sujigwak/NVAR huggingface dataset:
UniProt ID: P84022
Variant: T -> I at position 261-261
Variant annotation: in LDS3; dbSNP:rs387906851
Protein function: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Reference sequence:
MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS
UniProt ID: P84022
Variant: R -> K at position 279-279
Variant annotation: in LDS3; dbSNP:rs387906852
Protein function: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Reference sequence:
MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS
UniProt ID: P84022
Variant: R -> W at position 287-287
Variant annotation: in LDS3; dbSNP:rs387906850
Protein function: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Reference sequence:
MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS
UniProt ID: P84022
Variant: P -> L at position 393-393
Variant annotation: in a colorectal cancer sample; somatic mutation
Protein function: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Reference sequence:
MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS
UniProt ID: P84032
Variant: S -> G at position 31-31
Protein function: Cysteine proteinase inhibitor.
Reference sequence:
ARPKSDCEKHRESTEKTGTIMKLIPKCKENSDYEELQCYEDSKFCVCYDKKGHAASPISTKVKECGCYLKQKERKDSGRESAIIPQCEEDGKWAKKQLWEFNKSCWCVDEKGEQVGKIHHDCDSLKCE
UniProt ID: P84032
Variant: H -> Y at position 119-119
Protein function: Cysteine proteinase inhibitor.
Reference sequence:
ARPKSDCEKHRESTEKTGTIMKLIPKCKENSDYEELQCYEDSKFCVCYDKKGHAASPISTKVKECGCYLKQKERKDSGRESAIIPQCEEDGKWAKKQLWEFNKSCWCVDEKGEQVGKIHHDCDSLKCE
UniProt ID: P84032
Variant: K -> N at position 126-126
Protein function: Cysteine proteinase inhibitor.
Reference sequence:
ARPKSDCEKHRESTEKTGTIMKLIPKCKENSDYEELQCYEDSKFCVCYDKKGHAASPISTKVKECGCYLKQKERKDSGRESAIIPQCEEDGKWAKKQLWEFNKSCWCVDEKGEQVGKIHHDCDSLKCE
UniProt ID: P84062
Variant: D -> G at position 15-15
Protein function: Lethal neurotoxin. Causes spastic paralysis and death in mice in 4-6 min after intracerebroventricular injection at dose levels of 1.5 ug per mouse.
Reference sequence:
AELKSCFPVGHECDDDASNCNCCGDDVYCACGWGRWNCKCKVADQSYAYGICKDKVNCPNRHLWPAKECKMPCRRNCG
UniProt ID: P84077
Variant: Y -> H at position 35-35
Variant annotation: in PVNH8; decreased interaction with GGA3; dbSNP:rs879036238
Protein function: (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.
Reference sequence:
MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
UniProt ID: P84077
Variant: R -> H at position 99-99
Variant annotation: in PVNH8; uncertain significance
Protein function: (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.
Reference sequence:
MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
UniProt ID: P84077
Variant: K -> E at position 127-127
Variant annotation: in PVNH8
Protein function: (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase.
Reference sequence:
MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
UniProt ID: P84527
Variant: Y -> H at position 85-85
Protein function: pH-dependent, voltage-gated and anion-selective pore-forming peptide.
Reference sequence:
MAQLALLLLSLFLTLISLAPPGASISSCNGPCRDLNDCDGQLICIKGKCNDDPQVGTHICRGTTPSPQPGGCKPSGTLTCRGKSYPTYDCSPPVTSSTPAKLTNNDFSEGGDDGGPSECDESYHNNNERIVALSTGWYNGGSRCGKMIRITASNGKSVSAKVVDECDSRHGCDKEHAGQPPCRNNIVDGSNAVWSALGLDKNVGVVDITWSMA
UniProt ID: P84674
Variant: M -> K at position 7-7
Variant annotation: in P2-2
Protein function: Snake venom phospholipase A2 (PLA2) that has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Reference sequence:
SLLEFGMMILEETGKLAVPFYSSYGCYCGWGGKGTPKDATDRCCFVHDCCYGNLPDCTPKPDRYKYKRVNGAIVCEQGTSCENRICECDKAAAICFTKNLNTYSKIYMLYPDFLCKGELKC
UniProt ID: P84674
Variant: S -> D at position 23-23
Variant annotation: in P3
Protein function: Snake venom phospholipase A2 (PLA2) that has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Reference sequence:
SLLEFGMMILEETGKLAVPFYSSYGCYCGWGGKGTPKDATDRCCFVHDCCYGNLPDCTPKPDRYKYKRVNGAIVCEQGTSCENRICECDKAAAICFTKNLNTYSKIYMLYPDFLCKGELKC
UniProt ID: P84857
Variant: L -> LC at position 180-180
Protein function: Has antitumor activity.
Reference sequence:
MVVALLAVVALSKGEGGVIMQHCKLACEAPIAAGYRLEKWYPKERAVLLASTALFGNNFGQTWSPSGFYGGSDASGFTYGGSAGFYNELRVTVSAQRAAIGVPVVKGSGWRSVSGGWPPNCRPGQNNLDGQGAWGGGSCLCAGAIVLPVRDEGPLILDGGPSRDTVPDPPKPLKGPFEWLKMIFDPRQRRFTAEEIVSRLAQRSGGRKRFEMFREPGALKRWDTSVTVPKIEQYAKLPAGDGPTAKPNISVGGMALCAMKQMVKKVGPDSD
UniProt ID: P84996
Variant: R -> C at position 201-201
Variant annotation: in a colorectal cancer sample; somatic mutation
Protein function: May inhibit the adenylyl cyclase-stimulating activity of guanine nucleotide-binding protein G(s) subunit alpha which is produced from the same locus in a different open reading frame.
Reference sequence:
MMARPVDPQRSPDPTFRSSTRHSGKLEPMEATAHLLRKQCPSRLNSPAWEASGLHWSSLDSPVGSMQALRPSAQHSWSPEPSVVPDQAWEDTALHQKKLCPLSLTSLPREAAVNFSYRSQTLLQEAQVLQGSPELLPRSPKPSGLQRLAPEEATALPLRRLCHLSLMEKDLGTTAHPRGFPELSHKSTAAASSRQSRPRVRSASLPPRTRLPSGSQAPSAAHPKRLSDLLLTSRAAAPGWRSPDPRSRLAAPPLGSTTLPSTWTAPQSRLTARPSRSPEPQIRESEQRDPQLRRKQQRWKEPLMPRREEKYPLRGTDPLPPGQPQRIPLPGQPLQPQPILTPGQPQKIPTPGQHQPILTPGHSQPIPTPGQPLPPQPIPTPGRPLTPQPIPTPGRPLTPQPIQMPGRPLRLPPPLRLLRPGQPMSPQLRQTQGLPLPQPLLPPGQPKSAGRPLQPLPPGPDARSISDPPAPRSRLPIRLLRGLLARLPGGASPRAAAAAACTTMKGWPAATMTPAETSPTMGPPDASAGFSIGEIAAAESPSATYSATFSCKPSGAASVDLRVPSPKPRALSRSRRYPWRRSADRCAKKPWRSGPRSAQRRNAVSSSTNNSRTKRWATCVRTACCF
UniProt ID: P84996
Variant: R -> H at position 201-201
Variant annotation: in a colorectal cancer sample; somatic mutation
Protein function: May inhibit the adenylyl cyclase-stimulating activity of guanine nucleotide-binding protein G(s) subunit alpha which is produced from the same locus in a different open reading frame.
Reference sequence:
MMARPVDPQRSPDPTFRSSTRHSGKLEPMEATAHLLRKQCPSRLNSPAWEASGLHWSSLDSPVGSMQALRPSAQHSWSPEPSVVPDQAWEDTALHQKKLCPLSLTSLPREAAVNFSYRSQTLLQEAQVLQGSPELLPRSPKPSGLQRLAPEEATALPLRRLCHLSLMEKDLGTTAHPRGFPELSHKSTAAASSRQSRPRVRSASLPPRTRLPSGSQAPSAAHPKRLSDLLLTSRAAAPGWRSPDPRSRLAAPPLGSTTLPSTWTAPQSRLTARPSRSPEPQIRESEQRDPQLRRKQQRWKEPLMPRREEKYPLRGTDPLPPGQPQRIPLPGQPLQPQPILTPGQPQKIPTPGQHQPILTPGHSQPIPTPGQPLPPQPIPTPGRPLTPQPIPTPGRPLTPQPIQMPGRPLRLPPPLRLLRPGQPMSPQLRQTQGLPLPQPLLPPGQPKSAGRPLQPLPPGPDARSISDPPAPRSRLPIRLLRGLLARLPGGASPRAAAAAACTTMKGWPAATMTPAETSPTMGPPDASAGFSIGEIAAAESPSATYSATFSCKPSGAASVDLRVPSPKPRALSRSRRYPWRRSADRCAKKPWRSGPRSAQRRNAVSSSTNNSRTKRWATCVRTACCF
UniProt ID: P84996
Variant: P -> T at position 374-374
Variant annotation: in GNASHYP; dbSNP:rs1376506169
Protein function: May inhibit the adenylyl cyclase-stimulating activity of guanine nucleotide-binding protein G(s) subunit alpha which is produced from the same locus in a different open reading frame.
Reference sequence:
MMARPVDPQRSPDPTFRSSTRHSGKLEPMEATAHLLRKQCPSRLNSPAWEASGLHWSSLDSPVGSMQALRPSAQHSWSPEPSVVPDQAWEDTALHQKKLCPLSLTSLPREAAVNFSYRSQTLLQEAQVLQGSPELLPRSPKPSGLQRLAPEEATALPLRRLCHLSLMEKDLGTTAHPRGFPELSHKSTAAASSRQSRPRVRSASLPPRTRLPSGSQAPSAAHPKRLSDLLLTSRAAAPGWRSPDPRSRLAAPPLGSTTLPSTWTAPQSRLTARPSRSPEPQIRESEQRDPQLRRKQQRWKEPLMPRREEKYPLRGTDPLPPGQPQRIPLPGQPLQPQPILTPGQPQKIPTPGQHQPILTPGHSQPIPTPGQPLPPQPIPTPGRPLTPQPIPTPGRPLTPQPIQMPGRPLRLPPPLRLLRPGQPMSPQLRQTQGLPLPQPLLPPGQPKSAGRPLQPLPPGPDARSISDPPAPRSRLPIRLLRGLLARLPGGASPRAAAAAACTTMKGWPAATMTPAETSPTMGPPDASAGFSIGEIAAAESPSATYSATFSCKPSGAASVDLRVPSPKPRALSRSRRYPWRRSADRCAKKPWRSGPRSAQRRNAVSSSTNNSRTKRWATCVRTACCF
UniProt ID: P84996
Variant: P -> PQPIPTPGRPLTP at position 375-375
Variant annotation: in GNASHYP
Protein function: May inhibit the adenylyl cyclase-stimulating activity of guanine nucleotide-binding protein G(s) subunit alpha which is produced from the same locus in a different open reading frame.
Reference sequence:
MMARPVDPQRSPDPTFRSSTRHSGKLEPMEATAHLLRKQCPSRLNSPAWEASGLHWSSLDSPVGSMQALRPSAQHSWSPEPSVVPDQAWEDTALHQKKLCPLSLTSLPREAAVNFSYRSQTLLQEAQVLQGSPELLPRSPKPSGLQRLAPEEATALPLRRLCHLSLMEKDLGTTAHPRGFPELSHKSTAAASSRQSRPRVRSASLPPRTRLPSGSQAPSAAHPKRLSDLLLTSRAAAPGWRSPDPRSRLAAPPLGSTTLPSTWTAPQSRLTARPSRSPEPQIRESEQRDPQLRRKQQRWKEPLMPRREEKYPLRGTDPLPPGQPQRIPLPGQPLQPQPILTPGQPQKIPTPGQHQPILTPGHSQPIPTPGQPLPPQPIPTPGRPLTPQPIPTPGRPLTPQPIQMPGRPLRLPPPLRLLRPGQPMSPQLRQTQGLPLPQPLLPPGQPKSAGRPLQPLPPGPDARSISDPPAPRSRLPIRLLRGLLARLPGGASPRAAAAAACTTMKGWPAATMTPAETSPTMGPPDASAGFSIGEIAAAESPSATYSATFSCKPSGAASVDLRVPSPKPRALSRSRRYPWRRSADRCAKKPWRSGPRSAQRRNAVSSSTNNSRTKRWATCVRTACCF
UniProt ID: P84996
Variant: L -> V at position 397-397
Variant annotation: in GNASHYP
Protein function: May inhibit the adenylyl cyclase-stimulating activity of guanine nucleotide-binding protein G(s) subunit alpha which is produced from the same locus in a different open reading frame.
Reference sequence:
MMARPVDPQRSPDPTFRSSTRHSGKLEPMEATAHLLRKQCPSRLNSPAWEASGLHWSSLDSPVGSMQALRPSAQHSWSPEPSVVPDQAWEDTALHQKKLCPLSLTSLPREAAVNFSYRSQTLLQEAQVLQGSPELLPRSPKPSGLQRLAPEEATALPLRRLCHLSLMEKDLGTTAHPRGFPELSHKSTAAASSRQSRPRVRSASLPPRTRLPSGSQAPSAAHPKRLSDLLLTSRAAAPGWRSPDPRSRLAAPPLGSTTLPSTWTAPQSRLTARPSRSPEPQIRESEQRDPQLRRKQQRWKEPLMPRREEKYPLRGTDPLPPGQPQRIPLPGQPLQPQPILTPGQPQKIPTPGQHQPILTPGHSQPIPTPGQPLPPQPIPTPGRPLTPQPIPTPGRPLTPQPIQMPGRPLRLPPPLRLLRPGQPMSPQLRQTQGLPLPQPLLPPGQPKSAGRPLQPLPPGPDARSISDPPAPRSRLPIRLLRGLLARLPGGASPRAAAAAACTTMKGWPAATMTPAETSPTMGPPDASAGFSIGEIAAAESPSATYSATFSCKPSGAASVDLRVPSPKPRALSRSRRYPWRRSADRCAKKPWRSGPRSAQRRNAVSSSTNNSRTKRWATCVRTACCF
UniProt ID: P85298
Variant: Y -> C at position 172-172
Variant annotation: in dbSNP:rs16992915
Protein function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.
Reference sequence:
MAGQDPALSTSHPFYDVARHGILQVAGDDRFGRRVVTFSCCRMPPSHELDHQRLLEYLKYTLDQYVENDYTIVYFHYGLNSRNKPSLGWLQSAYKEFDRKDGDLTMWPRLVSNSKLKRSSHLSLPKYWDYRYKKNLKALYVVHPTSFIKVLWNILKPLISHKFGKKVIYFNYLSELHEHLKYDQLVIPPEVLRYDEKLQSLHEGRTPPPTKTPPPRPPLPTQQFGVSLQYLKDKNQGELIPPVLRFTVTYLREKGLRTEGLFRRSASVQTVREIQRLYNQGKPVNFDDYGDIHIPAVILKTFLRELPQPLLTFQAYEQILGITCVESSLRVTGCRQILRSLPEHNYVVLRYLMGFLHAVSRESIFNKMNSSNLACVFGLNLIWPSQGVSSLSALVPLNMFTELLIEYYEKIFSTPEAPGEHGLAPWEQGSRAAPLQEAVPRTQATGLTKPTLPPSPLMAARRRL
UniProt ID: P85298
Variant: G -> R at position 333-333
Variant annotation: in dbSNP:rs6007344
Protein function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.
Reference sequence:
MAGQDPALSTSHPFYDVARHGILQVAGDDRFGRRVVTFSCCRMPPSHELDHQRLLEYLKYTLDQYVENDYTIVYFHYGLNSRNKPSLGWLQSAYKEFDRKDGDLTMWPRLVSNSKLKRSSHLSLPKYWDYRYKKNLKALYVVHPTSFIKVLWNILKPLISHKFGKKVIYFNYLSELHEHLKYDQLVIPPEVLRYDEKLQSLHEGRTPPPTKTPPPRPPLPTQQFGVSLQYLKDKNQGELIPPVLRFTVTYLREKGLRTEGLFRRSASVQTVREIQRLYNQGKPVNFDDYGDIHIPAVILKTFLRELPQPLLTFQAYEQILGITCVESSLRVTGCRQILRSLPEHNYVVLRYLMGFLHAVSRESIFNKMNSSNLACVFGLNLIWPSQGVSSLSALVPLNMFTELLIEYYEKIFSTPEAPGEHGLAPWEQGSRAAPLQEAVPRTQATGLTKPTLPPSPLMAARRRL
UniProt ID: P85298
Variant: P -> L at position 415-415
Variant annotation: in dbSNP:rs2071762
Protein function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.
Reference sequence:
MAGQDPALSTSHPFYDVARHGILQVAGDDRFGRRVVTFSCCRMPPSHELDHQRLLEYLKYTLDQYVENDYTIVYFHYGLNSRNKPSLGWLQSAYKEFDRKDGDLTMWPRLVSNSKLKRSSHLSLPKYWDYRYKKNLKALYVVHPTSFIKVLWNILKPLISHKFGKKVIYFNYLSELHEHLKYDQLVIPPEVLRYDEKLQSLHEGRTPPPTKTPPPRPPLPTQQFGVSLQYLKDKNQGELIPPVLRFTVTYLREKGLRTEGLFRRSASVQTVREIQRLYNQGKPVNFDDYGDIHIPAVILKTFLRELPQPLLTFQAYEQILGITCVESSLRVTGCRQILRSLPEHNYVVLRYLMGFLHAVSRESIFNKMNSSNLACVFGLNLIWPSQGVSSLSALVPLNMFTELLIEYYEKIFSTPEAPGEHGLAPWEQGSRAAPLQEAVPRTQATGLTKPTLPPSPLMAARRRL
UniProt ID: P85298
Variant: P -> R at position 418-418
Variant annotation: in dbSNP:rs9614957
Protein function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.
Reference sequence:
MAGQDPALSTSHPFYDVARHGILQVAGDDRFGRRVVTFSCCRMPPSHELDHQRLLEYLKYTLDQYVENDYTIVYFHYGLNSRNKPSLGWLQSAYKEFDRKDGDLTMWPRLVSNSKLKRSSHLSLPKYWDYRYKKNLKALYVVHPTSFIKVLWNILKPLISHKFGKKVIYFNYLSELHEHLKYDQLVIPPEVLRYDEKLQSLHEGRTPPPTKTPPPRPPLPTQQFGVSLQYLKDKNQGELIPPVLRFTVTYLREKGLRTEGLFRRSASVQTVREIQRLYNQGKPVNFDDYGDIHIPAVILKTFLRELPQPLLTFQAYEQILGITCVESSLRVTGCRQILRSLPEHNYVVLRYLMGFLHAVSRESIFNKMNSSNLACVFGLNLIWPSQGVSSLSALVPLNMFTELLIEYYEKIFSTPEAPGEHGLAPWEQGSRAAPLQEAVPRTQATGLTKPTLPPSPLMAARRRL
UniProt ID: P85299
Variant: V -> M at position 243-243
Variant annotation: in dbSNP:rs36082900
Protein function: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. PRR5 plays an important role in regulation of PDGFRB expression and in modulation of platelet-derived growth factor signaling. May act as a tumor suppressor in breast cancer.
Reference sequence:
MRTLRRLKFMSSPSLSDLGKREPAAAADERGTQQRRACANATWNSIHNGVIAVFQRKGLPDQELFSLNEGVRQLLKTELGSFFTEYLQNQLLTKGMVILRDKIRFYEGQKLLDSLAETWDFFFSDVLPMLQAIFYPVQGKEPSVRQLALLHFRNAITLSVKLEDALARAHARVPPAIVQMLLVLQGVHESRGVTEDYLRLETLVQKVVSPYLGTYGLHSSEGPFTHSCILEKRLLRRSRSGDVLAKNPVVRSKSYNTPLLNPVQEHEAEGAAAGGTSIRRHSVSEMTSCPEPQGFSDPPGQGPTGTFRSSPAPHSGPCPSRLYPTTQPPEQGLDPTRSSLPRSSPENLVDQILESVDSDSEGIFIDFGRGRGSGMSDLEGSGGRQSVV
UniProt ID: P85800
Variant: E -> H at position 31-31
Protein function: Thrombin inhibitor. Does not inhibit other serine proteases.
Reference sequence:
SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES
UniProt ID: P86383
Variant: I -> T at position 5-5
Variant annotation: in isozyme B
Protein function: Has bacteriolytic activity against Gram-positive bacteria M.luteus. Also has chitinase activity.
Reference sequence:
FAGGIVSQRCLSCICKMESGCRNVGCKMDMGSLSCGYFQIKEAYWIDCGRPGSSWKSCAASSYCASLCVQNYMKRYAKWAGCPLRCEGFAREHNGGPRGCKKGSTIGYWNRLQKISGCHGVQ
UniProt ID: P86468
Variant: N -> D at position 17-17
Protein function: Has both toxic and EGF activity.
Reference sequence:
DQGTACTGEHAHNFCLNGGTCRHIQSLGEYYCICPEGYTGHRCEK
UniProt ID: P86469
Variant: N -> D at position 17-17
Protein function: Has both toxic and EGF activity.
Reference sequence:
DQGTACTGEHAHSFCLNGGTCRHIQQLGE
UniProt ID: P87187
Variant: T -> A at position 374-374
Variant annotation: in strain: CHAU1
Protein function: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. Plays a role in both tRNA-processing and mitochondrial metabolism. Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.
Reference sequence:
MYKTVLKNSGRIQRNFIFRNVSSTLQRSLATSASTSSSTTTSNAETGELHVSTPLDSPSVHPPDGSSISLKSATRDASLFGTRPIYLDVQATTPVDPRVLDKMLEFYTGLYGNPHSSTHAYGWETDKEVEKARGYIADVINADPKEIIFTSGATETNNMAIKGVPRFYKKTKKHIITTQTEHKCVLDSARHMQDEGFDITYLPVNSEGLINLDDLKKAIRKDTVLVSVMAVNNEIGVIQPLKEIGQICRENKIFFHTDAAQAYGKIPIDVNEMNIDLLSISSHKIYGPKGIGACYVRRRPRVRLDPIITGGGQERGLRSGTLAPPLVAGFGEAARLMKQESAFDKKHIEKLSTKLKNGLLSIPSTQFNGCNNPTYQYPGCVNVSFAYIEGESLLMALKDIALSSGSACTSASLEPSYVLHALGADDALAHSSIRFGIGRFTTEAEVDYVIQAINERVDFLRKMSPLWEMVQGGIDLNSIEWSGH
UniProt ID: P91627
Variant: V -> L at position 13-13
Variant annotation: in strain: 0101.3, 0101.4, 0101.5, 0101.7, 0101.9, MSH22, MA28, MA32, MSH38, SP138, SP235 and SP295
Protein function: Component of the larval cuticle.
Reference sequence:
MFKFVMVFAVLGVAAAGVAHVPHPQVSHPVGRSEDVHAEVKSEHSDVRADGFDADLLVSNSIQQASSGDVHGNIHGSFSWISPEGEHVEIKYVADENGYQPVGAVLPTPPPIPEAIARAVAWLEAHPQAPEPVHHSHH
UniProt ID: P91627
Variant: P -> Q at position 29-29
Variant annotation: in strain: 0101.3, 0101.4, 0101.5, 0101.7, 0101.9, MSH22, MA28, MA32, MSH38, SP138, SP235 and SP295
Protein function: Component of the larval cuticle.
Reference sequence:
MFKFVMVFAVLGVAAAGVAHVPHPQVSHPVGRSEDVHAEVKSEHSDVRADGFDADLLVSNSIQQASSGDVHGNIHGSFSWISPEGEHVEIKYVADENGYQPVGAVLPTPPPIPEAIARAVAWLEAHPQAPEPVHHSHH
UniProt ID: P91627
Variant: V -> I at position 47-47
Variant annotation: in strain: 0101.3, 0101.4, 0101.5, 0101.7, 0101.9, MSH22, MA28, MA32, MSH38, SP138, SP235 and SP295
Protein function: Component of the larval cuticle.
Reference sequence:
MFKFVMVFAVLGVAAAGVAHVPHPQVSHPVGRSEDVHAEVKSEHSDVRADGFDADLLVSNSIQQASSGDVHGNIHGSFSWISPEGEHVEIKYVADENGYQPVGAVLPTPPPIPEAIARAVAWLEAHPQAPEPVHHSHH
UniProt ID: P91627
Variant: F -> Y at position 52-52
Variant annotation: in strain: SP235
Protein function: Component of the larval cuticle.
Reference sequence:
MFKFVMVFAVLGVAAAGVAHVPHPQVSHPVGRSEDVHAEVKSEHSDVRADGFDADLLVSNSIQQASSGDVHGNIHGSFSWISPEGEHVEIKYVADENGYQPVGAVLPTPPPIPEAIARAVAWLEAHPQAPEPVHHSHH
UniProt ID: P91627
Variant: D -> H at position 53-53
Variant annotation: in strain: 0101.5
Protein function: Component of the larval cuticle.
Reference sequence:
MFKFVMVFAVLGVAAAGVAHVPHPQVSHPVGRSEDVHAEVKSEHSDVRADGFDADLLVSNSIQQASSGDVHGNIHGSFSWISPEGEHVEIKYVADENGYQPVGAVLPTPPPIPEAIARAVAWLEAHPQAPEPVHHSHH
UniProt ID: P91627
Variant: L -> F at position 56-56
Variant annotation: in strain: MSH22
Protein function: Component of the larval cuticle.
Reference sequence:
MFKFVMVFAVLGVAAAGVAHVPHPQVSHPVGRSEDVHAEVKSEHSDVRADGFDADLLVSNSIQQASSGDVHGNIHGSFSWISPEGEHVEIKYVADENGYQPVGAVLPTPPPIPEAIARAVAWLEAHPQAPEPVHHSHH
UniProt ID: P91627
Variant: A -> V at position 129-129
Variant annotation: in strain: 0101.3, 0101.4, 0101.5, 0101.7, 0101.9, MSH22, MA28, MA32, MSH38, SP138, SP235 and SP295
Protein function: Component of the larval cuticle.
Reference sequence:
MFKFVMVFAVLGVAAAGVAHVPHPQVSHPVGRSEDVHAEVKSEHSDVRADGFDADLLVSNSIQQASSGDVHGNIHGSFSWISPEGEHVEIKYVADENGYQPVGAVLPTPPPIPEAIARAVAWLEAHPQAPEPVHHSHH
UniProt ID: P91793
Variant: K -> Q at position 2-2
Variant annotation: in forms A3, A4, A5 and A2 from strain Liverpool
Protein function: Antibacterial peptide mostly active against Gram-positive bacteria. Has activity against the bacteria Gram-negative E.cloacae beta12.
Reference sequence:
MKSITVICFLALCTVAITSAYPQEPVLADEARPFANSLFDELPEETYQAAVENFRLKRATCDLLSGFGVGDSACAAHCIARGNRGGYCNSKKVCVCRN
UniProt ID: P91793
Variant: S -> P at position 3-3
Variant annotation: in form A4
Protein function: Antibacterial peptide mostly active against Gram-positive bacteria. Has activity against the bacteria Gram-negative E.cloacae beta12.
Reference sequence:
MKSITVICFLALCTVAITSAYPQEPVLADEARPFANSLFDELPEETYQAAVENFRLKRATCDLLSGFGVGDSACAAHCIARGNRGGYCNSKKVCVCRN
UniProt ID: P91793
Variant: I -> L at position 4-4
Variant annotation: in forms A2, A3, A4 and A2 from strain Liverpool
Protein function: Antibacterial peptide mostly active against Gram-positive bacteria. Has activity against the bacteria Gram-negative E.cloacae beta12.
Reference sequence:
MKSITVICFLALCTVAITSAYPQEPVLADEARPFANSLFDELPEETYQAAVENFRLKRATCDLLSGFGVGDSACAAHCIARGNRGGYCNSKKVCVCRN