sujigwak/NVAR huggingface dataset:
UniProt ID: P54577
Variant: D -> Y at position 308-308
Variant annotation: found in a patient with proximal-predominant motor neuropathy; likely pathogenic; loss of function; dbSNP:rs1207371448
Effect: loss
Target: function
Protein function: Tyrosine--tRNA ligase that catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (Probable) . Also acts as a positive regulator of poly-ADP-ribosylation in the nucleus, independently of its tyrosine--tRNA ligase activity . Activity is switched upon resveratrol-binding: resveratrol strongly inhibits the tyrosine--tRNA ligase activity and promotes relocalization to the nucleus, where YARS1 specifically stimulates the poly-ADP-ribosyltransferase activity of PARP1 .
Reference sequence:
MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDEELKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS
UniProt ID: P54577
Variant: G -> R at position 525-525
Variant annotation: in IMNEPD2; uncertain significance; dbSNP:rs1553122256
Protein function: Tyrosine--tRNA ligase that catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (Probable) . Also acts as a positive regulator of poly-ADP-ribosylation in the nucleus, independently of its tyrosine--tRNA ligase activity . Activity is switched upon resveratrol-binding: resveratrol strongly inhibits the tyrosine--tRNA ligase activity and promotes relocalization to the nucleus, where YARS1 specifically stimulates the poly-ADP-ribosyltransferase activity of PARP1 .
Reference sequence:
MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDEELKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS
UniProt ID: P54619
Variant: T -> S at position 89-89
Variant annotation: in dbSNP:rs1126930
Protein function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.
Reference sequence:
METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP
UniProt ID: P54619
Variant: K -> N at position 329-329
Variant annotation: in dbSNP:rs34210356
Protein function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.
Reference sequence:
METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP
UniProt ID: P54704
Variant: T -> S at position 233-233
Variant annotation: in strain: WS576 and WS380B
Protein function: Required for incorporation of cotE into the spore coat and for the formation of the outer layer. Has a cross-bridging function between cellulose and other coat proteins.
Reference sequence:
MRLLSVLLIGFLCLAGTYAQKYQLSPAYNDPYLTDDKTGTHDFWVQNASLPVFYGFHDWNFQDNSGIMEINGDEMHITGKIYPTVNMGDCHRYNVDLVFKKDKSGNVMPKKELRESAYVPHGPIDPATWKYYTFVQGKWTGFGCDPQNVVFSGAEGGMPLQLGYGANGKNGDNGISVWLIYGYTIVDINCNIRPIITQSPTQPPTQPPTYPPTQPPTQPPTQPPTYPPTYPPTYPPTYPPTYPPTHPPTYPPTYPPTQPPTQPPVQDCSTLECPEGFHCEIVNNRRTCVCDTTVPPTHPPTQSPTYPPTQPPTQPPTYPPTYPPTYPPTQPPRASCDNVRCPRGYHCECNHWENVARCVRNEEPTHRPKPPHHGCRPDSCARGEKCICVRGKIYCIPKTTCDQVRCPRKHHCECNRKGQVFCVPDCPKLTCKQVGCPENHECVSRRGELHCVYVRPPTGRWGDDLSDLGYNQASVEAAIDAYEAQRGQRPHNNIPSNNLHQENNDNLGDGFYDGVEIGFADGGFDVNDLNGF
UniProt ID: P54704
Variant: T -> S at position 237-237
Variant annotation: in strain: WS576 and WS380B
Protein function: Required for incorporation of cotE into the spore coat and for the formation of the outer layer. Has a cross-bridging function between cellulose and other coat proteins.
Reference sequence:
MRLLSVLLIGFLCLAGTYAQKYQLSPAYNDPYLTDDKTGTHDFWVQNASLPVFYGFHDWNFQDNSGIMEINGDEMHITGKIYPTVNMGDCHRYNVDLVFKKDKSGNVMPKKELRESAYVPHGPIDPATWKYYTFVQGKWTGFGCDPQNVVFSGAEGGMPLQLGYGANGKNGDNGISVWLIYGYTIVDINCNIRPIITQSPTQPPTQPPTYPPTQPPTQPPTQPPTYPPTYPPTYPPTYPPTYPPTHPPTYPPTYPPTQPPTQPPVQDCSTLECPEGFHCEIVNNRRTCVCDTTVPPTHPPTQSPTYPPTQPPTQPPTYPPTYPPTYPPTQPPRASCDNVRCPRGYHCECNHWENVARCVRNEEPTHRPKPPHHGCRPDSCARGEKCICVRGKIYCIPKTTCDQVRCPRKHHCECNRKGQVFCVPDCPKLTCKQVGCPENHECVSRRGELHCVYVRPPTGRWGDDLSDLGYNQASVEAAIDAYEAQRGQRPHNNIPSNNLHQENNDNLGDGFYDGVEIGFADGGFDVNDLNGF
UniProt ID: P54704
Variant: PTYPPTQ -> RSYPQTP at position 252-258
Variant annotation: in strain: WS380B
Protein function: Required for incorporation of cotE into the spore coat and for the formation of the outer layer. Has a cross-bridging function between cellulose and other coat proteins.
Reference sequence:
MRLLSVLLIGFLCLAGTYAQKYQLSPAYNDPYLTDDKTGTHDFWVQNASLPVFYGFHDWNFQDNSGIMEINGDEMHITGKIYPTVNMGDCHRYNVDLVFKKDKSGNVMPKKELRESAYVPHGPIDPATWKYYTFVQGKWTGFGCDPQNVVFSGAEGGMPLQLGYGANGKNGDNGISVWLIYGYTIVDINCNIRPIITQSPTQPPTQPPTYPPTQPPTQPPTQPPTYPPTYPPTYPPTYPPTYPPTHPPTYPPTYPPTQPPTQPPVQDCSTLECPEGFHCEIVNNRRTCVCDTTVPPTHPPTQSPTYPPTQPPTQPPTYPPTYPPTYPPTQPPRASCDNVRCPRGYHCECNHWENVARCVRNEEPTHRPKPPHHGCRPDSCARGEKCICVRGKIYCIPKTTCDQVRCPRKHHCECNRKGQVFCVPDCPKLTCKQVGCPENHECVSRRGELHCVYVRPPTGRWGDDLSDLGYNQASVEAAIDAYEAQRGQRPHNNIPSNNLHQENNDNLGDGFYDGVEIGFADGGFDVNDLNGF
UniProt ID: P54704
Variant: TY -> SC at position 253-254
Variant annotation: in strain: WS576
Protein function: Required for incorporation of cotE into the spore coat and for the formation of the outer layer. Has a cross-bridging function between cellulose and other coat proteins.
Reference sequence:
MRLLSVLLIGFLCLAGTYAQKYQLSPAYNDPYLTDDKTGTHDFWVQNASLPVFYGFHDWNFQDNSGIMEINGDEMHITGKIYPTVNMGDCHRYNVDLVFKKDKSGNVMPKKELRESAYVPHGPIDPATWKYYTFVQGKWTGFGCDPQNVVFSGAEGGMPLQLGYGANGKNGDNGISVWLIYGYTIVDINCNIRPIITQSPTQPPTQPPTYPPTQPPTQPPTQPPTYPPTYPPTYPPTYPPTYPPTHPPTYPPTYPPTQPPTQPPVQDCSTLECPEGFHCEIVNNRRTCVCDTTVPPTHPPTQSPTYPPTQPPTQPPTYPPTYPPTYPPTQPPRASCDNVRCPRGYHCECNHWENVARCVRNEEPTHRPKPPHHGCRPDSCARGEKCICVRGKIYCIPKTTCDQVRCPRKHHCECNRKGQVFCVPDCPKLTCKQVGCPENHECVSRRGELHCVYVRPPTGRWGDDLSDLGYNQASVEAAIDAYEAQRGQRPHNNIPSNNLHQENNDNLGDGFYDGVEIGFADGGFDVNDLNGF
UniProt ID: P54704
Variant: T -> S at position 261-261
Variant annotation: in strain: WS380B
Protein function: Required for incorporation of cotE into the spore coat and for the formation of the outer layer. Has a cross-bridging function between cellulose and other coat proteins.
Reference sequence:
MRLLSVLLIGFLCLAGTYAQKYQLSPAYNDPYLTDDKTGTHDFWVQNASLPVFYGFHDWNFQDNSGIMEINGDEMHITGKIYPTVNMGDCHRYNVDLVFKKDKSGNVMPKKELRESAYVPHGPIDPATWKYYTFVQGKWTGFGCDPQNVVFSGAEGGMPLQLGYGANGKNGDNGISVWLIYGYTIVDINCNIRPIITQSPTQPPTQPPTYPPTQPPTQPPTQPPTYPPTYPPTYPPTYPPTYPPTHPPTYPPTYPPTQPPTQPPVQDCSTLECPEGFHCEIVNNRRTCVCDTTVPPTHPPTQSPTYPPTQPPTQPPTYPPTYPPTYPPTQPPRASCDNVRCPRGYHCECNHWENVARCVRNEEPTHRPKPPHHGCRPDSCARGEKCICVRGKIYCIPKTTCDQVRCPRKHHCECNRKGQVFCVPDCPKLTCKQVGCPENHECVSRRGELHCVYVRPPTGRWGDDLSDLGYNQASVEAAIDAYEAQRGQRPHNNIPSNNLHQENNDNLGDGFYDGVEIGFADGGFDVNDLNGF
UniProt ID: P54704
Variant: P -> S at position 315-315
Variant annotation: in strain: WS576
Protein function: Required for incorporation of cotE into the spore coat and for the formation of the outer layer. Has a cross-bridging function between cellulose and other coat proteins.
Reference sequence:
MRLLSVLLIGFLCLAGTYAQKYQLSPAYNDPYLTDDKTGTHDFWVQNASLPVFYGFHDWNFQDNSGIMEINGDEMHITGKIYPTVNMGDCHRYNVDLVFKKDKSGNVMPKKELRESAYVPHGPIDPATWKYYTFVQGKWTGFGCDPQNVVFSGAEGGMPLQLGYGANGKNGDNGISVWLIYGYTIVDINCNIRPIITQSPTQPPTQPPTYPPTQPPTQPPTQPPTYPPTYPPTYPPTYPPTYPPTHPPTYPPTYPPTQPPTQPPVQDCSTLECPEGFHCEIVNNRRTCVCDTTVPPTHPPTQSPTYPPTQPPTQPPTYPPTYPPTYPPTQPPRASCDNVRCPRGYHCECNHWENVARCVRNEEPTHRPKPPHHGCRPDSCARGEKCICVRGKIYCIPKTTCDQVRCPRKHHCECNRKGQVFCVPDCPKLTCKQVGCPENHECVSRRGELHCVYVRPPTGRWGDDLSDLGYNQASVEAAIDAYEAQRGQRPHNNIPSNNLHQENNDNLGDGFYDGVEIGFADGGFDVNDLNGF
UniProt ID: P54710
Variant: G -> R at position 41-41
Variant annotation: in HOMG2; fails to localize to plasma membrane; dbSNP:rs28938168
Protein function: May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase.
Reference sequence:
MTGLSMDGGGSPKGDVDPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRCGGNKKRRQINEDEP
UniProt ID: P54725
Variant: T -> A at position 131-131
Variant annotation: in dbSNP:rs11558955
Protein function: (Microbial infection) Involved in Vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome.
Reference sequence:
MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE
UniProt ID: P54725
Variant: R -> Q at position 179-179
Variant annotation: in dbSNP:rs4987203
Protein function: (Microbial infection) Involved in Vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome.
Reference sequence:
MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE
UniProt ID: P54725
Variant: T -> M at position 200-200
Variant annotation: in dbSNP:rs4987202
Protein function: (Microbial infection) Involved in Vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome.
Reference sequence:
MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE
UniProt ID: P54727
Variant: A -> V at position 249-249
Variant annotation: in dbSNP:rs1805329
Protein function: The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.
Reference sequence:
MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILNDDTALKEYKIDEKNFVVVMVTKPKAVSTPAPATTQQSAPASTTAVTSSTTTTVAQAPTPVPALAPTSTPASITPASATASSEPAPASAAKQEKPAEKPAETPVATSPTATDSTSGDSSRSNLFEDATSALVTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPQAASTGAPQSSAVAAAAATTTATTTTTSSGGHPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGGQGGGGGGGSGGIAEAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQNFDED
UniProt ID: P54753
Variant: R -> L at position 168-168
Variant annotation: in a lung small cell carcinoma sample; somatic mutation
Protein function: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance also plays an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt.
Reference sequence:
MARARPPPPPSPPPGLLPLLPPLLLLPLLLLPAGCRALEETLMDTKWVTSELAWTSHPESGWEEVSGYDEAMNPIRTYQVCNVRESSQNNWLRTGFIWRRDVQRVYVELKFTVRDCNSIPNIPGSCKETFNLFYYEADSDVASASSPFWMENPYVKVDTIAPDESFSRLDAGRVNTKVRSFGPLSKAGFYLAFQDQGACMSLISVRAFYKKCASTTAGFALFPETLTGAEPTSLVIAPGTCIPNAVEVSVPLKLYCNGDGEWMVPVGACTCATGHEPAAKESQCRPCPPGSYKAKQGEGPCLPCPPNSRTTSPAASICTCHNNFYRADSDSADSACTTVPSPPRGVISNVNETSLILEWSEPRDLGGRDDLLYNVICKKCHGAGGASACSRCDDNVEFVPRQLGLTERRVHISHLLAHTRYTFEVQAVNGVSGKSPLPPRYAAVNITTNQAAPSEVPTLRLHSSSGSSLTLSWAPPERPNGVILDYEMKYFEKSEGIASTVTSQMNSVQLDGLRPDARYVVQVRARTVAGYGQYSRPAEFETTSERGSGAQQLQEQLPLIVGSATAGLVFVVAVVVIAIVCLRKQRHGSDSEYTEKLQQYIAPGMKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLKQPGRREVFVAIKTLKVGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMILTEFMENCALDSFLRLNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDPSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAVEQDYRLPPPMDCPTALHQLMLDCWVRDRNLRPKFSQIVNTLDKLIRNAASLKVIASAQSGMSQPLLDRTVPDYTTFTTVGDWLDAIKMGRYKESFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRLQMNQTLPVQV
UniProt ID: P54753
Variant: R -> C at position 440-440
Variant annotation: in dbSNP:rs56029711
Protein function: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance also plays an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt.
Reference sequence:
MARARPPPPPSPPPGLLPLLPPLLLLPLLLLPAGCRALEETLMDTKWVTSELAWTSHPESGWEEVSGYDEAMNPIRTYQVCNVRESSQNNWLRTGFIWRRDVQRVYVELKFTVRDCNSIPNIPGSCKETFNLFYYEADSDVASASSPFWMENPYVKVDTIAPDESFSRLDAGRVNTKVRSFGPLSKAGFYLAFQDQGACMSLISVRAFYKKCASTTAGFALFPETLTGAEPTSLVIAPGTCIPNAVEVSVPLKLYCNGDGEWMVPVGACTCATGHEPAAKESQCRPCPPGSYKAKQGEGPCLPCPPNSRTTSPAASICTCHNNFYRADSDSADSACTTVPSPPRGVISNVNETSLILEWSEPRDLGGRDDLLYNVICKKCHGAGGASACSRCDDNVEFVPRQLGLTERRVHISHLLAHTRYTFEVQAVNGVSGKSPLPPRYAAVNITTNQAAPSEVPTLRLHSSSGSSLTLSWAPPERPNGVILDYEMKYFEKSEGIASTVTSQMNSVQLDGLRPDARYVVQVRARTVAGYGQYSRPAEFETTSERGSGAQQLQEQLPLIVGSATAGLVFVVAVVVIAIVCLRKQRHGSDSEYTEKLQQYIAPGMKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLKQPGRREVFVAIKTLKVGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMILTEFMENCALDSFLRLNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDPSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAVEQDYRLPPPMDCPTALHQLMLDCWVRDRNLRPKFSQIVNTLDKLIRNAASLKVIASAQSGMSQPLLDRTVPDYTTFTTVGDWLDAIKMGRYKESFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRLQMNQTLPVQV
UniProt ID: P54753
Variant: I -> V at position 579-579
Variant annotation: in dbSNP:rs56103851
Protein function: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance also plays an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt.
Reference sequence:
MARARPPPPPSPPPGLLPLLPPLLLLPLLLLPAGCRALEETLMDTKWVTSELAWTSHPESGWEEVSGYDEAMNPIRTYQVCNVRESSQNNWLRTGFIWRRDVQRVYVELKFTVRDCNSIPNIPGSCKETFNLFYYEADSDVASASSPFWMENPYVKVDTIAPDESFSRLDAGRVNTKVRSFGPLSKAGFYLAFQDQGACMSLISVRAFYKKCASTTAGFALFPETLTGAEPTSLVIAPGTCIPNAVEVSVPLKLYCNGDGEWMVPVGACTCATGHEPAAKESQCRPCPPGSYKAKQGEGPCLPCPPNSRTTSPAASICTCHNNFYRADSDSADSACTTVPSPPRGVISNVNETSLILEWSEPRDLGGRDDLLYNVICKKCHGAGGASACSRCDDNVEFVPRQLGLTERRVHISHLLAHTRYTFEVQAVNGVSGKSPLPPRYAAVNITTNQAAPSEVPTLRLHSSSGSSLTLSWAPPERPNGVILDYEMKYFEKSEGIASTVTSQMNSVQLDGLRPDARYVVQVRARTVAGYGQYSRPAEFETTSERGSGAQQLQEQLPLIVGSATAGLVFVVAVVVIAIVCLRKQRHGSDSEYTEKLQQYIAPGMKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLKQPGRREVFVAIKTLKVGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMILTEFMENCALDSFLRLNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDPSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAVEQDYRLPPPMDCPTALHQLMLDCWVRDRNLRPKFSQIVNTLDKLIRNAASLKVIASAQSGMSQPLLDRTVPDYTTFTTVGDWLDAIKMGRYKESFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRLQMNQTLPVQV