ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
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-suga... |
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-suga... |
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-suga... |
Q83SQ3 | MDSHTLVQALIYLGSAALIVPIAVRLGLGSVLGYLIAGCIIGPWGLRLVTDAESILHFAEIGVVLMLFIIGLELDPQRLWKLRAAVFGGGALQMVICGGLLGLFCMLLGLRWQVAELIGMTLALSSTAIAMQAMNERNLMVTQMGRSAFAVLLFQDIAAIPLVAMIPLLAASSASTTMGAFALSALKVAGALVLVVLLGRYVTRPALRFVARSGLREVFSAVALFLVFGFGLLLEEVGLSMAMGAFLAGVLLASSEYRHALESDIEPFKGLLLGLFFIGVGMSIDFGTLIENPLRIVILLLGFLIIKIAMLWLIARPLQV... | 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
|
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 Topolo... |
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 = for... |
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 = for... |
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 = for... |
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 = for... |
O44408 | MEVDLPVHNEYDASRFHQVTIRDPIAGADSTFTIPTRYVNLSFLNAGAQGTVVMADDLVTTQRVAIKKMQQPFVMTMSAKRAYREFILLTTIKHPNIIRLLNAFTPDTSLSTFREVYLVMELMTHNLHEVIHRLRLDHKTLSFFVYQSLCAIKHLHNSGVIHRDLKPSNIVVNDRCVLKVLDFGLARKKNVDTSMRMSDYVVTRYYRAPEVILGLPYSEKVDIWSVGCIFAEMINHTVLFPGKDRIDQWTKIYSVLGTPDDHFISQLGQSAAMYVRSLPRHQARAFSEIVPDTNFLPETENPRVHLTPHVARDLLFNMLK... | 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 . Ph... |
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
|
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
|
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
|
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
|
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
|
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
|
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, ... |
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.... |
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.... |
Q8KAW7 | MKTVTGFASATVGNVACGFDVLGFAITEPGDEVVLALHDERRSDCPVSITSIVGDGGALPLDPKKNTSSFVVLKFLEYIRTTKGISFDGHIDLVLKKNLPLSSGMGSSAASAAAALIAANELFGSPCTKMELVHFAIEGERVACGSAHADNAAPAMLGNFILIRSYNPLDLITIKPPKNLFGTLVHPHTELKTSFARSVLPKSIPLSTATQQWGNVGALIAGLLMEDYDLIGRALVDVVAEPKRAPLIPGFNEVKQAALDAGALGCSIAGSGPSVFAFSSSRQTAEAVGSAMQSAFLHSRAALQSDMWVSPICSQGARII... | 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.... |
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.... |
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.... |
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.... |
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.... |
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.... |
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.... |
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.... |
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.... |
B4R8T4 | MAVYTDITDDELAKLLADFDLGAPLSFKGIAEGVENSNFLLETEGGRFILTVYEKRVRAEDLPFFLGLMRWLSEHGFASGLPMADRGGEMLKTVRGKPCAIVSFLPGLSVRRPTVAHCREAGKGLAALHNAADGFPMRRENDLGQGAWAPMFERLKDDAERLKPGLAEVIARDVADLADRWPQGLPEGVIHADYFPDNVFFKEGVFAGAIDFYFACNDIRAYDIAVALNAWCFEADGSFNITAARALVAGYEAVRPLSEAERAALPVLAHGAALRFFLTRLHDWHATPAGALVKPKDPLEYERKLAVHRTSPDLVLFGAA... | 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
|
P09979 | MTQESLLLLDRIDSDDSYASLRNDQEFWEPLARRALEELGLPVPPVLRVPGESTNPVLVGEPDPVIKLFGEHWCGPESLASESEAYAVLADAPVPVPRLLGRGELRPGTGAWPWPYLVMSRMTGTTWRSAMDGTTDRNALLALARELGRVLGRLHRVPLTGNTVLTPHSEVFPELLRERRAATVEDHRGWGYLSPRLLDRLEDWLPDVDTLLAGREPRFVHGDLHGTNIFVDLAATEVTGIVDFTDVYAGDSRYSLVQLHLNAFRGDREILAALLDGAQWKRTEDFARELLAFTFLHDFEVFEETPLDLSGFTDPEELAQ... | 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
|
Q8NI77 | MSVTEEDLCHHMKVVVRVRPENTKEKAAGFHKVVHVVDKHILVFDPKQEEVSFFHGKKTTNQNVIKKQNKDLKFVFDAVFDETSTQSEVFEHTTKPILRSFLNGYNCTVLAYGATGAGKTHTMLGSADEPGVMYLTMLHLYKCMDEIKEEKICSTAVSYLEVYNEQIRDLLVNSGPLAVREDTQKGVVVHGLTLHQPKSSEEILHLLDNGNKNRTQHPTDMNATSSRSHAVFQIYLRQQDKTASINQNVRIAKMSLIDLAGSERASTSGAKGTRFVEGTNINRSLLALGNVINALADSKRKNQHIPYRNSKLTRLLKDSL... | 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 maintai... |
Q9BVG8 | MVPSRRTWNLGATPSLRGLWRVGRAPEPEPGMARPAPAPASPAARPFPHTGPGRLRTGRGKDTPVCGDEDSSARSAARPALAQCRALSVDWAGPGSPHGLYLTLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESE... | 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
|
B3TMR8 | MENPANANPIRVGVIGCADIAWRRALPALEAEPLTEVTAIASRRWDRAKRFTERFGGEPVEGYPALLERDDVDAVYVPLPAVLHAEWIDRALRAGKHVLAEKPLTTDRPQAERLFAVARERGLLLMENFMFLHHPQHRQVADMLDEGVIGEIRSFAASFTIPPKPQGDIRYQADVGGGALLDIGVYPIRAAGLFLGADLEFVGAVLRHERDRDVVVGGNALLTTRQGVTAQLTFGMEHAYTNNYEFRGSTGRLWMNRVFTPPATYQPVVHIERQDHAEQFVLPAHDQFAKSIRAFAQAVLSGEHPREWSEDSLRQASLVD... | 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-... |
Q55GK8 | MSTTSMILTKKNIIILSIIIITIIAYQFYITSPQSFPSSNTITNTINTSGKGLDYTELLNLQKDLKAQQTEIRKQLEQLKYSINDINQNQNENQNQINNEYNNNKLNDEQENNNNNNYNNNNNNNNNELINYKERIKKKSKEQPNTCIPVEGKLLCLPNFIVIGTMKSGTTFLDYYLQKHPQIAHHSKKEIWYFNSYYANGIEWYAKHFEQYTSLENQKLIGEATPFYINNPNTAPRLFTTLKNAKLILLLRDPVERSLSQYHFSIQWLKRNKSPPLEYSFEHLIHEEADVIETCIRGHERYKEAFKQRKEIEKNGGGGL... | 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.-
|
P96589 | MYHSIKRFLIGKPLKSQAAGEQKLTKLKALAMLSSDALSSVAYGTEQILIILATISAAAFWYSIPIAVGVLILLLALILSYRQIIYAYPQGGGAYIVSKENLGEKPGLIAGGSLLVDYILTVAVSISAGTDAITSAFPALHDYHVPIAIFLVLVIMILNLRGLSESASILAYPVYLFVVALLVLIAVGLFKLMTGQIDQPAHHTSLGTPVAGITLFLLLKAFSSGCSALTGVEAISNAIPAFKNPPARNAARTLAMMGILLAILFSGITVLAYGYGTAPKPDETVVSQIASETFGRNVFYYVIQGVTSLILVLAANTGFS... | 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
|
P46086 | MEVKARAPGKIILAGEHAVVHGSTAVAAAIDLYTYVTLRFPLPSAENNDRLTLQLKDISLEFSWSLARIKEAIPYDSSTLCRSTPASCSEETLKSIAVLVEEQNLPKEKMWLSSGISTFLWLYTRIIGFNPATVVINSELPYGSGLGSSAALCVALTAALLASSISEKTRGNGWSSLDETNLELLNKWAFEGEKIIHGKPSGIDNTVSAYGNMIKFCSGEITRLQSNMPLRMLITNTRVGRNTKALVSGVSQRAVRHPDAMKSVFNAVDSISKELAAIIQSKDETSVTEKEERIKELMEMNQGLLLSMGVSHSSIEAVIL... | 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... |
Q86AG7 | MISNQDNIIQVSAPGKIILFGEHAVVLEKTAIASALSLRTTVTFTPNTNNTLLLDFPDLAGFGVREWSLDEFKKLDHFPNDIDILKPIECSELFQQELNKIIDIKGIHTFLFLFCALTKCTKAYNIKITSDLPIGAGLGSSASFCVSICAGLLKAFDTYICGGCKQCIGGQGQQQQICNEQLNLINLWSLQGEKIMHGTPSGIDNAVATFGKALTFTRKNGYKILENGIPPLRILITNTRVSRSTKTLVEGVIQRSKLYPTLIDPVSNLIDTISSQCIESFNQYHTDKDYEKLQQTMDLMFDMNQHLLSGCYGVGHSSID... | 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 vi... |
Q03426 | MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKRAWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSICRKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKEDLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVPRNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDMNQHHLNALGVGHASLDQLCQ... | 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 diphosphat... |
P17256 | MLSEVLLVSAPGKVILHGEHAVVHGKVALAVALNLRTFLVLRPQSNGKVSLNLPNVGIKQVWDVATLQLLDTGFLEQGDVPAPTLEQLEKLKKVAGLPRDCVGNEGLSLLAFLYLYLAICRKQRTLPSLDIMVWSELPPGAGLGSSAAYSVCVAAALLTACEEVTNPLKDRGSIGSWPEEDLKSINKWAYEGERVIHGNPSGVDNSVSTWGGALRYQQGKMSSLKRLPALQILLTNTKVPRSTKALVAGVRSRLIKFPEIMAPLLTSIDAISLECERVLGEMAAAPVPEQYLVLEELMDMNQHHLNALGVGHASLDQLCQ... | 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... |
Q38997 | MDGSGTGSRSGVESILPNYKLGRTLGIGSFGRVKIAEHALTGHKVAIKILNRRKIKNMEMEEKVRREIKILRLFMHPHIIRLYEVIETPTDIYLVMEYVNSGELFDYIVEKGRLQEDEARNFFQQIISGVEYCHRNMVVHRDLKPENLLLDSKCNVKIADFGLSNIMRDGHFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGTLPFDDENIPNLFKKIKGGIYTLPSHLSPGARDLIPRMLVVDPMKRVTIPEIRQHPWFQAHLPRYLAVPPPDTVQQAKKIDEEILQEVINMGFDRNHLIESLRNRTQ... | 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 ro... |
Q2G5F0 | MAKLYFYYASMNAGKSTNLLQADFNYRERGMATMLWTAALDDRGGERAIESRIGLGADAHRFDAGTDLWQRISAAHAVQPLSCVLVDEAQFLRRDQVWQLARVADAAGIPVLCYGLRTDFQGELFEGSAALLGIADSLIELKAVCHCGRKATMNLRVDDSGAAVRAGRQTEIGGNDRYVALCRRHFSEAMGQ | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 21079
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 2.7.1.21
|
B2RJJ6 | MDYEIENNHADSIRRGSIEVICGSMFSGKTEELLRRLRRAKIARQTVEIFKPTIDIRYDETDVVSHDKNAIASAPVDNSANILLLSSQVDVVGIDEAQFFDEGLVEVAQQLADQGVRVVIAGLDMDFRRQPFGPMPGLCAIADSVTKVHAVCVECGRLASYSFRRVQGDQQVMLGELNEYSPLCRTCYRKCSSPPQTEEIHSTI | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 22711
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.7.1.21
|
Q6UDK9 | MGRIVVLYVDGAFGIGKTTVLRQIQKSAAYRFRRIYLEEPMRAWRSWFVDDHDAIREIYTTQELKDAGEIDLREASRRVCYAQVSLSAPFHIMNAVIYGIISGESEATSAHLGEGDYFVGVDRHPLASCLCFPVARFVTGYLEYTDLIALVATLPDYPRGASIAILDLSVEEQARRITERSRSGEHVNKTFLRILRNVFIIMYNTVAYLRNVSIDKACADREALEDFRGSQLESDMHKIDIQPRDDPNASETLFAVMASDATWRKNRKQSALFVYTMAKLDALLRSLNMHIVDINGLSQEQCAEKVVAISSKVPAVTARG... | 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 concen... |
Q8ZV53 | MLVVIVGPMFAGKTTELIRRVERYVIAGRRAIVFKPSLDVRYDASKVAAHNGLKFDAFVIPPDKDGVEIIRKMGAEYDVVAVDEIQFFPVDLADALNQLANGRIVIAAGLNLDFRGEPFETTARAMAFADRVISLSAVCKLCGKPATRTQRLINGVPAPRHSPRILIGGNESYEARCRRHYVIPP | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 20390
Sequence Length: 185
Subcellular Location: Cytoplasm
EC: 2.7.1.21
|
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
|
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... |
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 ... |
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
|
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... |
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
|
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 volta... |
Q5ZJU2 | MAGDVEGFSSSIHDTSVSAGFRALYEEGLLLDVTLVIEDHQFQAHKALLATQSDYFRIMFTADMRERDQDKIHLKGLTATGFSHVLQFMYYGTIELSMNTVHEILQAAMYVQLIEVVKFCCSFLLAKICLENCAEIMRLLDDFSVNIEGVREKLDSFLLENFVPLMSRPDFLSYLSFEKLMSYLDNDHLSRFPEIELYEAVQAWLRHDRRRWRHTDTIIQNIRFCLMTPSSVFEKVKTSEFYRYSRQLRHEVDQAMNYFHSVHQQPLMEMKSNKIRSAKPQTAVFRGMIGHSMVNSKILLLHKPRVWWELEGPQVPLRPD... | 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
|
Q96M94 | MAGDVEGFCSSIHDTSVSAGFRALYEEGLLLDVTLVIEDHQFQAHKALLATQSDYFRIMFTADMRERDQDKIHLKGLTATGFSHVLQFMYYGTIELSMNTVHEILQAAMYVQLIEVVKFCCSFLLAKICLENCAEIMRLLDDFGVNIEGVREKLDTFLLDNFVPLMSRPDFLSYLSFEKLMSYLDNDHLSRFPEIELYEAVQSWLRHDRRRWRHTDTIIQNIRFCLMTPTSVFEKVKTSEFYRYSRQLRYEVDQALNYFQNVHQQPLLDMKSSRIRSAKPQTTVFRGMIGHSMVNSKILLLKKPRVWWELEGPQVPLRPD... | 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 adap... |
Q6TDP4 | MQPRSERPAGRTQSPEHGSPGPGPEAPPPPPPQPPAPEAERTRPRQARPAAPMEGAVQLLSREGHSVAHNSKRHYHDAFVAMSRMRQRGLLCDIVLHVAAKEIRAHKVVLASCSPYFHAMFTNEMSESRQTHVTLHDIDPQALDQLVQFAYTAEIVVGEGNVQTLLPAASLLQLNGVRDACCKFLLSQLDPSNCLGIRGFADAHSCSDLLKAAHRYVLQHFVDVAKTEEFMLLPLKQVLELVSSDSLNVPSEEEVYRAVLSWVKHDVDARRQHVPRLMKCVRLPLLSRDFLLGHVDAESLVRHHPDCKDLLIEALKFHLL... | 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... |
Q6TDP3 | MQPRGERPAGRTQSPEHSSPGPGPEAPPPPQPPAPEAERARPRQARPAAPMEGAMQLLSREGHSVAHNSKRHYHDAFVAMSRMRQRGLLCDIVLHVAAKEIRAHKVVLASCSPYFHAMFTNEMSESRQTHVTLHDIDPQALDQLVQFAYTAEIVVGEGNVQTLLPAASLLQLNGVRDACCKFLLSQLDPSNCLGIRGFADTHSCSDLLKAAHRYVLQHFVDVAKTEEFMLLPLKQVLELVSSDSLNVPSEEDVYRAVLSWVKHDVDTRRQHVPRLMKCVRLPLLSRDFLLGHVDAESLVRHHPDCKDLLIEALKFHLLPE... | 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... |
Q9Y2M5 | MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSIQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVL... | 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... |
Q5R7B8 | MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSTQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVL... | 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... |
Q6DFF6 | MRRCLNTRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYVSDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFSYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSIQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVLFAVGG... | 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 al... |
Q9UEF7 | MPASAPPRRPRPPPPSLSLLLVLLGLGGRRLRAEPGDGAQTWARFSRPPAPEAAGLFQGTFPDGFLWAVGSAAYQTEGGWQQHGKGASIWDTFTHHPLAPPGDSRNASLPLGAPSPLQPATGDVASDSYNNVFRDTEALRELGVTHYRFSISWARVLPNGSAGVPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDAYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGIRGSPRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGQVSIALSSHWINPRRMTDHSIKECQKSL... | 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 acti... |
Q8WP17 | MPASAPPRRPRPPPPSLSLSLLLVLLGLAGRRLRAEPGDGAQTWARFARPPAPEAAGLFQGTFPDGFLWAVGSAAYQTEGGWQQHGKGASIWDTFTHHPLAPPGDSRIANVPSGAPSPLQPATGDVASDSYNNVFRDTEALRELGVTHYRFSISWARVLPNGSAGVPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDAYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGIRGSPRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGQVSIALSSHWINPRRMTDHSIKECQK... | 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 acti... |
O35082 | MLARAPPRRPPRLVLLRLLLLHLLLLALRARCLSAEPGQGAQTWARFARAPAPEAAGLLHDTFPDGFLWAVGSAAYQTEGGWRQHGKGASIWDTFTHHSGAAPSDSPIVVAPSGAPSPPLSSTGDVASDSYNNVYRDTEGLRELGVTHYRFSISWARVLPNGTAGTPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDTYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGVRGSSRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGRVSIALSSHWINPRRMTDYNIRECQK... | 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 acti... |
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 f... |
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
|
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
|
P01042 | MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRITEATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFSVATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLNEVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLRIASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFKIDNVKKARVQVVAGKKYFID... | 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... |
P09217 | MPSRTDPKMDRSGGRVRLKAHYGGDILITSVDPTTTFQDLCEEVRDMCGLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLACQGRDEVLIIHVFPSIPEQPGMPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHVLVPLTCRRHMDSVMPSQEPPVDDKNDGVDLPSEETDGIAYISSSRKHDNIKDDSEDLKPVIDGVDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCF... | 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... |
Q05652 | MSGVQTAEAEAQAQNQANGNRTRSRSHLDNTMAIRLLPLPVRAQLCAHLDALDVWQQLATAVKLYPDQVEQISSQKQRGRSASNEFLNIWGGQYNHTVQTLFALFKKLKLHNAMRLIKDYVSEDLHKYIPRSVPTISELRAAPDSSAKVNNGPPFPSSSGVSNSNNNRTSTTATEEIPSLESLGNIHISTVQRAAESLLEIDYAELENATDGWSPDNRLGQGGFGDVYRGKWKQLDVAIKVMNYRSPNIDQKMVELQQSYNELKYLNSIRHDNILALYGYSIKGGKPCLVYQLMKGGSLEARLRAHKAQNPLPALTWQQR... | 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 pl... |
P42818 | MVSSQRPVPNKIQKQQYLSISPSNSVLKDDVELEFSDVFGPLPEEANDIAYDEPAVVYSRSHSLVGPCSLDSHSLKLTKLTLLETEDSIDLVECLEGESLKENDDFSGNDDSDNEKALEGDLVKVSGVVGIDDFEVMKVVGKGAFGKVYQVRKKETSEIYAMKVMRKDHIMEKNHAEYMKAERDILTKIDHPFIVQLKYSFQTKYRLYLVLDFINGGHLFFQLYHQGLFREDLARVYTAEIVSAVSHLHEKGIMHRDLKPENILMDTDGHVMLTDFGLAKEFEENTRSNSMCGTTEYMAPEIVRGKGHDKAADWWSVGIL... | 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 ... |
Q02595 | MEKRYQQLFKGKRIDFPLATGAASHVSLTYDEKKNPYLLCWTYIYQEKPEFTVPLKGCRIINNITEIGPCIHIITSNEEYQFQCRSKEEFDEMSQFFNMLGYPILGFKNVYVLNKKIGKGSFSTAYIGTNILYGNRVVVKEVDKSKVKESNVYTEIEVLRKVMHKYIIKLISAYEQEGFVYLVLEYLKGGELFEYLNNNGPYTEQVAKKAMKRVLIALEALHSNGVVHRDLKMENLMLENPNDPSSLKIIDFGLASFLNSPSMNMRCGSPGYVAPEILKCASYGTKVDIFSLGVILFNILCGYPPFRGNNVKEIFKKNMR... | 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
|
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
|
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
|
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
|
P25697 | MAVSTIYSTQALNSTHFLTSSSSSKQVFLYRRQPQTNRRFNTLITCAQETIVIGLAADSGCGKSTFMRRLTSVFGGAAKPPKGGNPDSNTLISDTTTVICLDDYHSLDRYGRKEQKVTALDPRANDFDLMYEQVKALKNGIAVEKPIYNHVTGLLDPPELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAERGHSLESIKASIEARKPDFDAFIDPQKQYADAVIEVLPTTLIPDDNEGKVLRVRLIMKEGVKYFSPVYLFDEGSTISWIPCGRKLTCSYPGIKFNYEPDSYFDHEVSVLEMD... | 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
|
P19824 | MAFTMRAPAPRATAQSRVTANRARRSLVVRADKDKTVVIGLAADSGCGKSTFMRRMTSIFGGVPKPPAGGNPDSNTLISDMTTVICLDDYHCLDRNGRKVKGVTALAPEAQNFDLMYNQVKALKEGKSVDKPIYNHVSGLIDAPEKIESPPILVIEGLHPFYDKRVAELLDFKIYLDISDDIKFAWKIQRDMAERGHSLESIKSSIAARKPDFDAYIDPQKKDADMIIQVLPTQLVPDDKGQYLRVRLIMKEGSKMFDPVYLFDEGSTISWIPCGRKLTCSFPGIKMFYGPDTWYGQEVSVLEMDGQFDKLEELIYVESH... | 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
|
Q8FDQ2 | MSERHLPDDQSSTIDPYLITSVRQTLAEQSAALQNLSKQLDSGQYQRVLNLIMNCKGHVILSGMGKSGHVGRKISATLASTGTPSFFIHPAEAFHGDLGMITPYDLLILISASGETDEILKLVPSLKNFGNRIIAITNNGNSTLAKNADAVLELHMANETCPNNLAPTTSTTLTMAIGDALAIAMIHQRKFMPNDFARYHPGGSLGRRLLTRVADVMQHDVPAVQLDASFKTVIQRITSGCQGMVMVEDAEGGLAGIITDGDLRRFMEKEGSLTSATAAQMMTREPLTLPEDTMIIEAEEKMQKHRVSTLLVTNKANKVT... | 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
|
P11801 | MGCGTSKVLPEPPKDVQLDLVKKVEPFSGTKSDVYKHFITEVDSVGPVKAGFPAASQYAHPCPGPPTAGHTEPPSEPPRRARVAKYRAKFDPRVTAKYDIKALIGRGSFSRVVRVEHRATRQPYAIKMIETKYREGREVCESELRVLRRVRHANIIQLVEVFETQERVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVRYLHALGITHRDLKPENLLYYHPGTDSKIIITDFGLASARKKGDDCLMKTTCGTPEYIAPEVLVRKPYTNSVDMWALGVIAYILLSGTMPFEDDNRTRLYRQILRGKYSYSGEP... | 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-an... |
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
|
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
|
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
|
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-suga... |
A0A1S5RW73 | MSFATSLPRPTTTGAAGFGLPLATCISLSVSHSFSPKFGICNNTSLRLKSKAGSGCYEGIHRSQLAASTILEGHTPINPEVESEKIRLIERIRLMFRSMDDGEISVSPYDTAWVALVEDIGGSGGPQFPTSLEWISNNQLDDGSWGDRKFVLYDRILNTLACVVALTTWKMHPNKCEKGLRFISDNIEKLADEDEELMPVGFEIALPSLIDLAKRLCIEIPDNSASIKNIYAKRDSKLKRIPMDLMHKKPTSLLFSLEGMEGLNWDKLLDFQSEGSFLSSPSSTAYALHHTKDELCLEYLLKAVKKFNGGVPNAYPVDMF... | 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 diphosphat... |
P32044 | MKTKIVATIGPASSSPEIMKQMIDNGLSLVRINSAHADIKDVSKITQMVRSINRDVGIMIDLKGPELRTGEFAGGTLKISSGKDYVMGKDIVLNNMNVLSAVQVGDRILMSDGEVSFEVESTDPFTIRALNDGVLRDRSRVNIPGRFIELGTITDRDRAFIREGIADGVDFFALSFVQKSENVDSLRDFVIDSGGDQYIISKIETKSGLDNIEEIVKSSDGIMVARGDLGVELPLKEVVLAQKHIIKTAHEDGDFTIVATQVLESMVNNSSPTRAEISDITNAIIDNADALMLSEESAIGKYPVQAVRTLKEVSDYVEDK... | 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
|
Q56301 | MELPSHKTKIIATIGPASKQKETIKKMIKAGMSVARINFSHGTLEEHAKTIETVRDVAEKLERRVAILGDLPGLKMRVGKIKGDSVTLRKGDKVVLTTRDIEGDETTIPVEFKDLPKLVSKGDTIYLSDGYIMLRVEEVRENEVECVVVNGGILFSHKGINIPKANLPIEAITPRDFEIIEFAIEHGVDAIGLSFVGSVYDVLKVKSFLEKKSADLFVIAKIERPDAVRNFDEILNAADGIMIARGDLGVEMPIEKLPIMQKQLIKKTNLAAKPVITATQMLVSMTTERIPKRAEVTDVANAILDGTDAVMLSEETAIGK... | 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
|
Q9WY51 | MRSTKIVCTVGPRTDSYEMIEKMIDLGVNVFRINTSHGDWNEQEQKILKIKDLREKKKKPVAILIDLAGPKIRTGYLEKEFVELKEGQIFTLTTKEILGNEHIVSVNLSSLPKDVKKGDTILLSDGEIVLEVIETTDTEVKTVVKVGGKITHRRGVNVPTADLSVESITDRDREFIKLGTLHDVEFFALSFVRKPEDVLKAKEEIRKHGKEIPVISKIETKKALERLEEIIKVSDGIMVARGDLGVEIPIEEVPIVQKEIIKLSKYYSKPVIVATQILESMIENPFPTRAEVTDIANAIFDGADALLLTAETAVGKHPLE... | 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
|
P14618 | MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRA... | 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 pro... |
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
|
P42846 | MPRKKSAAKRAREQAKKEAAVPATDTATIKTSETSATTVKPAIEASKSYVPSEDEEEDEEEEEEEDDYGELITDEVENGINQVLDAIKNNKTDKLLDPKVKFFEDPESAAAKLANREGKHKPIYLKDYHRMNILSGDALKEDDEEYEHATVDGKQSFVSQQREEKTQLLNEIKSAFSDEENEESSGDEDDGFLKKKEPSTKKEGKNLPDPTVNEENFLEEFVNQQAWIPKKGDKVISLDLNNNEEDDEEFEDAAEKFENAYNFRYEDPNAAEIISYARSQATLRRSDDSSRRRKREEKRKIKEQIKAEKETALQKKKTKK... | 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
|
O00522 | MGNPENIEDAYVAVIRPKNTASLNSREYRAKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREASLFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTNVINPAYATESGQTENSLHMGYSALEIKSKMLALEKADTCIYNPLFGSDLQYTNRVDKVVINPYFGLGAPDYSKIQIPKQEKWQRSMSSVTEDKERQWVDDFPLHRSACEGDSELLSRLLSERFSVNQLDSD... | 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 p... |
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... |
Q09175 | MHPALLCGPILAIFLQFLVSSCSPLENDDLFLVQVEPEVDPVVAAEAIGAKYVRPLLNLKYHHLIKLHKGSDDSVQSSIRKRGIDAGILELERQTPRWRYKRDASESDELLNEFSNHFGISDPLFYGQWHIFNSNNPGHDLNLREVWDAGYFGENVTVAFVDDGIDFKHPDLQAAYTSLGSWDFNDNIADPLPKLSDDQHGTRCAGEVAAAWNDVCGVGIAPRAKVAGLRILSAPITDAVESEALNYGFQTNHIYSCSWGPADDGRAMDAPNTATRRALMNGVLNGRNGLGSIFVFASGNGGHYHDNCNFDGYTNSIFSA... | 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
... |
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 endoreduplica... |
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 ... |
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 ... |
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 ... |
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
|
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
|
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
|
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
|
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
|
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
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.