sujigwak/NVAR huggingface dataset:
UniProt ID: P33546
Variant: E -> G at position 443-443
Variant annotation: in plasmid pINV_F6_M1382
Protein function: Virulence-associated N-epsilon-fatty acyltransferase that mediates lysine-stearoylation of host Rho GTPase proteins, thereby disrupting the host actin cytoskeleton . Required at the post-invasion stage of Shigella pathogenicity .
Reference sequence:
MSLKISNFIDASNTKGPIRVEDTEHGPILIAQKFNLKDLFFRTLSTINAKINSQILNEQLKNYRLENQKSLLLFLNTLASEKSAESAFAAYEAAKNSIQHSFTGRDIKLMLNTAERFHGIGTAKNLERHLVFRCWGNRGITHLGHTSISIKNNLLQEPTHTYLSWYPGGNVTKDTEINYLFEKRSGYSVDTYKQDKLNMISEQTAERLDAGQEVRNLLNSKQDQNNNKKIFFPRANQKKDPYGYWGVSADKVYIPLSGDNKTKDGKISHNLFGLDETNMSKFICKKKADAFRQLANYKLISKSENCAGMALNVLKAGNSEIYFPLPDVKLVATPNDVYAYANKVRQRIESLNQSYNEIMKYIESDFDLSRLTQLRRSYLKSFNKINLIHTPKTFKPLSISLYKHPTENVSSEDFDAVINACHSYLVKSAPSNMTRVLNELKTEATDKKEEIIEKSIKIIDYYNSLKSPDLGTKLYIHDLLQINKLLLNNSHSNI
UniProt ID: P33546
Variant: E -> V at position 450-450
Variant annotation: in plasmid pINV_F6_M1382
Protein function: Virulence-associated N-epsilon-fatty acyltransferase that mediates lysine-stearoylation of host Rho GTPase proteins, thereby disrupting the host actin cytoskeleton . Required at the post-invasion stage of Shigella pathogenicity .
Reference sequence:
MSLKISNFIDASNTKGPIRVEDTEHGPILIAQKFNLKDLFFRTLSTINAKINSQILNEQLKNYRLENQKSLLLFLNTLASEKSAESAFAAYEAAKNSIQHSFTGRDIKLMLNTAERFHGIGTAKNLERHLVFRCWGNRGITHLGHTSISIKNNLLQEPTHTYLSWYPGGNVTKDTEINYLFEKRSGYSVDTYKQDKLNMISEQTAERLDAGQEVRNLLNSKQDQNNNKKIFFPRANQKKDPYGYWGVSADKVYIPLSGDNKTKDGKISHNLFGLDETNMSKFICKKKADAFRQLANYKLISKSENCAGMALNVLKAGNSEIYFPLPDVKLVATPNDVYAYANKVRQRIESLNQSYNEIMKYIESDFDLSRLTQLRRSYLKSFNKINLIHTPKTFKPLSISLYKHPTENVSSEDFDAVINACHSYLVKSAPSNMTRVLNELKTEATDKKEEIIEKSIKIIDYYNSLKSPDLGTKLYIHDLLQINKLLLNNSHSNI
UniProt ID: P33546
Variant: I -> T at position 458-458
Variant annotation: in plasmid pINV_F6_M1382
Protein function: Virulence-associated N-epsilon-fatty acyltransferase that mediates lysine-stearoylation of host Rho GTPase proteins, thereby disrupting the host actin cytoskeleton . Required at the post-invasion stage of Shigella pathogenicity .
Reference sequence:
MSLKISNFIDASNTKGPIRVEDTEHGPILIAQKFNLKDLFFRTLSTINAKINSQILNEQLKNYRLENQKSLLLFLNTLASEKSAESAFAAYEAAKNSIQHSFTGRDIKLMLNTAERFHGIGTAKNLERHLVFRCWGNRGITHLGHTSISIKNNLLQEPTHTYLSWYPGGNVTKDTEINYLFEKRSGYSVDTYKQDKLNMISEQTAERLDAGQEVRNLLNSKQDQNNNKKIFFPRANQKKDPYGYWGVSADKVYIPLSGDNKTKDGKISHNLFGLDETNMSKFICKKKADAFRQLANYKLISKSENCAGMALNVLKAGNSEIYFPLPDVKLVATPNDVYAYANKVRQRIESLNQSYNEIMKYIESDFDLSRLTQLRRSYLKSFNKINLIHTPKTFKPLSISLYKHPTENVSSEDFDAVINACHSYLVKSAPSNMTRVLNELKTEATDKKEEIIEKSIKIIDYYNSLKSPDLGTKLYIHDLLQINKLLLNNSHSNI
UniProt ID: P33546
Variant: I -> V at position 482-482
Variant annotation: in plasmid pINV_F6_M1382
Protein function: Virulence-associated N-epsilon-fatty acyltransferase that mediates lysine-stearoylation of host Rho GTPase proteins, thereby disrupting the host actin cytoskeleton . Required at the post-invasion stage of Shigella pathogenicity .
Reference sequence:
MSLKISNFIDASNTKGPIRVEDTEHGPILIAQKFNLKDLFFRTLSTINAKINSQILNEQLKNYRLENQKSLLLFLNTLASEKSAESAFAAYEAAKNSIQHSFTGRDIKLMLNTAERFHGIGTAKNLERHLVFRCWGNRGITHLGHTSISIKNNLLQEPTHTYLSWYPGGNVTKDTEINYLFEKRSGYSVDTYKQDKLNMISEQTAERLDAGQEVRNLLNSKQDQNNNKKIFFPRANQKKDPYGYWGVSADKVYIPLSGDNKTKDGKISHNLFGLDETNMSKFICKKKADAFRQLANYKLISKSENCAGMALNVLKAGNSEIYFPLPDVKLVATPNDVYAYANKVRQRIESLNQSYNEIMKYIESDFDLSRLTQLRRSYLKSFNKINLIHTPKTFKPLSISLYKHPTENVSSEDFDAVINACHSYLVKSAPSNMTRVLNELKTEATDKKEEIIEKSIKIIDYYNSLKSPDLGTKLYIHDLLQINKLLLNNSHSNI
UniProt ID: P33587
Variant: Q -> QQ at position 327-327
Variant annotation: in strain: BALB/c
Protein function: Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function.
Reference sequence:
MWQFRVFLLLMSTWGISSIPAHPDPVFSSSEHAHQVLRVRRANSFLEEMRPGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKYFDGDQCSAPPLDHQCDSPCCGHGTCIDGIGSFSCSCDKGWEGKFCQQELRFQDCRVNNGGCLHYCLEESNGRRCACAPGYELADDHMRCKSTVNFPCGKLGRWIEKKRKILKRDTDLEDELEPDPRIVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCVEGTKKLTVRLGEYDLRRRDHWELDLDIKEILVHPNYTRSSSDNDIALLRLAQPATLSKTIVPICLPNNGLAQELTQAGQETVVTGWGYQSDRIKDGRRNRTFILTFIRIPLVARNECVEVMKNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLKWIHSYIGEKGVSLKSQKL
UniProt ID: P33587
Variant: D -> N at position 392-392
Variant annotation: in strain: BALB/c
Protein function: Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function.
Reference sequence:
MWQFRVFLLLMSTWGISSIPAHPDPVFSSSEHAHQVLRVRRANSFLEEMRPGSLERECMEEICDFEEAQEIFQNVEDTLAFWIKYFDGDQCSAPPLDHQCDSPCCGHGTCIDGIGSFSCSCDKGWEGKFCQQELRFQDCRVNNGGCLHYCLEESNGRRCACAPGYELADDHMRCKSTVNFPCGKLGRWIEKKRKILKRDTDLEDELEPDPRIVNGTLTKQGDSPWQAILLDSKKKLACGGVLIHTSWVLTAAHCVEGTKKLTVRLGEYDLRRRDHWELDLDIKEILVHPNYTRSSSDNDIALLRLAQPATLSKTIVPICLPNNGLAQELTQAGQETVVTGWGYQSDRIKDGRRNRTFILTFIRIPLVARNECVEVMKNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVSWGEGCGHTNNYGIYTKVGSYLKWIHSYIGEKGVSLKSQKL
UniProt ID: P33609
Variant: S -> F at position 1180-1180
Variant annotation: in temperature-sensitive FT20 cell line; defective activity
Protein function: Catalytic subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis . During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, a regulatory subunit POLA2 and two primase subunits PRIM1 and PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes. In the cytosol, responsible for a substantial proportion of the physiological concentration of cytosolic RNA:DNA hybrids, which are necessary to prevent spontaneous activation of type I interferon responses.
Reference sequence:
MAPMHEEDCKLEASAVSDSGSFAASRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDLTSVYEEVDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDTCGKGSDGKAHRKDRKDVKKPSVTKPNNIKAMFIASAGKKTTDKAVDLSKDDLLGDILQDLNTETAQITPPPVLIPKKKRSTGALLNPFSVHTPKAIPSGKPASPVLRNEPLLTPIPLKRAELAGELAQPECPEDEQELGVMEFEDGDFDESMDTEKVDEKPVTAKTWDQETEPVERVEHEADPERGTTSYLENFLPDVSCWDIDQDDESIPQEVQVDSSNLPLVKGADDEQVFQFYWLDAYEDPYNQPGVVFLFGKVWIESVKTHVSCCVMVKNIERTLYFLPREMKFDLNTGKETAIPVTMKDVYEEFDSKISAKYKIMKFKSKIVEKNYAFEIPDVPEKSEYLEVRYSAEVPQLPQNLKGETFSHVFGTNTSSLELFLMNRKIKGPCWLEVKNPQLLNQPISWCKFEVMALKPDLVNVIKDVSPPPLVVMSFSMKTMQNVQNHQHEIIAMAALVHHSFALDKAPPEPPFQTHFCVVSKPKDCIFPCDFKEVISKKNMKVEIAATERTLIGFFLAKVHKIDPDILVGHNICSFELEVLLQRINECKVPYWSKIGRLRRSNMPKLGSRSGFGERNATCGRMICDVEISAKELIHCKSYHLSELVQQILKTERIVIPTENIRNMYSESSYLLYLLEHIWKDARFILQIMCELNVLPLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQKLGDEDEEIDGDTNKYKKGRKKATYAGGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNICFTTVQRVTSEVQKATEDEEQEQIPELPDPNLEMGILPREIRKLVERRKQVKQLMKQQDLNPDLVLQYDIRQKALKLTANSMYGCLGFSYSRFYAKPLAALVTYKGREILMHTKDMVQKMNLEVIYGDTDSIMINTNSTNLEEVFKLGNKVKSEVNKLYKLLEIDIDAVFKSLLLLKKKKYAALVVEPTSDGNYITKQELKGLDIVRRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKRLIEIGENVLNGSVPVSQFEINKALTKDPQDYPDRKSLPHVHVALWINSQGGRKVKAGDTVSYVICQDGSNLTATQRAYAPEQLQKLDNLAIDTQYYLAQQIHPVVARICEPIDGIDAVLIALWLGLDSTQFRVHQYHKDEENDALLGGPAQLTDEEKYKDCEKFKCLCPSCGTENIYDNVFEGSGLDMEPSLYRCSNVDCKVSPLTFMVQLSNKLIMDIRRCIKKYYDGWLICEEPTCCSRLRRLPLHFSRNGPLCPVCMKAVLRPEYSDKSLYTQLCFYRYIFDADCALEKLTEHEKDKLKKQFFPLRVLQDYRKVKNIAEQFLSWSGYSEVNLSKLFANYAGKS
UniProt ID: P33736
Variant: Q -> L at position 25-25
Variant annotation: in strain: 35
Protein function: This protein is transferred from male to female's hemolymph during mating, affecting egglaying and behavior after mating.
Reference sequence:
MNLILLCSQILLLLFTVANCDGEHQLDSSMDLKSDSTKSAVLKNVAPKNDATQAEIAKDDVALKSGKKGDYVMEIDVSDIPLDDYPINNSKSRKNSSTLPSQILTDKPNQGSNQIALKALKHRLLMEQNNNLFLRNHSVSLMNEIEARKTDIIQARQLNIDLELELEALKRELSEMNAQNARKSTKSCKKRPSKDIASPVNQLQEVIVKNTYRNKYLTLLTQLAQKINYEIANVNNPATDVPTGKSPSEGNPSTT
UniProt ID: P33736
Variant: K -> R at position 33-33
Variant annotation: in strain: 7
Protein function: This protein is transferred from male to female's hemolymph during mating, affecting egglaying and behavior after mating.
Reference sequence:
MNLILLCSQILLLLFTVANCDGEHQLDSSMDLKSDSTKSAVLKNVAPKNDATQAEIAKDDVALKSGKKGDYVMEIDVSDIPLDDYPINNSKSRKNSSTLPSQILTDKPNQGSNQIALKALKHRLLMEQNNNLFLRNHSVSLMNEIEARKTDIIQARQLNIDLELELEALKRELSEMNAQNARKSTKSCKKRPSKDIASPVNQLQEVIVKNTYRNKYLTLLTQLAQKINYEIANVNNPATDVPTGKSPSEGNPSTT
UniProt ID: P33736
Variant: S -> F at position 36-36
Variant annotation: in strain: 77 25 and Praslin
Protein function: This protein is transferred from male to female's hemolymph during mating, affecting egglaying and behavior after mating.
Reference sequence:
MNLILLCSQILLLLFTVANCDGEHQLDSSMDLKSDSTKSAVLKNVAPKNDATQAEIAKDDVALKSGKKGDYVMEIDVSDIPLDDYPINNSKSRKNSSTLPSQILTDKPNQGSNQIALKALKHRLLMEQNNNLFLRNHSVSLMNEIEARKTDIIQARQLNIDLELELEALKRELSEMNAQNARKSTKSCKKRPSKDIASPVNQLQEVIVKNTYRNKYLTLLTQLAQKINYEIANVNNPATDVPTGKSPSEGNPSTT
UniProt ID: P33736
Variant: T -> M at position 37-37
Variant annotation: in strain: 7
Protein function: This protein is transferred from male to female's hemolymph during mating, affecting egglaying and behavior after mating.
Reference sequence:
MNLILLCSQILLLLFTVANCDGEHQLDSSMDLKSDSTKSAVLKNVAPKNDATQAEIAKDDVALKSGKKGDYVMEIDVSDIPLDDYPINNSKSRKNSSTLPSQILTDKPNQGSNQIALKALKHRLLMEQNNNLFLRNHSVSLMNEIEARKTDIIQARQLNIDLELELEALKRELSEMNAQNARKSTKSCKKRPSKDIASPVNQLQEVIVKNTYRNKYLTLLTQLAQKINYEIANVNNPATDVPTGKSPSEGNPSTT
UniProt ID: P33736
Variant: K -> N at position 38-38
Variant annotation: in strain: 7
Protein function: This protein is transferred from male to female's hemolymph during mating, affecting egglaying and behavior after mating.
Reference sequence:
MNLILLCSQILLLLFTVANCDGEHQLDSSMDLKSDSTKSAVLKNVAPKNDATQAEIAKDDVALKSGKKGDYVMEIDVSDIPLDDYPINNSKSRKNSSTLPSQILTDKPNQGSNQIALKALKHRLLMEQNNNLFLRNHSVSLMNEIEARKTDIIQARQLNIDLELELEALKRELSEMNAQNARKSTKSCKKRPSKDIASPVNQLQEVIVKNTYRNKYLTLLTQLAQKINYEIANVNNPATDVPTGKSPSEGNPSTT
UniProt ID: P33736
Variant: S -> I at position 39-39
Variant annotation: in strain: 7
Protein function: This protein is transferred from male to female's hemolymph during mating, affecting egglaying and behavior after mating.
Reference sequence:
MNLILLCSQILLLLFTVANCDGEHQLDSSMDLKSDSTKSAVLKNVAPKNDATQAEIAKDDVALKSGKKGDYVMEIDVSDIPLDDYPINNSKSRKNSSTLPSQILTDKPNQGSNQIALKALKHRLLMEQNNNLFLRNHSVSLMNEIEARKTDIIQARQLNIDLELELEALKRELSEMNAQNARKSTKSCKKRPSKDIASPVNQLQEVIVKNTYRNKYLTLLTQLAQKINYEIANVNNPATDVPTGKSPSEGNPSTT
UniProt ID: P33736
Variant: L -> F at position 117-117
Variant annotation: in strain: 7
Protein function: This protein is transferred from male to female's hemolymph during mating, affecting egglaying and behavior after mating.
Reference sequence:
MNLILLCSQILLLLFTVANCDGEHQLDSSMDLKSDSTKSAVLKNVAPKNDATQAEIAKDDVALKSGKKGDYVMEIDVSDIPLDDYPINNSKSRKNSSTLPSQILTDKPNQGSNQIALKALKHRLLMEQNNNLFLRNHSVSLMNEIEARKTDIIQARQLNIDLELELEALKRELSEMNAQNARKSTKSCKKRPSKDIASPVNQLQEVIVKNTYRNKYLTLLTQLAQKINYEIANVNNPATDVPTGKSPSEGNPSTT
UniProt ID: P33736
Variant: I -> V at position 207-207
Variant annotation: in strain: 7
Protein function: This protein is transferred from male to female's hemolymph during mating, affecting egglaying and behavior after mating.
Reference sequence:
MNLILLCSQILLLLFTVANCDGEHQLDSSMDLKSDSTKSAVLKNVAPKNDATQAEIAKDDVALKSGKKGDYVMEIDVSDIPLDDYPINNSKSRKNSSTLPSQILTDKPNQGSNQIALKALKHRLLMEQNNNLFLRNHSVSLMNEIEARKTDIIQARQLNIDLELELEALKRELSEMNAQNARKSTKSCKKRPSKDIASPVNQLQEVIVKNTYRNKYLTLLTQLAQKINYEIANVNNPATDVPTGKSPSEGNPSTT
UniProt ID: P33736
Variant: G -> W at position 244-244
Variant annotation: in strain: 11
Protein function: This protein is transferred from male to female's hemolymph during mating, affecting egglaying and behavior after mating.
Reference sequence:
MNLILLCSQILLLLFTVANCDGEHQLDSSMDLKSDSTKSAVLKNVAPKNDATQAEIAKDDVALKSGKKGDYVMEIDVSDIPLDDYPINNSKSRKNSSTLPSQILTDKPNQGSNQIALKALKHRLLMEQNNNLFLRNHSVSLMNEIEARKTDIIQARQLNIDLELELEALKRELSEMNAQNARKSTKSCKKRPSKDIASPVNQLQEVIVKNTYRNKYLTLLTQLAQKINYEIANVNNPATDVPTGKSPSEGNPSTT
UniProt ID: P33739
Variant: A -> D at position 21-21
Variant annotation: in strain: 11, 35, 7725 and Robertson
Protein function: This protein is transferred from male to female during mating and may affect egglaying and behavior after mating.
Reference sequence:
MNYFAVLCIFSCICLWQFSDAAPFISVQSSSQSRSQKVMNGMLRTLYDYSVQDSVNDATGHLIHTHKSNFNSDVMSPEEIERVRQQLNMA
UniProt ID: P33739
Variant: S -> I at position 26-26
Variant annotation: in strain: Praslin
Protein function: This protein is transferred from male to female during mating and may affect egglaying and behavior after mating.
Reference sequence:
MNYFAVLCIFSCICLWQFSDAAPFISVQSSSQSRSQKVMNGMLRTLYDYSVQDSVNDATGHLIHTHKSNFNSDVMSPEEIERVRQQLNMA
UniProt ID: P33763
Variant: D -> G at position 54-54
Variant annotation: in dbSNP:rs3795393
Protein function: Binds calcium, zinc and copper. One subunit can simultaneously bind 2 calcium ions or 2 copper ions plus 1 zinc ion. Calcium and copper ions compete for the same binding sites.
Reference sequence:
METPLEKALTTMVTTFHKYSGREGSKLTLSRKELKELIKKELCLGEMKESSIDDLMKSLDKNSDQEIDFKEYSVFLTMLCMAYNDFFLEDNK
UniProt ID: P33764
Variant: R -> K at position 3-3
Variant annotation: in dbSNP:rs36022742
Protein function: Binds both calcium and zinc. May be involved in calcium-dependent cuticle cell differentiation, hair shaft and hair cuticular barrier formation.
Reference sequence:
MARPLEQAVAAIVCTFQEYAGRCGDKYKLCQAELKELLQKELATWTPTEFRECDYNKFMSVLDTNKDCEVDFVEYVRSLACLCLYCHEYFKDCPSEPPCSQ
UniProt ID: P33908
Variant: R -> G at position 651-651
Variant annotation: in dbSNP:rs35544784
Protein function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Reference sequence:
MPVGGLLPLFSSPAGGVLGGGLGGGGGRKGSGPAALRLTEKFVLLLVFSAFITLCFGAIFFLPDSSKLLSGVLFHSSPALQPAADHKPGPGARAEDAAEGRARRREEGAPGDPEAALEDNLARIRENHERALREAKETLQKLPEEIQRDILLEKKKVAQDQLRDKAPFRGLPPVDFVPPIGVESREPADAAIREKRAKIKEMMKHAWNNYKGYAWGLNELKPISKGGHSSSLFGNIKGATIVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNAEISVFEVNIRFVGGLLSAYYLSGEEIFRKKAVELGVKLLPAFHTPSGIPWALLNMKSGIGRNWPWASGGSSILAEFGTLHLEFMHLSHLSGNPIFAEKVMNIRTVLNKLEKPQGLYPNYLNPSSGQWGQHHVSVGGLGDSFYEYLLKAWLMSDKTDLEAKKMYFDAVQAIETHLIRKSSSGLTYIAEWKGGLLEHKMGHLTCFAGGMFALGADAAPEGMAQHYLELGAEIARTCHESYNRTFMKLGPEAFRFDGGVEAIATRQNEKYYILRPEVMETYMYMWRLTHDPKYRKWAWEAVEALENHCRVNGGYSGLRDVYLLHESYDDVQQSFFLAETLKYLYLIFSDDDLLPLEHWIFNSEAHLLPILPKDKKEVEIREE
UniProt ID: P33909
Variant: K -> R at position 230-230
Protein function: Positive regulation of conjugal transfer of Ti plasmids.
Reference sequence:
MQHWLDKLTDLTAIEGDGCILKTGLADVADHFGFTGYAYLHIQHKHIIAVTNYHHDWRSLYFDKKFDALDPVVKRARSRKQVFAWSGEQERPKLSEEERAFYAQAADFGIRSGITIPIRTANGSMSMFTLASERTAIPLDREIDAVAAAAAVGQLHARISFLRITPTAEDAAWLDPKEATYLRWIAVGKTMEEIADVEEVKYNSVRVKLREAMKRFDVRSKAHLTALAIKRKLI
UniProt ID: P33981
Variant: A -> V at position 97-97
Variant annotation: in dbSNP:rs2230513
Protein function: Phosphorylates proteins on serine, threonine, and tyrosine . Probably associated with cell proliferation . Phosphorylates MAD1L1 to promote mitotic checkpoint signaling . Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint .
Reference sequence:
MESEDLSGRELTIDSIMNKVRDIKNKFKNEDLTDELSLNKISADTTDNSGTVNQIMMMANNPEDWLSLLLKLEKNSVPLSDALLNKLIGRYSQAIEALPPDKYGQNESFARIQVRFAELKAIQEPDDARDYFQMARANCKKFAFVHISFAQFELSQGNVKKSKQLLQKAVERGAVPLEMLEIALRNLNLQKKQLLSEEEKKNLSASTVLTAQESFSGSLGHLQNRNNSCDSRGQTTKARFLYGENMPPQDAEIGYRNSLRQTNKTKQSCPFGRVPVNLLNSPDCDVKTDDSVVPCFMKRQTSRSECRDLVVPGSKPSGNDSCELRNLKSVQNSHFKEPLVSDEKSSELIITDSITLKNKTESSLLAKLEETKEYQEPEVPESNQKQWQSKRKSECINQNPAASSNHWQIPELARKVNTEQKHTTFEQPVFSVSKQSPPISTSKWFDPKSICKTPSSNTLDDYMSCFRTPVVKNDFPPACQLSTPYGQPACFQQQQHQILATPLQNLQVLASSSANECISVKGRIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENGKSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAKGTTEEMKYVLGQLVGLNSPNSILKAAKTLYEHYSGGESHNSSSSKTFEKKRGKK
UniProt ID: P33981
Variant: D -> N at position 758-758
Variant annotation: in dbSNP:rs2230512
Protein function: Phosphorylates proteins on serine, threonine, and tyrosine . Probably associated with cell proliferation . Phosphorylates MAD1L1 to promote mitotic checkpoint signaling . Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint .
Reference sequence:
MESEDLSGRELTIDSIMNKVRDIKNKFKNEDLTDELSLNKISADTTDNSGTVNQIMMMANNPEDWLSLLLKLEKNSVPLSDALLNKLIGRYSQAIEALPPDKYGQNESFARIQVRFAELKAIQEPDDARDYFQMARANCKKFAFVHISFAQFELSQGNVKKSKQLLQKAVERGAVPLEMLEIALRNLNLQKKQLLSEEEKKNLSASTVLTAQESFSGSLGHLQNRNNSCDSRGQTTKARFLYGENMPPQDAEIGYRNSLRQTNKTKQSCPFGRVPVNLLNSPDCDVKTDDSVVPCFMKRQTSRSECRDLVVPGSKPSGNDSCELRNLKSVQNSHFKEPLVSDEKSSELIITDSITLKNKTESSLLAKLEETKEYQEPEVPESNQKQWQSKRKSECINQNPAASSNHWQIPELARKVNTEQKHTTFEQPVFSVSKQSPPISTSKWFDPKSICKTPSSNTLDDYMSCFRTPVVKNDFPPACQLSTPYGQPACFQQQQHQILATPLQNLQVLASSSANECISVKGRIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENGKSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAKGTTEEMKYVLGQLVGLNSPNSILKAAKTLYEHYSGGESHNSSSSKTFEKKRGKK
UniProt ID: P33992
Variant: S -> T at position 136-136
Variant annotation: in dbSNP:rs2307334
Protein function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built . The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity .
Reference sequence:
MSGFDDPGIFYSDSFGGDAQADEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPAEHLQLLEEAAKEVADEVTRPRPSGEEVLQDIQVMLKSDASPSSIRSLKSDMMSHLVKIPGIIIAASAVRAKATRISIQCRSCRNTLTNIAMRPGLEGYALPRKCNTDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLTTSRGRDRVGVGIRSSYIRVLGIQVDTDGSGRSFAGAVSPQEEEEFRRLAALPNVYEVISKSIAPSIFGGTDMKKAIACLLFGGSRKRLPDGLTRRGDINLLMLGDPGTAKSQLLKFVEKCSPIGVYTSGKGSSAAGLTASVMRDPSSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVFGRWDETKGEDNIDFMPTILSRFDMIFIVKDEHNEERDVMLAKHVITLHVSALTQTQAVEGEIDLAKLKKFIAYCRVKCGPRLSAEAAEKLKNRYIIMRSGARQHERDSDRRSSIPITVRQLEAIVRIAEALSKMKLQPFATEADVEEALRLFQVSTLDAALSGTLSGVEGFTSQEDQEMLSRIEKQLKRRFAIGSQVSEHSIIKDFTKQKYPEHAIHKVLQLMLRRGEIQHRMQRKVLYRLK
UniProt ID: P33992
Variant: T -> S at position 180-180
Variant annotation: in dbSNP:rs2307340
Protein function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built . The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity .
Reference sequence:
MSGFDDPGIFYSDSFGGDAQADEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPAEHLQLLEEAAKEVADEVTRPRPSGEEVLQDIQVMLKSDASPSSIRSLKSDMMSHLVKIPGIIIAASAVRAKATRISIQCRSCRNTLTNIAMRPGLEGYALPRKCNTDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLTTSRGRDRVGVGIRSSYIRVLGIQVDTDGSGRSFAGAVSPQEEEEFRRLAALPNVYEVISKSIAPSIFGGTDMKKAIACLLFGGSRKRLPDGLTRRGDINLLMLGDPGTAKSQLLKFVEKCSPIGVYTSGKGSSAAGLTASVMRDPSSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVFGRWDETKGEDNIDFMPTILSRFDMIFIVKDEHNEERDVMLAKHVITLHVSALTQTQAVEGEIDLAKLKKFIAYCRVKCGPRLSAEAAEKLKNRYIIMRSGARQHERDSDRRSSIPITVRQLEAIVRIAEALSKMKLQPFATEADVEEALRLFQVSTLDAALSGTLSGVEGFTSQEDQEMLSRIEKQLKRRFAIGSQVSEHSIIKDFTKQKYPEHAIHKVLQLMLRRGEIQHRMQRKVLYRLK
UniProt ID: P33992
Variant: V -> I at position 258-258
Variant annotation: in dbSNP:rs2230933
Protein function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built . The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity .
Reference sequence:
MSGFDDPGIFYSDSFGGDAQADEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPAEHLQLLEEAAKEVADEVTRPRPSGEEVLQDIQVMLKSDASPSSIRSLKSDMMSHLVKIPGIIIAASAVRAKATRISIQCRSCRNTLTNIAMRPGLEGYALPRKCNTDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLTTSRGRDRVGVGIRSSYIRVLGIQVDTDGSGRSFAGAVSPQEEEEFRRLAALPNVYEVISKSIAPSIFGGTDMKKAIACLLFGGSRKRLPDGLTRRGDINLLMLGDPGTAKSQLLKFVEKCSPIGVYTSGKGSSAAGLTASVMRDPSSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVFGRWDETKGEDNIDFMPTILSRFDMIFIVKDEHNEERDVMLAKHVITLHVSALTQTQAVEGEIDLAKLKKFIAYCRVKCGPRLSAEAAEKLKNRYIIMRSGARQHERDSDRRSSIPITVRQLEAIVRIAEALSKMKLQPFATEADVEEALRLFQVSTLDAALSGTLSGVEGFTSQEDQEMLSRIEKQLKRRFAIGSQVSEHSIIKDFTKQKYPEHAIHKVLQLMLRRGEIQHRMQRKVLYRLK
UniProt ID: P33992
Variant: T -> I at position 466-466
Variant annotation: in MGORS8; dbSNP:rs1131692169
Protein function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built . The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity .
Reference sequence:
MSGFDDPGIFYSDSFGGDAQADEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPAEHLQLLEEAAKEVADEVTRPRPSGEEVLQDIQVMLKSDASPSSIRSLKSDMMSHLVKIPGIIIAASAVRAKATRISIQCRSCRNTLTNIAMRPGLEGYALPRKCNTDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLTTSRGRDRVGVGIRSSYIRVLGIQVDTDGSGRSFAGAVSPQEEEEFRRLAALPNVYEVISKSIAPSIFGGTDMKKAIACLLFGGSRKRLPDGLTRRGDINLLMLGDPGTAKSQLLKFVEKCSPIGVYTSGKGSSAAGLTASVMRDPSSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVFGRWDETKGEDNIDFMPTILSRFDMIFIVKDEHNEERDVMLAKHVITLHVSALTQTQAVEGEIDLAKLKKFIAYCRVKCGPRLSAEAAEKLKNRYIIMRSGARQHERDSDRRSSIPITVRQLEAIVRIAEALSKMKLQPFATEADVEEALRLFQVSTLDAALSGTLSGVEGFTSQEDQEMLSRIEKQLKRRFAIGSQVSEHSIIKDFTKQKYPEHAIHKVLQLMLRRGEIQHRMQRKVLYRLK