G3UW82 · MYH2_MOUSE
- ProteinMyosin-2
- GeneMyh2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1942 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | A band | |
Cellular Component | actomyosin contractile ring | |
Cellular Component | cell-cell junction | |
Cellular Component | cytoplasm | |
Cellular Component | Golgi apparatus | |
Cellular Component | muscle myosin complex | |
Cellular Component | myofibril | |
Cellular Component | myosin filament | |
Cellular Component | myosin II complex | |
Molecular Function | actin filament binding | |
Molecular Function | ATP binding | |
Molecular Function | microfilament motor activity | |
Biological Process | actin-mediated cell contraction | |
Biological Process | muscle contraction | |
Biological Process | plasma membrane repair | |
Biological Process | response to activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyosin-2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionG3UW82
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Thick filaments of the myofibrils.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000460618 | 1-1942 | Myosin-2 | |||
Sequence: MSSDAEMAVFGEAAPYLRKSEKERIEAQNRPFDAKTSVFVAEPKESFVKGTIQSKDAGKVTVKTEAGATLTVKEDQIFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSVKTLAYLFSGAQTAEAEASSGGAAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQAMCRGFLARVEYQKMVERRESIFCIQYNIRAFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDDLAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE | ||||||
Modified residue | 64 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 69 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 389 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 419 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 625 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 760 | Pros-methylhistidine | ||||
Sequence: H | ||||||
Modified residue | 1095 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1099 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1165 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1240 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1244 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1246 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1258 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1264 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1289 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1291 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1295 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1306 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1309 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1467 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1470 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1477 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1495 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1498 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1504 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1517 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1520 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1557 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1577 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1603 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1606 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1717 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1729 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1733 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1739 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1742 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in type 2a myofibers in the tibialis anterior and soleus muscles (at protein level).
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 33-82 | Myosin N-terminal SH3-like | ||||
Sequence: DAKTSVFVAEPKESFVKGTIQSKDAGKVTVKTEAGATLTVKEDQIFPMNP | ||||||
Domain | 86-785 | Myosin motor | ||||
Sequence: DKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSVKTLAYLFSGAQTAEAEASSGGAAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRD | ||||||
Region | 662-684 | Actin-binding | ||||
Sequence: LNKLMTNLRSTHPHFVRCIIPNE | ||||||
Domain | 788-817 | IQ | ||||
Sequence: LAQLITRTQAMCRGFLARVEYQKMVERRES | ||||||
Coiled coil | 849-1930 | |||||
Sequence: SAETEKEMATMKEEFQKTKDDLAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKIQHELEEAEERADIAESQVNKLRVK | ||||||
Compositional bias | 1130-1158 | Basic and acidic residues | ||||
Sequence: EAERASRAKAEKQRSDLSRELEEISERLE | ||||||
Region | 1130-1175 | Disordered | ||||
Sequence: EAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKRE |
Domain
The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.
Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2).
Sequence similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,942
- Mass (Da)223,219
- Last updated2011-11-16 v1
- Checksum9087D534CB3C4AD7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1130-1158 | Basic and acidic residues | ||||
Sequence: EAERASRAKAEKQRSDLSRELEEISERLE |
Keywords
- Technical term