bhf-ucl ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. J. Biol. Chem. (0021-9258) 2006 imex curation Liu C.J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E. Cardiac - Interactions involving cardiac related proteins Several experiments involved a plasmid described as COMP, however there is no information in the paper about the full length COMP plasmid, however in figure 5 it is apparent that COMP is full length therefore I have assumed Fig 2D, 4 and 5 refer to full length COMP protein. Have annotated the full length COMP as human see PMID 16585064, same authors: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. Four functional domains of mouse COMP AF257516: the N-terminal (amino acids 20–83), pDB-COMP-NT; EGF repeat domain (amino acids 84–261) pDB-COMP-EGF, type III repeat domain (amino acids 266–520) pDB-COMP-type III; and C-terminal domain (amino acids 521–755) pDB-COMP-CT cloned into yeast expression construct. human ADAMTS-12 domain based plasmids: pADAMTS-12 (26–240), pADAMTS-12-(241–463), pADAMTS-12-(464–701), pADAMTS-12-(702–995), pADAMTS-12-(996–1593), pADAMTS-12-(1316–1593), pADAMTS-12-(1531–1593), and pADA-MTS-12-(1316–1530). The catalytic domain of hADAMTS-12 (amino acids 241–463, AJ250725) and the EGF-like domain of COMP (amino acids 84–261) inserted into pGEX-3X to generate the pGEX12-CD and pGEX-COMP-EGF plasmids. His-tagged proteins in E. coli. A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) pedicesare@aol.com 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Liu C.J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E. Cardiac - Interactions involving cardiac related proteins Several experiments involved a plasmid described as COMP, however there is no information in the paper about the full length COMP plasmid, however in figure 5 it is apparent that COMP is full length therefore I have assumed Fig 2D, 4 and 5 refer to full length COMP protein. Have annotated the full length COMP as human see PMID 16585064, same authors: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. Four functional domains of mouse COMP AF257516: the N-terminal (amino acids 20–83), pDB-COMP-NT; EGF repeat domain (amino acids 84–261) pDB-COMP-EGF, type III repeat domain (amino acids 266–520) pDB-COMP-type III; and C-terminal domain (amino acids 521–755) pDB-COMP-CT cloned into yeast expression construct. human ADAMTS-12 domain based plasmids: pADAMTS-12 (26–240), pADAMTS-12-(241–463), pADAMTS-12-(464–701), pADAMTS-12-(702–995), pADAMTS-12-(996–1593), pADAMTS-12-(1316–1593), pADAMTS-12-(1531–1593), and pADA-MTS-12-(1316–1530). The catalytic domain of hADAMTS-12 (amino acids 241–463, AJ250725) and the EGF-like domain of COMP (amino acids 84–261) inserted into pGEX-3X to generate the pGEX12-CD and pGEX-COMP-EGF plasmids. His-tagged proteins in E. coli. A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) pedicesare@aol.com Accepted 2013-DEC-19 by ORCHARD J. Biol. Chem. (0021-9258) 2006 imex curation ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. J. Biol. Chem. (0021-9258) 2006 imex curation Liu C.J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E. Cardiac - Interactions involving cardiac related proteins Several experiments involved a plasmid described as COMP, however there is no information in the paper about the full length COMP plasmid, however in figure 5 it is apparent that COMP is full length therefore I have assumed Fig 2D, 4 and 5 refer to full length COMP protein. Have annotated the full length COMP as human see PMID 16585064, same authors: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. Four functional domains of mouse COMP AF257516: the N-terminal (amino acids 20–83), pDB-COMP-NT; EGF repeat domain (amino acids 84–261) pDB-COMP-EGF, type III repeat domain (amino acids 266–520) pDB-COMP-type III; and C-terminal domain (amino acids 521–755) pDB-COMP-CT cloned into yeast expression construct. human ADAMTS-12 domain based plasmids: pADAMTS-12 (26–240), pADAMTS-12-(241–463), pADAMTS-12-(464–701), pADAMTS-12-(702–995), pADAMTS-12-(996–1593), pADAMTS-12-(1316–1593), pADAMTS-12-(1531–1593), and pADA-MTS-12-(1316–1530). The catalytic domain of hADAMTS-12 (amino acids 241–463, AJ250725) and the EGF-like domain of COMP (amino acids 84–261) inserted into pGEX-3X to generate the pGEX12-CD and pGEX-COMP-EGF plasmids. His-tagged proteins in E. coli. A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) pedicesare@aol.com 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down anti tag western anti tag western blot anti tag western Liu C.J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E. Cardiac - Interactions involving cardiac related proteins Several experiments involved a plasmid described as COMP, however there is no information in the paper about the full length COMP plasmid, however in figure 5 it is apparent that COMP is full length therefore I have assumed Fig 2D, 4 and 5 refer to full length COMP protein. Have annotated the full length COMP as human see PMID 16585064, same authors: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. Four functional domains of mouse COMP AF257516: the N-terminal (amino acids 20–83), pDB-COMP-NT; EGF repeat domain (amino acids 84–261) pDB-COMP-EGF, type III repeat domain (amino acids 266–520) pDB-COMP-type III; and C-terminal domain (amino acids 521–755) pDB-COMP-CT cloned into yeast expression construct. human ADAMTS-12 domain based plasmids: pADAMTS-12 (26–240), pADAMTS-12-(241–463), pADAMTS-12-(464–701), pADAMTS-12-(702–995), pADAMTS-12-(996–1593), pADAMTS-12-(1316–1593), pADAMTS-12-(1531–1593), and pADA-MTS-12-(1316–1530). The catalytic domain of hADAMTS-12 (amino acids 241–463, AJ250725) and the EGF-like domain of COMP (amino acids 84–261) inserted into pGEX-3X to generate the pGEX12-CD and pGEX-COMP-EGF plasmids. His-tagged proteins in E. coli. A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) pedicesare@aol.com Accepted 2013-DEC-19 by ORCHARD J. Biol. Chem. (0021-9258) 2006 imex curation ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. J. Biol. Chem. (0021-9258) 2006 imex curation Liu C.J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E. Cardiac - Interactions involving cardiac related proteins Several experiments involved a plasmid described as COMP, however there is no information in the paper about the full length COMP plasmid, however in figure 5 it is apparent that COMP is full length therefore I have assumed Fig 2D, 4 and 5 refer to full length COMP protein. Have annotated the full length COMP as human see PMID 16585064, same authors: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. Four functional domains of mouse COMP AF257516: the N-terminal (amino acids 20–83), pDB-COMP-NT; EGF repeat domain (amino acids 84–261) pDB-COMP-EGF, type III repeat domain (amino acids 266–520) pDB-COMP-type III; and C-terminal domain (amino acids 521–755) pDB-COMP-CT cloned into yeast expression construct. human ADAMTS-12 domain based plasmids: pADAMTS-12 (26–240), pADAMTS-12-(241–463), pADAMTS-12-(464–701), pADAMTS-12-(702–995), pADAMTS-12-(996–1593), pADAMTS-12-(1316–1593), pADAMTS-12-(1531–1593), and pADA-MTS-12-(1316–1530). The catalytic domain of hADAMTS-12 (amino acids 241–463, AJ250725) and the EGF-like domain of COMP (amino acids 84–261) inserted into pGEX-3X to generate the pGEX12-CD and pGEX-COMP-EGF plasmids. His-tagged proteins in E. coli. A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) pedicesare@aol.com 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro elisa enzyme linked immunosorbent assay ELISA ELISA elisa antibody detection identification by antibody antibody detection Liu C.J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E. Cardiac - Interactions involving cardiac related proteins Several experiments involved a plasmid described as COMP, however there is no information in the paper about the full length COMP plasmid, however in figure 5 it is apparent that COMP is full length therefore I have assumed Fig 2D, 4 and 5 refer to full length COMP protein. Have annotated the full length COMP as human see PMID 16585064, same authors: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. Four functional domains of mouse COMP AF257516: the N-terminal (amino acids 20–83), pDB-COMP-NT; EGF repeat domain (amino acids 84–261) pDB-COMP-EGF, type III repeat domain (amino acids 266–520) pDB-COMP-type III; and C-terminal domain (amino acids 521–755) pDB-COMP-CT cloned into yeast expression construct. human ADAMTS-12 domain based plasmids: pADAMTS-12 (26–240), pADAMTS-12-(241–463), pADAMTS-12-(464–701), pADAMTS-12-(702–995), pADAMTS-12-(996–1593), pADAMTS-12-(1316–1593), pADAMTS-12-(1531–1593), and pADA-MTS-12-(1316–1530). The catalytic domain of hADAMTS-12 (amino acids 241–463, AJ250725) and the EGF-like domain of COMP (amino acids 84–261) inserted into pGEX-3X to generate the pGEX12-CD and pGEX-COMP-EGF plasmids. His-tagged proteins in E. coli. A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) pedicesare@aol.com Accepted 2013-DEC-19 by ORCHARD J. Biol. Chem. (0021-9258) 2006 imex curation ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. J. Biol. Chem. (0021-9258) 2006 imex curation Liu C.J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E. Cardiac - Interactions involving cardiac related proteins Several experiments involved a plasmid described as COMP, however there is no information in the paper about the full length COMP plasmid, however in figure 5 it is apparent that COMP is full length therefore I have assumed Fig 2D, 4 and 5 refer to full length COMP protein. Have annotated the full length COMP as human see PMID 16585064, same authors: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. Four functional domains of mouse COMP AF257516: the N-terminal (amino acids 20–83), pDB-COMP-NT; EGF repeat domain (amino acids 84–261) pDB-COMP-EGF, type III repeat domain (amino acids 266–520) pDB-COMP-type III; and C-terminal domain (amino acids 521–755) pDB-COMP-CT cloned into yeast expression construct. human ADAMTS-12 domain based plasmids: pADAMTS-12 (26–240), pADAMTS-12-(241–463), pADAMTS-12-(464–701), pADAMTS-12-(702–995), pADAMTS-12-(996–1593), pADAMTS-12-(1316–1593), pADAMTS-12-(1531–1593), and pADA-MTS-12-(1316–1530). The catalytic domain of hADAMTS-12 (amino acids 241–463, AJ250725) and the EGF-like domain of COMP (amino acids 84–261) inserted into pGEX-3X to generate the pGEX12-CD and pGEX-COMP-EGF plasmids. His-tagged proteins in E. coli. A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) pedicesare@aol.com 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro protease assay protease assay predetermined predetermined participant predetermined Liu C.J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E. Cardiac - Interactions involving cardiac related proteins Several experiments involved a plasmid described as COMP, however there is no information in the paper about the full length COMP plasmid, however in figure 5 it is apparent that COMP is full length therefore I have assumed Fig 2D, 4 and 5 refer to full length COMP protein. Have annotated the full length COMP as human see PMID 16585064, same authors: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. Four functional domains of mouse COMP AF257516: the N-terminal (amino acids 20–83), pDB-COMP-NT; EGF repeat domain (amino acids 84–261) pDB-COMP-EGF, type III repeat domain (amino acids 266–520) pDB-COMP-type III; and C-terminal domain (amino acids 521–755) pDB-COMP-CT cloned into yeast expression construct. human ADAMTS-12 domain based plasmids: pADAMTS-12 (26–240), pADAMTS-12-(241–463), pADAMTS-12-(464–701), pADAMTS-12-(702–995), pADAMTS-12-(996–1593), pADAMTS-12-(1316–1593), pADAMTS-12-(1531–1593), and pADA-MTS-12-(1316–1530). The catalytic domain of hADAMTS-12 (amino acids 241–463, AJ250725) and the EGF-like domain of COMP (amino acids 84–261) inserted into pGEX-3X to generate the pGEX12-CD and pGEX-COMP-EGF plasmids. His-tagged proteins in E. coli. A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) pedicesare@aol.com Accepted 2013-DEC-19 by ORCHARD J. Biol. Chem. (0021-9258) 2006 imex curation ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. J. Biol. Chem. (0021-9258) 2006 imex curation Liu C.J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E. Cardiac - Interactions involving cardiac related proteins Several experiments involved a plasmid described as COMP, however there is no information in the paper about the full length COMP plasmid, however in figure 5 it is apparent that COMP is full length therefore I have assumed Fig 2D, 4 and 5 refer to full length COMP protein. Have annotated the full length COMP as human see PMID 16585064, same authors: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. Four functional domains of mouse COMP AF257516: the N-terminal (amino acids 20–83), pDB-COMP-NT; EGF repeat domain (amino acids 84–261) pDB-COMP-EGF, type III repeat domain (amino acids 266–520) pDB-COMP-type III; and C-terminal domain (amino acids 521–755) pDB-COMP-CT cloned into yeast expression construct. human ADAMTS-12 domain based plasmids: pADAMTS-12 (26–240), pADAMTS-12-(241–463), pADAMTS-12-(464–701), pADAMTS-12-(702–995), pADAMTS-12-(996–1593), pADAMTS-12-(1316–1593), pADAMTS-12-(1531–1593), and pADA-MTS-12-(1316–1530). The catalytic domain of hADAMTS-12 (amino acids 241–463, AJ250725) and the EGF-like domain of COMP (amino acids 84–261) inserted into pGEX-3X to generate the pGEX12-CD and pGEX-COMP-EGF plasmids. His-tagged proteins in E. coli. A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) pedicesare@aol.com 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. anti tag coip anti tag coimmunoprecipitation anti tag coip polyclonal western polyclonal antibody western blot polyclonal western Liu C.J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E. Cardiac - Interactions involving cardiac related proteins Several experiments involved a plasmid described as COMP, however there is no information in the paper about the full length COMP plasmid, however in figure 5 it is apparent that COMP is full length therefore I have assumed Fig 2D, 4 and 5 refer to full length COMP protein. Have annotated the full length COMP as human see PMID 16585064, same authors: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. Four functional domains of mouse COMP AF257516: the N-terminal (amino acids 20–83), pDB-COMP-NT; EGF repeat domain (amino acids 84–261) pDB-COMP-EGF, type III repeat domain (amino acids 266–520) pDB-COMP-type III; and C-terminal domain (amino acids 521–755) pDB-COMP-CT cloned into yeast expression construct. human ADAMTS-12 domain based plasmids: pADAMTS-12 (26–240), pADAMTS-12-(241–463), pADAMTS-12-(464–701), pADAMTS-12-(702–995), pADAMTS-12-(996–1593), pADAMTS-12-(1316–1593), pADAMTS-12-(1531–1593), and pADA-MTS-12-(1316–1530). The catalytic domain of hADAMTS-12 (amino acids 241–463, AJ250725) and the EGF-like domain of COMP (amino acids 84–261) inserted into pGEX-3X to generate the pGEX12-CD and pGEX-COMP-EGF plasmids. His-tagged proteins in E. coli. A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) pedicesare@aol.com Accepted 2013-DEC-19 by ORCHARD J. Biol. Chem. (0021-9258) 2006 imex curation ats7_human A disintegrin and metalloproteinase with thrombospondin motifs 7 ADAMTS7 COMPase protein protein human Homo sapiens Human MPGGPSPRSPAPLLRPLLLLLCALAPGAPGPAPGRATEGRAALDIVHPVRVDAGGSFLSYELWPRALRKRDVSVRRDAPAFYELQYRGRELRFNLTANQHLLAPGFVSETRRRGGLGRAHIRAHTPACHLLGEVQDPELEGGLAAISACDGLKGVFQLSNEDYFIEPLDSAPARPGHAQPHVVYKRQAPERLAQRGDSSAPSTCGVQVYPELESRRERWEQRQQWRRPRLRRLHQRSVSKEKWVETLVVADAKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHITIVRLVLLEDEEEDLKITHHADNTLKSFCKWQKSINMKGDAHPLHHDTAILLTRKDLCAAMNRPCETLGLSHVAGMCQPHRSCSINEDTGLPLAFTVAHELGHSFGIQHDGSGNDCEPVGKRPFIMSPQLLYDAAPLTWSRCSRQYITRFLDRGWGLCLDDPPAKDIIDFPSVPPGVLYDVSHQCRLQYGAYSAFCEDMDNVCHTLWCSVGTTCHSKLDAAVDGTRCGENKWCLSGECVPVGFRPEAVDGGWSGWSAWSICSRSCGMGVQSAERQCTQPTPKYKGRYCVGERKRFRLCNLQACPAGRPSFRHVQCSHFDAMLYKGQLHTWVPVVNDVNPCELHCRPANEYFAEKLRDAVVDGTPCYQVRASRDLCINGICKNVGCDFEIDSGAMEDRCGVCHGNGSTCHTVSGTFEEAEGLGYVDVGLIPAGAREIRIQEVAEAANFLALRSEDPEKYFLNGGWTIQWNGDYQVAGTTFTYARRGNWENLTSPGPTKEPVWIQLLFQESNPGVHYEYTIHREAGGHDEVPPPVFSWHYGPWTKCTVTCGRGVQRQNVYCLERQAGPVDEEHCDPLGRPDDQQRKCSEQPCPARWWAGEWQLCSSSCGPGGLSRRAVLCIRSVGLDEQSALEPPACEHLPRPPTETPCNRHVPCPATWAVGNWSQCSVTCGEGTQRRNVLCTNDTGVPCDEAQQPASEVTCSLPLCRWPLGTLGPEGSGSGSSSHELFNEADFIPHHLAPRPSPASSPKPGTMGNAIEEEAPELDLPGPVFVDDFYYDYNFINFHEDLSYGPSEEPDLDLAGTGDRTPPPHSHPAAPSTGSPVPATEPPAAKEEGVLGPWSPSPWPSQAGRSPPPPSEQTPGNPLINFLPEEDTPIGAPDLGLPSLSWPRVSTDGLQTPATPESQNDFPVGKDSQSQLPPPWRDRTNEVFKDDEEPKGRGAPHLPPRPSSTLPPLSPVGSTHSSPSPDVAELWTGGTVAWEPALEGGLGPVDSELWPTVGVASLLPPPIAPLPEMKVRDSSLEPGTPSFPTPGPGSWDLQTVAVWGTFLPTTLTGLGHMPEPALNPGPKGQPESLSPEVPLSSRLLSTPAWDSPANSHRVPETQPLAPSLAEAGPPADPLVVRNAGWQAGNWSECSTTCGLGAVWRPVRCSSGRDEDCAPAGRPQPARRCHLRPCATWHSGNWSKCSRSCGGGSSVRDVQCVDTRDLRPLRPFHCQPGPAKPPAHRPCGAQPCLSWYTSSWRECSEACGGGEQQRLVTCPEPGLCEEALRPNTTRPCNTHPCTQWVVGPWGQCSGPCGGGVQRRLVKCVNTQTGLPEEDSDQCGHEAWPESSRPCGTEDCEPVEPPRCERDRLSFGFCETLRLLGRCQLPTIRTQCCRSCSPPSHGAPSRGHQRVARR AB38264B8E8DB740 comp_human Cartilage oligomeric matrix protein COMP Thrombospondin-5 protein protein human Homo sapiens Human MVPDTACVLLLTLAALGASGQGQSPLGSDLGPQMLRELQETNAALQDVRELLRQQVREITFLKNTVMECDACGMQQSVRTGLPSVRPLLHCAPGFCFPGVACIQTESGARCGPCPAGFTGNGSHCTDVNECNAHPCFPRVRCINTSPGFRCEACPPGYSGPTHQGVGLAFAKANKQVCTDINECETGQHNCVPNSVCINTRGSFQCGPCQPGFVGDQASGCQRRAQRFCPDGSPSECHEHADCVLERDGSRSCVCAVGWAGNGILCGRDTDLDGFPDEKLRCPERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEKDNCPLVRNPDQRNTDEDKWGDACDNCRSQKNDDQKDTDQDGRGDACDDDIDGDRIRNQADNCPRVPNSDQKDSDGDGIGDACDNCPQKSNPDQADVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQEDSDHDGQGDACDDDDDNDGVPDSRDNCRLVPNPGQEDADRDGVGDVCQDDFDADKVVDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGREIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTESQVRLLWKDPRNVGWKDKKSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTTMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYETHQLRQA A0B73AADB39FBC7B ats12_human A disintegrin and metalloproteinase with thrombospondin motifs 12 ADAMTS12 UNQ1918/PRO4389 protein protein human Homo sapiens Human MPCAQRSWLANLSVVAQLLNFGALCYGRQPQPGPVRFPDRRQEHFIKGLPEYHVVGPVRVDASGHFLSYGLHYPITSSRRKRDLDGSEDWVYYRISHEEKDLFFNLTVNQGFLSNSYIMEKRYGNLSHVKMMASSAPLCHLSGTVLQQGTRVGTAALSACHGLTGFFQLPHGDFFIEPVKKHPLVEGGYHPHIVYRRQKVPETKEPTCGLKDSVNISQKQELWREKWERHNLPSRSLSRRSISKERWVETLVVADTKMIEYHGSENVESYILTIMNMVTGLFHNPSIGNAIHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCKWQKSINPKSDLNPVHHDVAVLLTRKDICAGFNRPCETLGLSHLSGMCQPHRSCNINEDSGLPLAFTIAHELGHSFGIQHDGKENDCEPVGRHPYIMSRQLQYDPTPLTWSKCSEEYITRFLDRGWGFCLDDIPKKKGLKSKVIAPGVIYDVHHQCQLQYGPNATFCQEVENVCQTLWCSVKGFCRSKLDAAADGTQCGEKKWCMAGKCITVGKKPESIPGGWGRWSPWSHCSRTCGAGVQSAERLCNNPEPKFGGKYCTGERKRYRLCNVHPCRSEAPTFRQMQCSEFDTVPYKNELYHWFPIFNPAHPCELYCRPIDGQFSEKMLDAVIDGTPCFEGGNSRNVCINGICKMVGCDYEIDSNATEDRCGVCLGDGSSCQTVRKMFKQKEGSGYVDIGLIPKGARDIRVMEIEGAGNFLAIRSEDPEKYYLNGGFIIQWNGNYKLAGTVFQYDRKGDLEKLMATGPTNESVWIQLLFQVTNPGIKYEYTIQKDGLDNDVEQQMYFWQYGHWTECSVTCGTGIRRQTAHCIKKGRGMVKATFCDPETQPNGRQKKCHEKACPPRWWAGEWEACSATCGPHGEKKRTVLCIQTMVSDEQALPPTDCQHLLKPKTLLSCNRDILCPSDWTVGNWSECSVSCGGGVRIRSVTCAKNHDEPCDVTRKPNSRALCGLQQCPSSRRVLKPNKGTISNGKNPPTLKPVPPPTSRPRMLTTPTGPESMSTSTPAISSPSPTTASKEGDLGGKQWQDSSTQPELSSRYLISTGSTSQPILTSQSLSIQPSEENVSSSDTGPTSEGGLVATTTSGSGLSSSRNPITWPVTPFYNTLTKGPEMEIHSGSGEEREQPEDKDESNPVIWTKIRVPGNDAPVESTEMPLAPPLTPDLSRESWWPPFSTVMEGLLPSQRPTTSETGTPRVEGMVTEKPANTLLPLGGDHQPEPSGKTANRNHLKLPNNMNQTKSSEPVLTEEDATSLITEGFLLNASNYKQLTNGHGSAHWIVGNWSECSTTCGLGAYWRRVECSTQMDSDCAAIQRPDPAKRCHLRPCAGWKVGNWSKCSRNCSGGFKIREIQCVDSRDHRNLRPFHCQFLAGIPPPLSMSCNPEPCEAWQVEPWSQCSRSCGGGVQERGVFCPGGLCDWTKRPTSTMSCNEHLCCHWATGNWDLCSTSCGGGFQKRTVQCVPSEGNKTEDQDQCLCDHKPRPPEFKKCNQQACKKSADLLCTKDKLSASFCQTLKAMKKCSVPTVRAECCFSCPQTHITHTQRQRRQRLLQKSKEL C88563125F0F90D8 comp_mouse Cartilage oligomeric matrix protein Comp protein protein mouse Mus musculus Mouse MGPTACVLVLALAILRATGQGQIPLGGDLAPQMLRELQETNAALQDVRELLRQQVKEITFLKNTVMECDACGMQPARTPGLSVRPVPLCAPGSCFPGVVCSETATGARCGPCPPGYTGNGSHCTDVNECNAHPCFPRVRCINTSPGFHCEACPPGFSGPTHEGVGLTFAKSNKQVCTDINECETGQHNCVPNSVCVNTRGSFQCGPCQPGFVGDQTSGCQRRGQHFCPDGSPSPCHEKANCVLERDGSRSCVCAVGWAGNGLLCGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEQDNCPLVRNPDQRNSDSDKWGDACDNCRSKKNDDQKDTDLDGRGDACDDDIDGDRIRNVADNCPRVPNFDQSDSDGDGVGDACDNCPQKDNPDQRDVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQQDSDHDGKGDACDDDDDNDGVPDSRDNCRLVPNPGQEDNDRDGVGDACQGDFDADKVIDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTAMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYESHRLQRV 24C2F113E7945C0F comp-adamts12 1 pDB-COMP 9 unspecified role unspecified role bait bait egf-like domain required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain pPC86-ADAMTS-12 8 unspecified role unspecified role prey prey c-terminal required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 12 14 physical association physical association Fig 1B, 3, 4 comp-adamts12-1 2 TS-12 8 unspecified role unspecified role prey prey ha tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined chlae-cos_7 Cercopithecus aethiops simian cells transformed with SV40 Grivet cos_7 cercopithecus aethiops, by transformation with SV40 pDB-COMP 9 unspecified role unspecified role bait bait egf-like domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain gst-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association Fig 2A and 2B adamts12-comp 3 His-TS12C4TSP 8 unspecified role unspecified role bait bait c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain his-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) A cDNA segment encoding the four C-terminal TSP motifs (His-TS12C4TSP) of hADAMTS-12 (amino acids 1316–1530) was subcloned into the pBAD TOPO vector per the manufacturer's protocol. pDB-COMP 9 unspecified role unspecified role prey prey egf-like domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 26 23 direct interaction direct interaction Fig 2C as COMP is purified I have assumed it was the construct described in the section: Expression and Purification of GST and His-tagged Proteins, and would therefore be the pGEX-COMP-EGF plasmid. However COMP is described as COMP in the text, not as a COMP-fragment adamts12-comp-2 5 7 unspecified role unspecified role prey prey human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. TS-12 8 unspecified role unspecified role bait bait ha tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. physical association physical association Fig 2D It seems likely that full length COMP is human - see PMID: 16585064 published the same year as this one by these authors "(purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" comp-adamts12-4 1 6 unspecified role unspecified role prey prey pDB-COMP 9 unspecified role unspecified role bait bait not stated but assumed this is full length COMP physical association physical association Fig 3B Human ADAMTS-7 published by this group in PMID:16585064 therefore this construct annotated as human adamts12-comp-4 4 TS-12 8 enzyme enzyme neutral component neutral component catalytic region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) GST tag removed before incubation with COMP, therefore GST tag not included in annotation as a feature. Not stated but assumed this is full length COMP 7 enzyme target enzyme target substrate substrate neutral component neutral component human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. full length COMP is mostly likely to be human see PMID 16585064, by same authors who describe: "were incubated with 0.5 μg of human COMP (purified from HEK293 cells stably transfected with an expression plasmid encoding full-length human COMP)" published the same year as this one enzyme/enzyme target biological roles. protein cleavage protein cleavage Fig 5 2 mm of ZnCl2, pH 7.5 to pH 9.5 P58397 increases degradation at protein level of Q9R0G6