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stringlengths 6
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stringlengths 11
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stringlengths 108
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Q3A370 | MSITAVIPARYASSRFPGKPLARILGKTMIQRVYERTAQAACIDRVVVATDDSRIADVVSGFGGEVQMTRADHATGTDRLAEVTARIDTQLIVNVQGDEPLIDPHMIEAAVAPLSEDPAIPMGTLKTPLLNWQEYRDPNVVKVVTDRRGFALYFSRAPIPHPRELAVDDSAVSPASMGLFRHIGLYVYRKDFLLTFAGLPESPLERLEKLEQLRALENGYAIRVVETDRVSLGVDTPEDLVRVEAHLRGL | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27613
Sequence Length: 250
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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Q31KU9 | MVRILAVIPARYASERLPGKVLLPIAGRPMLQWVYEATIASNVFDQVAIATEDPRVVEAAAAFGAEAILTSADLASGTDRVAEASLHFPDCKVIANVQGDQPFVTPGLLQALVSPYRAGELPEMTTVGGPYDPAQDADDPNTVKVVCDQRGNALYFSRSAIPYPRTVVHDLPVYHHFGLYAFRRDFLAQYRQLPPTPLERCESLEQLRVLEQGYRIRVVPCADKVIEVNTADDLERANAWASQR | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 26890
Sequence Length: 244
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
|
B5YGT5 | MVTICVIPARYGSTRFPGKPLAFLKNKPIIQHVYERAKSSKMIDEVFVATDDSRILHTVESFGGKAIMTSSKHPSGTDRIAEAVDKLLQEGYNLQESSIVINLQGDEPLIKKEMIDQLIDLMKNENDSIGTLAKRIEKEDDFFNPNIVKVVFDKNGYALYFSRSPIPFDREKFIKGFSKNNFMYKHIGIYGYNVRILKNFVGLPMSRLEEIESLEQLRALENGIKIKVGLTEYDSFGIDTPEDLEVAEKCLNTYS | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 29002
Sequence Length: 255
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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Q83SQ3 | MDSHTLVQALIYLGSAALIVPIAVRLGLGSVLGYLIAGCIIGPWGLRLVTDAESILHFAEIGVVLMLFIIGLELDPQRLWKLRAAVFGGGALQMVICGGLLGLFCMLLGLRWQVAELIGMTLALSSTAIAMQAMNERNLMVTQMGRSAFAVLLFQDIAAIPLVAMIPLLAASSASTTMGAFALSALKVAGALVLVVLLGRYVTRPALRFVARSGLREVFSAVALFLVFGFGLLLEEVGLSMAMGAFLAGVLLASSEYRHALESDIEPFKGLLLGLFFIGVGMSIDFGTLIENPLRIVILLLGFLIIKIAMLWLIARPLQVPNKQRRWFAVLLGQGSEFAFVVFGAAQMANVLEPEWAKSLTLAVALSMAATPILLVILNRLEQSSTEEAREADEIDEEQPRVIIAGFGRFGQITGRLLLSSGVKMVVLDHDPDHIETLRKFGMKVFYGDATRMDLLESAGAAKAEVLINAIDDPQTNLQLTEMVKEHFPHLQIIARARDVDHYIRLRQAGVEKPERETFEGALKTGRLALESLGLGPYEARERADVFRRFNIQMVEEMAMVENDTKARAAVYKRTSAMLSEIITEDREHLSLIQRHGWQGTEEGKHTGNMADEPETKPSS | Function: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67706
Sequence Length: 620
Subcellular Location: Cell inner membrane
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A7ZHD9 | MILIIYAHPYPHHSHANKRMLEQARTLEGVEIRSLYQLYPDFNIDIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVFSHGWAYGHGGTALHGKHLLWAVTTGGGESHFEIGAHPGFDVLSQPLQATAIYCGLNWLPPFAMHCTFICDDETLEGQARHYKQRLLEWQEAHHG | Function: Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20170
Sequence Length: 176
Subcellular Location: Cell inner membrane
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A5DNX8 | MSSSKLLKYGSDDLQTIRVYRHDSGNHLSIIFIHGGAWRDPRNTFNDFEELVGKLPSTINTFGINYRLSPAVKHPAHLEDVVSAIEYLAKNYKVENVGLVGHSVGATLALQILNYKTILPGLERPLGIKMKFLVFLDGIYDVPKLVEEYPTYSSFVNEAFKTKQDYMRATPVSSEMPQFDISVEKCVILLVQSTEDELLSVQQTELMADFLQAKSIPFEKHLGAFGAHEQVYRHHKVAKLITDAIGANLDGLVRARPQN | Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
Catalytic Activity: H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine
Sequence Mass (Da): 29091
Sequence Length: 259
Domain: The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
EC: 3.5.1.9
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A3GGU3 | MSEKIVFYGKEQLQRIRIFNYSESNDKTLIVLHGGGWRDPRNSYNDFEDMANYILEEKKATNINIIGIDYRLSPFIKHPVHLIDVLTAFRYILENYKTGQLSIVGHSVGATLLLEILNYVEIIQTGLEQLETSEPSIEELQTLFDFISKNLTFKTMYFLDGIYDVRALLEEYPSYDFFVKSAFVSTVAIEEASQLSWKQHNEAFKIAVDKYEILHSLEDELLSLNQPKLFAKYLQDRKIECSFRTGNWGEHEQVYRSQAVSEHVLQNM | Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
Catalytic Activity: H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine
Sequence Mass (Da): 31245
Sequence Length: 268
Domain: The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
EC: 3.5.1.9
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A7TJ85 | MNDPTDTLYHQTAIHKLAEIGKNCKHLGIIFIHGGAWVDPLNTSNDFKGIAGEISKVIENNNTQGFNISMFGIEYRLSPSVKHPIHITDVITNTYKLINEYKIDILYIVGHSVGATLGLQLATDNRDYLIKYSSQLHLIRSTIQGLFLLDGIYSLQELLKEYPTYDSFISKAFTNYELEFQDPKEYLDKEQQFIKNLSFYIIHSFQDELLTLRQTDYLVELLKAKEISFNLSISDYGRHNDVYINDRVAKLIIFNILSNIN | Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
Catalytic Activity: H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine
Sequence Mass (Da): 30049
Sequence Length: 261
Domain: The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
EC: 3.5.1.9
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Q04066 | MSNTVRAISPDITLFNKTLTFQEISQNTREAVIYIHGGAWNDPENTPNDFNQLANTIKSMDTESTVCQYSIEYRLSPEITNPRNLYDAVSNITRLVKEKGLTNINMVGHSVGATFIWQILAALKDPQEKMSEAQLQMLGLLQIVKRVFLLDGIYSLKELLVEYPEYDCFTRLAFPDGIQMYEEEPSRVMPYVKKALSRFSIDMHLVHSYSDELLTLRQTNCLISCLQDYQLSFKLYLDDLGLHNDVYKNGKVAKYIFDNIC | Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
Catalytic Activity: H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine
Sequence Mass (Da): 29991
Sequence Length: 261
Domain: The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
EC: 3.5.1.9
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O44408 | MEVDLPVHNEYDASRFHQVTIRDPIAGADSTFTIPTRYVNLSFLNAGAQGTVVMADDLVTTQRVAIKKMQQPFVMTMSAKRAYREFILLTTIKHPNIIRLLNAFTPDTSLSTFREVYLVMELMTHNLHEVIHRLRLDHKTLSFFVYQSLCAIKHLHNSGVIHRDLKPSNIVVNDRCVLKVLDFGLARKKNVDTSMRMSDYVVTRYYRAPEVILGLPYSEKVDIWSVGCIFAEMINHTVLFPGKDRIDQWTKIYSVLGTPDDHFISQLGQSAAMYVRSLPRHQARAFSEIVPDTNFLPETENPRVHLTPHVARDLLFNMLKINPEERYSVEDALNHPYVKLWFKDDEVNAPASENRYDQEIDFADKTLIEWKELIFNEVQRYQADHDIFTG | Function: Mitogen-activated protein kinase which is an essential component of the JNK pathway composed of mlk-1, mek-1 and kgb-1 . Phosphorylates the transcription factor fos-1 which prevents fos-1 dimerization and promoter binding and results in activation of target genes including F53A9.2/kreg-1 and lys-3/kreg-2 . Phosphorylates jun-1 and activates the AP-1 transcription factor which is a heterodimer of jun-1 and fos-1 . Phosphorylates glh-1 in vitro which may play a role in controlling glh-1 protein levels in the germline by targeting it for degradation by the proteasome . Required for oogenesis and probably also for spermatogenesis . Involved in the response to environmental stress such as heavy metals, infection and protein folding stress in an age-dependent manner . In larvae, has a protective role which becomes detrimental in adults . May control susceptibility to infection, heavy metal stress and premature lethality by regulating daf-16 cellular localization . Involved in the transcriptional response to bacterial pore-forming toxins and to fasting . Required for fasting-induced longevity . Involved in axon regeneration after injury downstream of tyrosine receptor svh-2 .
PTM: May be phosphorylated by mek-1 on Ser-198 and/or Tyr-200 . Phosphorylation is induced upon Cu(2+) and arsenite-mediated cell stimulation and by fasting .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 45157
Sequence Length: 390
Subcellular Location: Cytoplasm
EC: 2.7.11.24
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Q98PN5 | MINIHKRNIVLLVGPSGVGKGTIEKILFESKTLKLSLSRSATTRKKREGEINGIHYFFISKEEFESKIENDEFMEWNEHFDNYYGTLLSEILLIFSQGRIPVLEVETYGAKKILQKYKDKKDFNWITIFVDPPSFEELENRIIKRGTDTKEKIAIRMAKAKEELKDRDLFEFKITNHTPEQAAEEIEKIILKKTMG | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 22918
Sequence Length: 196
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q4A6S7 | MNKKKKSIVIFTGPSGVGKGTVEQLVFNYDELNLSLSCSATTRSPRGGETNGIHYYFISKEEFKDRIKNKKFLEHSFHFDNYYGTLYSELDNIIARNKVPFLEIETNGAKIIAQKMQKLKNPPYNLITIFLSPPSITDIYKRIKNRGTENAQTIKNRVNKAKEELLEAGNFKYVVYNDRPERAAQEIREILHKELDID | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 22868
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q1D3A6 | MNANTVLPPGLLLVLSAPSGAGKTTLAHRLLKETPDAVFSISVTTRRPRGKEREGVDYNFVDVATFQSKIERGEFVEWAEVYGHFYGSPQSVVDEARARKSAAIFDIDVQGGQAIKRKHPDAVTIFVLPPSMEELERRLRDRQTDSDETIRRRMLAARSEIERGIASYDYVVVNDDFERAFSDLRSVVVAERCRRERVDVSKLGLGIGG | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23381
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q9JYB5 | MSAYRKGNIFIISAASGTGKTTLVSRLLANHNGLRVSVSHTTRPPREGEANGVHYHFVSKEEFESLIAQEAFLEYADVFGNYYGTGAEGVNALAAAGYDVILEIDVQGAAQVRDALPEAVGIFILPPSFDVLAARLNGRGTDSREVIQRRLSKARHEIEQSVLFDFVVVNDDLARAEEDLRHIVNACRLKRSRQLGFIADLLENS | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 22500
Sequence Length: 205
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q2GD44 | MRKGILFIISSPSGGGKTTVADFLVGQDLSIKRSISFTTRQPRGEEKDGIDYYFVSKDEFNRLLQEGEMLEHATVLQNQYGTSHRYIEETLALGIDVLCCIDWQGAEQIRKKTNCISIFLLPPSLQKLKTRLTSRGTDTADVIEYRLKVALEEIQHFSKYDYVLVNDDLTETKQKVLSIITAEREKLVQNHRVVECFVASLLEQTI | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23493
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q8ER28 | MIKEKGILFILSGPSGVGKGTVRKKLFEEETDLQYSISMTTRDRRPGEVDGVDYFYKTKEEFEQLIKDGQLLEYAQYVNNYYGTPRNYVEETLENGQDVFLEIEVQGALQVKENFPEGVFIFLFPPSLDELKNRIVSRGTESQELVLNRLKEARNEIEMMDAYDYVVVNDKVQHAVDKVKTIIKSEHLKRERIAKQYKKILEDGLS | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
Sequence Mass (Da): 23914
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.7.4.8
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Q9BKB7 | MKISFVLLLTLFICSIGWSEARPTDIKCSESYQCFPVCKSRFGKTNGRCVNGFCDCF | Function: Blocks human and/or rat Kv11.1/KCNH2/ERG1, Kv11.2/KCNH6/ERG2 and Kv11.3/KCNH7/ERG3 by binding to channel outer vestibule (S5P domain) with a 1:1 stoichiometry. Inhibition data are the following: hERG1 (reversible, Kd=7.7 nM , IC(50)=3.3 nM , IC(50)=11.9 nM ), rERG1 (reversible, Kd=19 nM) , hERG2 (reversible, Kd=77 nM) , rERG2 (irreversible, Kd=4.2 nM) , hERG3 (reversible, Kd=11.5 nM) and rERG3 (reversible, Kd=747 nM) potassium channels. Has also a minimal effect on rat ELK1/KCNH4 potassium channels (9% inhibition at 100 nM ). Both this toxin and CnErgTx1 (AC Q86QT3) share mechanism of action and have overlapping binding sites on ERG1 . The potency of these two toxins is not affected by elevating potassium ion concentration from 2 to 98 mM . In addition, at high toxin concentrations, block of ERG1 macroscopic currents by these two toxins is incomplete (88%) . The blockade by this toxin is preferentially closed channel state-dependent, with a component of open, but not inactive state-dependent blockade . This toxin produces a concentration-dependent prolongation of QTc in the isolated rabbit heart (16.3% at 100 nM) .
Sequence Mass (Da): 6452
Sequence Length: 57
Domain: Has the CSalpha/beta fold, which comprises one or two short alpha helices connected to anti-parallel beta-sheets stabilized by three or four disulfide bonds.
Subcellular Location: Secreted
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Q9PIZ3 | MKILVPATSANLGPGFDCLGLSLKLFNETQIQKSGVFSISIGGEGSDNIFLKKNNIFVNIFYEIYEKLSGKKDNFRFIFQNNIPLSRGLGSSSAVIVGAIASAYYMSGFKVEKECILDEALIYENHPDNIAPATLGGFVCSLVEKNKVYSIKKEIDKDLAAVVVIPNLAMSTEQSRQALAKNLSFNDAVFNLSHASFLTACFLEKKYEFLKFASQDKLHEINRMKNLPELFEVQKFALENKALMSTLSGSGSSFFSLAFKDDALALAKKIQTKFKDFRVQYLEFDDNGFEIC | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 32501
Sequence Length: 292
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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Q3AAV5 | MVCVLIPATSANLGPGFDAVGMALSFYNEVSLGPSPKELEIEVFGDGAELISRDKNNLVYVAITKIFERLGKTPRNLKLTLKNRVPLARGLGSSAAAIVGGLVAANAYLGNPLPKDELLRLATELEGHPDNVAPALLGGVVVSGFDRDKVKYLKLPVPEVEVVVAIPKFQLKTADSRQILPAEIPFSQAVLNVNRVSFLIAAFCLKKYEYLQIGMEDYLHQPYRSQLIPGFYQVVEEAKKAGAYGVALSGSGPTVIALAREGKAVGRAIEETFLNFGVEAEIIYTRPEERGAIDLINYKGEGDC | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 32790
Sequence Length: 304
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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Q8KAW7 | MKTVTGFASATVGNVACGFDVLGFAITEPGDEVVLALHDERRSDCPVSITSIVGDGGALPLDPKKNTSSFVVLKFLEYIRTTKGISFDGHIDLVLKKNLPLSSGMGSSAASAAAALIAANELFGSPCTKMELVHFAIEGERVACGSAHADNAAPAMLGNFILIRSYNPLDLITIKPPKNLFGTLVHPHTELKTSFARSVLPKSIPLSTATQQWGNVGALIAGLLMEDYDLIGRALVDVVAEPKRAPLIPGFNEVKQAALDAGALGCSIAGSGPSVFAFSSSRQTAEAVGSAMQSAFLHSRAALQSDMWVSPICSQGARIISTTS | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 33771
Sequence Length: 324
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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A5CQ46 | MRSALATGRRVQVRVPATSANLGPGFDTLGLALALYDDLTVTVRDAPGATVDVRGVGAGEVPTDETNLVVTAIAHTFAAFDQPMPGLDLVAENRIPHGRGLGSSGAAIVSGIMAAQGLLAGTVEIDADALLRLATEMEGHPDNVAPALFGGLTIAWVDGQGPQHKKLAVHRGVSPLVLVPVATMSTALARSLQPESVPHEDAIFNVSRSALLIAALIQSPELLLAATEDRLHQDYRAAAMPETNELVHLLRERGYAAVVSGAGPSLLVLGSDPGQRLTAAELVAERSTNPWTALMLAVDVKGSTVQVVDEGSAPAA | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 32631
Sequence Length: 316
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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Q97JN8 | MIRVKIPATSANMGAGFDTLGMALKLYNEITIEETEGETEIKLLGGELDRNYRNNLTYISIIKVYEFFNKEFKGFKIDMSKTNIPLSRGLGSSAACIVGGIVGANALLNEKMTIKDMLKIAVDIEGHPDNVAPALLGGVIISIKDMENIIYSRINVKSQLKYAVMVPDFKVSTELSRKVLPNEYSREDALFNISRCSMLVSALNNGENEKLRYLFEDKIHQPYRKKLINNIDSIFLKAKEYGSLGEFISGSGSTLIAVLEEADENFILKMKTYLDSLKDGWRIFEVENDNNGAVII | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 33072
Sequence Length: 296
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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Q8YZV9 | MSVVSSVTVKVPGTTANLGPGFDCIGAALTIYNQFQFTRLEESGLIIQATGAEAERVPTDESNLIYQAFAKLYQYIDQPAPGVKIEIELGVPLARGLGSSATAIVAANRLAGEPLSQAQVMALAIAIEGHPDNVVPALLGGCRLAATGASGWEICDVPWHSHIVPVLAIPDFELSTSEARRVLPTEYSRADAIFNTAHLGLLLRGLETGKGEWLRAALQDKLHQPYRQALIPGYDAVNTAAVAAGAYGMVISGAGPTLLALADVSHAAAVEAAMSTAWQEAGITAVVRSLALDTHGAT | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 31045
Sequence Length: 298
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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Q8ET01 | MTPFGISVPASSGNVGPGFDSTGLALGLYLHLNVEDANSIQFYSDGESTPTENHFIWNIAENIANKHGIRLPACKVQETNEIPLARGLGSSASAIVAGIELANQLGNLHLTPEQKLQYGTEIEGHPDNVAPSIYGGLVISTVLEKEIEHIQLRDIDVDIVAYIPNIELKTSVSRNCLPDSYNRDYAAKASAISNLTIAALYSKDYKLAGKLMEEDLFHEPFRSELIPNFAYIREEAKKYGAFGTILSGAGPTMLSITPKGNGPTLQNNMSKLSLLADYQVEYIPIDYQGISIQE | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 31958
Sequence Length: 294
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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Q9CPD3 | MLRIYAPASSANLSVGFDTLGTAVSPIDGSLLGDVVQIEALPSGFELESAGYFVRKLPKEAQKNIVYQAYVLFSERLKLRNIAVRPLRLTLEKNMPIGSGLGSSACSIVAALVALNKFHAEPFSKMELLEMMGELEGRISGSIHYDNVAPCYLGGVQLMVQSLGNICQQLPFFDEWYWVLAYPGIEVSTAEARAILPKSYTRQDVISQARHLGSFVHACHTRQAQLAALMMKDVIAEPYREALLPNFADVKQATRDLGALATGISGSGPTIFAIAPDLGTAMKLSTYLENHYLQNNEGFVHICKVDNQGARALD | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 34211
Sequence Length: 314
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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Q6D0A9 | MVKIYAPASIGNVSVGFDVLGAAVSPVDGSLLGDCVSVEAADLFSLRNEGRFVSKLPDNPKENIVYQCWELFCQEIGKTVPVAMTLEKNMPIGSGLGSSACSVVAGLMAMNEFCGKPLDDTRLLRLMGELEGRISGSVHYDNVAPCFLGGVQLMLEENGIISQPVPSFDDWLWVMAYPGIKVSTAEARAILPAQYRRQDCISHGRYLAGFIHACHTGQAELAAKLMKDVIAEPYRTKLLPGFAAARQAAEDIGALACGISGSGPTLFSVCNDMASAQRLADWLRDNYLQNDEGFVHICRLDKTGARQLG | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 33237
Sequence Length: 309
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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C0QQC5 | MKVLKVKVPATTANLGAGFDTLGLALTLYNEFIVEEHDGVVIETEPKNEFLEIPENNLFIQVIKYACERRGKTFHGAKLKQINRVPVARGLGSSATAIVGAIVVSSAVSKTELTDDIFFDIAYRFEPHPDNLIPAWKGGFITALKDREKTYYNSIDFPEDIKAVVVIPEFELSTEKARSVLPERIPLRDGIFNVQRVSLFLSALQNRRYDLLRVAMEDRFHQPYRKKLIPNFDRVVQNGYDAGALGVSLSGAGSAILALADRNFEEIGKAMTEGFSEAGIRSEYKILDIDREGANLEILE | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 33452
Sequence Length: 300
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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A9BGN7 | MIRVKVPATTANIGPGFDSLGIALQLYNIIEVEEINFGLEINIPVEDQAYIETNEHNLVYQAMKRLFDAVNIHPKGLRINLINNIPIARGLGSSAACIVGGLVVANELLNNPLKKEEIIYLAATMDGHTDNILPAFVGGLTVGSLLEKEVKYVKMDLPTQLKLLAIIPDFHFSTKKARSLLPKNVPIEDAVFNISRVGLLVASLVTSHFENLSEATKDKIHQPYRKDFIPYWEEITSKLMKIGTKGYFLSGSGPTIMGILDGDYKNIEDEMVNFLSHFDQGYKVTVLDVCHNGLEVINDEGSNGCYR | Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 33987
Sequence Length: 307
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.39
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B4R8T4 | MAVYTDITDDELAKLLADFDLGAPLSFKGIAEGVENSNFLLETEGGRFILTVYEKRVRAEDLPFFLGLMRWLSEHGFASGLPMADRGGEMLKTVRGKPCAIVSFLPGLSVRRPTVAHCREAGKGLAALHNAADGFPMRRENDLGQGAWAPMFERLKDDAERLKPGLAEVIARDVADLADRWPQGLPEGVIHADYFPDNVFFKEGVFAGAIDFYFACNDIRAYDIAVALNAWCFEADGSFNITAARALVAGYEAVRPLSEAERAALPVLAHGAALRFFLTRLHDWHATPAGALVKPKDPLEYERKLAVHRTSPDLVLFGAAAAE | Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
Sequence Mass (Da): 35333
Sequence Length: 323
Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
EC: 2.7.1.39
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P09979 | MTQESLLLLDRIDSDDSYASLRNDQEFWEPLARRALEELGLPVPPVLRVPGESTNPVLVGEPDPVIKLFGEHWCGPESLASESEAYAVLADAPVPVPRLLGRGELRPGTGAWPWPYLVMSRMTGTTWRSAMDGTTDRNALLALARELGRVLGRLHRVPLTGNTVLTPHSEVFPELLRERRAATVEDHRGWGYLSPRLLDRLEDWLPDVDTLLAGREPRFVHGDLHGTNIFVDLAATEVTGIVDFTDVYAGDSRYSLVQLHLNAFRGDREILAALLDGAQWKRTEDFARELLAFTFLHDFEVFEETPLDLSGFTDPEELAQFLWGPPDTAPGA | Function: The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation.
Catalytic Activity: ATP + hygromycin B = 7''-O-phosphohygromycin B + ADP + H(+)
Sequence Mass (Da): 37054
Sequence Length: 332
EC: 2.7.1.119
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Q8NI77 | MSVTEEDLCHHMKVVVRVRPENTKEKAAGFHKVVHVVDKHILVFDPKQEEVSFFHGKKTTNQNVIKKQNKDLKFVFDAVFDETSTQSEVFEHTTKPILRSFLNGYNCTVLAYGATGAGKTHTMLGSADEPGVMYLTMLHLYKCMDEIKEEKICSTAVSYLEVYNEQIRDLLVNSGPLAVREDTQKGVVVHGLTLHQPKSSEEILHLLDNGNKNRTQHPTDMNATSSRSHAVFQIYLRQQDKTASINQNVRIAKMSLIDLAGSERASTSGAKGTRFVEGTNINRSLLALGNVINALADSKRKNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSVFYDDTYNTLKYANRAKDIKSSLKSNVLNVNNHITQYVKICNEQKAEILLLKEKLKAYEEQKAFTNENDQAKLMISNPQEKEIERFQEILNCLFQNREEIRQEYLKLEMLLKENELKSFYQQQCHKQIEMMCSEDKVEKATGKRDHRLAMLKTRRSYLEKRREEELKQFDENTNWLHRVEKEMGLLSQNGHIPKELKKDLHCHHLHLQNKDLKAQIRHMMDLACLQEQQHRQTEAVLNALLPTLRKQYCTLKEAGLSNAAFESDFKEIEHLVERKKVVVWADQTAEQPKQNDLPGISVLMTFPQLGPVQPIPCCSSSGGTNLVKIPTEKRTRRKLMPSPLKGQHTLKSPPSQSVQLNDSLSKELQPIVYTPEDCRKAFQNPSTVTLMKPSSFTTSFQAISSNINSDNCLKMLCEVAIPHNRRKECGQEDLDSTFTICEDIKSSKCKLPEQESLPNDNKDILQRLDPSSFSTKHSMPVPSMVPSYMAMTTAAKRKRKLTSSTSNSSLTADVNSGFAKRVRQDNSSEKHLQENKPTMEHKRNICKINPSMVRKFGRNISKGNLR | Function: Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression.
PTM: Glycosylated.
Sequence Mass (Da): 102281
Sequence Length: 898
Subcellular Location: Cell projection
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Q9BVG8 | MVPSRRTWNLGATPSLRGLWRVGRAPEPEPGMARPAPAPASPAARPFPHTGPGRLRTGRGKDTPVCGDEDSSARSAARPALAQCRALSVDWAGPGSPHGLYLTLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVRPVTKEDGEGPEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQEVQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSVELGPGLRRAELGSWSSQEHLEWEPACQTPQPSARAHSAPSSGTSSRPGSIRRKLQPSGKSRPLPV | Function: Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 92775
Sequence Length: 833
Subcellular Location: Cell junction
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B3TMR8 | MENPANANPIRVGVIGCADIAWRRALPALEAEPLTEVTAIASRRWDRAKRFTERFGGEPVEGYPALLERDDVDAVYVPLPAVLHAEWIDRALRAGKHVLAEKPLTTDRPQAERLFAVARERGLLLMENFMFLHHPQHRQVADMLDEGVIGEIRSFAASFTIPPKPQGDIRYQADVGGGALLDIGVYPIRAAGLFLGADLEFVGAVLRHERDRDVVVGGNALLTTRQGVTAQLTFGMEHAYTNNYEFRGSTGRLWMNRVFTPPATYQPVVHIERQDHAEQFVLPAHDQFAKSIRAFAQAVLSGEHPREWSEDSLRQASLVDAVRTGARDIYFP | Function: Involved in the biosynthesis of L-digitoxose, an unusual dideoxysugar attached to various pharmacologically active natural products, including the antitumor antibiotic tetrocarcin A, and the antibiotics kijanimicin and jadomycin B. Catalyzes the reduction of the C-3 keto moiety of dTDP-3,4-diketo-2,6-dideoxy-alpha-D-glucose to yield dTDP-4-keto-2,6-dideoxy-alpha-D-glucose. Also able to reduce dTDP-3-keto-6-deoxy-D-galactose and dTDP-3-keto-6-deoxy-D-glucose to yield dTDP-fucose and dTDP-quinovose, respectively.
Catalytic Activity: dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP(+) = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H(+) + NADPH
Sequence Mass (Da): 37033
Sequence Length: 332
Pathway: Antibiotic biosynthesis.
EC: 1.1.1.384
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Q55GK8 | MSTTSMILTKKNIIILSIIIITIIAYQFYITSPQSFPSSNTITNTINTSGKGLDYTELLNLQKDLKAQQTEIRKQLEQLKYSINDINQNQNENQNQINNEYNNNKLNDEQENNNNNNYNNNNNNNNNELINYKERIKKKSKEQPNTCIPVEGKLLCLPNFIVIGTMKSGTTFLDYYLQKHPQIAHHSKKEIWYFNSYYANGIEWYAKHFEQYTSLENQKLIGEATPFYINNPNTAPRLFTTLKNAKLILLLRDPVERSLSQYHFSIQWLKRNKSPPLEYSFEHLIHEEADVIETCIRGHERYKEAFKQRKEIEKNGGGGLLNDNTSGEEFNLVDPFYTLHSEKNWTFYKDCIRCDKCFQIGSILHTSGHPTFGMLAKSLYFEQLDYWLNFFPLEQIHIIRYEDISSQPESVLSELEDFLDINHIDYGEFKPRNVVQHDPMNQEIKSYLINYFKQSNEKLYNLLNRDFKWQN | Function: Sulfotransferase involved in intracellular killing of bacteria.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 55568
Sequence Length: 471
Subcellular Location: Membrane
EC: 2.8.2.-
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P96589 | MYHSIKRFLIGKPLKSQAAGEQKLTKLKALAMLSSDALSSVAYGTEQILIILATISAAAFWYSIPIAVGVLILLLALILSYRQIIYAYPQGGGAYIVSKENLGEKPGLIAGGSLLVDYILTVAVSISAGTDAITSAFPALHDYHVPIAIFLVLVIMILNLRGLSESASILAYPVYLFVVALLVLIAVGLFKLMTGQIDQPAHHTSLGTPVAGITLFLLLKAFSSGCSALTGVEAISNAIPAFKNPPARNAARTLAMMGILLAILFSGITVLAYGYGTAPKPDETVVSQIASETFGRNVFYYVIQGVTSLILVLAANTGFSAFPQLAFNLARDQYMPRMFTVRGDRLGFSNGIIFLGFASIVLIILFGGQTEHLIPLYAVGVFIPFTLSQTGMCMKWIKQKPKGWIGKMLINSCGALISFMVLSILFVTKFNVVWPVLIFMPIVVLLFFAIKNHYTAVGEQLRIVDKEPEEIKGTVVIVPVAGVTTVVQKSIHYAKSLSDQVIAVHVSFDREQEKKFEKRWEELNNGVRLVTLHSSYRSLVHPFDKFLETVEAKAKKEQFSVMVLFPQFITKKRWHTILHNQSAFLLRVRLFWKKDIMVATLPYHFKK | Function: High-affinity potassium transporter . Functions as a K(+)/H(+) symporter .
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66771
Sequence Length: 607
Subcellular Location: Cell membrane
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P46086 | MEVKARAPGKIILAGEHAVVHGSTAVAAAIDLYTYVTLRFPLPSAENNDRLTLQLKDISLEFSWSLARIKEAIPYDSSTLCRSTPASCSEETLKSIAVLVEEQNLPKEKMWLSSGISTFLWLYTRIIGFNPATVVINSELPYGSGLGSSAALCVALTAALLASSISEKTRGNGWSSLDETNLELLNKWAFEGEKIIHGKPSGIDNTVSAYGNMIKFCSGEITRLQSNMPLRMLITNTRVGRNTKALVSGVSQRAVRHPDAMKSVFNAVDSISKELAAIIQSKDETSVTEKEERIKELMEMNQGLLLSMGVSHSSIEAVILTTVKHKLVSKLTGAGGGGCVLTLLPTGTVVDKVVEELESSGFQCFTALIGGNGAQICY | Function: Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis.
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 40644
Sequence Length: 378
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
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Q86AG7 | MISNQDNIIQVSAPGKIILFGEHAVVLEKTAIASALSLRTTVTFTPNTNNTLLLDFPDLAGFGVREWSLDEFKKLDHFPNDIDILKPIECSELFQQELNKIIDIKGIHTFLFLFCALTKCTKAYNIKITSDLPIGAGLGSSASFCVSICAGLLKAFDTYICGGCKQCIGGQGQQQQICNEQLNLINLWSLQGEKIMHGTPSGIDNAVATFGKALTFTRKNGYKILENGIPPLRILITNTRVSRSTKTLVEGVIQRSKLYPTLIDPVSNLIDTISSQCIESFNQYHTDKDYEKLQQTMDLMFDMNQHLLSGCYGVGHSSIDTIVSITKSLGFHTKLTGAGGGGCVITLLKQDTTIDQLSNLKLTLSSNGFESWEATIGDPGVSINILPIQK | Function: Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid biosynthesis.
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 42618
Sequence Length: 390
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
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Q03426 | MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKRAWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSICRKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKEDLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVPRNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDMNQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQALTSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL | Function: Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis .
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 42451
Sequence Length: 396
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
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P17256 | MLSEVLLVSAPGKVILHGEHAVVHGKVALAVALNLRTFLVLRPQSNGKVSLNLPNVGIKQVWDVATLQLLDTGFLEQGDVPAPTLEQLEKLKKVAGLPRDCVGNEGLSLLAFLYLYLAICRKQRTLPSLDIMVWSELPPGAGLGSSAAYSVCVAAALLTACEEVTNPLKDRGSIGSWPEEDLKSINKWAYEGERVIHGNPSGVDNSVSTWGGALRYQQGKMSSLKRLPALQILLTNTKVPRSTKALVAGVRSRLIKFPEIMAPLLTSIDAISLECERVLGEMAAAPVPEQYLVLEELMDMNQHHLNALGVGHASLDQLCQVTAAHGLHSKLTGAGGGGCGITLLKPGLERAKVEAAKQALTGCGFDCWETSIGAPGVSMHSATSIEDPVRQALGL | Function: Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis.
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 41988
Sequence Length: 395
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
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Q38997 | MDGSGTGSRSGVESILPNYKLGRTLGIGSFGRVKIAEHALTGHKVAIKILNRRKIKNMEMEEKVRREIKILRLFMHPHIIRLYEVIETPTDIYLVMEYVNSGELFDYIVEKGRLQEDEARNFFQQIISGVEYCHRNMVVHRDLKPENLLLDSKCNVKIADFGLSNIMRDGHFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGTLPFDDENIPNLFKKIKGGIYTLPSHLSPGARDLIPRMLVVDPMKRVTIPEIRQHPWFQAHLPRYLAVPPPDTVQQAKKIDEEILQEVINMGFDRNHLIESLRNRTQNDGTVTYYLILDNRFRASSGYLGAEFQETMEGTPRMHPAESVASPVSHRLPGLMEYQGVGLRSQYPVERKWALGLQSRAHPREIMTEVLKALQDLNVCWKKIGHYNMKCRWVPNSSADGMLSNSMHDNNYFGDESSIIENEAAVKSPNVVKFEIQLYKTRDDKYLLDLQRVQGPQFLFLDLCAAFLAQLRVL | Function: Catalytic subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, a central regulator of cellular energy homeostasis, which, in response to seemingly unrelated darkness, sugar and stress conditions, activates energy-producing pathways and inhibits energy-consuming processes. May play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase and in assimilation of nitrogen by phosphorylating nitrate reductase . In vitro, KIN10 exhibits kinase activity on sucrose phosphate synthase and the kinase activity is inhibited by PRL1 . May be a subunit of a SCF ubiquitin ligase complex and thus be involved in proteasomal ubiquitination . Phosphorylates GRIK1/SNAK2 and GRIK2/SNAK1 in vitro . Cooperates with FUS3 to regulate developmental phase transitions and lateral organ development and act both as positive regulators of abscisic acid (ABA) signaling during germination . Phosphorylates FUS3 in embryo . Negatively modulates MYC2 accumulation through its protein phosphorylation . Phosphorylates geminivirus (CaLCuV, TGMV, ToMoV) AL2 protein resulting in a delay in the viral DNA accumulation and symptom appearance during infection . Regulates bZIP63 activity to alter metabolism in response to starvation through its protein phosphorylation . Under sugar deprivation conditions, antagonizes the IDD8 function in flowering time control by its protein phosphorylation . Plays a cardinal role in the control of cell proliferation through inhibition of KRP6 activity by its protein phosphorylation . Under submergence, phosphorylates PTP1, leading to the release of the MPK6 signaling pathway inhibition . Triggers its own SUMO-mediated proteasomal degradation, establishing a negative feedback loop that attenuates SnRK1 signaling and prevents detrimental hyperactivation of stress responses . Phosphorylates RAPTOR1B in vitro . Phosphorylates and down-regulates HMGR1S in vitro . Kinase activity is redox-sensitive . Acts upstream of TOR in the regulation of autophagy. Required for the activation of autophagy by many abiotic stresses . Involved in positive regulation of autophagy, possibly by affecting the phosphorylation of ATG1 proteins . Negatively modulates WRI1 accumulation through its protein phosphorylation . Modulates leaf senescence progression by the negative regulation of EIN3 accumulation through its protein phosphorylation . Under extended darkness, C/S1-bZIP-SnRK1 complex interacts with the histone acetylation machinery to remodel chromatin and facilitate transcription. BZIP2-BZIP63-KIN10 complex binds to the ETFQO promoter to up-regulate its transcription . Phosphorylates and down-regulates IPK2b in vitro . Involved in the regulation of sucrose-induced hypocotyl elongation under light/dark cycles .
PTM: Phosphorylated at Thr-175 in response to glucose . Phosphorylated at Thr-175 under submergence . Autophosphorylated . Dephosphorylated at Thr-175 by ABI1 and PP2CA .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 58373
Sequence Length: 512
Domain: The regulatory domain (RD) contains the auto-inhibitory domain (AID) that inhibits kinase activity of the protein kinase domain (KD).
Subcellular Location: Plastid
EC: 2.7.11.1
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Q2G5F0 | MAKLYFYYASMNAGKSTNLLQADFNYRERGMATMLWTAALDDRGGERAIESRIGLGADAHRFDAGTDLWQRISAAHAVQPLSCVLVDEAQFLRRDQVWQLARVADAAGIPVLCYGLRTDFQGELFEGSAALLGIADSLIELKAVCHCGRKATMNLRVDDSGAAVRAGRQTEIGGNDRYVALCRRHFSEAMGQ | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 21079
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 2.7.1.21
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B2RJJ6 | MDYEIENNHADSIRRGSIEVICGSMFSGKTEELLRRLRRAKIARQTVEIFKPTIDIRYDETDVVSHDKNAIASAPVDNSANILLLSSQVDVVGIDEAQFFDEGLVEVAQQLADQGVRVVIAGLDMDFRRQPFGPMPGLCAIADSVTKVHAVCVECGRLASYSFRRVQGDQQVMLGELNEYSPLCRTCYRKCSSPPQTEEIHSTI | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 22711
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.1.21
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Q6UDK9 | MGRIVVLYVDGAFGIGKTTVLRQIQKSAAYRFRRIYLEEPMRAWRSWFVDDHDAIREIYTTQELKDAGEIDLREASRRVCYAQVSLSAPFHIMNAVIYGIISGESEATSAHLGEGDYFVGVDRHPLASCLCFPVARFVTGYLEYTDLIALVATLPDYPRGASIAILDLSVEEQARRITERSRSGEHVNKTFLRILRNVFIIMYNTVAYLRNVSIDKACADREALEDFRGSQLESDMHKIDIQPRDDPNASETLFAVMASDATWRKNRKQSALFVYTMAKLDALLRSLNMHIVDINGLSQEQCAEKVVAISSKVPAVTARGNAPDLLFDAVEAYNADMGV | Function: Catalyzes the transfer of the gamma-phospho group of ATP to thymidine to generate dTMP in the salvage pathway of pyrimidine synthesis. The dTMP serves as a substrate for DNA polymerase during viral DNA replication. Allows the virus to be reactivated and to grow in non-proliferative cells lacking a high concentration of phosphorylated nucleic acid precursors.
Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 38059
Sequence Length: 339
EC: 2.7.1.21
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Q8ZV53 | MLVVIVGPMFAGKTTELIRRVERYVIAGRRAIVFKPSLDVRYDASKVAAHNGLKFDAFVIPPDKDGVEIIRKMGAEYDVVAVDEIQFFPVDLADALNQLANGRIVIAAGLNLDFRGEPFETTARAMAFADRVISLSAVCKLCGKPATRTQRLINGVPAPRHSPRILIGGNESYEARCRRHYVIPP | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 20390
Sequence Length: 185
Subcellular Location: Cytoplasm
EC: 2.7.1.21
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Q90029 | MNGGHIQLIIGPMFSGKSTELIRRVRRYQIAQYKCITIKYTNDTRYGTGLWTHDKHNFSAMETTKLLNIIDAVTDFSVIGIDEGQFFPDIVEFCEYMANNGKIVIVAALDGTFQRKPFTTISNLIPLSEMVVKLTAVCMKCFKEASFSKRLGTETEIEIIGGEDMYQSVCRKCYINE | Function: Phosphorylates thymidine and thymidine analogs, such as azidothymidine (AZT). Part of the salvage pathway for pyrimidine deoxyribonucleotide synthesis.
Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 20091
Sequence Length: 177
EC: 2.7.1.21
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P27158 | MSYINLPTVLPISPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTRYSNSFSTHDRNTMDALPACMLKDVAQEALGVAVIGIDEGQFFPDIVDFCETMANTGKTVIV | Function: Cell-cycle-regulated enzyme of importance in nucleotide metabolism. Catalyzes the first enzymatic step in the salvage pathway converting thymidine into thymidine monophosphate. Transcriptional regulation limits expression to the S phase of the cell cycle and transient expression coincides with the oscillation in the intracellular dTTP concentration.
PTM: Phosphorylated on Ser-13 in mitosis. Phosphorylation of Ser-13 by CDK1 during mitosis reduces homotetramerization and catalytic efficiency when DNA replication is complete and intracellular TK1 is still present at a high level.
Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 13511
Sequence Length: 121
Domain: KEN box sequence located in the C-terminal region is required for its mitotic degradation by the APC/C-FZR1 ubiquitin ligase and interaction capability with FZR1.
Subcellular Location: Cytoplasm
EC: 2.7.1.21
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P86110 | MESSRKSYVLMLFLAFVIMNVCSVSGEPKDGEIAGFEMEEARYDACVNACLEHHPNVRECEEACKNPVPP | Function: Voltage-independently blocks potassium currents on hKv1.1/KCNA1 (IC(50)=217 uM), and hKv1.4/KCNA4 (IC(50)=71 uM) (expressed in CHO cells).
Sequence Mass (Da): 7823
Sequence Length: 70
Domain: Has the structural arrangement of two alpha-helices stabilized by disulfide bonds (CSalpha/alpha 2(S-S)).
Subcellular Location: Secreted
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C5J893 | MKTSKMICAFLLVLVVGTFNDISGAYGEYVEDQHSFKIERRFPPCVEVCVQHTGNVKECEAACGE | Function: Potassium channel inhibitor (Kv).
Sequence Mass (Da): 7229
Sequence Length: 65
Domain: Has the structural arrangement of two alpha-helices stabilized by disulfide bonds (CSalpha/alpha 2(S-S)).
Subcellular Location: Secreted
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P0DJ35 | GTVYVFLLLLAFGIFTDISNACSEQMDDEDSYEVEKRGNACIEVCLQHTGNPAECDKPCDK | Function: Voltage-gated potassium channel inhibitor (Kv) that acts on Kv1.3/KCNA3 and Kv7.1/KCNQ1. 1 uM of the toxin inhibits Kv1.3/KCNA3 currents by 35.1%, whereas 10 uM of the toxin inhibits Kv7.1/KCNQ1 currents by 44.9%.
Sequence Mass (Da): 6748
Sequence Length: 61
Domain: Has the structural arrangement of two alpha-helices stabilized by disulfide bonds (CSalpha/alpha 2(S-S)).
Subcellular Location: Secreted
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C0HKB3 | VDACYEACMHHHMNSDDCIEACKNPVPP | Function: Reversibly blocks voltage-gated potassium channels Kv1.2/KCNA2 and Kv1.3/KCNA3.
PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 3131
Sequence Length: 28
Subcellular Location: Secreted
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P0DJ41 | MKLLPLLFVILIVCAILPDEASCDQSELERKEENFKDESREIVKRSCKKECSGSRRTKKCMQKCNREHGHGR | Function: Weak blocker of potassium channels Kv1.1/KCNA1 (IC(50)=578.5 nM-9.9 uM) and Kv1.6/KCNA6 (~60% block at 30 uM of toxin) . Acts by binding to the pore and occluding it . Has a voltage-dependent mode of action, which can be explained by a high content of basic residues causing repulsions at higher membrane voltages . Shows a weak interaction with muscle-type nicotinic acetylcholine receptors (nAChR), since it inhibits alpha-bungarotoxin binding to muscle-type nAChR from T.californica (IC(50)=1.4 uM) . This suggests it probably weakly inhibits muscle nAChR . The mode of binding to potassium channels of this toxin differs from its homologs (including HefuTx1), since it lacks the key aromatic residue of the functionnal dyad. In contrast, its functionally important site is composed of a number of basic residues .
Sequence Mass (Da): 8380
Sequence Length: 72
Domain: Has the structural arrangement of two alpha-helices stabilized by disulfide bonds (CSalpha/alpha 2(S-S)).
Subcellular Location: Secreted
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Q5ZJU2 | MAGDVEGFSSSIHDTSVSAGFRALYEEGLLLDVTLVIEDHQFQAHKALLATQSDYFRIMFTADMRERDQDKIHLKGLTATGFSHVLQFMYYGTIELSMNTVHEILQAAMYVQLIEVVKFCCSFLLAKICLENCAEIMRLLDDFSVNIEGVREKLDSFLLENFVPLMSRPDFLSYLSFEKLMSYLDNDHLSRFPEIELYEAVQAWLRHDRRRWRHTDTIIQNIRFCLMTPSSVFEKVKTSEFYRYSRQLRHEVDQAMNYFHSVHQQPLMEMKSNKIRSAKPQTAVFRGMIGHSMVNSKILLLHKPRVWWELEGPQVPLRPDCLAIVNNFVFLLGGEELGPDGEFHASSKVFRYDPRQNTWLRMADMSVPRSEFAVGVIGRYVYAVAGRTRDETFYSTERYDITEDKWEFVDPYPVNKYGHEGTVLGNKLYITGGITSSSTSKQVCVFDPSKEGTVEQRTRRTQVATNCWENKCKMNYARCFHKMISYNA | Function: Substrate-specific adapter for CUL3 E3 ubiquitin-protein ligase complex.
Sequence Mass (Da): 56659
Sequence Length: 488
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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Q96M94 | MAGDVEGFCSSIHDTSVSAGFRALYEEGLLLDVTLVIEDHQFQAHKALLATQSDYFRIMFTADMRERDQDKIHLKGLTATGFSHVLQFMYYGTIELSMNTVHEILQAAMYVQLIEVVKFCCSFLLAKICLENCAEIMRLLDDFGVNIEGVREKLDTFLLDNFVPLMSRPDFLSYLSFEKLMSYLDNDHLSRFPEIELYEAVQSWLRHDRRRWRHTDTIIQNIRFCLMTPTSVFEKVKTSEFYRYSRQLRYEVDQALNYFQNVHQQPLLDMKSSRIRSAKPQTTVFRGMIGHSMVNSKILLLKKPRVWWELEGPQVPLRPDCLAIVNNFVFLLGGEELGPDGEFHASSKVFRYDPRQNSWLQMADMSVPRSEFAVGVIGKFIYAVAGRTRDETFYSTERYDITNDKWEFVDPYPVNKYGHEGTVLNNKLFITGGITSSSTSKQVCVFDPSKEGTIEQRTRRTQVVTNCWENKSKMNYARCFHKMISYNGKLYVFGGVCVILRASFESQGCPSTEVYNPETDQWTILASMPIGRSGHGVTVLDKQIMVLGGLCYNGHYSDSILTFDPDENKWKEDEYPRMPCKLDGLQVCNLHFPDYVLDEVRRCN | Function: Substrate-specific adapter for CUL3 E3 ubiquitin-protein ligase complex . Acts as an adapter for CUL3 to target the serine/threonine-protein phosphatase 2A (PP2A) subunit PPP2R5B for ubiquitination and subsequent proteasomal degradation, thus promoting exchange with other regulatory subunits . Acts as an adapter for CUL3 to target the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation . Through the regulation of RBBP8/CtIP protein turnover, plays a key role in DNA damage response, favoring DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR) .
Sequence Mass (Da): 69775
Sequence Length: 604
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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Q6TDP4 | MQPRSERPAGRTQSPEHGSPGPGPEAPPPPPPQPPAPEAERTRPRQARPAAPMEGAVQLLSREGHSVAHNSKRHYHDAFVAMSRMRQRGLLCDIVLHVAAKEIRAHKVVLASCSPYFHAMFTNEMSESRQTHVTLHDIDPQALDQLVQFAYTAEIVVGEGNVQTLLPAASLLQLNGVRDACCKFLLSQLDPSNCLGIRGFADAHSCSDLLKAAHRYVLQHFVDVAKTEEFMLLPLKQVLELVSSDSLNVPSEEEVYRAVLSWVKHDVDARRQHVPRLMKCVRLPLLSRDFLLGHVDAESLVRHHPDCKDLLIEALKFHLLPEQRGVLGTSRTRPRRCEGAGPVLFAVGGGSLFAIHGDCEAYDTRTDRWHVVASMSTRRARVGVAAVGNRLYAVGGYDGTSDLATVESYDPVTNTWQPEVSMGTRRSCLGVAALHGLLYSAGGYDGASCLNSAERYDPLTGTWTSVAAMSTRRRYVRVATLDGNLYAVGGYDSSSHLATVEKYEPQVNVWSPVASMLSRRSSAGVAVLEGALYVAGGNDGTSCLNSVERYSPKAGAWESVAPMNIRRSTHDLVAMDGWLYAVGGNDGSSSLNSIEKYNPRTNKWVAASCMFTRRSSVGVAVLELLNFPPPSSPTLSVSSTSL | Function: Substrate-recognition component of some cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes. The BCR(KLHL17) complex mediates the ubiquitination and subsequent degradation of GLUR6. May play a role in the actin-based neuronal function (By similarity).
Sequence Mass (Da): 69874
Sequence Length: 642
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Postsynaptic density
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Q6TDP3 | MQPRGERPAGRTQSPEHSSPGPGPEAPPPPQPPAPEAERARPRQARPAAPMEGAMQLLSREGHSVAHNSKRHYHDAFVAMSRMRQRGLLCDIVLHVAAKEIRAHKVVLASCSPYFHAMFTNEMSESRQTHVTLHDIDPQALDQLVQFAYTAEIVVGEGNVQTLLPAASLLQLNGVRDACCKFLLSQLDPSNCLGIRGFADTHSCSDLLKAAHRYVLQHFVDVAKTEEFMLLPLKQVLELVSSDSLNVPSEEDVYRAVLSWVKHDVDTRRQHVPRLMKCVRLPLLSRDFLLGHVDAESLVRHHPDCKDLLIEALKFHLLPEQRGVLGTSRTRPRRCEGAGPVLFAVGGGSLFAIHGDCEAYDTRTDRWHVVASMSTRRARVGVAAVGNRLYAVGGYDGTSDLATVESYDPVTNTWQPEVSMGTRRSCLGVAALHGLLYAAGGYDGASCLNSAERYDPLTGTWTSIAAMSTRRRYVRVATLDGNLYAVGGYDSSSHLATVEKYEPQVNSWTPVASMLSRRSSAGVAVLEGALYVAGGNDGTSCLNSVERYSTKAGAWESVAPMNIRRSTHDLVAMDGWLYAVGGNDGSSSLNSIEKYNPRTNKWVAASCMFTRRSSVGVAVLELLNFPPPSSPTLSVSSTSL | Function: Substrate-recognition component of some cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes. The BCR(KLHL17) complex mediates the ubiquitination and subsequent degradation of GLUR6. May play a role in the actin-based neuronal function (By similarity).
Sequence Mass (Da): 69732
Sequence Length: 640
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Postsynaptic density
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Q9Y2M5 | MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSIQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVLFAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTSTCRTSVGVAVLGGFLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERYNPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVGGFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis . The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination . Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking . Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 . In case of tumor, the BCR(KLHL20) E3 ubiquitin ligase complex is involved in tumor hypoxia: following hypoxia, the BCR(KLHL20)complex mediates ubiquitination and degradation of PML, potentiating HIF-1 signaling and cancer progression .
Sequence Mass (Da): 67955
Sequence Length: 609
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q5R7B8 | MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSTQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVLFAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTSTCRTSVGVAVLGGFLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERYNPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVRGFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis. The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination. Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking. Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (By similarity).
Sequence Mass (Da): 68042
Sequence Length: 609
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q6DFF6 | MRRCLNTRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYVSDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFSYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSIQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVLFAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTSTCRTSVGVAVLGGYLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERYNPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVGGFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome. It also specifically mediates 'Lys-33'-linked ubiquitination (By similarity).
Sequence Mass (Da): 67430
Sequence Length: 604
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q9UEF7 | MPASAPPRRPRPPPPSLSLLLVLLGLGGRRLRAEPGDGAQTWARFSRPPAPEAAGLFQGTFPDGFLWAVGSAAYQTEGGWQQHGKGASIWDTFTHHPLAPPGDSRNASLPLGAPSPLQPATGDVASDSYNNVFRDTEALRELGVTHYRFSISWARVLPNGSAGVPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDAYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGIRGSPRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGQVSIALSSHWINPRRMTDHSIKECQKSLDFVLGWFAKPVFIDGDYPESMKNNLSSILPDFTESEKKFIKGTADFFALCFGPTLSFQLLDPHMKFRQLESPNLRQLLSWIDLEFNHPQIFIVENGWFVSGTTKRDDAKYMYYLKKFIMETLKAIKLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVDFLSQDKMLLPKSSALFYQKLIEKNGFPPLPENQPLEGTFPCDFAWGVVDNYIQVDTTLSQFTDLNVYLWDVHHSKRLIKVDGVVTKKRKSYCVDFAAIQPQIALLQEMHVTHFRFSLDWALILPLGNQSQVNHTILQYYRCMASELVRVNITPVVALWQPMAPNQGLPRLLARQGAWENPYTALAFAEYARLCFQELGHHVKLWITMNEPYTRNMTYSAGHNLLKAHALAWHVYNEKFRHAQNGKISIALQADWIEPACPFSQKDKEVAERVLEFDIGWLAEPIFGSGDYPWVMRDWLNQRNNFLLPYFTEDEKKLIQGTFDFLALSHYTTILVDSEKEDPIKYNDYLEVQEMTDITWLNSPSQVAVVPWGLRKVLNWLKFKYGDLPMYIISNGIDDGLHAEDDQLRVYYMQNYINEALKAHILDGINLCGYFAYSFNDRTAPRFGLYRYAADQFEPKASMKHYRKIIDSNGFPGPETLERFCPEEFTVCTECSFFHTRKSLLAFIAFLFFASIISLSLIFYYSKKGRRSYK | Function: May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 239 and 872, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D (By similarity). Essential factor for the specific interaction between FGF23 and FGFR1 (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 116181
Sequence Length: 1012
Domain: Contains 2 glycosyl hydrolase 1 regions. However, the first region lacks the essential Glu active site residue at position 239, and the second one lacks the essential Glu active site residue at position 872.
Subcellular Location: Cell membrane
EC: 3.2.1.31
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Q8WP17 | MPASAPPRRPRPPPPSLSLSLLLVLLGLAGRRLRAEPGDGAQTWARFARPPAPEAAGLFQGTFPDGFLWAVGSAAYQTEGGWQQHGKGASIWDTFTHHPLAPPGDSRIANVPSGAPSPLQPATGDVASDSYNNVFRDTEALRELGVTHYRFSISWARVLPNGSAGVPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDAYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGIRGSPRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGQVSIALSSHWINPRRMTDHSIKECQKSLDFVLGWFAKPIFIDGDYPESMKNNLSSLLPDFTESEKKFIKGTADFFALSFGPTLSFQLLDPHMKFRQLESPSLRQLLSWIDLEYNHPQIFIVENGWFVSGTTKRDDAKYMYYLKKFIMETLKAIKLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVDFLSQEKTLLPKSSALFYQKLIEKNGFPPLPENQPLEGTFPCDFAWGIVDNYIQVDTTLSQFTDLNVYLWDVHHSKRLIKVDGVVTKKRKSYCVDFAAIQPQITLLQEMHVTHFRFSLDWALILPLGNQSQVNHTILQYYRCMVSELVRVNITPVVALWQPVAPNQGLPRLLARQGAWENPYTALAFAEYARLCFQELGHHVKLWITMNEPYTRNMTYSAGHNLLKAHALAWHVYNEKFRHAQNGKISIALQADWIEPACPFSQKDKEVAERVLEFDIGWLAEPIFGSGDYPWVMRDWLNQRNNFLLPYFTEDEKKLIQGTFDFLALSHYTTILVDSEKEDPIKYNDYLEVQEMTDITWLNSPSQVAVVPWGLRKVLNWLKFKYGDLPMYIISNGIDDGLHAEDDQLRVYYMQNYINEALKAHILDGINLCGYFAYSFNDRTAPRFGLYRFAADQFEPKPSMKHYRKIIDSNGFPGPETLEKFCPEEFTVCTECSFFHTRKPLVAFIAFLFFAFIVSLSLIFYYSKKGRRRYQ | Function: May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 241 and 874, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D (By similarity). Essential factor for the specific interaction between FGF23 and FGFR1 (By similarity).
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 116469
Sequence Length: 1014
Domain: Contains 2 glycosyl hydrolase 1 regions. However, the first region lacks the essential Glu active site residue at position 241, and the second one lacks the essential Glu active site residue at position 874.
Subcellular Location: Cell membrane
EC: 3.2.1.31
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O35082 | MLARAPPRRPPRLVLLRLLLLHLLLLALRARCLSAEPGQGAQTWARFARAPAPEAAGLLHDTFPDGFLWAVGSAAYQTEGGWRQHGKGASIWDTFTHHSGAAPSDSPIVVAPSGAPSPPLSSTGDVASDSYNNVYRDTEGLRELGVTHYRFSISWARVLPNGTAGTPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDTYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGVRGSSRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGRVSIALSSHWINPRRMTDYNIRECQKSLDFVLGWFAKPIFIDGDYPESMKNNLSSLLPDFTESEKRLIRGTADFFALSFGPTLSFQLLDPNMKFRQLESPNLRQLLSWIDLEYNHPPIFIVENGWFVSGTTKRDDAKYMYYLKKFIMETLKAIRLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVDFLSQDKELLPKSSALFYQKLIEDNGFPPLPENQPLEGTFPCDFAWGVVDNYVQVDTTLSQFTDPNVYLWDVHHSKRLIKVDGVVAKKRKPYCVDFSAIRPQITLLREMRVTHFRFSLDWALILPLGNQTQVNHTVLHFYRCMISELVHANITPVVALWQPAAPHQGLPHALAKHGAWENPHTALAFADYANLCFKELGHWVNLWITMNEPNTRNMTYRAGHHLLRAHALAWHLYDDKFRAAQKGKISIALQADWIEPACPFSQNDKEVAERVLEFDIGWLAEPIFGSGDYPRVMRDWLNQKNNFLLPYFTEDEKKLVRGSFDFLAVSHYTTILVDWEKEDPMKYNDYLEVQEMTDITWLNSPSQVAVVPWGLRKVLNWLRFKYGDLPMYVTANGIDDDPHAEQDSLRIYYIKNYVNEALKAYVLDDINLCGYFAYSLSDRSAPKSGFYRYAANQFEPKPSMKHYRKIIDSNGFLGSGTLGRFCPEEYTVCTECGFFQTRKSLLVFISFLVFTFIISLALIFHYSKKGQRSYK | Function: May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 241 and 874, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D. Essential factor for the specific interaction between FGF23 and FGFR1.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate
Sequence Mass (Da): 116398
Sequence Length: 1014
Domain: Contains 2 glycosyl hydrolase 1 regions. However, the first region lacks the essential Glu active site residue at position 241, and the second one lacks the essential Glu active site residue at position 874.
Subcellular Location: Cell membrane
EC: 3.2.1.31
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F4HXU3 | MDVKKDENSILENMKQEINHSLKEEAQEEEEILKKRISSHPLYGLLLHSHLNCLKVCSGDFDSPEIMNTADDLALSKLSLHPDSSSEATSSELDQFMVLFFFSPCQNIFTQQKTTFHVLLFFPLQINLTFKYSKFILPRKKQ | Function: Transcriptional regulator involved in leaf proximal/distal patterning. May act by sequestering BELL transcription factors.
Sequence Mass (Da): 16439
Sequence Length: 142
Domain: The MEINOX domain (33-138) is sufficient for interactions with BELL proteins . The BP-interacting domain (BPID, 1-32) is necessary for interactions with KNOX proteins .
Subcellular Location: Cytoplasm
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A6PVL3 | MDIPISSRDFRGLQLACVALGLVAGSIIIGISVSKAAAAMGGVFIGAAVLGLLILAYPFLKARFNLDHILPTIGSLRIHPHPGADHGEGRSSTNGNKEGARSSLSTVSRTLEKLKPGTRGAEEC | Function: May play a role in stabilizing dense microtubular networks or in vesicular trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12832
Sequence Length: 124
Subcellular Location: Membrane
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Q307W7 | MDIPISTRDFRCLQLACVALGLVAGSIIIGVSVSKAAAAVGGIFLGAAGLGLLIFAYPFLKARFNLDHILPAIGNLRIHPNSGPDHGEGRSSNNSNKEGARSGLSTVTRTLEKLKPGGRGTEEG | Function: May play a role in stabilizing dense microtubular networks or in vesicular trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12809
Sequence Length: 124
Subcellular Location: Membrane
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P01042 | MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRITEATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFSVATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLNEVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLRIASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFKIDNVKKARVQVVAGKKYFIDFVARETTCSKESNEELTESCETKKLGQSLDCNAEVYVVPWEKKIYPTVNCQPLGMISLMKRPPGFSPFRSSRIGEIKEETTVSPPHTSMAPAQDEERDSGKEQGHTRRHDWGHEKQRKHNLGHGHKHERDQGHGHQRGHGLGHGHEQQHGLGHGHKFKLDDDLEHQGGHVLDHGHKHKHGHGHGKHKNKGKKNGKHNGWKTEHLASSSEDSTTPSAQTQEKTEGPTPIPSLAKPGVTVTFSDFQDSDLIATMMPPISPAPIQSDDDWIPDIQIDPNGLSFNPISDFPDTTSPKCPGRPWKSVSEINPTTQMKESYYFDLTDGLS | Function: Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation of thrombocytes. LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting.
PTM: Bradykinin is inactivated by ACE, which removes the dipeptide Arg-Phe from its C-terminus.
Sequence Mass (Da): 71957
Sequence Length: 644
Subcellular Location: Secreted
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P09217 | MPSRTDPKMDRSGGRVRLKAHYGGDILITSVDPTTTFQDLCEEVRDMCGLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLACQGRDEVLIIHVFPSIPEQPGMPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHVLVPLTCRRHMDSVMPSQEPPVDDKNDGVDLPSEETDGIAYISSSRKHDNIKDDSEDLKPVIDGVDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSAEESV | Function: Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Phosphorylates VAMP2 in vitro (By similarity).
PTM: CDH5 is required for its phosphorylation at Thr-410. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2. Phosphorylation at Thr-410 by PI3K activates the kinase (By similarity).
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 67733
Sequence Length: 592
Domain: The PB1 domain mediate mutually exclusive interactions with SQSTM1 and PARD6B.
Subcellular Location: Cytoplasm
EC: 2.7.11.13
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Q05652 | MSGVQTAEAEAQAQNQANGNRTRSRSHLDNTMAIRLLPLPVRAQLCAHLDALDVWQQLATAVKLYPDQVEQISSQKQRGRSASNEFLNIWGGQYNHTVQTLFALFKKLKLHNAMRLIKDYVSEDLHKYIPRSVPTISELRAAPDSSAKVNNGPPFPSSSGVSNSNNNRTSTTATEEIPSLESLGNIHISTVQRAAESLLEIDYAELENATDGWSPDNRLGQGGFGDVYRGKWKQLDVAIKVMNYRSPNIDQKMVELQQSYNELKYLNSIRHDNILALYGYSIKGGKPCLVYQLMKGGSLEARLRAHKAQNPLPALTWQQRFSISLGTARGIYFLHTARGTPLIHGDIKPANILLDQCLQPKIGDFGLVREGPKSLDAVVEVNKVFGTKIYLPPEFRNFRQLSTGVDVYSFGIVLLEVFTGRQVTDRVPENETKKNLLDYVKQQWRQNRMELLEKHLAAPMGKELDMCMCAIEAGLHCTALDPQDRPSMNAVLKRFEPFVTD | Function: Plays an essential role in the Tl receptor signaling pathway that establishes embryonic dorsoventral polarity; the signal directs import of dl into ventral and ventrolateral nuclei, thereby establishing dorsoventral polarity. Tub recruits pll to the plasma membrane and protein-protein interaction activates pll.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 56160
Sequence Length: 501
Subcellular Location: Cell membrane
EC: 2.7.11.1
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P42818 | MVSSQRPVPNKIQKQQYLSISPSNSVLKDDVELEFSDVFGPLPEEANDIAYDEPAVVYSRSHSLVGPCSLDSHSLKLTKLTLLETEDSIDLVECLEGESLKENDDFSGNDDSDNEKALEGDLVKVSGVVGIDDFEVMKVVGKGAFGKVYQVRKKETSEIYAMKVMRKDHIMEKNHAEYMKAERDILTKIDHPFIVQLKYSFQTKYRLYLVLDFINGGHLFFQLYHQGLFREDLARVYTAEIVSAVSHLHEKGIMHRDLKPENILMDTDGHVMLTDFGLAKEFEENTRSNSMCGTTEYMAPEIVRGKGHDKAADWWSVGILLYEMLTGKPPFLGSKGKIQQKIVKDKIKLPQFLSNEAHAILKGLLQKEPERRLGSGLSGAEEIKQHKWFKGINWKKLEAREVMPSFKPEVSGRQCIANFDKCWTDMSVLDSPASSPSSDPKANPFTNFTYVRPPPSFLHQSTTTL | Function: Downstream effector of TOR signaling pathway involved in osmotic stress response . Could be involved in the control of plant growth and development . Phosphorylates the ribosomal proteins P14, P16 and S6 . Functions as a repressor of cell proliferation and required for maintenance of chromosome stability and ploidy levels through the RBR1-E2F pathway . Mediates the phosphorylation of MRFs (e.g. MRF1) .
PTM: Undergoes serine-specific autophosphorylation. Phosphorylated at Thr-449 by TOR.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 52588
Sequence Length: 465
Domain: The activation loop within the kinase domain is the target of phosphorylation.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q02595 | MEKRYQQLFKGKRIDFPLATGAASHVSLTYDEKKNPYLLCWTYIYQEKPEFTVPLKGCRIINNITEIGPCIHIITSNEEYQFQCRSKEEFDEMSQFFNMLGYPILGFKNVYVLNKKIGKGSFSTAYIGTNILYGNRVVVKEVDKSKVKESNVYTEIEVLRKVMHKYIIKLISAYEQEGFVYLVLEYLKGGELFEYLNNNGPYTEQVAKKAMKRVLIALEALHSNGVVHRDLKMENLMLENPNDPSSLKIIDFGLASFLNSPSMNMRCGSPGYVAPEILKCASYGTKVDIFSLGVILFNILCGYPPFRGNNVKEIFKKNMRCHISFNTKHWINKSESVKEIILWMCCKNPDDRCTALQALGHQWFLPKLTDMHMTANINELKRNEAIVHKSNDQQDMCKKCKHFNNTQNDDIYNNNNNNNQLDPNKNHKNNYNDYKNYFDTMLKIDDKYSENLIKDKTSMDSISLNKKDYDAYLVHSNEHDTVVLHGKCQTTKNSSSLLSYKCSRRSPPQN | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 59006
Sequence Length: 510
Subcellular Location: Membrane
EC: 2.7.11.1
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P19924 | MSERYPIIAITGSSGAGTTSVTRTFENIFCREGVKSVVIEGDSFHRYDRAEMKVKMAEAERTGNMNFSHFGAENNLFGDLESLFRSYAESGTGMRRRYLHSTEEAAPFGQQPGTFTAWEPLPADTDLLFYEGLHGGVVTDEVNVAQYPNLLIGVVPVINLEWIQKLWRDKKQRGYSTEAVTDTILRRMPDYVNYICPQFSRTHVNFQRVPCVDTSNPFISREIPAPDESMVVIRFANPKGIDFQYLLSMIHDSFMSRANTIVVPGGKMELAMQLIFTPFVLRMMERRKRAAL | Catalytic Activity: ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate + H(+)
Sequence Mass (Da): 33161
Sequence Length: 292
Pathway: Carbohydrate biosynthesis; Calvin cycle.
EC: 2.7.1.19
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P25933 | XEKXIVVGLAADSG | Catalytic Activity: ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate + H(+)
Sequence Mass (Da): 1381
Sequence Length: 14
Pathway: Carbohydrate biosynthesis; Calvin cycle.
EC: 2.7.1.19
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P25934 | ADEKXVVIGLAADSG | Catalytic Activity: ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate + H(+)
Sequence Mass (Da): 1456
Sequence Length: 15
Pathway: Carbohydrate biosynthesis; Calvin cycle.
EC: 2.7.1.19
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P25697 | MAVSTIYSTQALNSTHFLTSSSSSKQVFLYRRQPQTNRRFNTLITCAQETIVIGLAADSGCGKSTFMRRLTSVFGGAAKPPKGGNPDSNTLISDTTTVICLDDYHSLDRYGRKEQKVTALDPRANDFDLMYEQVKALKNGIAVEKPIYNHVTGLLDPPELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAERGHSLESIKASIEARKPDFDAFIDPQKQYADAVIEVLPTTLIPDDNEGKVLRVRLIMKEGVKYFSPVYLFDEGSTISWIPCGRKLTCSYPGIKFNYEPDSYFDHEVSVLEMDGQFDRLDELIYVESHLSNLSTKFYGEVTQQMLKHADFPGSNNGTGLFQTIVGLKIRDLYEQLIANKATARAEAKA | Catalytic Activity: ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate + H(+)
Sequence Mass (Da): 44464
Sequence Length: 395
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 2.7.1.19
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P19824 | MAFTMRAPAPRATAQSRVTANRARRSLVVRADKDKTVVIGLAADSGCGKSTFMRRMTSIFGGVPKPPAGGNPDSNTLISDMTTVICLDDYHCLDRNGRKVKGVTALAPEAQNFDLMYNQVKALKEGKSVDKPIYNHVSGLIDAPEKIESPPILVIEGLHPFYDKRVAELLDFKIYLDISDDIKFAWKIQRDMAERGHSLESIKSSIAARKPDFDAYIDPQKKDADMIIQVLPTQLVPDDKGQYLRVRLIMKEGSKMFDPVYLFDEGSTISWIPCGRKLTCSFPGIKMFYGPDTWYGQEVSVLEMDGQFDKLEELIYVESHLSNTSAKFYGEITQQMLKNSGFPGSNNGTGLFQTIVGLKVREVYERIVKKDVVPV | Catalytic Activity: ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate + H(+)
Sequence Mass (Da): 41892
Sequence Length: 375
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 2.7.1.19
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Q8FDQ2 | MSERHLPDDQSSTIDPYLITSVRQTLAEQSAALQNLSKQLDSGQYQRVLNLIMNCKGHVILSGMGKSGHVGRKISATLASTGTPSFFIHPAEAFHGDLGMITPYDLLILISASGETDEILKLVPSLKNFGNRIIAITNNGNSTLAKNADAVLELHMANETCPNNLAPTTSTTLTMAIGDALAIAMIHQRKFMPNDFARYHPGGSLGRRLLTRVADVMQHDVPAVQLDASFKTVIQRITSGCQGMVMVEDAEGGLAGIITDGDLRRFMEKEGSLTSATAAQMMTREPLTLPEDTMIIEAEEKMQKHRVSTLLVTNKANKVTGLVRIFD | Function: Involved in the biosynthesis of K-antigen capsules. Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P).
Catalytic Activity: D-arabinose 5-phosphate = D-ribulose 5-phosphate
Sequence Mass (Da): 35487
Sequence Length: 327
EC: 5.3.1.13
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P11801 | MGCGTSKVLPEPPKDVQLDLVKKVEPFSGTKSDVYKHFITEVDSVGPVKAGFPAASQYAHPCPGPPTAGHTEPPSEPPRRARVAKYRAKFDPRVTAKYDIKALIGRGSFSRVVRVEHRATRQPYAIKMIETKYREGREVCESELRVLRRVRHANIIQLVEVFETQERVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVRYLHALGITHRDLKPENLLYYHPGTDSKIIITDFGLASARKKGDDCLMKTTCGTPEYIAPEVLVRKPYTNSVDMWALGVIAYILLSGTMPFEDDNRTRLYRQILRGKYSYSGEPWPSVSNLAKDFIDRLLTVDPGARMTALQALRHPWVVSMAASSSMKNLHRSISQNLLKRASSRCQSTKSAQSTRSSRSTRSNKSRRVRERELRELNLRYQQQYNG | Function: May be a SFC-associated serine kinase (splicing factor compartment-associated serine kinase) with a role in intranuclear SR protein (non-snRNP splicing factors containing a serine/arginine-rich domain) trafficking and pre-mRNA processing.
PTM: Autophosphorylated on serine residues.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48035
Sequence Length: 424
Subcellular Location: Golgi apparatus
EC: 2.7.11.1
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P23889 | MARSGFEVQKVTVEALFLREIRTRFGKFRLGYLWAILEPSAHLLILLGILGYVMHRTMPDISFPVFLLNGLIPFFIFSSISKRSIGAIEANQGLFNYRPVKPIDTIIARALLETLIYVAVYILLMLIVWMTGEYFEITNFLQLVLTWSLLIILSCGVGLIFMVVGKTFPEMQKVLPILLKPLYFISCIMFPLHSIPKQYWSYLLWNPLVHVVELSREAVMPGYISEGVSLNYLAMFTLVTLFIGLALYRTREEAMLTS | Function: KpsM and KpsT constitute a system for the transport of polysialic acid across the cytoplasmic membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29558
Sequence Length: 258
Subcellular Location: Cell inner membrane
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P23888 | MIKIENLTKSYRTPTGRHYVFKNLNIIFPKGYNIALIGQNGAGKSTLLRIIGGIDRPDSGNIITEHKISWPVGLAGGFQGSLTGRENVKFVARLYAKRDELNERVDFVEEFSELGKYFDMPIKTYSSGMRSRLAFGLSMAFKFDYYLIDEITAVGDAKFKKKCSDIFDKIREKSHLIMVSHSERALKEYCDVAIYLNKEGQGKFYKNVTEAIADYKKDL | Function: Putative ATP-binding protein, and an energy coupling component for the transport of polysialic acid across the cytoplasmic membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24939
Sequence Length: 219
Subcellular Location: Cell inner membrane
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P24586 | MIKIENLTKSYRTPTGRHYVFKDLNIEIPSGKSVAFIGRNGAGKSTLLRMIGGIDRPDSGKIITNKTISWPVGLAGGFQGSLTGRENVKFVARLYAKQEELKEKIEFVEEFAELGKYFDMPIKTYSSGMRSRLGFGLSMAFKFDYYIVDEVTAVGDARFKEKCAQLFKERHKESSFLMVSHSLNSLKEFCDVAIVFKNSYIIGYYENVQSGIDEYKMYQDLDIE | Function: Putative ATP-binding protein, and an energy coupling component for the transport of polysialic acid across the cytoplasmic membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25481
Sequence Length: 224
Subcellular Location: Cell inner membrane
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P42216 | MSKAVIVIPARYGSSRLPGKPLLDIVGKPMIQHVYERALQVAGVAEVWVATDDPRVEQAVQAFGGKAIMTRNDHESGTDRLVEVMHKVEADIYINLQGDEPMIRPRDVETLLQGMRDDPALPVATLCHAISAAEAAEPSTVKVVVNTRQDALYFSRSPIPYPRNAEKARYLKHVGIYAYRRDVLQNYSQLPESMPEQAESLEQLRLMNAGINIRTFEVAATGPGVDTPACLEKVRALMAQELAENA | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27159
Sequence Length: 246
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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A0A1S5RW73 | MSFATSLPRPTTTGAAGFGLPLATCISLSVSHSFSPKFGICNNTSLRLKSKAGSGCYEGIHRSQLAASTILEGHTPINPEVESEKIRLIERIRLMFRSMDDGEISVSPYDTAWVALVEDIGGSGGPQFPTSLEWISNNQLDDGSWGDRKFVLYDRILNTLACVVALTTWKMHPNKCEKGLRFISDNIEKLADEDEELMPVGFEIALPSLIDLAKRLCIEIPDNSASIKNIYAKRDSKLKRIPMDLMHKKPTSLLFSLEGMEGLNWDKLLDFQSEGSFLSSPSSTAYALHHTKDELCLEYLLKAVKKFNGGVPNAYPVDMFEHLWSVDRLRRLGISRYFQVEIDECLDYVYRYWTNKGICWARNMCVQDSDDSSMGFRLLRLYGYDVSIDVFKQFEEGGQFCSIPGQMTHAITGMYNLYRASQLMFPQEHILADARNFTANLLHQKRVTNSIVDKWIITKDLPGEVAYALDVPFYASLPRLEARFFLEQYGGDDDVWIGKTLYRMLYVNCNTYLELAKLDYKHCQTVHQLEWNSMQTWYRECNLGEFGLSERSLLLAYYIAASTAFEPEKSSERLAWAITTILVETIMSQELSDEQKREFVDEFVNISIINNQNGGRYKPGNRLVEVLINTVTLMAEGRGTDQQLSNAWKNWLKTWEEGGDLGEAEARLLLHTIHLSSGLDESSFSHPKYQQLLEATSKVCHQLRLFQNLKANDAQGSTSRLVTVTTFQIEAGMQELVKLIFTKTLEDLTSATKQSFFNIARSFYYTAYCPADTIDSHINKVLFEKIV | Function: Involved in the biosynthesis of clerodane diterpenoids natural products, including salvinorin A with potent agonistic activity on brain kappa-opioid receptors, thus confering hallucinogenic properties . Diterpene synthase that catalyzes the formation of (-)-kolavenyl diphosphate from geranylgeranyl diphosphate (GGPP) as the first reaction in salvinorin A biosynthesis .
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = (-)-kolavenyl diphosphate
Sequence Mass (Da): 89377
Sequence Length: 787
Domain: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity through binding to Mg(2+).
Subcellular Location: Plastid
EC: 5.5.1.28
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P32044 | MKTKIVATIGPASSSPEIMKQMIDNGLSLVRINSAHADIKDVSKITQMVRSINRDVGIMIDLKGPELRTGEFAGGTLKISSGKDYVMGKDIVLNNMNVLSAVQVGDRILMSDGEVSFEVESTDPFTIRALNDGVLRDRSRVNIPGRFIELGTITDRDRAFIREGIADGVDFFALSFVQKSENVDSLRDFVIDSGGDQYIISKIETKSGLDNIEEIVKSSDGIMVARGDLGVELPLKEVVLAQKHIIKTAHEDGDFTIVATQVLESMVNNSSPTRAEISDITNAIIDNADALMLSEESAIGKYPVQAVRTLKEVSDYVEDKVSFDSSYYFKGNTIAYSVARAAKILSDDIKSDGIVALTHTGSTVRMISSLRPKAMVYAATVSESLARKLNIYFGVLPLHMEGNAEDLSFSEIMEYIVRSGRFADGSKLVMTSGDPYFTFGGTNDVKVAVVGKFIGRGYSFGDSLSGTATYGTKGDILMSEDGRIPGTDFRAFIFTSDIKPSLMSSLKGKTVVTKARLVRQIKEGERIYIDGNTGIILMASPDQK | Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 59147
Sequence Length: 544
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
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Q56301 | MELPSHKTKIIATIGPASKQKETIKKMIKAGMSVARINFSHGTLEEHAKTIETVRDVAEKLERRVAILGDLPGLKMRVGKIKGDSVTLRKGDKVVLTTRDIEGDETTIPVEFKDLPKLVSKGDTIYLSDGYIMLRVEEVRENEVECVVVNGGILFSHKGINIPKANLPIEAITPRDFEIIEFAIEHGVDAIGLSFVGSVYDVLKVKSFLEKKSADLFVIAKIERPDAVRNFDEILNAADGIMIARGDLGVEMPIEKLPIMQKQLIKKTNLAAKPVITATQMLVSMTTERIPKRAEVTDVANAILDGTDAVMLSEETAIGKYPVESVEMMAKIAKTTEEYRESLGYSRLRAWIDSLPKRSTIKEAITRSVIDALCAIDIKYILTPTRTGLTPRLISRFKPKQWILAFSSSERVCNNLAFSYGVYPFCMDENFNEKDIIMLVKGLGIVKEDDTVLLTEGRPIGKTVGTNTMRIFQIP | Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 52767
Sequence Length: 475
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
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Q9WY51 | MRSTKIVCTVGPRTDSYEMIEKMIDLGVNVFRINTSHGDWNEQEQKILKIKDLREKKKKPVAILIDLAGPKIRTGYLEKEFVELKEGQIFTLTTKEILGNEHIVSVNLSSLPKDVKKGDTILLSDGEIVLEVIETTDTEVKTVVKVGGKITHRRGVNVPTADLSVESITDRDREFIKLGTLHDVEFFALSFVRKPEDVLKAKEEIRKHGKEIPVISKIETKKALERLEEIIKVSDGIMVARGDLGVEIPIEEVPIVQKEIIKLSKYYSKPVIVATQILESMIENPFPTRAEVTDIANAIFDGADALLLTAETAVGKHPLEAIKVLSKVAKEAEKKLEFFRTIEYDTSDISEAISHACWQLSESLNAKLIITPTISGSTAVRVSKYNVSQPIVALTPEEKTYYRLSLVRKVIPVLAEKCSQELEFIEKGLKKVEEMGLAEKGDLVVLTSGVPGKVGTTNTIRVLKVD | Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 51892
Sequence Length: 466
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
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P14618 | MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP | Function: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP . The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production . The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival .
PTM: ISGylated.
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 57937
Sequence Length: 531
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.40
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Q9V447 | MSAPTDQPPRSEGAQTNSSERSSQQQEQPQQSQSQNVPAKLLQHFQTNRIDSALWALRLLVIFFTVSYVLPIFTSQQSAFSKVMLANAAISALRLHQRLPAFAFSREFLARLFAEDSCHYMMYSLIFFNIRPSLLVLIPVLLYSVLHASSYSLKLLDLIGQNSWWGARFIISIVEFQAANILKATAFCEIFIMPYAIVLAFMNHAGLMTPVIYYHYLVMRYSSRRNPYPRNAFAELRITFEALAARSPPAFAKIIRGGIGFVNRLAPQLQPAAAQE | Function: Member of the dosage-dependent hierarchy effective upon white gene expression.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31215
Sequence Length: 276
Subcellular Location: Membrane
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P42846 | MPRKKSAAKRAREQAKKEAAVPATDTATIKTSETSATTVKPAIEASKSYVPSEDEEEDEEEEEEEDDYGELITDEVENGINQVLDAIKNNKTDKLLDPKVKFFEDPESAAAKLANREGKHKPIYLKDYHRMNILSGDALKEDDEEYEHATVDGKQSFVSQQREEKTQLLNEIKSAFSDEENEESSGDEDDGFLKKKEPSTKKEGKNLPDPTVNEENFLEEFVNQQAWIPKKGDKVISLDLNNNEEDDEEFEDAAEKFENAYNFRYEDPNAAEIISYARSQATLRRSDDSSRRRKREEKRKIKEQIKAEKETALQKKKTKKLNKLTDILEQLTKEYGAEINADMVKKITDTLLKNDFKEEEWDNVVAELFNEEFYQQEGKPTWNEDDEIMGDFYADADGDDQTEEGEVEKEQKEEDEEEGPKRKKSKKEEKLQKKKEKRKVNELVENALEQNKLALIEEVEKEEEERKSRSRTKEEQDLKFRYREVSPESFGLTAREIFAADDTDLNEFIGLKKFAPYRSKELRAKDKRKVMKARRLREWRKKTFKNENGLAPVEAEAGEKDEDTILIPVEKASKSKHKRGHSHKHKGHQKK | Function: Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA.
PTM: N-glycosylated.
Sequence Mass (Da): 68654
Sequence Length: 591
Subcellular Location: Nucleus
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O00522 | MGNPENIEDAYVAVIRPKNTASLNSREYRAKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREASLFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTNVINPAYATESGQTENSLHMGYSALEIKSKMLALEKADTCIYNPLFGSDLQYTNRVDKVVINPYFGLGAPDYSKIQIPKQEKWQRSMSSVTEDKERQWVDDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRHITDQQGRSPLNICEENKQNNWEEAAKLLKEAINKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKAPHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLMPTERNS | Function: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits ERK1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Microtubule-associated protein that binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes in a GTP-bound RAP1-dependent manner. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels. May play a role in the regulation of macroautophagy through the down-regulation of the mTOR pathway .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84348
Sequence Length: 736
Domain: The FERM domain mediates binding to RAP1A and RAP1B and is necessary for binding to phosphatidylinositol 4,5-bisphosphate (PIP2).
Subcellular Location: Cytoplasm
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Q67Y93 | MVRKYRKAKGIVEAGVSSTYMQLRSRRIVYVRSEKSSSVSVVGDNGVSSSCSGSNEYKKKELIHLEEEDKDGDTETSTYRRGTKRKLFENLREEEKEELSKSMENYSSEFESAVKESLDCCCSGRKTMEETVTAEEEEKAKLMTEMPTESEIEDFFVEAEKQLKEKFKKKYNFDFEKEKPLEGRYEWVKLE | Function: Binds and inhibits CYCD2-1/CDKA-1 kinase complex activity. Regulates cell division which is crucial for plant growth, development and morphogenesis. Functions in turning cells from a mitotic to an endoreplicating cell cycle mode. Acts cell- and non-cell-autonomously to regulate endoreduplication by allowing S phase progression, but blocking entry into mitosis. Keeps on the one hand the plant cell cycle locally controlled, and on the other hand provides a possibility of linking cell cycle control in single cells with the supracellular organization of a tissue or an organ. May target specifically CDKA-1.
PTM: Ubiquitinated independently by RKP and SCF (SKP1-CUL1-FBL5/SKP2B) protein ligase complex, leading to proteasomal degradation.
Sequence Mass (Da): 22283
Sequence Length: 191
Subcellular Location: Nucleus
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Q09175 | MHPALLCGPILAIFLQFLVSSCSPLENDDLFLVQVEPEVDPVVAAEAIGAKYVRPLLNLKYHHLIKLHKGSDDSVQSSIRKRGIDAGILELERQTPRWRYKRDASESDELLNEFSNHFGISDPLFYGQWHIFNSNNPGHDLNLREVWDAGYFGENVTVAFVDDGIDFKHPDLQAAYTSLGSWDFNDNIADPLPKLSDDQHGTRCAGEVAAAWNDVCGVGIAPRAKVAGLRILSAPITDAVESEALNYGFQTNHIYSCSWGPADDGRAMDAPNTATRRALMNGVLNGRNGLGSIFVFASGNGGHYHDNCNFDGYTNSIFSATIGAVDAEHKIPFYSEVCAAQLVSAYSSGSHLSILTTNPEGTCTRSHGGTSAAAPLASAVYALALSIRPDLSWRDIQHITVYSASPFDSPSQNAEWQKTPAGFQFSHHFGFGKLDASKFVEVAKDWQVVNPQTWLIAPEINVNKSFGSVNNETITEMVSEFTVTKDMIEKSNFKRLEHVTVRVCIPFNRRGALEILLESPSGIRSILASERPYDENSKGFLDWTFMTVQHWAEPPEGVWKLLVNDRSGGKHEGTFENWQLALWGESENPSNTAPLPYDTLELPKEMVLGIYSEPNSDLTNSSTLLSPTSTSFTSYTVSATATPTSTSHIPIPTVLPPTQPVLEPSYREIVAFITFFLLFAFIFVAVIWTWISAFWKAKAPPPLSQQEIA | Function: Membrane-bound, subtilisin-like serine protease that processes the P-factor precursor and other precursor proteins. Essential for cell viability. Cleaves substrate on the C-terminal side of dibasic residues.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 78127
Sequence Length: 709
Subcellular Location: Golgi apparatus
EC: 3.4.21.-
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Q9SCR2 | MAAVRRRERDVVEENGVTTTTVKRRKMEEEVDLVESRIILSPCVQATNRGGIVARNSAGASETSVVIVRRRDSPPVEEQCQIEEEDSSVSCCSTSEEKSKRRIEFVDLEENNGDDRETETSWIYDDLNKSEESMNMDSSSVAVEDVESRRRLRKSLHETVKEAELEDFFQVAEKDLRNKLLECSMKYNFDFEKDEPLGGGRYEWVKLNP | Function: Binds and inhibits CYCD2-1/CDKA-1 complex kinase activity. Regulates cell division which is crucial for plant growth, development and morphogenesis. May regulate early lateral root initiation by blocking the G1/S phase transition. Controls the mitosis-to-endocycle transition and the onset of the endoreduplication cycle during leaf development through inhibition of mitotic CDKA-1 kinase complexes. Specifically targets CDKA-1.
PTM: Phosphorylated.
Sequence Mass (Da): 24037
Sequence Length: 209
Subcellular Location: Nucleus
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Q5Q995 | MAVSSGTSGMLATCLFMLLFATMQIYKSQLTSSQPMAIVGGFLGSVLFILILTAISNFETHFFGRNFQTKLIPEVVIALVIAMAASGMVHRVCITTCLIFSIVALYYVSRISIKVHGSGAGTATAIPVTKGKKGK | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14326
Sequence Length: 135
Subcellular Location: Membrane
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Q5RL79 | MVVGTGTSLALSSLLSLLLFAGMQIYSRQLASTEWLTIQGGLLGSGLFVFSLTAFNNLENLVFGKGFQAKIFPEILLCLLLALFASGLIHRVCVTTCFIFSMVGLYYINKISSTLYQATAPVLTPAKITGKGKKRN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14675
Sequence Length: 136
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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B2RZC9 | MVVGTGTSLALSSLLSLLLFAGMQIYSRQLASTEWLTIQGGLLGSGLFVFSLTAFNNLENLVFGKGFQAKIFPEILLCLLLALFASGLIHRVCVTTCFIFSMVGLYYINKISSTLYQATAPALTPAKVTGKSKKRN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14662
Sequence Length: 136
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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A4ZU96 | MIYILEGLDGTGKTSFASELIKSQVFSRPMYVYFSKEDSYENTKLAWVSLIKELSKLNFNIIMDRSIISTIAYHFTYRPSKEYENFIRSELESVLNLDPSKAVFIHFVKVHDSKKLLEYANRVKSIRDNYHLLMRILREKGFNVIVNGGQKDFNLF | Function: Catalyzes the conversion of dTMP to dTDP.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 18306
Sequence Length: 156
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.7.4.9
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A9NEH3 | MFITFEGGEGSGKTTLIEKLKHTLLEKKYDVLTTREPGGSKVAEKIRSVLLDNKNTEITAHTEALLFAASRAQHLDEVIIPNLDKVILCDRYIDSSYAYQAFGRNLGMEFVQSINSYALKYLPDLTFYIDLDPKTGIDRVKKNRLHKTDRLDMEVQTFHQKVREGYIRISEMFKERIVVIDGNQSIDAIYQIIMDNILKRL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23148
Sequence Length: 201
EC: 2.7.4.9
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A1TSN1 | MQRRGWFITFEGIDGAGKSSHIEAVAEALRREGRTVTVTREPGGTPLAETLRSLLLNEAMDALTESLVVFAGRRDHLRSVIAPALVRGEVVLCDRFTDATFAYQGAGRGFDRAVLAQLERITQSGLQEGTDAVLHPHLTLWFDLAPDVAAARLEGARAPDRFEAQPVEFFRRVAQGYADRAAADPGRFARLDADQPREAVRAQLMEILHRRGVLDAAQEGG | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24215
Sequence Length: 221
EC: 2.7.4.9
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Q6F9B5 | MFISFEGTEGVGKTTLIRKLYEHFEASGKQVVLTREPGGTPLAEQIRSLLLAVNHDEPMSSDTELLLMYAARAQHLQQVIVPALADEKLVLSDRFTDASYAYQCVGRGLSKDKLNTLNQTFVSHMPDITFWLDAPIELGMSRARERGALDRFEQEKVEFFQRVRQGYQQLHELYPERIKRLDATQAPEIVFQEALEHIQALV | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23049
Sequence Length: 202
EC: 2.7.4.9
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Q7WSH2 | MFISFEGCEGTGKTTHSRYLFEKLSKKYSCVLTKEPGGGLFNEVIRNILLHSSNKQIDFHTEALLFAADRAEHLSKLIIPALQQNKIVICDRYLDSTIAYQVYARGLSQDFVLNINNFALNYIPNITFYLDLDPKIGIQRVKQFRPKEINSFDLQKLSFHKKVRKGYLDLCQKDQQKRIFLIDASKPLENIYNIIEQKLKEVFQIEL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24083
Sequence Length: 207
EC: 2.7.4.9
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B3CR61 | MSNTTIGKFITFEGNEGSGKTTQSKLLYEKLLDNGIKAVWTREIGGTDIAELIRDIVLFKDMSITTELLLIMAARYEHIEKFIRPNLNEGKWVICDRFIDSTLCYQSENSEEQQLILELHRKLLDNFFPDLTLIINVSPSIAMQRIKIREIHKNTNQLNKFDSRNQQFHQKITDAFIQVSKLFPERIVQINGEPMIEDVSSEVINIINNKMKVNLLR | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 25171
Sequence Length: 217
EC: 2.7.4.9
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