTTCAGAGACTATCATTGAC ATCAATGGAACAGTCATGAACTATAGCGGTTGGAGCCACAGGGATGACTTCCTGCATGGC ATGGGCTACTCTGCCACGAAGGAAATTCTAATAGTGCAGATTCTTGCAACAGACCCCACT AAACCATTAGATGTCCGTTATAGCTTTTTTGTTCCCAAGAAGTCCACTCCAAAAGTAAAC TCTGTCACTAGTCATGGCAGCAATAAAGTGGGATCACACACTTCGCAGCCGCAGTGGGTC ACGGGCCCATGGCTCGCCTGCTCTAGGACCTGTGACACAGGTTGGCACACCAGAACGGTG CAGTGCCAGGATGGAAACCGGAAGTTAGCAAAAGGATGTCCTCTCTCCCAAAGGCCTTCT GCGTTTAAGCAATGCTTGTTGAAGAAATGTTAG PF00090 TSP_1 PF01562 Pep_M12B_propep PF01421 Reprolysin PF05986 ADAM_spacer1 component extracellular matrix function catalytic activity function peptidase activity function endopeptidase activity function hydrolase activity function metallopeptidase activity function ion binding function metalloendopeptidase activity function cation binding function transition metal ion binding function zinc ion binding function binding process metabolism process proteolysis process macromolecule metabolism process protein metabolism process physiological process process cellular protein metabolism "
drugbank:drugCategory	drugcategory:Antineoplastic Agents drugcategory:Protease Inhibitors
owl:sameAs	drug:EXPT00627

"Batimastat"

" 130370-60-4 experimental An anticancer drug that belongs to the family of drugs called angiogenesis inhibitors. Batimastat is a matrix metalloproteinase inhibitor. This compound belongs to the n-acyl-alpha amino acids and derivatives. These are compounds containing an alpha amino acid (or a derivative thereof) which bears an acyl group at his terminal nitrogen atom. N-acyl-alpha Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Alpha Amino Acid Amides N-acyl Amines Phenylpropylamines Amphetamines and Derivatives Thiophenes Hydroxamic Acids Secondary Carboxylic Acid Amides Carboxylic Acids Enolates Polyamines Thioethers amphetamine or derivative phenylpropylamine benzene thiophene carboxamide group hydroxamic acid secondary carboxylic acid amide thioether polyamine carboxylic acid enolate amine organonitrogen compound BB94 Antineoplastic Agents Protease Inhibitors Humans and other mammals logP 3.23 ALOGPS logS -5.4 ALOGPS Water Solubility 1.73e-03 g/l ALOGPS logP 3.27 ChemAxon IUPAC Name (2R,3S)-N-hydroxy-N'-[(1S)-1-(methylcarbamoyl)-2-phenylethyl]-2-(2-methylpropyl)-3-[(thiophen-2-ylsulfanyl)methyl]butanediamide ChemAxon Traditional IUPAC Name (2R,3S)-N-hydroxy-N'-[(1S)-1-(methylcarbamoyl)-2-phenylethyl]-2-(2-methylpropyl)-3-[(thiophen-2-ylsulfanyl)methyl]butanediamide ChemAxon Molecular Weight 477.64 ChemAxon Monoisotopic Weight 477.175597875 ChemAxon SMILES [H][C@@](CC1=CC=CC=C1)(NC(=O)[C@]([H])(CC(C)C)[C@]([H])(CSC1=CC=CS1)C(=O)NO)C(=O)NC ChemAxon Molecular Formula C23H31N3O4S2 ChemAxon InChI InChI=1S/C23H31N3O4S2/c1-15(2)12-17(18(22(28)26-30)14-32-20-10-7-11-31-20)21(27)25-19(23(29)24-3)13-16-8-5-4-6-9-16/h4-11,15,17-19,30H,12-14H2,1-3H3,(H,24,29)(H,25,27)(H,26,28)/t17-,18+,19+/m1/s1 ChemAxon InChIKey InChIKey=XFILPEOLDIKJHX-QYZOEREBSA-N ChemAxon Polar Surface Area (PSA) 107.53 ChemAxon Refractivity 127.3 ChemAxon Polarizability 49.79 ChemAxon Rotatable Bond Count 12 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 8.86 ChemAxon pKa (strongest basic) -0.57 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5362422 PubChem Substance 46505727 KEGG Drug D03061 ChemSpider 4515033 PDB BAT BE0001182 Neutrophil collagenase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Neutrophil collagenase Involved in protease activity and collagen degradation Can degrade fibrillar type I, II, and III collagens MMP8 11q22.3 Cytoplasmic granule. Note=Stored in intracellular granules None 6.86 53413.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7175 GenAtlas MMP8 GeneCards MMP8 GenBank Gene Database J05556 GenBank Protein Database 180618 UniProtKB P22894 UniProt Accession MMP8_HUMAN EC 3.4.24.34 Matrix metalloproteinase-8 MMP-8 Neutrophil collagenase precursor PMNL collagenase PMNL-CL >Neutrophil collagenase precursor MFSLKTLPFLLLLHVQISKAFPVSSKEKNTKTVQDYLEKFYQLPSNQYQSTRKNGTNVIV EKLKEMQRFFGLNVTGKPNEETLDMMKKPRCGVPDSGGFMLTPGNPKWERTNLTYRIRNY TPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGIL AHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYA FRETSNYSLPQDDIDGIQAIYGLSSNPIQPTGPSTPKPCDPSLTFDAITTLRGEILFFKD RYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGYDILQG YPKDISNYGFPSSVQAIDAAVFYRSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGI ESKVDAVFQQEHFFHVFSGPRYYAFDLIAQRVTRVARGNKWLNCRYG >1404 bp ATGTTCTCCCTGAAGACGCTTCCATTTCTGCTCTTACTCCATGTGCAGATTTCCAAGGCC TTTCCTGTATCTTCTAAAGAGAAAAATACAAAAACTGTTCAGGACTACCTGGAAAAGTTC TACCAATTACCAAGCAACCAGTATCAGTCTACAAGGAAGAATGGCACTAATGTGATCGTT GAAAAGCTTAAAGAAATGCAGCGATTTTTTGGGTTGAATGTGACGGGGAAGCCAAATGAG GAAACTCTGGACATGATGAAAAAGCCTCGCTGTGGAGTGCCTGACAGTGGTGGTTTTATG TTAACCCCAGGAAACCCCAAGTGGGAACGCACTAACTTGACCTACAGGATTCGAAACTAT ACCCCACAGCTGTCAGAGGCTGAGGTAGAAAGAGCTATCAAGGATGCCTTTGAACTCTGG AGTGTTGCATCACCTCTCATCTTCACCAGGATCTCACAGGGAGAGGCAGATATCAACATT GCTTTTTACCAAAGAGATCACGGTGACAATTCTCCATTTGATGGACCCAATGGAATCCTT GCTCATGCCTTTCAGCCAGGCCAAGGTATTGGAGGAGATGCTCATTTTGATGCCGAAGAA ACATGGACCAACACCTCCGCAAATTACAACTTGTTTCTTGTTGCTGCTCATGAATTTGGC CATTCTTTGGGGCTCGCTCACTCCTCTGACCCTGGTGCCTTGATGTATCCCAACTATGCT TTCAGGGAAACCAGCAACTACTCACTCCCTCAAGATGACATCGATGGCATTCAGGCCATC TATGGACTTTCAAGCAACCCTATCCAACCTACTGGACCAAGCACACCCAAACCCTGTGAC CCCAGTTTGACATTTGATGCTATCACCACACTCCGTGGAGAAATACTTTTCTTTAAAGAC AGGTACTTCTGGAGAAGGCATCCTCAGCTACAAAGAGTCGAAATGAATTTTATTTCTCTA TTCTGGCCATCCCTTCCAACTGGTATACAGGCTGCTTATGAAGATTTTGACAGAGACCTC ATTTTCCTATTTAAAGGCAACCAATACTGGGCTCTGAGTGGCTATGATATTCTGCAAGGT TATCCCAAGGATATATCAAACTATGGCTTCCCCAGCAGCGTCCAAGCAATTGACGCAGCT GTTTTCTACAGAAGTAAAACATACTTCTTTGTAAATGACCAATTCTGGAGATATGATAAC CAAAGACAATTCATGGAGCCAGGTTATCCCAAAAGCATATCAGGTGCCTTTCCAGGAATA GAGAGTAAAGTTGATGCAGTTTTCCAGCAAGAACATTTCTTCCATGTCTTCAGTGGACCA AGATATTACGCATTTGATCTTATTGCTCAGAGAGTTACCAGAGTTGCAAGAGGCAATAAA TGGCTTAACTGTAGATATGGCTGA PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix (sensu Metazoa) component extracellular matrix function catalytic activity function hydrolase activity function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process BE0001198 Macrophage metalloelastase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Macrophage metalloelastase Involved in protease activity May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3 MMP12 11q22.3 Cytoplasmic None 8.98 54002.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7158 GenAtlas MMP12 GeneCards MMP12 GenBank Gene Database L23808 GenBank Protein Database 435970 UniProtKB P39900 UniProt Accession MMP12_HUMAN EC 3.4.24.65 HME Macrophage elastase Macrophage metalloelastase precursor Matrix metalloproteinase-12 ME MMP-12 >Macrophage metalloelastase precursor MKFLLILLLQATASGALPLNSSTSLEKNNVLFGERYLEKFYGLEINKLPVTKMKYSGNLM KEKIQEMQHFLGLKVTGQLDTSTLEMMHAPRCGVPDVHHFREMPGGPVWRKHYITYRINN YTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGI LAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTY KYVDINTFRLSADDIRGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFF FKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNLRP EPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITK NFQGIGPKIDAVFYSKNKYYYFFQGSNQFEYDFLLQRITKTLKSNSWFGC >1413 bp ATGAAGTTTCTTCTAATACTGCTCCTGCAGGCCACTGCTTCTGGAGCTCTTCCCCTGAAC AGCTCTACAAGCCTGGAAAAAAATAATGTGCTATTTGGTGAGAGATACTTAGAAAAATTT TATGGCCTTGAGATAAACAAACTTCCAGTGACAAAAATGAAATATAGTGGAAACTTAATG AAGGAAAAAATCCAAGAAATGCAGCACTTCTTGGGTCTGAAAGTGACCGGGCAACTGGAC ACATCTACCCTGGAGATGATGCACGCACCTCGATGTGGAGTCCCCGATCTCCATCATTTC AGGGAAATGCCAGGGGGGCCCGTATGGAGGAAACATTATATCACCTACAGAATCAATAAT TACACACCTGACATGAACCGTGAGGATGTTGACTACGCAATCCGGAAAGCTTTCCAAGTA TGGAGTAATGTTACCCCCTTGAAATTCAGCAAGATTAACACAGGCATGGCTGACATTTTG GTGGTTTTTGCCCGTGGAGCTCATGGAGACTTCCATGCTTTTGATGGCAAAGGTGGAATC CTAGCCCATGCTTTTGGACCTGGATCTGGCATTGGAGGGGATGCACATTTCGATGAGGAC GAATTCTGGACTACACATTCAGGAGGCACAAACTTGTTCCTCACTGCTGTTCACGAGATT GGCCATTCCTTAGGTCTTGGCCATTCTAGTGATCCAAAGGCTGTAATGTTCCCCACCTAC AAATATGTCGACATCAACACATTTCGCCTCTCTGCTGATGACATACGTGGCATTCAGTCC CTGTATGGAGACCCAAAAGAGAACCAACGCTTGCCAAATCCTGACAATTCAGAACCAGCT CTCTGTGACCCCAATTTGAGTTTTGATGCTGTCACTACCGTGGGAAATAAGATCTTTTTC TTCAAAGACAGGTTCTTCTGGCTGAAGGTTTCTGAGAGACCAAAGACCAGTGTTAATTTA ATTTCTTCCTTATGGCCAACCTTGCCATCTGGCATTGAAGCTGCTTATGAAATTGAAGCC AGAAATCAAGTTTTTCTTTTTAAAGATGACAAATACTGGTTAATTAGCAATTTAAGACCA GAGCCAAATTATCCCAAGAGCATACATTCTTTTGGTTTTCCTAACTTTGTGAAAAAAATT GATGCAGCTGTTTTTAACCCACGTTTTTATAGGACCTACTTCTTTGTAGATAACCAGTAT TGGAGGTATGATGAAAGGAGACAGATGATGGACCCTGGTTATCCCAAACTGATTACCAAG AACTTCCAAGGAATCGGGCCTAAAATTGATGCAGTCTTCTATTCTAAAAACAAATACTAC TATTTCTTCCAAGGATCTAACCAATTTGAATATGACTTCCTACTCCAACGTATCACCAAA ACACTGAAAAGCAATAGCTGGTTTGGTTGTTAG PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix component extracellular matrix (sensu Metazoa) function catalytic activity function hydrolase activity function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process BE0001637 Matrix metalloproteinase-16 Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Matrix metalloproteinase-16 Involved in protease activity Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. The short isoform cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells MMP16 8q21 Isoform Long:Cell membrane; single-pass type I membrane protein (Potential). Isoform Short:Secreted 565-585 8.74 69522.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7162 GenAtlas MMP16 GeneCards MMP16 GenBank Gene Database AB009303 GenBank Protein Database 2662306 UniProtKB P51512 UniProt Accession MMP16_HUMAN EC 3.4.24.- Matrix metalloproteinase-16 precursor Membrane-type matrix metalloproteinase 3 Membrane-type-3 matrix metalloproteinase MMP- X2 MMP-16 MT-MMP 3 MT3-MMP MT3MMP MTMMP3 >Matrix metalloproteinase-16 precursor MILLTFSTGRRLDFVHHSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRM SVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFHIRRKRY ALTGQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKR DVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDL FLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPT RPLPTVPPHRSIPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVF KDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQ PGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITVW KGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRVK EGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCK RSMQEWV >1824 bp ATGATCTTACTCACATTCAGCACTGGAAGACGGTTGGATTTCGTGCATCATTCGGGGGTG TTTTTCTTGCAAACCTTGCTTTGGATTTTATGTGCTACAGTCTGCGGAACGGAGCAGTAT TTCAATGTGGAGGTTTGGTTACAAAAGTACGGCTACCTTCCACCGACTGACCCCAGAATG TCAGTGCTGCGCTCTGCAGAGACCATGCAGTCTGCCCTAGCTGCCATGCAGCAGTTCTAT GGCATTAACATGACAGGAAAAGTGGACAGAAACACAATTGACTGGATGAAGAAGCCCCGA TGCGGTGTACCTGACCAGACAAGAGGTAGCTCCAAATTTCATATTCGTCGAAAGCGATAT GCATTGACAGGACAGAAATGGCAGCACAAGCACATCACTTACAGTATAAAGAACGTAACT CCAAAAGTAGGAGACCCTGAGACTCGTAAAGCTATTCGCCGTGCCTTTGATGTGTGGCAG AATGTAACTCCTCTGACATTTGAAGAAGTTCCCTACAGTGAATTAGAAAATGGCAAACGT GATGTGGATATAACCATTATTTTTGCATCTGGTTTCCATGGGGACAGCTCTCCCTTTGAT GGAGAGGGAGGATTTTTGGCACATGCCTACTTCCCTGGACCAGGAATTGGAGGAGATACC CATTTTGACTCAGATGAGCCATGGACACTAGGAAATCCTAATCATGATGGAAATGACTTA TTTCTTGTAGCAGTCCATGAACTGGGACATGCTCTGGGATTGGAGCATTCCAATGACCCC ACTGCCATCATGGCTCCATTTTACCAGTACATGGAAACAGACAACTTCAAACTACCTAAT GATGATTTACAGGGCATCCAGAAAATATATGGTCCACCTGACAAGATTCCTCCACCTACA AGACCTCTACCGACAGTGCCCCCACACCGCTCTATTCCTCCGGCTGACCCAAGGAAAAAT GACAGGCCAAAACCTCCTCGGCCTCCAACCGGCAGACCCTCCTATCCCGGAGCCAAACCC AACATCTGTGATGGGAACTTTAACACTCTAGCTATTCTTCGTCGTGAGATGTTTGTTTTC AAGGACCAGTGGTTTTGGCGAGTGAGAAACAACAGGGTGATGGATGGATACCCAATGCAA ATTACTTACTTCTGGCGGGGCTTGCCTCCTAGTATCGATGCAGTTTATGAAAATAGCGAC GGGAATTTTGTGTTCTTTAAAGGTAACAAATATTGGGTGTTCAAGGATACAACTCTTCAA CCTGGTTACCCTCATGACTTGATAACCCTTGGAAGTGGAATTCCCCCTCATGGTATTGAT TCAGCCATTTGGTGGGAGGACGTCGGGAAAACCTATTTCTTCAAGGGAGACAGATATTGG AGATATAGTGAAGAAATGAAAACAATGGACCCTGGCTATCCCAAGCCAATCACAGTCTGG AAAGGGATCCCTGAATCTCCTCAGGGAGCATTTGTACACAAAGAAAATGGCTTTACGTAT TTCTACAAAGGAAAGGAGTATTGGAAATTCAACAACCAGATACTCAAGGTAGAACCTGGA CATCCAAGATCCATCCTCAAGGATTTTATGGGCTGTGATGGACCAACAGACAGAGTTAAA GAAGGACACAGCCCACCAGATGATGTAGACATTGTCATCAAACTGGACAACACAGCCAGC ACTGTGAAAGCCATAGCTATTGTCATTCCCTGCATCTTGGCCTTATGCCTCCTTGTATTG GTTTACACTGTGTTCCAGTTCAAGAGGAAAGGAACACCCCGCCACATACTGTACTGTAAA CGCTCTATGCAAGAGTGGGTGTGA PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix component extracellular matrix (sensu Metazoa) function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding function catalytic activity function hydrolase activity process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism BE0003872 Disintegrin and metalloproteinase domain-containing protein 28 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Disintegrin and metalloproteinase domain-containing protein 28 Involved in metalloendopeptidase activity May play a role in the adhesive and proteolytic events that occur during lymphocyte emigration or may function in ectodomain shedding of lymphocyte surface target proteins, such as FASL and CD40L. May be involved in sperm maturation ADAM28 8p21.2 Isoform 2:Secreted 666-686 6.8 87180.0 Human HUGO Gene Nomenclature Committee (HGNC) GNC:206 GeneCards ADAM28 GenBank Gene Database AF137334 GenBank Protein Database 4583505 UniProtKB Q9UKQ2 UniProt Accession ADA28_HUMAN ADAM 28 eMDC II Epididymial metalloproteinase-like, disintegrin-like, and cysteine-rich protein II MDC-L Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L >Disintegrin and metalloproteinase domain-containing protein 28 MLQGLLPVSLLLSVAVSAIKELPGVKKYEVVYPIRLHPLHKREAKEPEQQEQFETELKYK MTINGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYYQGHILNEKVSDAS ISTCRGLRGYFSQGDQRYFIEPLSPIHRDGQEHALFKYNPDEKNYDSTCGMDGVLWAHDL QQNIALPATKLVKLKDRKVQEHEKYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNM LYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATE LAGTTVGLAFMSTMCSPYSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYSCKCPSTI CVMDKALSFYIPTDFSSCSRLSYDKFFEDKLSNCLFNAPLPTDIISTPICGNQLVEMGED CDCGTSEECTNICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNG KSGNCPDDRFQVNGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNRNEGGSK YGYCRRVDDTLIPCKANDTMCGKLFCQGGSDNLPWKGRIVTFLTCKTFDPEDTSQEIGMV ANGTKCGDNKVCINAECVDIEKAYKSTNCSSKCKGHAVCDHELQCQCEEGWIPPDCDDSS VVFHFSIVVGVLFPMAVIFVVVAMVIRHQSSREKQKKDQRPLSTTGTRPHKQKRKPQMVK AVQPQEMSQMKPHVYDLPVEGNEPPASFHKDTNALPPTVFKDNPMSTPKDSNPEA >2328 bp ATGTTGCAAGGTCTCCTGCCAGTCAGTCTCCTCCTCTCTGTTGCAGTAAGTGCTATAAAA GAACTCCCTGGGGTGAAGAAGTATGAAGTGGTTTATCCTATAAGACTTCATCCACTGCAT AAAAGAGAGGCCAAAGAGCCAGAGCAACAGGAACAATTTGAAACTGAATTAAAGTATAAA ATGACAATTAATGGAAAAATTGCAGTGCTTTATTTGAAAAAAAACAAGAACCTCCTTGCA CCAGGCTACACGGAAACATATTATAATTCCACTGGAAAGGAGATCACCACAAGCCCACAA ATTATGGATGATTGTTATTATCAAGGACATATTCTTAATGAAAAGGTTTCTGACGCTAGC ATCAGCACATGTAGGGGTCTAAGGGGCTACTTCAGTCAGGGGGATCAAAGATACTTTATT GAACCTTTAAGCCCCATACATCGGGATGGACAGGAGCATGCACTCTTCAAGTATAACCCT GATGAAAAGAATTATGACAGCACCTGTGGGATGGATGGTGTGTTGTGGGCCCACGATTTG CAGCAGAACATTGCCCTACCTGCCACCAAACTAGTAAAATTGAAAGACAGGAAGGTTCAG GAACATGAGAAATACATAGAATATTATCTGGTCCTGGATAATGGTGAGTTTAAAAGGTAC AATGAGAATCAAGATGAGATCAGAAAGAGGGTATTTGAGATGGCTAATTATGTCAACATG CTTTATAAAAAGCTCAATACTCATGTGGCCTTAGTTGGTATGGAAATCTGGACTGACAAG GATAAGATAAAGATAACCCCAAATGCAAGCTTCACCTTGGAGAATTTTTCTAAATGGAGG GGGAGTGTTCTCTCAAGAAGAAAGCGTCATGATATTGCTCAGTTAATCACAGCAACAGAA CTTGCTGGAACGACTGTGGGTCTTGCATTTATGTCTACAATGTGTTCTCCTTATTCTGTT GGCGTTGTTCAGGACCACAGCGATAATCTTCTTAGAGTTGCAGGGACAATGGCACATGAA ATGGGCCACAACTTTGGAATGTTTCATGACGACTATTCTTGCAAGTGTCCTTCTACAATA TGTGTGATGGACAAAGCACTGAGCTTCTATATACCCACAGACTTCAGTTCCTGCAGCCGT CTCAGCTATGACAAGTTTTTTGAAGATAAATTATCAAATTGCCTCTTTAATGCTCCATTG CCTACAGATATCATATCCACTCCAATTTGTGGGAACCAGTTGGTGGAAATGGGAGAGGAC TGTGATTGTGGGACATCTGAGGAATGTACCAATATTTGCTGTGATGCTAAGACATGTAAA ATCAAAGCAACTTTTCAATGTGCATTAGGAGAATGTTGTGAAAAATGCCAATTTAAAAAG GCTGGGATGGTGTGCAGACCAGCAAAAGATGAGTGCGACCTGCCTGAAATGTGTAATGGT AAATCTGGTAATTGTCCTGATGATAGATTCCAAGTCAATGGCTTCCCTTGCCATCACGGG AAGGGCCACTGCTTGATGGGCACATGCCCCACACTGCGGGAGCAGTGCACAGAGCTGTGG GGACCAGGAACTGAGGTTGCAGATAAGTCATGTTACAACAGGAATGAAGGTGGGTCAAAG TACGGGTACTGTCGCAGAGTGGATGACACACTCATTCCCTGCAAAGCAAATGATACCATG TGTGGGAAGTTGTTCTGTCAAGGTGGGTCGGATAATTTGCCCTGGAAAGGACGGATAGTG ACTTTCCTGACATGTAAAACATTTGATCCTGAAGACACAAGTCAAGAAATAGGCATGGTG GCCAATGGAACTAAGTGTGGCGATAACAAGGTTTGCATTAATGCAGAATGTGTGGATATT GAGAAAGCCTACAAATCAACCAATTGCTCATCCAAGTGCAAAGGACATGCTGTGTGTGAC CATGAGCTCCAGTGTCAATGTGAGGAAGGATGGATCCCTCCCGACTGCGATGACTCCTCA GTGGTCTTCCACTTCTCCATTGTGGTTGGGGTGCTGTTCCCAATGGCGGTCATTTTTGTG GTGGTTGCTATGGTAATCCGGCACCAGAGCTCCAGAGAAAAGCAGAAGAAAGATCAGAGG CCACTATCTACCACTGGCACCAGGCCACACAAACAGAAGAGGAAACCCCAGATGGTAAAG GCTGTTCAACCCCAAGAGATGAGTCAGATGAAGCCCCATGTGTATGATCTGCCAGTAGAA GGCAATGAGCCCCCAGCCTCTTTTCATAAAGACACAAACGCACTTCCCCCTACTGTTTTC AAGGATAATCCAATGTCTACACCTAAGGACTCAAATCCAGAAGCATGA PF01562 Pep_M12B_propep PF01421 Reprolysin PF00200 Disintegrin PF08516 ADAM_CR component extracellular matrix component extracellular matrix (sensu Metazoa) function catalytic activity function peptidase activity function hydrolase activity function endopeptidase activity function ion binding function metallopeptidase activity function cation binding function metalloendopeptidase activity function transition metal ion binding function zinc ion binding function binding process protein metabolism process cellular protein metabolism process metabolism process macromolecule metabolism process proteolysis process physiological process BE0003730 A disintegrin and metalloproteinase with thrombospondin motifs 5 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown A disintegrin and metalloproteinase with thrombospondin motifs 5 Involved in integrin binding Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period ADAMTS5 21q21.3 Secreted, extracellular space, extracellular matrix (By similarity) None 9.01 101714.9 Human HUGO Gene Nomenclature Committee (HGNC) GNC:221 GeneCards ADAMTS5 GenBank Gene Database AF142099 GenBank Protein Database 5733438 UniProtKB Q9UNA0 UniProt Accession ATS5_HUMAN A disintegrin and metalloproteinase with thrombospondin motifs 11 ADAM-TS 11 ADAM-TS 5 ADAM-TS5 ADAMTS-11 ADAMTS-5 ADMP-2 Aggrecanase-2 >A disintegrin and metalloproteinase with thrombospondin motifs 5 MLLGWASLLLCAFRLPLAAVGPAATPAQDKAGQPPTAAAAAQPRRRQGEEVQERAEPPGH PHPLAQRRRSKGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDGSVGIAGFVPAGGGT SAPWRHRSHCFYRGTVDASPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEKGR VYGDGSARILHVYTREGFSFEALPPRASCETPASTPEAHEHAPAHSNPSGRAALASQLLD QSALSPAGGSGPQTWWRRRRRSISRARQVELLLVADASMARLYGRGLQHYLLTLASIANR LYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYD AAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSH DDSKFCEETFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQI LGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGT PCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPR NNGRYCTGKRAIYRSCSLMPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVL PADVCKLTCRAKGTGYYVVFSPKVTDGTECRPYSNSVCVRGKCVRTGCDGIIGSKLQYDK CGVCGGDNSSCTKIVGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKK NGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPT KPLDVRYSFFVPKKSTPKVNSVTSHGSNKVGSHTSQPQWVTGPWLACSRTCDTGWHTRTV QCQDGNRKLAKGCPLSQRPSAFKQCLLKKC >2793 bp ATGCTGCTCGGGTGGGCGTCCCTGCTGCTGTGCGCGTTCCGCCTGCCCCTGGCCGCGGTC GGCCCCGCCGCGACACCTGCCCAGGATAAAGCCGGGCAGCCTCCGACTGCTGCAGCAGCC GCCCAGCCCCGCCGGCGGCAGGGGGAGGAGGTGCAGGAGCGAGCCGAGCCTCCCGGCCAC CCGCACCCCCTGGCGCAGCGGCGCAGGAGCAAGGGGCTGGTGCAGAACATCGACCAACTC TACTCCGGCGGCGGCAAGGTGGGCTACCTCGTCTACGCGGGCGGCCGGAGGTTCCTCTTG GACCTGGAGCGAGATGGTTCGGTGGGCATTGCTGGCTTCGTGCCCGCAGGAGGCGGGACG AGTGCGCCCTGGCGCCACCGGAGCCACTGCTTCTATCGGGGCACAGTGGACGCTAGTCCC CGCTCTCTGGCTGTCTTTGACCTCTGTGGGGGTCTCGACGGCTTCTTCGCGGTCAAGCAC GCGCGCTACACCCTAAAGCCACTGCTGCGCGGACCCTGGGCGGAGGAAGAAAAGGGGCGC GTGTACGGGGATGGGTCCGCACGGATCCTGCACGTCTACACCCGCGAGGGCTTCAGCTTC GAGGCCCTGCCGCCGCGCGCCAGCTGCGAAACCCCCGCGTCCACACCGGAGGCCCACGAG CATGCTCCGGCGCACAGCAACCCGAGCGGACGCGCAGCACTGGCCTCGCAGCTCTTGGAC CAGTCCGCTCTCTCGCCCGCTGGGGGCTCAGGACCGCAGACGTGGTGGCGGCGGCGGCGC CGCTCCATCTCCCGGGCCCGCCAGGTGGAGCTGCTTCTGGTGGCTGACGCGTCCATGGCG CGGTTGTATGGCCGGGGCCTGCAGCATTACCTGCTGACCCTGGCCTCCATCGCCAATAGG CTGTACAGCCATGCTAGCATCGAGAACCACATCCGCCTGGCCGTGGTGAAGGTGGTGGTG CTAGGCGACAAGGACAAGAGCCTGGAAGTGAGCAAGAACGCTGCCACCACACTCAAGAAC TTTTGCAAGTGGCAGCACCAACACAACCAGCTGGGAGATGACCATGAGGAGCACTACGAT GCAGCTATCCTGTTTACTCGGGAGGATTTATGTGGGCATCATTCATGTGACACCCTGGGA ATGGCAGACGTTGGGACCATATGTTCTCCAGAGCGCAGCTGTGCTGTGATTGAAGACGAT GGCCTCCACGCAGCCTTCACTGTGGCTCACGAAATCGGACATTTACTTGGCCTCTCCCAT GACGATTCCAAATTCTGTGAAGAGACCTTTGGTTCCACAGAAGATAAGCGCTTAATGTCT TCCATCCTTACCAGCATTGATGCATCTAAGCCCTGGTCCAAATGCACTTCAGCCACCATC ACAGAATTCCTGGATGATGGCCATGGTAACTGTTTGCTGGACCTACCACGAAAGCAGATC CTGGGCCCCGAAGAACTCCCAGGACAGACCTACGATGCCACCCAGCAGTGCAACCTGACA TTCGGGCCTGAGTACTCCGTGTGTCCCGGCATGGATGTCTGTGCTCGCCTGTGGTGTGCT GTGGTACGCCAGGGCCAGATGGTCTGTCTGACCAAGAAGCTGCCTGCGGTGGAAGGGACG CCTTGTGGAAAGGGGAGAATCTGCCTGCAGGGCAAATGTGTGGACAAAACCAAGAAAAAA TATTATTCAACGTCAAGCCATGGCAACTGGGGATCTTGGGGATCCTGGGGCCAGTGTTCT CGCTCATGTGGAGGAGGAGTGCAGTTTGCCTATCGTCACTGTAATAACCCTGCTCCCAGA AACAACGGACGCTACTGCACAGGGAAGAGGGCCATCTACCGCTCCTGCAGTCTCATGCCC TGCCCACCCAATGGTAAATCATTTCGTCATGAACAGTGTGAGGCCAAAAATGGCTATCAG TCTGATGCAAAAGGAGTCAAAACTTTTGTGGAATGGGTTCCCAAATATGCAGGTGTCCTG CCAGCGGATGTGTGCAAGCTGACCTGCAGAGCCAAGGGCACTGGCTACTATGTGGTATTT TCTCCAAAGGTGACCGATGGCACTGAATGTAGGCCGTACAGTAATTCCGTCTGCGTCCGG GGGAAGTGTGTGAGAACTGGCTGTGACGGCATCATTGGCTCAAAGCTGCAGTATGACAAG TGCGGAGTATGTGGAGGAGACAACTCCAGCTGTACAAAGATTGTTGGAACCTTTAATAAG AAAAGTAAGGGTTACACTGACGTGGTGAGGATTCCTGAAGGGGCAACCCACATAAAAGTT CGACAGTTCAAAGCCAAAGACCAGACTAGATTCACTGCCTATTTAGCCCTGAAAAAGAAA AACGGTGAGTACCTTATCAATGGAAAGTACATGATCTCCACTTCAGAGACTATCATTGAC ATCAATGGAACAGTCATGAACTATAGCGGTTGGAGCCACAGGGATGACTTCCTGCATGGC ATGGGCTACTCTGCCACGAAGGAAATTCTAATAGTGCAGATTCTTGCAACAGACCCCACT AAACCATTAGATGTCCGTTATAGCTTTTTTGTTCCCAAGAAGTCCACTCCAAAAGTAAAC TCTGTCACTAGTCATGGCAGCAATAAAGTGGGATCACACACTTCGCAGCCGCAGTGGGTC ACGGGCCCATGGCTCGCCTGCTCTAGGACCTGTGACACAGGTTGGCACACCAGAACGGTG CAGTGCCAGGATGGAAACCGGAAGTTAGCAAAAGGATGTCCTCTCTCCCAAAGGCCTTCT GCGTTTAAGCAATGCTTGTTGAAGAAATGTTAG PF00090 TSP_1 PF01562 Pep_M12B_propep PF01421 Reprolysin PF05986 ADAM_spacer1 component extracellular matrix function catalytic activity function peptidase activity function endopeptidase activity function hydrolase activity function metallopeptidase activity function ion binding function metalloendopeptidase activity function cation binding function transition metal ion binding function zinc ion binding function binding process metabolism process proteolysis process macromolecule metabolism process protein metabolism process physiological process process cellular protein metabolism "

owl:sameAs

drug:EXPT00627

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