ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q6PDU4 | MAGIKALISLSFGGAIGLMFLMLGCALPIYNQYWPLFVLFFYILSPIPYCIARRLVDDTDAMSNACKELAIFLTTGVVVSAFGLPVVFARAHLIEWGACALVLTGNTVIFATILGFFLVFGSNDDFSWQQW | Function: Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14400
Sequence Length: 131
Subcellular Location: Membrane
|
Q93373 | MRLLLCLLLFSTLLINSTNACPGVITQACFCSEVHSGIVLDCSNSSASGILQIIRTNQAQVGLIQSLTMNQAELVELPPNFFSGLFIRRLDLSQNKIKKIDDAAFAGINPVLEEVVLNHNLIEKVPAAALAGLPNLLRLDLSNNSIVEIQEQEIFPNLNKLYDINLGSNKIFSIHTSTFQNVKNSIQTINLGHNNMTAVPSSAIRGLKQLQSLHLHKNRIEQLDALNFLNLPVLNLLNLAGNQIHELNRQAFLNVPSLRYLYLSGNKITKLTAYQFQTFEQLEMLDLTNNEIGAIPANSLSGLKQLRQLYLAHNKISNISSNAFTNSSIVVLVLSSNELKTLTAGIISGLPNLQQVSFRDNQIKTINRNAFYDAASLVMLDLAKNQLTEIAPTTFLAQLNLLLVDLSENKLPKTPYSAFNSRVGTVLLKENPLVCTENLHMLQQGTGVYVRDSPDIICGRKPTPKPEPVLVPIVTDSLISTQRPALVQIPKMQIHRNVHTTTGDQAPQIPSGAFQQIDLGKSRSLPRGHSRFILDKPSTREQSVEPTEELTPIQPIILPSREDEIRQSSMEAGTSQESVEATSQKIPSTTDIIDRPNVVLPFPVPFLKRGPNLSESKKVESTDMPSTSQVFHTLPPSILIEPGSTPKVAQPSTEANIKSEHIDEFALASSNSNEPTLQPRLEKSFFTTTIIFICVGTAVIVLVVVIAGLCISKHRQLQFENTYSDSSAARTSEYISTQYRQNSLRGTGGRVGRFEESPAWIYNPGSSYCNYYK | Function: Required for apical extracellular matrix organization and epithelial junction maintenance.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85297
Sequence Length: 773
Subcellular Location: Apical cell membrane
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P22981 | MTEYKLVVVGDGGVGKSALTIQLIQNHFVEEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNEAKSFENVANYREQIRRVKDSDDVPMVLVGNKCDLSSRSVDFRTVSETAKGYGIPNVDTSAKTRMGVDEAFYTLVREIRKHRERHDNNKPQKKKKCQIM | Function: The level of let-60 controls the switch between vulval and hypodermal cell fates during C.elegans vulval induction . May stimulate the guanine nucleotide exchange factor (GEF) activity of rap-1 . May induce nuclear condensation .
Location Topology: Lipid-anchor
Sequence Mass (Da): 20983
Sequence Length: 184
Subcellular Location: Cell membrane
|
Q8Y5R9 | MKKIQFFDTTLRDGEQTPGVNFDVKEKIQIALQLEKLGIDVIEAGFPISSPGDFECVKAIAKAIKHCSVTGLARCVEGDIDRAEEALKDAVSPQIHIFLATSDVHMEYKLKMSRAEVLASIKHHISYARQKFEVVQFSPEDATRSDRAFLIEAVQTAIDAGATVINIPDTVGYTNPTEFGQLFQDLRREIKQFDDITFASHCHDDLGMATANALAAIENGARRVEGTINGIGERAGNTALEEVAVALHIRKDFYQAETNIVLNQFKNSSDLISRLSGMPVPRNKAVIGGNAYAHESGIHQDGVLKNPDTYEIITPALVGVDKNSLPLGKLSGKHAFNTRMEEMGYTLTEQEQKDAFKRFKQLADAKKEVTEEDLHALILGQSSESADDFELKHLQVQYVTGGVQGAIVRIEERDGALVEDAATGSGSIEAIYNTINRLMKQDIELTDYRIQAITAGQDAQAEVHVVIKNDKGAEFHGIGIDFDVLTASAKAYLQASGKSKTASKQADFEEVK | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 56096
Sequence Length: 512
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
A0LBW3 | MNGSMPFHKYSPYPPVALANRQWPNRTLTKAPLWCSVDLRDGNQALANPMGPQAKRRMFDLLVEIGFKEIEVGFPSASRDDFQFLRDLIEQKAIPDDVTVQMLVQSRAHLIERTFEALQGAKRAIVHLYTPTSSLQRRVVFGKSQQEIIDVAVEGTQMIKEHAQRSPETEIVLEFSPESFTGTELPFALAISEAVQQVWQPTPAQPMILNLPATVEMSTPNIYADQIEWMLSHLSDPQSIIISLHAHNDRGTAVAATELAMLAGAGRVEGTLFGNGERTGNTDVVAVAMNLHSQGIDAGLNFSEMPRIIATSEACTGMSVPPRQPYAGELVFTAFSGSHQDAIRKGLHLHKQEQAQQWAVPYLPIDPQDLGRHYEPVIRINSQSGKGGMAFIMEERCGIHMPKAMQVEFSRVIQAVTDEMGRELQADEIEQLFFKNFVLQENPLSLGHVEHREETEERHHLHAQVSYAGTVQALQAHGNGPMSALVNALETFYSMTIQIHDYHQHARTAGRDSEAVSFVQISVNGGKPTFGVGLHTDSSRSALEAVLCSINRALATSLT | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 61808
Sequence Length: 559
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q8THA5 | MYTLKEGIDFYIEPMQNKKVTVFDTTLRDGEQTPGVSLTSSQKLEISRQLDKLGVDIIEAGFPISSEGDKESVKSISNAGLETTVCGLARVLKKDIDACFESDVGLVHTFVPTSDVQRIYTIKKSQEEVIQLAVEAVQYIKDHGLKCMFSAMDATRTDPAYLIEVFKAVQEAGCDIINVPDTVGVMVPSAMYRQIKDIAAEITIPIDVHCHNDFGLAVANSLMAVEAGASQVQVTINGIGERAGNADLAQTVMSLASIYGIKTNIRTEYLVETSKMIENYTGIRLPPNTPVVGQNAFSHESGIHSQGVLEKSDTFEPGIMTPEMVGHRRRIVLGKHTGKHAVKQSLESAGVKTSENQLDEIVLRIKEIANKGKQITDADLYAVASAVLGKASSEEELIKLKEVSVMTGNILTPTAVVKADIEGKEIIAAKTGVGPVDAALKAVRDILGESNHFRLQEFRIDAITGGADALADVYIGLENEKGRIVTARSANPDIVMASVEALINAMNLLYKKEKS | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 55693
Sequence Length: 515
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
EC: 2.3.3.13
|
B3DX88 | MEMTANRLIVFDTTLRDGEQCPGASMTSRQKLEVAKQLARLGVDVIEAGFPVISQGDFESVSEIAAQVKGPKICGLARCLPKDIEAAAEALKAAADAARIHVFLATSQIHRRFKLAKDEEEIVRIAVEGVRLAKRYVQDVEFSAEDASRTEPEFLAKIIQKVIEAGATTVNIPDTVGYAVPEEFASLIRYLFDHVQDIDKVVVSVHCHNDLGLAVSNSLAAIKAGARQVEGTINGIGERAGNAALEEIIMALHTRPDAFGKIETGIQLKEILRTSRLVSRMSGLAVQRNKAVVGENAFAHAAGIHQDGILKKRETYEIIDPKIIGWEQSELPLTKHSGRAALENRLKILGFELEKEEIDNIFSQFKQIGDKKKFIYDDDLVSLVEGQISRIKETYELEYVAVTVCSGGIPMATIKLRHGEEVLVDASTGDGAVDAAMKAVDRITGQHGHLVEYEVKSVTEGKDAIGEVTVKVNFDSKKLVTAKAASTDVIEASIKAYLNAVNKALL | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 55078
Sequence Length: 506
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q58595 | MIIYREENEIIKKALENLNIPDRVYIFDTTLRDGEQTPGVSLTPEEKIDIAIKLDDLGVDVIEAGFPVSSLGEQEAIKKICSLNLDAEICGLARAVKKDIDVAIDCGVDRIHTFIATSPLHRKYKLKKSKEEIIDIAVDAIEYIKEHGIRVEFSAEDATRTEIDYLIEVYKKAVDAGADIINVPDTVGVMIPRAMYYLINELKKEIKVPISVHCHNDFGLAVANSLAAVEAGAEQVHCTINGLGERGGNAALEEVVMSLMSIYGVKTNIKTQKLYEISQLVSKYTEIKVQPNKAIVGENAFAHESGIHAHGVLAHALTYEPIPPELVGQKRKIILGKHTGTHAIEAKLKELGIEVGKDINKDQFDEIVKRIKALGDKGKRVTDRDVEAIVEDVVGKLAKKDRVVELEQIAVMTGNRVIPTASVALKIEEEIKKSSAIGVGPVDAAVKAIQKAIGEKIKLKEYHINAITGGTDALAEVIVTLEGYGREITTKAASEDIVRASVEAVIDGINKILAKREK | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 56620
Sequence Length: 518
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
EC: 2.3.3.13
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Q8TYB1 | MPDRVRIFDTTLRDGEQTPGVSLTVEEKVEIARKLDEFGVDTIEAGFPVASEGEFEAVRAIAGEELDAEICGLARCVKGDIDAAIDADVDCVHVFIATSDIHLRYKLEMSREEALERAIEGVEYASDHGVTVEFSAEDATRTDRDYLLEVYKATVEAGADRVNVPDTVGVMTPPEMYRLTAEVVDAVDVPVSVHCHNDFGMAVANSLAAVEAGAEQVHVTVNGIGERAGNASLEQVVMALKALYDIELDVRTEMLVELSRLVERLTGVVVPPNTPIVGENAFAHESGIHSHGVIKKAETYEPIRPEDVGHRRRIVLGKHAGRHAIKKKLEEMGIEVTEEQLDEIVRRVKELGDKGKRVTEDDLEAIARDVVGEVPESEAAVKLEEIAVMTGNKFTPTASVRVYLDGEEHEAASTGVGSVDAAIRALREAIEELGMDVELKEYRLEAITGGTDALAEVTVRLEDEDGNVTTARGAAEDIVMASVKAFVRGVNRLARRRRD | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 54339
Sequence Length: 499
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
EC: 2.3.3.13
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B0JGK2 | MNTSPDRVIIFDTTLRDGEQSPGAALNVDEKLTIARALARLGVDVIEAGFPHASPGDFDAVQKIAASVGSEADSPIICGLARTTQKDIKSAADALRPAAKPRIHTFLATSDIHLQYKLKKTRQEVLEIVPEMVAYAKSFVDDVEFSPEDAGRSDPDFLYQVLERAIAAGATTVNIPDTVGYTTPSEFGALIRGIKENVPNIDQAIISVHGHDDLGLAVANFLEAVKNGARQLECTINGIGERAGNASLEELVMALHVRRSYFNPFLGRPAESTEPLTKINTKEIYRTSRLVSNLTGMIVQPNKAIVGANAFAHESGIHQDGVLKHKLTYEIMDAESIGLTHNQIVLGKLSGRNAFRSRLQELGFELSETELNNAFIQFKEMADRKKEITDRDLEAIVNDEIDTVPDHFRLELVQVSCGNSARPTATVTIRTPDGSELSDAAIGTGPVDALCKAIDRVVKIPNELISFSVREVTEGIDALGEVTIRLRYEGRTYSAHAADTDIIVASARAYVSALNRLHVALQQKEKTPEMLQV | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 58027
Sequence Length: 533
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
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Q7TVV6 | MTTSESPDAYTESFGAHTIVKPAGPPRVGQPSWNPQRASSMPVNRYRPFAEEVEPIRLRNRTWPDRVIDRAPLWCAVDLRDGNQALIDPMSPARKRRMFDLLVRMGYKEIEVGFPSASQTDFDFVREIIEQGAIPDDVTIQVLTQCRPELIERTFQACSGAHRAIVHFYNSTSILQRRVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSPESYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEMTTPNVYADSIEWMSRNLANRESVILSLHPHNDRGTAVAAAELGFAAGADRIEGCLFGNGERTGNVCLVTLGLNLFSRGVDPQIDFSNIDEIRRTVEYCNQLPVHERHPYGGDLVYTAFSGSHQDAINKGLDAMKLDADAADCDVDDMLWQVPYLPIDPRDVGRTYEAVIRVNSQSGKGGVAYIMKTDHGLSLPRRLQIEFSQVIQKIAEGTAGEGGEVSPKEMWDAFAEEYLAPVRPLERIRQHVDAADDDGGTTSITATVKINGVETEISGSGNGPLAAFVHALADVGFDVAVLDYYEHAMSAGDDAQAAAYVEASVTIASPAQPGEAGRHASDPVTIASPAQPGEAGRHASDPVTIASPAQPGEAGRHASDPVTIASPAQPGEAGRHASDPVTIASPAQPGEAGRHASDPVTSKTVWGVGIAPSITTASLRAVVSAVNRAAR | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 75683
Sequence Length: 701
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
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Q9CB76 | MASFSESLSQDPADAYKSAPSITKPMGPPSPGQPQWNPQRATSMPVFRYRPFAKEVEPIRLVDRTWPDRVIDCAPLWCAVDLRDGNQALIDPMSPICKRRMFDLLVRMGYKEIEVGFPSASQTDFDFVREIITDGTIPDDVTIQVLTQCRPELIERTFEACENASRVIVHFYNSTSILQRRVVFRADQATVKAIATDGARKCVEEAFKYPGTHWRFEYSPESYTGTELEYAKQVCDAVGEVIQPTPDNPIIFNLPATVEMATPNVYADSIEWMSRNLANRESVILSLHPHNDRGTAVAAAELGYHAGADRIEGCLFGNGERTGNVCLVTLGLNLFSRGVDPQIDFSNIDEIRRTVEYCNKLRVHERHPYGGDLVYTAFSGSHQDAINKGLDQMKIDADAADSDVDDILWQVPYLPIDPRDVGRTYEAVIRVNSQSGKGGVAYIMKADHGLELPRRLQIEFSRAIQKISEGEGGEITPTEMWDVFFEEYLSPVQPLERIKQRVNAAEEDGGSTSIAATVKINGEETEISGVGNGPLAAFIDALGHVGLQVAVLDYSEHAMNAGDDAQAAAYVEASVHGHTAWGVGIAPSITTASLRAVVSAVNRAMPR | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 66898
Sequence Length: 607
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
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P9WQB2 | MTTSESPDAYTESFGAHTIVKPAGPPRVGQPSWNPQRASSMPVNRYRPFAEEVEPIRLRNRTWPDRVIDRAPLWCAVDLRDGNQALIDPMSPARKRRMFDLLVRMGYKEIEVGFPSASQTDFDFVREIIEQGAIPDDVTIQVLTQCRPELIERTFQACSGAPRAIVHFYNSTSILQRRVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSPESYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEMTTPNVYADSIEWMSRNLANRESVILSLHPHNDRGTAVAAAELGFAAGADRIEGCLFGNGERTGNVCLVTLGLNLFSRGVDPQIDFSNIDEIRRTVEYCNQLPVHERHPYGGDLVYTAFSGSHQDAINKGLDAMKLDADAADCDVDDMLWQVPYLPIDPRDVGRTYEAVIRVNSQSGKGGVAYIMKTDHGLSLPRRLQIEFSQVIQKIAEGTAGEGGEVSPKEMWDAFAEEYLAPVRPLERIRQHVDAADDDGGTTSITATVKINGVETEISGSGNGPLAAFVHALADVGFDVAVLDYYEHAMSAGDDAQAAAYVEASVTIASPAQPGEAGRHASDPVTIASPAQPGEAGRHASDPVTSKTVWGVGIAPSITTASLRAVVSAVNRAAR | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 70114
Sequence Length: 644
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q2LWJ3 | MDSPEKRIYIFDTTLRDGEQSPGSSMNPAEKLRIARQLEKMGVDIIEAGFPIASEGDFLSVQQIAQEIRGAQIAGLARANNADIDRAWEAIRDAANPRIHTFISSSDIHLKYQLRKSREQVLKEAVAAVERARSYTPNVEFSPMDATRTDRGYLCEMVEAVIAAGASTVNIPDTVGYAIPQEFGELIAYLRANVPNISQAIISVHCHNDLGLAVANSLSAILNGARQVECTINGIGERAGNTAMEEVVMALRTRKDLFGFYTGIKTESIYQSSRLLTQITGVAVQPNKAIVGANAFAHESGIHQDGLIKEKITYEIMTPQSVGISDSHIVLGKHSGRHAVSEHLKKLGFNLSDTELNKIFVRFKELADAKKNVFDEDLEAIVYEELYRVEDKYKLIYLNVVSGNVAIPTATMQMEVDREIVQDAGFGVGPVDATFDAIRKITGTNYDLLRYVVNAISGGTDAQGEVTVQLKFNGRSVVGHGADLDVIVASARAYINALNRLEFLKRDAGKIKSEYE | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 56596
Sequence Length: 516
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q58130 | MHKICVIEGDGIGKEVVPATIQVLEATGLPFEFVYAEAGDEVYKRTGKALPEETIETALDCDAVLFGAAGETAADVIVKLRHILDTYANIRPVKAYKGVKCLRPDIDYVIVRENTEGLYKGIEAEIDEGITIATRVITEKACERIFRFAFNLARERKKMGKEGKVTCAHKANVLKLTDGLFKKIFYKVAEEYDDIKAEDYYIDAMNMYIITKPQVFDVVVTSNLFGDILSDGAAGTVGGLGLAPSANIGDEHGLFEPVHGSAPDIAGKKIANPTATILSAVLMLRYLGEYEAADKVEKALEEVLALGLTTPDLGGNLNTFEMAEEVAKRVREE | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate, which decarboxylates to 4-methyl-2-oxopentanoate (2-oxoisocaproate). Also catalyzes the oxidative decarboxylation of 3-methylmalate to 2-oxobutyrate, and that of D-malate to pyruvate. Cannot use NADP(+) instead of NAD(+). Cannot catalyze the oxidation of L-malate, L-tartrate, D-tartrate, DL-isocitrate, or DL-lactate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 36330
Sequence Length: 333
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
O27441 | MKSMKIAVIPGDGIGVEVMEAALHILNTLDLDLEFIHADAGDACLKRTGTALPEETLEAVGEARATLFGAAGESAADVIVRLRREFDLFANLRPVKSLPGVPCLYPDLDFVIVRENTEDLYVGDEEYTPEGAVAKRIITRTASRRISQFAFQYAQKEGMQKVTAVHKANVLKKTDGIFRDEFYKVASEYPQMEATDYYVDATAMYLITQPQEFQTIVTTNLFGDILSDEAAGLIGGLGLAPSANIGEKNALFEPVHGSAPQIAGKNIANPTAMILTTTLMLKHLNKKQEAQKIEKALQKTLAEGLVTPDLGGKLGTMEMAAEIARHLED | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (By similarity).
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 35785
Sequence Length: 329
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
Q73VI1 | MKLAVIGGDGIGPEVTAEALKVLDAVLPGVDKTEYDLGARRYHATGELLPDSVIDELRAHDAILLGAIGDPSVPSGVLERGLLLRLRFELDHHINLRPGRLYPGVSSPLAGNPDIDFVVVREGTEGPYTGTGGAIRVGTPNEVATEVSQNTAFGVRRVVVDAFERARRRRKHLTLVHKTNVLTFAGKLWSRIVAEVGRDYPDVEVAYQHIDAATIFMVTDPGRFDVIVTDNLFGDIITDLSAAVCGGIGLAASGNIDGTRTNPSMFEPVHGSAPDIAGQGIADPTAAIMSVALLLAHLGEDAAATRVDRAVERYLATRGNERPATTEVGERIAAAL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 35660
Sequence Length: 336
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
Q94AR8 | MASVISSSPFLCKSSSKSDLGISSFPKSSQISIHRCQKKSISRKIVSVMAPQKDRSPGTTGSVKTGMTMTEKILARASEKSLVVPGDNIWVNVDVLMTHDVCGPGAFGIFKREFGEKAKVWDPEKIVVIPDHYIFTADKRANRNVDIMREHCREQNIKYFYDITDLGNFKANPDYKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVENRTSVPFEPVYSDGNASFVADYRFDVSKLEPVVAKPHSPDNRALARECKDVKIDRVYIGSCTGGKTEDFMAAAKLFHAAGRKVKVPTFLVPATQKVWMDVYALPVPGAGGKTCAQIFEEAGCDTPASPSCGACLGGPADTYARLNEPQVCVSTTNRNFPGRMGHKEGQIYLASPYTAAASALTGRVADPREFLQ | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate . Functions in both the biosynthesis of leucine and in the methionine chain elongation pathway of aliphatic glucosinolate formation .
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 55014
Sequence Length: 509
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
Subcellular Location: Plastid
EC: 4.2.1.33
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P96195 | MAGKTLYDKLWDMHEVKRRDDGSSLIYIDRQILHEVTSPQVRGAAPGRANVARGCQHRHPGPQRADHPGSPVGGRRHRRRNLAHPGADPGRELRRVRHRRVQDERPAPGHRPCGRPGAGRHLPGMTVVCGDSHTSTHWCGALAHGIGTSEVEHVLATQCLVAKKMKNMQVRVEGELPLGVSAKDIVLAVIGRIGTAGGTGHALEFAGSAIRGLSMEGRMTLCNMAIEAGARVGMVAVDEKTIDYVKGRPYAPQGADWDKAVAQWRELVSDADAGFDTVVELKAEEIRPQVTWGTSPEMVLPVDERVPDPASESDPVKRDSIVRALKYMGLAANQPIGEIKVDRVFIGSCTNSRIEDLRAAAEVAKGARSPRASSRRWWCRAPGWSRSRRRRRGWTGSSSRPVSSGATGCSMCLAMNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAVAGRFVDVRQLLQA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 50894
Sequence Length: 470
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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Q2VZV4 | MAKLRTLFDKIWDAHLVDVQDDGTCLIYIDRHMVHEVTSPQAFEGLEMSGRKVRHPELTLAVADHNVPTTDRSKGIENEESRIQVETLEANAKKFGVEYLRMDDIRQGVVHIVGPEQGFTLPGTTIVCGDSHTATHGAFGSLAFGIGTSEVEHVLATQTLVQKPAKNMRITVTGKPGPGVTAKDIVLAIIGKIGTAGGTGYVVEFAGEAIRDLSMEGRMTVCNMTIEAGARAGLVAPDEKTFAYIAGKPRSPKGAAFEAAVSYWKTLFTDEGAHFDAEVTLDASTLVPQITWGTSPEDVIAITGTVPNPADIKDEAKRKAVERSLDYMGLTAGMKATDIAIDVVFIGSCTNGRIEDFRAAAEIFKGRKVAASVQALIVPGSGLVKEQAEQEGLDKIFIEAGAEWREPGCSMCLAMNADQLKPGQRSASTSNRNFEGRQGRGGRTHLVSPAMAAAAAITGKLTDVRSL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 49880
Sequence Length: 467
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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Q0AT09 | MSPETETGATSSVPRSLFDKVWDAHQVRAETAETPGLLYIDLHLVHEVTSPQAFSVLAERGLKVRRPDRTLATIDHATPTLDFAAGETPPYATAAAQNQVETLQSNTAQHGITLHGWGSGHRGVVHVIGPELGATQPGMTIVCGDSHTATHGAFGALAFGIGTTEVGHVLASQCLLQRKPKSMRVTVDGETAAGISAKDIILAIIAEIGVDGGTGCVIEYAGSAIEALDMEGRMTVCNMSIEAGARAGMIAPDETTFAWLEGREQVPTGSEWDAAIDRWRALRSDAGARFDHEVMIDAASIRPMVTWGTAPDTGIAVNAPIPQPRSPSHRKALAYMGLEAGMPVAGTQVDQVFIGSCTNSRITDLREAAAIMSGRRVADGIRALVVPGSVAVRAQAEAEGLDRIFTDAGAEWRQPGCSMCIAMNGDRGEPGQLVVSTSNRNFEGRQGPGVRTVLASPATAAAAAIAGHVIDPAELMEPAHA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 50379
Sequence Length: 481
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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Q82JR8 | MGRTLAEKVWDDHVVRRAEGEPDLLFIDLHLLHEVTSPQAFDGLRQAGRPVRRLDLTIATEDHNTPTLDIDKPIADPVSRAQLETLRKNCAEFGVRLHSLGDVEQGVVHVVGPQLGLTQPGTTVVCGDSHTSTHGAFGALAFGIGTSQVEHVLATQTLPLARPKTMAITVDGELPDGVTAKDLILAIIARIGTGGGQGYILEYRGSAIEKLSMEARMTICNMSIEAGARAGMIAPDETTFAYLKGRAHAPEGEEWDAAVAYWKTLKSDEDAEFDAEVVIAAAALSPFVTWGTNPGQGAPLSASVPDPASYEDASERFAAEKALEYMGLTAGQPLRDIKVDTVFVGSCTNGRIEDLRAAAAIVEGRKVADGVRMLIVPGSARVGLQAVSEGLDVVFKEAGAEWRHAGCSMCLGMNPDQLAPGERSASTSNRNFEGRQGKGGRTHLVSPQVAAATAVLGHLASPADLADENAARTPAGV | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 50346
Sequence Length: 477
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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Q5M406 | MSGKSIFDKLWDRHVITGDEGQPQLMYVDQHYIHEVTSPQAFQGLRDAGRKVRRPDLTFGTFDHNVPTVNIFDIRDAISKAQIDKLAENVIEFGIDNASHGSDKQGIVHMVGPETGRTQPGKFIVCGDSHTATHGAFGTIAFGIGTSEVEHVFATQTLWQVKPKKMLVEFTGNPQKGIYSKDYILALIAKYGVACGVGYVVEYRGEAIDRLTMEERMTICNMSIEFGSKMGIMNPDQTTYDYMRGRECVPEDFDAAVADWKTLVSDDDAEYDKVIRMDVSELAPMVTWGTNPSMGVDFDTPFPEVRDMNDERAYHYMGLRPGQKAEDINLGYIFIGSCTNARLSDLQLAARIVKGKKISPNLTAIVVPGSRPVKRAAEKIGLDKIFKDAGFEWREPGCSMCLGMNPDKVPDGVHCASTSNRNFEDRQGFGAKTHLCSPAMAAAAAISGHFVDVRRMPEVQ | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 50911
Sequence Length: 460
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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A1W1W9 | MQKFIIHKGIACPLEYANIDTDQIIPKQFLLAVSKQGFGKHLFHDLRYLDDKESVLNMDFNLNKKEYQNSSILVSFENFGSGSSREHAPWALVDYGIRAIIAPSFADIFKNNALGNGLLTIELAKDEVLGIVDELKKSQDKNIEISLLEKRVFFKDKIFSFDLDDFHRICLLEGLDNIALTLKHEAQIKAYEKNSKSFLV | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 22827
Sequence Length: 200
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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Q4FP16 | MQKFNSLTSIPAYLPIVNIDTDMIIPKQFLKTIKRTGLGKNLFFEMRYDDNGNEIKDFILNQKPHNQSKILIAGKNFGCGSSREHAPWALLDFGITCVISSSYADIFYSNCFKNGILPITLPEEKIKELSEYSKRKEEISIDLNEEKIIFGNSEIKFDIDPFKKKCLLEGLDDIALSLAKKEKIITFEENLKNNKPWIFNDKN | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 23350
Sequence Length: 203
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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B4RCC0 | MEAFTRLDAKAAPLPLANIDTDQIIPKQFLKTVERAGLAKGLFYDLRFDEQGREKPNFVLNRPEYKGAGVLVAGDNFGCGSSREHAPWALMDFGIRCVISTSFADIFYGNCFQNGLLPVVLKAEEVQQLMDEARGGNHVVSVDLEAQTVTSPSGAVFRFEIDPQRKDKMLRGLDAIGETLQSQKDIDVYEMKRALAQPWLEGA | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 22512
Sequence Length: 203
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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Q321T8 | MVPGPNTLFVLKNSVSSGMKGGYLAACGVFIGDAVLMFLAWAGVATLIKTTPILFNIVRYLGAFYLLYLESKILYATLKGKNNEAKSDEPQYGAIFKRALILSLTNPKAILFYVSFFVQFIDVNAPHTGISFFILATTLELVSFCYLSFLIISGAFVTQYIRTKKKLAKVGNSLIGLMFVGFAARLATLQS | Function: Exporter of leucine.
Catalytic Activity: H(+)(out) + L-leucine(in) = H(+)(in) + L-leucine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20896
Sequence Length: 191
Subcellular Location: Cell inner membrane
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P16150 | MATLLLLLGVLVVSPDALGSTTAVQTPTSGEPLVSTSEPLSSKMYTTSITSDPKADSTGDQTSALPPSTSINEGSPLWTSIGASTGSPLPEPTTYQEVSIKMSSVPQETPHATSHPAVPITANSLGSHTVTGGTITTNSPETSSRTSGAPVTTAASSLETSRGTSGPPLTMATVSLETSKGTSGPPVTMATDSLETSTGTTGPPVTMTTGSLEPSSGASGPQVSSVKLSTMMSPTTSTNASTVPFRNPDENSRGMLPVAVLVALLAVIVLVALLLLWRRRQKRRTGALVLSRGGKRNGVVDAWAGPAQVPEEGAVTVTVGGSGGDKGSGFPDGEGSSRRPTLTTFFGRRKSRQGSLAMEELKSGSGPSLKGEEEPLVASEDGAVDAPAPDEPEGGDGAAP | Function: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN) (By similarity). Negatively regulates Th2 cell differentiation and predisposes the differentiation of T-cells towards a Th1 lineage commitment. Promotes the expression of IFN-gamma by T-cells during T-cell receptor (TCR) activation of naive cells and induces the expression of IFN-gamma by CD4(+) T-cells and to a lesser extent by CD8(+) T-cells . Plays a role in preparing T-cells for cytokine sensing and differentiation into effector cells by inducing the expression of cytokine receptors IFNGR and IL4R, promoting IFNGR and IL4R signaling and by mediating the clustering of IFNGR with TCR . Acts as a major E-selectin ligand responsible for Th17 cell rolling on activated vasculature and recruitment during inflammation. Mediates Th17 cells, but not Th1 cells, adhesion to E-selectin. Acts as a T-cell counter-receptor for SIGLEC1 (By similarity).
PTM: Glycosylated; has a high content of sialic acid and O-linked carbohydrate structures.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40322
Sequence Length: 400
Subcellular Location: Membrane
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P15702 | MALHLLLLFGACWVQVASPDSLQRTTMLPSTPHITAPSTSEAQNASPSVSVGSGTVDSKETISPWGQTTIPVSLTPLETTELSSLETSAGASMSTPVPEPTASQEVSSKTSALLPEPSNVASDPPVTAANPVTDGPAANPVTDGTAASTSISKGTSAPPTTVTTSSNETSGPSVATTVSSKTSGPPVTTATGSLGPSSEMHGLPATTATSSVESSSVARGTSVSSRKTSTTSTQDPITTRSPSQESSGMLLVPMLIALVVVLALVALLLLWRQRQKRRTGALTLSGGGKRNGVVDAWAGPARVPDEEATTTSGAGGNKGSEVLETEGSGQRPTLTTFFSRRKSRQGSLVLEELKPGSGPNLKGEEEPLVGSEDEAVETPTSDGPQAKDEAAPQSL | Function: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN) . Negatively regulates Th2 cell differentiation and predisposes the differentiation of T-cells towards a Th1 lineage commitment . Promotes the expression of IFN-gamma by T-cells during T-cell receptor (TCR) activation of naive cells and induces the expression of IFN-gamma by CD4(+) T-cells and to a lesser extent by CD8(+) T-cells. Plays a role in preparing T-cells for cytokine sensing and differentiation into effector cells by inducing the expression of cytokine receptors IFNGR and IL4R, promoting IFNGR and IL4R signaling and by mediating the clustering of IFNGR with TCR (By similarity). Acts as a major E-selectin ligand responsible for Th17 cell rolling on activated vasculature and recruitment during inflammation. Mediates Th17 cells, but not Th1 cells, adhesion to E-selectin . Acts as a T-cell counter-receptor for SIGLEC1 .
PTM: Phosphorylation at Ser-347 is regulated by chemokines, requires its association with ERM proteins (EZR, RDX and MSN) and is essential for its function in the regulation of T-cell trafficking to lymph nodes.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40038
Sequence Length: 395
Subcellular Location: Membrane
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P13838 | WAQVVSQENLPNTMTMLPFTPNSESPSTSEALSTYSSIATVPVTEDPKESISPWGQTTAPASSIPLGTPELSSFFFTSAGASGNTPVPELTTSQEVSTEASLVLFPKSSGVASDPPVTITNPATSSAVASTSLETFKGTSAPPVTVTSSTMTSGPFVATTVSSETSGPPVTMATGSLGPSKETHGLSATIATSSGESSSVAGGTPVFSTKISTTSTPNPITTVPPRPGSSGMLLVSMLIALTVVLVLVALLLLWRQRQKRRTGALTLSRGGKRNGTVDAWAGPARVPDEEATTASGSGGNKSSGAPETDGSGQRPTLTTFFSRRKSRQGSVALEELKPGTGPNLKGEEEPLVGSEDEAVETPTSDGPQAKDGAAPQSL | Function: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN). Negatively regulates Th2 cell differentiation and predisposes the differentiation of T-cells towards a Th1 lineage commitment. Promotes the expression of IFN-gamma by T-cells during T-cell receptor (TCR) activation of naive cells and induces the expression of IFN-gamma by CD4(+) T-cells and to a lesser extent by CD8(+) T-cells. Plays a role in preparing T-cells for cytokine sensing and differentiation into effector cells by inducing the expression of cytokine receptors IFNGR and IL4R, promoting IFNGR and IL4R signaling and by mediating the clustering of IFNGR with TCR. Acts as a major E-selectin ligand responsible for Th17 cell rolling on activated vasculature and recruitment during inflammation. Mediates Th17 cells, but not Th1 cells, adhesion to E-selectin. Acts as a T-cell counter-receptor for SIGLEC1.
PTM: Has a high content of sialic acid and O-linked carbohydrate structures.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 38426
Sequence Length: 378
Subcellular Location: Membrane
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P08638 | MEGRSDFVATSQSGSEMSHSETRNRTGMNARKRKFACVECRQQKSKCDAHERAPEPCTKCAKKNVPCILKRDFRRTYKRARNEAIEKRFKELTRTLTNLTSDEILKKIEEEQEIVLDNSNFTKEKVKQLRKSAFETTEIEPRSYKTLRGEPISYSTNRRHTDSSPLTLLSSSTNFDPVHSTNVMTDDQLKCLPKSLGDVYLSSSDIAELFQEFATKYHQFLPVVDLSKGAERIYHLSPCLFWVILLIGLRRKFGATDLMTRLSVLVKSVLSEITISPIIRYTPSDKDEPVLNVASVYSVQAFLLYTFWPPLTSSLSADTSWNTIGTAMFQALRVGLNCAGFSKEYASANSELVNEQIRTWICCNVVSQTVASSFGFPAYVSFDYLVISSIRVPNSKSQVDIPNELRQMAQIARFENQIVNTMNSTPASVTGMVSQEEKQPLLHVLNQQLSQLEISLEENNLDDIRKFLLLVAKVHLLTYYFTDVTSQSAGKSNGNIYEGSYSIMELDTSFETKRGLVKVYNAAVNFLIHANSMWEHDPTIIKYFPGLFVLNIWQSACIISKLIHSSLHSMLDVNSGKKAYNNAISLTFNASVLKYDMAYRSSGIMRSIWSLFANMYDAWKNDQKEGGGRLNNDFNLGITIKSRMSVNVFFDCLYILKEKCGMAKLERETKVSTAYNVDEEEEEDEDEEGEEEEEEEELSSKVPENMDSQQLRTRKFTNVRHPEKKARKIIETIPLDPNPINAGSTSSGSSLTTPNSQVANTISYRGILNKMSPREQLNHANLDSSVSTDIKDTEAVNEPLPIGRNAEHPANQPPLSITQMQENTLPATQANSSLLETYPIVQSNPVTTTIKESPNSIMAGWDNWESDMVWRDVDILMNEFAFNPKV | Function: Factor for control of RNA levels of a group of leucine-specific genes.
Sequence Mass (Da): 100153
Sequence Length: 886
Domain: the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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A8MZ59 | MFEGPRRYRRPRTRFLSKQLTALRELLEKTMHPSLATMGKLASKLQLDLSVVKIWFKNQRAKWKRQQRQQMQTRPSLGPANQTTSVKKEETPSAITTANIRPVSPGISDANDHDLREPSGIKNPGGASASARVSSWDSQSYDIEQICLGASNPPWASTLFEIDEFVKIYDLPGEDDTSSLNQYLFPVCLEYDQLQSSV | Function: Paired-like homeobox transcription factor involved in embryogenesis . May act as a regulator of embryo genome activation . Binds to a 36 bp DNA elements containing a 5'-TAATCC-3' sequence motif, referred to as EEA motif (EGA-enriched Alu-motif), present in the promoters of target genes activated in early embryos .
Sequence Mass (Da): 22358
Sequence Length: 198
Domain: The homeobox contain essential residues (Ile-54, Lys-57, Ala-61) for binding to the 5'-TAATCC-3' motif of the targe gene promoters.
Subcellular Location: Nucleus
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Q314F2 | MGRNREDDITPLQQETLDEICRYVSAKGYPPTVKEMSETFGISHASVHDRINQLVRKGYLKREEGKARGLTVTKHPQTNAVALVAVPIVGTVAAGHPIFAHENITGEVLVEASVVGSGKCFALYTQGDSMIDAGINDGDLIIVRRQPIAEDGDIVIALLDDEATVKRLKIDNELIELVPENPRLKPIRVKPEDELRILGKVVGRKRI | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 22762
Sequence Length: 207
EC: 3.4.21.88
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B1ZZZ4 | MLTEKQEAILDYIRSVQAQRGVPPSTREIQRHFGYESQNAAMNHLRALARKGQLHQVDGATWGLKVSEVQGHFELPIYGTIPAGVPSMQEQQPKETITFDPAVFRLRRPERLWGLEVHGDSMIDAHILDGDIAVLERREAKPGDIVAALVDETTTTLKRLAYVKGKPVLKPENARYALIVPKDRLEIQGVFVGLIGRAKR | Function: Binds a consensus sequence 5'-TGTTC-N(4)-GAACA-3'; some genes have a tandem consensus sequence and their binding is cooperative . Binds to the promoters of a number of genes, including lexA and splB . Represses a number of genes involved in the response to DNA damage (SOS response).
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 22421
Sequence Length: 200
EC: 3.4.21.88
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A1R556 | MAAKATGGGAPLRSQQPQKSPKSLTVRQKKILETIQRSVNDNGYPPSMREIGDTVGLASLSSVTHQLSQLEKLGYLRRDPKRPRAMEVLMPLTLDGGAIPGVEAPTTLRSAGGLAVTELASASDTAMVPLVGRIAAGGPILADQTVEDVLALPRQLVGHGELFMLKVAGDSMIDAAICDGDWVVVRRQNDAINGDIVAALLDDEATVKTFRQRDGHTWLLPQNTQYEPILGDQATIMGKVVSVLRSL | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 26322
Sequence Length: 247
EC: 3.4.21.88
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A1B3Z0 | MLTRKQIQLLEFIQARMARDGVPPSFDEMKLALDLRSKSGIHRLVTALEERGFIRRLPHRARALEIVRLPESLSKGPGFQPRVIEGTMPDRPAPLPRGAMEVSVSAIELPVMGRIAAGVPIEAISEISHHIAVPTTMLSGQDRHYALEVRGDSMIEAGINDGDVVVIREQNAAESGDIVVALVDGYEATLKRYRRKGNMIALEAANPAYETRVLPEDKVRIQGRLVGLIRSY | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 25645
Sequence Length: 232
EC: 3.4.21.88
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Q6D9I5 | MKVLTARQQQVYDLIRDHIAHSGMPPTRAEIAQQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEETGIPLVGRVAAGEPLLAQEHIECRYQVDPAMFKPSADFLLRVSGMSMKNIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLKKQGNTVHLLAENEEFAPIVVDLRQQSFSIEGLAVGVIRNSDWS | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 22312
Sequence Length: 202
EC: 3.4.21.88
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A9BGA3 | MEELTKRQSQVLDFIKSYMEKNGFAPSIRDIMKHFNFKSPRAAHKHLIILEKKGYIERKNVSRGIKMMPKSGEIFATETLAPVSGKIAAGDAIEAIQTISDYIPIPTNFFPKNYEYFSLRVEGNSMIEAQIKSGDFVLIRKQDYAMDGDIVVALIDGNDATLKRYKRLNEDEVLLIPENKSMKEIKVKADHLKIQGKMVGLIRVL | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 23336
Sequence Length: 205
EC: 3.4.21.88
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Q9PNI5 | MKSSNLYSKLLNAPKNAPVFLSQNLEADFIVKAYTFGLFPWTSKPVTWWCPDPRCILIPNQIHIQKNMKKFINLYQIKLDYDFLKLITLCRDTRSQSWIDDEFITTYYKLFTQGYAHSLELYENNELIGGIYGLILGKVFFGESMVSIKKNASKVAMIKLCDLLKPYDFIIDCQVYNQHLEFMGAHNISRKEFLNILKEKCNQESGFKNFKDLIT | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 25142
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 2.3.2.6
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B9KCU7 | MQKSNLYSKLLKSPDDAPVFISEKLELDFISHAYSLGLFPWTSNPVTWWCPSPRMVLFPDEIHIQKSIKKALKTYEIRLDYDFALLIKHCSLRKKTWINQEFIETYTKLFEQNLAHSVEVYENDEFIGGLYGLIIGKVFFGESMISLKKDASKIALIKLCEILKPYDFLIDCQVPNEHLKFMGAKEMIKKDFLKILEKKVSLESGFENFQNLL | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 24856
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 2.3.2.6
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A4WSI3 | MTPPALTPRLLLRAYALGIFPMAESRDDPEIHWVDPRRRGIFPLDGFHISRSLARRIRRMDWTVTVNEDFAGTVRACADRDDTWINPTIFRLYVGLHALGHAHSLEVREGDALVGGVYGVTLGRAFFGESMFSRRTDASKVALAFLIDRLRAGGFTLFDTQFLTPHLASLGAIEIPRADYHRRLGEALAGKAEFAPPGYSPDPASVVQRSSQTS | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 23749
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 2.3.2.6
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Q8KFI0 | MIKVEDILRAYRHGFFPMADSREGTVSWCQPYQRAVVPLDSFRPSRSLRRVIGKKRFTIKINSVFEQVIRACSQPRSTGQETWLSEEIIKVFLKLHRLGVAHSVESWQDGELAGGLYGLSMGGAFFGESMFFFRSDASKVAFAWLVGYLKRKGYLLLDAQIMNPHLESLGAIEIPHEEYMVQLERALGKKISFV | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 22136
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 2.3.2.6
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Q3IH36 | MKKQLYQLSNTDIAFPPIECALDSPDGLLAIGGDLSLARLSNAYNNGIFPWFSEDEPIMWWSPSERGIVELDNFHISKSLRKHLKKHPVTVTINNAFIEVIEACCEQRIDTDGTWITSDMLTAYINAHNAGIAHSVEVWREGELAGGLYGIMQNGVFCGESMFHHQTNCSKLAMWALVNWLKRHNAHFIDCQLENPYLMSLGATVIPRPAFLAKLHAAQNYKVDPAMWIPQELNAIYE | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 26844
Sequence Length: 238
Subcellular Location: Cytoplasm
EC: 2.3.2.6
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Q4FUQ3 | MNNINDSSAIHITPETFVKQIRSLGRYNFPEPALVDPDGIGIVGIGGNLAPETLISAYAQGLFPWFNDDEPIAWWCPEPRCVMQPTDYQPSKSLRKQANNARWQLTLNQAFNEVIHACSLPRSNGLPEGEHTWIHDDMIEAYNELHAQGFAHSVEVWDDQGQLVGGLYGLKIGSIYFGESMFHIASNASKLAFWGLMRLCTQSNVTLVDCQLPNEHLMSLGAITLSRTEFLTQLDTLISNGSDAWHKNSHRPLAVSLLGNLQPWQLNP | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 29894
Sequence Length: 268
Subcellular Location: Cytoplasm
EC: 2.3.2.6
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A1SWY4 | MTLYIPELPINNTIFPDTSLALSDPDGLLAMGGDLSPQRIIKAYQQGIFPWFSDGQPILWWSPSQRAIIQPNLVHISSSMKKIISKNNFSLSINHAFHDVIDACAAPRGNQNETWITFDMIAAYQKLHQQGIAHSIEVWRDNKLVGGLYGVCIGSVFCGESMFSKEDNTSKIAFIALCQHFDKFKGQLIDCQILTKHLQSFGVQNESRDNFINYLNQYKNININKKCWDKQTIFIKNR | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 27072
Sequence Length: 238
Subcellular Location: Cytoplasm
EC: 2.3.2.6
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Q92QK2 | MKETRSKQPDITPDMLLRAYSIGLFPMADSADDPELFWVEPEIRGIIPLDRFHVSRSLAKAIRRRPFDIRFDTAFAEVMEGCAQPAPDRPTTWINDTIRSLYAALHNMGHAHSVEAWEGDALVGGLYGVSLGAAFFGESMFSRRTGASKICLVHLVERLRSKGFQLLDTQFTTEHLKSFGAVDVPKAQYEVLLAKAIASPNLEF | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 22784
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.3.2.6
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A5V9E5 | MKAIDPDLLLRAYSIGVFPMADSRAADDVYWVEPKKRGILPLDHFRLSRSLAKTIRSDRFAVTADRAFGEVVAECAAVTSQRPDTWINPAIEAAYADLHRRGHAHSIECWREGRLVGGLYGVRLGGAFFGESMFSRESNASKVALAWLVARLRAGGFRLLDCQFITDHLQSLGAIEVSRDDYVALLDVALGVVAGAGAAGGVAVAGAAAGWSAPDFFALDGGATDPDTRTVSGPISGCTIVQLLGQTS | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 26351
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.3.2.6
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Q6N734 | MASRDSSAASEITPDVLLRAYACGIFPMAESVDDPSLFWVEPDLRGIIPLGGFRVSSRLARTVRSDAFTVTVNRDFKAVIDGCAAPQPGRDDTWINRRIRELYIGLHDIGRCHSVEVWQDGDLAGGLYGVSLGRAFFGESMFHRARDASKVALVHLVARLLAGGYTLLDTQFVTDHLKSFGAIEVPRLRYRSLLDDALEGEASFAALPLDRPVTGTEALAIITRT | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 24622
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.3.2.6
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B3VI55 | MPIATSTGDNVLDFTVLGLNSGTSMDGIDCALCHFYQKTPDAPMEFELLEYGEVPLAQPIKQRVMRMILEDTTSPSELSEVNVILGEHFADAVRQFAAERNVDLSTIDAIASHGQTIWLLSMPEEGQVKSALTMAEGAILASRTGITSITDFRISDQAAGRQGAPLIAFFDALLLHHPTKLRACQNIGGIANVCFIPPDVDGRRTDEYYDFDTGPGNVFIDAVVRHFTNGEQEYDKDGAMGKRGKVDQELVDDFLKMPYFQLDPPKTTGREVFRDTLAHDLIRRAEAKGLSPDDIVATTTRITAQAIVDHYRRYAPSQEIDEIFMCGGGAYNPNIVEFIQQSYPNTKIMMLDEAGVPAGAKEAITFAWQGMEALVGRSIPVPTRVETRQHYVLGKVSPGLNYRSVMKKGMAFGGDAQQLPWVSEMIVKKKGKVITNNWA | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Levoglucosan kinase that catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP . In addition to the canonical kinase phosphotransfer reaction, the conversion requires cleavage of the 1,6-anhydro ring to allow ATP-dependent phosphorylation of the sugar O-6 atom .
Catalytic Activity: ATP + H2O + levoglucosan = ADP + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 48372
Sequence Length: 439
EC: 2.7.1.232
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Q03077 | MIILVLLISYSFGKTQDGKDQLSPNYPYGKMNKDVNFNKPFTSAVDSYQIQQYAENGVFSANQENYVRAKCKTCCRVIFASDYNYKTNTQFTDEDDKKGDERYVMDMEFDDKRSVRFRNGGYEQNILLRPLKQGNELQFFEFAPYRMYTSYAIPKRVHDIRGGANEGATLIIWPKNPPLSDAPGTRNQRFVYVHPYPTEWYPEYNSTTKYTQNGKTVIKTLKWPTYKRHFYLPYRLDVDLCYQARKATDGRSTWTGNKNLNTTSKSYQIIASRCSATEARQIFIPVFA | Function: Light subunit of a heterodimeric lectin; the heavy subunit binds galactose and N-acetyl-D-galactosamine of host glycoproteins and thus mediates adhesion to host cells.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33595
Sequence Length: 288
Subcellular Location: Cell membrane
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Q95M12 | MIWEFTVLLSLVLGTGAVPLEDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIVHRNGIPDEQIIVMMYDDIANSEDNPTPGIVINRPNGSDVYQGVLKDYTGEDVTPKNFLAVLRGDAEAVKGVGSGKVLKSGPRDHVFVYFTDHGATGILVFPNEDLHVKDLNETIRYMYEHKMYQKMVFYIEACESGSMMNHLPPDINVYATTAANPRESSYACYYDEQRSTFLGDWYSVNWMEDSDVEDLTKETLHKQYQLVKSHTNTSHVMQYGNKSISAMKLMQFQGLKHQASSPISLPAVSRLDLTPSPEVPLSIMKRKLMSTNDLQESRRLVQKIDRHLEARNIIEKSVRKIVTLVSGSAAEVDRLLSQRAPLTEHACYQTAVSHFRSHCFNWHNPTYEYALRHLYVLVNLCENPYPIDRIKLSMNKVCHGYY | Function: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity). Required for normal lysosomal protein degradation in renal proximal tubules. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.
PTM: Activated by autocatalytic processing at pH 4.
Catalytic Activity: Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
Sequence Mass (Da): 49284
Sequence Length: 433
Domain: In the zymogen form, the uncleaved propeptide blocks access to the active site.
Subcellular Location: Lysosome
EC: 3.4.22.34
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Q99538 | MVWKVAVFLSVALGIGAVPIDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIVVMMYDDIAYSEDNPTPGIVINRPNGTDVYQGVPKDYTGEDVTPQNFLAVLRGDAEAVKGIGSGKVLKSGPQDHVFIYFTDHGSTGILVFPNEDLHVKDLNETIHYMYKHKMYRKMVFYIEACESGSMMNHLPDNINVYATTAANPRESSYACYYDEKRSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKTISTMKVMQFQGMKRKASSPVPLPPVTHLDLTPSPDVPLTIMKRKLMNTNDLEESRQLTEEIQRHLDARHLIEKSVRKIVSLLAASEAEVEQLLSERAPLTGHSCYPEALLHFRTHCFNWHSPTYEYALRHLYVLVNLCEKPYPLHRIKLSMDHVCLGHY | Function: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity). May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.
PTM: Glycosylated.
Catalytic Activity: Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
Sequence Mass (Da): 49411
Sequence Length: 433
Domain: In the zymogen form, the uncleaved propeptide blocks access to the active site.
Subcellular Location: Lysosome
EC: 3.4.22.34
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O89017 | MTWRVAVLLSLVLGAGAVPVGVDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANSEENPTPGVVINRPNGTDVYKGVLKDYTGEDVTPENFLAVLRGDAEAVKGKGSGKVLKSGPRDHVFIYFTDHGATGILVFPNDDLHVKDLNKTIRYMYEHKMYQKMVFYIEACESGSMMNHLPDDINVYATTAANPKESSYACYYDEERGTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKSISTMKVMQFQGMKHRASSPISLPPVTHLDLTPSPDVPLTILKRKLLRTNDVKESQNLIGQIQQFLDARHVIEKSVHKIVSLLAGFGETAERHLSERTMLTAHDCYQEAVTHFRTHCFNWHSVTYEHALRYLYVLANLCEAPYPIDRIEMAMDKVCLSHY | Function: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation.
PTM: Glycosylated.
Catalytic Activity: Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
Sequence Mass (Da): 49373
Sequence Length: 435
Domain: In the zymogen form, the uncleaved propeptide blocks access to the active site.
Subcellular Location: Lysosome
EC: 3.4.22.34
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P39400 | MSTMNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIADLKNGQQVAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPADGIDPQAAALIEPFAISAHAVRRAAIAPGEQVLVVGAGPIGLGAAAIAKADGAQVVVADTSPARREHVATRLELPLLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATLAETYERDVINNRELIKGVITF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the oxidation of L-galactonate to D-tagaturonate. Required for growth on L-galactonate as the sole carbon source. In vitro, can also use L-gulonate.
Catalytic Activity: L-galactonate + NAD(+) = H(+) + keto-D-tagaturonate + NADH
Sequence Mass (Da): 36448
Sequence Length: 340
EC: 1.1.1.414
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P39398 | MEKENITIDPRSSFTPSSSADIPVPPDGLVQRSTRIKRIQTTAMLLLFFAAVINYLDRSSLSVANLTIREELGLSATEIGALLSVFSLAYGIAQLPCGPLLDRKGPRLMLGLGMFFWSLFQAMSGMVHNFTQFVLVRIGMGIGEAPMNPCGVKVINDWFNIKERGRPMGFFNAASTIGVAVSPPILAAMMLVMGWRGMFITIGVLGIFLAIGWYMLYRNREHVELTAVEQAYLNAGSVNARRDPLSFAEWRSLFRNRTMWGMMLGFSGINYTAWLYLAWLPGYLQTAYNLDLKSTGLMAAIPFLFGAAGMLVNGYVTDWLVKGGMAPIKSRKICIIAGMFCSAAFTLIVPQATTSMTAVLLIGMALFCIHFAGTSCWGLIHVAVASRMTASVGSIQNFASFICASFAPIITGFIVDTTHSFRLALIICGCVTAAGALAYIFLVRQPINDPRKD | Function: Probably responsible for the transport of L-galactonate from the periplasm across the inner membrane. Is essential for growth on L-galactonate as the sole carbon source.
Catalytic Activity: H(+)(in) + L-galactonate(in) = H(+)(out) + L-galactonate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49440
Sequence Length: 453
Subcellular Location: Cell inner membrane
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Q8L3C7 | MTTDTARRHTGAERANEMTYEQLARELLLVGPAPTNEDLKLRYLDVLIDNGLNPPGPPKRILIVGAGIAGLVAGDLLTRAGHDVTILEANANRVGGRIKTFHAKKGEPSPFADPAQYAEAGAMRLPSFHPLTLALIDKLGLKRRLFFNVDIDPQTGNQDAPVPPVFYKSFKDGKTWTNGAPSPEFKEPDKRNHTWIRTNREQVRRAQYATDPSSINEGFHLTGCETRLTVSDMVNQALEPVRDYYSVKQDDGTRVNKPFKEWLAGWADVVRDFDGYSMGRFLREYAEFSDEAVEAIGTIENMTSRLHLAFFHSFLGRSDIDPRATYWEIEGGSRMLPETLAKDLRDQIVMGQRMVRLEYYDPGRDGHHGELTGPGGPAVAIQTVPEGEPYAATQTWTGDLAIVTIPFSSLRFVKVTPPFSYKKRRAVIETHYDQATKVLLEFSRRWWEFTEADWKRELDAIAPGLYDYYQQWGEDDAEAALALPQSVRNLPTGLLGAHPSVDESRIGEEQVEYYRNSELRGGVRPATNAYGGGSTTDNPNRFMYYPSHPVPGTQGGVVLAAYSWSDDAARWDSFDDAERYGYALENLQSVHGRRIEVFYTGAGQTQSWLRDPYACGEAAVYTPHQMTAFHLDVVRPEGPVYFAGEHVSLKHAWIEGAVETAVRAAIAVNEAPVGDTGVTAAAGRRGAAAATEPMREEALTS | Function: Catalyzes the oxidative deamination of L-glutamate to 2-ketoglutarate along with the production of ammonia and hydrogen peroxide . Shows strict substrate specificity for L-glutamate, and exhibits only very weak activity with L-aspartate (Ref.2).
PTM: The precursor form is proteolytically cleaved by an endopeptidase into alpha, beta and gamma chains, which form the stable mature enzyme . Activation by proteolysis occurs after secretion (Probable).
Catalytic Activity: H2O + L-glutamate + O2 = 2-oxoglutarate + H2O2 + NH4(+)
Sequence Mass (Da): 77891
Sequence Length: 701
Domain: Contains a deeply buried active site and two entrances from the surface of the protein into the active site.
Subcellular Location: Secreted
EC: 1.4.3.11
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D6A5I3 | MTEDHAVVRSDGGLSRRSFAAVAGTATVATALTSGVAAALPAPAASGDSRGADFDRCLAVARALLVLDSDDRPLVPRYQSVLQKGLPAQRRTRPKNVLVIGAGPAGLVAAWLLKRAGHRVTVLEANGNRAGGRVKTFRSGGHERAEQPFADPRQYAEAGAMRIPGSHPLVMELIDQFELKKRRFHYVDVDSEGRPANRTWIHVNGIRVRRADYARAPRRVNRSFGVPRAHWDTPAAAILRSVLDPVRDEFSRVGRDGKRVDKPLPERLQGWARVVQRFGDWSMFRFLTEHAGLDERTIDLIGTLENLTSRLPLSFIHSFIGSSLISPDTPFYELEGGTAVLPDALLERVRKDVRFDRRVTRIQYHHPDRPSPDVEQVRSKGPHVWVDTVSEGRDGPVVREQFTADVAVVTVPFSGLRHVQIAPPLSYGKRRAVCELHYDSATKVLLEFSRRWWEFDEADWKRELRAVDPGLYDAYRTGRAAADGSLLGAHPSVPAGHITAGQRTHYAANRAVARDQPEAVDVVGGGSVSDNANRFMFHPSHPVPGSAGGVVLASYSWADDALRWDSLDDEARYPHALCGLQQVYGQRIEVFYTGAGRTQSWLRDPYAYGEASVLLPGQHTELLSAIPVAEGPLHFAGDHTSVKPAWIEGAVESAVRAALEIHTA | Function: Catalyzes the oxidative deamination of L-glutamate to 2-ketoglutarate along with the production of ammonia and hydrogen peroxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: H2O + L-glutamate + O2 = 2-oxoglutarate + H2O2 + NH4(+)
Sequence Mass (Da): 73021
Sequence Length: 664
Subcellular Location: Secreted
EC: 1.4.3.11
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E7FE13 | MALLAVRMLVLGLCVGGQAAAAGEGQSTPATCSPLCRCDEDGGADCSGRGLTSVPTGLSAFTYYLDISMNNITELPANVFRNLPYLEELRLAGNDLAFIHPEALSGLHQLKVLMLQNNQLKTVPSAALKNLNALQSLRLDANHITSVPEDSFEGLQQLRHLWLDDNSLTEVPISPLQHQSNLQALTLALNRITHIPDNAFANLSSLVVLHLHNNRIQEIGKNCFNGLDNLETLDLNFNNLKIFPEAIQMLPKLKELGFHSNNIASIPEGAFCRNSLLRTIHLFDNPLSFVGTTAFQNLSDLHSLMLRGASMMQDFPSLTGTINLESLTLTGTKIRSIPADLCEDLTVLRTVDLSYNDIEDLPSFQGCVRLQDINLQHNQIKQIDRGTFQGMTSLRVLDLSRNQIKFIHRDAFLSLSALTNLDLSLNSLASVPTAGLSALNQLKLTGNMELRNGLMSKTLPKLRSITVPYAYQCCAFVAYDSAVNPAEDDERRNAFGGEEDMERIPMVMHCSPLPGAFKPCEHLLGSWMIRLTVWFICLVALLFNCLVLAATFSPRTSSLSPSRFLVALLASANLLTGVYVAALTLLDTVTWGSFAEYGVWWETGAGCQVVGFLAVFSSEWAVLLLALAAVERCLAVRALMGKAGALRSRGERRERRRRFAIAALLLGLVSVAAACLSLYHGSAMGSPLCLPFSEGSSPGLGFTVALVLMNTLAYLLSAVVYTRLYCRLGRAQLADPEQAGSVRHIAWLIFTNCIFFCPVAAFSFAPLLAGTSNAVGGPEMAKSVTLIFFPLSACLNPVLYVCFSPSFRYDWLHLRGRGRTGGCGRLVAKTVTKGTVAGGSPVSDDGEGLSSDCGMYTKLHGDSRGMCEHCDAALHIRTSSSSGSSSSSACRHLVKSHSCPALMGNVPQCLSSEGYWPDTGTLSAQSEYGDEGDSFVSDSSEQVQACGRACFCQSRGLPLVHYSYNIPRMTD | Function: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May play a role in regulating the circadian rhythms of plasma lipids. Required for proper development of GnRH neurons (gonadotropin-releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105210
Sequence Length: 971
Subcellular Location: Cell membrane
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A2ARI4 | MPGPLRLLCFFALGLLGSAGPSGAAPPLCAAPCSCDGDRRVDCSGKGLTAVPEGLSAFTQALDISMNNITQLPEDAFKNFPFLEELQLAGNDLSFIHPKALSGLKELKVLTLQNNQLKTVPSEAIRGLSALQSLRLDANHITSVPEDSFEGLVQLRHLWLDDNILTEVPVRPLSNLPTLQALTLALNNISSIPDFAFTNLSSLVVLHLHNNKIKSLSQHCFDGLDNLETLDLNYNNLDEFPQAIKALPSLKELGFHSNSISVIPDGAFAGNPLLRTIHLYDNPLSFVGNSAFHNLSDLHSLVIRGASLVQWFPNLAGTVHLESLTLTGTKISSIPDDLCQNQKMLRTLDLSYNDIRDLPSFNGCRALEEISLQRNQISLIKETTFQGLTSLRILDLSRNLIREIHSGAFAKLGTITNLDVSFNELTSFPTEGLNGLNQLKLVGNFQLKDALAARDFANLRSLSVPYAYQCCAFWGCDSYANLNTEDNSPQDHSVTKEKGATDAANATSTAESEEHSQIIIHCTPSTGAFKPCEYLLGSWMIRLTVWFIFLVALLFNLLVILTVFASCSSLPASKLFIGLISVSNLLMGIYTGILTFLDAVSWGRFAEFGIWWETGSGCKVAGSLAVFSSESAVFLLTLAAVERSVFAKDVMKNGKSSHLRQFQVAALVALLGAAIAGCFPLFHGGQYSASPLCLPFPTGETPSLGFTVTLVLLNSLAFLLMAIIYTKLYCNLEKEDPSENSQSSMIKHVAWLIFTNCIFFCPVAFFSFAPLITAISISPEIMKSVTLIFFPLPACLNPVLYVFFNPKFKDDWKLLKRRVTRKHGSVSVSISSQGGCGEQDFYYDCGMYSHLQGNLTVCDCCESFLLTKPVSCKHLIKSHSCPVLTVASCQRPEAYWSDCGTQSAHSDYADEEDSFVSDSSDQVQACGRACFYQSRGFPLVRYAYNLPRVRD | Function: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Its function as activator of the Wnt signaling pathway is required for the development of various organs, including liver, kidney, intestine, bone, reproductive tract and eye. May also act as a receptor for norrin (NDP), such results however require additional confirmation in vivo. Required during spermatogenesis to activate the Wnt signaling pathway in peritubular myoid cells. Required for the maintenance of intestinal stem cells and Paneth cell differentiation in postnatal intestinal crypts. Acts as a regulator of bone formation and remodeling. Involved in kidney development; required for maintaining the ureteric bud in an undifferentiated state. Involved in the development of the anterior segment of the eye. Required during erythropoiesis. Also acts as a negative regulator of innate immunity by inhibiting TLR2/TLR4 associated pattern-recognition and pro-inflammatory cytokine production. Plays an important role in regulating the circadian rhythms of plasma lipids, partially through regulating the rhythmic expression of MTTP . Required for proper development of GnRH neurons (gonadotropin-releasing hormone expressing neurons) that control the release of reproductive hormones from the pituitary gland .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 104150
Sequence Length: 951
Subcellular Location: Cell membrane
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Q9FDM1 | MPFAFIEQMKSVIHFDALGLSPIAFDLGVWHLFGLTLHPLIHWYALAYITGILLAWRYVLFLLKQPGTPMKPEQTDDLVFWSTLGILVGGRLAYVLFYQPAILENPLEIFKLWEGGMSYHGGMIGVFLAIWWVKTTNHLSWLRIADYIGCAAPIGLFLGRLANFVNGELWGRPSTMPWAVIFPQAGALPRHPSQLYEAGLEGILLFAFLNYQFFATKARLHPGKLAGFFLVGYGLSRFIVEWFREPDVQLGTLSWGLTMGQTLTIPMVIAGLWLIITSKKREISL | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32173
Sequence Length: 285
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell inner membrane
EC: 2.5.1.145
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Q8W593 | MVRIIPMAASSIRPSLACFSDSPRFPISLLSRNLSRTLHVPQSQLFGLTSHKLLRRSVNCLGVAESGKAAQATTQDDLLTWVKNDKRRMLHVVYRVGDMDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSHFVIELTYNYGVDKYDIGAGFGHFGIAVDDVAKTVELVKAKGGKVSREPGPVKGGKTVIAFIEDPDGYKFELLERGPTPEPLCQVMLRVGDLDRAIKFYEKAFGMELLRTRDNPEYKYTIAMMGYGPEDKFPVLELTYNYGVTEYDKGNAYAQIAIGTDDVYKTAEAIKLFGGKITREPGPLPGISTKITACLDPDGWKSVFVDNIDFLKELE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 39167
Sequence Length: 350
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Subcellular Location: Plastid
EC: 4.4.1.5
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Q8H0V3 | MASEARESPANNPGLSTNRDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTTAPTDPTERTVWTFGQPATIELTHNWGTESDPEFKGYHNGNSEPRGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAFIKDPDGYWIEIFDLKTIGTTTVNAA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 20848
Sequence Length: 185
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
EC: 4.4.1.5
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P0AC82 | MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN | Cofactor: Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 14920
Sequence Length: 135
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
EC: 4.4.1.5
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P44638 | MQILHTMLRVGDLDRSIKFYQDVLGMRLLRTSENPEYKYTLAFLGYEDGESAAEIELTYNWGVDKYEHGTAYGHIAIGVDDIYATCEAVRASGGNVTREAGPVKGGSTVIAFVEDPDGYKIEFIENKSTKSGLGN | Cofactor: Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 14893
Sequence Length: 135
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
EC: 4.4.1.5
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Q04760 | MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM | Cofactor: Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione . Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B . Required for normal osteoclastogenesis (By similarity).
PTM: Glutathionylation at Cys-139 inhibits enzyme activity.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 20778
Sequence Length: 184
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
EC: 4.4.1.5
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P0A0T2 | MRLLHTMLRVGNLEKSLDFYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGNAYGHIAVEVDDAYEACERVKRQGGNVVREAGPMKHGTTVIAFVEDPDGYKIEFIQKKSGDDSVAYQTA | Cofactor: Binds 1 nickel ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 15669
Sequence Length: 138
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
EC: 4.4.1.5
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Q948T6 | MASGSEAEKSPEVVLEWPKKDKKRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGVDKYDIGAGFGHFAIATEDVYKLAEKIKSSCCCKITREPGPVKGGSTVIAFAQDPDGYMFELIQRGPTPEPLCQVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVAIGTEDVYKSAEAVELVTKELGGKILRQPGPLPGLNTKIASFLDPDGWKVVLVDNADFLKELQ | Cofactor: Binds 1 nickel ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (By similarity). Involved in the detoxifiation of methylglyoxal. Can functionally complement growth defect of a yeast mutant lacking GLY I. Involved in abiotic stress response. Over-expression of GLYI-11 in tobacco increases tolerance to osmotic, oxidative and salt stresses .
PTM: Phosphorylated after gibberellin treatment.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 32553
Sequence Length: 291
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
EC: 4.4.1.5
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P84719 | ITACLDPDGWKEPGPLPGISTK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 2296
Sequence Length: 22
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
EC: 4.4.1.5
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Q9HU72 | MSFNTEVQPGICMEPDAITQEYVFNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEVPDAVDERQRYTFGRQSVLELTHNWGSESDDSQYHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFVKPLDRGMKNVAFISDPDGYWVEIVQASLNGEMGRG | Cofactor: Binds 1 nickel or zinc ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 20215
Sequence Length: 176
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
EC: 4.4.1.5
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P16635 | MSLNDLNTLPGVTAQADPATAQFVFNHTMLRVKDIEKSLDFYTRVLGFKLVDKRDFVEAKFSLYFLALVDPATIPADDDARHQWMKSIPGVLELTHNHGTERDADFAYHHGNTDPRGFGHICVSVPDVVAACERFEALQVPFQKRLSDGRMNHLAFIKDPDGYWVEVIQPTPL | Cofactor: Binds 1 nickel or zinc ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 19540
Sequence Length: 173
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
EC: 4.4.1.5
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P0A1Q3 | MRLLHTMLRVGDLQRSIAFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVESYDMGNAYGHIALSVDNAAEACERIRQNGGNVTREAGPVKGGSTIIAFVEDPDGYKIELIEAKDAGRGLGN | Cofactor: Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 14822
Sequence Length: 135
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
EC: 4.4.1.5
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Q810M6 | MAGRGGTGAAEYGEEGEEEEEEEAREGGAEGSPGSKLPPIVGTASELAKRKVKKKKKKKKTKGSGKGDADKHHSRGRKNQPLSSSFHDILNPHKDHGLRAEPRDKEENRQTLPYSYSINHPCFAEIEDTLSSQINESLRWDGILTDPEAEKERIRIYKLNRRKRYRLMALKCFHSDPCVEESVENLPYLSDKDCSPCSKQPSSKGDHAHSYFEASKLLHPELATTVAE | Function: Participates in nucleolar liquid-liquid phase separation (LLPS) through its N-terminal intrinsically disordered region (IDR) . May be involved in ATE1-mediated N-terminal arginylation .
PTM: Post-translationally modified by JMJD6 lysyl-hydroxylase activity at its Lys-rich domain, which inhibits its self-association and nucleolar localization.
Sequence Mass (Da): 25512
Sequence Length: 228
Domain: The N-terminal intrinsically disordered region (IDR) facilitates its liquid-liquid phase separation (LLPS) in the nucleolus . In the IDR, the lysine-rich domain mediates self-association and targeting to the nucleolus .
Subcellular Location: Nucleus
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Q03974 | MSAIENIVISMENATERRKHITKQFESKKLSFSFFNAYTYQSINQSINQSINQSINQSINQSINQSINQSNSILHNIEESRILTKGEKGCLISHFLLWNKCVNENFEYLKIFEDDVILGENAEVFLNQNEWLKTRFDFNDIFIIRLETFLQPVKLEKQTKIPPFNSRNFDILKSTHWGTAGYIISQGAAKYVIEYLKNIPSDEIVAVDELIFNKLVDVDNYIVYQLNPAICIQELQANQSKSVLTSGLEKERQKRSKIRKKKTLKQRLTRIKENIIRALNRKKWKEQQRIKEMQGKEIVRFM | Function: Involved in extracellular lipooligosaccharide (LOS) biosynthesis and virulence expression. Involved in the synthesis of the oligosaccharide moiety of the LOS molecule by adding GalNAc.
Sequence Mass (Da): 35490
Sequence Length: 302
Domain: Between 2 and 7 copies of the SINQ repeats are to be found in different strains; these are thought to serve to generate phase-variable expression of this gene. The (SINQ)n peptide may form a random coiled structure that permits appropriate interactions between the N- and C-terminal domains of the protein.
EC: 2.-.-.-
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P46320 | MTKGLKIVTIGGGSSYTPELVEGFIKRYDELPVRELWLVDIPEGEEKLNIVGTLAKRMVEKAGVPIDIHLTLDRRKALKDADFVTTQFRVGLLQARAKDERIPLKYGVIGQETNGPGGLFKGLRTIPVILEIAKDIEELCPNAWLVNFTNPAGMVTEALLRYSNLKKVVGLCNVPIGIKMGVAKALDVDVDRVEVQFAGLNHMVFGLDVFLDGVSVKEQVIEAMGDPKNAMTMKNISGAEWEPDFLKALNVIPCGYHRYYFKTKEMLEHELEASQTEGTRAEVVQKVEKELFELYKDPNLAIKPPQLEKRGGAYYSDAACNLISSIYNDKHDIQPVNTINNGAIASIPDDSAVEVNCVMTKTGPKPIAVGDLPVSVRGLVQQIKSFERVAAEAAVTGDYQTALLAMTINPLVPSDTVAKQILDEMLEAHKAYLPQFFNKIEA | Function: Hydrolyzes phospho-beta-glucosides.
Catalytic Activity: 6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate
Sequence Mass (Da): 48711
Sequence Length: 442
EC: 3.2.1.86
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J3SDX8 | MWRLIIIAILFQGLVNSAMLERRKRGVDPETAMNISEIILFRGYPSEEYEVVTGDGYILCLNRIPYGKISQKTKEPKPAVFLQHGLLADGSNWVTNLDYNSLGFALADAGFDVWLGNSRGNTWSQKHINYTIKQKEFWMFSFNEMAMYDIPASVNFVLNKTGQEQLFYVGHSQGTTIGFIAFSVLPELAKKIKMFFGLAPVMTVKFSSGGLVKLGELPEFLLKEIFGTKQIFPQNAVIKWLATHVCGQVLIDELCGNFFFLLCGFNEKNLNMSRVEIYSTHCPAGTSVQNMLHWSQAVKSGEVRAFDWGSRKENMAHYKQPTPPPYKMERMLVPTALWTGGHDWLSDRKDIAILLTLIPNLIYHKEIPEWEHLDFIWGLDAPQRMFRDMIQMMHKVQYAH | Function: In physiological conditions, is crucial for intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. In venom, the biological contribution is unknown.
Catalytic Activity: a sterol ester + H2O = a fatty acid + a sterol + H(+)
Sequence Mass (Da): 45807
Sequence Length: 400
Subcellular Location: Secreted
EC: 3.1.1.13
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Q6DB58 | MWLRNSVFLIIIVVGGIGGFPAVAAVCPDWDNTRASKEIDALRQQLEQWDDVYYTEGKSPIEDDVYDQLREQLNQWSQCFQPQNVIPARLPDNGKQPHPVAHTGLKKLSDRVQLVQWIVQREDLWVQPKVDGVAVTLVYQHGKLVSAVSRGNGLQGEDWTEKARLIPDIPHLLSGAPSSFVLQGELFLKMTDHRQYAQGGVNARSIVAGEMRRHQPSPVLSQIGLFVWEWPDGPKAMPERLDKLKEMGFAMTADYTHAIESFADVEKWRDHWYHSPLPFVTDGVVIRQTKEPQGRYWRNTSADWAIAWKYPPVHQVAEVVDVAFSVGRTGKVAVVLKISPLKLDDKSVSRVNVGSLSRWKQWDVLPGDRVSVSLAGQGIPRLDNVVWRGTERPVIVSPDEHNFHAFSCFRYSVVCQQQFLARLVWLSGEHGLNLAGMRDGMWLRLMQHDLLGDVLSWLYLTEAQLNAVNGMGDKRARDIYMSLQSARQKSLSHWLLALGIPVPRSAISALNNVNWLALQQRTAQQWRQFSGIGERRAEEIMAFLNHPIVMELIARLDLEGIHR | Function: Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 63888
Sequence Length: 563
EC: 6.5.1.2
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Q7N9N4 | MLNLLILILFIVFSSPIVAAEIFVSNTEKNCPEWSQDKLQRETNSLMQQMAHWDQLYRQKGISEIDDEVYDQLMSELTHWQFCLKQAPHSDFPVEVFPDNKLVHPVAHTGLSKLKDKQEINRWLHGRLPVWLQPKIDGVAVTLVYQNGKLVSLISRGNGAEGVNWTAKSRYIPDIPQNIENAPPDLVLQGELFLHKEEHRQQLLGSDGARNRVAGLMMRKDHSSELKQIGLFIWSWPDGPAEMESKLRKLADMGFPLALRYSHKIEEPEQVQKLRMHYFEQPMLFATDGIVLKQEIEPKGNQWRSGSNSWAVAWKHPLRHQVTQVREVNFTIGRTGKISVVLGLDKVKLDDRQISRVNIGSVRRWRQLDVLPGDRVTLTLAGHGIPKLAQVVWRIKERQDIQPPDKQHYHALSCLTLTVGCEQQFNARLKWLGENLQMTGVSSGSWAMLTERKLVTDLTGWLALSAQQIAALPGIGDKRAQAIYSQFSKAKNQPFSYWMKGIGVPYMDKLSDNVYHWQQLEQKLAAAQLKQQLTVGQLKKLSDFVSDAQIKAIAEKLSVAGITGFDRENGVVVNPADMAQ | Function: Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 65926
Sequence Length: 580
EC: 6.5.1.2
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Q2Q1W2 | MASFPETDFQICLLCKEMCGSPAPLSSNSSASSSSSQTSTSSGGGGGGPGAAARRLHVLPCLHAFCRPCLEAHRLPAAGGGAAGEPLKLRCPVCDQKVVLAEAAGMDALPSSAFLLSNLLDAVVATADEPPPKNGRAGAPAGAGGHSNHRHHAHHAHPRASASAPPLPQAPQPPAPSRSAPGGPAASPSALLLRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPGAAAAAQQLGLGPPFPGPPFSILSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTMGRHGGHSFIYLQEALQDSRALTIQLLADAQQGRQAIQLSIEQAQTVAEQVEMKAKVVQSEVKAVTARHKKALEERECELLWKVEKIRQVKAKSLYLQVEKLRQNLNKLESTISAVQQVLEEGRALDILLARDRMLAQVQELKTVRSLLQPQEDDRVMFTPPDQALYLAIKSFGFVSSGAFAPLTKATGDGLKRALQGKVASFTVIGYDHDGEPRLSGGDLMSAVVLGPDGNLFGAEVSDQQNGTYVVSYRPQLEGEHLVSVTLCNQHIENSPFKVVVKSGRSYVGIGLPGLSFGSEGDSDGKLCRPWGVSVDKEGYIIVADRSNNRIQVFKPCGAFHHKFGTLGSRPGQFDRPAGVACDASRRIVVADKDNHRIQIFTFEGQFLLKFGEKGTKNGQFNYPWDVAVNSEGKILVSDTRNHRIQLFGPDGVFLNKYGFEGALWKHFDSPRGVAFNHEGHLVVTDFNNHRLLVIHPDCQSARFLGSEGTGNGQFLRPQGVAVDQEGRIIVADSRNHRVQMFESNGSFLCKFGAQGSGFGQMDRPSGIAITPDGMIVVVDFGNNRILVF | Function: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (Probable). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism . Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity). Specific regulator of miRNA biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression .
PTM: Autoubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 93385
Sequence Length: 868
Domain: The NHL domain, containing the 6 NHL repeats, is necessary and sufficient to target RNA but not to repress mRNA. The minimal region needed to execute repression consists of the coiled coil domain and the Filamin repeat. The RING-type domain is dispensable for mRNA repression.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q1PSW8 | MASFPETDFQICLLCKEMCGSPAPLSSNSSASSSSSQTSTSSAGGGGPGAAARRLHVLPCLHAFCRPCLEAHRLPAPGGAGPAEALKLRCPVCDQKVVLAEAAGMDALPSSAFLLSNLLDAVVATAEEPPPKNGRAGGGPGGAGGHSNHRHHAHHPAQRAAAPAPQPPPGPAASPGSLLMRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPAAASAAQQLGLGPPFAGAPFSILSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTLGRHGGHSFAYLQDALQDSRALTIQLLADAQQGRQALQLSIEQAQTVAEQVEMKAKVVQSEVKAVTARHKKALEDRECELLWKVEKIRQVKAKSLFLQVEKLRQSLSKLESTISAVQQVLEEGRALDILLARDRMLAQVQELKTIRGLLQPQEDDRIMFTPPDQALYLALKSIGFVSSGAFAPLTKATGDGIKRALQGKVASFTVMGYDHDGEPRHSGGDLMSVVVLGPDGNLFGAEVSDQQNGTYIVSYRPQLEGEHLVSVTLYNQHIENSPFKVVVKSGRSYVGIGLPGLSFGSEGDGEGKLCRPWGVSVDKEGFIIVADRSNNRIQVFKPCGSFHHKFGTLGSRPGQFDRPAGVACDASRRIIVADKDNHRIQIFTFEGQFLLKFGEKGTKNGQFNYPWDVAVNSEGKILVSDTRNHRIQLFGPDGVFLNKYGFEGSLWKHFDSPRGVAFNNEGHLVVTDFNNHRLLVIHPDCQSARFLGSEGSGNGQFLRPQGVAVDQEGRIIVADSRNHRVQMFEANGSFLCKFGAQGSGFGQMDRPSGIAVTPDGLIVVVDFGNNRILIF | Function: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance . Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A. Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression . In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism . Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 . Specific regulator of miRNA biogenesis. miRNA Binds MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (By similarity).
PTM: Autoubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 92054
Sequence Length: 855
Domain: The NHL domain, containing the 6 NHL repeats, is necessary and sufficient to target RNA but not to repress mRNA. The minimal region needed to execute repression consists of the coiled coil domain and the Filamin repeat. The RING-type domain is dispensable for mRNA repression.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q27886 | MRAAPFDFFFQSTALSTFFILCSLATNEIPTISGAPAGKIVQPPKPNILKQGCPSDLLHSRALRSIQLACRTHPATVISAFEGVQEGLQNCANRLRFQQWDCSEAGNIMHDPPLLRQGFRESSLIWALSSASAAWGVATACAQGWIDDCACNNQMGQNEYEFGGCTHGVQHGITASRKLLTKVGAVNTLLRKVEKHNLKAGRLAIKKTLISSCKCHGVSGSCQQKTCWKRTATLEHITDYLVEKYARAKLYTDDSVVKTTDLIYLEASPDVCKAKSVAGRVCAWRNETHTQGDCDRLCCGNGFSIRHEVVRVKCDCEFVWCCNLVCKDCIQHRWISTCNGTPPKSLIF | Function: Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Affects male tail development, vulval precursor cell specification and egg laying. Involved in morphogenesis by influencing polarity of asymmetric cell divisions of the B, U, and F cells in the male, and the T cell in males and hermaphrodites. Controls spindle orientation in B-gamma cell division during male copulatory spicule development. Involved in specification of the P7.p lineage during vulval development. Has a role in providing polarity and default lin-17 localization in axon development and positioning of neuromuscular synapses in DA9 regions by negatively regulating synaptogenesis. Plays a role in motorneuron development by promoting the extension of the anterior neurite of ventral D-type GABAergic motorneurons along the anterior-posterior axis of the ventral nerve cord . Positively regulates cilium position and dendrite morphogenesis in postembryonic PQR gas-sensing neurons . This is likely through regulating the localization of grdn-1 to the distal dendrites of PQR sensory neurons .
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 38381
Sequence Length: 348
Subcellular Location: Secreted
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Q95QD7 | MNQGEIVYQDDDDYYDESEIYDNYEEGAEFIEVNGQLVPHNPNLQAQQNRPGTSSMIQQHNRSMEVNQGLVKDEPIDTSSHRVYVPPPRPVQRKLFQPGPSTPGSSQYTVRNLSNLSGSPSMYDRQPASLPRTVQPMGLEMGNSEQRKVYIDMKDHVSHIRLKTKKKVFAPGQRKPCNCTKSQCLKLYCDCFANGEFCRDCNCKDCHNNIEYDSQRSKAIRQSLERNPNAFKPKIGIARGGITDIERLHQKGCHCKKSGCLKNYCECYEAKVPCTDRCKCKGCQNTETYRMTRYKNSGGAVSNTNALMSLTNASSTATPDSGPGSVVTDEHGDDYEDMLLSHKPKVEMDPRRFPWYYMTDEVVEAATMCMVAQAEEALNYEKVQTEDEKLINMEKLVLREFGRCLEQMITNTTELTQDLDAAPTDDIPGPSTSTS | Function: Synthetic multivulva class B (synMuvB) protein. SynMuvB proteins are required to repress the induction of vulval development by Ras signaling and probably act by forming the multiprotein DRM complex that repress transcription.
Sequence Mass (Da): 49109
Sequence Length: 435
Domain: The CRC domain mediates DNA-binding. It contains two CXC subdomains (joined by a flexible linker) which are both required for efficient association with target DNA. Each CXC subdomain coordinates three Zn(2+) ions.
Subcellular Location: Nucleus
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Q0BSW6 | MVTRVLIDHRQGGRHEAGVRHPEKQHRPDNPSQPKPSWIRVKAPNHPVYHQTQALMRENRLTTVCEEAACPNIGECWSQRHATMMIMGDTCTRACSFCNVKTGLPHALDGDEPARVADAVARLGLRHVVITSVDRDDLNDGGAAHIAAVIKAVRLAAPETTIEVLTPDFLRKPGAAETVAEARPDVFNHNLETVPRLYPAIRPGARYFQSLRLLDQVKRLDPSIFTKSGLMVGLGEDRAEIAQVMDDLRIAEVDFITLGQYLQPTPKHAAVDRFVTPDEFSDYASMARSKGFLMVSSSPLTRSSYHADADFAALRAARMEQQQRIA | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36155
Sequence Length: 326
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.8.1.8
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B9LR22 | MQRGRRKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWSGRDGPGTATFMLMGDRCSRGCNFCDVETGGMKSLDSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAGPDVIAHNVETVERLQWPVRDRRADYEQSLAVLDRVGRESDIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQPSRSHLDVFEYVHPDVFETWRAVAEREFDFLYCASGPMVRSSYKAGELFVEALLREGRSPEDARRHARAAGGD | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 35157
Sequence Length: 312
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.8.1.8
|
Q31F42 | MKARNESMSKGEYKTKSLKNRPDPTQPKLKKPSWIKAKLPSAKHIGRVKELKQVLREQGLNSVCEEASCPNLGECFGHGTATFMIMGHICTRKCPFCDVTHGRPNPLNQDEPRHLAKTIHAMNLNYVVITSVDRDDLRDGGATHFKNCTQAIRDKMPDIQIETLVPDFRGRLTVALDILAQQAPDVLNHNLETVPRLYEEARPGADYQASLDLLKRFKQMVPETKTKSGLMVGLGETFDEILQVMRDLRAHDVEMLTVGQYLQPSDFHLAVQRYWTPEEFKQLEQAGMEMGFTHVASGPMVRSSYHADLQAQGQFS | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 35700
Sequence Length: 316
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.8.1.8
|
Q97U63 | MEKKVQIAVYENENFKRVAEIVKKKSIATVCEEALCPNIMECWGSGTATFMIMGSICTRGCRFCYVLKGKPSPLDDEEPKRVAEAVKEMELDYVVITSVDRDDLSDGGAQHFANVVKTVKELNPGIIVEVLTPDFRGNIDAVKKVIDAGVDVFAHNVETVRRLTPIVRDPRASYEQSLNVLKYAENVIKKSSILLGLGETWDEIVETMRDLRSVGVSILVLSQYMRPSRKQLEVKKRYTLEEFKELEEIAYSMGFSAVISLPLARTSYKAKEAYFRAIENAKNHS | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 32111
Sequence Length: 285
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.8.1.8
|
Q6MPS6 | MADLIFQDWGLINYDEALKKQNDLVEKVHTEDLPGFLVFCTHPPVVTVGRATQAGDVFSWNGPVVEVTRGGRATYHGPSQLVVYPILNLAHVRKGRKDREINPYLKVFEDAIVDVLKTYGLTGIEGRSSAKSSFNRADADDTGVWVNDLKIASVGVGVRKWVAFHGAAINLTFDEKAFLGLRPCGFPSEVMVSLEQLTGAKVDVGEFKEKLKRRLLEVL | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 24227
Sequence Length: 219
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
Q2L1E2 | MSMNVAWLSPGAAYADVWEAMKAFTASRGPATPDEIWLCEHAPVYTLGQAGLPQHVLNPADIAVVRSDRGGQVTYHGPGQIVVYCLFDLRRAGMYVRDYVALLEETAIAVLGRAGIVAQRKPGAPGVYVEQPGQTLAKIAALGIKIRKGCAYHGLSLNVAMDLTPFHGINPCGYEGLQTTDMASCGLSCSVHEVGQALADELVRRLSAYQGSLSSGE | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23060
Sequence Length: 217
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
A9IH67 | MIKWLTRPADYAPVWQDMRAFTAGRGAATPDEVWLCEHAPVYTLGQAGKPEHLLNPGAIPVVMCDRGGQVTYHGPGQVVAYTLFDLRRAGLFVREYVRLLEDAAIGTLDDFGVPGACRKPGAPGVYVPLGPAGELAKIAALGIKIRNGYAYHGVALNVDMDLSPFLGINPCGYEGLVTVDMAACGVRRDLVDVGQRLAERLLAAMPEPAGATR | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 22757
Sequence Length: 213
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
Q89JM6 | MVNSPQNPRQDQRQDLDLTSFSATGGEPVEWRISDAPVPYPEAVAAMEARVAAIAAGEAPELVWLLEHPPLYTSGTSGKDSDLLDPRFPTFATGRGGQLTYHGPGQRVAYIMLDLKRRRPDVRAYVASLEELILKTLAAFNVRGERREDRVGVWVKRPDKGDGYEDKIAAIGVRLKRWVSFHGIAINVEPELSHFAGIVPCGVADPRYGVTSLVDLGQLVTMADVDVALRQAFEELFGPTRALVPEAAA | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 27244
Sequence Length: 249
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
Q2YKK8 | MPTGKLRQKPPYAAIMTNSPVTPSTETQQPKRDALYARFLPQEADAPPVEWLIAEGLTDYEEALAFMEARVQATREGTASELVWLVEHPPLYTAGTSANAEDLLTPDRFPVFNTGRGGEYTYHGPGQRVAYVMLDLKRRREDVRAFVASLEQWIIETLAAFNIKGERREDRVGVWVVRPEKPRLADGSMCEDKIAAIGIRLRRWVSFHGIAINVEPDLSHYGGIVPCGISEHGVTSLVDLGLPVTMGDVDVALGKAFESVFGPRQTK | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 29589
Sequence Length: 267
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
P57356 | MKKKIIFLRNLGIEHWLTTFNKMNNFIISRNPCTYDEIWFVEHYPIFTQGQSNEQKNLIVSNDIPVVQTNRGGQITYHGPGQQILYFLIDLKRRKMNIRQLINIMEQTVIETLNNFSIQAYTKKKMPGVYINEKKICSLGLRIKKGFTLHGLALNVNMNLTPFNYIHPCGDKNMKMTQIKDFNSNVKLKDVRFILIKELSKFLEIFIINSN | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 24775
Sequence Length: 211
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
Q8K9Q3 | MNNRIILFQNFGLKHWIDMFNKMHAFTEVRNINTYDEIWFLEHYPIFTQGLLQKINTITYNNDILHDIPIVSTDRGGQITYHGPGQQILYFLIDLKRRKITIRDLINIMQNLIIETLNYFSIKSHIKKNSPGVYVNNKKISSLGLRVKKGFTLHGLSLNVDMDLTPFNYIYPCGDINIKMTQVKEFNSFLTLNDIRVILIKKLSQLLNVSIIEKFSIK | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 25552
Sequence Length: 218
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
Q89AL8 | MYKKNIKIRNLGLRRIQDVCSSMNDFTITRKISTPDEIWLVQHYPVFTIGVSGTKHDVLVSNNIPIIFSNRGGKITYHAPGQLIIYVLINLFRRKLTVRRLILLMQNIIISTLKSFSIDSYILNNFPGVYVNNKKICSLGLRIRNGCSFHGMALNINMDLLPFEYINPCGNSFKMTQVIDIKPNLCFKIIKLMLMHKIREIFS | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23438
Sequence Length: 203
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
Q4FLP4 | MNIEIKKSIKPIKYEDAIKLLEERLLEINNGQKEDLIWILEHEEVYSAGTSYKEKEILNKDISLVKTNRGGKITYHGPGQLICYFVIDLKKRKKDIRKFITLIEETIIDSLSKFNIKTFGDPKNIGIWTDHKGKINKVAAIGVRVSKWIAYHGFAININNDLSKYKNIIPCGISDKGVINLKEIKDQDYKNLDEIIIETFSKNLEI | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23766
Sequence Length: 206
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
C0QQ61 | MLKIIDLGKTEYQEALEIQNRIFERKLTGEDQDNYFFITEHHPVYTAGKTTKPEHILNTEDIPVYYIDRGGSVTFHGEGQIVVYPVLSLKNRISVKRYVFTLEEIVIKTVKEIGINAYRKDRLRGVFTDKGKIASVGVKVSKGVTKHGISLNVNIEKRYFRRIIPCGIWDIPVCNITDFVEADIDKIKLKLIKHIIKEGRKLV | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23373
Sequence Length: 203
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
Q7N766 | MKFQLQHKTIFLRQLGIQPYEPISDAMHLFTEQRDTNTPDEIWLVQHPKVFTQGQAGKAEHLLSLGDIPVIQSDRGGQVTYHGPGQQVMYVMIDIKRARIGVRQLVTAIEDTVIKTLAHFGVKAYARPDAPGVYVNEAKICSLGLRIRKGCSFHGLALNIAMDLEPFQRINPCGYAGMKMIQLSDLVPGITVEQVQPVLVEKFCQQLGFKLNS | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23826
Sequence Length: 213
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
Q6LN88 | MQNSLIIRNLGRQDYEPTLQAMHEFTDQRTPETTDEVWLVEHNPVFTQGQAGKTEHLLNTGDIPVIQSDRGGQVTFHGPGQLVAYVLIDLRRNKLGVRDLVTHIENTVINTLSQFGVESNARPDAPGVYVDNKKICSLGLRIRRGCSFHGLALNINMDLTPFLRINPCGYAGMEMTQLALLSGPSELNKVQPVLVEELTKLLAYQSIEWITESN | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23908
Sequence Length: 214
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
A4T0B0 | MTVLVKHLGVVDYVSTYEVMRAFTKERNSTTPDEIWILEHPPVFTLGLAGDAGNLHSPSNQIPLVQVDRGGEITYHGPGQIVVYLLLDLKRLGIFVKELVSRIEQALINTLADFGLVAERRSGAPGIYVSLQPGISPEWIGAKVAALGLKVSKSCSYHGLALNVATDLEAFGRIHPCGYEGLKTVDMQTLGIKDNIDTISQRLLEHLQKQLMPT | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23427
Sequence Length: 214
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
Q12GR3 | MNMEIRHLGRVDYLPTYEAMQAFTLERTAATPNSLWICEHPPVYTQGLAGKIEHVLNPGDIPVVQTNRGGQVTYHGPGQVVAYPLIDLKQAGYYVKEYVYRIEEAVIRTLSHFGVTGHRVPGAPGIYVRLDDPFSHARLRPSPQPSPKGRGSSTPVLLPPLPGEGGGGGGPDPDPFHSLGKIAALGIKVSRHCTYHGVALNVAMDLEPFSRINPCGYAGLKTVDLRTIGVSVTWQEAADVLGQKLSSYLAP | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 27125
Sequence Length: 251
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
Q7MUY1 | MRCILLGSGTSTGVPEVGCHCRVCRSEDRHDKRTRTSLLIITDAGKRILIDCSPDFRQQALFAGIDSLDAVLLTHEHFDHVGGLDDLRTICWHRELAVYAEQNVLDSIRDRLHYVFRKNPYPGTPLLKLCEVKPDMPFQVADLTVEPLRIMHGRLPILGYKIGEMAFLTDMKDIAAEEIECLKSCRLLFINGLRYRKEHPSHQTIEQAIDTIGQIGNPESVLIHLSHHAPLHQEHLEILPPHIHSGYDGLEAIIDEKGIRIKDFEPHVSRSEYHYQDCGRIGYESALTLQRKLFHDAVADKLENRKPQNTLLFCEHEPVLTLGKHGHEENLLLSESELKSRDIRLFHIERGGDITYHGPGQITGYPIFDLEQYGIGLRSYIEMLEQCIIDLIAIFGLKGERSAGASGVWLDPDIPGRTRKICAIGVKSSRHITMHGFALNVNTDLDYFKLINPCGFSDRGVTSISRELGREQDFILVKQQLEAVFRRNFGAL | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 55795
Sequence Length: 492
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
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