sujigwak/NVAR huggingface dataset:
UniProt ID: P09884
Variant: P -> L at position 1381-1381
Variant annotation: in VEODS; no effect on protein abundance; decreased DNA replication; dbSNP:rs1569350993
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:
MAPVHGDDSLSDSGSFVSSRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDFTGVYEEVDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDADEKGKDGKARNKDKRNVKKLAVTKPNNIKSMFIACAGKKTADKAVDLSKDGLLGDILQDLNTETPQITPPPVMILKKKRSIGASPNPFSVHTATAVPSGKIASPVSRKEPPLTPVPLKRAEFAGDDVQVESTEEEQESGAMEFEDGDFDEPMEVEEVDLEPMAAKAWDKESEPAEEVKQEADSGKGTVSYLGSFLPDVSCWDIDQEGDSSFSVQEVQVDSSHLPLVKGADEEQVFHFYWLDAYEDQYNQPGVVFLFGKVWIESAETHVSCCVMVKNIERTLYFLPREMKIDLNTGKETGTPISMKDVYEEFDEKIATKYKIMKFKSKPVEKNYAFEIPDVPEKSEYLEVKYSAEMPQLPQDLKGETFSHVFGTNTSSLELFLMNRKIKGPCWLEVKSPQLLNQPVSWCKVEAMALKPDLVNVIKDVSPPPLVVMAFSMKTMQNAKNHQNEIIAMAALVHHSFALDKAAPKPPFQSHFCVVSKPKDCIFPYAFKEVIEKKNVKVEVAATERTLLGFFLAKVHKIDPDIIVGHNIYGFELEVLLQRINVCKAPHWSKIGRLKRSNMPKLGGRSGFGERNATCGRMICDVEISAKELIRCKSYHLSELVQQILKTERVVIPMENIQNMYSESSQLLYLLEHTWKDAKFILQIMCELNVLPLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQKLGDEDEEIDGDTNKYKKGRKKAAYAGGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNICFTTVQRVASEAQKVTEDGEQEQIPELPDPSLEMGILPREIRKLVERRKQVKQLMKQQDLNPDLILQYDIRQKALKLTANSMYGCLGFSYSRFYAKPLAALVTYKGREILMHTKEMVQKMNLEVIYGDTDSIMINTNSTNLEEVFKLGNKVKSEVNKLYKLLEIDIDGVFKSLLLLKKKKYAALVVEPTSDGNYVTKQELKGLDIVRRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKRLIEIGENVLNGSVPVSQFEINKALTKDPQDYPDKKSLPHVHVALWINSQGGRKVKAGDTVSYVICQDGSNLTASQRAYAPEQLQKQDNLTIDTQYYLAQQIHPVVARICEPIDGIDAVLIATWLGLDPTQFRVHHYHKDEENDALLGGPAQLTDEEKYRDCERFKCPCPTCGTENIYDNVFDGSGTDMEPSLYRCSNIDCKASPLTFTVQLSNKLIMDIRRFIKKYYDGWLICEEPTCRNRTRHLPLQFSRTGPLCPACMKATLQPEYSDKSLYTQLCFYRYIFDAECALEKLTTDHEKDKLKKQFFTPKVLQDYRKLKNTAEQFLSRSGYSEVNLSKLFAGCAVKS
UniProt ID: P09905
Variant: H -> Q at position 2-2
Variant annotation: in beta-1
Protein function: Involved in oxygen transport from the lung to the various peripheral tissues.
Reference sequence:
VHLTGEEKSGLTALWAKVNVEEIGGEALGRLLVVYPWTQRFFEHFGDLSTADAVMKNPKVKKHGQKVLASFGEGLKHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVVVLARHFGKEFTPELQTAYQKVVAGVANALAHKYH
UniProt ID: P09905
Variant: G -> A at position 5-5
Variant annotation: in beta-1
Protein function: Involved in oxygen transport from the lung to the various peripheral tissues.
Reference sequence:
VHLTGEEKSGLTALWAKVNVEEIGGEALGRLLVVYPWTQRFFEHFGDLSTADAVMKNPKVKKHGQKVLASFGEGLKHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVVVLARHFGKEFTPELQTAYQKVVAGVANALAHKYH
UniProt ID: P09905
Variant: L -> V at position 11-11
Variant annotation: in beta-1
Protein function: Involved in oxygen transport from the lung to the various peripheral tissues.
Reference sequence:
VHLTGEEKSGLTALWAKVNVEEIGGEALGRLLVVYPWTQRFFEHFGDLSTADAVMKNPKVKKHGQKVLASFGEGLKHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVVVLARHFGKEFTPELQTAYQKVVAGVANALAHKYH
UniProt ID: P09911
Variant: L -> I at position 59-59
Variant annotation: in strain: cv. Onward
Protein function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Reference sequence:
MATTPALYGTAVSTSFLRTQPMPMSVTTTKAFSNGFLGLKTSLKRGDLAVAMASYKVKLVTPDGTQEFECPSDVYILDHAEEVGIDLPYSCRAGSCSSCAGKVVGGEVDQSDGSFLDDEQIEAGFVLTCVAYPTSDVVIETHKEEDLTA
UniProt ID: P09911
Variant: I -> L at position 85-85
Variant annotation: in strain: cv. Onward
Protein function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Reference sequence:
MATTPALYGTAVSTSFLRTQPMPMSVTTTKAFSNGFLGLKTSLKRGDLAVAMASYKVKLVTPDGTQEFECPSDVYILDHAEEVGIDLPYSCRAGSCSSCAGKVVGGEVDQSDGSFLDDEQIEAGFVLTCVAYPTSDVVIETHKEEDLTA
UniProt ID: P09913
Variant: E -> A at position 79-79
Variant annotation: in dbSNP:rs17468739
Protein function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis.
Reference sequence:
MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAVAHLKKADEANDNLFRVCSILASLHALADQYEDAEYYFQKEFSKELTPVAKQLLHLRYGNFQLYQMKCEDKAIHHFIEGVKINQKSREKEKMKDKLQKIAKMRLSKNGADSEALHVLAFLQELNEKMQQADEDSERGLESGSLIPSASSWNGE
UniProt ID: P09913
Variant: K -> R at position 121-121
Variant annotation: in dbSNP:rs2070845
Protein function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis.
Reference sequence:
MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAVAHLKKADEANDNLFRVCSILASLHALADQYEDAEYYFQKEFSKELTPVAKQLLHLRYGNFQLYQMKCEDKAIHHFIEGVKINQKSREKEKMKDKLQKIAKMRLSKNGADSEALHVLAFLQELNEKMQQADEDSERGLESGSLIPSASSWNGE
UniProt ID: P09913
Variant: D -> E at position 352-352
Variant annotation: in dbSNP:rs1727
Protein function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis.
Reference sequence:
MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAVAHLKKADEANDNLFRVCSILASLHALADQYEDAEYYFQKEFSKELTPVAKQLLHLRYGNFQLYQMKCEDKAIHHFIEGVKINQKSREKEKMKDKLQKIAKMRLSKNGADSEALHVLAFLQELNEKMQQADEDSERGLESGSLIPSASSWNGE
UniProt ID: P09914
Variant: P -> H at position 131-131
Variant annotation: in dbSNP:rs11553019
Protein function: Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Exhibits antiviral activity against several viruses including human papilloma and hepatitis C viruses.
Reference sequence:
MSTNGDDHQVKDSLEQLRCHFTWELSIDDDEMPDLENRVLDQIEFLDTKYSVGIHNLLAYVKHLKGQNEEALKSLKEAENLMQEEHDNQANVRSLVTWGNFAWMYYHMGRLAEAQTYLDKVENICKKLSNPFRYRMECPEIDCEEGWALLKCGGKNYERAKACFEKVLEVDPENPESSAGYAISAYRLDGFKLATKNHKPFSLLPLRQAVRLNPDNGYIKVLLALKLQDEGQEAEGEKYIEEALANMSSQTYVFRYAAKFYRRKGSVDKALELLKKALQETPTSVLLHHQIGLCYKAQMIQIKEATKGQPRGQNREKLDKMIRSAIFHFESAVEKKPTFEVAHLDLARMYIEAGNHRKAEENFQKLLCMKPVVEETMQDIHFHYGRFQEFQKKSDVNAIIHYLKAIKIEQASLTRDKSINSLKKLVLRKLRRKALDLESLSLLGFVYKLEGNMNEALEYYERALRLAADFENSVRQGP
UniProt ID: P09919
Variant: L -> M at position 157-157
Variant annotation: in dbSNP:rs2227329
Protein function: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.
Reference sequence:
MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLVSECATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP
UniProt ID: P09919
Variant: A -> T at position 174-174
Variant annotation: in dbSNP:rs2227330
Protein function: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.
Reference sequence:
MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLVSECATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP
UniProt ID: P09923
Variant: R -> H at position 144-144
Variant annotation: in dbSNP:rs7559279
Protein function: Alkaline phosphatase that can hydrolyze various phosphate compounds.
Reference sequence:
MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLGDGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLCGVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADASQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRDPTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERAGQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVFNSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHVMAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP
UniProt ID: P09923
Variant: H -> L at position 298-298
Variant annotation: in dbSNP:rs1047223
Protein function: Alkaline phosphatase that can hydrolyze various phosphate compounds.
Reference sequence:
MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLGDGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLCGVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADASQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRDPTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERAGQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVFNSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHVMAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP
UniProt ID: P09941
Variant: L -> F at position 4-4
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: V -> A at position 6-6
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: L -> F at position 11-11
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: A -> V at position 22-22
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: A -> S at position 49-49
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: S -> Q at position 52-52
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: Y -> F at position 67-67
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: D -> G at position 89-89
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: E -> D at position 97-97
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: K -> E at position 108-108
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: Q -> R at position 112-112
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: L -> H at position 113-113
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09941
Variant: K -> Q at position 120-120
Variant annotation: in less than 10% of the chains
Protein function: Inhibition of trypsin.
Reference sequence:
RELLDVDGNFLRNGGSYYIVPAFRGKGGGLELARTGSETCPRTVVQAPAEQSRGLPARLSTPPRIRYIGPEFYLTIEFEEQKPPSCLRDSNLQWKVEEESQIVKIASKEEEQLFGSFQIKPYRDDYKLVYCEPQQGGR
UniProt ID: P09942
Variant: L -> P at position 1-1
Protein function: Inhibition of trypsin.
Reference sequence:
LECKDLGISIDDDNNRRLAVKEGDPLVVQFVNADREGN
UniProt ID: P09960
Variant: Y -> H at position 131-131
Variant annotation: in dbSNP:rs45630737
Protein function: Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities. Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4) . Has also aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides . In addition to its pro-inflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL) . Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions .
Reference sequence:
MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVGKDLKVD
UniProt ID: P09971
Variant: K -> N at position 109-109
Variant annotation: in strain: J106
Protein function: The three SGNPS are far less active than DH in inducing diapause eggs. Beta-SGNP expressed higher pban activity than PBAN-I, but alpha- and gamma-SGNP were far less active in pheromonotropic activity.
Reference sequence:
MYKTNIVFNVLALALFSIFFASCTDMKDESDRGAHSERGALWFGPRLGKRSMKPSTEDNRQTFLRLLEAADALKFYYDQLPYERQADEPETKVTKKIIFTPKLGRSVAKPQTHESLEFIPRLGRRLSEDMPATPADQEMYQPDPEEMESRTRYFSPRLGRTMSFSPRLGRELSYDYPTKYRVARSVNKTMDN
UniProt ID: P09971
Variant: L -> PL at position 126-126
Variant annotation: in MRCH-III
Protein function: The three SGNPS are far less active than DH in inducing diapause eggs. Beta-SGNP expressed higher pban activity than PBAN-I, but alpha- and gamma-SGNP were far less active in pheromonotropic activity.
Reference sequence:
MYKTNIVFNVLALALFSIFFASCTDMKDESDRGAHSERGALWFGPRLGKRSMKPSTEDNRQTFLRLLEAADALKFYYDQLPYERQADEPETKVTKKIIFTPKLGRSVAKPQTHESLEFIPRLGRRLSEDMPATPADQEMYQPDPEEMESRTRYFSPRLGRTMSFSPRLGRELSYDYPTKYRVARSVNKTMDN
UniProt ID: P09971
Variant: M -> I at position 139-139
Variant annotation: in strain: Daizo and J106
Protein function: The three SGNPS are far less active than DH in inducing diapause eggs. Beta-SGNP expressed higher pban activity than PBAN-I, but alpha- and gamma-SGNP were far less active in pheromonotropic activity.
Reference sequence:
MYKTNIVFNVLALALFSIFFASCTDMKDESDRGAHSERGALWFGPRLGKRSMKPSTEDNRQTFLRLLEAADALKFYYDQLPYERQADEPETKVTKKIIFTPKLGRSVAKPQTHESLEFIPRLGRRLSEDMPATPADQEMYQPDPEEMESRTRYFSPRLGRTMSFSPRLGRELSYDYPTKYRVARSVNKTMDN
UniProt ID: P09971
Variant: E -> V at position 146-146
Variant annotation: in strain: J106
Protein function: The three SGNPS are far less active than DH in inducing diapause eggs. Beta-SGNP expressed higher pban activity than PBAN-I, but alpha- and gamma-SGNP were far less active in pheromonotropic activity.
Reference sequence:
MYKTNIVFNVLALALFSIFFASCTDMKDESDRGAHSERGALWFGPRLGKRSMKPSTEDNRQTFLRLLEAADALKFYYDQLPYERQADEPETKVTKKIIFTPKLGRSVAKPQTHESLEFIPRLGRRLSEDMPATPADQEMYQPDPEEMESRTRYFSPRLGRTMSFSPRLGRELSYDYPTKYRVARSVNKTMDN
UniProt ID: P09983
Variant: A -> T at position 6-6
Variant annotation: in strain: 2001
Protein function: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by forming a pore.
Reference sequence:
MPTITAAQIKSTLQSAKQSAANKLHSAGQSTKDALKKAAEQTRNAGNRLILLIPKDYKGQGSSLNDLVRTADELGIEVQYDEKNGTAITKQVFGTAEKLIGLTERGVTIFAPQLDKLLQKYQKAGNKLGGSAENIGDNLGKAGSVLSTFQNFLGTALSSMKIDELIKKQKSGGNVSSSELAKASIELINQLVDTAASLNNVNSFSQQLNKLGSVLSNTKHLNGVGNKLQNLPNLDNIGAGLDTVSGILSAISASFILSNADADTGTKAAAGVELTTKVLGNVGKGISQYIIAQRAAQGLSTSAAAAGLIASVVTLAISPLSFLSIADKFKRANKIEEYSQRFKKLGYDGDSLLAAFHKETGAIDASLTRISTVLASVSSGISAAATTSLVGAPVSALVGAVTGIISGILEASKQAMFEHVASKMADVIAEWEKKHGKNYFENGYDARHAAFLEDNFKILSQYNKEYSVERSVLITQQHWDTLIGELAGVTRNGDKTLSGKSYIDYYEEGKRLEKKPDEFQKQVFDPLKGNIDLSDSKSSTLLKFVTPLLTPGEEIRERRQSGKYEYITELLVKGVDKWTVKGVQDKGSVYDYSNLIQHASVGNNQYREIRIESHLGDGDDKVFLSAGSANIYAGKGHDVVYYDKTDTGYLTIDGTKATEAGNYTVTRVLGGDVKVLQEVVKEQEVSVGKRTEKTQYRSYEFTHINGKNLTETDNLYSVEELIGTTRADKFFGSKFADIFHGADGDDHIEGNDGNDRLYGDKGNDTLSGGNGDDQLYGGDGNDKLIGGAGNNYLNGGDGDDELQVQGNSLAKNVLSGGKGNDKLYGSEGADLLDGGEGNDLLKGGYGNDIYRYLSGYGHHIIDDDGGKDDKLSLADIDFRDVAFRREGNDLIMYKAEGNVLSIGHKNGITFKNWFEKESGDISNHQIEQIFDKDGRVITPDSLKKALEYQQSNNKASYVYGNDALAYGSQGNLNPLINEISKIISAAGNFDVKEERAAASLLQLSGNASDFSYGRNSITLTASA
UniProt ID: P0A0J0
Variant: P -> S at position 209-209
Variant annotation: in plaC1 mutation; results in a narrower specificity for promoters
Protein function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
Reference sequence:
MSDNTVKIKKQTIDPTLTLEDVKKQLIEKGKKEGHLSHEEIAEKLQNFDIDSDQMDDFFDQLNDNDISLVNEKDSSDTDEKLNPSDLSAPPGVKINDPVRMYLKEIGRVNLLSAQEEIELAKRIEQGDEVAKSRLAEANLRLVVSIAKRYVGRGMLFLDLIQEGNMGLIKAVEKFDFNKGFKFSTYATWWIRQAITRAIADQARTIRIPVHMVETINKLIRVQRQLLQDLGRDPAPEEIGEEMDLPAEKVREILKIAQEPVSLETPIGEEDDSHLGDFIEDQEAQSPSDHAAYELLKEQLEDVLDTLTDREENVLRLRFGLDDGRTRTLEEVGKVFGVTRERIRQIEAKALRKLRHPSRSKRLKDFMD
UniProt ID: P0A0W2
Variant: G -> S at position 3-3
Variant annotation: in strain: BNCV / Serogroup B
Protein function: PPIases accelerate the folding of proteins.
Reference sequence:
MGGLIIEDLQEGFGKEAVKGKEITVHYTGWLENGTKFDSSLDRRQPLTITLGVGQVIKGWDEGFGGMKEGGKRKLTIPSEMGYGAHGAGGVIPPHATLIFEVELLKVYE
UniProt ID: P0A0W2
Variant: G -> S at position 12-12
Variant annotation: in strain: BNCV / Serogroup B
Protein function: PPIases accelerate the folding of proteins.
Reference sequence:
MGGLIIEDLQEGFGKEAVKGKEITVHYTGWLENGTKFDSSLDRRQPLTITLGVGQVIKGWDEGFGGMKEGGKRKLTIPSEMGYGAHGAGGVIPPHATLIFEVELLKVYE
UniProt ID: P0A0W2
Variant: N -> D at position 33-33
Variant annotation: in strain: BNCV / Serogroup B
Protein function: PPIases accelerate the folding of proteins.
Reference sequence:
MGGLIIEDLQEGFGKEAVKGKEITVHYTGWLENGTKFDSSLDRRQPLTITLGVGQVIKGWDEGFGGMKEGGKRKLTIPSEMGYGAHGAGGVIPPHATLIFEVELLKVYE
UniProt ID: P0A110
Variant: N -> K at position 4-4
Variant annotation: in strain: G7
Protein function: Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The alpha subunit has a catalytic role in the holoenzyme. Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene .
Reference sequence:
MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMGIDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFEKDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGLELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGLQMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTVFPNNSMLTCSGVFKVWNPIDANTTEVWTYAIVEKDMPEDLKRRLADSVQRTFGPAGFWESDDNDNMETASQNGKKYQSRDSDLLSNLGFGEDVYGDAVYPGVVGKSAIGETSYRGFYRAYQAHVSSSNWAEFEHASSTWHTELTKTTDR