P35580 · MYH10_HUMAN
- ProteinMyosin-10
- GeneMYH10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1976 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | actomyosin | |
Cellular Component | cell cortex | |
Cellular Component | cleavage furrow | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | lamellipodium | |
Cellular Component | midbody | |
Cellular Component | myosin complex | |
Cellular Component | myosin filament | |
Cellular Component | myosin II complex | |
Cellular Component | myosin II filament | |
Cellular Component | nucleus | |
Cellular Component | postsynaptic actin cytoskeleton | |
Cellular Component | stress fiber | |
Molecular Function | actin binding | |
Molecular Function | actin filament binding | |
Molecular Function | ADP binding | |
Molecular Function | ATP binding | |
Molecular Function | calmodulin binding | |
Molecular Function | microfilament motor activity | |
Molecular Function | mRNA 5'-UTR binding | |
Molecular Function | RNA stem-loop binding | |
Biological Process | actin filament-based movement | |
Biological Process | actomyosin structure organization | |
Biological Process | cell adhesion | |
Biological Process | mitotic cytokinesis | |
Biological Process | positive regulation of protein secretion | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyosin-10
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP35580
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_078649 | 270 | found in a patient with severe intellectual disease, microcephaly and feeding difficulties as well as cerebral atrophy; likely pathogenic; dbSNP:rs727504231 | |||
Sequence: R → C | ||||||
Natural variant | VAR_078650 | 908-1976 | found in a patient with intrauterine growth restriction, microcephaly, developmental delay, failure to thrive, congenital bilateral hip dysplasia, cerebral and cerebellar atrophy, hydrocephalus and congenital diaphragmatic hernia; likely pathogenic | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,771 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 (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000123421 | 1-1976 | UniProt | Myosin-10 | |||
Sequence: MAQRTGLEDPERYLFVDRAVIYNPATQADWTAKKLVWIPSERHGFEAASIKEERGDEVMVELAENGKKAMVNKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAKKEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQRLEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRGGPISFSSSRSGRRQLHLEGASLELSDDDTESKTSDVNETQPPQSE | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 18 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 214 | UniProt | In isoform P35580-2; Phosphoserine | ||||
Sequence: L | |||||||
Modified residue | 214 | UniProt | In isoform P35580-4; Phosphoserine | ||||
Sequence: L | |||||||
Modified residue | 442 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 641 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 929 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1012 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1013 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1145 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1145 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1203 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1241 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1293 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1301 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1645 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1930 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 1935 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1935 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1937 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1937 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1938 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1938 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1939 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1939 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1940 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 1952 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1952 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1956 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1956 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1960 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1960 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1962 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1975 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1975 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with ECPAS (PubMed:20682791).
Interacts with KIF26B (By similarity).
Interacts with LARP6 (PubMed:20603131).
Interacts with MCC (PubMed:22480440).
Interacts with CFAP95 (PubMed:28345668).
Protein-protein interaction databases
Chemistry
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: TAKKLVWIPSERHGFEAASIKEERGDEVMVELAENGKKAMVNKDDIQKMNP | ||||||
Domain | 85-783 | Myosin motor | ||||
Sequence: SKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD | ||||||
Region | 661-683 | Actin-binding | ||||
Sequence: LTKLMATLRNTNPNFVRCIIPNH | ||||||
Domain | 786-815 | IQ | ||||
Sequence: ITDIIIFFQAVCRGYLARKAFAKKQQQLSA | ||||||
Coiled coil | 845-1976 | |||||
Sequence: LQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIDELKLQLAKKEEELQGALARGDDETLHKNNALKVVRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEEETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKASKLQNELDNVSTLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDAEALSQRLEEKALAYDKLEKTKNRLQQELDDLTVDLDHQRQVASNLEKKQKKFDQLLAEEKSISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLIKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEITNSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNAELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRGGPISFSSSRSGRRQLHLEGASLELSDDDTESKTSDVNETQPPQSE | ||||||
Region | 1127-1147 | Disordered | ||||
Sequence: FESEKASRNKAEKQKRDLSEE | ||||||
Compositional bias | 1697-1717 | Basic and acidic residues | ||||
Sequence: ASSERARRHAEQERDELADEI | ||||||
Region | 1697-1728 | Disordered | ||||
Sequence: ASSERARRHAEQERDELADEITNSASGKSALL | ||||||
Compositional bias | 1872-1915 | Basic and acidic residues | ||||
Sequence: MEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE | ||||||
Region | 1872-1976 | Disordered | ||||
Sequence: MEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRGGPISFSSSRSGRRQLHLEGASLELSDDDTESKTSDVNETQPPQSE | ||||||
Compositional bias | 1950-1965 | Basic and acidic residues | ||||
Sequence: GASLELSDDDTESKTS |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
P35580-1
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
- Length1,976
- Mass (Da)228,999
- Last updated2008-11-25 v3
- ChecksumA7C91944EBC2368F
P35580-2
- Name2
- Differences from canonical
- 211-211: P → PQESPKPVKHQSGSLLY
P35580-3
- Name3
- Differences from canonical
- 621-621: D → DEIQNIQRASFYDSVSGLHEPP
P35580-4
- Name4
P35580-5
- Name5
- Differences from canonical
- 211-211: P → PESPKPVKHQ
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5KSC2 | A0A8I5KSC2_HUMAN | MYH10 | 199 | ||
A0A8I5KTT7 | A0A8I5KTT7_HUMAN | MYH10 | 207 | ||
A0A8I5KZ38 | A0A8I5KZ38_HUMAN | MYH10 | 1986 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_022013 | 211 | in isoform 2 | |||
Sequence: P → PQESPKPVKHQSGSLLY | ||||||
Alternative sequence | VSP_046033 | 211 | in isoform 4 | |||
Sequence: P → PQESPKPVKHQ | ||||||
Alternative sequence | VSP_054974 | 211 | in isoform 5 | |||
Sequence: P → PESPKPVKHQ | ||||||
Alternative sequence | VSP_022014 | 621 | in isoform 3 and isoform 4 | |||
Sequence: D → DEIQNIQRASFYDSVSGLHEPP | ||||||
Sequence conflict | 800 | in Ref. 1; AAA99177 | ||||
Sequence: Y → C | ||||||
Sequence conflict | 943-944 | in Ref. 5; AAH08968 | ||||
Sequence: NE → KK | ||||||
Sequence conflict | 1429 | in Ref. 5; AAI17691 | ||||
Sequence: L → P | ||||||
Compositional bias | 1697-1717 | Basic and acidic residues | ||||
Sequence: ASSERARRHAEQERDELADEI | ||||||
Sequence conflict | 1751 | in Ref. 9; AAB28952 | ||||
Sequence: N → D | ||||||
Compositional bias | 1872-1915 | Basic and acidic residues | ||||
Sequence: MEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE | ||||||
Compositional bias | 1950-1965 | Basic and acidic residues | ||||
Sequence: GASLELSDDDTESKTS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M69181 EMBL· GenBank· DDBJ | AAA99177.1 EMBL· GenBank· DDBJ | mRNA | ||
AB210026 EMBL· GenBank· DDBJ | BAE06108.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC011061 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC025518 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC026130 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471108 EMBL· GenBank· DDBJ | EAW90046.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90047.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90048.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90049.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000280 EMBL· GenBank· DDBJ | AAH00280.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008968 EMBL· GenBank· DDBJ | AAH08968.1 EMBL· GenBank· DDBJ | mRNA | ||
BC117690 EMBL· GenBank· DDBJ | AAI17691.1 EMBL· GenBank· DDBJ | mRNA | ||
BC117691 EMBL· GenBank· DDBJ | AAI17692.1 EMBL· GenBank· DDBJ | mRNA | ||
BC144668 EMBL· GenBank· DDBJ | AAI44669.1 EMBL· GenBank· DDBJ | mRNA | ||
BC150634 EMBL· GenBank· DDBJ | AAI50635.1 EMBL· GenBank· DDBJ | mRNA | ||
U15618 EMBL· GenBank· DDBJ | AAA87712.1 EMBL· GenBank· DDBJ | mRNA | ||
S67247 EMBL· GenBank· DDBJ | AAB28952.1 EMBL· GenBank· DDBJ | mRNA |