sujigwak/NVAR huggingface dataset:
UniProt ID: Q9FG67
Variant: N -> K at position 42-42
Variant annotation: in strain: cv. Ema-1 and cv. Pla-0
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Catalyzes exclusively the condensation reactions of both the first and second methionine carbon chain elongation.
Reference sequence:
MASSLLTSSVMIPTTGSTVVGRSVLPFQSSLHSLRLTHSYKNPALFISCCSSVSKNAATSSTDLKPVVERWPEYIPNKLPDGNYVRVFDTTLRDGEQSPGGSLTPPQKLEIARQLAKLRVDIMEVGFPGSSEEELETIKTIAKTVGNEVDEETGYVPVICAIARCKHRDIEATWEALKYAKRPRILVFTSTSDIHMKYKLKKTQEEVIEMAVSSIRFAKSLGFNDIQFGCEDGGRSDKDFLCKILGEAIKAGVTVVTIGDTVGINMPHEYGELVTYLKANTPGIDDVVVAVHCHNDLGLATANSIAGIRAGARQVEVTINGIGERSGNASLEEVVMALKCRGAYVINGVYTKIDTRQIMATSKMVQEYTGLYVQAHKPIVGANCFVHESGIHQDGILKNRSTYEILSPEDIGIVKSQNSGLVLGKLSGRHAVKDRLKELGYELDDEKLNAVFSLFRDLTKNKKRITDADLKALVTSSDEISLEKLNGANGLKSNGYIPVPQVSSNV
UniProt ID: Q9FG67
Variant: A -> T at position 44-44
Variant annotation: in strain: cv. Sorbo
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Catalyzes exclusively the condensation reactions of both the first and second methionine carbon chain elongation.
Reference sequence:
MASSLLTSSVMIPTTGSTVVGRSVLPFQSSLHSLRLTHSYKNPALFISCCSSVSKNAATSSTDLKPVVERWPEYIPNKLPDGNYVRVFDTTLRDGEQSPGGSLTPPQKLEIARQLAKLRVDIMEVGFPGSSEEELETIKTIAKTVGNEVDEETGYVPVICAIARCKHRDIEATWEALKYAKRPRILVFTSTSDIHMKYKLKKTQEEVIEMAVSSIRFAKSLGFNDIQFGCEDGGRSDKDFLCKILGEAIKAGVTVVTIGDTVGINMPHEYGELVTYLKANTPGIDDVVVAVHCHNDLGLATANSIAGIRAGARQVEVTINGIGERSGNASLEEVVMALKCRGAYVINGVYTKIDTRQIMATSKMVQEYTGLYVQAHKPIVGANCFVHESGIHQDGILKNRSTYEILSPEDIGIVKSQNSGLVLGKLSGRHAVKDRLKELGYELDDEKLNAVFSLFRDLTKNKKRITDADLKALVTSSDEISLEKLNGANGLKSNGYIPVPQVSSNV
UniProt ID: Q9FG67
Variant: N -> T at position 505-505
Variant annotation: in strain: cv. Sorbo
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Catalyzes exclusively the condensation reactions of both the first and second methionine carbon chain elongation.
Reference sequence:
MASSLLTSSVMIPTTGSTVVGRSVLPFQSSLHSLRLTHSYKNPALFISCCSSVSKNAATSSTDLKPVVERWPEYIPNKLPDGNYVRVFDTTLRDGEQSPGGSLTPPQKLEIARQLAKLRVDIMEVGFPGSSEEELETIKTIAKTVGNEVDEETGYVPVICAIARCKHRDIEATWEALKYAKRPRILVFTSTSDIHMKYKLKKTQEEVIEMAVSSIRFAKSLGFNDIQFGCEDGGRSDKDFLCKILGEAIKAGVTVVTIGDTVGINMPHEYGELVTYLKANTPGIDDVVVAVHCHNDLGLATANSIAGIRAGARQVEVTINGIGERSGNASLEEVVMALKCRGAYVINGVYTKIDTRQIMATSKMVQEYTGLYVQAHKPIVGANCFVHESGIHQDGILKNRSTYEILSPEDIGIVKSQNSGLVLGKLSGRHAVKDRLKELGYELDDEKLNAVFSLFRDLTKNKKRITDADLKALVTSSDEISLEKLNGANGLKSNGYIPVPQVSSNV
UniProt ID: Q9FG68
Variant: K -> R at position 142-142
Variant annotation: in strain: cv. Ag-0
Protein function: Transcription activator of genes involved in the regulation of meristematic competence, such as CUC2. Positively regulates axillary meristems (AMs) formation and development, especially at early phases of vegetative growth, probably by specifying a stem cell niche for AM formation. Modulates the negative regulation mediated by gibberellic acid on the timing of developmental phase transitions.
Reference sequence:
MGRAPCCDKTKVKRGPWSPEEDSKLRDYIEKYGNGGNWISFPLKAGLRRCGKSCRLRWLNYLRPNIKHGDFSEEEDRIIFSLFAAIGSRWSIIAAHLPGRTDNDIKNYWNTKLRKKLLSSSSDSSSSAMASPYLNPISQDVKRPTSPTTIPSSSYNPYAENPNQYPTKSLISSINGFEAGDKQIISYINPNYPQDLYLSDSNNNTSNANGFLLNHNMCDQYKNHTSFSSDVNGIRSEIMMKQEEIMMMMMIDHHIDQRTKGYNGEFTQGYYNYYNGHGDLKQMISGTGTNSNINMGGSGSSSSSISNLAENKSSGSLLLEYKCLPYFYS
UniProt ID: Q9FG68
Variant: R -> K at position 143-143
Variant annotation: in strain: cv. Br-0 and cv. Cal-0
Protein function: Transcription activator of genes involved in the regulation of meristematic competence, such as CUC2. Positively regulates axillary meristems (AMs) formation and development, especially at early phases of vegetative growth, probably by specifying a stem cell niche for AM formation. Modulates the negative regulation mediated by gibberellic acid on the timing of developmental phase transitions.
Reference sequence:
MGRAPCCDKTKVKRGPWSPEEDSKLRDYIEKYGNGGNWISFPLKAGLRRCGKSCRLRWLNYLRPNIKHGDFSEEEDRIIFSLFAAIGSRWSIIAAHLPGRTDNDIKNYWNTKLRKKLLSSSSDSSSSAMASPYLNPISQDVKRPTSPTTIPSSSYNPYAENPNQYPTKSLISSINGFEAGDKQIISYINPNYPQDLYLSDSNNNTSNANGFLLNHNMCDQYKNHTSFSSDVNGIRSEIMMKQEEIMMMMMIDHHIDQRTKGYNGEFTQGYYNYYNGHGDLKQMISGTGTNSNINMGGSGSSSSSISNLAENKSSGSLLLEYKCLPYFYS
UniProt ID: Q9FG68
Variant: L -> F at position 170-170
Variant annotation: in strain: cv. Cvi-0 and cv. Cvi-1
Protein function: Transcription activator of genes involved in the regulation of meristematic competence, such as CUC2. Positively regulates axillary meristems (AMs) formation and development, especially at early phases of vegetative growth, probably by specifying a stem cell niche for AM formation. Modulates the negative regulation mediated by gibberellic acid on the timing of developmental phase transitions.
Reference sequence:
MGRAPCCDKTKVKRGPWSPEEDSKLRDYIEKYGNGGNWISFPLKAGLRRCGKSCRLRWLNYLRPNIKHGDFSEEEDRIIFSLFAAIGSRWSIIAAHLPGRTDNDIKNYWNTKLRKKLLSSSSDSSSSAMASPYLNPISQDVKRPTSPTTIPSSSYNPYAENPNQYPTKSLISSINGFEAGDKQIISYINPNYPQDLYLSDSNNNTSNANGFLLNHNMCDQYKNHTSFSSDVNGIRSEIMMKQEEIMMMMMIDHHIDQRTKGYNGEFTQGYYNYYNGHGDLKQMISGTGTNSNINMGGSGSSSSSISNLAENKSSGSLLLEYKCLPYFYS
UniProt ID: Q9FG68
Variant: K -> N at position 222-222
Variant annotation: in strain: cv. An-1, cv. Bl-0, cv. Bla-10, cv. C24, cv. Br-0, cv. Cal-0, cv. Can-0, cv. Cnt-1, cv. Kon, cv. Ct-1, cv. Cvi-0, cv. Cvi-1, cv. Di-1, cv. Di-G, cv. Edi-0, cv. Ema-1, cv. Ga-0, cv. Hodja-Obi-Garm, cv. Ka-0, cv. Kas-1, cv. Kil-1, cv. Landsberg erecta, cv. Lip-0, cv. Ll-0, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Ms-0, cv. Nd-1, cv. No-0, cv. Nok-3, cv. Oy-0, cv. Pa-1, cv. Per-1, cv. Petergof, cv. Pi-0, cv. Pla-0, cv, cv. Se-0. Sei-0, cv. Sorbo, cv. Su-0, cv. Tac-0, cv. Tsu-1, cv. Van-0, cv. Wa-1, cv. Wl-0, cv. Wassilewskija and cv. Yo-0
Protein function: Transcription activator of genes involved in the regulation of meristematic competence, such as CUC2. Positively regulates axillary meristems (AMs) formation and development, especially at early phases of vegetative growth, probably by specifying a stem cell niche for AM formation. Modulates the negative regulation mediated by gibberellic acid on the timing of developmental phase transitions.
Reference sequence:
MGRAPCCDKTKVKRGPWSPEEDSKLRDYIEKYGNGGNWISFPLKAGLRRCGKSCRLRWLNYLRPNIKHGDFSEEEDRIIFSLFAAIGSRWSIIAAHLPGRTDNDIKNYWNTKLRKKLLSSSSDSSSSAMASPYLNPISQDVKRPTSPTTIPSSSYNPYAENPNQYPTKSLISSINGFEAGDKQIISYINPNYPQDLYLSDSNNNTSNANGFLLNHNMCDQYKNHTSFSSDVNGIRSEIMMKQEEIMMMMMIDHHIDQRTKGYNGEFTQGYYNYYNGHGDLKQMISGTGTNSNINMGGSGSSSSSISNLAENKSSGSLLLEYKCLPYFYS
UniProt ID: Q9FG68
Variant: I -> V at position 245-245
Variant annotation: in strain: cv. Cvi-0 and cv. Cvi-1
Protein function: Transcription activator of genes involved in the regulation of meristematic competence, such as CUC2. Positively regulates axillary meristems (AMs) formation and development, especially at early phases of vegetative growth, probably by specifying a stem cell niche for AM formation. Modulates the negative regulation mediated by gibberellic acid on the timing of developmental phase transitions.
Reference sequence:
MGRAPCCDKTKVKRGPWSPEEDSKLRDYIEKYGNGGNWISFPLKAGLRRCGKSCRLRWLNYLRPNIKHGDFSEEEDRIIFSLFAAIGSRWSIIAAHLPGRTDNDIKNYWNTKLRKKLLSSSSDSSSSAMASPYLNPISQDVKRPTSPTTIPSSSYNPYAENPNQYPTKSLISSINGFEAGDKQIISYINPNYPQDLYLSDSNNNTSNANGFLLNHNMCDQYKNHTSFSSDVNGIRSEIMMKQEEIMMMMMIDHHIDQRTKGYNGEFTQGYYNYYNGHGDLKQMISGTGTNSNINMGGSGSSSSSISNLAENKSSGSLLLEYKCLPYFYS
UniProt ID: Q9FJA2
Variant: Q -> L at position 174-174
Variant annotation: in strain: cv. Wassilewskija
Protein function: Transcription activator, when associated with BHLH2/EGL3/MYC146, BHLH12/MYC1, or BHLH42/TT8. Involved in the control of flavonoid late metabolism in developing siliques. Plays a key role in determining the tissue-specific activation of leucoanthocyanidin reductase (BANYULS).
Reference sequence:
MGKRATTSVRREELNRGAWTDHEDKILRDYITTHGEGKWSTLPNQAGLKRCGKSCRLRWKNYLRPGIKRGNISSDEEELIIRLHNLLGNRWSLIAGRLPGRTDNEIKNHWNSNLRKRLPKTQTKQPKRIKHSTNNENNVCVIRTKAIRCSKTLLFSDLSLQKKSSTSPLPLKEQEMDQGGSSLMGDLEFDFDRIHSEFHFPDLMDFDGLDCGNVTSLVSSNEILGELVPAQGNLDLNRPFTSCHHRGDDEDWLRDFTC
UniProt ID: Q9FN52
Variant: S -> I at position 10-10
Variant annotation: in strain: cv. Sorbo
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Accepts all the omega-methylthio-2-oxoalkanoic acids needed to form the known C3 to C8 glucosinolates. Also able to convert pyruvate to citramalate, 2-oxoisovalerate to isopropylmalate, 4-methyl-2-oxopentanoate and 5-methyl-2-oxohexanoate for Leu-derived glucosinolates, 3-methyl-2-oxopentanoate for Ile-derived glucosinolates and phenylpyruvate to phenylethylglucosinolate.
Reference sequence:
MASLLLTSSSMITTSCRSMVLRSGLPIGSSFPSLRLTRPYDKATLFVSCCSAESKKVATSATDLKPIMERRPEYIPNKLPHKNYVRVLDTTLRDGEQSPGAALTPPQKLEIARQLAKLRVDIMEVGFPVSSEEEFEAIKTIAKTVGNEVDEETGYVPVICGIARCKKRDIEATWEALKYAKRPRVMLFTSTSEIHMKYKLKKTKEEVIEMAVNSVKYAKSLGFKDIQFGCEDGGRTEKDFICKILGESIKAGATTVGFADTVGINMPQEFGELVAYVIENTPGADDIVFAIHCHNDLGVATANTISGICAGARQVEVTINGIGERSGNAPLEEVVMALKCRGESLMDGVYTKIDSRQIMATSKMVQEHTGMYVQPHKPIVGDNCFVHESGIHQDGILKNRSTYEILSPEDVGIVKSENSGIVLGKLSGRHAVKDRLKELGYEISDEKFNDIFSRYRELTKDKKRITDADLKALVVNGAEISSEKLNSKGINDLMSSPQISAVV
UniProt ID: Q9FN52
Variant: R -> P at position 17-17
Variant annotation: in strain: cv. Bl-0, cv. Di-G, cv. Ema-1, cv. Ka-0, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tsu-1, cv. Wl-0 and cv.Pla-0
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Accepts all the omega-methylthio-2-oxoalkanoic acids needed to form the known C3 to C8 glucosinolates. Also able to convert pyruvate to citramalate, 2-oxoisovalerate to isopropylmalate, 4-methyl-2-oxopentanoate and 5-methyl-2-oxohexanoate for Leu-derived glucosinolates, 3-methyl-2-oxopentanoate for Ile-derived glucosinolates and phenylpyruvate to phenylethylglucosinolate.
Reference sequence:
MASLLLTSSSMITTSCRSMVLRSGLPIGSSFPSLRLTRPYDKATLFVSCCSAESKKVATSATDLKPIMERRPEYIPNKLPHKNYVRVLDTTLRDGEQSPGAALTPPQKLEIARQLAKLRVDIMEVGFPVSSEEEFEAIKTIAKTVGNEVDEETGYVPVICGIARCKKRDIEATWEALKYAKRPRVMLFTSTSEIHMKYKLKKTKEEVIEMAVNSVKYAKSLGFKDIQFGCEDGGRTEKDFICKILGESIKAGATTVGFADTVGINMPQEFGELVAYVIENTPGADDIVFAIHCHNDLGVATANTISGICAGARQVEVTINGIGERSGNAPLEEVVMALKCRGESLMDGVYTKIDSRQIMATSKMVQEHTGMYVQPHKPIVGDNCFVHESGIHQDGILKNRSTYEILSPEDVGIVKSENSGIVLGKLSGRHAVKDRLKELGYEISDEKFNDIFSRYRELTKDKKRITDADLKALVVNGAEISSEKLNSKGINDLMSSPQISAVV
UniProt ID: Q9FN52
Variant: G -> A at position 24-24
Variant annotation: in strain: cv. Sorbo
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Accepts all the omega-methylthio-2-oxoalkanoic acids needed to form the known C3 to C8 glucosinolates. Also able to convert pyruvate to citramalate, 2-oxoisovalerate to isopropylmalate, 4-methyl-2-oxopentanoate and 5-methyl-2-oxohexanoate for Leu-derived glucosinolates, 3-methyl-2-oxopentanoate for Ile-derived glucosinolates and phenylpyruvate to phenylethylglucosinolate.
Reference sequence:
MASLLLTSSSMITTSCRSMVLRSGLPIGSSFPSLRLTRPYDKATLFVSCCSAESKKVATSATDLKPIMERRPEYIPNKLPHKNYVRVLDTTLRDGEQSPGAALTPPQKLEIARQLAKLRVDIMEVGFPVSSEEEFEAIKTIAKTVGNEVDEETGYVPVICGIARCKKRDIEATWEALKYAKRPRVMLFTSTSEIHMKYKLKKTKEEVIEMAVNSVKYAKSLGFKDIQFGCEDGGRTEKDFICKILGESIKAGATTVGFADTVGINMPQEFGELVAYVIENTPGADDIVFAIHCHNDLGVATANTISGICAGARQVEVTINGIGERSGNAPLEEVVMALKCRGESLMDGVYTKIDSRQIMATSKMVQEHTGMYVQPHKPIVGDNCFVHESGIHQDGILKNRSTYEILSPEDVGIVKSENSGIVLGKLSGRHAVKDRLKELGYEISDEKFNDIFSRYRELTKDKKRITDADLKALVVNGAEISSEKLNSKGINDLMSSPQISAVV
UniProt ID: Q9FN52
Variant: F -> L at position 46-46
Variant annotation: in strain: cv. Sorbo
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Accepts all the omega-methylthio-2-oxoalkanoic acids needed to form the known C3 to C8 glucosinolates. Also able to convert pyruvate to citramalate, 2-oxoisovalerate to isopropylmalate, 4-methyl-2-oxopentanoate and 5-methyl-2-oxohexanoate for Leu-derived glucosinolates, 3-methyl-2-oxopentanoate for Ile-derived glucosinolates and phenylpyruvate to phenylethylglucosinolate.
Reference sequence:
MASLLLTSSSMITTSCRSMVLRSGLPIGSSFPSLRLTRPYDKATLFVSCCSAESKKVATSATDLKPIMERRPEYIPNKLPHKNYVRVLDTTLRDGEQSPGAALTPPQKLEIARQLAKLRVDIMEVGFPVSSEEEFEAIKTIAKTVGNEVDEETGYVPVICGIARCKKRDIEATWEALKYAKRPRVMLFTSTSEIHMKYKLKKTKEEVIEMAVNSVKYAKSLGFKDIQFGCEDGGRTEKDFICKILGESIKAGATTVGFADTVGINMPQEFGELVAYVIENTPGADDIVFAIHCHNDLGVATANTISGICAGARQVEVTINGIGERSGNAPLEEVVMALKCRGESLMDGVYTKIDSRQIMATSKMVQEHTGMYVQPHKPIVGDNCFVHESGIHQDGILKNRSTYEILSPEDVGIVKSENSGIVLGKLSGRHAVKDRLKELGYEISDEKFNDIFSRYRELTKDKKRITDADLKALVVNGAEISSEKLNSKGINDLMSSPQISAVV
UniProt ID: Q9FN52
Variant: F -> S at position 46-46
Variant annotation: in strain: cv. Ema-1
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Accepts all the omega-methylthio-2-oxoalkanoic acids needed to form the known C3 to C8 glucosinolates. Also able to convert pyruvate to citramalate, 2-oxoisovalerate to isopropylmalate, 4-methyl-2-oxopentanoate and 5-methyl-2-oxohexanoate for Leu-derived glucosinolates, 3-methyl-2-oxopentanoate for Ile-derived glucosinolates and phenylpyruvate to phenylethylglucosinolate.
Reference sequence:
MASLLLTSSSMITTSCRSMVLRSGLPIGSSFPSLRLTRPYDKATLFVSCCSAESKKVATSATDLKPIMERRPEYIPNKLPHKNYVRVLDTTLRDGEQSPGAALTPPQKLEIARQLAKLRVDIMEVGFPVSSEEEFEAIKTIAKTVGNEVDEETGYVPVICGIARCKKRDIEATWEALKYAKRPRVMLFTSTSEIHMKYKLKKTKEEVIEMAVNSVKYAKSLGFKDIQFGCEDGGRTEKDFICKILGESIKAGATTVGFADTVGINMPQEFGELVAYVIENTPGADDIVFAIHCHNDLGVATANTISGICAGARQVEVTINGIGERSGNAPLEEVVMALKCRGESLMDGVYTKIDSRQIMATSKMVQEHTGMYVQPHKPIVGDNCFVHESGIHQDGILKNRSTYEILSPEDVGIVKSENSGIVLGKLSGRHAVKDRLKELGYEISDEKFNDIFSRYRELTKDKKRITDADLKALVVNGAEISSEKLNSKGINDLMSSPQISAVV
UniProt ID: Q9FN52
Variant: M -> V at position 68-68
Variant annotation: in strain: cv. Bl-0, cv. Di-G, cv. Landsberg erecta and cv. Petergof
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Accepts all the omega-methylthio-2-oxoalkanoic acids needed to form the known C3 to C8 glucosinolates. Also able to convert pyruvate to citramalate, 2-oxoisovalerate to isopropylmalate, 4-methyl-2-oxopentanoate and 5-methyl-2-oxohexanoate for Leu-derived glucosinolates, 3-methyl-2-oxopentanoate for Ile-derived glucosinolates and phenylpyruvate to phenylethylglucosinolate.
Reference sequence:
MASLLLTSSSMITTSCRSMVLRSGLPIGSSFPSLRLTRPYDKATLFVSCCSAESKKVATSATDLKPIMERRPEYIPNKLPHKNYVRVLDTTLRDGEQSPGAALTPPQKLEIARQLAKLRVDIMEVGFPVSSEEEFEAIKTIAKTVGNEVDEETGYVPVICGIARCKKRDIEATWEALKYAKRPRVMLFTSTSEIHMKYKLKKTKEEVIEMAVNSVKYAKSLGFKDIQFGCEDGGRTEKDFICKILGESIKAGATTVGFADTVGINMPQEFGELVAYVIENTPGADDIVFAIHCHNDLGVATANTISGICAGARQVEVTINGIGERSGNAPLEEVVMALKCRGESLMDGVYTKIDSRQIMATSKMVQEHTGMYVQPHKPIVGDNCFVHESGIHQDGILKNRSTYEILSPEDVGIVKSENSGIVLGKLSGRHAVKDRLKELGYEISDEKFNDIFSRYRELTKDKKRITDADLKALVVNGAEISSEKLNSKGINDLMSSPQISAVV
UniProt ID: Q9FN52
Variant: V -> A at position 156-156
Variant annotation: in strain: cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Tsu-1 and cv. Wl-0
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Accepts all the omega-methylthio-2-oxoalkanoic acids needed to form the known C3 to C8 glucosinolates. Also able to convert pyruvate to citramalate, 2-oxoisovalerate to isopropylmalate, 4-methyl-2-oxopentanoate and 5-methyl-2-oxohexanoate for Leu-derived glucosinolates, 3-methyl-2-oxopentanoate for Ile-derived glucosinolates and phenylpyruvate to phenylethylglucosinolate.
Reference sequence:
MASLLLTSSSMITTSCRSMVLRSGLPIGSSFPSLRLTRPYDKATLFVSCCSAESKKVATSATDLKPIMERRPEYIPNKLPHKNYVRVLDTTLRDGEQSPGAALTPPQKLEIARQLAKLRVDIMEVGFPVSSEEEFEAIKTIAKTVGNEVDEETGYVPVICGIARCKKRDIEATWEALKYAKRPRVMLFTSTSEIHMKYKLKKTKEEVIEMAVNSVKYAKSLGFKDIQFGCEDGGRTEKDFICKILGESIKAGATTVGFADTVGINMPQEFGELVAYVIENTPGADDIVFAIHCHNDLGVATANTISGICAGARQVEVTINGIGERSGNAPLEEVVMALKCRGESLMDGVYTKIDSRQIMATSKMVQEHTGMYVQPHKPIVGDNCFVHESGIHQDGILKNRSTYEILSPEDVGIVKSENSGIVLGKLSGRHAVKDRLKELGYEISDEKFNDIFSRYRELTKDKKRITDADLKALVVNGAEISSEKLNSKGINDLMSSPQISAVV
UniProt ID: Q9FN52
Variant: I -> L at position 241-241
Variant annotation: in strain: cv. Bl-0, cv. Di-G, cv. Ka-0, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Petergof, cv. Sei-0, cv. Tsu-1 and cv. Wl-0
Protein function: Determines the side chain length of aliphatic glucosinolate structures. Accepts all the omega-methylthio-2-oxoalkanoic acids needed to form the known C3 to C8 glucosinolates. Also able to convert pyruvate to citramalate, 2-oxoisovalerate to isopropylmalate, 4-methyl-2-oxopentanoate and 5-methyl-2-oxohexanoate for Leu-derived glucosinolates, 3-methyl-2-oxopentanoate for Ile-derived glucosinolates and phenylpyruvate to phenylethylglucosinolate.
Reference sequence:
MASLLLTSSSMITTSCRSMVLRSGLPIGSSFPSLRLTRPYDKATLFVSCCSAESKKVATSATDLKPIMERRPEYIPNKLPHKNYVRVLDTTLRDGEQSPGAALTPPQKLEIARQLAKLRVDIMEVGFPVSSEEEFEAIKTIAKTVGNEVDEETGYVPVICGIARCKKRDIEATWEALKYAKRPRVMLFTSTSEIHMKYKLKKTKEEVIEMAVNSVKYAKSLGFKDIQFGCEDGGRTEKDFICKILGESIKAGATTVGFADTVGINMPQEFGELVAYVIENTPGADDIVFAIHCHNDLGVATANTISGICAGARQVEVTINGIGERSGNAPLEEVVMALKCRGESLMDGVYTKIDSRQIMATSKMVQEHTGMYVQPHKPIVGDNCFVHESGIHQDGILKNRSTYEILSPEDVGIVKSENSGIVLGKLSGRHAVKDRLKELGYEISDEKFNDIFSRYRELTKDKKRITDADLKALVVNGAEISSEKLNSKGINDLMSSPQISAVV
UniProt ID: Q9FQA3
Variant: E -> D at position 141-141
Protein function: Involved in multiple disease resistance (MDR).
Reference sequence:
MAEKGVKVLGMWASPMVIRVEWALRLKGVEYEYVDEDLANKSADLLRHNPVTKKVPVLVHDGKPVAESTIIVEYIDEVWKGGYPIMPGDPYERAQARFWARFAEDKCNAALYPIFTATGEAQRKAVHEAQQCLKTLETALEGKKFFGGDAVGYLDIVVGWFAHWLPVIEEVTGASVVTHEELPLMKAWFGRFLALDVVKAALPDRDRLLAANKARREQLLSA
UniProt ID: Q9FQA3
Variant: H -> D at position 179-179
Protein function: Involved in multiple disease resistance (MDR).
Reference sequence:
MAEKGVKVLGMWASPMVIRVEWALRLKGVEYEYVDEDLANKSADLLRHNPVTKKVPVLVHDGKPVAESTIIVEYIDEVWKGGYPIMPGDPYERAQARFWARFAEDKCNAALYPIFTATGEAQRKAVHEAQQCLKTLETALEGKKFFGGDAVGYLDIVVGWFAHWLPVIEEVTGASVVTHEELPLMKAWFGRFLALDVVKAALPDRDRLLAANKARREQLLSA
UniProt ID: Q9FQA3
Variant: L -> V at position 195-195
Protein function: Involved in multiple disease resistance (MDR).
Reference sequence:
MAEKGVKVLGMWASPMVIRVEWALRLKGVEYEYVDEDLANKSADLLRHNPVTKKVPVLVHDGKPVAESTIIVEYIDEVWKGGYPIMPGDPYERAQARFWARFAEDKCNAALYPIFTATGEAQRKAVHEAQQCLKTLETALEGKKFFGGDAVGYLDIVVGWFAHWLPVIEEVTGASVVTHEELPLMKAWFGRFLALDVVKAALPDRDRLLAANKARREQLLSA
UniProt ID: Q9FRH7
Variant: L -> I at position 114-114
Variant annotation: in strain: cv. Lisse
Protein function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Reference sequence:
MSFRGIVQDLRDGFGSLSRRSFDFRLSSLHKGKAQGSSFREYSSSRDLLSPVIVQTSRWANLPPELLFDVIKRLEESESNWPARKHVVACASVCRSWRAMCQEIVLGPEICGKLTFPVSLKQPGPRDAMIQCFIKRDKSKLTFHLFLCLSPALLVENGKFLLSAKRTRRTTRTEYIISMDADNISRSSNSYLGKLRSNFLGTKFLVYDTQPPPNTSSSALITDRTSRSRFHSRRVSPKVPSGSYNIAQITYELNVLGTRGPRRMHCIMNSIPISSLEPGGSVPNQPEKLVPAPYSLDDSFRSNISFSKSSFDHRSLDFSSSRFSEMGISCDDNEEEASFRPLILKNKQPRWHEQLQCWCLNFRGRVTVASVKNFQLVAARQPQPQGTGAAAAPTSAPAHPEQDKVILQFGKVGKDMFTMDYRYPLSAFQAFAICLSSFDTKLACE
UniProt ID: Q9FRH7
Variant: Y -> F at position 244-244
Variant annotation: in strain: cv. Bretagny
Protein function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Reference sequence:
MSFRGIVQDLRDGFGSLSRRSFDFRLSSLHKGKAQGSSFREYSSSRDLLSPVIVQTSRWANLPPELLFDVIKRLEESESNWPARKHVVACASVCRSWRAMCQEIVLGPEICGKLTFPVSLKQPGPRDAMIQCFIKRDKSKLTFHLFLCLSPALLVENGKFLLSAKRTRRTTRTEYIISMDADNISRSSNSYLGKLRSNFLGTKFLVYDTQPPPNTSSSALITDRTSRSRFHSRRVSPKVPSGSYNIAQITYELNVLGTRGPRRMHCIMNSIPISSLEPGGSVPNQPEKLVPAPYSLDDSFRSNISFSKSSFDHRSLDFSSSRFSEMGISCDDNEEEASFRPLILKNKQPRWHEQLQCWCLNFRGRVTVASVKNFQLVAARQPQPQGTGAAAAPTSAPAHPEQDKVILQFGKVGKDMFTMDYRYPLSAFQAFAICLSSFDTKLACE
UniProt ID: Q9FT81
Variant: S -> Y at position 307-307
Variant annotation: in strain: cv. Wassilewskija-2
Protein function: Transcription activator, when associated with MYB75/PAP1 or MYB90/PAP2. Involved in the control of flavonoid pigmentation. Plays a key role in regulating leucoanthocyanidin reductase (BANYULS) and dihydroflavonol-4-reductase (DFR). Not required for leucoanthocyanidin dioxygenase (LDOX) expression.
Reference sequence:
MDESSIIPAEKVAGAEKKELQGLLKTAVQSVDWTYSVFWQFCPQQRVLVWGNGYYNGAIKTRKTTQPAEVTAEEAALERSQQLRELYETLLAGESTSEARACTALSPEDLTETEWFYLMCVSFSFPPPSGMPGKAYARRKHVWLSGANEVDSKTFSRAILAKSAKIQTVVCIPMLDGVVELGTTKKVREDVEFVELTKSFFYDHCKTNPKPALSEHSTYEVHEEAEDEEEVEEEMTMSEEMRLGSPDDEDVSNQNLHSDLHIESTHTLDTHMDMMNLMEEGGNYSQTVTTLLMSHPTSLLSDSVSTSSYIQSSFATWRVENGKEHQQVKTAPSSQWVLKQMIFRVPFLHDNTKDKRLPREDLSHVVAERRRREKLNEKFITLRSMVPFVTKMDKVSILGDTIAYVNHLRKRVHELENTHHEQQHKRTRTCKRKTSEEVEVSIIENDVLLEMRCEYRDGLLLDILQVLHELGIETTAVHTSVNDHDFEAEIRAKVRGKKASIAEVKRAIHQVIIHDTNL
UniProt ID: Q9FZ80
Variant: W -> R at position 183-183
Variant annotation: in strain: cv. C24
Protein function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of desulfo-glucosinolates (dsGSs), the final step in the biosynthesis of the glucosinolate core structure. Substrate preference is desulfo-benzyl glucosinolate > desulfo-6-methylthiohexyl glucosinolate. Increased specific activity with increasing chain length of desulfo-glucosinolate derived from methionine. Preferred substrate is desulfo-8-methylthiooctyl glucosinolate.
Reference sequence:
MESKTINDVVVSESNHELASSSPSEFEKNQKHYQEIIATLPHKDGWRPKDPFVEYGGHWWLQPLLEGLLHAQKFFKARPNDFFVCSYPKTGTTWLKALTFAIANRSKFDVSTNPLLKRNPHEFVPYIEIDFPFFPSVDVLKDEGNTLFSTHIPYDLLPESVVKSGCKIVYIWRDPKDTFVSMWTFAHKERSQQGPVVSIEEAFDKYCQGLSAYGPYLDHVLGYWKAYQANPDQILFLKYETMRADPLPYVKRLAEFMGYGFTKEEEEGNVVEKVVKLCSFETLKNLEANKGEKDREDRPAVYANSAYFRKGKVGDWQNYLTPEMVARIDGLMEEKFKGTGFLSSKS
UniProt ID: Q9FZ80
Variant: S -> T at position 344-344
Variant annotation: in strain: cv. C24
Protein function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of desulfo-glucosinolates (dsGSs), the final step in the biosynthesis of the glucosinolate core structure. Substrate preference is desulfo-benzyl glucosinolate > desulfo-6-methylthiohexyl glucosinolate. Increased specific activity with increasing chain length of desulfo-glucosinolate derived from methionine. Preferred substrate is desulfo-8-methylthiooctyl glucosinolate.
Reference sequence:
MESKTINDVVVSESNHELASSSPSEFEKNQKHYQEIIATLPHKDGWRPKDPFVEYGGHWWLQPLLEGLLHAQKFFKARPNDFFVCSYPKTGTTWLKALTFAIANRSKFDVSTNPLLKRNPHEFVPYIEIDFPFFPSVDVLKDEGNTLFSTHIPYDLLPESVVKSGCKIVYIWRDPKDTFVSMWTFAHKERSQQGPVVSIEEAFDKYCQGLSAYGPYLDHVLGYWKAYQANPDQILFLKYETMRADPLPYVKRLAEFMGYGFTKEEEEGNVVEKVVKLCSFETLKNLEANKGEKDREDRPAVYANSAYFRKGKVGDWQNYLTPEMVARIDGLMEEKFKGTGFLSSKS
UniProt ID: Q9G0S9
Variant: T -> A at position 2-2
Variant annotation: in strain: Isolate RMR 24
Protein function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Reference sequence:
MTNIRKTHPLMKIMNNSFIDLPAPSNISSWWNFGSLLGACLVIQIITGLFLAMHYTADTTTAFSSVTHICRDVNQGWIIRYLHANGASMFFLCLFLHVGRGMYYGSFTLTETWNIGIILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYMGTDLVEWIWGGFSVDKATLTRFFAFHFILPFVILALVMVHLLFLHETGSNNPLGIPSESDKIPFHPYYTIKDLLGLMFLLITLMILVLFSPDLLGDPDNYMPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVMSILILAIIPMLQTAKQRSMTFRPLSQIMFWILTADLLILTWIGGQPVEHPFVTIGQVASILYFSLILIIMPTVSLFENKMLKW
UniProt ID: Q9G0S9
Variant: V -> A at position 42-42
Variant annotation: in strain: Isolate Jorg 37
Protein function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Reference sequence:
MTNIRKTHPLMKIMNNSFIDLPAPSNISSWWNFGSLLGACLVIQIITGLFLAMHYTADTTTAFSSVTHICRDVNQGWIIRYLHANGASMFFLCLFLHVGRGMYYGSFTLTETWNIGIILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYMGTDLVEWIWGGFSVDKATLTRFFAFHFILPFVILALVMVHLLFLHETGSNNPLGIPSESDKIPFHPYYTIKDLLGLMFLLITLMILVLFSPDLLGDPDNYMPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVMSILILAIIPMLQTAKQRSMTFRPLSQIMFWILTADLLILTWIGGQPVEHPFVTIGQVASILYFSLILIIMPTVSLFENKMLKW