sujigwak/NVAR huggingface dataset:
UniProt ID: P01242
Variant: R -> W at position 90-90
Variant annotation: in dbSNP:rs5389
Protein function: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
Reference sequence:
MAAGSRTSLLLAFGLLCLSWLQEGSAFPTIPLSRLFDNAMLRARRLYQLAYDTYQEFEEAYILKEQKYSFLQNPQTSLCFSESIPTPSNRVKTQQKSNLELLRISLLLIQSWLEPVQLLRSVFANSLVYGASDSNVYRHLKDLEEGIQTLMWRLEDGSPRTGQIFNQSYSKFDTKSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
UniProt ID: P01258
Variant: G -> R at position 2-2
Variant annotation: in dbSNP:rs34587547
Protein function: Katacalcin is a potent plasma calcium-lowering peptide.
Reference sequence:
MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSSLDSPRSKRCGNLSTCMLGTYTQDFNKFHTFPQTAIGVGAPGKKRDMSSDLERDHRPHVSMPQNAN
UniProt ID: P01258
Variant: D -> N at position 57-57
Variant annotation: in dbSNP:rs5239
Protein function: Katacalcin is a potent plasma calcium-lowering peptide.
Reference sequence:
MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSSLDSPRSKRCGNLSTCMLGTYTQDFNKFHTFPQTAIGVGAPGKKRDMSSDLERDHRPHVSMPQNAN
UniProt ID: P01258
Variant: E -> K at position 67-67
Variant annotation: in dbSNP:rs34164367
Protein function: Katacalcin is a potent plasma calcium-lowering peptide.
Reference sequence:
MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSSLDSPRSKRCGNLSTCMLGTYTQDFNKFHTFPQTAIGVGAPGKKRDMSSDLERDHRPHVSMPQNAN
UniProt ID: P01258
Variant: S -> R at position 76-76
Variant annotation: in dbSNP:rs5241
Protein function: Katacalcin is a potent plasma calcium-lowering peptide.
Reference sequence:
MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSSLDSPRSKRCGNLSTCMLGTYTQDFNKFHTFPQTAIGVGAPGKKRDMSSDLERDHRPHVSMPQNAN
UniProt ID: P01258
Variant: S -> T at position 123-123
Variant annotation: in dbSNP:rs34414857
Protein function: Katacalcin is a potent plasma calcium-lowering peptide.
Reference sequence:
MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSSLDSPRSKRCGNLSTCMLGTYTQDFNKFHTFPQTAIGVGAPGKKRDMSSDLERDHRPHVSMPQNAN
UniProt ID: P01258
Variant: Q -> P at position 138-138
Variant annotation: in dbSNP:rs13306224
Protein function: Katacalcin is a potent plasma calcium-lowering peptide.
Reference sequence:
MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSSLDSPRSKRCGNLSTCMLGTYTQDFNKFHTFPQTAIGVGAPGKKRDMSSDLERDHRPHVSMPQNAN
UniProt ID: P01270
Variant: C -> R at position 18-18
Variant annotation: in FIH1; dominant form; leads to inefficient processing of the precursor; the expressed mutant hormone is trapped intracellularly in the endoplasmic reticulum resulting in apoptosis; mutant protein-expressing cells also show marked up-regulation of the endoplasmic reticulum stress-responsive hormones HSPA5 and EIF2AK3 and the proapoptotic transcription factor DDIT3; dbSNP:rs104894271
Protein function: PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells.
Reference sequence:
MIPAKDMAKVMIVMLAICFLTKSDGKSVKKRSVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFVALGAPLAPRDAGSQRPRKKEDNVLVESHEKSLGEADKADVNVLTKAKSQ
UniProt ID: P01270
Variant: S -> P at position 23-23
Variant annotation: in FIH1; recessive form; might lead to inefficient processing of the precursor; dbSNP:rs104894272
Protein function: PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells.
Reference sequence:
MIPAKDMAKVMIVMLAICFLTKSDGKSVKKRSVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFVALGAPLAPRDAGSQRPRKKEDNVLVESHEKSLGEADKADVNVLTKAKSQ
UniProt ID: P01298
Variant: E -> G at position 78-78
Variant annotation: in dbSNP:rs7215698
Protein function: The physiological role for the icosapeptide has not yet been elucidated.
Reference sequence:
MAAARLCLSLLLLSTCVALLLQPLLGAQGAPLEPVYPGDNATPEQMAQYAADLRRYINMLTRPRYGKRHKEDTLAFSEWGSPHAAVPRELSPLDL
UniProt ID: P01303
Variant: L -> P at position 7-7
Variant annotation: in dbSNP:rs16139
Protein function: NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.
Reference sequence:
MLGNKRLGLSGLTLALSLLVCLGALAEAYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRYGKRSSPETLISDLLMRESTENVPRTRLEDPAMW
UniProt ID: P01303
Variant: L -> M at position 22-22
Variant annotation: in dbSNP:rs5571
Protein function: NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.
Reference sequence:
MLGNKRLGLSGLTLALSLLVCLGALAEAYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRYGKRSSPETLISDLLMRESTENVPRTRLEDPAMW
UniProt ID: P01344
Variant: K -> N at position 120-120
Variant annotation: in dbSNP:rs14367
Protein function: Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.
Reference sequence:
MGIPMGKSMLVLLTFLAFASCCIAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSTPPTVLPDNFPRYPVGKFFQYDTWKQSTQRLRRGLPALLRARRGHVLAKELEAFREAKRHRPLIALPTQDPAHGGAPPEMASNRK
UniProt ID: P01344
Variant: P -> Q at position 173-173
Variant annotation: in dbSNP:rs1050342
Protein function: Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.
Reference sequence:
MGIPMGKSMLVLLTFLAFASCCIAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSTPPTVLPDNFPRYPVGKFFQYDTWKQSTQRLRRGLPALLRARRGHVLAKELEAFREAKRHRPLIALPTQDPAHGGAPPEMASNRK
UniProt ID: P01344
Variant: K -> N at position 180-180
Variant annotation: in dbSNP:rs12993
Protein function: Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.
Reference sequence:
MGIPMGKSMLVLLTFLAFASCCIAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSTPPTVLPDNFPRYPVGKFFQYDTWKQSTQRLRRGLPALLRARRGHVLAKELEAFREAKRHRPLIALPTQDPAHGGAPPEMASNRK
UniProt ID: P01353
Variant: A -> T at position 85-85
Protein function: Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine.
Reference sequence:
MQRLCVYVLILALALATFSEASWKPRSRLQDAPSGPGANRGLEPHGLDQLGPASHHRRQLGLQGPPQLVADLSKKQGPWMEEEEAAYGWMDFGRRSAEEGDQRP
UniProt ID: P01362
Variant: S -> M at position 26-26
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01362
Variant: V -> A at position 43-43
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01362
Variant: S -> Y at position 62-62
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01362
Variant: G -> E at position 63-63
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01362
Variant: E -> Q at position 64-64
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01362
Variant: F -> L at position 75-75
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01362
Variant: F -> I at position 119-119
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01362
Variant: D -> E at position 140-140
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01362
Variant: V -> A at position 143-143
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01362
Variant: G -> E at position 165-165
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01362
Variant: Q -> P at position 236-236
Protein function: Beta-BCP specifically excites 2 neurons, L1 and R1, in the abdominal ganglion.
Reference sequence:
MKRPNNRPTNTMSLILCLTLSSLCVSSQSASVHGKNFATNRAVKSSSPFVVLSPDDNVVSMSGENGYRSALREAFDKSSRDYDDNGEDVFSNEKRRLRFHKRRLRFDRRDQDEGNFRRFPTNAVSMSADENSPFDLSNEDGAVYQRDLRAPRLRFYSLRKRAAGGMEQSEGQNPETESHSRRKRSVLTPSLSSLGESLESGISKRISINQDLKAITDMLLTEQIRERQRYLADLRQRLLEKGKRSSGVSLLTSNKDEEQRELLKAISNLLD
UniProt ID: P01372
Variant: V -> L at position 2-2
Variant annotation: in 30% of the molecules
Protein function: Represses female sexual receptivity and stimulates oviposition. This peptide has a low activity.
Reference sequence:
DVPSANANANNQRTAAAKPQANAEASS
UniProt ID: P01374
Variant: C -> R at position 13-13
Variant annotation: in dbSNP:rs2229094
Protein function: Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM . In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo.
Reference sequence:
MTPPERLFLPRVCGTTLHLLLLGLLLVLLPGAQGLPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL
UniProt ID: P01374
Variant: H -> P at position 51-51
Variant annotation: in dbSNP:rs2229092
Protein function: Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM . In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo.
Reference sequence:
MTPPERLFLPRVCGTTLHLLLLGLLLVLLPGAQGLPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL
UniProt ID: P01374
Variant: T -> N at position 60-60
Variant annotation: in allele TNFB*2; dbSNP:rs1041981
Protein function: Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM . In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo.
Reference sequence:
MTPPERLFLPRVCGTTLHLLLLGLLLVLLPGAQGLPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL
UniProt ID: P01374
Variant: T -> P at position 125-125
Variant annotation: in allele 8.1
Protein function: Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM . In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo.
Reference sequence:
MTPPERLFLPRVCGTTLHLLLLGLLLVLLPGAQGLPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL
UniProt ID: P01379
Variant: I -> K at position 40-40
Variant annotation: in LSIII-5
Protein function: Binds with high affinity to muscular (tested on Torpedo marmorata, Kd=1.6 nM) and neuronal (chimeric alpha-7/CHRNA7, Kd=3 nM) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission . Also shows a very weak inhibition on GABA(A) receptors . The toxin (10 uM) inhibits 83% of current in channels composed of alpha-1-beta-3-gamma-2 (GABRA1-GABRB3-GABRG2) subunits, 39% of current in channels composed of alpha-2-beta-2-gamma-2 (GABRA2-GABRB2-GABRG2) subunits, and 33% of current in channels composed of alpha-5-beta-2-gamma-2 (GABRA5-GABRB2-GABRG2) subunits .
Reference sequence:
MKTLLLTLVVVTIVCLDLGYTRECYLNPHDTQTCPSGQEICYVKSWCNAWCSSRGKVLEFGCAATCPSVNTGTEIKCCSADKCNTYP
UniProt ID: P01459
Variant: Y -> H at position 4-4
Variant annotation: in toxin CM-8A
Protein function: Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity.
Reference sequence:
LKCYKLVPPFWKTCPEGKNLCYKMYMVSTLTVPVKRGCIDVCPKNSALVKYVCCNTDKCN
UniProt ID: P01462
Variant: M -> V at position 52-52
Variant annotation: in toxin V(II)2A
Protein function: Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity.
Reference sequence:
LKCHKLVPPFWKTCPEGKNLCYKMYMVATPMLPVKRGCIDVCPKDSALVKYMCCNTDKCN
UniProt ID: P01462
Variant: N -> S at position 55-55
Variant annotation: in toxin V(II)2A
Protein function: Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity.
Reference sequence:
LKCHKLVPPFWKTCPEGKNLCYKMYMVATPMLPVKRGCIDVCPKDSALVKYMCCNTDKCN
UniProt ID: P01465
Variant: M -> V at position 52-52
Variant annotation: in minor component
Protein function: Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity.
Reference sequence:
LKCHKLVPPFWKTCPEGKNLCYKMYMVATPMLPVKRGCIDVCPKDSALVKYMCCNTNKCN
UniProt ID: P01465
Variant: N -> S at position 55-55
Variant annotation: in minor component
Protein function: Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity.
Reference sequence:
LKCHKLVPPFWKTCPEGKNLCYKMYMVATPMLPVKRGCIDVCPKDSALVKYMCCNTNKCN
UniProt ID: P01466
Variant: M -> V at position 52-52
Variant annotation: in minor component
Protein function: Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity.
Reference sequence:
LKCHKLVPPFWKTCPEGKNLCYKMYMVATPMLPVKRGCINVCPKDSALVKYMCCNTNKCN
UniProt ID: P01466
Variant: N -> S at position 55-55
Variant annotation: in minor component
Protein function: Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity.
Reference sequence:
LKCHKLVPPFWKTCPEGKNLCYKMYMVATPMLPVKRGCINVCPKDSALVKYMCCNTNKCN
UniProt ID: P01474
Variant: N -> K at position 36-36
Variant annotation: in V-II-3
Protein function: Has low cytotoxic activity.
Reference sequence:
IKCHNTLLPFIYKTCPEGQNLCFKGTLKFPKKTTYNRGCAATCPKSSLLVKYVCCNTNKCN
UniProt ID: P01479
Variant: V -> I at position 36-36
Variant annotation: in neurotoxin-1'
Protein function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. Is active against mammals and binds with high affinity rat brain synaptosomes.
Reference sequence:
MNYLVMISLALLLMIGVESKRDGYIVYPNNCVYHCVPPCDGLCKKNGGSSGSCSFLVPSGLACWCKDLPDNVPIKDTSRKCTR
UniProt ID: P01497
Variant: F -> L at position 17-17
Protein function: Excitatory insect beta-toxins induce a spastic paralysis. They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active only on insects.
Reference sequence:
MKFLLLFLVVLPIMGVFGKKNGYAVDSSGKAPECLLSNYCNNECTKVHYADKGYCCLLSCYCFGLNDDKKVLEISDTRKSYCDTTIIN
UniProt ID: P01501
Variant: T -> S at position 53-53
Variant annotation: in melittin-S
Protein function: Melittin-2: Has strong hemolytic activity .
Reference sequence:
MKFLVNVALVFMVVYISYIYAAPEPEPAPEPEAEADAEADPEAGIGAVLKVLTTGLPALISWIKRKRQQG
UniProt ID: P01501
Variant: K -> S at position 64-64
Variant annotation: in melittin-2; possibly an artifact
Protein function: Melittin-2: Has strong hemolytic activity .
Reference sequence:
MKFLVNVALVFMVVYISYIYAAPEPEPAPEPEAEADAEADPEAGIGAVLKVLTTGLPALISWIKRKRQQG
UniProt ID: P01501
Variant: K -> KK at position 66-66
Variant annotation: in melittin-2; possibly an artifact
Protein function: Melittin-2: Has strong hemolytic activity .
Reference sequence:
MKFLVNVALVFMVVYISYIYAAPEPEPAPEPEAEADAEADPEAGIGAVLKVLTTGLPALISWIKRKRQQG
UniProt ID: P01528
Variant: V -> I at position 2-2
Variant annotation: in 50% of the molecules
Protein function: Binds specifically to voltage-gated sodium channels (Nav) (site 3), thereby delaying their inactivation. Has a strong effect on crustaceans and insects (DmNav1) and a weaker effect on mammals. This toxin is highly potent at mammalian Nav1.1/SCN1A (EC(50)=6.01 nM) and Nav1.2/SCN2A (EC(50)=7.88 nM) . It has also great activity on Nav1.5/SCN5A (EC(50)=49.05 nM), Nav1.4/SCN4A (EC(50)=109.49 nM) and Nav1.6/SCN8A (EC(50)=about 180 nM) and is less potent on Nav1.3/SCN3A (EC(50)=759.22 nM) (when measured as the increase in the slow component) .
Reference sequence:
GVPCLCDSDGPSVRGNTLSGIIWLAGCPSGWHNCKKHGPTIGWCCKQ
UniProt ID: P01529
Variant: P -> G at position 39-39
Variant annotation: in 50% of the molecules
Protein function: Binds specifically to voltage-gated sodium channels (Nav), thereby delaying their inactivation during signal transduction. Thus it strongly stimulates mammalian cardiac muscle contraction.
Reference sequence:
GVPCLCDSDGPSVRGNTLSGILWLAGCPSGWHNCKKHKPTIGWCCK
UniProt ID: P01533
Variant: A -> P at position 3-3
Variant annotation: in about 20% of the molecules
Protein function: Binds specifically to voltage-gated sodium channels (Nav) and delays their inactivation during signal transduction (when tested on the soma membrane of a crustacean neuron). Has also been observed to affect the activation of the sodium current.
Reference sequence:
GAACLCKSDGPNTRGNSMSGTIWVFGCPSGWNNCEGRAIIGYCCKQ
UniProt ID: P01542
Variant: P -> S at position 22-22
Variant annotation: in isoform SI
Protein function: The function of this hydrophobic plant seed protein is not known.
Reference sequence:
TTCCPSIVARSNFNVCRLPGTPEALCATYTGCIIIPGATCPGDYAN
UniProt ID: P01542
Variant: L -> I at position 25-25
Variant annotation: in isoform SI
Protein function: The function of this hydrophobic plant seed protein is not known.
Reference sequence:
TTCCPSIVARSNFNVCRLPGTPEALCATYTGCIIIPGATCPGDYAN
UniProt ID: P01562
Variant: V -> A at position 10-10
Variant annotation: in dbSNP:rs1758567
Protein function: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Reference sequence:
MASPFALLMVLVVLSCKSSCSLGCDLPETHSLDNRRTLMLLAQMSRISPSSCLMDRHDFGFPQEEFDGNQFQKAPAISVLHELIQQIFNLFTTKDSSAAWDEDLLDKFCTELYQQLNDLEACVMQEERVGETPLMNADSILAVKKYFRRITLYLTEKKYSPCAWEVVRAEIMRSLSLSTNLQERLRRKE
UniProt ID: P01562
Variant: A -> V at position 137-137
Variant annotation: in alpha-1B; dbSNP:rs2230050
Protein function: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Reference sequence:
MASPFALLMVLVVLSCKSSCSLGCDLPETHSLDNRRTLMLLAQMSRISPSSCLMDRHDFGFPQEEFDGNQFQKAPAISVLHELIQQIFNLFTTKDSSAAWDEDLLDKFCTELYQQLNDLEACVMQEERVGETPLMNADSILAVKKYFRRITLYLTEKKYSPCAWEVVRAEIMRSLSLSTNLQERLRRKE