sujigwak/NVAR huggingface dataset:
UniProt ID: Q5ZPR3
Variant: T -> M at position 378-378
Variant annotation: in dbSNP:rs145827704
Protein function: May participate in the regulation of T-cell-mediated immune response. May play a protective role in tumor cells by inhibiting natural-killer mediated cell lysis as well as a role of marker for detection of neuroblastoma cells. May be involved in the development of acute and chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. Could also play a key role in providing the placenta and fetus with a suitable immunological environment throughout pregnancy. Both isoform 1 and isoform 2 appear to be redundant in their ability to modulate CD4 T-cell responses. Isoform 2 is shown to enhance the induction of cytotoxic T-cells and selectively stimulates interferon gamma production in the presence of T-cell receptor signaling.
Reference sequence:
MLRRRGSPGMGVHVGAALGALWFCLTGALEVQVPEDPVVALVGTDATLCCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFAEGQDQGSAYANRTALFPDLLAQGNASLRLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPYSKPSMTLEPNKDLRPGDTVTITCSSYQGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSILRVVLGANGTYSCLVRNPVLQQDAHSSVTITPQRSPTGAVEVQVPEDPVVALVGTDATLRCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFTEGRDQGSAYANRTALFPDLLAQGNASLRLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPYSKPSMTLEPNKDLRPGDTVTITCSSYRGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSVLRVVLGANGTYSCLVRNPVLQQDAHGSVTITGQPMTFPPEALWVTVGLSVCLIALLVALAFVCWRKIKQSCEEENAGAEDQDGEGEGSKTALQPLKHSDSKEDDGQEIA
UniProt ID: Q60452
Variant: R -> Q at position 286-286
Protein function: ATP-dependent 5'-3' DNA helicase, 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. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. 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. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers.
Reference sequence:
MKLNVDGLLVYFPYDYIYPEQFSYMLELKRTLDAKGHGVLEMPSGTGKTVSLLALIVAYQRAFPLEVTKLIYCSRTVPEIEKVIEELRKLLSFYEQQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQQDASLPHCRFYEEFDAHGRQVPLPAGIYNLDDLKALGQRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQSNLDTLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLHTLEIADLADFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARADKRGKLPRWIQEHLTDSNLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLQSEETLRRVEQIAQQL
UniProt ID: Q60692
Variant: A -> T at position 38-38
Protein function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB6 displays a peptidylglutamyl-hydrolyzing activity also termed postacidic or caspase-like activity, meaning that the peptides bond hydrolysis occurs directly after acidic residues.
Reference sequence:
MAAALAVRRAGSAPAFGPEALTPDWENREVSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTANALALAMERDGSSGGVIRLAAIQESGVERQVLLGDQIPKFTIATLPPP
UniProt ID: Q60692
Variant: A -> T at position 89-89
Protein function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB6 displays a peptidylglutamyl-hydrolyzing activity also termed postacidic or caspase-like activity, meaning that the peptides bond hydrolysis occurs directly after acidic residues.
Reference sequence:
MAAALAVRRAGSAPAFGPEALTPDWENREVSTGTTIMAVQFNGGVVLGADSRTTTGSYIANRVTDKLTPIHDHIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKDECLQFTANALALAMERDGSSGGVIRLAAIQESGVERQVLLGDQIPKFTIATLPPP
UniProt ID: Q60856
Variant: A -> S at position 36-36
Variant annotation: in strain: BID, DHA, MPR
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: S -> F at position 45-45
Variant annotation: in strain: MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: R -> Q at position 47-47
Variant annotation: in strain: DHA
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: V -> G at position 50-50
Variant annotation: in strain: DHA
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: G -> C at position 63-63
Variant annotation: in strain: BID, DHA, MPR, MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: T -> A at position 65-65
Variant annotation: in strain: BALB/c, BID, C57BL/6J, C3H/He, MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: S -> Y at position 83-83
Variant annotation: in strain: BID, DHA, MPR, MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: Q -> R at position 90-90
Variant annotation: in strain: DHA
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: C -> Y at position 103-103
Variant annotation: in strain: MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: V -> I at position 105-105
Variant annotation: in strain: DHA
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: C -> F at position 111-111
Variant annotation: in strain: MPR, DHA, MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: H -> Q at position 118-118
Variant annotation: in strain: MPR, MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: L -> V at position 151-151
Variant annotation: in strain: BID, MPR
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: P -> L at position 176-176
Variant annotation: in strain: MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: K -> E at position 181-181
Variant annotation: in strain: DHA
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: S -> L at position 183-183
Variant annotation: in strain: BID, MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: I -> T at position 184-184
Variant annotation: in strain: BID, DHA, MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: R -> Q at position 190-190
Variant annotation: in strain: BALB/c, C57BL/6J, C3H/He
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: R -> H at position 206-206
Variant annotation: in strain: MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: Q -> R at position 266-266
Variant annotation: in strain: BID, C3H/RV, DHA, MPR, MBT/Pas, PWD/Phj
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: H -> L at position 277-277
Variant annotation: in strain: BID
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
UniProt ID: Q60856
Variant: Q -> P at position 278-278
Variant annotation: in strain: DHA
Protein function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Reference sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG