| IED ID | IndEnz0002001779 |
| Enzyme Type ID | protease001779 |
| Protein Name |
Titin EC 2.7.11.1 Connectin |
| Gene Name | Ttn |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | !!! TO LONG IT DOES NOT FIT IN EXCELL, NOT REPRESENTABLE IN EXCELL !!! |
| Enzyme Length | 35213 |
| Uniprot Accession Number | A2ASS6 |
| Absorption | |
| Active Site | ACT_SITE 33160; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P28523, ECO:0000255|PROSITE-ProRule:PRU00159" |
| Activity Regulation | ACTIVITY REGULATION: Full activation of the protein kinase domain requires both phosphorylation of Tyr-33203, preventing it from blocking the catalytic aspartate residue, and binding of Ca/CALM to the C-terminal regulatory tail of the molecule which results in ATP binding to the kinase. {ECO:0000250|UniProtKB:Q8WZ42}. |
| Binding Site | BINDING 33069; /note="ATP"; /evidence="ECO:0000250|UniProtKB:P28523, ECO:0000255|PROSITE-ProRule:PRU00159" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q8WZ42}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q8WZ42}; |
| DNA Binding | |
| EC Number | 2.7.11.1 |
| Enzyme Function | FUNCTION: Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase. {ECO:0000250|UniProtKB:Q8WZ42, ECO:0000269|PubMed:16702235, ECO:0000269|PubMed:17261657}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 33046..33054; /note="ATP"; /evidence="ECO:0000250|UniProtKB:P28523, ECO:0000255|PROSITE-ProRule:PRU00159" |
| Features | Active site (1); Alternative sequence (4); Binding site (1); Chain (1); Coiled coil (2); Compositional bias (51); Disulfide bond (45); Domain (277); Modified residue (63); Nucleotide binding (1); Region (33); Repeat (144) |
| Keywords | 3D-structure;ATP-binding;Alternative splicing;Calcium;Calmodulin-binding;Coiled coil;Cytoplasm;Direct protein sequencing;Disulfide bond;Immunoglobulin domain;Kelch repeat;Kinase;Magnesium;Metal-binding;Methylation;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;TPR repeat;Transferase;WD repeat |
| Interact With | Q70IV5 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q8WZ42}. |
| Modified Residue | MOD_RES 263; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 264; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 266; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 278; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 286; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 296; /note="Asymmetric dimethylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 296; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 299; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 301; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 304; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 307; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 322; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 756; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1251; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1415; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1420; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1424; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1429; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1434; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 2078; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 2080; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 3516; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 3784; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 8387; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 9144; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 9164; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8WZ42"; MOD_RES 9168; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q8WZ42"; MOD_RES 9459; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 10281; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 12869; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 12884; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 12972; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 13904; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 21152; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 21895; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 21980; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 22390; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 23387; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8WZ42"; MOD_RES 23396; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q8WZ42"; MOD_RES 25920; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 32870; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 33203; /note="Phosphotyrosine"; /evidence="ECO:0000250|UniProtKB:Q8WZ42"; MOD_RES 33859; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 33861; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 33875; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 33880; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 33915; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 34009; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 34292; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 34464; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 34467; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 34470; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 34476; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 34481; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 34756; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES A2ASS6-3:3432; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES A2ASS6-3:3636; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES A2ASS6-3:3678; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES A2ASS6-3:3763; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES A2ASS6-3:3827; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES A2ASS6-3:3836; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES A2ASS6-3:4672; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES A2ASS6-3:4720; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079" |
| Post Translational Modification | PTM: Autophosphorylated. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 6YJ0; |
| Mapped Pubmed ID | 10330145; 10481174; 10607827; 10929709; 11044609; 11130978; 11217851; 11717165; 11829483; 11956126; 12355177; 12464612; 12466851; 12651156; 14600266; 14610273; 14741210; 15136139; 15138196; 15475267; 15967462; 16115818; 16141072; 16337936; 16470336; 16481394; 16717059; 16881058; 17038546; 17360664; 17522126; 17664162; 17904117; 18310072; 18579686; 18753318; 18799693; 18849322; 19091769; 19406126; 19679835; 19679839; 19683008; 19850579; 20442316; 20507834; 20855473; 20860623; 21041693; 21255582; 21267068; 21289070; 2129545; 21536590; 21555460; 21659647; 21677750; 21708170; 21835910; 21840390; 21943419; 2203673; 22160926; 22778266; 22846424; 23047121; 23060211; 23220127; 23246787; 23266827; 23283722; 23297410; 23709671; 23824195; 24470484; 24470489; 24500875; 24515436; 24565863; 24599837; 24603287; 24680892; 24725620; 24850911; 24855944; 24952961; 24982444; 25125171; 25246556; 25264194; 25447537; 25450617; 25573826; 25759365; 25877298; 26039991; 26075897; 26272747; 26394485; 26504781; 26682816; 26708556; 2680424; 2693040; 26944495; 27120339; 27171814; 27470639; 27689697; 27889803; 27914791; 27986994; 27994045; 28164238; 28353642; 28476659; 28939561; 29051486; 29078393; 29360543; 29978560; 30121012; 30475793; 30523116; 30565562; 30567709; 30700140; 30987448; 31015287; 31097600; 31158359; 31421188; 31628386; 31688894; 31757849; 31776291; 31862847; 32345978; 32376900; 32492876; 32547410; 32561764; 32619437; 32900999; 32929035; 32994313; 33357376; 33397958; 33414188; 33637999; 33811919; 33854441; 34401916; 7720554; 7720708; 7896287; 8307566; 8359022; 8486363; 8604138; 8618961; 9040657; 9618202; 9817758; |
| Motif | |
| Gene Encoded By | |
| Mass | 3,906,488 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17989; RHEA:46608 |
| Cross Reference Brenda |