sujigwak/NVAR huggingface dataset:
UniProt ID: P40815
Variant: S -> T at position 350-350
Variant annotation: in strain: LT7
Protein function: A type III restriction enzyme that recognizes 2 inversely oriented double-stranded sequences 5'-CAGAG-3' and cleaves DNA 25-27 base pairs downstream. After binding to one recognition site undergoes random one-dimensional diffusion along DNA until it collides with a stationary enzyme bound to the second DNA site, which is when DNA cleavage occurs. DNA restriction requires both the Res and Mod subunits.
Reference sequence:
MMNILLEELPHQEQALAAILASFTGIDHAQADHNHYANPLIKERYDDKANIDVKMETGTGKTYVYTRLMYELHQKYGLFKFVLVVPTPAIKEGARNFITSDYARQHFSQFYENTRMELCTINAGDFKVKSGRKNFPAQLLSFTDASRRDSHTIQVLLINAQMLNSASMTRDDYDQTLLGGLTSPVKGLQMTRPVVIIDEPHRFARDNKFYRAIQAIQPQMIVRFGATFPDIVEGKGKNKCVRKDYYRRQPQFDLNAVDSFNDGLVKGIDIYYPNLPEEQANNRYIVDSVTAKKLILRRGSKIAEVGVGENLADVDAGFEGSIEYAGSKMLSNDLELEAGMALVPGTFGASYQELIIQDAIDKHFDTEQANFLRSNEPENNAPRIKTLSLFFIDSIKSYRDDEGWLKVTFERLLKKKLTQLIDDYQRKTLPREVEYLSFLQATLASLHSDNQNVHAGYFGEDRGSGDEAIQAEVDDILKNKEKLLSFSDHHGNWETRRFLFSKWTLREGWDNPNVFVIAKLRSSGSESSKIQEVGRGLRLPVDENGHRVHQEEWPSRLSFLIGYDEKAFASMLVDEINRDSKVQLNEQKLDEAMITLIVTERQKVDPAFTELRLLEDLDDKKLINRSNEFKPSVTLNGETKSGFAWLLEFYPELTQARVRADRIRDNKPASRLRVRLRKENWEQLSSIWEQFSRRYMLQFERSGASLEQIAAEVLRDPALYIRQKPSQVQQRLVSNEDNGRFEVAQREGELAASEFMAGMKYGHFLKQLALRTSLPVNVLHPVLMAMLRDVLHGDSRYLSEISLDNMTRALQTRINAHFAQRHDYLPLDFQASTSVFDSTARQFREEISAEIVGKNVDENAIDDPRSLYQIPPLRYDSVDPELPLLKYDYPQQVSVFGKLPKRAIQIPKYTGGSTTPDFVYRIERQDADSVYLLVETKAENMRVGDQVILDAQRKFFDMLRRQNINVEFAEATSAPAVFSTINGLIEGKAN
UniProt ID: P40815
Variant: L -> V at position 420-420
Variant annotation: in strain: LT7
Protein function: A type III restriction enzyme that recognizes 2 inversely oriented double-stranded sequences 5'-CAGAG-3' and cleaves DNA 25-27 base pairs downstream. After binding to one recognition site undergoes random one-dimensional diffusion along DNA until it collides with a stationary enzyme bound to the second DNA site, which is when DNA cleavage occurs. DNA restriction requires both the Res and Mod subunits.
Reference sequence:
MMNILLEELPHQEQALAAILASFTGIDHAQADHNHYANPLIKERYDDKANIDVKMETGTGKTYVYTRLMYELHQKYGLFKFVLVVPTPAIKEGARNFITSDYARQHFSQFYENTRMELCTINAGDFKVKSGRKNFPAQLLSFTDASRRDSHTIQVLLINAQMLNSASMTRDDYDQTLLGGLTSPVKGLQMTRPVVIIDEPHRFARDNKFYRAIQAIQPQMIVRFGATFPDIVEGKGKNKCVRKDYYRRQPQFDLNAVDSFNDGLVKGIDIYYPNLPEEQANNRYIVDSVTAKKLILRRGSKIAEVGVGENLADVDAGFEGSIEYAGSKMLSNDLELEAGMALVPGTFGASYQELIIQDAIDKHFDTEQANFLRSNEPENNAPRIKTLSLFFIDSIKSYRDDEGWLKVTFERLLKKKLTQLIDDYQRKTLPREVEYLSFLQATLASLHSDNQNVHAGYFGEDRGSGDEAIQAEVDDILKNKEKLLSFSDHHGNWETRRFLFSKWTLREGWDNPNVFVIAKLRSSGSESSKIQEVGRGLRLPVDENGHRVHQEEWPSRLSFLIGYDEKAFASMLVDEINRDSKVQLNEQKLDEAMITLIVTERQKVDPAFTELRLLEDLDDKKLINRSNEFKPSVTLNGETKSGFAWLLEFYPELTQARVRADRIRDNKPASRLRVRLRKENWEQLSSIWEQFSRRYMLQFERSGASLEQIAAEVLRDPALYIRQKPSQVQQRLVSNEDNGRFEVAQREGELAASEFMAGMKYGHFLKQLALRTSLPVNVLHPVLMAMLRDVLHGDSRYLSEISLDNMTRALQTRINAHFAQRHDYLPLDFQASTSVFDSTARQFREEISAEIVGKNVDENAIDDPRSLYQIPPLRYDSVDPELPLLKYDYPQQVSVFGKLPKRAIQIPKYTGGSTTPDFVYRIERQDADSVYLLVETKAENMRVGDQVILDAQRKFFDMLRRQNINVEFAEATSAPAVFSTINGLIEGKAN
UniProt ID: P40815
Variant: SG -> R at position 464-465
Variant annotation: in strain: LT7
Protein function: A type III restriction enzyme that recognizes 2 inversely oriented double-stranded sequences 5'-CAGAG-3' and cleaves DNA 25-27 base pairs downstream. After binding to one recognition site undergoes random one-dimensional diffusion along DNA until it collides with a stationary enzyme bound to the second DNA site, which is when DNA cleavage occurs. DNA restriction requires both the Res and Mod subunits.
Reference sequence:
MMNILLEELPHQEQALAAILASFTGIDHAQADHNHYANPLIKERYDDKANIDVKMETGTGKTYVYTRLMYELHQKYGLFKFVLVVPTPAIKEGARNFITSDYARQHFSQFYENTRMELCTINAGDFKVKSGRKNFPAQLLSFTDASRRDSHTIQVLLINAQMLNSASMTRDDYDQTLLGGLTSPVKGLQMTRPVVIIDEPHRFARDNKFYRAIQAIQPQMIVRFGATFPDIVEGKGKNKCVRKDYYRRQPQFDLNAVDSFNDGLVKGIDIYYPNLPEEQANNRYIVDSVTAKKLILRRGSKIAEVGVGENLADVDAGFEGSIEYAGSKMLSNDLELEAGMALVPGTFGASYQELIIQDAIDKHFDTEQANFLRSNEPENNAPRIKTLSLFFIDSIKSYRDDEGWLKVTFERLLKKKLTQLIDDYQRKTLPREVEYLSFLQATLASLHSDNQNVHAGYFGEDRGSGDEAIQAEVDDILKNKEKLLSFSDHHGNWETRRFLFSKWTLREGWDNPNVFVIAKLRSSGSESSKIQEVGRGLRLPVDENGHRVHQEEWPSRLSFLIGYDEKAFASMLVDEINRDSKVQLNEQKLDEAMITLIVTERQKVDPAFTELRLLEDLDDKKLINRSNEFKPSVTLNGETKSGFAWLLEFYPELTQARVRADRIRDNKPASRLRVRLRKENWEQLSSIWEQFSRRYMLQFERSGASLEQIAAEVLRDPALYIRQKPSQVQQRLVSNEDNGRFEVAQREGELAASEFMAGMKYGHFLKQLALRTSLPVNVLHPVLMAMLRDVLHGDSRYLSEISLDNMTRALQTRINAHFAQRHDYLPLDFQASTSVFDSTARQFREEISAEIVGKNVDENAIDDPRSLYQIPPLRYDSVDPELPLLKYDYPQQVSVFGKLPKRAIQIPKYTGGSTTPDFVYRIERQDADSVYLLVETKAENMRVGDQVILDAQRKFFDMLRRQNINVEFAEATSAPAVFSTINGLIEGKAN
UniProt ID: P40815
Variant: GL -> AV at position 536-537
Variant annotation: in strain: LT7
Protein function: A type III restriction enzyme that recognizes 2 inversely oriented double-stranded sequences 5'-CAGAG-3' and cleaves DNA 25-27 base pairs downstream. After binding to one recognition site undergoes random one-dimensional diffusion along DNA until it collides with a stationary enzyme bound to the second DNA site, which is when DNA cleavage occurs. DNA restriction requires both the Res and Mod subunits.
Reference sequence:
MMNILLEELPHQEQALAAILASFTGIDHAQADHNHYANPLIKERYDDKANIDVKMETGTGKTYVYTRLMYELHQKYGLFKFVLVVPTPAIKEGARNFITSDYARQHFSQFYENTRMELCTINAGDFKVKSGRKNFPAQLLSFTDASRRDSHTIQVLLINAQMLNSASMTRDDYDQTLLGGLTSPVKGLQMTRPVVIIDEPHRFARDNKFYRAIQAIQPQMIVRFGATFPDIVEGKGKNKCVRKDYYRRQPQFDLNAVDSFNDGLVKGIDIYYPNLPEEQANNRYIVDSVTAKKLILRRGSKIAEVGVGENLADVDAGFEGSIEYAGSKMLSNDLELEAGMALVPGTFGASYQELIIQDAIDKHFDTEQANFLRSNEPENNAPRIKTLSLFFIDSIKSYRDDEGWLKVTFERLLKKKLTQLIDDYQRKTLPREVEYLSFLQATLASLHSDNQNVHAGYFGEDRGSGDEAIQAEVDDILKNKEKLLSFSDHHGNWETRRFLFSKWTLREGWDNPNVFVIAKLRSSGSESSKIQEVGRGLRLPVDENGHRVHQEEWPSRLSFLIGYDEKAFASMLVDEINRDSKVQLNEQKLDEAMITLIVTERQKVDPAFTELRLLEDLDDKKLINRSNEFKPSVTLNGETKSGFAWLLEFYPELTQARVRADRIRDNKPASRLRVRLRKENWEQLSSIWEQFSRRYMLQFERSGASLEQIAAEVLRDPALYIRQKPSQVQQRLVSNEDNGRFEVAQREGELAASEFMAGMKYGHFLKQLALRTSLPVNVLHPVLMAMLRDVLHGDSRYLSEISLDNMTRALQTRINAHFAQRHDYLPLDFQASTSVFDSTARQFREEISAEIVGKNVDENAIDDPRSLYQIPPLRYDSVDPELPLLKYDYPQQVSVFGKLPKRAIQIPKYTGGSTTPDFVYRIERQDADSVYLLVETKAENMRVGDQVILDAQRKFFDMLRRQNINVEFAEATSAPAVFSTINGLIEGKAN
UniProt ID: P40815
Variant: DQVILDAQRKFFDMLRRQNINVEFAEATSAPAVFSTINGLIEGKAN -> IRLFLMRNVNSSICCVGKISMSSLRKDQRAGGIFYDQWLD at position 945-990
Variant annotation: in strain: LT7
Protein function: A type III restriction enzyme that recognizes 2 inversely oriented double-stranded sequences 5'-CAGAG-3' and cleaves DNA 25-27 base pairs downstream. After binding to one recognition site undergoes random one-dimensional diffusion along DNA until it collides with a stationary enzyme bound to the second DNA site, which is when DNA cleavage occurs. DNA restriction requires both the Res and Mod subunits.
Reference sequence:
MMNILLEELPHQEQALAAILASFTGIDHAQADHNHYANPLIKERYDDKANIDVKMETGTGKTYVYTRLMYELHQKYGLFKFVLVVPTPAIKEGARNFITSDYARQHFSQFYENTRMELCTINAGDFKVKSGRKNFPAQLLSFTDASRRDSHTIQVLLINAQMLNSASMTRDDYDQTLLGGLTSPVKGLQMTRPVVIIDEPHRFARDNKFYRAIQAIQPQMIVRFGATFPDIVEGKGKNKCVRKDYYRRQPQFDLNAVDSFNDGLVKGIDIYYPNLPEEQANNRYIVDSVTAKKLILRRGSKIAEVGVGENLADVDAGFEGSIEYAGSKMLSNDLELEAGMALVPGTFGASYQELIIQDAIDKHFDTEQANFLRSNEPENNAPRIKTLSLFFIDSIKSYRDDEGWLKVTFERLLKKKLTQLIDDYQRKTLPREVEYLSFLQATLASLHSDNQNVHAGYFGEDRGSGDEAIQAEVDDILKNKEKLLSFSDHHGNWETRRFLFSKWTLREGWDNPNVFVIAKLRSSGSESSKIQEVGRGLRLPVDENGHRVHQEEWPSRLSFLIGYDEKAFASMLVDEINRDSKVQLNEQKLDEAMITLIVTERQKVDPAFTELRLLEDLDDKKLINRSNEFKPSVTLNGETKSGFAWLLEFYPELTQARVRADRIRDNKPASRLRVRLRKENWEQLSSIWEQFSRRYMLQFERSGASLEQIAAEVLRDPALYIRQKPSQVQQRLVSNEDNGRFEVAQREGELAASEFMAGMKYGHFLKQLALRTSLPVNVLHPVLMAMLRDVLHGDSRYLSEISLDNMTRALQTRINAHFAQRHDYLPLDFQASTSVFDSTARQFREEISAEIVGKNVDENAIDDPRSLYQIPPLRYDSVDPELPLLKYDYPQQVSVFGKLPKRAIQIPKYTGGSTTPDFVYRIERQDADSVYLLVETKAENMRVGDQVILDAQRKFFDMLRRQNINVEFAEATSAPAVFSTINGLIEGKAN
UniProt ID: P40818
Variant: Q -> K at position 310-310
Variant annotation: found in a patient with spastic paraplegia; uncertain significance; dbSNP:rs587777201
Protein function: Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation .
Reference sequence:
MPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAKGSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSIKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLGPRVTDVAT
UniProt ID: P40818
Variant: D -> G at position 443-443
Variant annotation: in dbSNP:rs3743044
Protein function: Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation .
Reference sequence:
MPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAKGSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSIKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLGPRVTDVAT
UniProt ID: P40818
Variant: S -> C at position 718-718
Variant annotation: in PITA4; uncertain significance; somatic mutation; dbSNP:rs672601308
Protein function: Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation .
Reference sequence:
MPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAKGSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSIKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLGPRVTDVAT
UniProt ID: P40818
Variant: S -> P at position 718-718
Variant annotation: in PITA4; uncertain significance; somatic mutation; localizes to nucleus instead of cytoplasm; dbSNP:rs672601307
Protein function: Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation .
Reference sequence:
MPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAKGSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSIKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLGPRVTDVAT
UniProt ID: P40818
Variant: P -> R at position 720-720
Variant annotation: in PITA4; uncertain significance; somatic mutation; dbSNP:rs672601311
Protein function: Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation .
Reference sequence:
MPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAKGSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSIKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLGPRVTDVAT
UniProt ID: P40818
Variant: T -> A at position 739-739
Variant annotation: in dbSNP:rs11638390
Protein function: Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation .
Reference sequence:
MPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAKGSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSIKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLGPRVTDVAT