ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
F4K2M8 | MPTGCEFPMIKTFENALTAADFESTVELTNFPAVFRGCASVWDAYSKWNPFNSGLDYLEERAGSVEVEAMLSRTAPVFNGDIRSHERVSLPFSDFIRFCKQHMRGKGNGSGVDAKSADLNPMCEDYRPGQIYLAQFPILNDEKEEKVLLKILRQDIQTPTFLDAKSLSSINFWMNSAEARSSTHYDPHHNLLCVVSGRKKVVLWPPSASPSLYPMPIYGEASNHSSVGLENPNLSDYPRAEHSLKQSQEITLNAGDAVFIPEGWFHQVDSDELTVAVNFWWQSNYMSNMPEHMDSYYLRRITRSLLVSKPSSTDLRHLSE... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: May function as histone H3 lysine demethylase and be involved in regulation of gene expression.
Sequence Mass (Da): 61906
Sequence Length: 549
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q0WVR4 | MAKEIENLWREVRELSLGTKIDRFDSQPSPVKFLRNYVSQSKPCVISKAITHWPALKLWSDPAYLTGALSDDVVSLHLTPNGCADAVTGDSDLCFASAHVEKVLFPEALKVVQSSCKGLKVGYLQQQNDCFRTEYSTVALDCDGDIEWATEAFGCSPEAVNLWIGTDDSVTSFHKDHYENLYAVVSGEKHFLLLPPTDVHRLYIEQYPAANYSYHRDTDAFKLEVEEPVRHVPWSSVDPYPSPEKEASERLKFPLFFDGPKPFHCTVKAGEVLYLPSMWFHHVSQTPGDGGYTIAVNYWYDMQFDIKYAYFNFLQSLLYK... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that demethylates 'Lys-27' (H3K27me) of histone H3 with a specific activity for H3K27me3 and H3K27me2, and involved in the regulation of gene expression . No activity on H3K27me1 . Together with JMJ30, regulates the flowering-repressor FLOWERING LO... |
Q08BY5 | MDRETFHSCSSLVKLPRQIHQQHCSSHFIEYIEREIPYSKFFKNYLIPNQPCMFSKKFTEEWNCRKKWVTAEGKPNLQRLLHEFDETPVPVANCSVKEYNANPKQIMPFKEFIQYWRESIQNGHSSPKGCLYLKDWHMQRNFPEHNIYKTPIYFSSDWLNEYWDTIEVDDYRFVYMGPKGSWTPFHADVFRSYSWSANICGRKKWLLYPPGQEDFLRDCHGNLAYDVTAPILQDKGLYAQFEEACQPLEIIQEAGEIIFVPSGWHHQVYNLEDTISINHNWLNGCNLDIMWQFLQDELSSVQREIEEWRDTMDTWHQHCQ... | Function: Catalyzes the 2-oxoglutarate and iron-dependent C4-lysyl hydroxylation of ETF1 at 'Lys-63' thereby promoting the translational termination efficiency of ETF1.
Catalytic Activity: 2-oxoglutarate + L-lysyl-[protein] + O2 = 4-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 49892
Sequence Length: ... |
Q9VJ97 | MASEERDGDVLLQLHPEEVVETDPQLPEEIERCSGLDYNDFFWRYMHKNIPVIIANVSNDWECQNWTVGQSSPESRDLNSNPSASSINFDYLKTKISDGPVPVANCNSSYFNSHTKLELNFHDYLAKWRSSIESQSSAAWTSAEVNSNVAPASGDNLYLKDWHLAAQMPGYNFYKVPKYFASDWLNEQLIQQGKDDYRFVYMGPKNSWTSYHADVFGSFSWSTNIVGLKKWLIMPPGEELKLNDRLGNLPFSIDEKMLDEHNVRYYTINQRANEAVFVPSGWFHQVWNLTDTISVNHNWFNGCNISMVWQNLKNNLKAVC... | Catalytic Activity: 2-oxoglutarate + L-lysyl-[protein] + O2 = 4-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 49169
Sequence Length: 425
Subcellular Location: Cytoplasm
EC: 1.14.11.-
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Q9H9V9 | MRAGPEPQALAGQKRGALRLLVPRLVLTVSAPAEVRRRVLRPVLSWMDRETRALADSHFRGLGVDVPGVGQAPGRVAFVSEPGAFSYADFVRGFLLPNLPCVFSSAFTQGWGSRRRWVTPAGRPDFDHLLRTYGDVVVPVANCGVQEYNSNPKEHMTLRDYITYWKEYIQAGYSSPRGCLYLKDWHLCRDFPVEDVFTLPVYFSSDWLNEFWDALDVDDYRFVYAGPAGSWSPFHADIFRSFSWSVNVCGRKKWLLFPPGQEEALRDRHGNLPYDVTSPALCDTHLHPRNQLAGPPLEITQEAGEMVFVPSGWHHQVHNL... | Function: Catalyzes the 2-oxoglutarate and iron-dependent C4-lysyl hydroxylation of ETF1 at 'Lys-63' thereby promoting the translational termination efficiency of ETF1.
Catalytic Activity: 2-oxoglutarate + L-lysyl-[protein] + O2 = 4-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 52493
Sequence Length: ... |
Q8BFT6 | MDRETRTFAERYYRDLRDPVPSGGGGPTPSGVTFIQTPNAFSYADFVKGFLLPNLPCVFSSAFTEGWGSRRRWVTSEGKPDFEYLQQKYGDAVVPVANCGVREYNSNPKEHMSFRDYISYWKDYIQGSYSSSRGCLYLKDWHLCRDSLVNDLEDIFTLPVYFSSDWLNEFWDVLNVDDYRFVYAGPRGTWSPFHADIFRSFSWSVNICGKKKWLFFPPGEEEALRDCHGNLPYDVTSTELLDTHLYPKIQHHSLPIEVIQEPGEMVFVPSGWHHQVYNLDDTISINHNWVNGCNLPNMWHFLQQELQAVQHEVEEWKDSM... | Function: Catalyzes the 2-oxoglutarate and iron-dependent C4-lysyl hydroxylation of ETF1 at 'Lys-63' thereby promoting the translational termination efficiency of ETF1 (By similarity). Not essential for embryonic stem cell (ESC) maintenance and the embryonic and postnatal development .
Catalytic Activity: 2-oxoglutarat... |
Q58DS6 | MNHKSKKRIREAKRSARPELKDSLDWTRHNYFESFPLNPAAVADNVERADALQLSVEEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTREEGGNQQDEAITWFNIIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEH... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylat... |
B1P1G9 | MKTSVLVTVLGLAVISVLCSASQDEEQDMYDELLSAVFEVNDELQSEARCGEKNDRCKTNQDCCSGFRCTKFRRCGRR | Function: Probable ion channel inhibitor.
Sequence Mass (Da): 8788
Sequence Length: 78
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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B1P1H0 | MYDEILSAFFEVNDELQSEARCGEKNDRCKTNQDCCSGFRCTKFRRCGRR | Function: Probable ion channel inhibitor.
Sequence Mass (Da): 5918
Sequence Length: 50
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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B1P1E5 | MKTSVLLVILGIAAITVQCTASESVEQDSLRTFVDTVLGWNAEMASEARCGGWMAKCADSDDCCETFHCTRFNVCGK | Function: Probable ion channel inhibitor.
Sequence Mass (Da): 8327
Sequence Length: 77
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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B1P1F8 | MQVSVLITLAVLGVMFVWTSAAELEERGSDQPAWLKSLERIFQSEERDCRALYGGCTKDEDCCKHLACRRTLPTYCAWDLTFP | Function: Probable ion channel inhibitor.
Sequence Mass (Da): 9461
Sequence Length: 83
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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A0A330KW27 | MNTKLVVVFLLSAILFVSVTASRPGKDLERDEAYETYDDENKRACKDVFPAATCRHAKSVGNCSSEKYKRNCAITCGAC | Function: Toxin that weakly blocks two voltage-gated potassium channels (IC(50)=1.8-2.5 uM on Kv1.2/KCNA2 and IC(50)=5.6-6.2 uM on Kv1.6/KCNA6).
PTM: Two similar peptides (OspTx2a-p1 and -p2) are obtained after synthesis and oxidative folding. They may differ by a D-Cys at position 76 (corresponding to OspTx2a-p2). Sin... |
P23354 | MSLQAITVTLNPAIDQTIQLDRLQPGAVHRASSVRNDAGGKGINVAACLADWGSQVAALGVLGVGNAGVFEALFRERGITDHCHRVAGDTRTNLKLVEAQVNETTDINLPGLQLGQAHLQGVADHLAPLLRAGLPVVLSGSLPAGLPEDSWAQLQAQASAAGARVLLDTSGAPLVAALAAAPVAMPYAVKPNRHELEAWTGHPLGDHAALTAAAHALIARGIQLVVISMGTEGALFVQRDQQLIARPPRLAQGSSVGAGDAMVAGLAAALLDDATELEQCARLATAFSMCRLESGDARRITPEGVRDAAAAVVIGAVP | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 32592
Sequence Length: 318
EC: 2.7.1.56
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Q2HRD5 | MFLYVVCSLAVCFRGLLSLSLQSSPNLCPGVISTPYTLTCPSNTSLPTSWYCNDTRLLRVTQGTLTVDTLICNFSCVGQSGHRYSLWITWYAQPVLQTFCGQPSNTVTCGQHVTLYCSTSGNNVTVWHLPNGQNETVSQTKYYNFTLMNQTEGCYACSNGLSSRLSNRLCFSARCANITPETHTVSVSSTTGFRTFATAPTLFVMKEVKSTYLYIQEHLLVFMTLVALIGTMCGILGTIIFAHCQKQRDSNKTVPQQLQDYYSLHDLCTEDYTQPVDWY | Function: Promotes host cell survival pathways and may contribute to pathogenesis by preventing infected cells from undergoing apoptosis. Acts in host B-cells by mimicking the activated B-cell receptor complex. The cytoplasmic tail of K1 can induce the phosphorylation of a number of different kinases, leading to the ac... |
Q5A4Q1 | MSIEDLKNTVTKLQERIQELEKKAGIIPDVPKSVRMVLIGPPGAGKGTQAPNLKEKFCACHLATGDMLRAQVAAKTALGVEAKKIMDQGGLVSDEIMVNMIKSELENNQECSKGFILDGFPRTIPQAEKLDSMLESRKTPLEKAVELKIDDELLVARITGRLVHPASGRSYHKLFNPPKKDMTDDVTGEPLVQRSDDNEDALKKRLVTYHKQTEPIVAYYQKTGIWSGVDASQKPTKVWSDILKCLGQN | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Catal... |
Q6FM32 | MSSSDSIRMVLIGPPGAGKGTQAPNLVERFHAAHLATGDMLRSQISKGTELGLQAKKIMDQGGLVSDDIMVNMIKDELTNNPACKNGFILDGFPRTIPQAEKLDNMLKERGTPLEKAVELKIDDELLVARITGRLIHPASGRSYHKLFNPPKEDMKDDVTGEPLVQRSDDNEDALKKRLGAYHDQTEPIVDFYKKTGIWADVDASQPPETVWSAILKALGKN | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Catal... |
P0CO43 | MSGNSEVEYLKSLVSQLQDKIHHLEKSTSTSVSNTISSVTSALSPSSSIKPPRMVLIGPPGAGKGTQAPNISSKYCICHLATGDMLREQVARQTELGKAAKQIMDQGGLVSDEIMVGMIKQELEKNAECKNGFILDGFPRTVPQASKLDAMLAERKQAIDHAIELKIPDVLLISRITGRLVHPASGRSYHKEFNPPKKPMTDDITGEPLIQRSDDNVGTLRKRLDTYHAQTGPVVDYYKGTGVWTPVDAAQSPKLVWASISSILESKKN | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Catal... |
Q1L8L9 | MAPSTQEDDTVSGIRKGIRAILLGPPGAGKGTQAPKLAEKYCVCHLATGDMLRAMVASGSELGQRLKETMDAGKLVSDEMVVELIDNNLDTPACKNGFLLDGFPRTVKQAEMLDDLMEKRSEKLDSVIEFSVDDSLLVRRICGRLIHQPSGRSYHEEFHPPKEHMKDDVTGEPLIRRSDDNETTLRSRLESYHRQTSPLVQYYSARGLHTAIDASQSTDLVFASILAAFSAATCKDLVYFV | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays... |
Q54QJ9 | MEPQFKVKIDNDSARILKELAEKKRDEGLRVVFIGPPGSGKGTQAPLVKEDYCLCHLSTGDMLRAAIEQGTETGKQAKTIMDQGGLVPDEVMVNMIKENIQTPECKKGFILDGFPRTVPQAEKLDKMLAEDNKKIDHVLDFAIDDSLLVKRITGRLVHPSSGRSYHREFFPPKVDMIDDITGEPLIQRSDDNEEVLKKRLESFHKNTTPVLGYYQNKGILSTIDASKSAPFVSHTIKSIFLSTLHFPHNASIFKTFHQKMKMQVHSTETPLAAEIL | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Catal... |
Q8UE38 | MRLIFLGPPGAGKGTQAKRLTDKYGIPQLSTGDMLRAAVSAGTEIGKRAKAVMDAGGLVSDDIVNQIVSERIEAPDCAKGFILDGYPRTVPQAKALADNMRKKNQVLDAVIELKVDEEALIRRIENRVAETIAAGGTVRSDDNPEAFRKRLTEYREKTAPLSAYYSEQGELVTLDGMADVDAVTEAIERVLEKASA | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21177
Sequence Length: 196
Domain: Consists of three domains, a large ce... |
Q2IJ70 | MILILLGPPGAGKGTQAKLLSTELGIPHISTGDMFRDHKARGTEIGKQVQAIMDGGGLVTDDITNAMVKERLSRPDVAPGFILDGYPRTVVQAEYLDGLLRSLGRSIGRALSYEVAEELVVERISGRRSCPRCGAVYHVSQNPPRRAGYCDRDDAELVQREDDKPENVRKRMQEYGTKTEPLKRYYRDRGELTEVEGVGTPEGILAATKKVLGR | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23564
Sequence Length: 214
Domain: Consists of three domains, a large ce... |
B2KEK1 | MIIVLLGAPGAGKGTQSVLVAEKYGLKHISTGDLLREEIANNTELGKQAKKLIDGGNLVPDEMILGLLKNAFLNRGKGVVLDGFPRTLSQAEMMHPIVKGLAEKLSAVINIKLSEDEITQRIVLRRQCKNCGNIFNLRFIKNFDGKCPKCGSTDIYQRADDNEESAKNRINVYHSQTEPVVGFYKNKTYYKEVDGSKNKEEVFEEISKFINRKK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23933
Sequence Length: 214
Domain: Consists of three domains, a large ce... |
Q8SVC2 | MKYSRIVVMGPPGCGKGTQSSLISEKYEIPHVSSGDIIREEMKKSSKEATVIREMVNSGRLAPDEIVNELVLKKIRSMSKYILDGYPRRIEQAGMLGDDVDLVIFIDVDEDTCISRICGRNEGRDDDDEEVGRKRCMVYNKETAPVLEFYKRHGKLLTINGCASPGTVFEEIRRSIE | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 19963
Sequence Length: 177
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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B1GZA3 | MNYIILGPPGAGKGTQAKKIAVKFGILHLSTGDMFREAKKSDESISKLLSSGQLVPDEIVVNMVRKRLEKNNIKKGFLLDGFPRTVKQTGELDRMLMSENIKIDSVFLISVPFEEAAKRIAGRIVCACGASYHTMLLPPKEFGKCDCCGGVLFHRSDDKEEDIIRDRFSVYEKQTKPLIEYYKESGLLIYIDGLKSESDVFEQISGCIINGE | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23659
Sequence Length: 212
Domain: Consists of three domains, a large ce... |
O96907 | MAKVFLIMLGGPGAGKGTQCANIEKHLNSSAHISTGDLLRAEIKNKTEIGLKVEDIIRNGQLVSDEIICNMVNNFIAKNEKEVIVFDGYPRAVSQLEALLKEATAETKICVINLEIPDEILIQRIVSRGKTSGRADDNTEAAAKRLAVYHAQHDEMIKAIKAKNLPYFVVDHLGGPDEVFNEIKGVFANVGLH | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP . Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity).
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21102
Sequence Length: 193
Subcellular Location: Cytopl... |
Q2S1E4 | MRLIIFGPPGAGKGTQAGLLEERHGITQISTGDILREAMAQETELGQKAKSYIDAGELVPDALVRDLAEQAIADEGHDDFMLDGYPRTDQQAEWLTEFLASNETPLDGVLSMKVPDDVLVRRLSRRRVHEETGETYHLDHDPPPEDVDPDLIVQRSDDEPETIQNRLDVYREETAPLATYYEERDLLVPVDGTGGIEEVFGRIEEALDALER | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23722
Sequence Length: 212
Domain: Consists of three domains, a large ce... |
P25824 | MTDQKLAKAKVIFVLGGPGSGKGTQCEKLVQKFHFNHLSSGDLLRAEVQSGSPKGKELKAMMERGELVPLEVVLALLKEAMINWLTKIVISLSIRYPRELDQGIKFEKEVCPCLCVINFDVSEEVMRKRLLKRAETSNRVDDNEETIVKRFRTFNELTKPVIEHYKQQNKVITIDASGTVDAIFDKVNHELQKFGVK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22344
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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O29153 | MIALGIEGTAWSLSIGVVDEEGVIALENDPYIPKEGGIHPREASQHHSERLPSLLSRVFEKVDKNSIDVVAFSQGPGMGPCLRVVATAARLLAIKLEKPLVGVNHCLAHVEVGRWQTGARKPVSLYVSGGNSQVIARRGNRYRVFGETLDIGIGNALDKLARHMGLKHPGGPKIEELAKKGQKYHFLPYVVKGMDFSFSGMVTAAQRLFDSGVRMEDVAFSFQETAFAMLTEVTERALAYLDLNEVLLVGGVAANKRLQEMLRIMCEDRGAKFYVPPKELAGDNGAMIAYTGLLMYKHGHQTPVEKSYVRPDFRIEDVEV... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcar... |
Q4WDE9 | MIAIGLEGSANKLGVGIMLHPEDGSTPRVLANIRHTYVSPPGEGFLPKDTARHHRSWVVKLVKRALREARISVRDVDCICFTKGPGMGAPLQSVAVAARMLSLLWGKELVGVNHCVGHIEMGRLITGSTNPVVLYVSGGNTQVIAYSSQRYRIFGETLDIAVGNCLDRFARTLHISNDPAPGYNIEQLAKKGKQLVDLPYTVKGMDCSFSGILAAIDGLAASYGLNGEEKEEEGAGDDSKPTRADLCFSLQETVFSMLVEITERAMAHVGSKEVLIVGGVGCNERLQEMMGIMARDRGGSVHATDERFCIDNGIMIAQAG... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbam... |
Q5A6A4 | MVVDLDKYLKPGKDHYLALGLEGSANKLGVGVIKHNKGPLSSTNRAEVLSNIRDTYITPPGEGFLPRDTARHHRNWVVRIIKQALATAKIAGKDIDVICFTQGPGMGAPLQSVVIAARTLAQLWNIPIVGVNHCVGHIEMGREITGAENPVVLYVSGGNTQVIAYSKQRYRIFGETLDIAIGNCLDRFARTLKIPNEPAPGYNIEQMAKKGKHLVPLPYTVKGMDLSMSGILAAIDSIAKEMFGKQQKKLIDEESGEPITAEDLCFSLQETLFSMLVEITERALAHVDSNQVLIVGGVGSNQRLQEMMKLMIQDRKNGQI... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbam... |
Q8SQQ3 | MIAMGLEGSANKLGVGIMRDDEILANERLTYAPPPGEGFIPVKTAEHHRSRILGLVAVSLEKAGVDLDDVDIFCYTKGPGMGLPLSVVATVARTLSLYCNKPLVPVNHCIAHIEMGRFITKASNPVILYASGGNTQIIAYHNRRYKIFGETLDIAVGNCIDRFARALKLPNFPAPGLSVERYAKLGKNYIELPYVVKGMDVSFSGILSNIKRKIAEDEQVKRDLCYSLQETVFSALVEVTERAMAFSSSKEVLIVGGVGCNLRLQEMMGIMARERGGVCYATDERFCIDNGVMIAYVGMLMAKSGAAFKLGECFVTQRYR... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbam... |
P86244 | SLRECELYVQKTDSREDEISPPPPNPVVKRGAISAEVYTEEDAASYVRNVLFSHLDDNERILMGSTLRMYEEFLSKVSILESLDKLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRVLGPCSDILKR | Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.
Sequence Mass (Da): 18794
Sequence Length: 167
Subcellular Location: Cell... |
P31321 | MASPPACPSEEDESLKGCELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEENRQILARQKSNSQSDSHDEEVSPTPPNPVVKARRRRGGVSAEVYTEEDAVSYVRKVIPKDYKTMTALAKAISKNVLFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGEWVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVEVGRLGP... | Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.
Sequence Mass (Da): 43073
Sequence Length: 381
Subcellular Location: Cell... |
P00515 | MSHIQIPPGLTELLQGYTVEVLRQRPPDLVDFAVDYFTRLREARSRASTPPAAPPSGSQDFDPGAGLVADAVADSESEDEEDLDVPIPGRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDPEQLSQVLDAMFERTVKVDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKVYKDGERIITQGEKADSFYIIESGEVSILIKSKTKVNKDGENQ... | Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase (By similarity).
PTM: A second phosphorylation site has not been located.
Sequence Mass (Da): 45094
S... |
P13861 | MSHIQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARAPASVLPAATPRQSLGHPPPEPGPDRVADAKGDSESEEDEDLEVPVPSRFNRRVSVCAETYNPDEEEEDTDPRVIHPKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERIVKADEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKIYKDGERIITQGEKADSFYIIESGEVSILIRSRTKSNKDG... | Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
PTM: Phosphorylated by the activated catalytic chain.
Sequence Mass (Da): 45518
Sequence Length: 404... |
P05207 | SGSQDLEPSSGLVTDAIADSESEDDEDLDVPIPSRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERTVKVDEHVIDQRDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMY | Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
PTM: Phosphorylated by the activated catalytic chain.
Sequence Mass (Da): 17706
Sequence Length: 155... |
P12368 | MSHIQIPPGLTELLQGYTVEVLRQQPPDLVDFAVEYFTRLREARRQESDSFIAPPTTFHAQESSGVPVIEEDGESESDSDDEDLEVPIPSKFTRRVSVCAETFNPDEEEDNDPRVVHPKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFEKIVKTDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIVATSDGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLFKSLEMSERMKIVDVIGEKIYKDGERIITQGEKADSFYIIESGEVSILIRSKTKTNKNGGNQ... | Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
PTM: Phosphorylated by the activated catalytic chain.
Sequence Mass (Da): 45480
Sequence Length: 401... |
P31322 | MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQEENERKGTARFGHEGRTWGDAGAAGGGGTPSKGVNFAEEPRHSDSENGEEEEEEAADAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKEGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEVSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGE... | Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
PTM: Phosphorylated by the activated catalytic chain.
Sequence Mass (Da): 46336
Sequence Length: 418... |
P31323 | MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGTARFGHEGRTWGDLGAAAGGGTPSKGVNFAEEPMQSDSEDGEEEEAAPADAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGE... | Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
PTM: Phosphorylated by the activated catalytic chain.
Sequence Mass (Da): 46302
Sequence Length: 418... |
P31324 | MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGAARFGHEGRTWGDAGAAAGGGIPSKGVNFAEEPMRSDSENGEEEEAAEAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKEGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEVSERLKVVDVIGTKVYNDGEQIIAQGDLADSFFIVESGEVK... | Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
PTM: Phosphorylated by the activated catalytic chain.
Sequence Mass (Da): 46167
Sequence Length: 416... |
A4QUT2 | MHASLSSWLLAASLLTQPISVSGQGCPFAKRDGTVDSSLPQKRADAPETTTFGRCAVKSNQAGGGTRSHDWWPCQLRLDVLRQFQPSQNPLGGDFDYAEAFQSLDYEAVKKDIAALMTESQDWWPADFGNYGGLFVRMAWHSAGTYRAMDGRGGGGMGQQRFAPLNSWPDNQNLDKARRLIWPIKQKYGNKISWADLMLLTGNVALENMGFKTLGFGGGRADTWQSDEAVYWGAETTFVPQGNDVRYNNSVDINARADKLEKPLAATHMGLIYVNPEGPNGTPDPAASAKDIREAFGRMGMNDTETVALIAGGHAFGKTH... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
Function: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early s... |
A0QXX7 | MSSDTSDSRPPNPDTKTASTSESENPAIPSPKPKSGAPLRNQDWWPNQIDVSRLHPHPPQGNPLGEDFDYAEEFAKLDVNALKADLTALMTQSQDWWPADYGHYGGLFIRMSWHSAGTYRIHDGRGGGGQGAQRFAPINSWPDNVSLDKARRLLWPIKQKYGNKISWADLLVFTGNVALESMGFKTFGFGFGREDIWEPEEILFGEEDEWLGTDKRYGGGEQRQLAEPYGATTMGLIYVNPEGPEGQPDPLAAAHDIRETFGRMAMNDEETAALIVGGHTFGKTHGAGDASLVGPEPEAAPIEQQGLGWKSSYGTGKGPD... | Cofactor: Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.
Function: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria.
PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not... |
A6T9H9 | MSTSNDPSNNASAGKCPFHAETPKQSAGSGTANRDWWPNQLRVDLLNQHSNRSNPLGENFNYREEFKKLDYSALKADLRALLTDSQEWWPADWGSYIGLFIRMAWHGAGTYRTVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLYMLAGNVALENAGFRTFGFGAGREDVWEPDLDVDWGDEKEWLAHRHPESLAKQAIGATEMGLIYVNPEGPNASGEPLSAAAAIRATFGNMAMDDEEIVALIAGGHTLGKTHGAAETSHVGAEPEAAPLEAQGLGWHSSYGSGAGADAITSGLEVVWTQ... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Function: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.
Catalytic Activity: AH2... |
P84744 | VGCEECPMHCKGKHAVPTCDDGVCNCNV | Function: Blocks voltage-gated potassium channels Kv1.1/KCNA1 (IC(50)=145 nM), Kv1.2/KCNA2 (IC(50)=2.5 nM), and Kv1.3/KCNA3 (IC(50)=15). Also inhibits calcium-activated potassium channels (KCa/KCNN).
Sequence Mass (Da): 2949
Sequence Length: 28
Domain: Has the structural arrangement of an alpha-helix connected to a bet... |
P83406 | VGCEECPAHCKGKNAIPTCDDGVCNCNV | Function: Calcium channel activator. Rapidly and reversibly activates ryanodine receptor 1 (RYR1).
Sequence Mass (Da): 2880
Sequence Length: 28
Domain: Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).
Subcellular Location: Secreted
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P0C8X7 | KRKCGLCKYRCCSGG | Function: May block voltage-gated potassium channels (Kv).
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 1662
Sequence Length: 15
Subcellular Location: Secreted
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P86121 | GWINEEKIQKKIDEP | Function: Has antimicrobial activity against S.aureus (78% growth inhibition at 1.8 uM).
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 1827
Sequence Length: 15
Subcellular Location: Secreted
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Q2HR82 | MPRMKDIPTKSSPGTDNSEKDEAVIEEDLSLNGQPFFTDNTDGGENEVSWTSSLLSTYVGCQPPAIPVCETVIDLTAPSQSGAPGDEHLPCSLNAETKFHIPDPSWTLSHTPPRGPHISQQLPTRRSKRRLHRKFEEERLCTKAKQGAGRPVPASVVKVGNITPHYGEELTRGDAVPAAPITPPYPRVQRPAQPTHVLFSPVFVSLKAEVCDQSHSPTRKQGRYGRVSSKAYTRQLQQALEEKDAQLCFLAARLEAHKEQIIFLRDMLMRMCQQPASPTDAPLPPC | Function: Plays a role in viral gene regulation and seems to be essential for KSHV reactivation. Disrupts host G1 cell cycle control thus allowing viral transcription and translation to proceed at the early stages of infection. Catalyzes its own SUMO modification as well as that of its interacting partners such as host... |
Q8SS96 | MTTEIRNIKLVQKIASGAFGDIFIGQNTVTNQTVAVKLEKKAHYGQLKHEYGVYKALGGTRTPRIYEYGKILYENVYVNGLVMELMGKSLEQLFVTCSRRFSLKTVLMLGERMVDNVEYLHHRNYVHRDIKPDNFVFDVQGDRLYLIDYGLAKEFRNPMTFKHREMRTDKSLTGTARYASLRTHQGYEQSRRDDLESVGFCMVYFLKGRLPWQGLKAKTKQEKYDRIRESKESISLYELCMGLPKEIHSFCFYVRNLGYEDMPNYAYLRTLLSDALRQRGLRSDGVFDWMVRTPSDSMGDLEIL | Function: Involved in DNA repair. May regulate the activity of protein(s) involved in double strand break repair caused by gamma rays (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35525
Sequence Length: 304
Subcellular Location: Nucleus
EC: 2... |
P23291 | MSMPIASTTLAVNNLTNINGNANFNVQANKQLHHQAVDSPARSSMTATTAANSNSNSSRDDSTIVGLHYKIGKKIGEGSFGVLFEGTNMINGVPVAIKFEPRKTEAPQLRDEYKTYKILNGTPNIPYAYYFGQEGLHNILVIDLLGPSLEDLFDWCGRKFSVKTVVQVAVQMITLIEDLHAHDLIYRDIKPDNFLIGRPGQPDANNIHLIDFGMAKQYRDPKTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDMEALGHVFFYFLRGHLPWQGLKAPNNKQKYEKIGEKKRSTNVYDLAQGLPVQFGRYLEIVRSL... | Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
PTM: Palmitoylated by AKR1.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 61715
Sequence Len... |
Q8SQR2 | MRGEIMDYTICREIGKGGFGKVYEVKKKADQKSYALKIETNAPKAGRNSIINEIQAYSELQGCEKIPRLVDHGSYEGLTFLVLPLLKYSLKDLLERHPRFFTKKSATIVGKKLLNAIEFIHGKGRLHRDIKPENVMFGHNNRIYLVDFGMSAPYLRGDGSHIPEVGGKSVSGTLWYMSINTHRGIEQSRRDDLESLFYLLILLYKSRLPWMEPGASVSKKQEARTKEIKENLSVYDLCDGIHGKEHLIKFFQHISSLEFAEKPNYRYLNSLLDKIFHSNKELQGYKRAPKKEDTGLIRTSLWHKFISILSPFEVKYDG | Function: Involved in DNA repair. May regulate the activity of protein(s) involved in double strand break repair caused by gamma rays (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 36589
Sequence Length: 318
Subcellular Location: Nucleus
EC: 2... |
P23292 | MSQVQSPLTATNSGLAVNNNTMNSQMPNRSNVRLVNGTLPPSLHVSSNLNHNTGNSSASYSGSQSRDDSTIVGLHYKIGKKIGEGSFGVLFEGTNMINGLPVAIKFEPRKTEAPQLKDEYRTYKILAGTPGIPQEYYFGQEGLHNILVIDLLGPSLEDLFDWCGRRFSVKTVVQVAVQMITLIEDLHAHDLIYRDIKPDNFLIGRPGQPDANKVHLIDFGMAKQYRDPKTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDMEAMGHVFFYFLRGQLPWQGLKAPNNKQKYEKIGEKKRLTNVYDLAQGLPIQFGRY... | Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
PTM: Palmitoylated by AKR1, which is required for proper plasma membrane localization of YCK2.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) +... |
P39962 | MSQRSSQHIVGIHYAVGPKIGEGSFGVIFEGENILHSCQAQTGSKRDSSIIMANEPVAIKFEPRHSDAPQLRDEFRAYRILNGCVGIPHAYYFGQEGMHNILIIDLLGPSLEDLFEWCGRKFSVKTTCMVAKQMIDRVRAIHDHDLIYRDIKPDNFLISQYQRISPEGKVIKSCASSSNNDPNLIYMVDFGMAKQYRDPRTKQHIPYRERKSLSGTARYMSINTHFGREQSRRDDLESLGHVFFYFLRGSLPWQGLKAPNNKLKYEKIGMTKQKLNPDDLLLNNAIPYQFATYLKYARSLKFDEDPDYDYLISLMDDALR... | Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 60261
Sequence Length: 524
Domain: The YXXZ (T... |
Q9JM63 | MTSVAKVYYSQTTQTESRPLVAPGIRRRRVLTKDGRSNVRMEHIADKRFLYLKDLWTTFIDMQWRYKLLLFSATFAGTWFLFGVVWYLVAVAHGDLLELGPPANHTPCVVQVHTLTGAFLFSLESQTTIGYGFRYISEECPLAIVLLIAQLVLTTILEIFITGTFLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANMRKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDTASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVLILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSAS... | Function: May be responsible for potassium buffering action of glial cells in the brain. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as e... |
Q14654 | MLSRKGIIPEEYVLTRLAEDPAKPRYRARQRRARFVSKKGNCNVAHKNIREQGRFLQDVFTTLVDLKWPHTLLIFTMSFLCSWLLFAMAWWLIAFAHGDLAPSEGTAEPCVTSIHSFSSAFLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAETLIFSKHAVIALRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPMENGVGGNSIFLVAPLIIYHVIDANSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQARTSYLADEILWGQRFVPIVA... | Function: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the vol... |
Q61743 | MLSRKGIIPEEYVLTRLAEDPAEPRYRTRERRARFVSKKGNCNVAHKNIREQGRFLQDVFTTLVDLKWPHTLLIFTMSFLCSWLLFAMVWWLIAFAHGDLAPGEGTNVPCVTSIHSFSSAFLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAETLIFSKHAVITLRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPMENGVGGNGIFLVAPLIIYHVIDSNSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQARTSYLADEILWGQRFVPIVA... | Function: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the vol... |
F1NHE9 | MTAGRVNPYSIVSSEEDGLRLTTMPGINGFGNGKIHTRRKCRNRFVKKNGQCNVEFTNMDDKPQRYIADMFTTCVDIRWRYMLLLFSLAFLVSWLLFGLIFWLIALIHGDLENPGGDDTFKPCVLQVNGFVAAFLFSIETQTTIGYGFRCVTEECPLAVFMVVVQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVAMRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRITEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEINEDSPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLASE... | Function: Inward rectifying potassium channel that is activated by phosphatidylinositol 4,5-bisphosphate and that probably participates in controlling the resting membrane potential in electrically excitable cells. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow in... |
Q14500 | MTAASRANPYSIVSSEEDGLHLVTMSGANGFGNGKVHTRRRCRNRFVKKNGQCNIEFANMDEKSQRYLADMFTTCVDIRWRYMLLIFSLAFLASWLLFGIIFWVIAVAHGDLEPAEGRGRTPCVMQVHGFMAAFLFSIETQTTIGYGLRCVTEECPVAVFMVVAQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVALRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRVTEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEIDEASPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLANE... | Function: Inward rectifying potassium channel that is activated by phosphatidylinositol 4,5-bisphosphate and that probably participates in controlling the resting membrane potential in electrically excitable cells. Probably participates in establishing action potential waveform and excitability of neuronal and muscle t... |
O60928 | MDSSNCKVIAPLLSQRYRRMVTKDGHSTLQMDGAQRGLAYLRDAWGILMDMRWRWMMLVFSASFVVHWLVFAVLWYVLAEMNGDLELDHDAPPENHTICVKYITSFTAAFSFSLETQLTIGYGTMFPSGDCPSAIALLAIQMLLGLMLEAFITGAFVAKIARPKNRAFSIRFTDTAVVAHMDGKPNLIFQVANTRPSPLTSVRVSAVLYQERENGKLYQTSVDFHLDGISSDECPFFIFPLTYYHSITPSSPLATLLQHENPSHFELVVFLSAMQEGTGEICQRRTSYLPSEIMLHHCFASLLTRGSKGEYQIKMENFDK... | Function: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to... |
Q9UNX9 | MGLARALRRLSGALDSGDSRAGDEEEAGPGLCRNGWAPAPVQSPVGRRRGRFVKKDGHCNVRFVNLGGQGARYLSDLFTTCVDVRWRWMCLLFSCSFLASWLLFGLAFWLIASLHGDLAAPPPPAPCFSHVASFLAAFLFALETQTSIGYGVRSVTEECPAAVAAVVLQCIAGCVLDAFVVGAVMAKMAKPKKRNETLVFSENAVVALRDHRLCLMWRVGNLRRSHLVEAHVRAQLLQPRVTPEGEYIPLDHQDVDVGFDGGTDRIFLVSPITIVHEIDSASPLYELGRAELARADFELVVILEGMVEATAMTTQCRSSY... | Function: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to... |
E1BNE9 | MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQGPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQSEQFEIVVILEGIVETTGMTCQARTSYTEDE... | Function: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised... |
P48549 | MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQDPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQTEQFEIVVILEGIVETTGMTCQARTSYTEDE... | Function: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised... |
P63250 | MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQGPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQTEQFEVVVILEGIVETTGMTCQARTSYTEDE... | Function: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised... |
P48050 | MHGHSRNGQAHVPRRKRRNRFVKKNGQCNVYFANLSNKSQRYMADIFTTCVDTRWRYMLMIFSAAFLVSWLFFGLLFWCIAFFHGDLEASPGVPAAGGPAAGGGGAAPVAPKPCIMHVNGFLGAFLFSVETQTTIGYGFRCVTEECPLAVIAVVVQSIVGCVIDSFMIGTIMAKMARPKKRAQTLLFSHHAVISVRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPYMTQEGEYLPLDQRDLNVGYDIGLDRIFLVSPIIIVHEIDEDSPLYGMGKEELESEDFEIVVILEGMVEATAMTTQARSSYLASEILWGHRFEP... | Function: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to... |
P48051 | MAKLTESMTNVLEGDSMDQDVESPVAIHQPKLPKQARDDLPRHISRDRTKRKIQRYVRKDGKCNVHHGNVRETYRYLTDIFTTLVDLKWRFNLLIFVMVYTVTWLFFGMIWWLIAYIRGDMDHIEDPSWTPCVTNLNGFVSAFLFSIETETTIGYGYRVITDKCPEGIILLLIQSVLGSIVNAFMVGCMFVKISQPKKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAKLIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKEELEIVVILEGMVEATGMTCQ... | Function: This potassium channel may be involved in the regulation of insulin secretion by glucose and/or neurotransmitters acting through G-protein-coupled receptors. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltag... |
P56696 | MAEAPPRRLGLGPPPGDAPRAELVALTAVQSEQGEAGGGGSPRRLGLLGSPLPPGAPLPGPGSGSGSACGQRSSAAHKRYRRLQNWVYNVLERPRGWAFVYHVFIFLLVFSCLVLSVLSTIQEHQELANECLLILEFVMIVVFGLEYIVRVWSAGCCCRYRGWQGRFRFARKPFCVIDFIVFVASVAVIAAGTQGNIFATSALRSMRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFASFLVYLAEKDANSDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFALLGISFFALPAGILGS... | Function: Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea. KCNQ4 channels are blocked by linopirdin, XE991 and bepridil, whereas clofilium is without significant effect. Muscarinic agonist oxotremorin... |
Q9JK96 | DRIRISISQKRTGPSKQHLAPPPIPTSPSSEQVGEASSPSKVQKSWSFNDRTRFRASLRLKPRCSAEEGPSEEVAEEKSYQCELTVDDVMPAVKTVIRSVRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQARVDQIVGRGPGDRKTREKGDKGPS | Function: Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18845
Sequence Length: 168
Domain: The segment S4 is probably the voltage-... |
Q9NR82 | MPRHHAGGEEGGAAGLWVKSGAAAAAAGGGRLGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAATLGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFIYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPL... | Function: Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. Therefore, it is important in the regulation of neuronal excitabilit... |
Q9JK45 | MPRHHAGGEEGGAAGLWVRSGAAAAAGAGGGRPGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAAALGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFVYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTP... | Function: Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. Therefore, it is important in the regulation of neuronal excitabilit... |
Q96KK3 | MLMLLVRGTHYENLRSKVVLPTPLGGRSTETFVSEFPGPDTGIRWRRSDEALRVNVGGVRRQLSARALARFPGTRLGRLQAAASEEQARRLCDDYDEAAREFYFDRHPGFFLSLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALAACCRARYLERRLTQPHAWDEDSDTPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSISVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSPEGVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTL... | Function: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 .
Location Topology: Multi-pass membrane protein
... |
O35173 | MVSEFPGPGSRVPWRPRDEALRVNVGGVRRLLSARALARFPGTRLGRLQAAASEEQARRLCDDYDAAAHEFYFDRHPGFFLGLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALATCCRARYLERRVARPRAWDEDSDAPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSIGVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSAEEVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLAGAALGDQRGASGEELGDLGKVVQVFRLMR... | Function: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 .
Location Topology: Multi-pass membrane protein
... |
A7GN34 | MDKRISIAIDGPAAAGKSTVAKVVAKQLSYVYIDTGAMYRTLTYAALEQNIDIENEEKLMEVLQSIRIEFQQGKDTQQVFLNGQDVSEVIRTPDVTNRVSIVAKHRLVREEMVRRQQELAAQGGVVMDGRDIGTHVLPNAEVKIFMLASVEERAERRHLENMRKGFSSNLEQLKKEIAQRDKLDSEREVSPLKKAEDAFELDTTSLSIEEVVRNIMAIVSEALQK | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25386
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q5L9K4 | MKKITIAIDGFSSCGKSTMAKDLAKEIGYIYIDSGAMYRAVTLYSIENGIFHGDTIDTDELKRRIGDIHISFRIDPETGRPNTYLNGVNVENKIRTMEVSSKVSPISALGFVREAMVAQQQEMGKAKGIVMDGRDIGTTVFPDAELKIFVTASAEIRAQRRYDELKAKGQETGFEEILENVKQRDHIDQTREVSPLKKADDALLLDNSHLTIAEQKEWLMAEYQKAIKA | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25649
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q65I08 | MEKKLCIAIDGPAAAGKSTVAKIVARKKSYIYIDTGAMYRAITYLALEKGVDLNDEAALTALLKESAIDLTVSPEGEQKVYIAGEDVTEAIRTDSVSNQVSIVAKYAGIREEMTKRQQQLAEKGGVVMDGRDIGTHVLPNAEVKIFLLASVEERAKRRFEENVKKGYNVNYETLAEEIRRRDKLDSEREISPLKKADDALEIDTTSLTIDEVAEKILQIVDKKAQK | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25048
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
P38493 | MEKKLSIAIDGPAAAGKSTVAKIVAEKKSYIYIDTGAMYRAITYAALQENVDLTDEEKLAELLKRTDIELITTKDGQKVFVNGTDVTEAIRTDEISNQVSIAAKHRSVREEMVKRQQQLGEKGGVVMDGRDIGTHVLPNAEVKIFLLASVEERAKRRYEENVKKGFDVNYETLIEEIARRDKLDSEREVSPLRKAEDALEIDTTSLSIQEVADKILEAVEQKSR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25096
Sequence Length: 224
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q8A626 | MKKITIAIDGFSSCGKSTMAKDLAREVGYIYIDSGAMYRAVTLYSIENGIFNGDVIDTEKLKEAIRDIRITFRPNPETGRPDTYLNGVNVENKIRTMGVSSKVSPISALDFVREAMVAQQQAMGKEKGIVMDGRDIGTTVFPDAELKIFVTATPEIRAQRRFDELKAKGQEGSFEEILENVKQRDYIDQHREVSPLRKADDALLLDNSNLSIEQQKEWLSEQFGKVVKE | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25759
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q83E10 | MNARQKPAPVITIDGPSGSGKGTIAFRIAQTLNWYLLDSGIIYRAIAWAMAHYKVPLEDSAGLARLLKRVQISIENRILGKKAKISCDGHDITLAIRSEECGALASRASALPIVREAVLQYQRDFRQRPGLVADGRDMGTVVFPDAVLKFYFDADSQQRAYRRYKELQDRGINVSLPDIQEDLEERDRRDITRSISPTKPAEDAVIIDTTHLSIEAVFATVMNHVRQRGLANVANEK | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 26459
Sequence Length: 237
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q0KDH7 | MTIVNVIAIDGPTASGKGTVAHKVADAVGFHLLDSGALYRLVALASDRAGIDLADVDALAKIASRLDVKFGPDRVWLQGEEVSLAIRAEAIGNRASAIAVHQPVRDALTQLQRSFRKLPGLVADGRDMGTVIFPDAPLKVFLTASVEARARRRYKQLIDKGISANIEDLLRDLEARDVRDRTRTAAPLRPAEDAKLLDTSDMTVDQAVAQVLEWFAAVRPDA | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 23969
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q6A8F7 | MSTSPLVIAIDGPSGSGKSSTSRGVANRLGLARLDTGSMYRAVACRVAHLGIDPTTNPRDAIKVAQSCHLEIDTSAIDDRVVIDGEDVTKEIRDPQTSAKVSAVATIQPVRDALTARMRQVAADRGRIVMEGRDITTVVCPDAQVRVLLVADPAIRVARRQAELGEKVDMAQVIDSIVRRDRDDSTVSTFEEPAEGVTVVDSTHLNLDQVIDAVIDLVPVTLR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 23916
Sequence Length: 223
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q11YY6 | MKKIIVAIDGYSACGKSTTAKILAAKLGYVYIDTGAMYRSVALYFIQHYINSTNPKAVAEALNQIHISFVHNNKTETCETYLNGLNVESEIRKMYVSEKVSEVSAIPEVRKRMVELQQKMARKRGVVMDGRDIGTHVFPDAELKIFMVADMHVRAFRRQQELFERKQIIDLDDIIKNIESRDLMDTTREESPLRKASDAYEIDTTYITVEEQVDCIMNIAVGKMIELEYNIENI | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 26827
Sequence Length: 234
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q7ZWE9 | MKPQVVFVLGGPGAGKGTQCARIVENYSYTHLSAGDLLREERSRTDSEFGQLIDSYIKEGKIVPVQITINLLRKAMEETMKADEKKFRFLIDGFPRNQDNLQGWNTEMDGKADVKFVLFFDCSNEVCIDRCLERGKSSGRTDDNRESLEKRIQTYLQSTRPIIELYEKQGKVQRIDASRSVDEVFADVKNILEKDD | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase... |
Q9RRE9 | MIVTIDGVAASGKSSVSSGVARALGIPYVSSGLLYRAATLLGLEAALDLSDAPRLLAHLRALPLRLEPLAEGNRVWSGERDLTPGLHQSAVDAGVSTVAAHPELRAWVDEQLRQLPPPFVAEGRDMGTNVFPDAPAKFYLTASPRIRAERRSAERPEDVDAIEAALIARDRKDAAQSAPAPDARVIDTGPLGLEEVIGEILGEIGQ | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 21781
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
A4J3N3 | MTEHKCIAIDGPAGAGKSTVAKKVAQKLNLLYIDTGAMYRAVTLKALRERINLWDDIALIELAKRTIITLLAGQKQSVLLDGLDVTREIRTPEVTNNVSIVAKIAGVREVLVQRQREMAEEAGVVMDGRDIGTVVLPKAKAKFFLTASAEERARRRAKEMMNFGYDVDLEQLIKEIEERDFMDSNRAVSPLVPAEDAVLIDSSGMTIDEVVNSIITWVEKGK | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24568
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q72DA1 | MPDTTGGHPAALKVVTLDGPAGVGKTTLARRVADALGIPYLDTGAMFRTMAWRLGPDGPDLDEALLRDRLAGFVFTLRGRGGASVLSCNGEDIGNEIRTEEVGAMASRIAALPVVRECLKAAQQRMGAAQPLVVEGRDMGTVVFPGARHKFFLDAAPEIRAMRRYTQLQTMGEAHDLALLTEQIRSRDEQDRNRAVAPLRPAADAIIVDTGDLDIDGVFGVIMQHIRSRDGL | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24955
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
P20425 | MMEKSKPNVVFVLGGPGSGKGTQCANIVRDFGWVHLSAGDLLRQEQQSGSKDGEMIATMIKNGEIVPSIVTVKLLKNAIDANQGKNFLVDGFPRNEENNNSWEENMKDFVDTKFVLFFDCPEEVMTQRLLKRGESSGRSDDNIESIKKRFNTFNVQTKLVIDHYNKFDKVKIIPANRDVNEVYNDVENLFKSMGF | Cofactor: Binds 1 Mg(2+) ion per monomer. The Mg(2+) ion binds to water and substrates.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
Cat... |
Q7UEW6 | MIITIDGPAGAGKSSIARRVASELGFEFLDTGAMYRAVTWGVMQQGIAWDDVESLVEFADAAQLIWQDDRIYLDNQDISEEIRTPQVTSHIRYLADPPRIRERITAQQRRIATGRDIVTEGRDQGTEVFPDAHCKIFLTASPEERARRRQRQLAENGRVMSVEEILAAQNQRDLEDRMRPVGRLRAASDAIVVQTDGMSPDEVREEVLRLVRECVQASAANSASSDVTR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25696
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q0SI81 | MSTSKLVVAMDGPSGTGKSSVSRMLAQRLDARYLDTGAMYRIATLHALRKGVDLTDPAAIADATAGLPWSIGTDPAGEQVLLDGEDVGEEIRGDAVTKAVSAVSAVPAVRELLVAAQRRLAGEAERIVVEGRDIGTVVIPDADVKIYLTASAEARAQRRNAQNLAEGRGDDYAAVLADVQRRDHLDSTRAVSPLRPADDSVLVDTSELGIDDVIGRLLLVVSERTGAGQ | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24066
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q2RXP6 | MIIAIDGPAASGKGTLARRLATQLRFAYLDTGKLYRAVGMAVIKGGADPHDAKAALAAARALDPATLGDRLLSTDTAGKAASVVGAIPEVRAALLDLQRDFATHPPQGAPGAVLDGRDIGTVVCPEAEVKIFVTASVEVRAHRRLQELRSGGHDVKEDDVLRDMRERDARDSGRAVAPMAIAADAVVLDTSRMTAEQALTAALDILAHKSQKT | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 22305
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q9ZD27 | MIDLKTKAFDIAQNFTISLDGPAASGKGTVGLILAKKFSLKYFQSSIVYRQLAFNCINQQIDITDIDAVIALSKELKLDNNIDLENEDIGDIASQIAVISDVRNNLNENLINLVKTTPRIIMEGRDIGTVVAPDADLKIFITASPYVRAIRRYNQLQAKGKTCILDEIIQQIILRDKRDKERKAGPLLPALGAFIIDTSKLSAIEIVEEVTNYIKNKIT | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24319
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q8NT57 | MARFSPQDLADHLKDGLLSFPATAFQDDLEVDEAAYVEHIEWQSSYPVAGLFAAGGTGEGFSLTVEENHRVTQLAVQASSPEVPVLGSATGSTKSAIANAQGAEAAGAEGVLLLPPYLTECDAEGLYNHAAAVCESTSLGVIVYNRANAIYSPEVIARLSERYPNFIGFKDGTGNIEHLAKITTLCGDRLFYLGGLPTAETFALPLLQMGMSTYSSAMFNFIPDFALSFYADVRAQDSAAVKQKLSDFVLPYLDIRDRAQGYGVSIVKGGLKAVGRNAGGVRPPLRNLSEQDIADLSDLLATSGAGSYRLPVEVKA | Catalytic Activity: 5-dehydro-4-deoxy-D-glucarate + H(+) = 2,5-dioxopentanoate + CO2 + H2O
Sequence Mass (Da): 33552
Sequence Length: 316
Pathway: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-dioxopentanoate from D-glucarate: step 2/2.
EC: 4.2.1.41
|
B2RXH2 | MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDP... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code.
Catalytic Activity: 2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(9)-[... |
Q9U297 | MASAATTTHFPSSRIPSEPCASSGPLFPDDVLFTTEASSASSSSCHVENDSRPLSPTMFTDGRTPVNISAKHLKDHPLHEPTGTSEVLTFYPTMREFKNFSQYIKKIEQNGGHLKAGIAKIVAPEGWTPRPTRKDFSDVDDYEITQPARETIEATEKPGAYFKRNVTCRRKMPVREFRTLANSAQYRNPRPDLKGSEIEKHYFDNILHGEPIYGADTEGSFYDAQVEEWNMNRLGTILEDTNYEIKGVNTVYLYFGMYKTTFPWHAEDMDLYSINFLHFGAPKYWFAISSEHADRFERFMSQQFSYQNEYAPQCKAFLRH... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code . Demethylation of Lys residue generates formaldehyde and succinate. Involved in the negative regulation of lifespan in a ger... |
Q81HP9 | MEKKQSILSPIIRITFTFLVLCGLVYPLIVTGIAQAVMKDNADGSLIYNDKNEVIGSKLIGQNFTDPRYFQGRVSSIEYKAEASGSNNYAPSNPDLEKRVEKSIEEWKKQNPSVPVTEVPIDLVTNSGSGLDPDISPKAASVQVDRISKLTDIPKEKLNQLIKDQTEGAALGLFGETRVNVLKLNLALQELMK | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
Q8A521 | MKTLFKSLKITLVFCVFFSVFYILILWLFAQVAGPNKGNAEVATLDGKVVGAANVGQMFTKDIYFWGRPSCAGDGYDASSSSGSNKGPTNPEYLAEVEARIDTFLVHHPYLSRKDVPAEMVTASASGLDPNITPQCAYVQVKRVAQARGLTENQVKEIVDQSVEKPLLGIFGTEKINVLKLNIALEENK | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
A4Z016 | MLKEIRPAIFVLLALTLITGLLYPLAMTGLAVTIFPAQAAGSLITRNGQVIGSALIGQEFKDDRYFHGRPSATSTADPNDSTKTVPAPYNAANSSGSNLGPTSKALADRVKEDVDKLKAENPAQPVPVDLVTTSASGLDPHVSPEAAMFQVPRVAKARGVPEDRVRALVVKNTEGRLIGLLGEPRVNVLALNLALDAATATK | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
A6X5I0 | MLKQLRPALVMIVSLTVITGLLYPLGMTGIAQVIFPANANGSLIEKDGTIIGSELIGQGFTGDRYFHGRPSAAGQNGYDAASSGGSNLGPTNPKLIERIKADATALSQDEGSARPPIDLVTTSASGLDPHISPETAFYQVPRVAKARGIDEAALREIVEQQVEARELGFLGEPVVNVLKLNLVLDRTSTK | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
Q9X8Z8 | MNTSLTNAARLFTAGLRALLVLTVVTGIVYPLVVTGVAQGLFPGKANGSEIKADGKVVGSSLIGQSYNLPLKEGRETPEPDLRWFQGRPANGLGTNTVNTRYELILSGATNRSADDPELLQWVQDAKAAVVRDNSVPGHPVRPEDVPADAVTSSGSGLDPDISPRYADLQVHRVAAKNGLPAERVQELVDEHTTPRTLGFIGEPRVNVLELNIALVELVAPGAGH | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
P57688 | MKSYLKALVFAVLFLFILGFVYPTVTSLITEHALPFQSEGQPVEIDGHIYGSYLLAEAFNSSFFFHPRPSAIDYNLSESGSYDYSLGNPAMLNLTEKYLHRFLSENPGVNISEIPYAMISYSGSGLDPGIPLQGAIIQIPRISIAIHNITNLSVSDLYSYLYNLVNSTKTQNFPFFGSYYVNVVRLNVDIVEFLLKGGYISQSQI | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
B3EAQ1 | MKDIKPAILLFIMFTIICGGIYPALVTGIAHALFPDQAKGSLIIDKAGKELGSNLIGQPFSAPQYLWPRPSVTAEFGYNPSASGGSNSGQTNPDYLKTVAERVKTLRESGMTGLIPTELAQASASGLDPHLSPQAARLQAARIAKARGIPETAVQKLINENTAGPQLGILGAARVNVLAVNLKLDTLTR | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
Q8PPC8 | MPLRDDGVLRGSLVLAVFTLFGLGLAYSLIATGITGALFSEQATGSLMRVDARVVGSALVAQPFTDARYFQPRPSAAKYDLTAAAGSNQARSNPDLLARIATTRAQVAARDGIAPEAVPGELLTQSGSGLDPHLSPAGAQVQIRRVAAARGWPEQRVAALVQATTEAAPQFGLLGQPRVNVLALNLALDQAGNGESGRGNGVKQAH | Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the... |
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