Q92616 · GCN1_HUMAN
- ProteinStalled ribosome sensor GCN1
- GeneGCN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2671 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ribosome collision sensor that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (PubMed:32610081, PubMed:36638793, PubMed:37651229, PubMed:37951215, PubMed:37951216).
Directly binds to the ribosome and acts as a sentinel for colliding ribosomes: activated following ribosome stalling and promotes recruitment of RNF14, which directly ubiquitinates EEF1A1/eEF1A, leading to its degradation (PubMed:36638793, PubMed:37951215, PubMed:37951216).
In addition to EEF1A1/eEF1A, the RNF14-RNF25 translation quality control pathway mediates degradation of ETF1/eRF1 and ubiquitination of ribosomal protein (PubMed:36638793, PubMed:37651229).
GCN1 also acts as a positive activator of the integrated stress response (ISR) by mediating activation of EIF2AK4/GCN2 in response to amino acid starvation (By similarity).
Interaction with EIF2AK4/GCN2 on translating ribosomes stimulates EIF2AK4/GCN2 kinase activity, leading to phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) (By similarity).
EIF2S1/eIF-2-alpha phosphorylation converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (By similarity).
Directly binds to the ribosome and acts as a sentinel for colliding ribosomes: activated following ribosome stalling and promotes recruitment of RNF14, which directly ubiquitinates EEF1A1/eEF1A, leading to its degradation (PubMed:36638793, PubMed:37951215, PubMed:37951216).
In addition to EEF1A1/eEF1A, the RNF14-RNF25 translation quality control pathway mediates degradation of ETF1/eRF1 and ubiquitination of ribosomal protein (PubMed:36638793, PubMed:37651229).
GCN1 also acts as a positive activator of the integrated stress response (ISR) by mediating activation of EIF2AK4/GCN2 in response to amino acid starvation (By similarity).
Interaction with EIF2AK4/GCN2 on translating ribosomes stimulates EIF2AK4/GCN2 kinase activity, leading to phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) (By similarity).
EIF2S1/eIF-2-alpha phosphorylation converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (By similarity).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | cytosolic ribosome | |
Cellular Component | membrane | |
Cellular Component | ribosome | |
Molecular Function | cadherin binding | |
Molecular Function | molecular adaptor activity | |
Molecular Function | protein kinase regulator activity | |
Molecular Function | protein serine/threonine kinase activator activity | |
Molecular Function | RNA binding | |
Molecular Function | stalled ribosome sensor activity | |
Molecular Function | translation factor activity, RNA binding | |
Biological Process | cellular response to amino acid starvation | |
Biological Process | GCN2-mediated signaling | |
Biological Process | protein-RNA covalent cross-linking repair | |
Biological Process | regulation of translation | |
Biological Process | rescue of stalled ribosome |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStalled ribosome sensor GCN1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ92616
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associates with ribosomes in undifferentiated neuroblastoma cells and increases after neuronal differentiation.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_062228 | 2155 | in dbSNP:rs3864938 | |||
Sequence: D → Y | ||||||
Mutagenesis | 2312 | Abolished interaction with RNF14 and decreased interaction with EIF2AK4/GCN2. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,376 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000087443 | 2-2671 | UniProt | Stalled ribosome sensor GCN1 | |||
Sequence: AADTQVSETLKRFAGKVTTASVKERREILSELGKCVAGKDLPEGAVKGLCKLFCLTLHRYRDAASRRALQAAIQQLAEAQPEATAKNLLHSLQSSGIGSKAGVPSKSSGSAALLALTWTCLLVRIVFPSRAKRQGDIWNKLVEVQCLLLLEVLGGSHKHAVDGAVKKLTKLWKENPGLVEQYLSAILSLEPNQNYAGMLGLLVQFCTSHKEMDVVSQHKSALLDFYMKNILMSKVKPPKYLLDSCAPLLRYLSHSEFKDLILPTIQKSLLRSPENVIETISSLLASVTLDLSQYAMDIVKGLAGHLKSNSPRLMDEAVLALRNLARQCSDSSAMESLTKHLFAILGGSEGKLTVVAQKMSVLSGIGSVSHHVVSGPSSQVLNGIVAELFIPFLQQEVHEGTLVHAVSVLALWCNRFTMEVPKKLTEWFKKAFSLKTSTSAVRHAYLQCMLASYRGDTLLQALDLLPLLIQTVEKAASQSTQVPTITEGVAAALLLLKLSVADSQAEAKLSSFWQLIVDEKKQVFTSEKFLVMASEDALCTVLHLTERLFLDHPHRLTGNKVQQYHRALVAVLLSRTWHVRRQAQQTVRKLLSSLGGFKLAHGLLEELKTVLSSHKVLPLEALVTDAGEVTEAGKAYVPPRVLQEALCVISGVPGLKGDVTDTEQLAQEMLIISHHPSLVAVQSGLWPALLARMKIDPEAFITRHLDQIIPRMTTQSPLNQSSMNAMGSLSVLSPDRVLPQLISTITASVQNPALRLVTREEFAIMQTPAGELYDKSIIQSAQQDSIKKANMKRENKAYSFKEQIIELELKEEIKKKKGIKEEVQLTSKQKEMLQAQLDREAQVRRRLQELDGELEAALGLLDIILAKNPSGLTQYIPVLVDSFLPLLKSPLAAPRIKNPFLSLAACVMPSRLKALGTLVSHVTLRLLKPECVLDKSWCQEELSVAVKRAVMLLHTHTITSRVGKGEPGAAPLSAPAFSLVFPFLKMVLTEMPHHSEEEEEWMAQILQILTVQAQLRASPNTPPGRVDENGPELLPRVAMLRLLTWVIGTGSPRLQVLASDTLTTLCASSSGDDGCAFAEQEEVDVLLCALQSPCASVRETVLRGLMELHMVLPAPDTDEKNGLNLLRRLWVVKFDKEEEIRKLAERLWSMMGLDLQPDLCSLLIDDVIYHEAAVRQAGAEALSQAVARYQRQAAEVMGRLMEIYQEKLYRPPPVLDALGRVISESPPDQWEARCGLALALNKLSQYLDSSQVKPLFQFFVPDALNDRHPDVRKCMLDAALATLNTHGKENVNSLLPVFEEFLKNAPNDASYDAVRQSVVVLMGSLAKHLDKSDPKVKPIVAKLIAALSTPSQQVQESVASCLPPLVPAIKEDAGGMIQRLMQQLLESDKYAERKGAAYGLAGLVKGLGILSLKQQEMMAALTDAIQDKKNFRRREGALFAFEMLCTMLGKLFEPYVVHVLPHLLLCFGDGNQYVREAADDCAKAVMSNLSAHGVKLVLPSLLAALEEESWRTKAGSVELLGAMAYCAPKQLSSCLPNIVPKLTEVLTDSHVKVQKAGQQALRQIGSVIRNPEILAIAPVLLDALTDPSRKTQKCLQTLLDTKFVHFIDAPSLALIMPIVQRAFQDRSTDTRKMAAQIIGNMYSLTDQKDLAPYLPSVTPGLKASLLDPVPEVRTVSAKALGAMVKGMGESCFEDLLPWLMETLTYEQSSVDRSGAAQGLAEVMAGLGVEKLEKLMPEIVATASKVDIAPHVRDGYIMMFNYLPITFGDKFTPYVGPIIPCILKALADENEFVRDTALRAGQRVISMYAETAIALLLPQLEQGLFDDLWRIRFSSVQLLGDLLFHISGVTGKMTTETASEDDNFGTAQSNKAIITALGVERRNRVLAGLYMGRSDTQLVVRQASLHVWKIVVSNTPRTLREILPTLFGLLLGFLASTCADKRTIAARTLGDLVRKLGEKILPEIIPILEEGLRSQKSDERQGVCIGLSEIMKSTSRDAVLYFSESLVPTARKALCDPLEEVREAAAKTFEQLHSTIGHQALEDILPFLLKQLDDEEVSEFALDGLKQVMAIKSRVVLPYLVPKLTTPPVNTRVLAFLSSVAGDALTRHLGVILPAVMLALKEKLGTPDEQLEMANCQAVILSVEDDTGHRIIIEDLLEATRSPEVGMRQAAAIILNIYCSRSKADYTSHLRSLVSGLIRLFNDSSPVVLEESWDALNAITKKLDAGNQLALIEELHKEIRLIGNESKGEHVPGFCLPKKGVTSILPVLREGVLTGSPEQKEEAAKALGLVIRLTSADALRPSVVSITGPLIRILGDRFSWNVKAALLETLSLLLAKVGIALKPFLPQLQTTFTKALQDSNRGVRLKAADALGKLISIHIKVDPLFTELLNGIRAMEDPGVRDTMLQALRFVIQGAGAKVDAVIRKNIVSLLLSMLGHDEDNTRISSAGCLGELCAFLTEEELSAVLQQCLLADVSGIDWMVRHGRSLALSVAVNVAPGRLCAGRYSSDVQEMILSSATADRIPIAVSGVRGMGFLMRHHIETGGGQLPAKLSSLFVKCLQNPSSDIRLVAEKMIWWANKDPLPPLDPQAIKPILKALLDNTKDKNTVVRAYSDQAIVNLLKMRQGEEVFQSLSKILDVASLEVLNEVNRRSLKKLASQADSTEQVDDTILT | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 593 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 729 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 786 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 786 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 937 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1022 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1412 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1491 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1859 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2274 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2276 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2276 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2490 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2612 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2657 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with EIF2AK4/GCN2; this interaction stimulates the EIF2AK4/GCN2 kinase activity and is impaired by IMPACT upon a variety of stress conditions, such as amino acid depletion, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation (PubMed:36638793).
Interacts with IMPACT; this prevents the interaction of GCN1 with EIF2AK4/GCN2 and inhibits EIF2AK4/GCN2 kinase activity (By similarity).
Interacts with RNF14; interaction takes place following ribosome stalling and promotes recruitment of RNF14 (PubMed:36638793).
Interacts with IMPACT; this prevents the interaction of GCN1 with EIF2AK4/GCN2 and inhibits EIF2AK4/GCN2 kinase activity (By similarity).
Interacts with RNF14; interaction takes place following ribosome stalling and promotes recruitment of RNF14 (PubMed:36638793).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, coiled coil, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 140-178 | HEAT 1 | ||||
Sequence: NKLVEVQCLLLLEVLGGSHKHAVDGAVKKLTKLWKENPG | ||||||
Repeat | 257-293 | HEAT 2 | ||||
Sequence: EFKDLILPTIQKSLLRSPENVIETISSLLASVTLDLS | ||||||
Repeat | 294-331 | HEAT 3 | ||||
Sequence: QYAMDIVKGLAGHLKSNSPRLMDEAVLALRNLARQCSD | ||||||
Repeat | 385-423 | HEAT 4 | ||||
Sequence: IVAELFIPFLQQEVHEGTLVHAVSVLALWCNRFTMEVPK | ||||||
Repeat | 425-459 | HEAT 5 | ||||
Sequence: LTEWFKKAFSLKTSTSAVRHAYLQCMLASYRGDTL | ||||||
Repeat | 460-503 | HEAT 6 | ||||
Sequence: LQALDLLPLLIQTVEKAASQSTQVPTITEGVAAALLLLKLSVAD | ||||||
Repeat | 560-597 | HEAT 7 | ||||
Sequence: NKVQQYHRALVAVLLSRTWHVRRQAQQTVRKLLSSLGG | ||||||
Repeat | 599-636 | HEAT 8 | ||||
Sequence: KLAHGLLEELKTVLSSHKVLPLEALVTDAGEVTEAGKA | ||||||
Repeat | 697-732 | HEAT 9 | ||||
Sequence: DPEAFITRHLDQIIPRMTTQSPLNQSSMNAMGSLSV | ||||||
Repeat | 733-770 | HEAT 10 | ||||
Sequence: LSPDRVLPQLISTITASVQNPALRLVTREEFAIMQTPA | ||||||
Coiled coil | 804-863 | |||||
Sequence: QIIELELKEEIKKKKGIKEEVQLTSKQKEMLQAQLDREAQVRRRLQELDGELEAALGLLD | ||||||
Repeat | 879-925 | HEAT 11 | ||||
Sequence: VLVDSFLPLLKSPLAAPRIKNPFLSLAACVMPSRLKALGTLVSHVTL | ||||||
Repeat | 979-1016 | HEAT 12 | ||||
Sequence: SLVFPFLKMVLTEMPHHSEEEEEWMAQILQILTVQAQL | ||||||
Repeat | 1035-1072 | HEAT 13 | ||||
Sequence: LPRVAMLRLLTWVIGTGSPRLQVLASDTLTTLCASSSG | ||||||
Repeat | 1078-1115 | HEAT 14 | ||||
Sequence: FAEQEEVDVLLCALQSPCASVRETVLRGLMELHMVLPA | ||||||
Repeat | 1155-1192 | HEAT 15 | ||||
Sequence: DLQPDLCSLLIDDVIYHEAAVRQAGAEALSQAVARYQR | ||||||
Repeat | 1210-1250 | HEAT 16 | ||||
Sequence: YRPPPVLDALGRVISESPPDQWEARCGLALALNKLSQYLDS | ||||||
Repeat | 1251-1289 | HEAT 17 | ||||
Sequence: SQVKPLFQFFVPDALNDRHPDVRKCMLDAALATLNTHGK | ||||||
Repeat | 1290-1332 | HEAT 18 | ||||
Sequence: ENVNSLLPVFEEFLKNAPNDASYDAVRQSVVVLMGSLAKHLDK | ||||||
Repeat | 1335-1372 | HEAT 19 | ||||
Sequence: PKVKPIVAKLIAALSTPSQQVQESVASCLPPLVPAIKE | ||||||
Repeat | 1374-1410 | HEAT 20 | ||||
Sequence: AGGMIQRLMQQLLESDKYAERKGAAYGLAGLVKGLGI | ||||||
Repeat | 1413-1451 | HEAT 21 | ||||
Sequence: LKQQEMMAALTDAIQDKKNFRRREGALFAFEMLCTMLGK | ||||||
Repeat | 1455-1492 | HEAT 22 | ||||
Sequence: PYVVHVLPHLLLCFGDGNQYVREAADDCAKAVMSNLSA | ||||||
Repeat | 1493-1530 | HEAT 23 | ||||
Sequence: HGVKLVLPSLLAALEEESWRTKAGSVELLGAMAYCAPK | ||||||
Repeat | 1534-1571 | HEAT 24 | ||||
Sequence: SCLPNIVPKLTEVLTDSHVKVQKAGQQALRQIGSVIRN | ||||||
Repeat | 1573-1609 | HEAT 25 | ||||
Sequence: EILAIAPVLLDALTDPSRKTQKCLQTLLDTKFVHFID | ||||||
Repeat | 1611-1648 | HEAT 26 | ||||
Sequence: PSLALIMPIVQRAFQDRSTDTRKMAAQIIGNMYSLTDQ | ||||||
Repeat | 1653-1690 | HEAT 27 | ||||
Sequence: PYLPSVTPGLKASLLDPVPEVRTVSAKALGAMVKGMGE | ||||||
Repeat | 1692-1729 | HEAT 28 | ||||
Sequence: CFEDLLPWLMETLTYEQSSVDRSGAAQGLAEVMAGLGV | ||||||
Repeat | 1731-1769 | HEAT 29 | ||||
Sequence: KLEKLMPEIVATASKVDIAPHVRDGYIMMFNYLPITFGD | ||||||
Repeat | 1773-1810 | HEAT 30 | ||||
Sequence: PYVGPIIPCILKALADENEFVRDTALRAGQRVISMYAE | ||||||
Repeat | 1812-1848 | HEAT 31 | ||||
Sequence: AIALLLPQLEQGLFDDLWRIRFSSVQLLGDLLFHISG | ||||||
Repeat | 1921-1958 | HEAT 32 | ||||
Sequence: EILPTLFGLLLGFLASTCADKRTIAARTLGDLVRKLGE | ||||||
Repeat | 1959-1996 | HEAT 33 | ||||
Sequence: KILPEIIPILEEGLRSQKSDERQGVCIGLSEIMKSTSR | ||||||
Repeat | 2001-2038 | HEAT 34 | ||||
Sequence: YFSESLVPTARKALCDPLEEVREAAAKTFEQLHSTIGH | ||||||
Repeat | 2039-2076 | HEAT 35 | ||||
Sequence: QALEDILPFLLKQLDDEEVSEFALDGLKQVMAIKSRVV | ||||||
Repeat | 2078-2106 | HEAT 36 | ||||
Sequence: PYLVPKLTTPPVNTRVLAFLSSVAGDALT | ||||||
Repeat | 2107-2146 | HEAT 37 | ||||
Sequence: RHLGVILPAVMLALKEKLGTPDEQLEMANCQAVILSVEDD | ||||||
Repeat | 2147-2184 | HEAT 38 | ||||
Sequence: TGHRIIIEDLLEATRSPEVGMRQAAAIILNIYCSRSKA | ||||||
Repeat | 2188-2225 | HEAT 39 | ||||
Sequence: SHLRSLVSGLIRLFNDSSPVVLEESWDALNAITKKLDA | ||||||
Repeat | 2259-2296 | HEAT 40 | ||||
Sequence: KGVTSILPVLREGVLTGSPEQKEEAAKALGLVIRLTSA | ||||||
Region | 2260-2408 | RWDBD region | ||||
Sequence: GVTSILPVLREGVLTGSPEQKEEAAKALGLVIRLTSADALRPSVVSITGPLIRILGDRFSWNVKAALLETLSLLLAKVGIALKPFLPQLQTTFTKALQDSNRGVRLKAADALGKLISIHIKVDPLFTELLNGIRAMEDPGVRDTMLQAL | ||||||
Repeat | 2301-2338 | HEAT 41 | ||||
Sequence: PSVVSITGPLIRILGDRFSWNVKAALLETLSLLLAKVG | ||||||
Repeat | 2339-2380 | HEAT 42 | ||||
Sequence: IALKPFLPQLQTTFTKALQDSNRGVRLKAADALGKLISIHIK | ||||||
Repeat | 2382-2417 | HEAT 43 | ||||
Sequence: DPLFTELLNGIRAMEDPGVRDTMLQALRFVIQGAGA | ||||||
Repeat | 2422-2459 | HEAT 44 | ||||
Sequence: VIRKNIVSLLLSMLGHDEDNTRISSAGCLGELCAFLTE | ||||||
Repeat | 2546-2583 | HEAT 45 | ||||
Sequence: QLPAKLSSLFVKCLQNPSSDIRLVAEKMIWWANKDPLP | ||||||
Repeat | 2588-2625 | HEAT 46 | ||||
Sequence: QAIKPILKALLDNTKDKNTVVRAYSDQAIVNLLKMRQG | ||||||
Repeat | 2627-2661 | HEAT 47; degenerate | ||||
Sequence: EVFQSLSKILDVASLEVLNEVNRRSLKKLASQADS |
Domain
The RWDBD (RWD-binding domain) region mediates binding to RWD domain-containing proteins, such as EIF2AK4/GCN2, IMPACT and RNF14.
Sequence similarities
Belongs to the GCN1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,671
- Mass (Da)292,710
- Last updated2022-02-23 v7
- ChecksumFC34F505103A0158
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 292 | in Ref. 1; BAA13209 and 4; AAI53882 | ||||
Sequence: L → F | ||||||
Sequence conflict | 842 | in Ref. 7; AAC51648 | ||||
Sequence: A → G | ||||||
Sequence conflict | 1584 | in Ref. 7; AAC51648 | ||||
Sequence: A → V | ||||||
Sequence conflict | 1683 | in Ref. 7; AAC51648 | ||||
Sequence: A → V | ||||||
Sequence conflict | 1760 | in Ref. 6; AAD00655 | ||||
Sequence: F → S | ||||||
Sequence conflict | 2298 | in Ref. 7; AAC51648 | ||||
Sequence: A → V | ||||||
Sequence conflict | 2486 | in Ref. 6; AAD00655 | ||||
Sequence: S → T | ||||||
Sequence conflict | 2549 | in Ref. 7; AAC51648 | ||||
Sequence: A → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D86973 EMBL· GenBank· DDBJ | BAA13209.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC004812 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF459556 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF511175 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC004263 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC021129 EMBL· GenBank· DDBJ | AAH21129.1 EMBL· GenBank· DDBJ | mRNA | ||
BC032335 EMBL· GenBank· DDBJ | AAH32335.1 EMBL· GenBank· DDBJ | mRNA | ||
BC046177 EMBL· GenBank· DDBJ | AAH46177.1 EMBL· GenBank· DDBJ | mRNA | ||
BC064346 EMBL· GenBank· DDBJ | AAH64346.1 EMBL· GenBank· DDBJ | mRNA | ||
BC153881 EMBL· GenBank· DDBJ | AAI53882.1 EMBL· GenBank· DDBJ | mRNA | ||
U88836 EMBL· GenBank· DDBJ | AAD00655.1 EMBL· GenBank· DDBJ | mRNA | ||
U88837 EMBL· GenBank· DDBJ | AAD00656.1 EMBL· GenBank· DDBJ | mRNA | ||
U77700 EMBL· GenBank· DDBJ | AAC51648.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |