| IED ID | IndEnz0002001778 |
| Enzyme Type ID | protease001778 |
| Protein Name |
Titin EC 2.7.11.1 Connectin Rhabdomyosarcoma antigen MU-RMS-40.14 |
| Gene Name | TTN |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | !!! TO LONG IT DOES NOT FIT IN EXCELL, NOT REPRESENTABLE IN EXCELL !!! |
| Enzyme Length | 34350 |
| Uniprot Accession Number | Q8WZ42 |
| Absorption | |
| Active Site | ACT_SITE 32298; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| Activity Regulation | ACTIVITY REGULATION: Full activation of the protein kinase domain requires both phosphorylation of Tyr-32341, 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:0000269|PubMed:9804419}. |
| Binding Site | BINDING 32207; /note=ATP; /evidence=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; 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; |
| 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:0000269|PubMed:9804419}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 32184..32192; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| Features | Active site (1); Alternative sequence (24); Beta strand (202); Binding site (1); Chain (1); Coiled coil (4); Compositional bias (37); Disulfide bond (46); Domain (285); Frameshift (2); Helix (37); Modified residue (15); Mutagenesis (2); Natural variant (297); Nucleotide binding (1); Region (33); Repeat (38); Sequence caution (2); Sequence conflict (96); Turn (10) |
| Keywords | 3D-structure;ATP-binding;Alternative splicing;Calcium;Calmodulin-binding;Cardiomyopathy;Coiled coil;Cytoplasm;Direct protein sequencing;Disease variant;Disulfide bond;Immunoglobulin domain;Kinase;Limb-girdle muscular dystrophy;Magnesium;Metal-binding;Myofibrillar myopathy;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase |
| Interact With | P12814; P35609; P0DP24; P20807; O75953; O75923; P06733; Q14324; Q13203; P20929; Q5VST9; O75147; O15061; O15273; Q969Q1; Itself; O15273; Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16410549}. Nucleus {ECO:0000269|PubMed:16410549}. |
| Modified Residue | MOD_RES 263; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 265; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 267; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 6920; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 9122; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 11503; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 12007; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 12009; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 12022; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 30443; /note=Phosphothreonine; /evidence=ECO:0000250; MOD_RES 32341; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:9804419; MOD_RES 33245; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 33247; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 33602; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 33614; /note=Phosphoserine; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Autophosphorylated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (10); Electron microscopy (1); X-ray crystallography (37) |
| Cross Reference PDB | 1BPV; 1G1C; 1NCT; 1NCU; 1TIT; 1TIU; 1TKI; 1TNM; 1TNN; 1WAA; 1YA5; 2A38; 2BK8; 2F8V; 2ILL; 2J8H; 2J8O; 2NZI; 2RQ8; 2WP3; 2WWK; 2WWM; 2Y9R; 3B43; 3KNB; 3LCY; 3LPW; 3PUC; 3Q5O; 3QP3; 4C4K; 4JNW; 4O00; 4QEG; 4UOW; 5BS0; 5JDD; 5JDE; 5JDJ; 5JOE; 6DL4; 6H4L; 6HCI; 6I0Y; 6SDB; 6YGN; 7AHS; 7NIP; |
| Mapped Pubmed ID | 10747208; 11101506; 11448995; 11746675; 11799131; 11800567; 11812150; 12198551; 12221049; 12414993; 12785101; 12816538; 12865504; 14593205; 14630798; 15174051; 15175163; 15211512; 15238456; 15322090; 15345656; 15507486; 15582318; 15632200; 15849252; 16341830; 16465472; 16531234; 16627476; 16713295; 16733766; 16766517; 16902413; 16949617; 16962094; 16962974; 17028145; 17215480; 17327674; 17353931; 17366640; 17496052; 17522126; 17574571; 17620599; 17669421; 17721511; 17890397; 17920806; 18157088; 18212128; 18519573; 18654987; 18948003; 19003986; 19013176; 19023132; 19179657; 19282282; 19282960; 19608031; 19622741; 19651040; 19679839; 19911250; 19913121; 20031603; 20095049; 20133654; 20149875; 20171214; 20360068; 20414336; 20414364; 20467438; 20479164; 20489725; 20542041; 20562859; 20571043; 20618440; 20625501; 20628086; 20808825; 20860622; 20860623; 20926005; 20952631; 21041693; 21050039; 21150319; 21257761; 21728583; 21741357; 21810661; 22162032; 22223454; 22335739; 22466703; 22475360; 22523089; 22555292; 22577215; 22577218; 22768802; 22778266; 23063534; 23220127; 23224300; 23283722; 23414517; 23418287; 23439446; 23446887; 23486992; 23514108; 23602568; 23764881; 23902751; 23907728; 23975875; 24105469; 24189400; 24315344; 24395473; 24458745; 24470489; 24503780; 24558114; 24606918; 24625729; 24630725; 24636144; 24850911; 25077715; 25152160; 25421125; 25447537; 25490259; 25589632; 25604459; 25637629; 25739468; 25877298; 26024954; 26315439; 26392295; 26394485; 26516846; 26567375; 26682816; 26735901; 26746183; 26758806; 26777568; 27021163; 27115767; 27321809; 27350668; 27496873; 27531639; 27544385; 27625337; 27625338; 27683155; 27736720; 27796757; 27813223; 27854229; 27869827; 27991570; 28045975; 28223422; 28295036; 28436080; 28581678; 28700999; 28704380; 28712031; 28822653; 29057560; 29093449; 29109008; 29175173; 29343782; 29377983; 29386531; 29435569; 29472025; 29518215; 29523065; 29568937; 29575618; 29750433; 29760016; 29997384; 30062220; 30289063; 30332462; 30354343; 30413621; 30535219; 30666435; 30681174; 30778519; 30810839; 30858397; 30947911; 30959043; 30978303; 30989819; 30998980; 31112426; 31209521; 31216868; 31295985; 31353864; 31421188; 31484291; 31489791; 31587567; 31610194; 31638414; 31660661; 31664938; 31705051; 31712709; 31833097; 31856237; 31909301; 32039858; 32164899; 32371228; 32396765; 32492876; 32523538; 32553263; 32572052; 32815318; 32945477; 32955937; 32964742; 33190517; 33360523; 33373724; 33449170; 33610015; 33647290; 33678800; 33836065; 33870097; 33974263; 34108290; 34152365; 34201072; 34315225; 34402565; 7607248; 8805538; 9020985; 9501083; |
| Motif | |
| Gene Encoded By | |
| Mass | 3,816,030 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17989; RHEA:46608 |
| Cross Reference Brenda | 2.7.11.1; |