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F4K2M8 | MPTGCEFPMIKTFENALTAADFESTVELTNFPAVFRGCASVWDAYSKWNPFNSGLDYLEERAGSVEVEAMLSRTAPVFNGDIRSHERVSLPFSDFIRFCKQHMRGKGNGSGVDAKSADLNPMCEDYRPGQIYLAQFPILNDEKEEKVLLKILRQDIQTPTFLDAKSLSSINFWMNSAEARSSTHYDPHHNLLCVVSGRKKVVLWPPSASPSLYPMPIYGEASNHSSVGLENPNLSDYPRAEHSLKQSQEITLNAGDAVFIPEGWFHQVDSDELTVAVNFWWQSNYMSNMPEHMDSYYLRRITRSLLVSKPSSTDLRHLSEHIDQSRIEMAEGGNDNIGNESIKKGLSTLHEKASLHDLDPSASQALHDLISLVHDHVNAVDTSKGLQHTSPSCSEGGEKSKFLVNAMSCLEDDRVAHLLWNLEASRLRDVLLAMALELSYLKLLVKMEIFVLVLHKIFETLEALILHMLSPIAAEVLTQKFDEIDQQTGEEDRTQFFREFYSAFDDEAAAMDIILSRKEAFAFQVCSLASLCRLRTYHKLKGEKFSASY | 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 | MAKEIENLWREVRELSLGTKIDRFDSQPSPVKFLRNYVSQSKPCVISKAITHWPALKLWSDPAYLTGALSDDVVSLHLTPNGCADAVTGDSDLCFASAHVEKVLFPEALKVVQSSCKGLKVGYLQQQNDCFRTEYSTVALDCDGDIEWATEAFGCSPEAVNLWIGTDDSVTSFHKDHYENLYAVVSGEKHFLLLPPTDVHRLYIEQYPAANYSYHRDTDAFKLEVEEPVRHVPWSSVDPYPSPEKEASERLKFPLFFDGPKPFHCTVKAGEVLYLPSMWFHHVSQTPGDGGYTIAVNYWYDMQFDIKYAYFNFLQSLLYKSSSLNPVLSWREDEDSESSDAEIAP | 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 LOCUS C (FLC) locus by removing the repressive histone modification H3 lysine 27 trimethylation (H3K27me3), especially at elevated temperatures (e.g. 29 degrees Celsius), thus preventing extreme precocious flowering . JMJ30 and JMJ32 are regulators involved in the integration of abscisic acid (ABA) and brassinosteroids (BR) signaling pathways . Together with JMJ30, controls ABA-mediated growth arrest during the post-germination stage in unfavorable conditions, and responses to ABA during root development, via the removal of repressive histone mark (H3K27me3) from the SnRK2.8 promoter, thus promoting SnRK2.8 expression and subsequent kinase-dependent ABI3 activation . In addition, removes the repressive histone marks (H3K27me3) from the BZR1 locus in response to stress and ABA, thus activating the BR signaling pathway which, in turn, inhibits the ABA signaling pathway .
Catalytic Activity: 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3] + succinate
Sequence Mass (Da): 39123
Sequence Length: 345
Subcellular Location: Nucleus
EC: 1.14.11.68
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Q08BY5 | MDRETFHSCSSLVKLPRQIHQQHCSSHFIEYIEREIPYSKFFKNYLIPNQPCMFSKKFTEEWNCRKKWVTAEGKPNLQRLLHEFDETPVPVANCSVKEYNANPKQIMPFKEFIQYWRESIQNGHSSPKGCLYLKDWHMQRNFPEHNIYKTPIYFSSDWLNEYWDTIEVDDYRFVYMGPKGSWTPFHADVFRSYSWSANICGRKKWLLYPPGQEDFLRDCHGNLAYDVTAPILQDKGLYAQFEEACQPLEIIQEAGEIIFVPSGWHHQVYNLEDTISINHNWLNGCNLDIMWQFLQDELSSVQREIEEWRDTMDTWHQHCQVIMKSCTGIDYAEFASFLKTIANNRISFLNSSPRNADSCQDLLAESLCALGPHHAAFDLQRVLHIFEIMLNNEDFKRLDPATLSFKPEDLLQEIREAIRTIV | 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: 422
Subcellular Location: Cytoplasm
EC: 1.14.11.-
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Q9VJ97 | MASEERDGDVLLQLHPEEVVETDPQLPEEIERCSGLDYNDFFWRYMHKNIPVIIANVSNDWECQNWTVGQSSPESRDLNSNPSASSINFDYLKTKISDGPVPVANCNSSYFNSHTKLELNFHDYLAKWRSSIESQSSAAWTSAEVNSNVAPASGDNLYLKDWHLAAQMPGYNFYKVPKYFASDWLNEQLIQQGKDDYRFVYMGPKNSWTSYHADVFGSFSWSTNIVGLKKWLIMPPGEELKLNDRLGNLPFSIDEKMLDEHNVRYYTINQRANEAVFVPSGWFHQVWNLTDTISVNHNWFNGCNISMVWQNLKNNLKAVCNEISDCQQMDNFEAHCQTMLRASFGINYLDFIELLEFIAARRLAEGTVATKFLLFDSYTMNDYHVQYDLECLWKITRTLTEDPTIQCSPLQLEDRCQGLLARLEF | 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 | MRAGPEPQALAGQKRGALRLLVPRLVLTVSAPAEVRRRVLRPVLSWMDRETRALADSHFRGLGVDVPGVGQAPGRVAFVSEPGAFSYADFVRGFLLPNLPCVFSSAFTQGWGSRRRWVTPAGRPDFDHLLRTYGDVVVPVANCGVQEYNSNPKEHMTLRDYITYWKEYIQAGYSSPRGCLYLKDWHLCRDFPVEDVFTLPVYFSSDWLNEFWDALDVDDYRFVYAGPAGSWSPFHADIFRSFSWSVNVCGRKKWLLFPPGQEEALRDRHGNLPYDVTSPALCDTHLHPRNQLAGPPLEITQEAGEMVFVPSGWHHQVHNLDDTISINHNWVNGFNLANMWRFLQQELCAVQEEVSEWRDSMPDWHHHCQVIMRSCSGINFEEFYHFLKVIAEKRLLVLREAAAEDGAGLGFEQAAFDVGRITEVLASLVAHPDFQRVDTSAFSPQPKELLQQLREAVDAAAAP | 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: 463
Subcellular Location: Cytoplasm
EC: 1.14.11.-
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Q8BFT6 | MDRETRTFAERYYRDLRDPVPSGGGGPTPSGVTFIQTPNAFSYADFVKGFLLPNLPCVFSSAFTEGWGSRRRWVTSEGKPDFEYLQQKYGDAVVPVANCGVREYNSNPKEHMSFRDYISYWKDYIQGSYSSSRGCLYLKDWHLCRDSLVNDLEDIFTLPVYFSSDWLNEFWDVLNVDDYRFVYAGPRGTWSPFHADIFRSFSWSVNICGKKKWLFFPPGEEEALRDCHGNLPYDVTSTELLDTHLYPKIQHHSLPIEVIQEPGEMVFVPSGWHHQVYNLDDTISINHNWVNGCNLPNMWHFLQQELQAVQHEVEEWKDSMPDWHHHCQVIMKSCTGINFEEFYHFLKVIAEKRLLVLEQGLKGDSGDSRSLDLGLQQAAFDIGRLADVLASVVVNPDFQRVDTSAFSPQPEELLQQLEDAVAAAEAL | 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-oxoglutarate + L-lysyl-[protein] + O2 = 4-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 49152
Sequence Length: 427
Subcellular Location: Cytoplasm
EC: 1.14.11.-
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Q58DS6 | MNHKSKKRIREAKRSARPELKDSLDWTRHNYFESFPLNPAAVADNVERADALQLSVEEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTREEGGNQQDEAITWFNIIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEHPELAVLADSVDLQESTGIASDSSSDSSSSSSSSSSDSDSECESGSEGEGTMHRRKKRRTCGMVGNGDTTSQDDCVSKERSSSR | 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-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for homooligomerization (By similarity). Plays a role in the regulation of nucleolar liquid-liquid phase separation (LLPS) by post-translationally modifying LIAT1 at its lysine-rich domain which inhibits LIAT1 nucleolar targeting (By similarity). In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation. Demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), including mono-, symmetric di- and asymmetric dimethylated forms, thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. In collaboration with BRD4, interacts with the positive transcription elongation factor b (P-TEFb) complex in its active form to regulate polymerase II promoter-proximal pause release for transcriptional activation of a large cohort of genes. On distal enhancers, so called anti-pause enhancers, demethylates both histone H4R3me2 and the methyl cap of 7SKsnRNA leading to the dismissal of the 7SKsnRNA:HEXIM1 inhibitor complex. After removal of repressive marks, the complex BRD4:JMJD6 attract and retain the P-TEFb complex on chromatin, leading to its activation, promoter-proximal polymerase II pause release, and transcriptional activation. Demethylates other arginine methylated-proteins such as ESR1. Has no histone lysine demethylase activity (By similarity). Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65 (By similarity). Seems to be necessary for the regulation of macrophage cytokine responses (By similarity).
PTM: Hydroxylates its own N-terminus; hydroxylation is required for homooligomerization.
Catalytic Activity: 2-oxoglutarate + L-lysyl-[protein] + O2 = (5S)-5-hydroxy-L-lysyl-[protein] + CO2 + succinate
Sequence Mass (Da): 46527
Sequence Length: 403
Domain: The nuclear localization signal motifs are necessary and sufficient to target it into the nucleus.
Subcellular Location: Nucleus
EC: 1.14.11.-
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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). Since C-terminal Cys residues are prone to racemization during solid-phase peptide synthesis, and if the presence of a D-amino acid is correct, it is probable that OspTx2a-p1 (L-Cys-76 form) corresponds to the native peptide.
Sequence Mass (Da): 8711
Sequence Length: 79
Subcellular Location: Secreted
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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 activation of survival signaling pathways.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 31162
Sequence Length: 279
Subcellular Location: Host membrane
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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.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 27580
Sequence Length: 249
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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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.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24400
Sequence Length: 222
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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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.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 29289
Sequence Length: 269
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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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 a key role in hematopoiesis.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 26616
Sequence Length: 241
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Subcellular Location: Mitochondrion intermembrane space
EC: 2.7.4.3
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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.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 30985
Sequence Length: 276
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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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 central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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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 central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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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 central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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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 central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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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: Cytoplasm
EC: 2.7.4.3
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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 central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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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 | MIALGIEGTAWSLSIGVVDEEGVIALENDPYIPKEGGIHPREASQHHSERLPSLLSRVFEKVDKNSIDVVAFSQGPGMGPCLRVVATAARLLAIKLEKPLVGVNHCLAHVEVGRWQTGARKPVSLYVSGGNSQVIARRGNRYRVFGETLDIGIGNALDKLARHMGLKHPGGPKIEELAKKGQKYHFLPYVVKGMDFSFSGMVTAAQRLFDSGVRMEDVAFSFQETAFAMLTEVTERALAYLDLNEVLLVGGVAANKRLQEMLRIMCEDRGAKFYVPPKELAGDNGAMIAYTGLLMYKHGHQTPVEKSYVRPDFRIEDVEVNWD | 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 threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 35604
Sequence Length: 323
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q4WDE9 | MIAIGLEGSANKLGVGIMLHPEDGSTPRVLANIRHTYVSPPGEGFLPKDTARHHRSWVVKLVKRALREARISVRDVDCICFTKGPGMGAPLQSVAVAARMLSLLWGKELVGVNHCVGHIEMGRLITGSTNPVVLYVSGGNTQVIAYSSQRYRIFGETLDIAVGNCLDRFARTLHISNDPAPGYNIEQLAKKGKQLVDLPYTVKGMDCSFSGILAAIDGLAASYGLNGEEKEEEGAGDDSKPTRADLCFSLQETVFSMLVEITERAMAHVGSKEVLIVGGVGCNERLQEMMGIMARDRGGSVHATDERFCIDNGIMIAQAGLLAYKTGFRTPLKESTCTQRFRTDDVFVKWRD | 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 threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 38273
Sequence Length: 352
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q5A6A4 | MVVDLDKYLKPGKDHYLALGLEGSANKLGVGVIKHNKGPLSSTNRAEVLSNIRDTYITPPGEGFLPRDTARHHRNWVVRIIKQALATAKIAGKDIDVICFTQGPGMGAPLQSVVIAARTLAQLWNIPIVGVNHCVGHIEMGREITGAENPVVLYVSGGNTQVIAYSKQRYRIFGETLDIAIGNCLDRFARTLKIPNEPAPGYNIEQMAKKGKHLVPLPYTVKGMDLSMSGILAAIDSIAKEMFGKQQKKLIDEESGEPITAEDLCFSLQETLFSMLVEITERALAHVDSNQVLIVGGVGSNQRLQEMMKLMIQDRKNGQIYATDERFCIDNGIMIAHAGLLSYRTGQTNQLNNTVCTQRFRTDEVFVKWRDD | 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 threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. KAE1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 41103
Sequence Length: 372
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q8SQQ3 | MIAMGLEGSANKLGVGIMRDDEILANERLTYAPPPGEGFIPVKTAEHHRSRILGLVAVSLEKAGVDLDDVDIFCYTKGPGMGLPLSVVATVARTLSLYCNKPLVPVNHCIAHIEMGRFITKASNPVILYASGGNTQIIAYHNRRYKIFGETLDIAVGNCIDRFARALKLPNFPAPGLSVERYAKLGKNYIELPYVVKGMDVSFSGILSNIKRKIAEDEQVKRDLCYSLQETVFSALVEVTERAMAFSSSKEVLIVGGVGCNLRLQEMMGIMARERGGVCYATDERFCIDNGVMIAYVGMLMAKSGAAFKLGECFVTQRYRTDSVEVTWRDY | 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 threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. KAE1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 36400
Sequence Length: 331
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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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 membrane
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P31321 | MASPPACPSEEDESLKGCELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEENRQILARQKSNSQSDSHDEEVSPTPPNPVVKARRRRGGVSAEVYTEEDAVSYVRKVIPKDYKTMTALAKAISKNVLFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGEWVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRYNSFISLTV | 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 membrane
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P00515 | MSHIQIPPGLTELLQGYTVEVLRQRPPDLVDFAVDYFTRLREARSRASTPPAAPPSGSQDFDPGAGLVADAVADSESEDEEDLDVPIPGRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDPEQLSQVLDAMFERTVKVDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKVYKDGERIITQGEKADSFYIIESGEVSILIKSKTKVNKDGENQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSMDLIDPGQ | 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
Sequence Length: 401
Subcellular Location: Cytoplasm
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P13861 | MSHIQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARAPASVLPAATPRQSLGHPPPEPGPDRVADAKGDSESEEDEDLEVPVPSRFNRRVSVCAETYNPDEEEEDTDPRVIHPKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERIVKADEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKIYKDGERIITQGEKADSFYIIESGEVSILIRSRTKSNKDGGNQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSVDLGNLGQ | 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
Subcellular Location: Cytoplasm
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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
Subcellular Location: Cytoplasm
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P12368 | MSHIQIPPGLTELLQGYTVEVLRQQPPDLVDFAVEYFTRLREARRQESDSFIAPPTTFHAQESSGVPVIEEDGESESDSDDEDLEVPIPSKFTRRVSVCAETFNPDEEEDNDPRVVHPKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFEKIVKTDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIVATSDGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLFKSLEMSERMKIVDVIGEKIYKDGERIITQGEKADSFYIIESGEVSILIRSKTKTNKNGGNQEVEIAHCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSNLDLLDPGQ | 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
Subcellular Location: Cytoplasm
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P31322 | MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQEENERKGTARFGHEGRTWGDAGAAGGGGTPSKGVNFAEEPRHSDSENGEEEEEEAADAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKEGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEVSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEENGAVEIARCSRGQYFGELALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA | 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
Subcellular Location: Cytoplasm
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P31323 | MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGTARFGHEGRTWGDLGAAAGGGTPSKGVNFAEEPMQSDSEDGEEEEAAPADAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEENGAVEIARCSRGQYFGELALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA | 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
Subcellular Location: Cytoplasm
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P31324 | MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGAARFGHEGRTWGDAGAAAGGGIPSKGVNFAEEPMRSDSENGEEEEAAEAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKEGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEVSERLKVVDVIGTKVYNDGEQIIAQGDLADSFFIVESGEVKITMKRKGKSEVEENGAVEIARCFRGQYFGELALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA | 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
Subcellular Location: Cytoplasm
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A4QUT2 | MHASLSSWLLAASLLTQPISVSGQGCPFAKRDGTVDSSLPQKRADAPETTTFGRCAVKSNQAGGGTRSHDWWPCQLRLDVLRQFQPSQNPLGGDFDYAEAFQSLDYEAVKKDIAALMTESQDWWPADFGNYGGLFVRMAWHSAGTYRAMDGRGGGGMGQQRFAPLNSWPDNQNLDKARRLIWPIKQKYGNKISWADLMLLTGNVALENMGFKTLGFGGGRADTWQSDEAVYWGAETTFVPQGNDVRYNNSVDINARADKLEKPLAATHMGLIYVNPEGPNGTPDPAASAKDIREAFGRMGMNDTETVALIAGGHAFGKTHGAVKGSNIGPAPEAADLGMQGLGWHNSVGDGNGPNQMTSGLEVIWTKTPTKWSNGYLESLINNNWTLVESPAGAHQWEAVNGTVDYPDPFDKTKFRKATMLTSDLALINDPEYLKISQRWLEHPEELADAFAKAWFKLLHRDLGPTTRYLGPEVPKESFIWQDPLPAREGDLIDDADVDKLKAAILSTDGLDVSKLASTAMACATTYRNSDKRGGCNGARIALEPQRNWVSNNPTQLSAVLDALKKVQSDFNGSNGNKKVSLADLIVLGGTAAVEKAAKDAGVDIKVPFSAGRVDATQEQTDVTQFSYLEPQADGFRNYGRGTARARTEEIMVDKASQLTLTPPELTVLVGGMRALGANYDGSDVGVFTANKGKLTPDFFVNLVDMNIAWTASGADGESWVGTDRKSRSEKYKGSRADLVFGSHAELRAIAEVYAENGNQEKFVKDFVAAWTKVMNLDRFDLKVKK | 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 stage of plant infection.
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 + H2O2 = A + 2 H2O
Sequence Mass (Da): 85587
Sequence Length: 786
Subcellular Location: Secreted
EC: 1.11.1.21
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A0QXX7 | MSSDTSDSRPPNPDTKTASTSESENPAIPSPKPKSGAPLRNQDWWPNQIDVSRLHPHPPQGNPLGEDFDYAEEFAKLDVNALKADLTALMTQSQDWWPADYGHYGGLFIRMSWHSAGTYRIHDGRGGGGQGAQRFAPINSWPDNVSLDKARRLLWPIKQKYGNKISWADLLVFTGNVALESMGFKTFGFGFGREDIWEPEEILFGEEDEWLGTDKRYGGGEQRQLAEPYGATTMGLIYVNPEGPEGQPDPLAAAHDIRETFGRMAMNDEETAALIVGGHTFGKTHGAGDASLVGPEPEAAPIEQQGLGWKSSYGTGKGPDTITSGLEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQFTAKDGAGAGTIPDPFGGPGRNPTMLVTDISMRVDPIYGKITRRWLDHPEELSEAFAKAWYKLLHRDMGPISRYLGPWVAEPQLWQDPVPAVDHPLVDDQDIAALKSTVLDSGLSTGQLIKTAWASAASYRNTDKRGGANGARVRLEPQKNWDVNEPAELATVLPVLERIQQDFNASASGGKKVSLADLIVLAGSAAIEKAAKDGGYNVTVPFAPGRTDASQENTDVESFAVLEPRADGFRNYVRPGEKVQLEKMLLERAYFLGVTAPQLTALVGGLRALDVNHGGTKHGVFTDRPGALTNDFFVNLLDMGTEWKTSETTENVYEGVDRKTGQLKWTATANDLVFGSHSVLRAVAEVYAQSDNGERFVNDFVKAWVKVMNNDRFDLK | 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 the peroxidase activity of the enzyme.
Catalytic Activity: AH2 + H2O2 = A + 2 H2O
Sequence Mass (Da): 81998
Sequence Length: 748
EC: 1.11.1.21
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A6T9H9 | MSTSNDPSNNASAGKCPFHAETPKQSAGSGTANRDWWPNQLRVDLLNQHSNRSNPLGENFNYREEFKKLDYSALKADLRALLTDSQEWWPADWGSYIGLFIRMAWHGAGTYRTVDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPVKQKYGQKISWADLYMLAGNVALENAGFRTFGFGAGREDVWEPDLDVDWGDEKEWLAHRHPESLAKQAIGATEMGLIYVNPEGPNASGEPLSAAAAIRATFGNMAMDDEEIVALIAGGHTLGKTHGAAETSHVGAEPEAAPLEAQGLGWHSSYGSGAGADAITSGLEVVWTQTPTQWSNYFFENLFKYEWVQTRSPAGAIQFEAKDAPEIIPDPFNPEKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKSRYLGPEVPKEDLIWQDPLPAATHQPSAEDIASLKTAIAGAGLSVSELVSVAWASASTFRGGDKRGGANGARLALAPQKDWPVNAIASRVLPTLQAIQRASGKASLADIIVLAGVVGVEQAAAAAGVSVNVPFTPGRVDALPEQTDVESFDLLQPLADGFRNYRRIEGGVSTETLLIDKAQQLTLTAPEMTVLVGGLRVLGANYDGSKHGVFTDRVGVLSNDFFVNLLDMATVWKAADDNAELFTGSDRKTGEAKYSATRVDLVFGSNSVLRALAEVYACADGQQKLVHDFVAAWTKVMNLDRFDL | 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 + H2O2 = A + 2 H2O
Sequence Mass (Da): 78966
Sequence Length: 725
EC: 1.11.1.21
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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 beta-sheet by disulfide bonds (CSalpha/beta).
Subcellular Location: Secreted
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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 TP53 and RB1.
PTM: Sumoylated.
Sequence Mass (Da): 31574
Sequence Length: 286
Pathway: Protein modification; protein sumoylation.
EC: 2.3.2.-
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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: 2.7.11.1
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P23291 | MSMPIASTTLAVNNLTNINGNANFNVQANKQLHHQAVDSPARSSMTATTAANSNSNSSRDDSTIVGLHYKIGKKIGEGSFGVLFEGTNMINGVPVAIKFEPRKTEAPQLRDEYKTYKILNGTPNIPYAYYFGQEGLHNILVIDLLGPSLEDLFDWCGRKFSVKTVVQVAVQMITLIEDLHAHDLIYRDIKPDNFLIGRPGQPDANNIHLIDFGMAKQYRDPKTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDMEALGHVFFYFLRGHLPWQGLKAPNNKQKYEKIGEKKRSTNVYDLAQGLPVQFGRYLEIVRSLSFEECPDYEGYRKLLLSVLDDLGETADGQYDWMKLNDGRGWDLNINKKPNLHGYGHPNPPNEKSRKHRNKQLQMQQLQMQQLQQQQQQQQYAQKTEADMRNSQYKPKLDPTSYEAYQHQTQQKYLQEQQKRQQQQKLQEQQLQEQQLQQQQQQQQQLRATGQPPSQPQAQTQSQQFGARYQPQQQPSAALRTPEQHPNDDNSSLAASHKGFFQKLGCC | 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 Length: 538
Subcellular Location: Cell membrane
EC: 2.7.11.1
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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: 2.7.11.1
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P23292 | MSQVQSPLTATNSGLAVNNNTMNSQMPNRSNVRLVNGTLPPSLHVSSNLNHNTGNSSASYSGSQSRDDSTIVGLHYKIGKKIGEGSFGVLFEGTNMINGLPVAIKFEPRKTEAPQLKDEYRTYKILAGTPGIPQEYYFGQEGLHNILVIDLLGPSLEDLFDWCGRRFSVKTVVQVAVQMITLIEDLHAHDLIYRDIKPDNFLIGRPGQPDANKVHLIDFGMAKQYRDPKTKQHIPYREKKSLSGTARYMSINTHLGREQSRRDDMEAMGHVFFYFLRGQLPWQGLKAPNNKQKYEKIGEKKRLTNVYDLAQGLPIQFGRYLEIVRNLSFEETPDYEGYRMLLLSVLDDLGETADGQYDWMKLNGGRGWDLSINKKPNLHGYGHPNPPNEKSKRHRSKNHQYSSPDHHHHYNQQQQQQQAQAQAQAQAQAKVQQQQLQQAQAQQQANRYQLQPDDSHYDEEREASKLDPTSYEAYQQQTQQKYAQQQQKQMQQKSKQFANTGANGQTNKYPYNAQPTANDEQNAKNAAQDRNSNKSSKGFFSKLGCC | 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(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 62079
Sequence Length: 546
Subcellular Location: Cell membrane
EC: 2.7.11.1
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P39962 | MSQRSSQHIVGIHYAVGPKIGEGSFGVIFEGENILHSCQAQTGSKRDSSIIMANEPVAIKFEPRHSDAPQLRDEFRAYRILNGCVGIPHAYYFGQEGMHNILIIDLLGPSLEDLFEWCGRKFSVKTTCMVAKQMIDRVRAIHDHDLIYRDIKPDNFLISQYQRISPEGKVIKSCASSSNNDPNLIYMVDFGMAKQYRDPRTKQHIPYRERKSLSGTARYMSINTHFGREQSRRDDLESLGHVFFYFLRGSLPWQGLKAPNNKLKYEKIGMTKQKLNPDDLLLNNAIPYQFATYLKYARSLKFDEDPDYDYLISLMDDALRLNDLKDDGHYDWMDLNGGKGWNIKINRRANLHGYGNPNPRVNGNTARNNVNTNSKTRNTTPVATPKQQAQNSYNKDNSKSRISSNPQSFTKQQHVLKKIEPNSKYIPETHSNLQRPIKSQSQTYDSISHTQNSPFVPYSSSKANPKRSNNEHNLPNHYTNLANKNINYQSQRNYEQENDAYSDDENDTFCSKIYKYCCCCFCCC | 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 (Tyr-Xaa-Xaa-Zaa, where Zaa is a hydrophobic residue) motif mediates the targeting to the lysosomal compartments.
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9JM63 | MTSVAKVYYSQTTQTESRPLVAPGIRRRRVLTKDGRSNVRMEHIADKRFLYLKDLWTTFIDMQWRYKLLLFSATFAGTWFLFGVVWYLVAVAHGDLLELGPPANHTPCVVQVHTLTGAFLFSLESQTTIGYGFRYISEECPLAIVLLIAQLVLTTILEIFITGTFLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANMRKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDTASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVLILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSASGKYIADFSLFDQVVKVASPSGLRDSTVRYGDPEKLKLEESLREQAEKEGSALSVRISNV | 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 external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42432
Sequence Length: 379
Subcellular Location: Membrane
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Q14654 | MLSRKGIIPEEYVLTRLAEDPAKPRYRARQRRARFVSKKGNCNVAHKNIREQGRFLQDVFTTLVDLKWPHTLLIFTMSFLCSWLLFAMAWWLIAFAHGDLAPSEGTAEPCVTSIHSFSSAFLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAETLIFSKHAVIALRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPMENGVGGNSIFLVAPLIIYHVIDANSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQARTSYLADEILWGQRFVPIVAEEDGRYSVDYSKFGNTVKVPTPLCTARQLDEDHSLLEALTLASARGPLRKRSVPMAKAKPKFSISPDSLS | 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 voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium (By similarity). Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation.
PTM: Phosphorylation by MAPK1 results in changes in channel gating that destabilize the closed states and reduce the ATP sensitivity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43526
Sequence Length: 390
Subcellular Location: Membrane
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Q61743 | MLSRKGIIPEEYVLTRLAEDPAEPRYRTRERRARFVSKKGNCNVAHKNIREQGRFLQDVFTTLVDLKWPHTLLIFTMSFLCSWLLFAMVWWLIAFAHGDLAPGEGTNVPCVTSIHSFSSAFLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAETLIFSKHAVITLRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPMENGVGGNGIFLVAPLIIYHVIDSNSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQARTSYLADEILWGQRFVPIVAEEDGRYSVDYSKFGNTIKVPTPLCTARQLDEDRSLLDALTLASSRGPLRKRSVAVAKAKPKFSISPDSLS | 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 voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium. Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation (By similarity).
PTM: Phosphorylation by MAPK1 results in changes in channel gating that destabilize the closed states and reduce the ATP sensitivity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43562
Sequence Length: 390
Subcellular Location: Membrane
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F1NHE9 | MTAGRVNPYSIVSSEEDGLRLTTMPGINGFGNGKIHTRRKCRNRFVKKNGQCNVEFTNMDDKPQRYIADMFTTCVDIRWRYMLLLFSLAFLVSWLLFGLIFWLIALIHGDLENPGGDDTFKPCVLQVNGFVAAFLFSIETQTTIGYGFRCVTEECPLAVFMVVVQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVAMRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRITEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEINEDSPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLASEILWGHRFEPVLFEEKNQYKVDYSHFHKTYEVPSTPRCSAKDLVENKFLLPSTNSFCYENELAFMSRDEDEEDDDSRGLDDLSPDNRHEFDRLQATIALDQRSYRRESEI | 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 into the cell rather than out of it. The inward rectification is probably due to the blockage of outward current by cytoplasmic polyamines and/or magnesium ions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49083
Sequence Length: 429
Domain: Phosphatidylinositol 4,5-bisphosphate binding to the cytoplasmic side of the channel triggers a conformation change leading to channel opening.
Subcellular Location: Membrane
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Q14500 | MTAASRANPYSIVSSEEDGLHLVTMSGANGFGNGKVHTRRRCRNRFVKKNGQCNIEFANMDEKSQRYLADMFTTCVDIRWRYMLLIFSLAFLASWLLFGIIFWVIAVAHGDLEPAEGRGRTPCVMQVHGFMAAFLFSIETQTTIGYGLRCVTEECPVAVFMVVAQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVALRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRVTEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEIDEASPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLANEILWGHRFEPVLFEEKNQYKIDYSHFHKTYEVPSTPRCSAKDLVENKFLLPSANSFCYENELAFLSRDEEDEADGDQDGRSRDGLSPQARHDFDRLQAGGGVLEQRPYRRESEI | 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 tissues. 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 more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49001
Sequence Length: 433
Domain: Phosphatidylinositol 4,5-bisphosphate binding to the cytoplasmic side of the channel triggers a conformation change leading to channel opening.
Subcellular Location: Membrane
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O60928 | MDSSNCKVIAPLLSQRYRRMVTKDGHSTLQMDGAQRGLAYLRDAWGILMDMRWRWMMLVFSASFVVHWLVFAVLWYVLAEMNGDLELDHDAPPENHTICVKYITSFTAAFSFSLETQLTIGYGTMFPSGDCPSAIALLAIQMLLGLMLEAFITGAFVAKIARPKNRAFSIRFTDTAVVAHMDGKPNLIFQVANTRPSPLTSVRVSAVLYQERENGKLYQTSVDFHLDGISSDECPFFIFPLTYYHSITPSSPLATLLQHENPSHFELVVFLSAMQEGTGEICQRRTSYLPSEIMLHHCFASLLTRGSKGEYQIKMENFDKTVPEFPTPLVSKSPNRTDLDIHINGQSIDNFQISETGLTE | 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 more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ13 has a very low single channel conductance, low sensitivity to block by external barium and cesium, and no dependence of its inward rectification properties on the internal blocking particle magnesium.
PTM: Phosphorylation at Ser-201 by PKC strongly inhibits ionic currents, while phosphorylation at Ser-287 by PKA increases them.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40530
Sequence Length: 360
Subcellular Location: Membrane
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Q9UNX9 | MGLARALRRLSGALDSGDSRAGDEEEAGPGLCRNGWAPAPVQSPVGRRRGRFVKKDGHCNVRFVNLGGQGARYLSDLFTTCVDVRWRWMCLLFSCSFLASWLLFGLAFWLIASLHGDLAAPPPPAPCFSHVASFLAAFLFALETQTSIGYGVRSVTEECPAAVAAVVLQCIAGCVLDAFVVGAVMAKMAKPKKRNETLVFSENAVVALRDHRLCLMWRVGNLRRSHLVEAHVRAQLLQPRVTPEGEYIPLDHQDVDVGFDGGTDRIFLVSPITIVHEIDSASPLYELGRAELARADFELVVILEGMVEATAMTTQCRSSYLPGELLWGHRFEPVLFQRGSQYEVDYRHFHRTYEVPGTPVCSAKELDERAEQASHSLKSSFPGSLTAFCYENELALSCCQEEDEDDETEEGNGVETEDGAASPRVLTPTLALTLPP | 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 more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ14 gives rise to low-conductance channels with a low affinity to the channel blockers Barium and Cesium (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47846
Sequence Length: 436
Subcellular Location: Membrane
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E1BNE9 | MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQGPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQSEQFEIVVILEGIVETTGMTCQARTSYTEDEVLWGHRFFPVISLEEGFFKVDYSQFHATFEVPTPPYSVKEQEEMLLMSSPLIAPAITNSKERHNSVECLDGLDDISTKLPSKLQKITGREDFPKKLLRMSSTTSEKAYSLGDLPMKLQRISSVPGNSEEKLVSKTTKMLSDPMSQSVADLPPKLQKMAGGATRMEGNLPAKLRKMNSDRFT | 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, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56547
Sequence Length: 501
Subcellular Location: Membrane
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P48549 | MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQDPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQTEQFEIVVILEGIVETTGMTCQARTSYTEDEVLWGHRFFPVISLEEGFFKVDYSQFHATFEVPTPPYSVKEQEEMLLMSSPLIAPAITNSKERHNSVECLDGLDDITTKLPSKLQKITGREDFPKKLLRMSSTTSEKAYSLGDLPMKLQRISSVPGNSEEKLVSKTTKMLSDPMSQSVADLPPKLQKMAGGAARMEGNLPAKLRKMNSDRFT | 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, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56603
Sequence Length: 501
Subcellular Location: Membrane
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P63250 | MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQGPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQTEQFEVVVILEGIVETTGMTCQARTSYTEDEVLWGHRFFPVISLEEGFFKVDYSQFHATFEVPTPPYSVKEQEEMLLMSSPLIAPAITNSKERHNSVECLDGLDDISTKLPSKLQKITGREDFPKKLLRMSSTTSEKAYSLGDLPMKLQRISSVPGNSEEKLVSKTTKMLSDPMSQSVADLPPKLQKMAGGPTRMEGNLPAKLRKMNSDRFT | 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, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56573
Sequence Length: 501
Subcellular Location: Membrane
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P48050 | MHGHSRNGQAHVPRRKRRNRFVKKNGQCNVYFANLSNKSQRYMADIFTTCVDTRWRYMLMIFSAAFLVSWLFFGLLFWCIAFFHGDLEASPGVPAAGGPAAGGGGAAPVAPKPCIMHVNGFLGAFLFSVETQTTIGYGFRCVTEECPLAVIAVVVQSIVGCVIDSFMIGTIMAKMARPKKRAQTLLFSHHAVISVRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPYMTQEGEYLPLDQRDLNVGYDIGLDRIFLVSPIIIVHEIDEDSPLYGMGKEELESEDFEIVVILEGMVEATAMTTQARSSYLASEILWGHRFEPVVFEEKSHYKVDYSRFHKTYEVAGTPCCSARELQESKITVLPAPPPPPSAFCYENELALMSQEEEEMEEEAAAAAAVAAGLGLEAGSKEEAGIIRMLEFGSHLDLERMQASLPLDNISYRRESAI | 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 more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49500
Sequence Length: 445
Domain: The Val/Gly/Ala/Pro stretch may have a functional role in the conductance or permeation properties.
Subcellular Location: Cell membrane
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P48051 | MAKLTESMTNVLEGDSMDQDVESPVAIHQPKLPKQARDDLPRHISRDRTKRKIQRYVRKDGKCNVHHGNVRETYRYLTDIFTTLVDLKWRFNLLIFVMVYTVTWLFFGMIWWLIAYIRGDMDHIEDPSWTPCVTNLNGFVSAFLFSIETETTIGYGYRVITDKCPEGIILLLIQSVLGSIVNAFMVGCMFVKISQPKKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAKLIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKEELEIVVILEGMVEATGMTCQARSSYITSEILWGYRFTPVLTLEDGFYEVDYNSFHETYETSTPSLSAKELAELASRAELPLSWSVSSKLNQHAELETEEEEKNLEEQTERNGDVANLENESKV | 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 voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48451
Sequence Length: 423
Subcellular Location: Membrane
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P56696 | MAEAPPRRLGLGPPPGDAPRAELVALTAVQSEQGEAGGGGSPRRLGLLGSPLPPGAPLPGPGSGSGSACGQRSSAAHKRYRRLQNWVYNVLERPRGWAFVYHVFIFLLVFSCLVLSVLSTIQEHQELANECLLILEFVMIVVFGLEYIVRVWSAGCCCRYRGWQGRFRFARKPFCVIDFIVFVASVAVIAAGTQGNIFATSALRSMRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFASFLVYLAEKDANSDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRMPAANLIQAAWRLYSTDMSRAYLTATWYYYDSILPSFRELALLFEHVQRARNGGLRPLEVRRAPVPDGAPSRYPPVATCHRPGSTSFCPGESSRMGIKDRIRMGSSQRRTGPSKQHLAPPTMPTSPSSEQVGEATSPTKVQKSWSFNDRTRFRASLRLKPRTSAEDAPSEEVAEEKSYQCELTVDDIMPAVKTVIRSIRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQTRVDQIVGRGPGDRKAREKGDKGPSDAEVVDEISMMGRVVKVEKQVQSIEHKLDLLLGFYSRCLRSGTSASLGAVQVPLFDPDITSDYHSPVDHEDISVSAQTLSISRSVSTNMD | 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 oxotremorine-M strongly suppress KCNQ4 current in CHO cells in which cloned KCNQ4 channels were coexpressed with M1 muscarinic receptors.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77101
Sequence Length: 695
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
Subcellular Location: Basal cell membrane
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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-sensor and is characterized by a series of positively charged amino acids at every third position.
Subcellular Location: Basal cell membrane
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Q9NR82 | MPRHHAGGEEGGAAGLWVKSGAAAAAAGGGRLGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAATLGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFIYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLSAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSVSIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSPSTDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGTDDVYDEKGCQCDVSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQILGKGQITSDKKSREKITAEHETTDDLSMLGRVVKVEKQVQSIESKLDCLLDIYQQVLRKGSASALALASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLSRSTSANISRGLQFILTPNEFSAQTFYALSPTMHSQATQVPISQSDGSAVAATNTIANQINTAPKPAAPTTLQIPPPLPAIKHLPRPETLHPNPAGLQESISDVTTCLVASKENVQVAQSNLTKDRSMRKSFDMGGETLLSVCPMVPKDLGKSLSVQNLIRSTEELNIQLSGSESSGSRGSQDFYPKWRESKLFITDEEVGPEETETDTFDAAPQPAREAAFASDSLRTGRSRSSQSICKAGESTDALSLPHVKLK | 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 excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991. Activated by niflumic acid and the anticonvulsant retigabine. As the native M-channel, the potassium channel composed of KCNQ3 and KCNQ5 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102179
Sequence Length: 932
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
Subcellular Location: Cell membrane
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Q9JK45 | MPRHHAGGEEGGAAGLWVRSGAAAAAGAGGGRPGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAAALGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFVYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLSAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSVSIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSPSTDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGIDDVYDEKGCQCDVSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQILGKGQMTSDKKSREKITAEHETTDDPSMLARVVKVEKQVQSIESKLDCLLDIYQQVLRKGSASALTLASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLTRSASANISRGLQFILTPNEFSAQTFYALSPTMHSQATQVPMSQNDGSSVVATNNIANQISAAPKPAAPTTLQIPPPLSAIKHLSRPEPLLSNPTGLQESISDVTTCLVASKESVQFAQSNLTKDRSLRKSFDMGGETLLSVRPMVPKDLGKSLSVQNLIRSTEELNLQFSGSESSGSRGSQDFYPKWRESKLFITDEEVGAEETETDTFDGTPPPAGEAAFSSDSLRTGRSRSSQNICKTGDSTDALSLPHVKLN | 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 excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102258
Sequence Length: 933
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
Subcellular Location: Cell membrane
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Q96KK3 | MLMLLVRGTHYENLRSKVVLPTPLGGRSTETFVSEFPGPDTGIRWRRSDEALRVNVGGVRRQLSARALARFPGTRLGRLQAAASEEQARRLCDDYDEAAREFYFDRHPGFFLSLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALAACCRARYLERRLTQPHAWDEDSDTPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSISVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSPEGVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLAGVALGDQGGKEFGHLGKVVQVFRLMRIFRVLKLARHSTGLRSLGATLKHSYREVGILLLYLAVGVSVFSGVAYTAEKEEDVGFNTIPACWWWGTVSMTTVGYGDVVPVTVAGKLAASGCILGGILVVALPITIIFNKFSHFYRRQKALEAAVRNSNHQEFEDLLSSIDGVSEASLETSRETSQEGQSADLESQAPSEPPHPQMY | 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
Sequence Mass (Da): 58372
Sequence Length: 526
Domain: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.
Subcellular Location: Cell membrane
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O35173 | MVSEFPGPGSRVPWRPRDEALRVNVGGVRRLLSARALARFPGTRLGRLQAAASEEQARRLCDDYDAAAHEFYFDRHPGFFLGLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALATCCRARYLERRVARPRAWDEDSDAPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSIGVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSAEEVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLAGAALGDQRGASGEELGDLGKVVQVFRLMRIFRVLKLARHSTGLRSLGATLKHSYREVGILLLYLAVGVSVFSGVAYTAEEENEGFHTIPACWWWGTVSMTTVGYGDVVPETVGGKLAASGCILGGILVVALPITIIFNKFSHFYRRQKALEAAVRSSGQREFEDLLSSVDGVSDVSLETSRDTSQEGRSTDLETQAPREPAKSHSY | 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
Sequence Mass (Da): 54918
Sequence Length: 497
Domain: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.
Subcellular Location: Cell membrane
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A7GN34 | MDKRISIAIDGPAAAGKSTVAKVVAKQLSYVYIDTGAMYRTLTYAALEQNIDIENEEKLMEVLQSIRIEFQQGKDTQQVFLNGQDVSEVIRTPDVTNRVSIVAKHRLVREEMVRRQQELAAQGGVVMDGRDIGTHVLPNAEVKIFMLASVEERAERRHLENMRKGFSSNLEQLKKEIAQRDKLDSEREVSPLKKAEDAFELDTTSLSIEEVVRNIMAIVSEALQK | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25386
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q5L9K4 | MKKITIAIDGFSSCGKSTMAKDLAKEIGYIYIDSGAMYRAVTLYSIENGIFHGDTIDTDELKRRIGDIHISFRIDPETGRPNTYLNGVNVENKIRTMEVSSKVSPISALGFVREAMVAQQQEMGKAKGIVMDGRDIGTTVFPDAELKIFVTASAEIRAQRRYDELKAKGQETGFEEILENVKQRDHIDQTREVSPLKKADDALLLDNSHLTIAEQKEWLMAEYQKAIKA | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25649
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q65I08 | MEKKLCIAIDGPAAAGKSTVAKIVARKKSYIYIDTGAMYRAITYLALEKGVDLNDEAALTALLKESAIDLTVSPEGEQKVYIAGEDVTEAIRTDSVSNQVSIVAKYAGIREEMTKRQQQLAEKGGVVMDGRDIGTHVLPNAEVKIFLLASVEERAKRRFEENVKKGYNVNYETLAEEIRRRDKLDSEREISPLKKADDALEIDTTSLTIDEVAEKILQIVDKKAQK | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25048
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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P38493 | MEKKLSIAIDGPAAAGKSTVAKIVAEKKSYIYIDTGAMYRAITYAALQENVDLTDEEKLAELLKRTDIELITTKDGQKVFVNGTDVTEAIRTDEISNQVSIAAKHRSVREEMVKRQQQLGEKGGVVMDGRDIGTHVLPNAEVKIFLLASVEERAKRRYEENVKKGFDVNYETLIEEIARRDKLDSEREVSPLRKAEDALEIDTTSLSIQEVADKILEAVEQKSR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25096
Sequence Length: 224
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q8A626 | MKKITIAIDGFSSCGKSTMAKDLAREVGYIYIDSGAMYRAVTLYSIENGIFNGDVIDTEKLKEAIRDIRITFRPNPETGRPDTYLNGVNVENKIRTMGVSSKVSPISALDFVREAMVAQQQAMGKEKGIVMDGRDIGTTVFPDAELKIFVTATPEIRAQRRFDELKAKGQEGSFEEILENVKQRDYIDQHREVSPLRKADDALLLDNSNLSIEQQKEWLSEQFGKVVKE | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25759
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q83E10 | MNARQKPAPVITIDGPSGSGKGTIAFRIAQTLNWYLLDSGIIYRAIAWAMAHYKVPLEDSAGLARLLKRVQISIENRILGKKAKISCDGHDITLAIRSEECGALASRASALPIVREAVLQYQRDFRQRPGLVADGRDMGTVVFPDAVLKFYFDADSQQRAYRRYKELQDRGINVSLPDIQEDLEERDRRDITRSISPTKPAEDAVIIDTTHLSIEAVFATVMNHVRQRGLANVANEK | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 26459
Sequence Length: 237
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q0KDH7 | MTIVNVIAIDGPTASGKGTVAHKVADAVGFHLLDSGALYRLVALASDRAGIDLADVDALAKIASRLDVKFGPDRVWLQGEEVSLAIRAEAIGNRASAIAVHQPVRDALTQLQRSFRKLPGLVADGRDMGTVIFPDAPLKVFLTASVEARARRRYKQLIDKGISANIEDLLRDLEARDVRDRTRTAAPLRPAEDAKLLDTSDMTVDQAVAQVLEWFAAVRPDA | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 23969
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q6A8F7 | MSTSPLVIAIDGPSGSGKSSTSRGVANRLGLARLDTGSMYRAVACRVAHLGIDPTTNPRDAIKVAQSCHLEIDTSAIDDRVVIDGEDVTKEIRDPQTSAKVSAVATIQPVRDALTARMRQVAADRGRIVMEGRDITTVVCPDAQVRVLLVADPAIRVARRQAELGEKVDMAQVIDSIVRRDRDDSTVSTFEEPAEGVTVVDSTHLNLDQVIDAVIDLVPVTLR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 23916
Sequence Length: 223
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q11YY6 | MKKIIVAIDGYSACGKSTTAKILAAKLGYVYIDTGAMYRSVALYFIQHYINSTNPKAVAEALNQIHISFVHNNKTETCETYLNGLNVESEIRKMYVSEKVSEVSAIPEVRKRMVELQQKMARKRGVVMDGRDIGTHVFPDAELKIFMVADMHVRAFRRQQELFERKQIIDLDDIIKNIESRDLMDTTREESPLRKASDAYEIDTTYITVEEQVDCIMNIAVGKMIELEYNIENI | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 26827
Sequence Length: 234
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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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 activity.
Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 22423
Sequence Length: 196
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Subcellular Location: Nucleus
EC: 2.7.4.14
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Q9RRE9 | MIVTIDGVAASGKSSVSSGVARALGIPYVSSGLLYRAATLLGLEAALDLSDAPRLLAHLRALPLRLEPLAEGNRVWSGERDLTPGLHQSAVDAGVSTVAAHPELRAWVDEQLRQLPPPFVAEGRDMGTNVFPDAPAKFYLTASPRIRAERRSAERPEDVDAIEAALIARDRKDAAQSAPAPDARVIDTGPLGLEEVIGEILGEIGQ | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 21781
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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A4J3N3 | MTEHKCIAIDGPAGAGKSTVAKKVAQKLNLLYIDTGAMYRAVTLKALRERINLWDDIALIELAKRTIITLLAGQKQSVLLDGLDVTREIRTPEVTNNVSIVAKIAGVREVLVQRQREMAEEAGVVMDGRDIGTVVLPKAKAKFFLTASAEERARRRAKEMMNFGYDVDLEQLIKEIEERDFMDSNRAVSPLVPAEDAVLIDSSGMTIDEVVNSIITWVEKGK | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24568
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q72DA1 | MPDTTGGHPAALKVVTLDGPAGVGKTTLARRVADALGIPYLDTGAMFRTMAWRLGPDGPDLDEALLRDRLAGFVFTLRGRGGASVLSCNGEDIGNEIRTEEVGAMASRIAALPVVRECLKAAQQRMGAAQPLVVEGRDMGTVVFPGARHKFFLDAAPEIRAMRRYTQLQTMGEAHDLALLTEQIRSRDEQDRNRAVAPLRPAADAIIVDTGDLDIDGVFGVIMQHIRSRDGL | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24955
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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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.
Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 22074
Sequence Length: 195
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Subcellular Location: Cytoplasm
EC: 2.7.4.14
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Q7UEW6 | MIITIDGPAGAGKSSIARRVASELGFEFLDTGAMYRAVTWGVMQQGIAWDDVESLVEFADAAQLIWQDDRIYLDNQDISEEIRTPQVTSHIRYLADPPRIRERITAQQRRIATGRDIVTEGRDQGTEVFPDAHCKIFLTASPEERARRRQRQLAENGRVMSVEEILAAQNQRDLEDRMRPVGRLRAASDAIVVQTDGMSPDEVREEVLRLVRECVQASAANSASSDVTR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25696
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q0SI81 | MSTSKLVVAMDGPSGTGKSSVSRMLAQRLDARYLDTGAMYRIATLHALRKGVDLTDPAAIADATAGLPWSIGTDPAGEQVLLDGEDVGEEIRGDAVTKAVSAVSAVPAVRELLVAAQRRLAGEAERIVVEGRDIGTVVIPDADVKIYLTASAEARAQRRNAQNLAEGRGDDYAAVLADVQRRDHLDSTRAVSPLRPADDSVLVDTSELGIDDVIGRLLLVVSERTGAGQ | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24066
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q2RXP6 | MIIAIDGPAASGKGTLARRLATQLRFAYLDTGKLYRAVGMAVIKGGADPHDAKAALAAARALDPATLGDRLLSTDTAGKAASVVGAIPEVRAALLDLQRDFATHPPQGAPGAVLDGRDIGTVVCPEAEVKIFVTASVEVRAHRRLQELRSGGHDVKEDDVLRDMRERDARDSGRAVAPMAIAADAVVLDTSRMTAEQALTAALDILAHKSQKT | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 22305
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q9ZD27 | MIDLKTKAFDIAQNFTISLDGPAASGKGTVGLILAKKFSLKYFQSSIVYRQLAFNCINQQIDITDIDAVIALSKELKLDNNIDLENEDIGDIASQIAVISDVRNNLNENLINLVKTTPRIIMEGRDIGTVVAPDADLKIFITASPYVRAIRRYNQLQAKGKTCILDEIIQQIILRDKRDKERKAGPLLPALGAFIIDTSKLSAIEIVEEVTNYIKNKIT | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24319
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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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
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B2RXH2 | MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL | 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)-[histone H3] + 2 succinate
Sequence Mass (Da): 56804
Sequence Length: 506
Subcellular Location: Nucleus
EC: 1.14.11.66
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Q9U297 | MASAATTTHFPSSRIPSEPCASSGPLFPDDVLFTTEASSASSSSCHVENDSRPLSPTMFTDGRTPVNISAKHLKDHPLHEPTGTSEVLTFYPTMREFKNFSQYIKKIEQNGGHLKAGIAKIVAPEGWTPRPTRKDFSDVDDYEITQPARETIEATEKPGAYFKRNVTCRRKMPVREFRTLANSAQYRNPRPDLKGSEIEKHYFDNILHGEPIYGADTEGSFYDAQVEEWNMNRLGTILEDTNYEIKGVNTVYLYFGMYKTTFPWHAEDMDLYSINFLHFGAPKYWFAISSEHADRFERFMSQQFSYQNEYAPQCKAFLRHKTYLVTPELLRQAGIPYATMVQRPNEFIITFPRGYHMGFNLGYNLAESTNFASQRWIDYGKDAVLCDCNKDSVKIDMTHFMAKYRPDEYTTWWTYWYGGGRELWIPKKKKEVPKKRRQSLADASKIAKRARLGASSTATDSDGSSGSSGSEEATEGSSFMRALPAGYTVHNWQLRPDYDELLRKYKKETKLLRSDTRIDFYQEREFNHARRAEWPHCAVCQYFQPPHMNAINHTVPNSSRRLIPKWCFSKTDTKKHEDHHEPPPPLDRLLTCSNCHVTVHSHCCSGGGGGGGDDDDVTSSGEPWRCPRCRNRTDVEIRTTSCQLCELRGGALIPCQIGTDSTWAHVACALFNRRAIFDCPNRPGACFVEPSPRQQSETPRMPPRRLSEEYRAELGDLYENSRWECVVCHRTDEGLAPCVLCIEEQATTSLPTLAHVTCARRVGFVCEVRDYPRGVVMICHKHEHSYLVNKTTQQQAYTNVKVGDFVFVEDVVEPPQKLFTRGAIVRADKKETVVVDFLDNSCSRDNHVEDIISCECLFCENGDHQYGARVKVVWDDKQVYDAYFRGKGQMIEYTVRLEDGREVRHPRNRLKTKRELNAYLKK | 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 germline-dependent fashion .
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)-[histone H3] + 2 succinate
Sequence Mass (Da): 105659
Sequence Length: 922
Subcellular Location: Nucleus
EC: 1.14.11.66
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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 formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21234
Sequence Length: 193
Subcellular Location: Cell membrane
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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 formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20649
Sequence Length: 189
Subcellular Location: Cell inner membrane
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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 formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21187
Sequence Length: 202
Subcellular Location: Cell inner membrane
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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 formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20065
Sequence Length: 190
Subcellular Location: Cell inner membrane
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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 formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23837
Sequence Length: 225
Subcellular Location: Cell membrane
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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 formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22894
Sequence Length: 205
Subcellular Location: Cell membrane
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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 formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19886
Sequence Length: 189
Subcellular Location: Cell inner membrane
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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 formation of a transient KdpB/KdpC/ATP ternary complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21275
Sequence Length: 206
Subcellular Location: Cell inner membrane
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