Q92614 · MY18A_HUMAN
- ProteinUnconventional myosin-XVIIIa
- GeneMYO18A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2054 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160).
May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity).
Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346).
Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:16087679, PubMed:21123169).
Strongly enhances natural killer cell cytotoxicity (PubMed:27467939).
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUnconventional myosin-XVIIIa
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ92614
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation (By similarity).
Isoform 1
Isoform 2
Isoform 5
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 114-115 | No effect on interaction with actin. | ||||
Sequence: RG → AA | ||||||
Mutagenesis | 117-118 | Abolishes interaction with actin. | ||||
Sequence: VL → AA | ||||||
Natural variant | VAR_030585 | 958 | in dbSNP:rs8076604 | |||
Sequence: A → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,159 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
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_0000123476 | 1-2054 | UniProt | Unconventional myosin-XVIIIa | |||
Sequence: MFNLMKKDKDKDGGRKEKKEKKEKKERMSAAELRSLEEMSLRRGFFNLNRSSKRESKTRLEISNPIPIKVASGSDLHLTDIDSDSNRGSVILDSGHLSTASSSDDLKGEEGSFRGSVLQRAAKFGSLAKQNSQMIVKRFSFSQRSRDESASETSTPSEHSAAPSPQVEVRTLEGQLVQHPGPGIPRPGHRSRAPELVTKKFPVDLRLPPVVPLPPPTLRELELQRRPTGDFGFSLRRTTMLDRGPEGQACRRVVHFAEPGAGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQPIPELSELSRSWLRSGEGPRREPSDAKTEEQIAAEEAWNETEKVWLVHRDGFSLASQLKSEELNLPEGKVRVKLDHDGAILDVDEDDVEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRSTSFRQGPEESGLGDGTGPKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGGSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVRSLARTDEARGLLWLLEEEALVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPHHFLLGHSHGTNWVEYNVTGWLNYTKQNPATQNAPRLLQDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWAGEPRSASSRRVSSSSELDLPSGDHCEAGLLQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIVVDERRAVEELLECLDLEKSSCCMGLSRVFFRAGTLARLEEQRDEQTSRNLTLFQAACRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRPLIEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKRKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAASDDGSLKSSSPTSYWKSLAPDRSDDEHDPLDNTSRPRYSHSYLSDSDTEAKLTETNA | |||||||
Modified residue | 35 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 35 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 52 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 72 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 74 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 74 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 79 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 83 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 83 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 98 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 99 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 99 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 102 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 103 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 112 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 140 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 142 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 145 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 145 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 157 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 157 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 160 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 160 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 164 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 164 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 228 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 234 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 403 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 728 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 736 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 806 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 980 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 982 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 985 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 987 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 987 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1008 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1067 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1067 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1068 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1068 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1070 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1070 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1076 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1309 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1501 | UniProt | In isoform Q92614-5; Phosphoserine | ||||
Sequence: Q | |||||||
Modified residue (large scale data) | 1528 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1640 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1640 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1843 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1922 | UniProt | In isoform Q92614-3; Phosphoserine | ||||
Sequence: L | |||||||
Modified residue | 1942 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1942 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1959 | UniProt | In isoform Q92614-4; Phosphoserine | ||||
Sequence: Y | |||||||
Modified residue | 1970 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1970 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1974 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1974 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1998 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1998 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2002 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2002 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2005 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2006 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2006 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2007 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2007 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2014 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2014 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2020 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2020 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2030 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2031 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2035 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 2035 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 2036 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2036 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2038 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2039 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 2041 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2041 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2043 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2043 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2045 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2045 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Isoform 5 interacts with CD11B (PubMed:25965346).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q92614 | GOLPH3 Q9H4A6 | 6 | EBI-949059, EBI-2465479 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-34 | Disordered | ||||
Sequence: MFNLMKKDKDKDGGRKEKKEKKEKKERMSAAELR | ||||||
Region | 1-398 | Mediates nucleotide-independent binding to F-actin and interaction with GOLPH3 | ||||
Sequence: MFNLMKKDKDKDGGRKEKKEKKEKKERMSAAELRSLEEMSLRRGFFNLNRSSKRESKTRLEISNPIPIKVASGSDLHLTDIDSDSNRGSVILDSGHLSTASSSDDLKGEEGSFRGSVLQRAAKFGSLAKQNSQMIVKRFSFSQRSRDESASETSTPSEHSAAPSPQVEVRTLEGQLVQHPGPGIPRPGHRSRAPELVTKKFPVDLRLPPVVPLPPPTLRELELQRRPTGDFGFSLRRTTMLDRGPEGQACRRVVHFAEPGAGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQPIPELSELSRSWLRSGEGPRREPSDAKTEEQIAAEEAWNETEKVWLVHRDGFSLASQLKSEELNLPEGKVRVKLDHDGAILDVDEDDVEK | ||||||
Motif | 114-118 | Interaction with actin | ||||
Sequence: RGSVL | ||||||
Compositional bias | 140-164 | Polar residues | ||||
Sequence: SFSQRSRDESASETSTPSEHSAAPS | ||||||
Region | 140-167 | Disordered | ||||
Sequence: SFSQRSRDESASETSTPSEHSAAPSPQV | ||||||
Domain | 220-311 | PDZ | ||||
Sequence: ELELQRRPTGDFGFSLRRTTMLDRGPEGQACRRVVHFAEPGAGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQPIP | ||||||
Region | 318-338 | Disordered | ||||
Sequence: RSWLRSGEGPRREPSDAKTEE | ||||||
Compositional bias | 322-338 | Basic and acidic residues | ||||
Sequence: RSGEGPRREPSDAKTEE | ||||||
Domain | 349-401 | Myosin N-terminal SH3-like | ||||
Sequence: TEKVWLVHRDGFSLASQLKSEELNLPEGKVRVKLDHDGAILDVDEDDVEKANA | ||||||
Domain | 405-1185 | Myosin motor | ||||
Sequence: DRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRSTSFRQGPEESGLGDGTGPKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGGSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVRSLARTDEARGLLWLLEEEALVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPHHFLLGHSHGTNWVEYNVTGWLNYTKQNPATQNAPRLLQDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWAGEPRSASSRRVSSSSELDLPSGDHCEAGLLQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIVVDERRAVEELLECLDLEKSSCCMGLSRVFFRAGTLARLEEQRD | ||||||
Domain | 1188-1217 | IQ | ||||
Sequence: TSRNLTLFQAACRGYLARQHFKKRKIQDLA | ||||||
Coiled coil | 1246-1971 | |||||
Sequence: LIEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKRKNKLEGDSD | ||||||
Region | 1450-1480 | Disordered | ||||
Sequence: QVRNHELEKKQRRFDSELSQAHEEAQREKLQ | ||||||
Region | 1852-1901 | Disordered | ||||
Sequence: MEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKK | ||||||
Compositional bias | 1962-1985 | Basic and acidic residues | ||||
Sequence: RKNKLEGDSDVDSELEDRVDGVKS | ||||||
Region | 1962-2054 | Disordered | ||||
Sequence: RKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAASDDGSLKSSSPTSYWKSLAPDRSDDEHDPLDNTSRPRYSHSYLSDSDTEAKLTETNA | ||||||
Compositional bias | 1999-2014 | Polar residues | ||||
Sequence: DDGSLKSSSPTSYWKS | ||||||
Compositional bias | 2016-2031 | Basic and acidic residues | ||||
Sequence: APDRSDDEHDPLDNTS | ||||||
Compositional bias | 2032-2054 | Polar residues | ||||
Sequence: RPRYSHSYLSDSDTEAKLTETNA |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 6 isoforms produced by Alternative splicing.
Q92614-1
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
- SynonymsAlpha, SP-R210L
- Length2,054
- Mass (Da)233,115
- Last updated2003-07-25 v3
- Checksum52BFA0AA273E18F7
Q92614-2
- Name2
- SynonymsBeta
Q92614-3
- Name3
- Differences from canonical
- 1571-1607: Missing
- 1952-1966: Missing
Q92614-4
- Name4
- Differences from canonical
- 1952-1966: Missing
Q92614-5
- Name5
- SynonymsSP-R210S
- Differences from canonical
- 1-458: Missing
- 1952-1966: Missing
O95411-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameTIAF1
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
O95411 | TIAF1_HUMAN | MYO18A | 115 | ||
H0YEV9 | H0YEV9_HUMAN | MYO18A | 172 | ||
A0A1B0GV45 | A0A1B0GV45_HUMAN | MYO18A | 464 | ||
A0A1B0GWJ6 | A0A1B0GWJ6_HUMAN | MYO18A | 340 | ||
E9PN42 | E9PN42_HUMAN | MYO18A | 27 | ||
K7EKB3 | K7EKB3_HUMAN | MYO18A | 93 | ||
A0A994J771 | A0A994J771_HUMAN | MYO18A | 2051 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_007869 | 1-331 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023058 | 1-458 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 140-164 | Polar residues | ||||
Sequence: SFSQRSRDESASETSTPSEHSAAPS | ||||||
Compositional bias | 322-338 | Basic and acidic residues | ||||
Sequence: RSGEGPRREPSDAKTEE | ||||||
Alternative sequence | VSP_007870 | 332-333 | in isoform 2 | |||
Sequence: SD → MR | ||||||
Sequence conflict | 1014 | in Ref. 1; BAD66838 and 2; AAV80770 | ||||
Sequence: A → V | ||||||
Sequence conflict | 1020 | in Ref. 4; CAI45931 | ||||
Sequence: S → P | ||||||
Alternative sequence | VSP_007871 | 1571-1607 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 1757 | in Ref. 4; CAI45931 | ||||
Sequence: E → K | ||||||
Sequence conflict | 1889 | in Ref. 4; CAI45931 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_007872 | 1952-1966 | in isoform 3, isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 1962-1985 | Basic and acidic residues | ||||
Sequence: RKNKLEGDSDVDSELEDRVDGVKS | ||||||
Compositional bias | 1999-2014 | Polar residues | ||||
Sequence: DDGSLKSSSPTSYWKS | ||||||
Compositional bias | 2016-2031 | Basic and acidic residues | ||||
Sequence: APDRSDDEHDPLDNTS | ||||||
Compositional bias | 2032-2054 | Polar residues | ||||
Sequence: RPRYSHSYLSDSDTEAKLTETNA |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB177858 EMBL· GenBank· DDBJ | BAD66836.1 EMBL· GenBank· DDBJ | mRNA | ||
AB177860 EMBL· GenBank· DDBJ | BAD66838.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY703984 EMBL· GenBank· DDBJ | AAV80770.1 EMBL· GenBank· DDBJ | mRNA | ||
D86970 EMBL· GenBank· DDBJ | BAA13206.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
CR933614 EMBL· GenBank· DDBJ | CAI45931.1 EMBL· GenBank· DDBJ | mRNA | ||
BC039612 EMBL· GenBank· DDBJ | AAH39612.1 EMBL· GenBank· DDBJ | mRNA |