sujigwak/NVAR huggingface dataset:
UniProt ID: P32745
Variant: R -> H at position 414-414
Variant annotation: in dbSNP:rs4988471
Protein function: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase.
Reference sequence:
MDMLHPSSVSTTSEPENASSAWPPDATLGNVSAGPSPAGLAVSGVLIPLVYLVVCVVGLLGNSLVIYVVLRHTASPSVTNVYILNLALADELFMLGLPFLAAQNALSYWPFGSLMCRLVMAVDGINQFTSIFCLTVMSVDRYLAVVHPTRSARWRTAPVARTVSAAVWVASAVVVLPVVVFSGVPRGMSTCHMQWPEPAAAWRAGFIIYTAALGFFGPLLVICLCYLLIVVKVRSAGRRVWAPSCQRRRRSERRVTRMVVAVVALFVLCWMPFYVLNIVNVVCPLPEEPAFFGLYFLVVALPYANSCANPILYGFLSYRFKQGFRRVLLRPSRRVRSQEPTVGPPEKTEEEDEEEEDGEESREGGKGKEMNGRVSQITQPGTSGQERPPSRVASKEQQLLPQEASTGEKSSTMRISYL
UniProt ID: P32780
Variant: R -> W at position 234-234
Variant annotation: in dbSNP:rs4150603
Protein function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Reference sequence:
MATSSEEVLLIVKKVRQKKQDGALYLMAERIAWAPEGKDRFTISHMYADIKCQKISPEGKAKIQLQLVLHAGDTTNFHFSNESTAVKERDAVKDLLQQLLPKFKRKANKELEEKNRMLQEDPVLFQLYKDLVVSQVISAEEFWANRLNVNATDSSSTSNHKQDVGISAAFLADVRPQTDGCNGLRYNLTSDIIESIFRTYPAVKMKYAENVPHNMTEKEFWTRFFQSHYFHRDRLNTGSKDLFAECAKIDEKGLKTMVSLGVKNPLLDLTALEDKPLDEGYGISSVPSASNSKSIKENSNAAIIKRFNHHSAMVLAAGLRKQEAQNEQTSEPSNMDGNSGDADCFQPAVKRAKLQESIEYEDLGKNNSVKTIALNLKKSDRYYHGPTPIQSLQYATSQDIINSFQSIRQEMEAYTPKLTQVLSSSAASSTITALSPGGALMQGGTQQAINQMVPNDIQSELKHLYVAVGELLRHFWSCFPVNTPFLEEKVVKMKSNLERFQVTKLCPFQEKIRRQYLSTNLVSHIEEMLQTAYNKLHTWQSRRLMKKT
UniProt ID: P32780
Variant: S -> F at position 285-285
Variant annotation: in dbSNP:rs4150636
Protein function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Reference sequence:
MATSSEEVLLIVKKVRQKKQDGALYLMAERIAWAPEGKDRFTISHMYADIKCQKISPEGKAKIQLQLVLHAGDTTNFHFSNESTAVKERDAVKDLLQQLLPKFKRKANKELEEKNRMLQEDPVLFQLYKDLVVSQVISAEEFWANRLNVNATDSSSTSNHKQDVGISAAFLADVRPQTDGCNGLRYNLTSDIIESIFRTYPAVKMKYAENVPHNMTEKEFWTRFFQSHYFHRDRLNTGSKDLFAECAKIDEKGLKTMVSLGVKNPLLDLTALEDKPLDEGYGISSVPSASNSKSIKENSNAAIIKRFNHHSAMVLAAGLRKQEAQNEQTSEPSNMDGNSGDADCFQPAVKRAKLQESIEYEDLGKNNSVKTIALNLKKSDRYYHGPTPIQSLQYATSQDIINSFQSIRQEMEAYTPKLTQVLSSSAASSTITALSPGGALMQGGTQQAINQMVPNDIQSELKHLYVAVGELLRHFWSCFPVNTPFLEEKVVKMKSNLERFQVTKLCPFQEKIRRQYLSTNLVSHIEEMLQTAYNKLHTWQSRRLMKKT
UniProt ID: P32780
Variant: L -> V at position 517-517
Variant annotation: in dbSNP:rs4150665
Protein function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Reference sequence:
MATSSEEVLLIVKKVRQKKQDGALYLMAERIAWAPEGKDRFTISHMYADIKCQKISPEGKAKIQLQLVLHAGDTTNFHFSNESTAVKERDAVKDLLQQLLPKFKRKANKELEEKNRMLQEDPVLFQLYKDLVVSQVISAEEFWANRLNVNATDSSSTSNHKQDVGISAAFLADVRPQTDGCNGLRYNLTSDIIESIFRTYPAVKMKYAENVPHNMTEKEFWTRFFQSHYFHRDRLNTGSKDLFAECAKIDEKGLKTMVSLGVKNPLLDLTALEDKPLDEGYGISSVPSASNSKSIKENSNAAIIKRFNHHSAMVLAAGLRKQEAQNEQTSEPSNMDGNSGDADCFQPAVKRAKLQESIEYEDLGKNNSVKTIALNLKKSDRYYHGPTPIQSLQYATSQDIINSFQSIRQEMEAYTPKLTQVLSSSAASSTITALSPGGALMQGGTQQAINQMVPNDIQSELKHLYVAVGELLRHFWSCFPVNTPFLEEKVVKMKSNLERFQVTKLCPFQEKIRRQYLSTNLVSHIEEMLQTAYNKLHTWQSRRLMKKT
UniProt ID: P32805
Variant: G -> E at position 110-110
Variant annotation: in strain: Sgu52E and Sgu52F
Protein function: May function as a transcription factor.
Reference sequence:
MTDIGRTKSRNYKCSFDGCEKVYNRPSLLQQHQNSHTNQKPYHCDEPGCGKKFIRPCHLRVHKWTHSQIKPKACTLCQKRFVTNQQLRRHLNSHERKSKLASRIDRKHEGVNANVKAELNGKEGGFDPKLPSGSPMCGEEFSQGHLPGYDDMQVLQCPYKSCQKVTSFNDDLINHMLQHHIASKLVVPSGDPSLKESLPTSEKSSSTDTTSIPQLSFSTTGTSSSESVDSTTAQTPTDPESYWSDNRCKHSDCQELSPFASVFDLIDHYDHTHAFIPETLVKYSYIHLYKPSVWDLFEY
UniProt ID: P32805
Variant: N -> D at position 120-120
Variant annotation: in strain: MMW1-15h2, MMW1-2h2, Sgu52E and Sgu52F
Protein function: May function as a transcription factor.
Reference sequence:
MTDIGRTKSRNYKCSFDGCEKVYNRPSLLQQHQNSHTNQKPYHCDEPGCGKKFIRPCHLRVHKWTHSQIKPKACTLCQKRFVTNQQLRRHLNSHERKSKLASRIDRKHEGVNANVKAELNGKEGGFDPKLPSGSPMCGEEFSQGHLPGYDDMQVLQCPYKSCQKVTSFNDDLINHMLQHHIASKLVVPSGDPSLKESLPTSEKSSSTDTTSIPQLSFSTTGTSSSESVDSTTAQTPTDPESYWSDNRCKHSDCQELSPFASVFDLIDHYDHTHAFIPETLVKYSYIHLYKPSVWDLFEY
UniProt ID: P32805
Variant: V -> I at position 228-228
Variant annotation: in strain: MMW1-15h2, MMW1-2h2, Sgu52E and Sgu52F
Protein function: May function as a transcription factor.
Reference sequence:
MTDIGRTKSRNYKCSFDGCEKVYNRPSLLQQHQNSHTNQKPYHCDEPGCGKKFIRPCHLRVHKWTHSQIKPKACTLCQKRFVTNQQLRRHLNSHERKSKLASRIDRKHEGVNANVKAELNGKEGGFDPKLPSGSPMCGEEFSQGHLPGYDDMQVLQCPYKSCQKVTSFNDDLINHMLQHHIASKLVVPSGDPSLKESLPTSEKSSSTDTTSIPQLSFSTTGTSSSESVDSTTAQTPTDPESYWSDNRCKHSDCQELSPFASVFDLIDHYDHTHAFIPETLVKYSYIHLYKPSVWDLFEY
UniProt ID: P32805
Variant: D -> N at position 238-238
Variant annotation: in strain: MMW1-15h2 and MMW1-2h2
Protein function: May function as a transcription factor.
Reference sequence:
MTDIGRTKSRNYKCSFDGCEKVYNRPSLLQQHQNSHTNQKPYHCDEPGCGKKFIRPCHLRVHKWTHSQIKPKACTLCQKRFVTNQQLRRHLNSHERKSKLASRIDRKHEGVNANVKAELNGKEGGFDPKLPSGSPMCGEEFSQGHLPGYDDMQVLQCPYKSCQKVTSFNDDLINHMLQHHIASKLVVPSGDPSLKESLPTSEKSSSTDTTSIPQLSFSTTGTSSSESVDSTTAQTPTDPESYWSDNRCKHSDCQELSPFASVFDLIDHYDHTHAFIPETLVKYSYIHLYKPSVWDLFEY
UniProt ID: P32807
Variant: T -> K at position 21-21
Variant annotation: in strain: ABYS 60 and SK1
Protein function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.
Reference sequence:
MRSVTNAFGNSGELNDQVDETGYRKFDIHEGILFCIELSETMFKESSDLEYKSPLLEILESLDELMSQLVITRPGTAIGCYFYYCNREDAKEGIYELFPLRDINATFMKKLNDLLEDLSSGRISLYDYFMFQQTGSEKQVRLSVLFTFMLDTFLEEIPGQKQLSNKRVFLFTDIDKPQEAQDIDERARLRRLTIDLFDNKVNFATFFIGYADKPFDNEFYSDILQLGSHTNENTGLDSEFDGPSTKPIDAKYIKSRILRKKEVKRIMFQCPLILDEKTNFIVGVKGYTMYTHEKAGVRYKLVYEHEDIRQEAYSKRKFLNPITGEDVTGKTVKVYPYGDLDINLSDSQDQIVMEAYTQKDAFLKIIGFRSSSKSIHYFNNIDKSSFIVPDEAKYEGSIRTLASLLKILRKKDKIAILWGKLKSNSHPSLYTLSPSSVKDYNEGFYLYRVPFLDEIRKFPSLLSYDDGSEHKLDYDNMKKVTQSIMGYFNLRDGYNPSDFKNPLLQKHYKVLHDYLLQIETTFDENETPNTKKDRMMREDDSLRKLYYIRNKILESEKSEDPIIQRLNKYVKIWNMFYKKFNDDNISIKEEKKPFDKKPKFNI
UniProt ID: P32807
Variant: E -> D at position 50-50
Variant annotation: in strain: ABYS 60, DBVPG6044, SK1 and YPS128
Protein function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.
Reference sequence:
MRSVTNAFGNSGELNDQVDETGYRKFDIHEGILFCIELSETMFKESSDLEYKSPLLEILESLDELMSQLVITRPGTAIGCYFYYCNREDAKEGIYELFPLRDINATFMKKLNDLLEDLSSGRISLYDYFMFQQTGSEKQVRLSVLFTFMLDTFLEEIPGQKQLSNKRVFLFTDIDKPQEAQDIDERARLRRLTIDLFDNKVNFATFFIGYADKPFDNEFYSDILQLGSHTNENTGLDSEFDGPSTKPIDAKYIKSRILRKKEVKRIMFQCPLILDEKTNFIVGVKGYTMYTHEKAGVRYKLVYEHEDIRQEAYSKRKFLNPITGEDVTGKTVKVYPYGDLDINLSDSQDQIVMEAYTQKDAFLKIIGFRSSSKSIHYFNNIDKSSFIVPDEAKYEGSIRTLASLLKILRKKDKIAILWGKLKSNSHPSLYTLSPSSVKDYNEGFYLYRVPFLDEIRKFPSLLSYDDGSEHKLDYDNMKKVTQSIMGYFNLRDGYNPSDFKNPLLQKHYKVLHDYLLQIETTFDENETPNTKKDRMMREDDSLRKLYYIRNKILESEKSEDPIIQRLNKYVKIWNMFYKKFNDDNISIKEEKKPFDKKPKFNI
UniProt ID: P32807
Variant: T -> A at position 230-230
Variant annotation: in strain: DBVPG6044
Protein function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.
Reference sequence:
MRSVTNAFGNSGELNDQVDETGYRKFDIHEGILFCIELSETMFKESSDLEYKSPLLEILESLDELMSQLVITRPGTAIGCYFYYCNREDAKEGIYELFPLRDINATFMKKLNDLLEDLSSGRISLYDYFMFQQTGSEKQVRLSVLFTFMLDTFLEEIPGQKQLSNKRVFLFTDIDKPQEAQDIDERARLRRLTIDLFDNKVNFATFFIGYADKPFDNEFYSDILQLGSHTNENTGLDSEFDGPSTKPIDAKYIKSRILRKKEVKRIMFQCPLILDEKTNFIVGVKGYTMYTHEKAGVRYKLVYEHEDIRQEAYSKRKFLNPITGEDVTGKTVKVYPYGDLDINLSDSQDQIVMEAYTQKDAFLKIIGFRSSSKSIHYFNNIDKSSFIVPDEAKYEGSIRTLASLLKILRKKDKIAILWGKLKSNSHPSLYTLSPSSVKDYNEGFYLYRVPFLDEIRKFPSLLSYDDGSEHKLDYDNMKKVTQSIMGYFNLRDGYNPSDFKNPLLQKHYKVLHDYLLQIETTFDENETPNTKKDRMMREDDSLRKLYYIRNKILESEKSEDPIIQRLNKYVKIWNMFYKKFNDDNISIKEEKKPFDKKPKFNI
UniProt ID: P32807
Variant: F -> I at position 368-368
Variant annotation: in strain: YPS128
Protein function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.
Reference sequence:
MRSVTNAFGNSGELNDQVDETGYRKFDIHEGILFCIELSETMFKESSDLEYKSPLLEILESLDELMSQLVITRPGTAIGCYFYYCNREDAKEGIYELFPLRDINATFMKKLNDLLEDLSSGRISLYDYFMFQQTGSEKQVRLSVLFTFMLDTFLEEIPGQKQLSNKRVFLFTDIDKPQEAQDIDERARLRRLTIDLFDNKVNFATFFIGYADKPFDNEFYSDILQLGSHTNENTGLDSEFDGPSTKPIDAKYIKSRILRKKEVKRIMFQCPLILDEKTNFIVGVKGYTMYTHEKAGVRYKLVYEHEDIRQEAYSKRKFLNPITGEDVTGKTVKVYPYGDLDINLSDSQDQIVMEAYTQKDAFLKIIGFRSSSKSIHYFNNIDKSSFIVPDEAKYEGSIRTLASLLKILRKKDKIAILWGKLKSNSHPSLYTLSPSSVKDYNEGFYLYRVPFLDEIRKFPSLLSYDDGSEHKLDYDNMKKVTQSIMGYFNLRDGYNPSDFKNPLLQKHYKVLHDYLLQIETTFDENETPNTKKDRMMREDDSLRKLYYIRNKILESEKSEDPIIQRLNKYVKIWNMFYKKFNDDNISIKEEKKPFDKKPKFNI
UniProt ID: P32807
Variant: I -> T at position 562-562
Variant annotation: in strain: ABYS 60, DBVPG6044, SK1 and YPS128
Protein function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.
Reference sequence:
MRSVTNAFGNSGELNDQVDETGYRKFDIHEGILFCIELSETMFKESSDLEYKSPLLEILESLDELMSQLVITRPGTAIGCYFYYCNREDAKEGIYELFPLRDINATFMKKLNDLLEDLSSGRISLYDYFMFQQTGSEKQVRLSVLFTFMLDTFLEEIPGQKQLSNKRVFLFTDIDKPQEAQDIDERARLRRLTIDLFDNKVNFATFFIGYADKPFDNEFYSDILQLGSHTNENTGLDSEFDGPSTKPIDAKYIKSRILRKKEVKRIMFQCPLILDEKTNFIVGVKGYTMYTHEKAGVRYKLVYEHEDIRQEAYSKRKFLNPITGEDVTGKTVKVYPYGDLDINLSDSQDQIVMEAYTQKDAFLKIIGFRSSSKSIHYFNNIDKSSFIVPDEAKYEGSIRTLASLLKILRKKDKIAILWGKLKSNSHPSLYTLSPSSVKDYNEGFYLYRVPFLDEIRKFPSLLSYDDGSEHKLDYDNMKKVTQSIMGYFNLRDGYNPSDFKNPLLQKHYKVLHDYLLQIETTFDENETPNTKKDRMMREDDSLRKLYYIRNKILESEKSEDPIIQRLNKYVKIWNMFYKKFNDDNISIKEEKKPFDKKPKFNI
UniProt ID: P32856
Variant: S -> T at position 42-42
Variant annotation: in dbSNP:rs17564
Protein function: Essential for epithelial morphogenesis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm.
Reference sequence:
MRDRLPDLTACRKNDDGDTVVVVEKDHFMDDFFHQVEEIRNSIDKITQYVEEVKKNHSIILSAPNPEGKIKEELEDLNKEIKKTANKIRAKLKAIEQSFDQDESGNRTSVDLRIRRTQHSVLSRKFVEAMAEYNEAQTLFRERSKGRIQRQLEITGRTTTDDELEEMLESGKPSIFTSDIISDSQITRQALNEIESRHKDIMKLETSIRELHEMFMDMAMFVETQGEMINNIERNVMNATDYVEHAKEETKKAIKYQSKARRKKWIIIAVSVVLVAIIALIIGLSVGK
UniProt ID: P32856
Variant: K -> R at position 54-54
Variant annotation: in dbSNP:rs7301926
Protein function: Essential for epithelial morphogenesis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm.
Reference sequence:
MRDRLPDLTACRKNDDGDTVVVVEKDHFMDDFFHQVEEIRNSIDKITQYVEEVKKNHSIILSAPNPEGKIKEELEDLNKEIKKTANKIRAKLKAIEQSFDQDESGNRTSVDLRIRRTQHSVLSRKFVEAMAEYNEAQTLFRERSKGRIQRQLEITGRTTTDDELEEMLESGKPSIFTSDIISDSQITRQALNEIESRHKDIMKLETSIRELHEMFMDMAMFVETQGEMINNIERNVMNATDYVEHAKEETKKAIKYQSKARRKKWIIIAVSVVLVAIIALIIGLSVGK
UniProt ID: P32881
Variant: E -> K at position 137-137
Variant annotation: in dbSNP:rs3739630
Protein function: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Reference sequence:
MALTFYLLVALVVLSYKSFSSLGCDLPQTHSLGNRRALILLAQMRRISPFSCLKDRHDFEFPQEEFDDKQFQKAQAISVLHEMIQQTFNLFSTKDSSAALDETLLDEFYIELDQQLNDLESCVMQEVGVIESPLMYEDSILAVRKYFQRITLYLTEKKYSSCAWEVVRAEIMRSFSLSINLQKRLKSKE
UniProt ID: P32887
Variant: K -> KK at position 134-134
Variant annotation: in ACL1.A3
Protein function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Reference sequence:
MATTFSASVSTLATSLATPTRISFQKPALVSRTNLSFNLRRSIPTRLSVSCAAKPETIEKVSKIVKKQLSLKDDQKVVAETKFADLGADSLDTVEIVMGLEEEFDIEMAEEKAQKIATVEEAAELIEELVLLKK
UniProt ID: P32890
Variant: T -> A at position 96-96
Variant annotation: in strain: 240-3 / ETEC
Protein function: The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
Reference sequence:
MNKVKCYVLFTALLSSLYAHGAPQTITELCSEYRNTQIYTINDKILSYTESMAGKREMVIITFKSGETFQVEVPGSQHIDSQKKAIERMKDTLRITYLTETKIDKLCVWNNKTPNSIAAISMKN
UniProt ID: P32926
Variant: V -> M at position 509-509
Variant annotation: in dbSNP:rs16961975
Protein function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Reference sequence:
MMGLFPRTTGALAIFVVVILVHGELRIETKGQYDEEEMTMQQAKRRQKREWVKFAKPCREGEDNSKRNPIAKITSDYQATQKITYRISGVGIDQPPFGIFVVDKNTGDINITAIVDREETPSFLITCRALNAQGLDVEKPLILTVKILDINDNPPVFSQQIFMGEIEENSASNSLVMILNATDADEPNHLNSKIAFKIVSQEPAGTPMFLLSRNTGEVRTLTNSLDREQASSYRLVVSGADKDGEGLSTQCECNIKVKDVNDNFPMFRDSQYSARIEENILSSELLRFQVTDLDEEYTDNWLAVYFFTSGNEGNWFEIQTDPRTNEGILKVVKALDYEQLQSVKLSIAVKNKAEFHQSVISRYRVQSTPVTIQVINVREGIAFRPASKTFTVQKGISSKKLVDYILGTYQAIDEDTNKAASNVKYVMGRNDGGYLMIDSKTAEIKFVKNMNRDSTFIVNKTITAEVLAIDEYTGKTSTGTVYVRVPDFNDNCPTAVLEKDAVCSSSPSVVVSARTLNNRYTGPYTFALEDQPVKLPAVWSITTLNATSALLRAQEQIPPGVYHISLVLTDSQNNRCEMPRSLTLEVCQCDNRGICGTSYPTTSPGTRYGRPHSGRLGPAAIGLLLLGLLLLLLAPLLLLTCDCGAGSTGGVTGGFIPVPDGSEGTIHQWGIEGAHPEDKEITNICVPPVTANGADFMESSEVCTNTYARGTAVEGTSGMEMTTKLGAATESGGAAGFATGTVSGAASGFGAATGVGICSSGQSGTMRTRHSTGGTNKDYADGAISMNFLDSYFSQKAFACAEEDDGQEANDCLLIYDNEGADATGSPVGSVGCCSFIADDLDDSFLDSLGPKFKKLAEISLGVDGEGKEVQPPSKDSGYGIESCGHPIEVQQTGFVKCQTLSGSQGASALSTSGSVQPAVSIPDPLQHGNYLVTETYSASGSLVQPSTAGFDPLLTQNVIVTERVICPISSVPGNLAGPTQLRGSHTMLCTEDPCSRLI
UniProt ID: P32926
Variant: T -> A at position 912-912
Variant annotation: in dbSNP:rs1380866
Protein function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Reference sequence:
MMGLFPRTTGALAIFVVVILVHGELRIETKGQYDEEEMTMQQAKRRQKREWVKFAKPCREGEDNSKRNPIAKITSDYQATQKITYRISGVGIDQPPFGIFVVDKNTGDINITAIVDREETPSFLITCRALNAQGLDVEKPLILTVKILDINDNPPVFSQQIFMGEIEENSASNSLVMILNATDADEPNHLNSKIAFKIVSQEPAGTPMFLLSRNTGEVRTLTNSLDREQASSYRLVVSGADKDGEGLSTQCECNIKVKDVNDNFPMFRDSQYSARIEENILSSELLRFQVTDLDEEYTDNWLAVYFFTSGNEGNWFEIQTDPRTNEGILKVVKALDYEQLQSVKLSIAVKNKAEFHQSVISRYRVQSTPVTIQVINVREGIAFRPASKTFTVQKGISSKKLVDYILGTYQAIDEDTNKAASNVKYVMGRNDGGYLMIDSKTAEIKFVKNMNRDSTFIVNKTITAEVLAIDEYTGKTSTGTVYVRVPDFNDNCPTAVLEKDAVCSSSPSVVVSARTLNNRYTGPYTFALEDQPVKLPAVWSITTLNATSALLRAQEQIPPGVYHISLVLTDSQNNRCEMPRSLTLEVCQCDNRGICGTSYPTTSPGTRYGRPHSGRLGPAAIGLLLLGLLLLLLAPLLLLTCDCGAGSTGGVTGGFIPVPDGSEGTIHQWGIEGAHPEDKEITNICVPPVTANGADFMESSEVCTNTYARGTAVEGTSGMEMTTKLGAATESGGAAGFATGTVSGAASGFGAATGVGICSSGQSGTMRTRHSTGGTNKDYADGAISMNFLDSYFSQKAFACAEEDDGQEANDCLLIYDNEGADATGSPVGSVGCCSFIADDLDDSFLDSLGPKFKKLAEISLGVDGEGKEVQPPSKDSGYGIESCGHPIEVQQTGFVKCQTLSGSQGASALSTSGSVQPAVSIPDPLQHGNYLVTETYSASGSLVQPSTAGFDPLLTQNVIVTERVICPISSVPGNLAGPTQLRGSHTMLCTEDPCSRLI
UniProt ID: P32927
Variant: E -> Q at position 249-249
Variant annotation: in dbSNP:rs16845
Protein function: Cell surface receptor that plays a role in immune response and controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Acts by forming an heterodimeric receptor through interaction with different partners such as IL3RA, IL5RA or CSF2RA . In turn, participates in various signaling pathways including interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor/CSF2 pathways. In unstimulated conditions, interacts constitutively with JAK1 and ligand binding leads to JAK1 stimulation and subsequent activation of the JAK-STAT pathway .
Reference sequence:
MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYIVSVQPRRAEKHIKSSVNIQMAPPSLNVTKDGDSYSLRWETMKMRYEHIDHTFEIQYRKDTATWKDSKTETLQNAHSMALPALEPSTRYWARVRVRTSRTGYNGIWSEWSEARSWDTESVLPMWVLALIVIFLTIAVLLALRFCGIYGYRLRRKWEEKIPNPSKSHLFQNGSAELWPPGSMSAFTSGSPPHQGPWGSRFPELEGVFPVGFGDSEVSPLTIEDPKHVCDPPSGPDTTPAASDLPTEQPPSPQPGPPAASHTPEKQASSFDFNGPYLGPPHSRSLPDILGQPEPPQEGGSQKSPPPGSLEYLCLPAGGQVQLVPLAQAMGPGQAVEVERRPSQGAAGSPSLESGGGPAPPALGPRVGGQDQKDSPVAIPMSSGDTEDPGVASGYVSSADLVFTPNSGASSVSLVPSLGLPSDQTPSLCPGLASGPPGAPGPVKSGFEGYVELPPIEGRSPRSPRNNPVPPEAKSPVLNPGERPADVSPTSPQPEGLLVLQQVGDYCFLPGLGPGPLSLRSKPSSPGPGPEIKNLDQAFQVKKPPGQAVPQVPVIQLFKALKQQDYLSLPPWEVNKPGEVC
UniProt ID: P32927
Variant: P -> T at position 603-603
Variant annotation: in dbSNP:rs1801122
Protein function: Cell surface receptor that plays a role in immune response and controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Acts by forming an heterodimeric receptor through interaction with different partners such as IL3RA, IL5RA or CSF2RA . In turn, participates in various signaling pathways including interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor/CSF2 pathways. In unstimulated conditions, interacts constitutively with JAK1 and ligand binding leads to JAK1 stimulation and subsequent activation of the JAK-STAT pathway .
Reference sequence:
MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYIVSVQPRRAEKHIKSSVNIQMAPPSLNVTKDGDSYSLRWETMKMRYEHIDHTFEIQYRKDTATWKDSKTETLQNAHSMALPALEPSTRYWARVRVRTSRTGYNGIWSEWSEARSWDTESVLPMWVLALIVIFLTIAVLLALRFCGIYGYRLRRKWEEKIPNPSKSHLFQNGSAELWPPGSMSAFTSGSPPHQGPWGSRFPELEGVFPVGFGDSEVSPLTIEDPKHVCDPPSGPDTTPAASDLPTEQPPSPQPGPPAASHTPEKQASSFDFNGPYLGPPHSRSLPDILGQPEPPQEGGSQKSPPPGSLEYLCLPAGGQVQLVPLAQAMGPGQAVEVERRPSQGAAGSPSLESGGGPAPPALGPRVGGQDQKDSPVAIPMSSGDTEDPGVASGYVSSADLVFTPNSGASSVSLVPSLGLPSDQTPSLCPGLASGPPGAPGPVKSGFEGYVELPPIEGRSPRSPRNNPVPPEAKSPVLNPGERPADVSPTSPQPEGLLVLQQVGDYCFLPGLGPGPLSLRSKPSSPGPGPEIKNLDQAFQVKKPPGQAVPQVPVIQLFKALKQQDYLSLPPWEVNKPGEVC