ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6FLR5 | MSPDPKYSAYLLDIEGTLCPLSFVKDTLYPFFVLHVQRIVYENFNEEHPKDEFIAEQLAKYDIKEEGQAGKNKLVEHLLDLVANDTKDSTLKALQGHVWEVGYNSGELEVPLYPDVIDFLVRNDGRGDDKVPVYIYSSGSIHAQKLLFGHVKNSGNSHAKIAGNWDLNRFIDGYFDINTAGKKTESNSYKKILDEIKMTDKPHDVLFLSDNAKELDAAKECGISVGLAMRAGNVTVPNAIDYKQYFQFTKL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 28315
Sequence Length: 251
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
Q2H683 | MAAAKKPRVVLLDIEGTVCPISFVKDVLFPYALSALPSTLAQEWDAPAFARYRAAFPAEHASTPSALAAHARDLMARDVKIGYLKALQGYLWEAGYASGALRAPLFEDVAPKVREWTSAAGEEGGVARVMIYSSGSVPAQKLLFRHTSGEPADLTDAITDYFDTVNAGPKTEPASYERIAAKYPEVPAGEWLFLSDNVREVEAAREAGMRACVVQRPGNAELPEDVRGRLEVVESFEEL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 25944
Sequence Length: 239
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
C4Y3W1 | MSIALLDIEGTVCPITFVKDCLFPYFSKQYPSYLRDVSFPIDKSDGGLADVLAGFPKEAVASIDQLKNHIDDLVARDVKDPVLKSFQGLVWKEGYAKGDLKAPVYEDAIAFINRSKSVYIYSSGSVGAQKLLFSHVDVNGASVDLTPKLKGYFDITTAGFKQEKDSYLKIAADIGCDPADVIFYSDNVLEVKAALEAGMASKVVVRPGNAELSESDKKSYECISSFTAE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 24923
Sequence Length: 229
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
B0WQG0 | MRYQQDTLFPYALKNVEEYLKANWNEDATKTVVAALREQADEDKKAEVEGALTIPAGDSEDIIPDIVKYVEWQTSRDAKTGSLKTLQGLVWAKGYKDGSIKGHVYDDVSKALEQWTEGGRKIYVYSSGSVDAQKMLFEHSEQGDLVKYLAGHYDTKIGAKTEKDSYEAILKNIEATAEEALFLTDVVAEAKAAKEAGLNVVVLERPGNAELSEDDRKEFTVVKSFADIPLESIVESANGAGAKRKIDEAQEEDEAQPPTKVVKKDENGDAAAKKDETAKVDEPAAKATNGDAAAKEEAAAPAEGKMEVDEAAAAAAPPADAAEEKKETEEAKPETEKVTEKTESTAAEKKEEDKKEEVAESKEAAPKEVVAEEAKKEEEVKAAAPAEEVKKVEEPVPAEAKKVVEEEKMEVDGGAEAVAEEKEAEKKEEDKAAEPAAEKKPAEEAVVTSTEEPAKEEPKVESSTAEAEPAKEKPAEAEAKAAPAETTKAEVVEKPAETPAAESMETDSEPSADKEAEAKPEAKPVEEVKKAEAEKKVEAEKKPAESEAEAKEVATKPVEETKGEETTTAGPVEEIAVEAKEDAAKPEEKKSDADEVSTTTTTTSTESKTENGTHENGVSKEATPVNGKEESRVPENGEAEPAAEAVVTSNGNGKHEEKGDSDKENDTATSNTTEEPAANGNGVENGSTTSSTTTPAPDAAAEIKSKKVIDSSTTPTPPIEAES | Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 77070
Sequence Length: 723
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
Q55FM6 | MTPNIHTVILDIEGTTTPISFVHDVLFPYIRDNLVRHINQKWGSEELKQDIKELYKLYLEDNKASELVVNNQFNTPEILNPDDESTDKEKLIESVIRNVIYQMDNDRKSTPLKQLQGHMWLEGYENELVKGVVFPEVPKAFENWNLNHIDIYIYSSGSIAAQKLLFNYSNFGSLLPYIKGHFDTTIGGKLHPSSYEKILSTINNGSPNSYLFVTDSILEAKAARESGLNVCLSIRDGNPPIVDRELLNTFDQVSSFDQLFNKFNFKN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Mass (Da): 30594
Sequence Length: 267
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Subcellular Location: Cytoplasm
EC: 3.1.3.77
|
O29133 | MIIEDVHYRVVFDSRGNETVECEVVAGEVVAKAMAPSGASTGSGEAVVVSPYRYEEIEEEVSKAIIGMSVFDQESVDEALRELDGTDNFSRIGGNFAITASLAVAKAAAEILGLPLYAYVGGVFAKELPYPLGNVIGGGRHAEGSTSIQEFLVIPVGAKTFFEAQRANAAVHKQLKKIFKERGIFAAKGDEGAWAAQISDEQAFEILSEAIQRVEDELGVKVRMGIDVAATELWDGERYVYSDRKLTTEEQIAYMAELADRYDLLYIEDPLHEKDFEGFAELTKQVKCMVCGDDIFVTNPEIIKKGIEVGAANTVLIKPNQNGTLSGTAKAVKIAKDNGYSVVVSHRSGETEDETLAHLAVAFNAKLIKTGVVGGERISKLNELIRIEELMDKPRMVMI | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 43420
Sequence Length: 399
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
|
Q96X30 | MPISKIHARSVYDSRGNPTVEVDVVTETGLHRAIVPSGASTGQHEAHELRDGDKTQWGGKGVLKAVKNVNETIGPALIKENIDVKDQSKVDEFLNKLDGTANKSNLGANAILGVSLAVAKAGAAEKGVPLYAHISDLAGTKKPYVLPVPFQNVLNGGSHAGGRLAFQEFMIVPDSAPSFSEALRQGAEVYQKLKALAKKKYGQSAGNVGDEGGVAPDIQTAEEALDLITEAIEQAGYTGKIKIAMDVASSEFYKADVKKYDLDFKNPESDPSKWLTYEQLADLYKSLAAKYPIVSIEDPFAEDDWEAWSYFYKTSDFQIVGDDLTVTNPGRIKKAIELKSCNALLLKVNQIGTLTESIQAAKDSYADNWGVMVSHRSGETEDVTIADIAVGLRSGQIKTGAPCRSERLAKLNQILRIEEELGENAVYAGSKFRTAVNL | Cofactor: Mg(2+) is required for catalysis and for stabilizing the dimer.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 47305
Sequence Length: 438
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
|
O02654 | MVIKKVHSRQIFDSRGNPTVEVDLWTDKGMFRAAVPSGASTGIYEALEMRDKDAKNYHGKTLFNAVGNVNKIIAPALVDKKMDEKDQTAVDNFLLALDGTENKNKLGANAILGVSLAVCKAGAAAKGVPLYRHIADLAGNKEVILPVPAFNVINGGSHAGNKLAMQEFMILPTGAKNFTEAMKMGTEVYHHLKSVIKKKYGQDACNVGDEGGFAPNILDNKEGLELLKTAIANAGYTAEIEIGMDVAASEFCKEKKYDLDFKNPDSNPNDWLTSDQLADVYKDFVKNYPVVSIEDPFDQDDWEAYTKMTKDMDIQIVGDDLLVTNPKRVQKGIDLKAANALLLKVNQIGSVTESIQACKMSQDAGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQILRIEEELGDKAVFAGKKFRNPLK | Cofactor: Mg(2+) is required for catalysis and for stabilizing the dimer.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 47426
Sequence Length: 434
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
|
P15007 | MSWTASVFLRTSTTSMKFLRLRWPLPRIPQNKSANVAPRFRSKSAVSQLSSGFKFVQIRKSTCDSNEMTIKAIKARQIYDSRGNPTVEVDLTTELGLFRAAVPSGASTGVHEALELRDNDKANYHGKSVLKAVGHVNDTLGPELIKANLDVVDQASIDNFMIKLDGTENKSKFGANAILGVSLAVAKAGAAKKGVPLYKHIADLAGNKEIILPVPAFNVINGGSHAGNKLAMQEFMILPTGATSFTEAMKMGSEVYHHLKNVIKAKFGLDATAVGDEGGFAPNIQSNKEALNLISDAIAKAGYTGKIEIGMDVAASEFYKDGQYDLDFKNEKSDKSQWLPADKLANLYQEFIKDFPIVSIEDPFDQDHWEAWSNLTGCTDIQIVGDDLTVTNPKRIATAVEKKACNCLLLKVNQIGTVTESIAAHLLAKKNGWGTMVSHRSGETEDSFIGDLVVGLSTGQIKTGAPCRSERLAKYNQILRIEEEIGAGVKFAGKSFRKPQ | Cofactor: Mg(2+) is required for catalysis and for stabilizing the dimer.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 54310
Sequence Length: 500
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
|
Q9CD42 | MPVIEQVGAREILDSRGNPTVEVEVVLIDGTFARAAVPSGASTGEYEAVELRDGDGRYGGKGVKRAVDAVLDEIGPVVIGLNANDQRLIDQELLDLDGTPDKSRLGGNAILGVSLAVAKAAADSAELPLFRYIGGSNAHILPVPMMNILNGGAHADTAVDVQEFMVAPIGAPSFVEALRWGAEVYHALKSVLKKKGLSTGLGDEGGFAPEVAGTTAALDLVTLAIEAAGFKPGADVALALDAAATEFYTDGIGYHFEGMTHTADQMTEFYADLLGSYPLVSIEDPLSEDDWDGWAALTASIGEQVQIVGDDIFATNPERLEEGIGRGVANALLVKVNQIGTLTETLEAVALAHHSGYRTMISHRSGETEDTMIADLVVALGSGQIKTGAPARSERVAKYNQLLRIEEELGDAARYAGDLAFLRYVVETR | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 45202
Sequence Length: 429
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
|
P75189 | MSAQTGTDLFKIADLFAYQVFDSRGFPTVACVVKLASGHTGEAMVPSGASTGEKEAIELRDGDPKAYFGKGVSQAVQNVNQTIAPKLIGLNATDQAAIDALMIQLDGTPNKAKLGANAILAVSLAVAKAAASAQKTSLFKYLANQVMGLNKTEFILTVPMLNVINGGAHADNNIDFQEFMIMPLGANSMHQALKMASETFHALQKLLKQRGLNTNKGDEGGFAPNLKLAEEALDLMVEAIKAAGYQPGSDIAIALDVAASEFYDDTTKRYVFKKGIKAKILDEKEWSLTTAQMIAYLKKLTEQYPIISIEDGLSEHDWEGMETLTKTLGQHIQIVGDDLYCTNPAIAEKGVAHKATNSILIKLNQIGTLTETIKAINIAKDANWSQVISHRSGETEDTTIADLAVAACTGQIKTGSMSRSERIAKYNRLLQIELELGNNAKYLGWNTFKNIKPQKA | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 49228
Sequence Length: 456
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
|
Q98Q50 | MSEIVKIKALEVLDSRGNPTIQVEVHTISGAYGKALVPSGASTGSREALELRDESTKYKDNWYASKGVQKAVDNVNNKIADLLIGQNVLDQRNIDNIMIEADGTENKSKFGANAILGVSLAAAHAGANFLQIPLYRYIGGINANMLPLPMLNVINGGEHASNTIDFQEFMIMPMGAKTFKESLQMANKVFHNLAKLLKKAGHGTQVGDEGGFAPNLKNHEEVLDFLMQAIEVAGFVASTSKEKGIAIAIDAASSELYDQSTGKYTFKKLKQAIKTKQPGFENVEKTKLDFTSDELIAYYGELISKYPIISIEDGFAESDWQGFAKFTKIYGEKLQIVGDDLTVTNSKILERAIKEKSMNSILVKLNQIGSLSETLDTINMAHKAGFSAVISHRSGETEDTTIADLAVALNTGQIKTGSLSRTDRIAKYNRLLEIEDQLEEAAVFPGKKAFWNLKNR | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 49878
Sequence Length: 456
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytoplasm
EC: 4.2.1.11
|
Q566N0 | MQISAYLCALIACCGLTLSAPTANNKSSSEAPPLLLVSFDGFRADYLNKYSFPNLEKFFSDGVLVHELTNVFTTKTFPNHYSLVTGLYAESHGMLASIMYDPVAKKHFSIKNDSDPFWWDEATPIWVSVEESGYHAASAMWPGSDVNIQNHTLKYTFKYDSRVSFKERLGNITQWMTTDKSLKFASLYWEEPDFSGHTYGPDNTTEMARVLKEVDGHVGYLMEELDRMELWGKINVIITSDHGMAQCSEERIIRLDDCVSPSSYTLVDLTPVAAIIPLEDKTTVYNNLSSCHVHLKAYMKNDVPDRLHYKNNERIQPIILVADEGWTIVKNGRLPRLGDHGYDNTLPSMHPFLAAHGPAFRKGYKMSSFNSVDLYPLMCHLIGIPPKANNGSFAHVRCTLVNEQCGELALAVGLVMGVLIILTTFTCLFKLMKNRNVSSPRPFARLELDDDGDDEPLLE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to induce proliferation of vascular smooth muscle cells. Acts as a procoagulant, mediating platelet aggregation at the site of nascent thrombus via release of ADP from Ap3A and activation of ADP receptors (By similarity).
Catalytic Activity: H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2 H(+)
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 51603
Sequence Length: 459
Subcellular Location: Cell membrane
EC: 3.6.1.29
|
Q9Y6X5 | MKLLVILLFSGLITGFRSDSSSSLPPKLLLVSFDGFRADYLKNYEFPHLQNFIKEGVLVEHVKNVFITKTFPNHYSIVTGLYEESHGIVANSMYDAVTKKHFSDSNDKDPFWWNEAVPIWVTNQLQENRSSAAAMWPGTDVPIHDTISSYFMNYNSSVSFEERLNNITMWLNNSNPPVTFATLYWEEPDASGHKYGPEDKENMSRVLKKIDDLIGDLVQRLKMLGLWENLNVIITSDHGMTQCSQDRLINLDSCIDHSYYTLIDLSPVAAILPKINRTEVYNKLKNCSPHMNVYLKEDIPNRFYYQHNDRIQPIILVADEGWTIVLNESSQKLGDHGYDNSLPSMHPFLAAHGPAFHKGYKHSTINIVDIYPMMCHILGLKPHPNNGTFGHTKCLLVDQWCINLPEAIAIVIGSLLVLTMLTCLIIIMQNRLSVPRPFSRLQLQEDDDDPLIG | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to induce proliferation of vascular smooth muscle cells. Acts as a procoagulant, mediating platelet aggregation at the site of nascent thrombus via release of ADP from Ap3A and activation of ADP receptors.
Catalytic Activity: H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2 H(+)
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 51641
Sequence Length: 453
Subcellular Location: Cell membrane
EC: 3.6.1.29
|
Q9EQG7 | MIPEFLLASCTLATLCHSAPFSLQPEEQKVLVVSFDGFRWDYLYKVPTPHFHYIMKNGVHVNQVTNVFITKTYPNHYTLVTGLFAENHGIVANDMFDPILNKSFSLEHMDIYDSKFWEEATPIWITNQRAGHASGAAMWPGADVKIHDSFPTYYLPYNESVSFEDRVAKIIEWFTAKDPINLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKLWNNVNLIVTSDHGMTQCSKQRVIELDRYLDKEHYTLIDHSPVAAILPKEGKFDEVYDALAGAHPNLTVYKKEEIPERWHYKHNDRVQPIVAVADEGWYILQNKSDDFLLGNHGYDNALAEMHPIFLAHGPAFRKNFTKEAMNSTDLYSLLCHLLNLTALPHNGSFWNVQDLLSSATPKPIPYTQSTTLLLGSDKPGEDEQEESYPYYIGVSLGSIIAMVFFVVLIKHLIRSQVHTLQYRQVEVAQPLLQA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Can hydrolyze NAD but cannot hydrolyze nucleotide di- and triphosphates . Lacks lysopholipase D activity. May play a role in neuronal cell communication (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54387
Sequence Length: 477
Subcellular Location: Secreted
EC: 3.1.-.-
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F1N5C8 | MAGKLGVLLLALVLSLAQPASARRKLLVFLLDGFRADYISDEALESLPGFKEIVSRGVKVDYLTPDFPTLSYPNYYSLMTGRHCEVHQMTGNYMWDPDTNKSFDLGINRDSRLPLWWNGSEPLWVTLTKAKRKVYMYYWPGCEVEILGVRPTYCLEYKSVPTDINFVNAVSGALDVFKSGQADLAAIYYERVDVEGHHYGPSSPQRKDAVKAVDTVMAYMTKWIQERDLQDDLNVIIFSDHGMTDISWTDKVIKLDNYINLRDLQQLKGRGPVVSLWPAPGKHSEIYNKVRRVEHMTVYAKEDIPSRFYYKKGKFVSPLTLVADEGWFITENRESLPFWMNSTVTRKPEGWQWGWHGYDNELRAMRGIFLAFGPDFKSDFRAAPIRVVDIYNLMCKVTGVTPLPNNGSWSRVMCMLKDPASSAPGAPPCACALVTVLLVLLAILA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells . Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. In vitro, hydrolyzes only choline-containing lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet-activating factor (PAF) and lysoPAF, but not other lysophospholipids (By similarity).
Catalytic Activity: H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + phosphocholine
Location Topology: Lipid-anchor
Sequence Mass (Da): 50495
Sequence Length: 445
Subcellular Location: Cell membrane
EC: 3.1.4.-
|
Q5BKW7 | MTRTLLKIYTLFILLLCRQRDANRKLLVFLIDGFRHDYMDDLHNLPGFREIVENGVKVDYLTPDFPSLSYPNYYSLMTGRHCEVHQMTGNYMWDTDTQKEFLIGTNPDSRLPMWWDGSEPLWVTMQKLGKKVYMYYWPGCEVTILGVRPTFCEEYVYNPSEKNLTDSMENALNALKSSKADMAGIYYEKIDVEGHHFGPRSPEIQRAIRSLDQAFQILNQKIREKNMRDTINVVLFSDHGMTQLKWMEKIIELDNYINMSHIIKMMDRGPVVSLWPKQDKFEEIYQNLSTADNMNVYKKHEIPDRFHYKNGQFVSTLTLVAEPGWFITENKAKLPFWNNGTEAAGGWQHGWHGYDNEFVDMRGSFLAQGPDFKSNYRAGPIRTVDVYNVLCKTLGMNPLPNNGSWSRVECMMRSSAATAGASLISCCFLLLLTLTGVC | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells. Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. In vitro, hydrolyzes only choline-containing lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet-activating factor (PAF) and lysoPAF, but not other lysophospholipids.
Catalytic Activity: H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + phosphocholine
Location Topology: Lipid-anchor
Sequence Mass (Da): 50694
Sequence Length: 438
Subcellular Location: Cell membrane
EC: 3.1.4.-
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Q6UWR7 | MAVKLGTLLLALALGLAQPASARRKLLVFLLDGFRSDYISDEALESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPTTNKSFDIGVNKDSLMPLWWNGSEPLWVTLTKAKRKVYMYYWPGCEVEILGVRPTYCLEYKNVPTDINFANAVSDALDSFKSGRADLAAIYHERIDVEGHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTDIFWMDKVIELNKYISLNDLQQVKDRGPVVSLWPAPGKHSEIYNKLSTVEHMTVYEKEAIPSRFYYKKGKFVSPLTLVADEGWFITENREMLPFWMNSTGRREGWQRGWHGYDNELMDMRGIFLAFGPDFKSNFRAAPIRSVDVYNVMCNVVGITPLPNNGSWSRVMCMLKGRASTAPPVWPSHCALALILLFLLA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells . Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. In vitro, hydrolyzes only choline-containing lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet-activating factor (PAF) and lysoPAF, but not other lysophospholipids (By similarity).
Catalytic Activity: H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + phosphocholine
Location Topology: Lipid-anchor
Sequence Mass (Da): 50241
Sequence Length: 440
Subcellular Location: Cell membrane
EC: 3.1.4.-
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Q8BGN3 | MAAKLWTFLLGFGLSWVWPASAHRKLLVLLLDGFRSDYISEDALASLPGFREIVNRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPRTNKSFDIGVNRDSLMPLWWNGSEPLWITLMKARRKVYMYYWPGCEVEILGVRPTYCLEYKTVPTDINFANAVSDALDSLKSGRADLAAIYHERIDVEGHHYGPSSPQRKDALRAVDTVLKYMIQWIQDRGLQQDLNVILFSDHGMTDIFWMDKVIELSNYISLDDLQQVKDRGPVVSLWPVPGKHSEIYHKLRTVEHMTVYEKESIPNRFYYKKGKFVSPLTLVADEGWFIAESREMLPFWMNSTGKREGWQRGWHGYDNELMDMRGIFLAIGPDFKSNFRAAPIRSVDVYNIMCHVAGITPLPNNGSWSRVVCMLKGQTSSAPPTPLNSCALVLILLLYFV | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells . Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids . In vitro, hydrolyzes only choline-containing lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet-activating factor (PAF) and lysoPAF, but not other lysophospholipids .
Catalytic Activity: H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + phosphocholine
Location Topology: Lipid-anchor
Sequence Mass (Da): 50618
Sequence Length: 440
Subcellular Location: Cell membrane
EC: 3.1.4.-
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Q6DDP3 | MAKYSTLSLILLTLSLLPPSSARPKLLLFLIDGFRFDYISDGELQHLPGFRHMVERGVKVDYMTPAFPSLSYPNYYTLMTGRHCETHHMTGNFMWDPKKNISFDIGANEDSRLPQWWDGAEPLWVTMEKAKRKVSMYYWPGCEVEIRAIKPNYCREYFYYPSEAEFGKSVTDALQSLTRGNAEMAAVYYERIDVEGHHHGPWSEERKNVTRELDQILWHLHQQIREMGLESELNVILFSDHGMTDVFWMDKVIELKNYIDMQDIIQMKDRGPVVSLWPAEGKLSKVYEELRAVQHMNVYQKEDIPERFHYKKGTFVSPLTLVAELGWFIIERKEKLPFWNNGTSINIAWQHGWHGYDNELMDMRGVFLAYGPDFKVNFRSAPIRSTDVYNIMCNVLGIEPLPNNGSWSRVQFMLRSSSGFPTTLHLINLWLSVLPLSLILF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Choline-specific glycerophosphodiester phosphodiesterase. Has a lysophospholipase C activity (By similarity).
Catalytic Activity: H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) + phosphocholine
Location Topology: Lipid-anchor
Sequence Mass (Da): 51486
Sequence Length: 441
Subcellular Location: Cell membrane
EC: 3.1.4.-
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Q6UWV6 | MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA | Function: Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract . Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation . Does not have nucleotide pyrophosphatase activity . May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen (By similarity).
PTM: N-glycosylated; required for activity and transport to the plasma membrane.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine
Sequence Mass (Da): 51478
Sequence Length: 458
Subcellular Location: Cell membrane
EC: 3.1.4.12
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Q03137 | MAGIFYFILFSFLFGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEASQNNWLRTDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRESQFGKIDTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEEQNGECQACKIGYYKALSTDASCAKCPPHSYSVWEGATSCTCDRGFFRADNDAASMPCTRPPSAPLNLISNVNETSVNLEWSSPQNTGGRQDISYNVVCKKCGAGDPSKCRPCGSGVHYTPQQNGLKTTRVSITDLLAHTNYTFEIWAVNGVSKYNPSPDQSVSVTVTTNQAAPSSIALVQAKEVTRYSVALAWLEPDRPNGVILEYEVKYYEKDQNERSYRIVRTAARNTDIKGLNPLTSYVFHVRARTAAGYGDFSEPLEVTTNTVPSRIIGDGANSTVLLVSVSGSVVLVVILIAAFVISRRRSKYSKAKQEADEEKHLNQGVRTYVDPFTYEDPNQAVREFAKEIDASCIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRPKFGQIVNMLDKLIRNPNSLKRTGSESSRPNTALLDPSSPEFSAVVSVGDWLQAIKMDRYKDNFTAAGYTTLEAVVHMSQDDLARIGITAITHQNKILSSVQAMRTQMQQMHGRMVPV | Function: Receptor tyrosine kinase which binds membrane-bound ephrin 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. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity . Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections . May also control the segregation of motor and sensory axons during neuromuscular circuit developmen . In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis . In the nervous system, also plays a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation . Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium . During development of the cochlear organ of Corti, regulates pillar cell separation by forming a ternary complex with ADAM10 and CADH1 which facilitates the cleavage of CADH1 by ADAM10 and disruption of adherens junctions . Phosphorylates CAPRIN1, promoting CAPRIN1-dependent formation of a membraneless compartment .
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 109814
Sequence Length: 986
Domain: The protein kinase domain mediates interaction with NGEF.
Subcellular Location: Cell membrane
EC: 2.7.10.1
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P54755 | MGLRGGGGRAGGPAPGWTCLLLCAALRSLLASPGSEVNLLDSRTVMGDLGWIAYPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGRPASSFELKFTLRDCNSLPGGLGTCKETFNMYYFESDDEDGRNIRENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLTKKGFYLAFQDVGACIALVSVRVYYKKCPSVIRNLARFPDTITGADSSQLLEVSGVCVNHSVTDEAPKMHCSAEGEWLVPIGKCLCKAGYEEKNNTCQVCRPGFFKASPHSPSCSKCPPHSYTLDEASTSCLCEEHYFRRESDPPTMACTRPPSAPRSAISNVNETSVFLEWIPPADTGGRKDVSYYIACKKCNSHSGLCEACGSHVRYLPQQTGLKNTSVMMVDLLAHTNYTFEIEAVNGVSDQNPGARQFVSVNVTTNQAAPSPVSSVKKGKITKNSISLSWQEPDRPNGIILEYEIKYFEKDQETSYTIIKSKETAITADGLKPGSAYVFQIRARTAAGYGGFSRRFEFETSPVLAASSDQSQIPIIVVSVTVGVILLAVVIGFLLSGSCCDHGCGWASSLRAVAYPSLIWRCGYSKAKQDPEEEKMHFHNGHIKLPGVRTYIDPHTYEDPNQAVHEFAKEIEASCITIERVIGAGEFGEVCSGRLKLQGKREFPVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIHLEGVVTKSKPVMIVTEYMENGSLDTFLKKNDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVMSYGERPYWEMTNQDVIKAVEEGYRLPSPMDCPAALYQLMLDCWQKDRNSRPKFDEIVSMLDKLIRNPSSLKTLVNASSRVSNLLVEHSPVGSGAYRSVGEWLEAIKMGRYTEIFMENGYSSMDSVAQVTLEDLRRLGVTLVGHQKKIMNSLQEMKVQLVNGMVPL | Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A 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. Among GPI-anchored ephrin-A ligands, EFNA5 most probably constitutes the cognate/functional ligand for EPHA5. Functions as an axon guidance molecule during development and may be involved in the development of the retinotectal, entorhino-hippocampal and hippocamposeptal pathways. Together with EFNA5 plays also a role in synaptic plasticity in adult brain through regulation of synaptogenesis (By similarity).
PTM: Phosphorylated. Phosphorylation is stimulated by the ligand EFNA5 (By similarity).
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 112246
Sequence Length: 1013
Subcellular Location: Cell membrane
EC: 2.7.10.1
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Q60629 | MRGSGPRGAGHRRTQGRGGGDDTPRVPASLAGCYSAPLKGPLWTCLLLCAALRTLLASPSNEVNLLDSRTVMGDLGWIAFPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNSLPGGLGTCKETFNMYYFESDDENGRSIKENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLSKKGFYLAFQDVGACIALVSVRVYYKKCPSVVRHLAIFPDTITGADSSQLLEVSGSCVNHSVTDDPPKMHCSAEGEWLVPIGKCMCKAGYEEKNGTCQAPSPVTNVKKGKIAKNSISLSWQEPDRPNGIILEYEIKYFEKDQETSYTIIKSKETSITAEGLKPASVYVFQIRARTAAGYGVFSRRFEFETTPVSVAASNDQSQIPIIAVSVTVGVILLAVMIGFLLSGSCCDCGCGRASSLCAVAHPSLIWRCGYSKAKQDPEEEKMHFHNGHIKLPGVRTYIDPHTYEDPNQAVHEFAKEIEASCITIERVIGAGEFGEVCSGRLKLPGKRELPVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIHLEGVVTKSKPVMIVTEYMENGSLDTFLKKNDGQFTVIQLVGMLRGIAAGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAFRKFTSSSDVWSYGIVMWEVVSYGERPYWEMTNQDVIKAVEEGYRLPSPMDCPAALYQLMLDCWQKDRNSRPKFDEIVNMLDKLIRNPSSLKTLVNASSRVSTLLAEHGSLGSGAYRSVGEWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMSSLQEMKVQMVNGMVPV | Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A 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. Among GPI-anchored ephrin-A ligands, EFNA5 most probably constitutes the cognate/functional ligand for EPHA5. Functions as an axon guidance molecule during development and may be involved in the development of the retinotectal, entorhino-hippocampal and hippocamposeptal pathways. Together with EFNA5 plays also a role in synaptic plasticity in adult brain through regulation of synaptogenesis. In addition to its function in the nervous system, the interaction of EPHA5 with EFNA5 mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion.
PTM: Phosphorylated. Phosphorylation is stimulated by the ligand EFNA5. Dephosphorylation upon stimulation by glucose, inhibits EPHA5 forward signaling and results in insulin secretion.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 97056
Sequence Length: 876
Subcellular Location: Cell membrane
EC: 2.7.10.1
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Q61772 | MVVQTRFPSWIILCYIWLLGFAHTGEAQAAKEVLLLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCWSIVENLAVFPDTVTGSEFSSLVEVRGTCVSSAEEEAENSPRMHCSAEGEWLVPIGKCICKAGYQQKGDTCEPCGRRFYKSSSQDLQCSRCPTHSFSDREGSSRCECEDGYYRAPSDPPYVACTRPPSAPQNLIFNINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNIGYMPQQTGLEDNYVTVMDLLAHANYTFEVEAVNGVSDLSRSQRLFAAVSITTGQAAPSQVSGVMKERVLQRSVQLSWQEPEHPNGVITEYEIKYYEKDQRERTYSTLKTKSTSASINNLKPGTVYVFQIRAVTAAGYGNYSPRLDVATLEEASGKMFEATAVSSEQNPVIIIAVVAVAGTIILVFMVFGFIIGRRHCGYSKADQEGDEELYFHFKFPGTKTYIDPETYEDPNRAVHQFAKELDASCIKIERVIGAGEFGEVCSGRLKLPGKRDVAVAIKTLKVGYTEKQRRDFLCEASIMGQFDHPNVVHLEGVVTRGKPVMIVIEFMENGALDAFLRKHDGQFTVIQLVGMLRGIAAGMRYLADMGYVHRDLAARNILVNSNLVCKVSDFGLSRVIEDDPEAVYTTTGGKIPVRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPAPMDCPAGLHQLMLDCWQKDRAERPKFEQIVGILDKMIRNPSSLKTPLGTCSRPLSPLLDQSTPDFTAFCSVGEWLQAIKMERYKDNFTAAGYNSLESVARMTIDDVMSLGITLVGHQKKIMSSIQTMRAQMLHLHGTGIQV | Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A 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. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 and MAPK3 which are phosphorylated upon activation of EPHA7. Isoform 4 which lacks the kinase domain may regulate isoform 1 adhesive properties.
PTM: Phosphorylated. Isoform 4 inhibits isoform 1 phosphorylation and may regulate its function in adhesion.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 111860
Sequence Length: 998
Subcellular Location: Cell membrane
EC: 2.7.10.1
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O09127 | MAPARARLSPALWVVTAAAAATCVSAGRGEVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNSIPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGACLAILSLRIYYKKCPAMVRNLAAFSEAVTGADSSSLVEVRGQCVRHSEERDTPKMYCSAEGEWLVPIGKCVCSAGYEERRDACMACELGFYKSAPGDQLCARCPPHSHSATPAAQTCRCDLSYYRAALDPPSAACTRPPSAPVNLISSVNGTSVTLEWAPPLDPGGRSDITYNAVCRRCPWALSHCEACGSGTRFVPQQTSLAQASLLVANLLAHMNYSFWIEAVNGVSNLSPEPRSAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKDKEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSAGCGRFSQAMEVETGKPRPRYDTRTIVWICLTLITGLVVLLLLLICKKRHCGYSKAFQDSDEEKMHYQNGQAPPPVFLPLNHPPGKFPETQFSAEPHTYEEPGRAGRSFTREIEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHSPESLRATATVSRCPPPAFARSCFDLRAGGSGNGDLTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLSSTQGPRRHL | Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A 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. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system also plays a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth.
PTM: Phosphorylated. Phosphorylation is stimulated upon binding of its ligands including EFNA2, EFNA3 and EFNA5. Autophosphorylation on Tyr-615 is critical for association with FYN. Autophosphorylation on Tyr-838 modulates tyrosine kinase activity.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 110705
Sequence Length: 1004
Subcellular Location: Cell membrane
EC: 2.7.10.1
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Q5JZY3 | METCAGPHPLRLFLCRMQLCLALLLGPWRPGTAEEVILLDSKASQAELGWTALPSNGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSSIPGAAGTCKETFNVYYLETEADLGRGRPRLGGSRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRRGFHLAFQDVGACVALVSVRVYYKQCRATVRGLATFPATAAESAFSTLVEVAGTCVAHSEGEPGSPPRMHCGADGEWLVPVGRCSCSAGFQERGDFCEACPPGFYKVSPRRPLCSPCPEHSRALENASTFCVCQDSYARSPTDPPSASCTRPPSAPRDLQYSLSRSPLVLRLRWLPPADSGGRSDVTYSLLCLRCGREGPAGACEPCGPRVAFLPRQAGLRERAATLLHLRPGARYTVRVAALNGVSGPAAAAGTTYAQVTVSTGPGAPWEEDEIRRDRVEPQSVSLSWREPIPAGAPGANDTEYEIRYYEKGQSEQTYSMVKTGAPTVTVTNLKPATRYVFQIRAASPGPSWEAQSFNPSIEVQTLGEAASGSRDQSPAIVVTVVTISALLVLGSVMSVLAIWRRPCSYGKGGGDAHDEEELYFHFKVPTRRTFLDPQSCGDLLQAVHLFAKELDAKSVTLERSLGGGRFGELCCGCLQLPGRQELLVAVHMLRDSASDSQRLGFLAEALTLGQFDHSHIVRLEGVVTRGSTLMIVTEYMSHGALDGFLRRHEGQLVAGQLMGLLPGLASAMKYLSEMGYVHRGLAARHVLVSSDLVCKISGFGRGPRDRSEAVYTTMSGRSPALWAAPETLQFGHFSSASDVWSFGIIMWEVMAFGERPYWDMSGQDVIKAVEDGFRLPPPRNCPNLLHRLMLDCWQKDPGERPRFSQIHSILSKMVQDPEPPKCALTTCPRPPTPLADRAFSTFPSFGSVGAWLEALDLCRYKDSFAAAGYGSLEAVAEMTAQDLVSLGISLAEHREALLSGISALQARVLQLQGQGVQV | Function: Receptor for members of the ephrin-A family. Binds to EFNA3, EFNA4 and EFNA5.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 109716
Sequence Length: 1008
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cell membrane
EC: 2.7.10.1
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I6YGS0 | MGAPTERLVDTNGVRLRVVEAGEPGAPVVILAHGFPELAYSWRHQIPALADAGYHVLAPDQRGYGGSSRPEAIEAYDIHRLTADLVGLLDDVGAERAVWVGHDWGAVVVWNAPLLHADRVAAVAALSVPALPRAQVPPTQAFRSRFGENFFYILYFQEPGIADAELNGDPARTMRRMIGGLRPPGDQSAAMRMLAPGPDGFIDRLPEPAGLPAWISQEELDHYIGEFTRTGFTGGLNWYRNFDRNWETTADLAGKTISVPSLFIAGTADPVLTFTRTDRAAEVISGPYREVLIDGAGHWLQQERPGEVTAALLEFLTGLELR | Function: Could be involved in detoxification of extraneous host-cell epoxides. Catalyzes the hydrolysis of epoxide-containing substrates.
Catalytic Activity: an epoxide + H2O = an ethanediol
Sequence Mass (Da): 35097
Sequence Length: 322
EC: 3.3.2.10
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P54762 | MALDYLLLLLLASAVAAMEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKPGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPAEASPICTCRTGYYRADFDPPEVACTSVPSGPRNVISIVNETSIILEWHPPRETGGRDDVTYNIICKKCRADRRSCSRCDDNVEFVPRQLGLTECRVSISSLWAHTPYTFDIQAINGVSSKSPFPPQHVSVNITTNQAAPSTVPIMHQVSATMRSITLSWPQPEQPNGIILDYEIRYYEKEHNEFNSSMARSQTNTARIDGLRPGMVYVVQVRARTVAGYGKFSGKMCFQTLTDDDYKSELREQLPLIAGSAAAGVVFVVSLVAISIVCSRKRAYSKEAVYSDKLQHYSTGRGSPGMKIYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVYKGRLKLPGKREIYVAIKTLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLAEMNYVHRDLAARNILVNSNLVCKVSDFGLSRYLQDDTSDPTYTSSLGGKIPVRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPMDCPAALHQLMLDCWQKDRNSRPRFAEIVNTLDKMIRNPASLKTVATITAVPSQPLLDRSIPDFTAFTTVDDWLSAIKMVQYRDSFLTAGFTSLQLVTQMTSEDLLRIGITLAGHQKKILNSIHSMRVQISQSPTAMA | 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. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. 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 synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation (By similarity).
PTM: Phosphorylated. Autophosphorylation is stimulated by the ligand EFNB1. Required for interaction with SH2 domain-containing interactors, for activation of the MAPK/ERK and JUN signaling cascades and for ubiquitination by CBL.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 109885
Sequence Length: 984
Subcellular Location: Cell membrane
EC: 2.7.10.1
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B0XMC1 | MAIQTTTGLAARLVAKRATFPASRRNFSASRSALKEIQEAYILSGARTPTAKFNGSFVSVSAPELGAVAIKSAVSKSGVPVEKITDVYMGNVLQGAVGQAPARQASMFAGLSPTVESMTVNKVCASGLKAVALAAQNIQLGLAEAQVAGGMENMSRVPYYLPRSTQLPPFGEIKLQDGLIQDGLWDVYNQFHMGICAEKTAKKYEISREEQDQYAIQSYQRAQAAWKENKFAEEIAPVTVKGKKGETVVERDEGYENLRIDKMATLKPAFLRDGTGTVTAGNASTMNDGASALVLGSKAIAREFAQGNRALARIVSTADAAIDPVDFPVAPAKAVPIALERAGITKDQVAVWEFNEAFAAVIKANEKILGLQNARVNPLGGAISLGHALGSSGSRILVTLLHQLQPGEYGVAAICNGGGAATAMVVQKLDRVD | Function: Mitochondrial acetyl-CoA acetyltransferase that catalyzes both the formation and degradation of acetoacetyl-CoA . Has no overlapping function with erg10B and seems not to be involved in ergosterol biosynthesis . Plays an important role in growth, morphogenesis and maintaining mitochondrial function including the response to oxidative stresses .
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 45710
Sequence Length: 433
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Subcellular Location: Mitochondrion
EC: 2.3.1.9
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B0YA65 | MSSLPAVYIVSSARTPVGSFLGSLSSLTAPQLGAHAIKAALAKVDGLKPSDVQEVFFGNVISANVGQNPARQCALGAGLEESTICTTVNKVCASGLKAIILGAQTIMTGNADVVVAGGTESMSNAPHYLPNLRTGAKYGHQSLVDGIMKDGLTDAGKQELMGLQAEECAQDHGFSREQQDEYAIRTYEKAQAAQKAGLFDEEIAPIQLPGFRGKPDVTVTQDEEPKNLNPEKLRAIKPAFIPGSGTVTAPNSSPLNDGAAAVVLVSEAKLKELNLKPVAKILGWGDAAQQPSKFTTAPALAIPKALKHAGVGQDAIDAFEINEAFSVVALANMKLLGIPEEKVNLHGGAVAIGHPIGASGARILTTLLGVLKAKKGKLGCAGICNGGGGASALVVELL | Function: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (Probable). In this module, the cytosolic acetyl-CoA acetyltransferase erg10B catalyzes the formation of acetoacetyl-CoA . The hydroxymethylglutaryl-CoA synthases AFUA_8G07210 and AFUA_3G10660 then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA (Probable). The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2 . Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) .
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 40909
Sequence Length: 398
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.3.1.9
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I1RY81 | MANLPPVYIVSTARTPIGSFLGSLSSQTAVQLGSVAIKGAVERAGIKPEDVDEVFFGNVLSAGVGQGPARQCALGAGLPQTVIATTVNKVCASSLKAIILGAQNIMLGTSDIVVAGGTESMSNTPHYLPNLRNGAKYGDQTLVDGVLKDGLTDSFKKDHMGISAELCVDDHDLTREAQDEYAINSYKKAQAATEAGLFTEIVPVEIPGGRGKPAIKVERDDEVKNLNVDKLKAMRPAFKPDGTVTAPNAAPINDGAAAVVLVSEAKLKELNLKPVAKILGWGDAEREPERFTIAPALAIPKAIKHAGLTAEQVEYYEINEAFSAVALANMKILGLNPDQVNVYGGSVAIGHPLGCSGARIVTTLTSVLKERKAKIGAVGICNGGGGASAMVIENLQ | Function: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). ERG10B catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 (Probable).
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 41189
Sequence Length: 396
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.3.1.9
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Q4WXT8 | MSARPQNVGIKAIEVYFPSQCVDQAELEKFDGVSEGKYTIGLGQTKMSFCDDREDIYSIALTTCSSLLRKYNIDPKSIGRLEVGTETLLDKSKSVKSVLMQLFAPHGNTNIEGVDTVNACYGGTNAVFNSINWVESSAWDGRDAIVVCGDIALYAKGAARPTGGAGAVAMLIGPDAPIVFEPGLRGSYVTHAYDFFKPDLTSEYPVVDGHFSLKCYTEAVDACYKAYAAREKVLKAKVQNGTNGVENDETKTPLDRFDYVLFHAPTCKLVQKSYGRMLYNDYLANPSHPAFAEVPSELRDLDYEKSFTDKTVEKTFMGLTKKTFAERVRPGLDVATLCGNMYTATVYAGLASLLSNVTFDPSQPKRVALFSYGSGLASSMFSVKIVGDVSGMVEKLDLHKRLNARTVLPPQTYDEMCILREHAHLKKNFKPTGNPDTLFPGTYYLTEIDDMFRRKYEIKA | Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). Erg13A and erg13B condense acetyl-CoA with acetoacetyl-CoA to form hydroxymethylglutaryl-CoA (HMG-CoA) (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase erg10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13A and erg13B then condense acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hmg1 and hmg2. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (Probable).
Catalytic Activity: acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+)
Sequence Mass (Da): 50797
Sequence Length: 460
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
EC: 2.3.3.10
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Q4WKA5 | MAPRKDFEDKATVPIQPVPGKRGYEFGGPLGAFVFIFGLSTLIYCLTFLCNDVSGCPVPSLLNPSTLSLDKLKEEAGWPQEGLKAFFDVRVTVWVLSYYVLSLVLYVFLPGEVVEGTELACKGRLRYKFNALPSAILILGGLALGTYMHGADFVVWTFLWDNYVQIITANLIICVVLAIFVYARSFSIPAPGQPNPELRELAPGGHSGNALYDFFIGRELNPRVQLPIPFVDEASRTIDINVWCEMRPGLLGWIILNLSNIARQYRTYGYITNSIVLSTVFQTFYVLDALYMEPAVLTTMDVIMDGFGYMLSFGHLVWVPFIYNIQTRYLAVFPLELRLREILLILAVTGAGYAIFRGANNQKNRFRRDPSDPRMMHIKYIQTSSGSKLMISGWWGLARHINYLGDWLMSWSYSLPTGIAGYTIIESINSSGDMQKQAIQTPEVRGWGMIFTYFFLVYFGALLIHREGRDEEKCKSKYGTDWERYTSIVRSRIIPGIY | Function: Delta(14)-sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . Catalyzes the reduction of the C14=C15 double bond within 4,4,24-trimethyl ergosta-8,14,24(28)-trienolto produce 4,4-dimethylfecosterol . The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56389
Sequence Length: 498
Pathway: Steroid metabolism; ergosterol biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.3.1.-
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I1RR90 | MAVKPKQPPAQEQHGYEFFGPPGAFAISFFLPVLVYVFNFVCNDISGCPAPSLLQPKTFSLDALKQEVGWPHNGVAGLVSWNGTLAVIGYNVLSLILYRVLPAIEVEGTQLSSGGRLKYRFNTLYSSTFTLAVLAAGTIAQGAEFPVWTFMSENFIQILSANIIYSYLVSTFVYVRSFSVKHGNKENRELAAGGHSGNILYDWFIGRELNPRIEIPLIGEVDIKEFLELRPGMMGWIIMNCSWCAQQYRNYGFVTDSSILITAVQALYVFDSWWNEPAILTTMDITTDGFGMMLAFGDIVWVPYVYSLQTRYLSVHPVSLGPLGLAAMLGLIGLGFYIFRSANNEKNRFRTNPNDPRVSHLKYIQTKTGSKLLTTGWWGMSRHINYLGDWIQSWPYCLPTGLAGYQIMSAGANIEGAYVMHDGREVVQGEAQGWGMLITYFYILYFGILLIHRERRDDEKCHRKYGKDWEEYRKIVRSRIVPGLY | Function: Delta(14)-sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . Catalyzes the reduction of the C14=C15 double bond within 4,4,24-trimethyl ergosta-8,14,24(28)-trienolto produce 4,4-dimethylfecosterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase ERG1 and the lanosterol synthase ERG7. Then, the delta(24)-sterol C-methyltransferase ERG6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by CYP51A, CYP51B and CYP51C, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. CYP51B encodes the enzyme primarily responsible for sterol 14-alpha-demethylation, and plays an essential role in ascospore formation. CYP51A encodes an additional sterol 14-alpha-demethylase, induced on ergosterol depletion and responsible for the intrinsic variation in azole sensitivity. The third CYP51 isoform, CYP51C, does not encode a sterol 14-alpha-demethylase, but is required for full virulence on host wheat ears. The C-14 reductase ERG24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases ERG25, the sterol-4-alpha-carboxylate 3-dehydrogenase ERG26 and the 3-keto-steroid reductase ERG27, leads to the production of fecosterol via 4-methylfecosterol. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum. The C-8 sterol isomerase ERG2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturases ERG3A and ERG3BB then catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturases ERG5A and ERG5B further convert 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable).
Catalytic Activity: 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54819
Sequence Length: 485
Pathway: Steroid metabolism; ergosterol biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.3.1.70
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Q4WBI8 | MDSLNSSYPQSAMATYSDLLDLAAQQQPHLSGLERLWWAHYAYWDNNIVATATGIITFLAHEIIYFSRCLPWIIADSLPSIFLKYKIQDQKPPPSAAEQWACTKYILLIHFVVELPLIVLFHPMMELCGLSFTIPFPDLRTLTAQIIIFFLLEDTYHYWLHRAMHWGPLYRSIHRIHHQYAAPFGLTAEYASPWETLLLGLGTIGPPLLLALMDCNVHLVTVLAWVTLRQFQAIDSHSGYDFPWSLRRILPFWGGADWHDDHHRYFWGNYSSSFRHWDVLMGTVAGPEAREKRRAEREKRQA | Function: Sterol-C4-methyl oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . Erg25A is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4-dimethylfecosterol into fecosterol via 4-methylfecosterol . The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35109
Sequence Length: 302
Domain: The histidine box domains may contain the active site and/or be involved in metal ion binding.
Pathway: Steroid metabolism; ergosterol biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.18.-
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Q4W9I3 | MNSTLYSTSPGTYWEQYEEVSQHSAHLNVVERLWSAWYAWMQNDVLATGIMSFVMHEIVYFGRSVPWILIDTLGLFKNYKIQNNKIPSLREQWDCAKFVLLSHFTVELPQIWLFHPMAQFFGLSTSVPFPSVWTMMYQIAIFFVLEDTWHYFSHRALHWGPLYKAIHKIHHQYSAPFGMAAEYASPIEVMILGFGTVGCPILWCALTGDLHIFTMYVWIVLRLFQAIDAHSGYEFPWSLHHFLPFWAGADHHDLHHEKFVGNYSSSFRWWDYLLDTEYTPEALKRRREGKLTKKAQ | Function: Sterol-C4-methyl oxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . Erg25B is a catalytic component of the C-4 demethylation complex that catalyzes the conversion of 4,4-dimethylfecosterol into fecosterol via 4-methylfecosterol . The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34910
Sequence Length: 296
Domain: The histidine box domains may contain the active site and/or be involved in metal ion binding.
Pathway: Steroid metabolism; ergosterol biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.18.-
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Q8EW66 | MKYGIVSIVGKPNVGKSTLLNNIFEREVVISSNKPQTTRNMIEISYDSIEDCVINFIDTPGLHNPKNKLDLFLNSQVKASLKKSDLVLFLFDLSRDFDSEDEECLKVLKDFNCNNVVLVLNKRDLKSEEEIKNAKQSISKMFDFTNVLEINSKSKEDVSVLLNTIKEHIKEYEGEKKDLELLKKEVSDKFFVSELIREIIINSFRQEIPYGVAILIDEMKYEQDKNLLTIVYSIIVEKESQKPIIIGKGGSMIKKINISLRERLSDIYDCKIFTNSYVKVKKDWRNNETQIKELGYKK | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34509
Sequence Length: 298
Subcellular Location: Cytoplasm
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A1U2V4 | MTDITRPENPESRCGFVAIVGRPNVGKSTLLNHILGQKLSITSRKPQTTRHQVLGIKTEGPVQAIYVDTPGMHEDEPRALNRYMNKAAASALIDVDVVVFVVDQLAWTSADEMVLEKLKRVKCPVILAVNKVDKLEKRELLLPHLEALSKKRDFAEIIPLSALKETNLEPLESAVGRFLPESVHFYPDDQITDRSERFMAAEMVREKITRQLGAELPYSVAVEIEEFKHQGNTLHVSALILVEREGQKKIIIGDKGERLRSIGQEARVDMERMFGSKVMLRLWVKVKRGWADSDRALKSLGMSDF | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34418
Sequence Length: 305
Subcellular Location: Cytoplasm
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P47627 | MKVLKVGVLGPTNAGKSTLINFLHNDDSLMVSSMNNTTLLSISTEVINQANKNIVFIDVPGFTEKKHSNYELITKEIRKALSGIDVLLLVVRSDQNNKIEFLKTQLQQLKRYQNLTRIFLINKFHQKSLSEVNKAIILEEFKPQKTIEINLLKFDKNLFWSIFKQVELRYNIFRKDINFIDANNDDFKILEGLREQIIFYCKNEIPHIARIEIIEKSFNKEKNLLKIHLVISVPKLSQKKIIIGKNAEMIKAIGIATRKKLLNHFDCDIFIDIFVKTEKQKLPVYSFLSK | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33722
Sequence Length: 290
Subcellular Location: Cytoplasm
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Q98QI1 | MKILFSTIIGRPNVGKSTLLNNILEYDLAIVSSKPQATRDQIMGIYSDDDYQLIFTDTPGIYKTKTKFGENLNAQSYESLKDIDLVIFLSPANEEIGPGDEFICEKIKNFTNKIALITKIDLENSEEVLKKKAEKLKSLGFKEIFAISSKDHGSIKKLINEIKKYSYEGERQFDEDMITEKSEKFIAKESIREACIDLLEQELPHSILVEIDSFSEEEREEKNLVEIHSTIYVNKESQKGILIGKGGSKIKKIGISARKKIQRKLGVNVKLFLKIKVKKNWVNQEKIFKKFDN | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33550
Sequence Length: 293
Subcellular Location: Cytoplasm
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P18074 | MKLNVDGLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDAHGREVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLHTLEITDLADFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARGDKRGKLPRWIQEHLTDANLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLESEETLKRIEQIAQQL | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers.
PTM: ISGylated.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 86909
Sequence Length: 760
Subcellular Location: Nucleus
EC: 3.6.4.12
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O00835 | MSSGDSNLKRRRGGNTGQSSKSYNTWTDYEEDLEESGEFNQSIKKTTNTSSATLTSSEEKGSLLDYSKRCILKQDNKSRPIWVCPDGHIFLETFSAIYKQASDFLVAIAEPVCRPQNIHEYQLTPYSLYAAVSVGLETNDIITVLGRLSKLALPKEVEQFVRQCTQSYGKVKLVLQKNKYFVESAYPEVLEFLLKDSSIATARIKPTLEESVVDPKTGFIINKEVVTGAQISGGLQANQSLDPVLKNDALSNLLEEEEEDTVNNSDQHFHSFEIDPQQVEEVKKRCIQLDYPVLEEYDFRNDTVNPNLNIDLKPTTMIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLSGITAACTVKKSILVLCTSAVSVEQWKYQFKLWSNIEERQISKFTSDNKEKISNVAGVTITTYTMVAFGGRRSAESLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLTVTKAHCKLGLTATLLREDEKIQDLNFLIGPKLYEANWLDLQKAGFLANVSCSEVWCPMTAEFYKEYLINDSQGKKKLLYTMNPNKFRACEYLIRFHEQRGDKIIVFSDNVYALQKYAKGLGRYFIYGPTSGHERMSILSKFQHDPTVRTIFISKVGDTSIDIPEATVIIQVSSHYGSRRQEAQRLGRILRPKPKSDGLYNAFFYSLVSKDTQEMYYSTKRQQFLIDQGYSFKVISELPGIDQEVNLKYSSKQDQLDLLAQVLGEGEDSGKNEILEEDFDDITRGAKKSKSSAPTVSRTTGGSTRALSGGNDMNYMEYQAPAIYKSIPTQHALFKQRAKNKQ | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/repB, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/repB is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 90257
Sequence Length: 800
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q02870 | MGPPKKSRKDRSGGDKFGKKRRAEDEAFTQLVDDNDSLDATESEGIPGAASKNAETNDEQINTDEYGAKDYRSQMQLRPDHGNRPLWVAPNGHVFLESFSPVYKHAHDFLIAISEPVCRPEHIHEYKLTAYSLYAAVSVGLQTHDIVEYLKRLSKTSIPEGILEFIRLCTLSYGKVKLVLKHNKYFIESPHPEVLQKLLKDPVIQKCRLIRSEGEDFIQGTLDGKAITQFGTKLPPGATDKPTPDPAAAAGADGTTAVPEDITDFYEKIDKEEEDEDEANLKTVSFEVAQEKIEVIQKRCIEIEHPLLAEYDFRNDTNNPDINIDLKPAAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTACCTVRKRALVLCNSGVSVEQWKQQFKMWSTADDSMICRFTSEAKDKPMGCGILVTTYSMITHTQKRSWEAEQTMRWLQEQEWGIMVLDEVHTIPAKMFRRVLTIVQSHCKLGLTATLLREDDKIADLNFLIGPKLYEANWLELQKKGYIARVQCAEVWCPMSPEFYREYLTTKTSKKMLLYVMNPSKFRSCQFLIKYHEQRGDKTIVFSDNVFALKHYAIKMNKPFIYGPTSQNERIQILQNFKFNSKVNTIFVSKVADTSFDLPEANVLIQISSHGGSRRQEAQRLGRILRAKKGAIAEEYNAFFYTLVSQDTMEMSYSRKRQRFLVNQGYSYKVITHLKGMDTDSDLMYGTQEEQGQLLQLVLSASDLDCEDEKLPGEPGYRPSGSGGAVRRVGGLSSMSGGDDAIYYEHRKKNIGSVHPLFKKFRG | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of haywire/XPB/ERCC3, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of haywire/XPB/ERCC3 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 90348
Sequence Length: 798
Subcellular Location: Nucleus
EC: 3.6.4.12
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P19447 | MGKRDRADRDKKKSRKRHYEDEEDDEEDAPGNDPQEAVPSAAGKQVDESGTKVDEYGAKDYRLQMPLKDDHTSRPLWVAPDGHIFLEAFSPVYKYAQDFLVAIAEPVCRPTHVHEYKLTAYSLYAAVSVGLQTSDITEYLRKLSKTGVPDGIMQFIKLCTVSYGKVKLVLKHNRYFVESCHPDVIQHLLQDPVIRECRLRNSEGEATELITETFTSKSAISKTAESSGGPSTSRVTDPQGKSDIPMDLFDFYEQMDKDEEEEEETQTVSFEVKQEMIEELQKRCIHLEYPLLAEYDFRNDSVNPDINIDLKPTAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTAACTVRKRCLVLGNSAVSVEQWKAQFKMWSTIDDSQICRFTSDAKDKPIGCSVAISTYSMLGHTTKRSWEAERVMEWLKTQEWGLMILDEVHTIPAKMFRRVLTIVQAHCKLGLTATLVREDDKIVDLNFLIGPKLYEANWMELQNNGYIAKVQCAEVWCPMSPEFYREYVAIKTKKRILLYTMNPNKFRACQFLIKFHERRNDKIIVFADNVFALKEYAIRLNKPYIYGPTSQGERMQILQNFKHNPKINTIFISKVGDTSFDLPEANVLIQISSHGGSRRQEAQRLGRVLRAKKGMVAEEYNAFFYSLVSQDTQEMAYSTKRQRFLVDQGYSFKVITKLAGMEEEDLAFSTKEEQQQLLQKVLAATDLDAEEEVVAGEFGSRSSQASRRFGTMSSMSGADDTVYMEYHSSRSKAPSKHVHPLFKRFRK | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/ERCC3, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation . When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape . The ATP-dependent helicase activity of XPB/ERCC3 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 89278
Sequence Length: 782
Subcellular Location: Nucleus
EC: 3.6.4.12
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P49135 | MGKRDRVDRDKKKSKKRQYEEEEEDEDDIPGNESQEAVPSAAGKQVDESSTKVDEYGAKDYRQQMPLKGDHTSRPLWVAPDGHIFLEAFSPVYKYAQDFLVAIAEPVCRPTHVHEYKLTAYSLYAAVSVGLQTSDITEYLRKLSKTGVPDGIIQFIKLCTVSYGKVKLVLKHNRYFVESSHPDVIQHLLQDPVIRECRLRNAEGEATELITETFTSKSAISKTAAEGSGGPSTSQGVDAQATSDIPKDLFDFYEQMDKDEEEEEETQTVSFEVKQEMIEELQKRCICLEYPLLAEYDFRNDTLNPDINIDLKPTAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTAACTVRKRCLVLGNSAVSVEQWKAQFKMWSTIDDSQICRFTSDAKDKPIGCSVAISTYSMLGHTTKRSWEAERVMEWLKTQEWGLMILDEVHTIPARMFRRVLTIVQAHCKLGLTATLVREDDKIVDLNFLIGPKLYEANWMELQNNGYIAKVQCAEVWCPMSPEFYREYVAIKTKKRILLYTMNPNKFRACQFLIKFHERRNDKIIVFADNVFALKEYAIRLNKPYIYGPTSQGERMQILQNFKHNPKINTIFISKVGDTSFDLPEANVLIQISSHGGSRRQEAQRLGRVLRAKKGMVAEEYNAFFYSLVSQDTQEMAYSTKRQRFLVDQGYSFKVITKLAGMEEEELAFSTKEEQQQLLQKVLAATDLDAEEEVVAGEFGSRSGQASRRCGTMSSLSGADDTVYMEYHSSRSKASSKHVHPLFKRFRK | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/ERCC3, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/ERCC3 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 89126
Sequence Length: 783
Subcellular Location: Nucleus
EC: 3.6.4.12
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O13768 | MSLKRKNNAREGTPDEDLEEYSDYSDVDNYGEEDDDSYKPAPRIRINNNKTKAQTTTNSNEARQSGISAMFGQNDFSNLLGLKLDHTARPLWINPIDGRIILEAFSPLAEQAIDFLVTISEPVSRPAFIHEYRITAYSLYAAVSVGLKTEDIIAVLDRLSKTPIPPSIVDFIRACTVSYGKVKLVLKKNRYFIESGDASVLRLLLRDPVIGPLRIDYSTQSSKQKSSKPSNEDNVEDKKDITNDSSKETAEKSSSDELFSAVVGLQEEEDDEDAVHLFEIKHSSVETIKKRCAEIDYPLLEEYDFRNDNINPDLPIDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFLQWSNIKPDHIAVFTADHKERFHSEAGVVVSTYSMVANTRNRSYDSQKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTIAAHTKLGLTATLVREDDKIDDLNFLIGPKMYEANWMDLAQKGHIAKVQCAEVWCAMTTEFYNEYLRENSRKRMLLYIMNPKKFQACQFLIDYHEKRGDKIIVFSDNVYALRAYAIKLGKYFIYGGTPQQERMRILENFQYNELVNTIFLSKVGDTSIDLPEATCLIQISSHYGSRRQEAQRLGRILRAKRRNDEGFNAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMENLPNLAYASKAERLELLQEVLLQNEEAADLDDGEDTSFGSRSLSRAPAKAKRSSGSLSTLAGADNMAYVEYNKSANKQLKKDSKEHHALFRKHLYTKRR | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/ptr8, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/ptr8 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription (By similarity). Plays a role in mRNA export .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 91345
Sequence Length: 804
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q13216 | MLGFLSARQTGLEDPLRLRRAESTRRVLGLELNKDRDVERIHGGGINTLDIEPVEGRYMLSGGSDGVIVLYDLENSSRQSYYTCKAVCSIGRDHPDVHRYSVETVQWYPHDTGMFTSSSFDKTLKVWDTNTLQTADVFNFEETVYSHHMSPVSTKHCLVAVGTRGPKVQLCDLKSGSCSHILQGHRQEILAVSWSPRYDYILATASADSRVKLWDVRRASGCLITLDQHNGKKSQAVESANTAHNGKVNGLCFTSDGLHLLTVGTDNRMRLWNSSNGENTLVNYGKVCNNSKKGLKFTVSCGCSSEFVFVPYGSTIAVYTVYSGEQITMLKGHYKTVDCCVFQSNFQELYSGSRDCNILAWVPSLYEPVPDDDETTTKSQLNPAFEDAWSSSDEEG | Function: Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair. The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes. Plays a role in DNA single-strand and double-strand breaks (DSSBs) repair; involved in repair of DSSBs by non-homologous end joining (NHEJ) .
Sequence Mass (Da): 44055
Sequence Length: 396
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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G4SW86 | MSEQESRDNAAVDAVRQKYGFGFSWLVLMIALPPLVYYLWICVTYYQGELVFTSDAAAWRRFWSHVAPPTWHAAGLYAAWFLGQAALQVWAPGPTVQGMKLPDGSRLDYRMNGIFSFLFTLAVVFGLVTMGWLDATVLYDQLGPLLTVVNIFTFVFAGFLYFWGLNGKQWERPTGRPFYDYFMGTALNPRIGSLDLKLFCEARPGMIFWLLMNLSMAAKQYELHGTVTVPMLLVVGFQSFYLIDYFIHEEAVLTTWDIKHEKFGWMLCWGDLVWLPFTYTLQAQYLVHHTHDLPVWGIIAIVALNLAGYAIFRGANIQKHHFRRDPNRIVWGKPAKYIKTKQGSLLLTSGWWGIARHMNYFGDLMIALSWCLPAAFGSPIPYFHIVYFTILLLHREKRDDAMCLAKYGEDWLQYRKKVPWRIVPKIY | Function: Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Complements the deletion of the Delta(14)-sterol reductase gene ERG24 in yeast.
Catalytic Activity: 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49418
Sequence Length: 427
Pathway: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol.
Subcellular Location: Cell inner membrane
EC: 1.3.1.70
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Q75D30 | MNDKVAATLVLVVTYSIVGASLWCLTYAWHDETKLYYWCIVQLLPVMLWVWCVISWCGAQLFGYAKRGKAD | Function: Probable component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI-anchors for cell surface proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8163
Sequence Length: 71
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
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O44406 | MSADEPSPEDEKYLESLRDLLKISQEFDASNAKQNDEPEKTAVEVESAETRTDESEKSIDIPREQQLLPSERVEPLKSMVEPEYVKKVIRQMDTMTAEQLKQALMKIKVSTGGNKKTLRKRVAQYYRKENALLNRKMEPNADKTARFFDYLIAIDFECTCVEIIYDYPHEIIELPAVLIDVREMKIISEFRTYVRPVRNPKLSEFCMQFTKIAQETVDAAPYFREALQRLYTWMRKFNLGQKNSRFAFVTDGPHDMWKFMQFQCLLSNIRMPHMFRSFINIKKTFKEKFNGLIKGNGKSGIENMLERLDLSFVGNKHSGLDDATNIAAIAIQMMKLKIELRINQKCSYKENQRSAARKDEERELEDAANVDLTSVDISRRDFQLWMRRLPLKLSSVTRREFINEEYLDCDSCDDLTDDKNDEAAFQEKMAIREYLENKQTEDFAKIAAERGIFKIGEIKSYQTARPIIEDDDVDVESEEEDYGTEFEMLEVVERMPPVSSTLHTEVDLDAVWERDGGSDSERENLSNAPSLHEFPSSSTSSPHATSEHVTSSSPLHIDDDVDRVLNAPPKNSLASSSNRSSF | Function: RNA exonuclease that acts as a negative regulator of RNA interference (RNAi) . Probably acts by degrading the 3'-overhangs of short interfering RNAs (siRNAs) . Component of the ERI/DICER complex which is involved in processing amplified double-stranded RNA (dsRNA) intermediates during small-RNA-mediated gene-silencing or RNA interference (RNAi) (Probable).
Sequence Mass (Da): 67214
Sequence Length: 582
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q7SEY9 | MKPASRLFYLSLFALWSPEAQCKSDESCAISPKAIVSDACASYSTLEQLNRDIKPALEDLTRTTDFFSHYRLNLFNKECPFWNDENGMCGNIACAVETLDNEEDIPEVWRAKELGKLEGPRAKHPGKSVQKEEPKRPLQGKLGEDVGESCVVEYDDECDDRDYCVPDDEGASSKGDYVSLLRNPERFTGYAGDGAKQVWDAIYRENCFQKSSFPKSASLGDTYSVPKNPAAQDFRAVMQAAGRQHMLEQQREQNPLVPFVTKTGLESEDECLEKRVFYKIVSGMHASISTHLCWDFLNQTTGQWQPNLSCYINRLHKFPERISNLYFNYALLTRAVAKLGPYLSSHEEYTFCTGDPAQDADTRAKVLAVTSKAANTVPGPVFDESIMFKNGEGPSLKEDFRNRFRNISRLMDCVGCDKCRLWGKLQTAGYGTALKVLFEFANNDTSATSSETDEIPFKLKRTELVALFNTYARLSSSLDAIQKFRAMVEESEEGQQPQSHEQIEGSENSGAHHIPDRAKKPRHVIVPTPDAADHAEASDTNTATTAVDEAKAAGVTPAPKVEHQQQVEVDNNDDDDDDDEFHEFQRQPQQPDTDPNFVYKKRTLKDDFENEFRAVFAAFKLVIRSYLNLPALIYEITITELKRFWQFYVGLPVMPRTWEFRRPSLDEL | Function: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly pdi1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on pdi1 to transfer oxidizing equivalent. Does not oxidize all pdi related proteins, suggesting that it can discriminate between pdi1 and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75607
Sequence Length: 668
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.8.4.-
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Q03103 | MRLRTAIATLCLTAFTSATSNNSYIATDQTQNAFNDTHFCKVDRNDHVSPSCNVTFNELNAINENIRDDLSALLKSDFFKYFRLDLYKQCSFWDANDGLCLNRACSVDVVEDWDTLPEYWQPEILGSFNNDTMKEADDSDDECKFLDQLCQTSKKPVDIEDTINYCDVNDFNGKNAVLIDLTANPERFTGYGGKQAGQIWSTIYQDNCFTIGETGESLAKDAFYRLVSGFHASIGTHLSKEYLNTKTGKWEPNLDLFMARIGNFPDRVTNMYFNYAVVAKALWKIQPYLPEFSFCDLVNKEIKNKMDNVISQLDTKIFNEDLVFANDLSLTLKDEFRSRFKNVTKIMDCVQCDRCRLWGKIQTTGYATALKILFEINDADEFTKQHIVGKLTKYELIALLQTFGRLSESIESVNMFEKMYGKRLNGSENRLSSFFQNNFFNILKEAGKSIRYTIENINSTKEGKKKTNNSQSHVFDDLKMPKAEIVPRPSNGTVNKWKKAWNTEVNNVLEAFRFIYRSYLDLPRNIWELSLMKVYKFWNKFIGVADYVSEETREPISYKLDIQ | Function: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.
PTM: The Cys-100/Cys-105 and Cys-352/Cys-355 disulfide bonds constitute the redox-active center. The Cys-100/Cys-105 disulfide bond may accept electron from PDI1 and funnel them to the active site disulfide Cys-352/Cys-355.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65033
Sequence Length: 563
Domain: The C-terminal part (437-563) is required for the association with the endoplasmic reticulum lumen membrane.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.8.4.-
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Q09216 | MLRRRGGPNELRDELNNSKNQPEDDQRTKRGRESIGFRHWIYFVLTVAIVYAGVVALHRKMPAVRDGTSFEDFSEQRARVLLKQLTALGSRPSGSDNLEVKAFGMIQDRIGKIHSVVDEVGVNRLESDVQRPSGCFDLKFLSSFTLCYHKITNVVVRIGPKKGPSGNSLLLNCHFDTMPDTPGATDDAVACTIMMDVLEVLAHSKTELENDVVFLFNGAEENFLQAAHGFINQHPWRHDIRAFINLEGTGSGGREILFQAGPGNSWLLQTYLENAPHPFCSVLAQEIFQSGIIPSDTDFRIFRDYGRISGLDIAYTKNGWFYHTEFDEEWRIEPGAIQRAGENVLAVVRAILKSPYLEKPATFDEENRWVFYDVVGLFTVYYSVNVGKLLNYIACFATYFLVVLRIRNRLYSVGDLAIAFKHHVVAFLAMVITMLLIIAFVVQMDLVMCWYKMPEIVGALYVLPMLIAGAIVHSHYADNNRIRNVEMVQYDTILLSFASILFLMTFYNLSSAFYVLNNLILPVFKDIIIWALGLFGVIRRVTPRVLFFTQLFCFLPTFVFAAYAISQCVDFFVPVMGRLGNAINPEFIMGPLGLVIASGFILFVNNLFYISRRMNYIIRLLFAIFALFILVLITTKVGNPYEYSHENPRLRRIIALHANRTIYDFEGHLTQKDNALFVHSLDYRGASDLPDHSFLQGSSAPNCTGVVDEYCRMPYYTAIHELFPPEQSLWVPVPSPVVLPYPIDLKLVSRHAMGENLNLTFEIRGGYDKMSLHVTPLNDYDLLSWSFTDIDIKEFGRRQTYFVFMTYGHEAPEVRRFWILLKNKNGVAPDPEKHENIELSVATHYAHGIYQDTETLRQLRAMISSRRQTPEQAVGWWRWGITMVGGRSEIVVKIF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102122
Sequence Length: 895
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.-.-
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Q18600 | MSTGIRRRHADEKKNILEKESLQNDETQREMEKDISLLRPAHWNFIGLFFLVLIIGTTFLHKCLPEPKDPNQEETQFSEKRAVKVLQELSDYGWKPAGSYNCEELTRNRILKELNDIRSQNQNVENLRFDIDTQYVSGCFDIPAHDTEGMNICYRNVSNVMARLGKGEKKDKISVLLNCHYDSWPTSNAGSDDLSSCALMLELIRLYSKNPHLLNHDVIFLFNGAEESSLLAAHGFITQHSWRHEIRAFINLEASGSGGRELLFQAGPANQWLLNSYLEAAIHPHCSVIGQEVFQSGVYPGDTDFRIFRDHGRVPGLDLAFVQNGYWWHTEFDTAERITKGSLQRAGENVYSTLNHLLKSPYLEKPAEYADRKTVFFDFLGLFVIIYPLSIAHLVNMLTICTVIALMSHRFYSKTFITFLALRDYVLTILTIALVLKAMTFMSLFTYGALRWYTRHWLALVAYGLPSVWAGISVQGLLTARLAPKAREEYGSTLELIHLTLISGILLAFTYYDIASGFLFALLLVPAIKSIITYFGAWPTCPTFNTILTLILSFPGCAMAIYTTEMLLSIFIPIMGRSSYNPEPAVSFFVAFSAGCIVLSLGGLVAKSRNSRSSNEAGLLELIYNILGVLLVTLTILYVFSSFWPSPYRFDNVYPTAKRTQFFHVNQMLYDRNGQISVNDTRFYAISHDYRGAEDIPFVKKDPEYTGLQCHYENNPWCETPFLFPTKGRLNERNIRVRSVDERLKFKHPVKILGISKRHGVDSKDGKGNIEYSFSVIGTGQISVYIIPDTTWLITNTSVTQPKTPQENMFLYYTCSTPNNICEWMFKVTIKKTTQTPSDDKPLLIGISSHYLHGPEMQSESIKNMIAKIQENRVNSPEWTVTASAWNVDQVYKYF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101896
Sequence Length: 895
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.-.-
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Q05359 | MLLTSLLQVFACCLVLPAQVTAFYYYTSGAERKCFHKELSKGTLFQATYKAQIYDDQLQNYRDAGAQDFGVLIDIEETFDDNHLVVHQKGSASGDLTFLASDSGEHKICIQPEAGGWLIKAKTKIDVEFQVGSDEKLDSKGKATIDILHAKVNVLNSKIGEIRREQKLMRDREATFRDASEAVNSRAMWWIVIQLIVLAVTCGWQMKHLGKFFVKQKIL | Function: Involved in vesicular protein trafficking.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24723
Sequence Length: 219
Subcellular Location: Endoplasmic reticulum membrane
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P39704 | MIKSTIALPSFFIVLILALVNSVAASSSYAPVAISLPAFSKECLYYDMVTEDDSLAVGYQVLTGGNFEIDFDITAPDGSVITSEKQKKYSDFLLKSFGVGKYTFCFSNNYGTALKKVEITLEKEKTLTDEHEADVNNDDIIANNAVEEIDRNLNKITKTLNYLRAREWRNMSTVNSTESRLTWLSILIIIIIAVISIAQVLLIQFLFTGRQKNYV | Function: Involved in vesicular protein trafficking.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24064
Sequence Length: 215
Subcellular Location: Endoplasmic reticulum membrane
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Q12403 | MSNLCVLFFQFFFLAQFFAEASPLTFELNKGRKECLYTLTPEIDCTISYYFAVQQGESNDFDVNYEIFAPDDKNKPIIERSGERQGEWSFIGQHKGEYAICFYGGKAHDKIVDLDFKYNCERQDDIRNERRKARKAQRNLRDSKTDPLQDSVENSIDTIERQLHVLERNIQYYKSRNTRNHHTVCSTEHRIVMFSIYGILLIIGMSCAQIAILEFIFRESRKHNV | Function: Involved in vesicular protein trafficking.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26511
Sequence Length: 225
Subcellular Location: Endoplasmic reticulum membrane
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P11474 | MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVALAPGPAPTRCLPGHKEEEDGEGAGPGEQGGGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAAPVNALVSHLLVVEPEKLYAMPDPAGPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD | Function: Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism. Induces the expression of PERM1 in the skeletal muscle.
PTM: Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.
Sequence Mass (Da): 45510
Sequence Length: 423
Subcellular Location: Nucleus
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O08580 | MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVTLASGPAPARCLPGHKEEEDGEGAGSGEQGSGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAPVNALVSHLLVVEPEKLYAMPDPASPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGDLGAALLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD | Function: Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism. Induces the expression of PERM1 in the skeletal muscle (By similarity).
PTM: Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.
Sequence Mass (Da): 45464
Sequence Length: 422
Subcellular Location: Nucleus
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O95718 | MSSDDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGLALGTHANGLDSPPMFAGAGLGGTPCRKSYEDCASGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSESSPYLSLQISPPAKKPLTKIVSYLLVAEPDKLYAMPPPGMPEGDIKALTTLCDLADRELVVIIGWAKHIPGFSSLSLGDQMSLLQSAWMEILILGIVYRSLPYDDKLVYAEDYIMDEEHSRLAGLLELYRAILQLVRRYKKLKVEKEEFVTLKALALANSDSMYIEDLEAVQKLQDLLHEALQDYELSQRHEEPWRTGKLLLTLPLLRQTAAKAVQHFYSVKLQGKVPMHKLFLEMLEAKV | Function: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcription activity . Plays a role, in a LIF-independent manner, in maintainance of self-renewal and pluripotency of embryonic and trophoblast stem cells through different signaling pathways including FGF signaling pathway and Wnt signaling pathways. Upon FGF signaling pathway activation, interacts with KDM1A by directly binding to enhancer site of ELF5 and EOMES and activating their transcription leading to self-renewal of trophoblast stem cells. Also regulates expression of multiple rod-specific genes and is required for survival of this cell type (By similarity). Plays a role as transcription factor activator of GATA6, NR0B1, POU5F1 and PERM1 . Plays a role as transcription factor repressor of NFE2L2 transcriptional activity and ESR1 transcriptional activity . During mitosis remains bound to a subset of interphase target genes, including pluripotency regulators, through the canonical ESRRB recognition (ERRE) sequence, leading to their transcriptional activation in early G1 phase. Can coassemble on structured DNA elements with other transcription factors like SOX2, POU5F1, KDM1A and NCOA3 to trigger ESRRB-dependent gene activation. This mechanism, in the case of SOX2 corecruitment prevents the embryonic stem cells (ESCs) to epiblast stem cells (EpiSC) transition through positive regulation of NR0B1 that inhibits the EpiSC transcriptional program. Also plays a role inner ear development by controlling expression of ion channels and transporters and in early placentation (By similarity).
PTM: Acetylated by PCAF/KAT2 (in vitro).
Sequence Mass (Da): 48054
Sequence Length: 433
Subcellular Location: Nucleus
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Q61539 | MSSEDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGIALSTHANGLDSPPMFAGAGLGGNPCRKSYEDCTSGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYNCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSENSPYLNLPISPPAKKPLTKIVSNLLGVEQDKLYAMPPNDIPEGDIKALTTLCELADRELVFLINWAKHIPGFPSLTLGDQMSLLQSAWMEILILGIVYRSLPYDDKLAYAEDYIMDEEHSRLVGLLDLYRAILQLVRRYKKLKVEKEEFMILKALALANSDSMYIENLEAVQKLQDLLHEALQDYELSQRHEEPRRAGKLLLTLPLLRQTAAKAVQHFYSVKLQGKVPMHKLFLEMLEAKV | Function: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcriptional activity . Plays a role, in a LIF-independent manner, in maintainance of self-renewal and pluripotency of embryonic and trophoblast stem cells through different signaling pathways including FGF signaling pathway and Wnt signaling pathways . Upon FGF signaling pathway activation, interacts with KDM1A by directly binding to enhancer site of ELF5 and EOMES and activating their transcription leading to self-renewal of trophoblast stem cells . Also regulates expression of multiple rod-specific genes and is required for survival of this cell type . Plays a role as transcription factor activator of GATA6, NR0B1, POU5F1 and PERM1 . Plays a role as transcription factor repressor of NFE2L2 transcriptional activity and ESR1 transcriptional activity (By similarity). During mitosis remains bound to a subset of interphase target genes, including pluripotency regulators, through the canonical ESRRB recognition (ERRE) sequence, leading to their transcriptional activation in early G1 phase . Can coassemble on structured DNA elements with other transcription factors like SOX2, POU5F1, KDM1A and NCOA3 to trigger ESRRB-dependent gene activation . This mechanism, in the case of SOX2 corecruitment prevents the embryonic stem cells (ESCs) to epiblast stem cells (EpiSC) transition through positive regulation of NR0B1 that inhibits the EpiSC transcriptional program . Also plays a role inner ear development by controlling expression of ion channels and transporters and in early placentation .
PTM: Acetylated by PCAF/KAT2 (in vitro).
Sequence Mass (Da): 48328
Sequence Length: 433
Subcellular Location: Nucleus
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P62508 | MDSVELCLPESFSLHYEEELLCRMSNKDRHIDSSCSSFIKTEPSSPASLTDSVNHHSPGGSSDASGSYSSTMNGHQNGLDSPPLYPSAPILGGSGPVRKLYDDCSSTIVEDPQTKCEYMLNSMPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRIDAENSPYLNPQLVQPAKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVIIGWAKHIPGFSTLSLADQMSLLQSAWMEILILGVVYRSLSFEDELVYADDYIMDEDQSKLAGLLDLNNAILQLVKKYKSMKLEKEEFVTLKAIALANSDSMHIEDVEAVQKLQDVLHEALQDYEAGQHMEDPRRAGKMLMTLPLLRQTSTKAVQHFYNIKLEGKVPMHKLFLEMLEAKV | Function: Orphan receptor that acts as transcription activator in the absence of bound ligand. Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements (By similarity). Induces the expression of PERM1 in the skeletal muscle.
PTM: Acetylated by PCAF/KAT2 (in vitro).
Sequence Mass (Da): 51306
Sequence Length: 458
Subcellular Location: Nucleus
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Q5RAM2 | MSNKDRHIDSSCSSFIKTEPSSPASLTDSVNHHSPGGSSDASGSYSSTMNGHQNGLDSPPLYPSAPILGGSGPVRKLYDDCSSTIVEDPQTKCEYMLNSMPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRIDAENSPYLNPQLVQPAKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVIIGWAKHIPGFSTLSLADQMSLLQSAWMEILILGVVYRSLSFEDELVYADDYIMDEDQSKLAGLLDLNNAILQLVKKYKSMKLEKEEFVTLKAIALANSDSMHIEDVEAVQKLQDVLHEALQDYEAGQHMEDPRRAGKMLMTLPLLRQTSTKAVQHFYNIKLEGKVPMHKLFSEMLEAKV | Function: Orphan receptor that acts as transcription activator in the absence of bound ligand. Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements. Induces the expression of PERM1 in the skeletal muscle (By similarity).
PTM: Acetylated by PCAF/KAT2 (in vitro).
Sequence Mass (Da): 48555
Sequence Length: 435
Subcellular Location: Nucleus
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P05432 | MSTAGVAAQDIRVPLKTGFLHNGQALGNMKTCWGSRNEFEKNFLNIDPITMAYNLNSPAPEHLTTLGCASPSAPGSGHFFAERGPSPKSSLPPLVIPPSESSGQREEDQVLCGFKKLSVNGVCASTPPLTPIQSCSSPFPCAAPCDRSSRPLPPLPISEDPSLDEADCEVEFLTSADTDFLLEDCVPSDFKYDVPGRRSFRGCGQINYAYFDSPTVSVADLSCASDQNRVVPDPNPPPPQSHRRLRRSHSGPAGSFNKPAIRISSCTHRASPSSDEDKPEIPPRVPIPPRPAKPDYRRWSAEVTSNTYSDEDRPPKVPPREPLSRSNSRTPSPKSLPSYLNGVMPPTQSFAPDPKYVSSKALQRQSSEGSAKAPCILPIIENGKKVSSTHYYLLPERPPYLDKYEKYFREAEEANPSTQIQPLPAACGMVSATDKLASRMKMDVGGHGKRKHLSYVVSP | Function: Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49941
Sequence Length: 459
Domain: The EGFR-binding region prevents binding of a cyclin-like activator to the EGFR kinase domain, and thereby keeps EGFR in an inactive conformation. Also maintains EGFR in an inactive conformation by preventing formation of an asymmetric homodimer (By similarity).
Subcellular Location: Cytoplasm
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Q38846 | MESCDCFETHVNQDDLLVKYQYISDALIALAYFSIPLELIYFVQKSAFFPYKWVLMQFGAFIILCGATHFINLWMFFMHSKAVAIVMTIAKVSCAVVSCATALMLVHIIPDLLSVKNRELFLKKKADELDREMGLILTQEETGRHVRMLTHGIRRTLDRHTILRTTLVELGKTLCLEECALWMPSQSGLYLQLSHTLSHKIQVGSSVPINLPIINELFNSAQAMHIPHSCPLAKIGPPVGRYSPPEVVSVRVPLLHLSNFQGSDWSDLSGKGYAIMVLILPTDGARKWRDHELELVENVADQVAVALSHAAILEESMHARDQLMEQNFALDKARQEAEMAVHARNDFLAVMNHEMRTPMHAIISLSSLLLETELSPEQRVMIETILKSSNLVATLISDVLDLSRLEDGSLLLENEPFSLQAIFEEVISLIKPIASVKKLSTNLILSADLPTYAIGDEKRLMQTILNIMGNAVKFTKEGYISIIASIMKPESLQELPSPEFFPVLSDSHFYLCVQVKDTGCGIHTQDIPLLFTKFVQPRTGTQRNHSGGGLGLALCKRFVGLMGGYMWIESEGLEKGCTASFIIRLGICNGPSSSSGSMALHLAAKSQTRPWNW | Cofactor: Binds 1 copper ion per dimer.
Function: Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
PTM: Autophosphorylated on both His and Ser residues in the presence of manganese. Loss of His autophosphorylation in the presence of both manganese and magnesium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68333
Sequence Length: 613
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.11.-
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Q8RY71 | MAPTLQGQWIKVGQKGGTGPGPRSSHGIAAVGDKLYSFGGELTPNKHIDKDLYVFDFNTQTWSIAQPKGDAPTVSCLGVRMVAVGTKIYIFGGRDENRNFENFRSYDTVTSEWTFLTKLDEVGGPEARTFHSMASDENHVYVFGGVSKGGTMNTPTRFRTIEAYNIADGKWAQLPDPGDNFEKRGGAGFAVVQGKIWVVYGFATSIVPGGKDDYESNAVQFYDPASKKWTEVETTGAKPSARSVFAHAVVGKYIIIFAGEVWPDLNGHYGPGTLSNEGYALDTETLVWEKLGEEGAPAIPRGWTAYTAATVDGKNGLLMHGGKLPTNERTDDLYFYAVNSA | Function: Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation (By similarity). Converts glucosinolates both to epithionitriles and to simple nitriles in the presence of myrosinase . Promotes the formation of epithionitriles after hydrolysis of alkenylglucosinolates containing a terminal double bond. Mediates indol-3-ylacetonitrile (IACN) production from indol-3-ylmethylglucosinolate (glucobrassicin) . Triggers the production of 3,4-epithiobutylnitrile from 2-propenylisothiocyanate, product of 2-propenylglucosinolate (sinigrin) catalysis by myrosinase . Seems inactive toward benzylglucosinolate (glucotropaeolin) . Acts as a negative regulator of senescence.
Catalytic Activity: a (Z)-N-(sulfonatooxy)alkenimidothioate = an epithionitrile + sulfate
Sequence Mass (Da): 37008
Sequence Length: 341
Subcellular Location: Cytoplasm
EC: 4.8.1.5
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Q9YHT3 | YEVGMMKGGIRKDRRGGRMLKHKRQREENDSRNAGALTEARSTALWPSPLMIKHSKKNSPALSLTADQMVSALLEAEPPVVYSEYDPSRPFNEASVMTLLTNLADRELVHMINWAKRVPGFVDLALHDQVHLLECAWLEILMVGLVWRSMEHPGKLLFAPNLLLDRSHGKVVEGFVEIFDMLLAASSRFRMMNVRGEEFVCLKSIILLNPGIYTYLSSTLKSVEERDHIHRVLDKITDTLMHLMAKSGLSLQQQHRRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPAAKGSPPSEDDPLNQLAVPSPSMHSLLPCYVNKQEEGNEQEAI | Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Sequence Mass (Da): 39560
Sequence Length: 349
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Subcellular Location: Nucleus
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Q91424 | GHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRILKHKRQREEHDNRNAGAIVERRSPNLWPSPLMITHNKKNSPALSLTADQIVSALLEAEPPVVYSEYDPSRPFSEASMMTLLTNLADRELVHMINWAKRVPGFVDLSLHDQVHLLECAWLEILMIGLVWRSVEHPGKLLFAPNLLLDRNQGKCVEGFVEIFDMLLATSSRFRMMNVQGEEFVCLKSIILLNSGIYTFLSSTLKSLEEKDHIHRVLDKIIDTLLHLMAKSGLSLQQQHRRLAQLLLILSHFRHMSNKGM | Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Sequence Mass (Da): 35202
Sequence Length: 307
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Subcellular Location: Nucleus
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P49884 | MTMTLHTKASGMALLHQIQANELEPLNRPQLKIPLERPLGEVYMDSSKPAVYNYPEGAAYDFNAAAPASAPVYGQSGLPYGPGSEAAAFGANGLGAFPPLNSVSPSPLVLLHPPPQPLSPFLHPHGQQVPYYLENESSGYAVREAGPPAYYRPNSDNRRQGGRERLASTSDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRNEAVPSGDMRAANLWPSPIMIKHTKKNSPVLSLTADQMISALLEAEPPIIYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLALHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLRSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHRRLAQLLLILSHFRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPANFGSAPPEDVNQSQLAPTGCTSSHSLQTYYITGEAENFPSTV | Function: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (By similarity).
PTM: Glycosylated; contains N-acetylglucosamine, probably O-linked.
Sequence Mass (Da): 66489
Sequence Length: 596
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The modulating domain, also known as A/B or AF-1 domain has a ligand-independent transactivation function. The C-terminus contains a ligand-dependent transactivation domain, also known as E/F or AF-2 domain which overlaps with the ligand binding domain. AF-1 and AF-2 activate transcription independently and synergistically and act in a promoter- and cell-specific manner (By similarity).
Subcellular Location: Nucleus
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P06212 | MTMTLHTKASGVTLLHQIQGTELETLSRPQLKIPLERSLSDMYVESNKTGVFNYPEGATYDFGTTAPVYGSTTLSYAPTSESFGSSSLAGFHSLNNVPPSPVVFLQTAPQLSPFIHHHSQQVPYYLENEQGSFGMREAAPPAFYRPSSDNRRHSIRERMSSTNEKGSLSMESTKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGEMMKQKRQREEQDSRNGEASSTELRAPTLWTSPLVVKHNKKNSPALSLTAEQMVSALLEAEPPIVYSEYDPNRPFNEASMMTLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATAARFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEERDYIHRVLDKITDTLIHLMAKSGLSLQQQHRRLAQLLLILSHIRHMSNKGMEHLYNMKCKNVVPLYDLLLEMLDAHRLHAPAARSAAPMEEENRNQLTTAPASSHSLQSFYINSKEEESMQNTI | Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Sequence Mass (Da): 66746
Sequence Length: 589
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The modulating domain, also known as A/B or AF-1 domain has a ligand-independent transactivation function. The C-terminus contains a ligand-dependent transactivation domain, also known as E/F or AF-2 domain which overlaps with the ligand binding domain. AF-1 and AF-2 activate transcription independently and synergistically and act in a promoter- and cell-specific manner (By similarity).
Subcellular Location: Nucleus
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P03372 | MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV | Function: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 .
PTM: Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Self-association induces phosphorylation. Dephosphorylation at Ser-118 by PPP5C inhibits its transactivation activity. Phosphorylated by LMTK3 in vitro.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66216
Sequence Length: 595
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The modulating domain, also known as A/B or AF-1 domain has a ligand-independent transactivation function. The C-terminus contains a ligand-dependent transactivation domain, also known as E/F or AF-2 domain which overlaps with the ligand binding domain. AF-1 and AF-2 activate transcription independently and synergistically and act in a promoter- and cell-specific manner. AF-1 seems to provide the major transactivation function in differentiated cells.
Subcellular Location: Nucleus
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Q9YHZ7 | MSEEQARAEAPAGARQRRRSELEGYSVSLASLKLSPMYPEEEQRTTGGISSTAHYLDGTFNYTTNPDATNSSVDYYSVAPEPQEENLQPLPNGSSSPPVFVPSSPQLSPFLGHPPAGQHTAQQVPYYLEPSGTSIYRSSVLASAGSRVELCSAPGRQDVYTAVGASGPSGASGPSGAIGLVKEIRYCSVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYVCPATNQCTIDRNRRKSCQACRLRKCYEVGMMKGGFRKERGGRIIKHNRRPSGLKERERGYSKAQSGSDVREALPQDGQSSSGIGGGVADVVCMSPEQVLLLLLRAEPPTLCSRQKHSRPYSELTIMSLLTNMADRELVHMIAWAKKVPGFQDLSLHDQVQLLESSWLEILMIGLIWRSIYTPGKLIFAQDLILDKSEGECVEGMAEIFDMLLATVARFRTLKLKSEEFVCLKAIILLNSGAFSFCSSPVEPLRDGFMVQCMMDNITDALIYYISQSGISVQLQSRRQAQLLLLLSHIRHMSYKGMEHLYSMKCKNKVPLYDLLLEMLDAHRLRPLGKVPRIWADRVSSSPTTTATTPTTNTTTTTTTTTHHPSNGSTCPADLPSNPPGPGQSPSP | Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Sequence Mass (Da): 67671
Sequence Length: 617
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Subcellular Location: Nucleus
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P49886 | LFAPNLLLDRNQGKCVEGMVESFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHRRLAQLLLILSHIRHMSNKGME | Function: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (By similarity).
PTM: Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1 proteasomal degradation. Deubiquitinated by OTUB1.
Sequence Mass (Da): 13836
Sequence Length: 121
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The modulating domain, also known as A/B or AF-1 domain has a ligand-independent transactivation function. The C-terminus contains a ligand-dependent transactivation domain, also known as E/F or AF-2 domain which overlaps with the ligand binding domain. AF-1 and AF-2 activate transcription independently and synergistically and act in a promoter- and cell-specific manner (By similarity).
Subcellular Location: Nucleus
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O24602 | MASRMGMVAIVSLFVCALAASTSVNANVWQTDDIPVVNSNMVRHSNMERQQQQGGFIGHRPRLASFNRASNQDGDRKRTVPSGPDHMHHSIPSHTPQHPPVYVQALYEDDRSRTSSGPSKSIGPPPLSDRY | Function: Extracellular signal peptide that regulates cell fate.
PTM: The O-glycosylation (arabinosylation) of the hydroxyproline Pro-84 enhances binding affinity of the ESR1p peptide for its receptor.
Sequence Mass (Da): 14432
Sequence Length: 131
Subcellular Location: Secreted
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P38117 | MAELRVLVAVKRVIDYAVKIRVKPDRTGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALAMGADRGIHVEVPPAEAERLGPLQVARVLAKLAEKEKVDLVLLGKQAIDDDCNQTGQMTAGFLDWPQGTFASQVTLEGDKLKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVIKPGDLGVDLTSKLSVISVEDPPQRTAGVKVETTEDLVAKLKEIGRI | Function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase . It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (Probable). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism . ETFB binds an AMP molecule that probably has a purely structural role .
PTM: Methylated. Trimethylation at Lys-200 and Lys-203 may negatively regulate the activity in electron transfer from acyl-CoA dehydrogenases.
Sequence Mass (Da): 27844
Sequence Length: 255
Domain: The recognition loop recognizes a hydrophobic patch at the surface of interacting dehydrogenases and acts as a static anchor at the interface.
Subcellular Location: Mitochondrion matrix
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Q9DCW4 | MAELRALVAVKRVIDFAVKIRVKPDKSGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEIIAVSCGPSQCQETIRTALAMGADRGIHVEIPGAQAESLGPLQVARVLAKLAEKEKVDLLFLGKQAIDDDCNQTGQMTAGLLDWPQGTFASQVTLEGDKVKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVVKAGDLGVDLTSKVSVISVEEPPQRSAGVKVETTEDLVAKLKEVGRI | Function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (By similarity). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism . ETFB binds an AMP molecule that probably has a purely structural role (By similarity).
PTM: Methylated . Trimethylation at Lys-200 and Lys-203 may negatively regulate the activity in electron transfer from acyl-CoA dehydrogenases.
Sequence Mass (Da): 27623
Sequence Length: 255
Domain: The recognition loop recognizes a hydrophobic patch at the surface of interacting dehydrogenases and acts as a static anchor at the interface.
Subcellular Location: Mitochondrion matrix
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Q7F9U3 | MKILVAVKRVVDYAVKVRVRPDRTGVETASVKMSMNPFCEIAVEEALRLRESGAATEVVAATVGPSQSADTLRTALAMGADRAVHVLHDPDPSRPLLPLAVAKILRALALQENPGLVILGKQAIDDDCNQTGQMLAGLLNWPQGTFASKVILNKEKATVEREVDGGIETISLDLPAVITTDLRLNQPRYATLPNIMKAKSKVIKKVTPEDLDVDIRSDMEVVEVTEPPKRKAGVILSSVDELVDRLKNEARVL | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
Sequence Mass (Da): 27469
Sequence Length: 253
Subcellular Location: Mitochondrion matrix
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Q6UAQ8 | MAELRALVAVKRVIDFAVKIRVKPDRTGVVMDGVKHSMNPFCEIAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALAMGADRGIHVEVPAAEAHHLGPLQVARVLAKLAQKEKVDLVLLGKQAIDDDCNQTGQMTAGFLDWPQGTFASQVTLEGDKVKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVIKAGDLGVDLTSKLSVVSVEDPPQRVAGVKVETTEDLVAKLREIGRI | Function: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase. Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism. ETFB binds an AMP molecule that probably has a purely structural role.
PTM: Methylated. Trimethylation at Lys-200 and Lys-203 may negatively regulate the activity in electron transfer from acyl-CoA dehydrogenases.
Sequence Mass (Da): 27764
Sequence Length: 255
Domain: The recognition loop recognizes a hydrophobic patch at the surface of interacting dehydrogenases and acts as a static anchor at the interface.
Subcellular Location: Mitochondrion matrix
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Q9UTH2 | MSKIRILVGVKRTLDYMLKPRINATKTAVDLSGQKMSINPFCDIAVEEAIRMKETLKNRIEDTLVVTAGQTSSEPILRQCLAKGIGRAALINVGEKELEPLSVAKLLKATVEKEKSNLVLLGKQAIDDDAHQTGGMLAAMLGWPQFTSASKVRIEGDKVIVTREIDGGEETLSSTLPAIITTDLRLNVPRFANLAKVMKARKAPLGKMSPEDLGVTIDQRLQTVSVSEPVQKRQNIMVKSVDEMVKTLKELGAL | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
Sequence Mass (Da): 27744
Sequence Length: 254
Subcellular Location: Mitochondrion matrix
|
Q0AZ34 | MNLKVLVCVKQTFDTEAKIELKDGKIADAGINLIINPYDEVAVEGAIQLKEKGVAKEIVVVAAGSDKAMDAIRTALAMGADRGILVQQDTAADEFARAVALAEAIKGENPDIILAGHVAADDGSSQVPTRVAEILGLPHVNVITAVEIAGGKATCTSEADGGTQVTEVSLPAVISSQVSWNEPRYPSMKGIMAAKKKPVATAAAAAAESKVKILEFSLPPAKAAGIKIEDEPEVCATKLAEWMKNTVKVEVK | Cofactor: Binds 1 AMP per subunit.
Function: Part of an electron transfer flavoprotein involved in syntrophic growth of S.wolfei with butyrate. Probably receives electrons from butyryl-CoA dehydrogenases, and transfers them to the membrane-bound quinone oxidoreductase Swol_0698.
Sequence Mass (Da): 26280
Sequence Length: 252
Pathway: Lipid metabolism; butanoate metabolism.
Subcellular Location: Cytoplasm
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P42940 | MSAKQQLRILVPVKRVVDFQIKPRVNKTLTGIETSGIKFSINPFDDIAVEEAIRIKEKNKSLVESTHAVSIGSAKAQDILRNCLAKGIDTCSLIDSVGKENIEPLAIAKILKAVVEKKGSNLVLMGKQAIDDDCNNTGQMLAGLLNWPQATNAAKVEFLDNGRVQVTREIDDGEEVIEASLPMVITTDLRLNTPRYVGLPKLMKAKKKPIEKLDIAKDFPEINIEPQLKIVSMEEPKTKSPGVKLNSVDELIEKLKEVKAI | Cofactor: Binds 1 FAD per dimer.
Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
Sequence Mass (Da): 28759
Sequence Length: 261
Subcellular Location: Mitochondrion matrix
|
P41212 | MSETPAQCSIKQERISYTPPESPVPSYASSTPLHVPVPRALRMEEDSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHILKQRKPRILFSPFFHPGNSIHTQPEVILHQNHEEDNCVQRTPRPSVDNVHHNPPTIELLHRSRSPITTNHRPSPDPEQRPLRSPLDNMIRRLSPAERAQGPRPHQENNHQESYPLSVSPMENNHCPASSESHPKPSSPRQESTRVIQLMPSPIMHPLILNPRHSVDFKQSRLSEDGLHREGKPINLSHREDLAYMNHIMVSVSPPEEHAMPIGRIADCRLLWDYVYQLLSDSRYENFIRWEDKESKIFRIVDPNGLARLWGNHKNRTNMTYEKMSRALRHYYKLNIIRKEPGQRLLFRFMKTPDEIMSGRTDRLEHLESQELDEQIYQEDEC | Function: Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'. Plays a role in hematopoiesis and malignant transformation.
PTM: Phosphorylation of Ser-257 by MAPK14 (p38) inhibits ETV6 transcriptional repression.
Sequence Mass (Da): 53000
Sequence Length: 452
Subcellular Location: Nucleus
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P0A0L2 | MKKTAFTLLLFIALTLTTSPLVNGSEKSEEINEKDLRKKSELQGTALGNLKQIYYYNEKAKTENKESHDQFLQHTILFKGFFTDHSWYNDLLVDFDSKDIVDKYKGKKVDLYGAYYGYQCAGGTPNKTACMYGGVTLHDNNRLTEEKKVPINLWLDGKQNTVPLETVKTNKKNVTVQELDLQARRYLQEKYNLYNSDVFDGKVQRGLIVFHTSTEPSVNYDLFGAQGQYSNTLLRIYRDNKTINSENMHIDIYLYTS | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is necessary for the toxin interaction with MHC class II.
Function: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules . In turn, waves of cellular activation, cytokine production, and migration into the lung tissue and airways occur via alphabeta T-cells . Causes also the intoxication staphylococcal food poisoning syndrome. The illness is characterized by high fever, hypotension, diarrhea, shock, and in some cases death (Probable).
Sequence Mass (Da): 29669
Sequence Length: 257
Subcellular Location: Secreted
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P20723 | MKKFNILIALLFFTSLVISPLNVKANENIDSVKEKELHKKSELSSTALNNMKHSYADKNPIIGENKSTGDQFLENTLLYKKFFTDLINFEDLLINFNSKEMAQHFKSKNVDVYPIRYSINCYGGEIDRTACTYGGVTPHEGNKLKERKKIPINLWINGVQKEVSLDKVQTDKKNVTVQELDAQARRYLQKDLKLYNNDTLGGKIQRGKIEFDSSDGSKVSYDLFDVKGDFPEKQLRIYSDNKTLSTEHLHIDIYLYEK | Cofactor: A zinc-binding site contributes directly to formation of the homodimer.
Function: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of pro-inflammatory cytokines . In addition, induces B-cell proliferation and differentiation in the presence of T-cells . Causes also the intoxication staphylococcal food poisoning syndrome .
Sequence Mass (Da): 29746
Sequence Length: 258
Subcellular Location: Secreted
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P0A0M0 | MINKIKILFSFLALLLSFTSYAKAEDLHDKSELTDLALANAYGQYNHPFIKENIKSDEISGEKDLIFRNQGDSGNDLRVKFATADLAQKFKNKNVDIYGASFYYKCEKISENISECLYGGTTLNSEKLAQERVIGANVWVDGIQKETELIRTNKKNVTLQELDIKIRKILSDKYKIYYKDSEISKGLIEFDMKTPRDYSFDIYDLKGENDYEIDKIYEDNKTLKSDDISHIDVNLYTKKKV | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is necessary for interaction with host MHC class II molecules.
Function: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules via their alpha domain, in particular TRAV27 . In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of pro-inflammatory cytokines . Causes also the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death .
Sequence Mass (Da): 27859
Sequence Length: 241
Subcellular Location: Secreted
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A2RQG7 | MFCLNTFKSRWPREFQNLKKKKKKTCVKLSIPIRSVTGDAASLTVVVTMYKRDDYVRNKPGGVFSRWQGFARSMLLPKPFSETAELRRTVADYSLISRGLAPKILREAKGNREDLRVGKDFVGSRYRVQESIQGLGVAVNIHDADDISHGQTESIRTRLRSYGRPVPLLKKLGDNASQTITQKKTGGRSKDKKHGFEEERDVSRVEAEENNTNSVHASVLRLSRSRPQPVLERHDDIVDGSDSASVCGVLQEDGTTCLTAPVTGRKRCTEHKGQRITCAPPVKNPPCEEETEEICGVILPEMVRCRSKPVSGRKRCEDHKGMRVNAFFFLLNPTERDKILKEDKSKPKTRTSSTNQEEPGESLICEATTKNGLPCTRSAPNGSKRCWQHKDETVDQKSSENVQTSTTVCGVKLHNGSVCEKTPVKGRKRCQEHKGMRITS | Function: Transcription regulator that negatively modulates gibberellin-mediated developmental processes. May act as transcriptional repressor of giberellin controlled genes. Binds DNA without sequence preference.
Sequence Mass (Da): 49323
Sequence Length: 440
Domain: Contains a bacterial GIY-YIG-like domain.
Subcellular Location: Nucleus
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P10229 | MPLRASEHAYRPLGPGTPPMRARLPAAAWVGVGTIIGGVVIIAALVLVPSRASWALSPCDSGWHEFNLGCISWDPTPMEHEQAVGGCSAPATLIPRAAAKQLAAVARVQSARSSGYWWVSGDGIRACLRLVDGVGGIDQFCEEPALRICYYPRSPGGFVQFVTSTRNALGLP | Function: Important virulence factor of HSV neurotropism. Seems to be required for glycoprotein B-induced fusion. Dispensable for growth in vitro (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 18180
Sequence Length: 172
Subcellular Location: Virion membrane
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Q6UDL6 | MRPNGARTQTAPPPAAAEGTADVHGNGEAATIQLDGQPSAPSPPLTTVFEATDDYKARRRNLESEPPFEVRAILDDELSDYPVAAPLDAVPQKHSCCCGVCLRRCAFVLTGMAVGMLLAAALLATIAAFAVPESVWTGGVCERGWVQHMGVCYKPGRTPPPSSAADGNFSAATFAGANTNCAAAGGSIVSSDQALSFLVLLSKTASGPNSAPPRGSWWTTHSGSCAIVHYAPSSTLEVYGNTSSLQSLALRTRDALDVSIAEDTQCSGSAGVMCAAAPAPPTALKYAQALRAILTLGVRAE | Function: Seems to be required for glycoprotein B-induced fusion.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 30945
Sequence Length: 301
Subcellular Location: Virion membrane
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L7MC74 | MAHKIAIGLVCVLYALHIMSAVCEVSEQEGVGEDNATEDEDYEDFFKPVTCYFANSTVGPLRPPNCTVVCTNNTAWWNDTKSDGGHCYSEYRPEKRTHSREIYNCTIGVCGNGTCIANHTYADCW | Function: Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL1, CCL2, CCL3, CCL3L1, CCL7, CCL8, CCL11, CCL12, CCL13, CCL14, CCL15, CCL16, CCL18 and CCL23 . Binds to CCL8 with 1:1 stoichiometry and disrupts CCL8 homodimer formation .
Sequence Mass (Da): 13925
Sequence Length: 125
Domain: The N-terminal region is required for binding to CCL8.
Subcellular Location: Secreted
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Q08CB3 | MVTAFLNERQATTEEMALVSNALAAYSFIADQPERAALYFVCGVCLGLVLTLIALVVQISCRTDCKTQQAPKKTGKTVENTSDTSDSDSDWDNTSDLSARRHRRFERTLGNVFTSAEELERAQRLEERERIIREIWMNGQPDMPGTRSLNRYY | Function: Acts as a regulator of programmed cell death, mediating both autophagy and apoptosis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17374
Sequence Length: 153
Subcellular Location: Endoplasmic reticulum membrane
|
Q9H8M9 | MRLPLSHSPEHVEMALLSNILAAYSFVSENPERAALYFVSGVCIGLVLTLAALVIRISCHTDCRRRPGKKFLQDRESSSDSSDSEDGSEDTVSDLSVRRHRRFERTLNKNVFTSAEELERAQRLEERERIIREIWMNGQPEVPGTRSLNRYY | Function: Acts as a regulator of programmed cell death, mediating both autophagy and apoptosis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17470
Sequence Length: 152
Subcellular Location: Endoplasmic reticulum membrane
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Q91WM6 | MKLPLSPSTEPVATEPLGMALLSSILAAWSYISENPERAALYFVSGVCIGLFLTLAALVMRISCHTDCRRGPRRRCLQDRECSDSSDSEDGSEDTASDLSVRRHRRFERTLNKNVFTSAEELERAQRLEERERIIREIWMNGQPEVPGTRSLNRYY | Function: Acts as a regulator of programmed cell death, mediating both autophagy and apoptosis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17810
Sequence Length: 156
Subcellular Location: Endoplasmic reticulum membrane
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P54521 | MGEAAYVTVSALTKYIKRKFDVDPHLENIWIKGELSNVKIHTRGHIYFTLKDENARMQSVMFARQSERLPFKPENGMKVLVRGGISVYEPSGNYQLYAKEMQPDGVGALYLAYEELKKKLAGEGLFDDRYKKQIPAFPATIGVVTSPTGAAVRDVITTLKRRYPLVKVIVLPALVQGENASRSIVTRIEEANEKEICDVLIVGRGGGSIEELWAFNEEIVARAIFASNIPIISAVGHETDFTISDFVADIRAATPTGAAEIAVPHTTDLIERTKTAEVRMTRAMQQHLGQKKERIQTLQSSYAFRFPKRLYAQKEQQFDLAYQQFQAQLTALLDRKSRQLERETYRLEALHPHEQLKQARTRYQEQTNQLRKNMNIQMKQLHSQFQTVLGKLNALSPLQVMERGYSLAYKEDKLIKSVSQIEEQDRLEIKLKDGVLTCEVLEKRGEEK | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 51048
Sequence Length: 448
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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A1UTK7 | MADFFTEKPVATNVAEFSVSEIANALKRVVEDKFGYVRIRGEISGYRGAHASGHAYFALKDDKARLEAVIWLSVMKKLSFPPEEGMEVIAVGKLTTYPGSSKYQIVIEALEPTGVGALMTLLENRKKKLAEEGLFDAANKKPLPYMPKIIGVVTSPTGAVIRDIIHRIFDRFPLHILVWPVRVQGETCGREVASAVEGFNALFLGGGIPKPDLIIVARGGGSLEDLWGFNDEAVVRAVYASAIPVISAVGHETDWTLIDYAADWRAPTPTGAAERAVPVKLDIEVHLASINSRFRVGLARYFDFHQQKLRALVRGLPTVDQLFALPRRGFDEISSRLQRALCVSYDKKCFYFHALSLRFSPRLLNTKKAQYAIQEYTGRLHRAFLRNVEKQRAQVEMACRLLKSTSYQNILERGFVLALGKDHKPIKRLMQLPETGQISLRFFDGEIDVSTHDRAVNRSLKNKRIKSQKDDQGLLF | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 53314
Sequence Length: 476
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q6FZ30 | MNLFFEKTEATNVAEFSVSEIAGALKRVVEERFGYVRVRGEISGYRGAHASGHVYFSLKDDKARLEAVIWRGIMEKLKFPPEEGMEVIAVGKLTTYPGSSKYQIVIEALEPTGVGALMTLLENRKKKLADEGLFDEAKKKPLPYMPRIIGVVTSPTGAVIRDIIHRISDRFPLHILVWPVRVQGDTSGREVADALKGFNALPFGGLVPKPDLIIVARGGGSLEDLWGFNDEAVVRAVYESALPVISAVGHETDWTLIDYVADWRAPTPTGAAERAVPVKLDLEVQVASLGARLRMGLARYFDFHQQKLRALVRGLPTVDQLFALPRRGFDEISSRLQRALCVSCDKKRFYFHGLNLRLSPRLLNTEKELRNTKEYTARLHRAFVRNVEKQRAQLEVASRLLKSTSYQNILERGFVLALGPDNKLIKRLVQFPETGQINLRFFDGEMSVSARDHGLNRSSKSKRIKSKQDDQGTLF | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 53315
Sequence Length: 475
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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Q7VVB6 | MTIGLSVTNDVFARDILTVAQLNQAVGQLLERSIPSLWVRGEISNFTQAASGHWYFTLKDSRAAVRTVMFRSRAAQVGFVPRPGDQVEVRARVSLYEPRGDYQLQADGMRRAGVGNLYEAFLRLKAQLQDEGLFDPQRKRQPARLPRAIGVVTSLHAAALRDVLSALARRAPQVPVIIYPAPVQGADAAARLAARVAQANQRAEVDTLLLVRGGGSIEDLWSFNDEALAREVAASDIPVISGVGHETDFTIVDFVADLRAPTPTAAAELACVPRGDLLAALRHTAEWLARAQQRRLDQAAQRLDRAAAMLTSPAQRLAHQQERLNTLRHRLASAWRGPQGHRVARLDMLAQRLAHRRPDTGRAAERSAALLAQLGRAQARLAAARQARLDTLAAQLRALDPQHTLARGYAIVRDAAGAIVTDATRLAARDRIEIAVARGRIGADVTDIGTPDGTDGNPALRRG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 50274
Sequence Length: 463
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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C0ZC06 | MALQDILSVSDLNRYIKLVLEKEPHLQDIWVRGEISNFTHHSSGHMYFTLKDKQSRIKVVMFASYNRFLRFLPKDGAKAIVRGSISAYERDGAYQFYAKEMQPDGLGSLYLAFEQLKEKLAQEGLFAAERKRMLPRFPKRVGVVTSPTGAAIRDICTTIRRRYPQAEIVLSPAVVQGADAPASIVSAIRIMNDQPDIDVLIVGRGGGSIEELWAFNDENVARAIATSLIPVISAVGHETDVTIADFVADVRAATPTAAAELAVPHYLEWVERVRQLEIRMHRAVRGTMTEQRNRLTRLGNSYAMRQPERRLEEAAERLDRAHLRMRQSMKHLLDRRRERYTRLDEQIKRYRLADQIGEKRKNLSKLRATLDERMLGRLNQKRMAFAARIATLEALSPLKVMQRGFSLVYTNDRLVKSVEQFAPGDEIMVRLSDGSATARVEKVNREEEKQSGSQKNGTRD | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 52405
Sequence Length: 460
Subcellular Location: Cytoplasm
EC: 3.1.11.6
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A6X3A0 | MGSDSSFTGASSNVAEYSVSEISGALKRTVEDTFGHVRVRGEISGYRGPHSSGHAYFALKDDRARLEAVIWRGSMSRLRFRPEEGMEVIATGKLTTYPGSSKYQIVIEQMEPAGAGALMALLEERKRRLATEGLFDPAVKQLLPFMPRVIGVVTSPTGAVIRDIIHRIADRYPLHVIVWPVRVQGETSGPEVAAAVDGFNALPDEGNIPRPDVLIVARGGGSLEDLWGFNDEIVVRAVAASHIPVISAVGHETDWTLIDLAADIRAPTPTGAAEMAVPVKADLLATLAGQSARLSSAMSRFIDLKRQAHRSAARALPSADQLLALPRRRFDEAAARLTRALFVNTQKKRVHFDGHARQLSPRLLQRRFTELQRDVSALGQRLPRALEAFLRERRTAFIHRANRLSAEPILRRTKLTSVAIEQLDRRRDQAVRLLIERAKRRGQELERLMRTLSYESVLERGFAVVFDEEGKPVKQAGSVSAGDALSIRFRDGEVAVVAGDEDESEPAKLVQTKKVQSPGSGNQGSLF | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 57887
Sequence Length: 527
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q5FJG6 | MAENKYLTVTDLNYYITQKFKNDPYLHKVFLQGELSNFRYRRNSHQYFSLKDEKSKINVVMFRSYFDKVKFKPEEGMKVYVTGYVSVYGPQGSYQFYAENMEPAGLGALYEQLKQLQVKLAKEGLFNPEHKKKIPRFPDRIAVVTSASGAVIHDIMVTANRRFPHAEIDLFPAQVQGDTAAESLVRAMRQIAAEGDKYDVMIIGRGGGSLEDLWPFNEEEVVRQVYNMQMPVISSVGHETDTTLCDLVADARAATPTAAAEYATPNLMDELAGIHQLQSRLFSSMQTIIRQKRDRLNRIQNSIIMREPTRLYDQQIETVDRLKQRLQNSMQNKLDHSKQDYRLLNQRLFAVNPDKQINQMKQQRLFLAKRLSDNMQHYLKDKRNIFAQIVQQLDDYSPLKTLERGFVYTTDRDGKTISSVKQVNKNDSLNLHFKDGQVAAKVVEVKEEKNANEEK | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 52602
Sequence Length: 455
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
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