MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint markov-2008-1 Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation. in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Markov DI., Pivovarova AV., Chernik IS., Gusev NB., Levitsky DI. Virus - Publications including interactions involving viral proteins FEBS Lett. (0014-5793) 2008 Only protein-protein interactions imex curation markov-2008-3 Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation. in vitro In vitro dls dynamic light scattering dls predetermined predetermined participant predetermined Markov DI., Pivovarova AV., Chernik IS., Gusev NB., Levitsky DI. Virus - Publications including interactions involving viral proteins FEBS Lett. (0014-5793) 2008 Only protein-protein interactions imex curation markov-2008-2 Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation. in vitro In vitro cosedimentation cosedimentation predetermined predetermined participant predetermined Markov DI., Pivovarova AV., Chernik IS., Gusev NB., Levitsky DI. Virus - Publications including interactions involving viral proteins FEBS Lett. (0014-5793) 2008 Only protein-protein interactions imex curation myss_rabit Myosin heavy chain, skeletal muscle protein protein rabit Oryctolagus cuniculus (Rabbit) Rabbit SAETEKEMANMKEEFEKTKESLAKAEAKRKELEEKMVALMQEKNDLQLQVQAEADSLADAEERQDLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQETSMDIENDKQQLDEKLKKLEFMTNLQSKIEDEQALMTNLQRIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFEKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLAGNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEHQRLINELSAQKARLHTESGEFSRQLDEKDAMVSQLSRGGQAFTQQIEGLKRQLEEETKAKSALAHALQSSRRDCDLLREQYEEEQEAKAELQRAMSKANSEVSQWRTKCETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEAEDLMIDVERSNATCARMDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTEVFKVKNAYEESLDHLETLKRENKNLQQEISDLTEQIAESAKHIHELEKVKKQIDQEKSELQAALEEAEGSLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIKNLRNTQGILKDTQLHLDDAVRGQDDHKEQLAMVERRANLMQAEIEELRASLEQTERSRRVADQDLLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQQRLDEAEQLALKGGKKQIQKLEARVKELENEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNINLSKFRKLQHELEEAEERADIAESQVNKLRVKSRDVHSKVISEE fragmentation type: fragments Muscle contraction mint myl1_rabit Myosin light chain 1/3, skeletal muscle isoform MYL1 Myosin light chain alkali 1/2 protein protein rabit Oryctolagus cuniculus (Rabbit) Rabbit MAPKKDVKKPAAAAAPAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQDEFKEAFLLYDRTGDSKITLSQVGDVLRALGTNPTNAEVKKVLGNPSNEEMNAKKIEFEQFLPMLQAISNNKDQGTYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALMAGQEDSNGCINYEAFVKHIMSI Regulatory light chain of myosin. Does not bind calcium mint hspb1_human Heat shock protein beta-1 HSPB1 HSP27 HSP28 Heat shock 27 kDa protein Stress-responsive protein 27 Estrogen-regulated 24 kDa protein 28 kDa heat shock protein protein protein human Homo sapiens Human MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK 1B4DC44A6F6606D5 hspb1-myl1-2 730537 myss_rabit Myosin subfragment 1 (S1) 730540 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false myl1_rabit LC1 (S1) 730541 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified hspb1_human Hsp27 730542 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association false false false F3 Interaction occurs only if S1 is thermally denatured. Heat shock temperature induces S1 aggregation. Hsp27 suppresses in a concentration-dependent manner the heat-induced aggregation of S1 mint hspb1-myl1-2 730537 myss_rabit Myosin subfragment 1 (S1) 730540 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false myl1_rabit LC1 (S1) 730541 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified hspb1_human Hsp27 730542 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P04792:p.Ser78Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P04792:p.Ser15Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P04792:p.Ser82Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false F3 Interaction occurs only if S1 is thermally denatured. Heat shock temperature induces S1 aggregation. Hsp27-3D, more than Hsp27 wt, suppresses in a concentration-dependent manner the heat-induced aggregation of S1 mint hspb1-myl1-2 730538 myl1_rabit LC1 (S1) 730541 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified myss_rabit Myosin subfragment 1 (S1) 730540 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false hspb1_human Hsp27 730542 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association false false false F4 Interaction occurs only if S1 is thermally denatured. Heat shock temperature induces S1 aggregation. Hsp27 suppresses in a concentration-dependent manner the heat-induced aggregation of S1 mint hspb1-myl1-2 730538 myl1_rabit LC1 (S1) 730541 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified myss_rabit Myosin subfragment 1 (S1) 730540 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false hspb1_human Hsp27 730542 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P04792:p.Ser15Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P04792:p.Ser78Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P04792:p.Ser82Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false F4 Interaction occurs only if S1 is thermally denatured. Heat shock temperature induces S1 aggregation. Hsp27-3D, more than Hsp27 wt, suppresses in a concentration-dependent manner the heat-induced aggregation of S1 mint hspb1-myl1-2 730539 myl1_rabit LC1 (S1) 730541 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified myss_rabit Myosin subfragment 1 (S1) 730540 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false hspb1_human Hsp27 730542 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P04792:p.Ser82Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P04792:p.Ser15Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P04792:p.Ser78Asp mutation increasing interaction mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false colocalization colocalization false false false F5B F5C F5D F5E Heat shock temperature induces S1 aggregation. Hsp27-3D suppresses in a concentration-dependent manner the heat-induced aggregation of S1 mint