P35749 · MYH11_HUMAN
- ProteinMyosin-11
- GeneMYH11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1972 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | melanosome | |
Cellular Component | muscle myosin complex | |
Cellular Component | myosin filament | |
Cellular Component | myosin II complex | |
Molecular Function | actin filament binding | |
Molecular Function | ATP binding | |
Molecular Function | calmodulin binding | |
Molecular Function | microfilament motor activity | |
Molecular Function | structural constituent of muscle | |
Biological Process | actomyosin structure organization | |
Biological Process | cardiac muscle cell development | |
Biological Process | elastic fiber assembly | |
Biological Process | skeletal muscle myosin thick filament assembly | |
Biological Process | smooth muscle contraction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyosin-11
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP35749
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Aortic aneurysm, familial thoracic 4 (AAT4)
- Note
- DescriptionA disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.
- See alsoMIM:132900
Natural variants in AAT4
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_031734 | 1241-1264 | missing | in AAT4 | |
VAR_031735 | 1758 | R>Q | in AAT4; dbSNP:rs142546324 |
Megacystis-microcolon-intestinal hypoperistalsis syndrome 2 (MMIHS2)
- Note
- DescriptionA form of megacystis-microcolon-intestinal hypoperistalsis syndrome, a congenital visceral myopathy primarily affecting females, and characterized by loss of smooth muscle contraction in the bladder and intestine. Affected individuals present at birth with functional obstruction of intestine, microcolon, dilation of bladder, and secondary hydronephrosis. The majority of cases have a fatal outcome due to malnutrition and sepsis, followed by multiorgan failure. MMIHS2 inheritance is autosomal recessive.
- See alsoMIM:619351
Natural variants in MMIHS2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_085645 | 677 | R>H | in MMIHS2 | |
VAR_085646 | 1200-1972 | missing | in MMIHS2 |
Visceral myopathy 2 (VSCM2)
- Note
- DescriptionA form of visceral myopathy, a gastrointestinal pseudo-obstruction disorder characterized by impaired function of enteric smooth muscle cells, intestinal dysmotility and paresis, severe abdominal pain, and malnutrition. The disease shows inter- and intrafamilial variability. VSCM2 inheritance is autosomal dominant.
- See alsoMIM:619350
Natural variants in VSCM2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_085647 | 1555 | L>V | in VSCM2; uncertain significance |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_085875 | 616 | ||||
Sequence: A → G | ||||||
Natural variant | VAR_085645 | 677 | in MMIHS2 | |||
Sequence: R → H | ||||||
Natural variant | VAR_050205 | 1104 | in dbSNP:rs34263860 | |||
Sequence: A → T | ||||||
Natural variant | VAR_085646 | 1200-1972 | in MMIHS2 | |||
Sequence: Missing | ||||||
Natural variant | VAR_030239 | 1234 | in dbSNP:rs16967494 | |||
Sequence: A → T | ||||||
Natural variant | VAR_031734 | 1241-1264 | in AAT4 | |||
Sequence: Missing | ||||||
Natural variant | VAR_030240 | 1289 | in dbSNP:rs16967510 | |||
Sequence: V → A | ||||||
Natural variant | VAR_030241 | 1310 | in dbSNP:rs7196804 | |||
Sequence: V → M | ||||||
Natural variant | VAR_050206 | 1508 | in dbSNP:rs35176378 | |||
Sequence: M → V | ||||||
Natural variant | VAR_085647 | 1555 | in VSCM2; uncertain significance | |||
Sequence: L → V | ||||||
Natural variant | VAR_031735 | 1758 | in AAT4; dbSNP:rs142546324 | |||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 4,564 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000123424 | 1-1972 | UniProt | Myosin-11 | |||
Sequence: MAQKGQLSDDEKFLFVDKNFINSPVAQADWAAKRLVWVPSEKQGFEAASIKEEKGDEVVVELVENGKKVTVGKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIMAFQAMCRGYLARKAFAKRQQQLTAMKVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNETSFVPSRRSGGRRVIENADGSEEETDTRDADFNGTKASE | |||||||
Modified residue | 8 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 23 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 40 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 129 | UniProt | N6,N6,N6-trimethyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 371 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 548 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 559 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 589 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 637 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 638 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 641 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 643 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 687 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 883 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 998 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1009 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1034 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1121 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1162 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1177 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1189 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1291 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1312 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1314 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1315 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1347 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1374 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1385 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1408 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1635 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1667 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1684 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1684 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1719 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1720 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1722 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1722 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1756 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1770 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1935 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1954 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1954 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1958 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1958 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1971 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1971 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P35749 | MYL12B O14950 | 2 | EBI-1052928, EBI-1642165 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-81 | Myosin N-terminal SH3-like | ||||
Sequence: AAKRLVWVPSEKQGFEAASIKEEKGDEVVVELVENGKKVTVGKDDIQKMNP | ||||||
Domain | 85-783 | Myosin motor | ||||
Sequence: SKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERD | ||||||
Region | 661-683 | Actin-binding | ||||
Sequence: LGKLMTTLRNTTPNFVRCIIPNH | ||||||
Region | 762-776 | Actin-binding | ||||
Sequence: RIGQSKIFFRTGVLA | ||||||
Domain | 786-815 | IQ | ||||
Sequence: ITDVIMAFQAMCRGYLARKAFAKRQQQLTA | ||||||
Coiled coil | 844-1934 | |||||
Sequence: LLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNET | ||||||
Region | 858-882 | Disordered | ||||
Sequence: EDELQKTKERQQKAENELKELEQKH | ||||||
Region | 1744-1800 | Disordered | ||||
Sequence: ELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSK | ||||||
Compositional bias | 1761-1787 | Polar residues | ||||
Sequence: KATQQAEQLSNELATERSTAQKNESAR | ||||||
Compositional bias | 1866-1915 | Basic and acidic residues | ||||
Sequence: EQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNE | ||||||
Region | 1866-1972 | Disordered | ||||
Sequence: EQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNETSFVPSRRSGGRRVIENADGSEEETDTRDADFNGTKASE | ||||||
Region | 1935-1972 | C-terminal | ||||
Sequence: SFVPSRRSGGRRVIENADGSEEETDTRDADFNGTKASE | ||||||
Compositional bias | 1945-1972 | Basic and acidic residues | ||||
Sequence: RRVIENADGSEEETDTRDADFNGTKASE |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
P35749-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsSM-A
- Length1,972
- Mass (Da)227,339
- Last updated2001-04-27 v3
- Checksum67665BB2AECE1277
P35749-2
- Name2
- SynonymsSM-B1
- NoteThis isoform with a 7 AA insert in the head domain is predominantly expressed in rapidly contracting phasic muscles.
- Differences from canonical
- 211-211: T → TQGPSFAY
P35749-3
- Name3
- SynonymsSM-B2
- NoteThis isoform with a 7 AA insert in the head domain is predominantly expressed in rapidly contracting phasic muscles.
- Differences from canonical
- 211-211: T → TQGPSFAY
- 1930-1972: RGNETSFVPSRRSGGRRVIENADGSEEETDTRDADFNGTKASE → GPPPQETSQ
P35749-4
- Name4
- Differences from canonical
- 1930-1972: RGNETSFVPSRRSGGRRVIENADGSEEETDTRDADFNGTKASE → GPPPQETSQ
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A494C024 | A0A494C024_HUMAN | MYH11 | 635 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043017 | 211 | in isoform 2 and isoform 3 | |||
Sequence: T → TQGPSFAY | ||||||
Sequence conflict | 887-889 | in Ref. 9; D10667 | ||||
Sequence: EEK → NSE | ||||||
Sequence conflict | 1558 | in Ref. 9; D10667 | ||||
Sequence: T → S | ||||||
Sequence conflict | 1610-1611 | in Ref. 9; D10667 | ||||
Sequence: KQ → NE | ||||||
Compositional bias | 1761-1787 | Polar residues | ||||
Sequence: KATQQAEQLSNELATERSTAQKNESAR | ||||||
Sequence conflict | 1786 | in Ref. 10; CAA49154 | ||||
Sequence: A → S | ||||||
Compositional bias | 1866-1915 | Basic and acidic residues | ||||
Sequence: EQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNE | ||||||
Alternative sequence | VSP_043018 | 1930-1972 | in isoform 3 and isoform 4 | |||
Sequence: RGNETSFVPSRRSGGRRVIENADGSEEETDTRDADFNGTKASE → GPPPQETSQ | ||||||
Compositional bias | 1945-1972 | Basic and acidic residues | ||||
Sequence: RRVIENADGSEEETDTRDADFNGTKASE | ||||||
Sequence conflict | 1958 | in Ref. 9; D10667 | ||||
Sequence: T → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY520816 EMBL· GenBank· DDBJ | AAS98910.1 EMBL· GenBank· DDBJ | mRNA | ||
AY520817 EMBL· GenBank· DDBJ | AAS98911.1 EMBL· GenBank· DDBJ | mRNA | ||
AF001548 EMBL· GenBank· DDBJ | AAC31665.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U91323 EMBL· GenBank· DDBJ | AAC35212.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB020673 EMBL· GenBank· DDBJ | BAA74889.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
GU143399 EMBL· GenBank· DDBJ | ACZ58373.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
GU143400 EMBL· GenBank· DDBJ | ACZ58374.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC024120 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC026401 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC130651 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471226 EMBL· GenBank· DDBJ | EAW53924.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471226 EMBL· GenBank· DDBJ | EAW53926.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC101677 EMBL· GenBank· DDBJ | AAI01678.1 EMBL· GenBank· DDBJ | mRNA | ||
BC104906 EMBL· GenBank· DDBJ | AAI04907.1 EMBL· GenBank· DDBJ | mRNA | ||
BC143364 EMBL· GenBank· DDBJ | AAI43365.1 EMBL· GenBank· DDBJ | mRNA | ||
D10667 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
X69292 EMBL· GenBank· DDBJ | CAA49154.1 EMBL· GenBank· DDBJ | mRNA |