P52179 · MYOM1_HUMAN
- ProteinMyomesin-1
- GeneMYOM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1685 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | M band | |
Cellular Component | striated muscle myosin thick filament | |
Molecular Function | identical protein binding | |
Molecular Function | kinase binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | structural constituent of muscle | |
Biological Process | extraocular skeletal muscle development | |
Biological Process | positive regulation of gene expression | |
Biological Process | positive regulation of protein secretion | |
Biological Process | protein kinase A signaling | |
Biological Process | sarcomere organization |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyomesin-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP52179
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_047221 | 22 | in dbSNP:rs1791085 | |||
Sequence: V → L | ||||||
Natural variant | VAR_047222 | 181 | in dbSNP:rs1962519 | |||
Sequence: S → P | ||||||
Natural variant | VAR_047223 | 215 | in dbSNP:rs2230165 | |||
Sequence: T → M | ||||||
Natural variant | VAR_047224 | 341 | in dbSNP:rs8099021 | |||
Sequence: G → A | ||||||
Natural variant | VAR_047225 | 600 | in dbSNP:rs9807556 | |||
Sequence: E → V | ||||||
Natural variant | VAR_047226 | 960 | in dbSNP:rs1071600 | |||
Sequence: I → T | ||||||
Natural variant | VAR_047227 | 1408 | in dbSNP:rs3765623 | |||
Sequence: D → N | ||||||
Natural variant | VAR_047228 | 1453 | in dbSNP:rs16944397 | |||
Sequence: M → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,112 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 (large scale data), modified residue, disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000072684 | 1-1685 | UniProt | Myomesin-1 | |||
Sequence: MSLPFYQRCHQHYDLSYRNKDVRSTVSHYQREKKRSAVYTQGSTAYSSRSSAAHRRESEAFRRASASSSQQQASQHALSSEVSRKAASAYDYGSSHGLTDSSLLLDDYSSKLSPKPKRAKHSLLSGEEKENLPSDYMVPIFSGRQKHVSGITDTEEERIKEAAAYIAQRNLLASEEGITTSKQSTASKQTTASKQSTASKQSTASKQSTASRQSTASRQSVVSKQATSALQQEETSEKKSRKVVIREKAERLSLRKTLEETETYHAKLNEDHLLHAPEFIIKPRSHTVWEKENVKLHCSIAGWPEPRVTWYKNQVPINVHANPGKYIIESRYGMHTLEINGCDFEDTAQYRASAMNVKGELSAYASVVVKRYKGEFDETRFHAGASTMPLSFGVTPYGYASRFEIHFDDKFDVSFGREGETMSLGCRVVITPEIKHFQPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYVFVRDADAEIEGAPAAPLDVKCLEANKDYIIISWKQPAVDGGSPILGYFIDKCEVGTDSWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNKMGIGFPSRVSEPVAALDPAEKARLKSRPSAPWTGQIIVTEEEPSEGIVPGPPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCEAGTENWQRVNTELPVKSPRFALFDLAEGKSYCFRVRCSNSAGVGEPSEATEVTVVGDKLDIPKAPGKIIPSRNTDTSVVVSWEESKDAKELVGYYIEASVAGSGKWEPCNNNPVKGSRFTCHGLVTGQSYIFRVRAVNAAGLSEYSQDSEAIEVKAAIGGGVSPDVCPALSDEPGGLTASRGRVHEASPPTFQKDALLGSKPNKPSLPSSSQNLGQTEVSKVSETVQEELTPPPQKAAPQGKSKSDPLKKKTDRAPPSPPCDITCLESFRDSMVLGWKQPDKIGGAEITGYYVNYREVIDGVPGKWREANVKAVSEEAYKISNLKENMVYQFQVAAMNMAGLGAPSAVSECFKCEEWTIAVPGPPHSLKCSEVRKDSLVLQWKPPVHSGRTPVTGYFVDLKEAKAKEDQWRGLNEAAIKNVYLKVRGLKEGVSYVFRVRAINQAGVGKPSDLAGPVVAETRPGTKEVVVNVDDDGVISLNFECDKMTPKSEFSWSKDYVSTEDSPRLEVESKGNKTKMTFKDLGMDDLGIYSCDVTDTDGIASSYLIDEEELKRLLALSHEHKFPTVPVKSELAVEILEKGQVRFWMQAEKLSGNAKVNYIFNEKEIFEGPKYKMHIDRNTGIIEMFMEKLQDEDEGTYTFQLQDGKATNHSTVVLVGDVFKKLQKEAEFQRQEWIRKQGPHFVEYLSWEVTGECNVLLKCKVANIKKETHIVWYKDEREISVDEKHDFKDGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKLVDEAFKELMMEVCKKIALSATDLKIQSTAEGIQLYSFVTYYVEDLKVNWSHNGSAIRYSDRVKTGVTGEQIWLQINEPTPNDKGKYVMELFDGKTGHQKTVDLSGQAYDEAYAEFQRLKQAAIAEKNRARVLGGLPDVVTIQEGKALNLTCNVWGDPPPEVSWLKNEKALASDDHCNLKFEAGRTAYFTINGVSTADSGKYGLVVKNKYGSETSDFTVSVFIPEEEARMAALESLKGGKKAK | |||||||
Modified residue (large scale data) | 58 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 67 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 69 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 79 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 113 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 113 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 125 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 152 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 184 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 220 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 236 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 257 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 444 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 451 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 470 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 694 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 797 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 883 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 887 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 992 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 996 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 999 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1044 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1054 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1054 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1065 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 1160↔1210 | UniProt | |||||
Sequence: CDKMTPKSEFSWSKDYVSTEDSPRLEVESKGNKTKMTFKDLGMDDLGIYSC | |||||||
Modified residue (large scale data) | 1177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1178 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1181 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1399 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1493 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1497 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1615 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1677 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with TTN/titin (By similarity).
Interacts with PNKD
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P52179 | DYSF O75923 | 3 | EBI-5353249, EBI-2799016 | |
BINARY | P52179 | MYOM1 P52179 | 4 | EBI-5353249, EBI-5353249 | |
BINARY | P52179-1 | MYOM1 P52179-1 | 7 | EBI-15971501, EBI-15971501 | |
BINARY | P52179-2 | KRT31 Q15323 | 3 | EBI-12010196, EBI-948001 | |
BINARY | P52179-2 | KRTAP1-1 Q07627 | 3 | EBI-12010196, EBI-11959885 | |
BINARY | P52179-2 | KRTAP5-7 Q6L8G8 | 3 | EBI-12010196, EBI-11987425 | |
BINARY | P52179-2 | MTUS2 Q5JR59-3 | 3 | EBI-12010196, EBI-11522433 | |
BINARY | P52179-2 | PDE4DIP Q5VU43-2 | 3 | EBI-12010196, EBI-9640281 | |
BINARY | P52179-2 | PPP1R16A Q96I34 | 3 | EBI-12010196, EBI-710402 | |
BINARY | P52179-2 | TFIP11 Q9UBB9 | 3 | EBI-12010196, EBI-1105213 | |
BINARY | P52179-2 | TRIM23 P36406 | 3 | EBI-12010196, EBI-740098 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 33-80 | Disordered | ||||
Sequence: KKRSAVYTQGSTAYSSRSSAAHRRESEAFRRASASSSQQQASQHALSS | ||||||
Compositional bias | 36-51 | Polar residues | ||||
Sequence: SAVYTQGSTAYSSRSS | ||||||
Compositional bias | 63-80 | Polar residues | ||||
Sequence: RASASSSQQQASQHALSS | ||||||
Compositional bias | 177-233 | Polar residues | ||||
Sequence: GITTSKQSTASKQTTASKQSTASKQSTASKQSTASRQSTASRQSVVSKQATSALQQE | ||||||
Region | 177-244 | Disordered | ||||
Sequence: GITTSKQSTASKQTTASKQSTASKQSTASKQSTASRQSTASRQSVVSKQATSALQQEETSEKKSRKVV | ||||||
Repeat | 182-187 | 1 | ||||
Sequence: KQSTAS | ||||||
Region | 182-217 | 6 X 6 AA tandem repeats | ||||
Sequence: KQSTASKQTTASKQSTASKQSTASKQSTASRQSTAS | ||||||
Repeat | 188-193 | 2 | ||||
Sequence: KQTTAS | ||||||
Repeat | 194-199 | 3 | ||||
Sequence: KQSTAS | ||||||
Repeat | 200-205 | 4 | ||||
Sequence: KQSTAS | ||||||
Repeat | 206-211 | 5 | ||||
Sequence: KQSTAS | ||||||
Repeat | 212-217 | 6 | ||||
Sequence: RQSTAS | ||||||
Domain | 277-368 | Ig-like C2-type 1 | ||||
Sequence: PEFIIKPRSHTVWEKENVKLHCSIAGWPEPRVTWYKNQVPINVHANPGKYIIESRYGMHTLEINGCDFEDTAQYRASAMNVKGELSAYASVV | ||||||
Domain | 396-498 | Ig-like C2-type 2 | ||||
Sequence: PYGYASRFEIHFDDKFDVSFGREGETMSLGCRVVITPEIKHFQPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYVF | ||||||
Domain | 512-607 | Fibronectin type-III 1 | ||||
Sequence: APLDVKCLEANKDYIIISWKQPAVDGGSPILGYFIDKCEVGTDSWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNKMGIGFPSRVSEPVAALDP | ||||||
Domain | 640-734 | Fibronectin type-III 2 | ||||
Sequence: PPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCEAGTENWQRVNTELPVKSPRFALFDLAEGKSYCFRVRCSNSAGVGEPSEATEVTVVGD | ||||||
Domain | 741-834 | Fibronectin type-III 3 | ||||
Sequence: APGKIIPSRNTDTSVVVSWEESKDAKELVGYYIEASVAGSGKWEPCNNNPVKGSRFTCHGLVTGQSYIFRVRAVNAAGLSEYSQDSEAIEVKAA | ||||||
Region | 840-938 | Disordered | ||||
Sequence: SPDVCPALSDEPGGLTASRGRVHEASPPTFQKDALLGSKPNKPSLPSSSQNLGQTEVSKVSETVQEELTPPPQKAAPQGKSKSDPLKKKTDRAPPSPPC | ||||||
Compositional bias | 880-907 | Polar residues | ||||
Sequence: NKPSLPSSSQNLGQTEVSKVSETVQEEL | ||||||
Domain | 933-1034 | Fibronectin type-III 4 | ||||
Sequence: PPSPPCDITCLESFRDSMVLGWKQPDKIGGAEITGYYVNYREVIDGVPGKWREANVKAVSEEAYKISNLKENMVYQFQVAAMNMAGLGAPSAVSECFKCEEW | ||||||
Domain | 1041-1140 | Fibronectin type-III 5 | ||||
Sequence: PPHSLKCSEVRKDSLVLQWKPPVHSGRTPVTGYFVDLKEAKAKEDQWRGLNEAAIKNVYLKVRGLKEGVSYVFRVRAINQAGVGKPSDLAGPVVAETRPG | ||||||
Domain | 1132-1230 | Ig-like C2-type 3 | ||||
Sequence: PVVAETRPGTKEVVVNVDDDGVISLNFECDKMTPKSEFSWSKDYVSTEDSPRLEVESKGNKTKMTFKDLGMDDLGIYSCDVTDTDGIASSYLIDEEELK | ||||||
Domain | 1358-1444 | Ig-like C2-type 4 | ||||
Sequence: PHFVEYLSWEVTGECNVLLKCKVANIKKETHIVWYKDEREISVDEKHDFKDGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKLV | ||||||
Domain | 1573-1662 | Ig-like C2-type 5 | ||||
Sequence: RVLGGLPDVVTIQEGKALNLTCNVWGDPPPEVSWLKNEKALASDDHCNLKFEAGRTAYFTINGVSTADSGKYGLVVKNKYGSETSDFTVS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P52179-1
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
- Length1,685
- Mass (Da)187,627
- Last updated2008-11-04 v2
- ChecksumF0DBB25EB6323DF8
P52179-2
- Name2
- Differences from canonical
- 836-931: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3KRK2 | J3KRK2_HUMAN | MYOM1 | 121 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 36-51 | Polar residues | ||||
Sequence: SAVYTQGSTAYSSRSS | ||||||
Compositional bias | 63-80 | Polar residues | ||||
Sequence: RASASSSQQQASQHALSS | ||||||
Compositional bias | 177-233 | Polar residues | ||||
Sequence: GITTSKQSTASKQTTASKQSTASKQSTASKQSTASRQSTASRQSVVSKQATSALQQE | ||||||
Sequence conflict | 247 | in Ref. 5; CAA48833 | ||||
Sequence: E → G | ||||||
Sequence conflict | 442 | in Ref. 5; CAA48833 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 599 | in Ref. 4; AAI16184 | ||||
Sequence: S → F | ||||||
Sequence conflict | 601 | in Ref. 5; CAA48833 | ||||
Sequence: P → A | ||||||
Sequence conflict | 615 | in Ref. 4; AAI16184 | ||||
Sequence: S → G | ||||||
Sequence conflict | 616-625 | in Ref. 5; CAA48833 | ||||
Sequence: RPSAPWTGQI → PLSTLDWTV | ||||||
Sequence conflict | 776 | in Ref. 5; CAA48833 | ||||
Sequence: S → N | ||||||
Sequence conflict | 793-794 | in Ref. 5; CAA48833 | ||||
Sequence: GS → TH | ||||||
Alternative sequence | VSP_035663 | 836-931 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 880-907 | Polar residues | ||||
Sequence: NKPSLPSSSQNLGQTEVSKVSETVQEEL | ||||||
Sequence conflict | 992 | in Ref. 5; CAA48833 | ||||
Sequence: S → R | ||||||
Sequence conflict | 1001 | in Ref. 2; BAC86128 | ||||
Sequence: L → S | ||||||
Sequence conflict | 1080 | in Ref. 5; CAA48833 | ||||
Sequence: Missing | ||||||
Sequence conflict | 1141 | in Ref. 5; CAA48833 | ||||
Sequence: T → R | ||||||
Sequence conflict | 1615-1616 | in Ref. 5; CAA48833 | ||||
Sequence: SD → QT | ||||||
Sequence conflict | 1617 | in Ref. 2; BAC86128 | ||||
Sequence: D → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ621424 EMBL· GenBank· DDBJ | CAF18565.1 EMBL· GenBank· DDBJ | mRNA | ||
AK125322 EMBL· GenBank· DDBJ | BAC86128.1 EMBL· GenBank· DDBJ | mRNA | ||
AP005329 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP005431 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC116183 EMBL· GenBank· DDBJ | AAI16184.1 EMBL· GenBank· DDBJ | mRNA | ||
X69090 EMBL· GenBank· DDBJ | CAA48833.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |