sujigwak/NVAR huggingface dataset:
UniProt ID: P11766
Variant: V -> I at position 309-309
Variant annotation: in dbSNP:rs28730628
Protein function: Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione . Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate . Class-III ADH is remarkably ineffective in oxidizing ethanol . Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage .
Reference sequence:
MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGYGAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATECINPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEEIATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFELMHSGKSIRTVVKI
UniProt ID: P11766
Variant: D -> E at position 353-353
Variant annotation: in dbSNP:rs16996593
Protein function: Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione . Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate . Class-III ADH is remarkably ineffective in oxidizing ethanol . Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage .
Reference sequence:
MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGYGAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATECINPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEEIATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFELMHSGKSIRTVVKI
UniProt ID: P11802
Variant: R -> C at position 24-24
Variant annotation: in CMM3; somatic and familial; generates a dominant oncogene resistant to inhibition by p16(INK4a); dbSNP:rs11547328
Protein function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.
Reference sequence:
MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE
UniProt ID: P11802
Variant: R -> H at position 24-24
Variant annotation: in CMM3; dbSNP:rs104894340
Protein function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.
Reference sequence:
MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE
UniProt ID: P11802
Variant: N -> S at position 41-41
Variant annotation: in CMM3; sporadic; dbSNP:rs144890720
Protein function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.
Reference sequence:
MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE
UniProt ID: P11802
Variant: R -> Q at position 82-82
Variant annotation: in dbSNP:rs3211612
Protein function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.
Reference sequence:
MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE
UniProt ID: P11802
Variant: R -> H at position 122-122
Variant annotation: in dbSNP:rs34386532
Protein function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.
Reference sequence:
MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE
UniProt ID: P11840
Variant: T -> I at position 156-156
Protein function: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
Reference sequence:
MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKEERFFNDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLPNTVPAKSCQAQPTTMTRHPHPHLSFMAIPPKKNQDKTEIPTINTIVSVEPTSTPTTEAIENTVATLEASSEVIESVPETNTAQVTSTVV
UniProt ID: P11840
Variant: E -> D at position 172-172
Protein function: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
Reference sequence:
MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKEERFFNDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLPNTVPAKSCQAQPTTMTRHPHPHLSFMAIPPKKNQDKTEIPTINTIVSVEPTSTPTTEAIENTVATLEASSEVIESVPETNTAQVTSTVV
UniProt ID: P11844
Variant: S -> C at position 40-40
Variant annotation: found in a patient with congenital bilateral cataract; uncertain significance; dbSNP:rs371745828
Protein function: Crystallins are the dominant structural components of the vertebrate eye lens.
Reference sequence:
MGKITFYEDRDFQGRCYNCISDCPNLRVYFSRCNSIRVDSGCWMLYERPNYQGHQYFLRRGKYPDYQHWMGLSDSVQSCRIIPHTSSHKLRLYERDDYRGLMSELTDDCACVPELFRLPEIYSLHVLEGCWVLYEMPNYRGRQYLLRPGDYRRYHDWGGADAKVGSLRRVTDLY
UniProt ID: P11844
Variant: R -> H at position 80-80
Variant annotation: found in a patient with congenital pediatric onset cataracts; uncertain significance; dbSNP:rs139353014
Protein function: Crystallins are the dominant structural components of the vertebrate eye lens.
Reference sequence:
MGKITFYEDRDFQGRCYNCISDCPNLRVYFSRCNSIRVDSGCWMLYERPNYQGHQYFLRRGKYPDYQHWMGLSDSVQSCRIIPHTSSHKLRLYERDDYRGLMSELTDDCACVPELFRLPEIYSLHVLEGCWVLYEMPNYRGRQYLLRPGDYRRYHDWGGADAKVGSLRRVTDLY
UniProt ID: P11844
Variant: P -> L at position 148-148
Variant annotation: in dbSNP:rs763049410
Protein function: Crystallins are the dominant structural components of the vertebrate eye lens.
Reference sequence:
MGKITFYEDRDFQGRCYNCISDCPNLRVYFSRCNSIRVDSGCWMLYERPNYQGHQYFLRRGKYPDYQHWMGLSDSVQSCRIIPHTSSHKLRLYERDDYRGLMSELTDDCACVPELFRLPEIYSLHVLEGCWVLYEMPNYRGRQYLLRPGDYRRYHDWGGADAKVGSLRRVTDLY
UniProt ID: P11860
Variant: S -> T at position 6-6
Variant annotation: possible variant of component I
Protein function: Involved in nuclear basic protein transition: histones are replaced by spermatid specific proteins which are themselves replaced by protamines in late spermatids.
Reference sequence:
AKAKRSPRKKKAAVKKSSKSKAKKPKSPKKKKAAKKPAKKAAKKK
UniProt ID: P11860
Variant: A -> T at position 12-12
Variant annotation: in component II
Protein function: Involved in nuclear basic protein transition: histones are replaced by spermatid specific proteins which are themselves replaced by protamines in late spermatids.
Reference sequence:
AKAKRSPRKKKAAVKKSSKSKAKKPKSPKKKKAAKKPAKKAAKKK
UniProt ID: P11860
Variant: S -> T at position 17-17
Variant annotation: possible variant of component I
Protein function: Involved in nuclear basic protein transition: histones are replaced by spermatid specific proteins which are themselves replaced by protamines in late spermatids.
Reference sequence:
AKAKRSPRKKKAAVKKSSKSKAKKPKSPKKKKAAKKPAKKAAKKK
UniProt ID: P11860
Variant: S -> T at position 18-18
Variant annotation: possible variant of component I
Protein function: Involved in nuclear basic protein transition: histones are replaced by spermatid specific proteins which are themselves replaced by protamines in late spermatids.
Reference sequence:
AKAKRSPRKKKAAVKKSSKSKAKKPKSPKKKKAAKKPAKKAAKKK
UniProt ID: P11860
Variant: K -> R at position 39-39
Variant annotation: in component III
Protein function: Involved in nuclear basic protein transition: histones are replaced by spermatid specific proteins which are themselves replaced by protamines in late spermatids.
Reference sequence:
AKAKRSPRKKKAAVKKSSKSKAKKPKSPKKKKAAKKPAKKAAKKK
UniProt ID: P11880
Variant: A -> T at position 288-288
Variant annotation: in murF2; temperature-sensitive mutant with low activity
Protein function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Reference sequence:
MISVTLSQLTDILNGELQGADITLDAVTTDTRKLTPGCLFVALKGERFDAHDFADQAKAGGAGALLVSRPLDIDLPQLIVKDTRLAFGELAAWVRQQVPARVVALTGSSGKTSVKEMTAAILSQCGNTLYTAGNLNNDIGVPMTLLRLTPEYDYAVIELGANHQGEIAWTVSLTRPEAALVNNLAAAHLEGFGSLAGVAKAKGEIFSGLPENGIAIMNADNNDWLNWQSVIGSRKVWRFSPNAANSDFTATNIHVTSHGTEFTLQTPTGSVDVLLPLPGRHNIANALAAAALSMSVGATLDAIKAGLANLKAVPGRLFPIQLAENQLLLDDSYNANVGSMTAAVQVLAEMPGYRVLVVGDMAELGAESEACHVQVGEAAKAAGIDRVLSVGKQSHAISTASGVGEHFADKTALITRLKLLIAEQQVITILVKGSRSAAMEEVVRALQENGTC
UniProt ID: P11884
Variant: Q -> R at position 86-86
Variant annotation: in allele Aldh2*2 and allele Aldh2*3; in strains UChA and UChB
Protein function: Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage.
Reference sequence:
MLRAALSTARRGPRLSRLLSAAATSAVPAPNQQPEVFCNQIFINNEWHDAVSKKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAAQAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
UniProt ID: P11884
Variant: E -> K at position 498-498
Variant annotation: in allele Aldh2*3; in strain: UChB
Protein function: Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage.
Reference sequence:
MLRAALSTARRGPRLSRLLSAAATSAVPAPNQQPEVFCNQIFINNEWHDAVSKKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAAQAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
UniProt ID: P11964
Variant: S -> A at position 55-55
Protein function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Reference sequence:
MASQTLVSPSPLSSHSLLRTSFSGVSVKLAPQFSTLATSNFKPLTVVAAAKKAVSVLKGTSAVEGVVTLTQDDEGPTTVNVRITGLTPGLHGFHLHEYGDTTNGCISTGPHFNPNKLTHGAPEDEIRHAGDLGNIVANAEGVAEATIVDNQIPLTGPNSVVGRALVVHELQDDLGKGGHELSLSTGNAGGRLACGVVGLTPV
UniProt ID: P11978
Variant: P -> L at position 994-994
Protein function: The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR . The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure . Involves the compaction of chromatin fiber into a more condensed form .
Reference sequence:
MPNDNKTPNRSSTPKFTKKPVTPNDKIPEREEKSNEVKTPKIPLFTFAKSKNYSRPSTAIHTSPHQPSDVKPTSHKQLQQPKSSPLKKNNYNSFPHSNLEKISNSKLLSLLRSKTSAGRIESNNPSHDASRSLASFEQTAFSRHAQQQTSTFNSKPVRTIVPISTSQTNNSFLSGVKSLLSEEKIRDYSKEILGINLANEQPVLEKPLKKGSADIGASVISLTKDKSIRKDTVEEKKEEKLNIGKNFAHSDSLSVPKVSAGDSGISPEESKARSPGIAKPNAIQTEVYGINEESTNERLEINQEKPVKLDENSANSTVASALDTNGTSATTETLTSKKIVPSPKKVAIDQDKITLHDEKTLAPSKHQPITSEQKMKEDADLKRMEILKSPHLSKSPADRPQGRRNSRNFSTRDEETTKLAFLVEYEGQENNYNSTSRSTEKKNDMNTSAKNKNGENKKIGKRPPEIMSTEAHVNKVTEETTKQIQSVRIDGRKVLQKVQGESHIDSRNNTLNVTPSKRPQLGEIPNPMKKHKPNEGRTPNISNGTINIQKKLEPKEIVRDILHTKESSNEAKKTIQNPLNKSQNTALPSTHKVTQKKDIKIGTNDLFQVESAPKISSEIDRENVKSKDEPVSKAVESKSLLNLFSNVLKAPFIKSESKPFSSDALSKEKANFLETIASTEKPENKTDKVSLSQPVSASKHEYSDNFPVSLSQPSKKSFANHTEDEQIEKKKICRGRMNTIITHPGKMELVYVSDSDDSSSDNDSLTDLESLSSGESNEIKVTNDLDTSAEKDQIQAGKWFDPVLDWRKSDRELTKNILWRIADKTTYDKETITDLIEQGIPKHSYLSGNPLTSVTNDICSVENYETSSAFFYQQVHKKDRLQYLPLYAVSTFENTNNTEKNDVTNKNINIGKHSQEQNSSSAKPSQIPTVSSPLGFEETKLSTTPTKSNRRVSHSDTNSSKPKNTKENLSKSSWRQEWLANLKLISVSLVDEFPSELSDSDRQIINEKMQLLKDIFANNLKSAISNNFRESDIIILKGEIEDYPMSSEIKIYYNELQNKPDAKKARFWSFMKTQRFVSNMGFDIQKSCEPVSISTSVKPHVVEPEHMADAKIMPKDILQITKKPLMVKNVKPSSPPDVKSLVQLSTMETKTLPEKKQFDSIFNSNKAKIIPGNGKHASENISLSFSRPASYGYFSVGKRVPIVEDRRVKQLDDITDSNTTEILTSVDVLGTHSQTGTQQSNMYTSTQKTELEIDNKDSVTECSKDMKEDGLSFVDIVLSKAASALDEKEKQLAVANEIIRSLSDEVMRNEIRITSLQGDLTFTKKCLENARSQISEKDAKINKLMEKDFQVNKEIKPY
UniProt ID: P11985
Variant: Q -> E at position 17-17
Variant annotation: in T-haplotype
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P11985
Variant: R -> S at position 23-23
Variant annotation: in T-haplotype
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P11985
Variant: K -> R at position 26-26
Variant annotation: in T-haplotype
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P11985
Variant: ERL -> P at position 41-43
Variant annotation: in T-haplotype
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P11985
Variant: H -> R at position 48-48
Variant annotation: in T-haplotype
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P11985
Variant: Y -> F at position 52-52
Variant annotation: in T-haplotype
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P11985
Variant: S -> A at position 60-60
Variant annotation: in T-haplotype
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P11985
Variant: V -> S at position 64-64
Variant annotation: in T-haplotype; requires 2 nucleotide substitutions
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P11985
Variant: L -> S at position 93-93
Variant annotation: in T-haplotype
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P11985
Variant: G -> R at position 125-125
Variant annotation: in T-haplotype
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P11985
Variant: A -> G at position 153-153
Variant annotation: in T-haplotype
Protein function: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility.
Reference sequence:
MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE
UniProt ID: P12004
Variant: S -> I at position 228-228
Variant annotation: in ATLD2; a hypomorphic mutation affecting DNA repair in response to UV; results in significantly decreased interaction with FEN1, LIG1 and ERCC5; dbSNP:rs369958038
Protein function: Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand . Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways . Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion .
Reference sequence:
MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS
UniProt ID: P12018
Variant: D -> N at position 76-76
Variant annotation: in dbSNP:rs1320
Protein function: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation.
Reference sequence:
MSWAPVLLMLFVYCTGCGPQPVLHQPPAMSSALGTTIRLTCTLRNDHDIGVYSVYWYQQRPGHPPRFLLRYFSQSDKSQGPQVPPRFSGSKDVARNRGYLSISELQPEDEAMYYCAMGARSSEKEEREREWEEEMEPTAARTRVP
UniProt ID: P12018
Variant: S -> L at position 122-122
Variant annotation: in dbSNP:rs11089979
Protein function: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation.
Reference sequence:
MSWAPVLLMLFVYCTGCGPQPVLHQPPAMSSALGTTIRLTCTLRNDHDIGVYSVYWYQQRPGHPPRFLLRYFSQSDKSQGPQVPPRFSGSKDVARNRGYLSISELQPEDEAMYYCAMGARSSEKEEREREWEEEMEPTAARTRVP
UniProt ID: P12018
Variant: E -> K at position 132-132
Variant annotation: in dbSNP:rs5995720
Protein function: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation.
Reference sequence:
MSWAPVLLMLFVYCTGCGPQPVLHQPPAMSSALGTTIRLTCTLRNDHDIGVYSVYWYQQRPGHPPRFLLRYFSQSDKSQGPQVPPRFSGSKDVARNRGYLSISELQPEDEAMYYCAMGARSSEKEEREREWEEEMEPTAARTRVP