ids
stringlengths 6
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stringlengths 11
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stringlengths 108
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P43188 | ALADPLKVMISGAPASGKGTQCELIKTKYQLAHISAGDLLRAEIAAGSENGKRAKEFMEKGQLVPDEIVVNMVKERLRQPDAQENGWLLDGYPRSYSQAMALETLEIRPDTFILLDVPDELLVERVVGRRLDPVTGKIYHLKYSPPENEEIASRLTQRFDDTEEKVKLRLETYYQNIESLLSTYENIIVKVQGDATVDAVFAKIDELLGSILEKKNEMVSST | 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. The maize enzyme also works with CMP, albeit with 10% of the activity with AMP.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24867
Sequence Length: 222
Subcellular Location: Plastid
EC: 2.7.4.3
|
P49983 | MLSTLAKRFASGKKDRMVVFFGPPGVGKGTQAKLLEKEFNLYQISTGDALRAEIRGQTPLGKRVKGIIESGGLVDDDTIMDILQACMQKNTDNNGYIFDGIPRTIGQVEKLDALLAKMGTPLTHVLYLSVNIDELRERVCGRLFHPGSGRVYHKVTNPPKKPMTDDITGEPLIIRKDDTPEVFNQRMNQYFGTFQPCIDYYSKKGILQTFPVDGQPIDVVHKKLHAALQ | 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): 25550
Sequence Length: 229
Subcellular Location: Hydrogenosome
EC: 2.7.4.3
|
Q493A3 | MIRIIFLGPPGSGKGTQAHLIANKYNIPNISTGTMLRQALTRSTHKSYELHKNIMHTGDLVNDEFMVQLISTRINQNDCRNGFLLDGFPRTILQAKSMKQCKIFVNYIIEFFASDSVIIDRIAGRRIHVGSGRTYHIKFNPPRNYGLDDITGEILTTRKDDHEEAIRKRLSNYYQHTEPVLDYYREESKYKKMKYFSVDGNRDISKIYKELINIISS | 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): 25153
Sequence Length: 217
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
|
O51378 | MGLVFLGPPGSGKGTISKIISNEFKYQHISTGDLFRENILNSTALGQEIKKIVERGELVPDLITIKIVEDKIKAIKKNKDFILDGFPRNICQAEALDKFLPNVKIINFLIDEELVIKRLSGRRICKSCNNIFNIYTLTTKKNGICDVCGGDLYQREDDKEECLKTRLKEYKLQTKPLIEFYSKCSRLNNVDASVKIDEIKKKIIKIMLKKN | 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): 24099
Sequence Length: 211
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
|
C0R000 | MLNIIFIGAPGVGKGTQSALIEKDYSISHIATGDMLRENIANGTELGKTAKSYMDKGELVPDSLVIDMLKDRIKKDDCKNGFMLDGFPRTIEQAKELSNILESLNYKISAVIDIFASEEIIIDRLLKRGRADDNEETIKNRLKVFENQSKPVLDYYSDKAKIIKIESIGTPEEVYAKIKKELDVL | 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): 20757
Sequence Length: 185
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
|
P49982 | MQSLIKYQPKSPLKYLSSYFGDRKKNLFKLVLLGAPGAGKGTQAKHLVSKYSLKHISPGNLLREEMNRNSPITAQIKDYVSKGQLVPDSIVIKLIENHIATIGDSNWLLDGFPRSESQAAALRASPDLFPTHIVELKVDQEAVVQRLGGRRFDPITGNTYHIIYDPPPPDIADRVVVRTDDREDVIRERFRVYAENKDLVDKVFNHSVVSINCEGQTIDEVSLQLDRVLSMPSTIHPSIIMPERNKKQ | 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): 27965
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
Q7NKT5 | MATRRLMLLGAPGAGKGTQAQLLMQELGLPQVSTGDILRAAVKEGTPLGLEAQSYMNRGALVPDAVVVGLIEDRLARPDAGGGWILDGFPRTPAQAEALDGLLAHLAQSLEAVVLIDVPEAQLIERLTGRRTCPLCKRIFHVRFNPPPAAPPFCTDHTDCPSELVQRPDDTLEVVSKRLNVYRESTEPLIRYYQEQQKLTSVDGDRSPEVVYSELRELLG | 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): 24031
Sequence Length: 220
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
|
A9H3J9 | MNVIFLGPPGAGKGTQSKRLEARYGIAQISTGDMLRAEVAAESAIGKQARALMDAGQLVPDDVIVAMLESRIAQPDCAKGFILDGFPRTQGQAVALDSMLKRRGARIDVVLFLEVDEEALADRIAGRFTCATCGAGYNDLFKKPKVEGTCDVCGGHSFVRREDDRRETVAARLVAYRKQTAPILPYYEAEGLLRRIDGMADIDTVTAKVFEIMDAITKK | 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): 23799
Sequence Length: 219
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
|
P38372 | MNLILMGLPGAGKGTQAEKIIEKYGIPHISTGDMFRAAMKNETELGLKAKSYMDAGELVPDEVTIGIVRDRLSQDDCQNGFLLDGFPRTVAQAEALEDILASLDKKLDYVINIDVPEQLLMDRLTGRRVSPTSGRTYHVIFNPPKVEGICDVDGSELIQRDDDKPETVKKRLEVNQKQAQPLIDFYSEKGYLQNINGDQDISRVFEDINELLKGLSS | 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): 24170
Sequence Length: 217
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
|
B0R683 | MSHPNVLLLGAPGAGKGTQSRRLVDEFGVEHVTTGDALRANKTKDITHLDVEYDTPGAYMDAGELVPDAVVNEIVKTALDDADGYVLDGYPRNESQTEYLDSITDLDVVLYLDVDEDELVGRLTGRRVCEDCGATFHVSFNQPETEGVCDACGGSLYQREDDTEETARERITVYEENTAPVVEYFREQGVLAEVDGERTPDEVWTDVAAAVDERTA | 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): 23711
Sequence Length: 216
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
|
A1B049 | MAINIILLGPPGAGKGTQARRLIDERGLVQLSTGDMLREARSSGTEMGKRVAEVMDRGELVTDEIVIGLIREKLGQGGKGFIFDGFPRTLAQADALQALMAEMDQRIDAVIEMRVDDAALVSRISGRFTCGNCGEVYHDVTKPTKEPGKCDVCGSTDLRRRADDNEESLKTRLMEYYKKTSPLIGYYYVKGNLNPVDGLAEIDEVAAQVAKVMDKIPA | 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): 23811
Sequence Length: 218
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
|
A7HWT2 | MKLILLGPPGAGKGTQAKRLEEAHGLVQLSTGDMLRAAVAQGSEVGKVAEGIMARGELVPDDVVVGIIADRIEQPDAVNGYILDGFPRNVAQAEALDKMLAGKGTTLDAVVELGVDDSILLKRIETRAAETAGGPRADDNAEALAKRLKVYHEQTAPLIAYYKAKGKLRTVDGMKSMDEVTGQIETVLGISKRKGSWLSRLTGKK | 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): 21744
Sequence Length: 205
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
|
Q6D7Z5 | MRIILLGAPGAGKGTQAQFIMGKYGIPQISTGDMLRAAVKAGTELGKQAKEIMDAGKLVTDELVIALVKERIAQDDCRNGFLLDGFPRTIPQADAMKDAGIDVDYVIEFAVPDELIIDRIIGRRVHAASGRVYHVKFNPPKVEDKDDVTGEDLSVRKDDQEDTVRKRLVEYHQQTAPLVSYYQKEADAGNTRYFKVEGTRKVEEVRAELETILG | 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): 23733
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.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
Q4FLN8 | MNIILFGPPGAGKGTQAQSIVKKHNYFQLSTGNLLRDEVKSKTDLGVDIEKLISNGKFVSDEIVNTLLRQSLTNLKYRDRIIFDGYPRNVEQAINLEVLLNEFNQTIGHTIFLNVSRDIIEKRIMGRMTCEKCNMTLNEYFNKEQIELHPCGVEHLKKRKDDNLEIVISRYDTYMSSTKPVLEFYSKNSNFTEIDGAGEIDQITNKINEILKV | 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): 24450
Sequence Length: 213
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
|
A9BFZ7 | MRLLFFGPPGAGKGTQAKKVAQEFQIVHISTGDILRDAVSKGTELGKMAKAIMDRGELVSDEIMNSLVKERLEELDSFILDGYPRTLDQAKFLDQATKELQKEIDAAVLIDVSEEEIVKRISNRRVCPNCGKVYNLITLQPKEDEKCDVCGTKLIQRDDDKEEVVRERYKVYKKNTEPVIEYYRKNNKIITIDGAQNVEDVTKELFNILRSFNKQ | 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): 24573
Sequence Length: 215
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
|
B4R8N8 | MNLILFGPPAAGKGTQAKRLVEQRRMVQLSTGDMLRAAIASGSELGQRVSGIMERGELVSDAIVIELIEQRLPEAEAAGGAIFDGFPRTLAQAEALDAMLAGRGRRIDLVVRLKVDDAALMQRIAGRFAESGRADDNPESFKVRLDAYNRQTAPLLPYYEGQGKLVEVDGMGSIDQVAAAIDAALTGAAA | 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): 20180
Sequence Length: 190
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
|
Q9X1I8 | MMAYLVFLGPPGAGKGTYAKRLQEITGIPHISTGDIFRDIVKKENDELGKKIKEIMERGELVPDELVNEVVKRRLSEKDCERGFILDGYPRTVAQAEFLDGFLKTQNKELTAAVLFEVPEEVVVQRLTARRICPKCGRIYNLISLPPKEDELCDDCKVKLVQREDDKEETVRHRYKVYLEKTQPVIDYYDKKGILKRVDGTIGIDNVIAEVLKIIGWSDK | 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): 25169
Sequence Length: 220
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
|
Q59WU8 | MNIVLLIYCLAMVVAHDLQLFGDFKFELSDNWRNDCAKKALEPIINQCAEGIETISPFQQKSIAIQLSICEFENAEISYPSECRSQNLDTCILLLEKSPQYWTTFSGYYREIRNICHQVSLPFAKDQILQVYGNITEFYRTLMDEMTNSSKYTENMQNELKAKFDKLIGVIDLILADREKNREDLKSSFNMFKNNFEKSLNNALVVMKHSYEDANSNVKELESHLNYFINDMSQVYILINEKALEVKSQQDRIKEHNADILNQIEEIKKNLDNAYEEASEVQISNNQLVHDIQSSLDYSLFTVSNLNSHLQLSINDFIEKNEDIRSRAPIIFEEIFGLFLNHLNESGQLAMDSFEAALDLSLNMLHQKLNQTERSIDNLNSKVSDLAHFADSLKKYASSIFNVPNYVRTSMNHKIQQWREFGNIMVVGGVFFFVVLTLLVLSFIRTQVMKVFRFAFIGIPMITGIALAIFILRLLSMPMKVVDID | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56008
Sequence Length: 485
Subcellular Location: Endoplasmic reticulum membrane
|
Q6FU40 | MSMSITQPIKDLLSSQFQSYNISEQVKLYDIFPLLKPSCIKEAITDVVEVCTGYGPESLDPSIRAKAAVKLSLCEFEAVGLSIIPQGCYSNSIEEMMDCMLEIEHSSHWWTTYSGNYQRLSDVCSTYREYYQEKAIIETFLNITDFMADFHNQFKSSVVSETQEFQSNMKDKFAGVYNQFTHFESLLSQMIQKHSGIINDSIVAIKNKLSTEFVDELQMLKNDRYILINQILESDTEIKKTIDSMLVELTEDMKNQISAKSEFLINHMNITRLNESTALHDIIEENLQERFKDIAIFLDKFMVEIQTETNKVLLEVNEKLPTLEQQYLGNFAQALSNIDKQVLSASLQWQYDYDVVFANLYAALDLLNSNLNSSVKKIEQIEHVIDTIIVDTSFLNDQLANLILIPSTILRAFSFIGVKRVIIAIIVLYFKSTLLCLVHYGQSFRIAALLMSATAGIFCSKLLMSYIYN | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53659
Sequence Length: 469
Subcellular Location: Endoplasmic reticulum membrane
|
Q6BNJ4 | MDCVNISWFLITLFAAIATSTMHDGENNNVGKMLQEPTYLQSEMIESIMSRHLESFSLTESDFEDIIFMKPRSKCVKDALKDIIPECMRLGVDSIEPGLQKKAAIQLSICEFENSKVTYPSSCYNMINDNDFDSCIFDIERAPQYWTTFSGYYREITKICYEESLPFEKEQIISLYSNITKLYSKMFQDLNDSYKDSTHIQQMMKNEFKELQRMMKVILDQNEKTSEEVKEKYEEFSEQYSSMLSTSLEISKKFSLGTENLVEDMANNIKYLDFELSRISIAIEDLDFETKLTDMKNSVLDDVRNLSDESISLLDSILTNLESLDILSQDAQNITNGISQSLKKNEVLSNNMNNALIETDTQLHEHNEVIRFEFEETISYLSQFSDQAIDNAIRDTSEEITKHVATFIDSINLRLEETTTKLEEVIYNIDDLSDKVGNASSYLIEGLNLLTSNGIMDALLLTYNNVASGLESGFGMLTTLKSDIFKIVRFITACILFAILFIWSMNRLFSQNRTKHTTLSSISPIGILNFRRIFRFLTNLALWLSVMGGTLLAVIVTNFLIQLKVYISKLSTND | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65792
Sequence Length: 574
Subcellular Location: Endoplasmic reticulum membrane
|
Q6CIJ3 | MWFLVFSIWIASGQLLPHISNVIEKELDQLEITELSREYINNKFPITQSSCVKNALGEFLEICMRKGFEFVDADLRVITAVRLSVCEFESSGLTNYPSECHEKRLGGIDTISCVNALESSPQWWTTYSGNYQNLPHICMENSLPFEKEQILELFLNITDMYSEFQRNIENYWKSFSSDLEINGKENIDMIQNLFNSLVNDLIQNHKMKDEELITEFDKMKAEFDIRFFNFTESFDNLNDEVNEDLSLIKSHLIETFRQVDSEYMAQLQKNKNSTDKAFNELESMSTYILDHQKTSMELIDSFFSDLIDLTRDKNLVISDELMQTQEETIHLIFQYNKLVHESVIPLLTDDLLPVVRGVSNSIVENLDNMNVELTSHLENVSQTIEVKFKALEKETDRSLLKAKEVESNLRNLNNLVSTSLKGLQTIVRLLTFLLKRQVVLVGILQIFLRKYISMNLYLYAIAVVVTALAGSKVGSWGSLLMKSFVTR | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56279
Sequence Length: 487
Subcellular Location: Endoplasmic reticulum membrane
|
A5E4Z8 | MVGASAISGVVIIANVVAAIAAAAGDGDGGIASTTDTILTLDGIKILNNALLQWKDDCNQRALAEVMPQCIHGVENITPSQQKHTAMELSICEFENNGLDYPLECHASVRNLNTNTCIQALEKSPQYWTTFSGNYRAVKDICHQISLPYEKDQIIEVYENMTLLYRSVMEDLKSSHHKYTVELEMKIQNKFNKLFSVVDDLMRSRAEENNKVNQTFNKFYENFQVSISNALVVMQNSYDGANTNFELMQRHVSYFATELQRILLLVQEQGEKLQVQQEQLVTGNVKLSIQQERLFDNMQLFGNELDKLHNAEVSRVSSVNKQLKLTEFSIRHANSILRENTDELHLQRMLIAEYTPIILGNITTLLMHFLNQSASEIVENFEHSLNLSLEKLSLKIDETANSLAVVNATIARCSIFASSVVETLDSLKNSTIRMMMLFMSMITPSVTFDGLISGAKAIIAFFTLVTRLAAVIAICLLIILIWPIVKSLFFQPLCYLMRRCSYIVVSILVGVAAANFSVWLLQK | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58786
Sequence Length: 523
Subcellular Location: Endoplasmic reticulum membrane
|
A5DJU3 | MKKILRLVFILVYTNISTFVSAHELEDAASFTADELDRLLEDPPGCIQLAMRPIFEKCVLNGIHAVDPKDRRSSAIEMSVCEFESAGVEYPAECSTTDYDTCIWKLGLVPQYWTTFSGNYRDIGLFCEGVSRNNEKEQLVLLYSNITKVFAGFRHAFYESYSKSQEMKDEMEEGFSRWSADFDIAKDQHKEFYEFVAKQQEHIKIELMKNQKVIFDFHDEQEVRFNSYSNHIVDVIDSMAVDLDIILAKLADDGIIEDMENQKSKSLDIMKSYSEDAELTLSRIVSELERVGIIQKNDVSIVENLNSGLADTSNKVSKLNKDFEDLDSHFQHTKDLIESEVSFLFANLIGEMETKLSQALENVDDRIELHFVSQLEFLDKSLNETWEAILTFKQDWQIFTSIFENFENIPKSISHFVTSGLYKTNEILTQTSYFWSTILNIPVSLLSNILRYTMAASWIAILFILISLRYGSTKSFLLVIMVLLVVFLNTHRW | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56885
Sequence Length: 493
Subcellular Location: Endoplasmic reticulum membrane
|
Q09684 | MKFHPTRPFGLYFEFFIIISFFFTSESTGDVESFMKYSNVAFSEGLAGFDSLAHVYQALLKKSTCYQEVAATLISKCSLLNTELTIDNRIHSAIQMTLCDFERSQILAPSECVRGSQSECVSKLESTSTWWLSFTSHFHDVNHLCRLANLEMQKELSIEVNMNVTLVQKQFLEMVILHLRNFESVTDKMNQRIDKFDGKFNSVIENSFKDINFRVNQEIMGLVELQNHQQEGMVQQKEILSTIKQLKSEIFDINSFFANFIEESAGYSNSLIEKLNEKFTSENAIALSAIGKYTSEFSAFMEKRIKNLITTTEDSLQQSVQSNIDFVNSGFQPLYDLTIQLKEELQSLKRLSSEQQNLQHEQILQWKSDFLNVSKDHLKVLQQLRPLIDIVEKFMNVYFKGLSNIISSFAFIGFTLFATLSSLFFKVLKIHRRPIIVFGSLSIIFIHIYCFKITSWVNLYGWITCTIARTLSFIKLNIRTFYLTAFLCALLNFLRYLKYRNSKKDTELSLFLPAPEECNIYHNEHIQVQEDNYLCPIENSLIDLFGSENNKEKLGKQENVRFAFLNSESLEQSPWWD | Function: Required for nuclear membrane fusion during karyogamy.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66973
Sequence Length: 577
Subcellular Location: Endoplasmic reticulum membrane
|
Q6C994 | MSLSYSFNTTIFTENRDLVAALQPQTNCARTALTLIVSDCGKLSSFNEDQQLRVSLAVGLAVCEFKAAQVTYPDACNNIEDWMSTSACTQQLVSSPQWWTTYHGCYNSVKQICHMHEASRECDRALKTHSQIVDMQEKLHTKMDQYWELVETMSDHRDAVLDYWNDTFDFMSETLAHMKETSVSLNAVYRDNFAQAQEHFQMLSENLQEARVQMENLGWAAQDAVVSLSKSTLAEQSLVSERLKNDASSLHKLLVLAHQDTTESFETQLQQSLTILVESSDNVLLNHVQQVSSRLSALMSDLEESQKKNMDMQHQLQQKVRTINDDIEGFTDTVKQGLEASHSLLNLVKSKIQLVNGVVSIFSRPVRSAFQLASFIIMIRAAFIGGIYTSIGLVMGSMLGVLVMQQV | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45815
Sequence Length: 407
Subcellular Location: Endoplasmic reticulum membrane
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Q04746 | MFEMRYVYLFAICIKFVSSSELGKINNLLQGRLIYTDNSVATNVLESKFPFLKSTCVKDALKLFLPQCIANGLESIDAETRVETAIKLSICEFQASGLGEIPENCMVDDLGSMMDCMFELESSSQWWTTYSGNYQRLSSICYENLLPFEKEQILKLFLNITELYDSFGDDVDTKLNHLMFQMEQDSQNFLDDLARMFRNYDNELRNATESNRIILENDLSFFRNKVNDVLYETSEQLEVQIIEKNSQLMNEVDTVHHIMSDLADELAKNDIKSKINDLKDDSLNNLQDLVEMSNDVKEYYSRNNKLVNTELENFSMGLKKQLGGMSKDLSESQMEAIELLQGFNSILHDSLLPSMTDEIVPEMTNFKNTLLQEWTAITSTLNGDFALWNEEIFSTFNDISEKLNGTKKKLDDIEIRVSLVHKNVMTMMRVLDFMWKTSKMIIRCGYLAVKNKYYWLLCSVVWIWSKYRTSRVNVKMIPIKRYYQWAALLLSIYLGAKTGSLIDF | Function: Required for nuclear membrane fusion during karyogamy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58440
Sequence Length: 504
Subcellular Location: Endoplasmic reticulum membrane
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Q004B5 | MADAAVIEKLEAGFKKLEAATDCKSLLKKYLTKEVFDKLKDKRTSLGATLLDVIQSGVENLDSGVGIYAPDAEAYTLFAPLFDPIIEDYHVGFKQTDKHPNKDFGDVNSFVNVDPEGKFVISTRVRCGRSLQGYPFNPCLTESQYKEMEAKVSSTLSSLEGELKGTYYPLTGMSKEVQQKLIDDHFLFKEGDRFLQAANACRYWPAGRGIYHNDNKTFLVWVNEEDHLRIISMQMGGDLGQVFRRLTSAVNEIEKRIPFSHHDRLGFLTFCPTNLGTTVRASVHIKLPKLAANREKLEEVAGKYNLQVRGTRGEHTEAEGGIYDISNKRRMGLTEFQAVKEMQDGILELIKIEKEM | Function: Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine . Has nucleoside diphosphate kinase-like activity toward dTDP. Binds and phosphorylates dTDP using ATP as a phosphate donor. Does not phosphorylate dADP, dCDP, dGDP, dTMP or thymidine .
Catalytic Activity: ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine
Sequence Mass (Da): 40160
Sequence Length: 356
EC: 2.7.3.3
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G1ESZ9 | MAEELFKTLQNAKECHSLLKKHLTKERFDKLKGLKTKFGGTLADCIRSGCKNPDSGVGIYASDPDAYTVFAEVLDAVIMDYHKIDKVHHPIPDFGDVNNLNIGDLDPSGNMIVSTRVRVGRSHDSFGFPPVLKKDDRIKMEQVSVEALKSLDGELAGSYFPLANMSADVQKQLTEDHFLFNDSDRFLKAASGYDDWPIGRGIYFSENKTFLCWVNEEDHLRLISMQKGGNLGEVYKRLVSAINKMEKKLNFAKKDNMGYLTFCPSNLGTTMRASVHIKIPKLSQRSDFKSICDKYNLQARGIHGEHTESVCGVYDISNKRRMGLTEYEAVTEMMRGVNEIIREETNST | Function: Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine.
Catalytic Activity: ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine
Sequence Mass (Da): 39239
Sequence Length: 348
EC: 2.7.3.3
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O61367 | MVDQAVLDKLETGFSKLSSSDSKSLLKKYLSKDVFDQLKTKKTSFDSTLLDCIQSGIENLDSGVGIYAPDAEAYTLFADLFDPIIEDYHGGFKKTDKHPPKDFGDVDSLGNLDPANEFIVSTRVRCGRSLEGYPFNPCLTEAQYKEMEEKVSSTLSGLEGELKGTFYPLTGMSKETQQKLIDDHFLFKEGDRFLQAANACRFWPTGRGIYHNDDKTFLVWCNEEDHLRIISMQMGGDLGQVYRRLVHAVNEIEKRLLFSHNDRLGFLTFCPTNLGTTVRASVHIKLPKLAANRAKLEEIAGKFNLQVRGTRGEHTEAEGGIYDISNKRRLGLTEYQAVKEMHDGIAELIKLEKEL | Function: May play an important role in the energy releasing mechanism in the visual system. By acting as an energy shuttle and/or as an energy reservoir, ARGK can provide both spatial and temporal buffering in delivering energy in sensory cells.
Catalytic Activity: ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine
Sequence Mass (Da): 40008
Sequence Length: 355
EC: 2.7.3.3
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Q08415 | MTKRLQARRLDGIDQNLWVEFGKLTKEYDVVNLGQGFPDFSPPDFATQAFQQATSGNFMLNQYTRAFGYPPLTNVLASFFGKLLGQEMDPLTNVLVTVGAYGALFTRFQALVDEGDEVIIMEPAFDCYEPMTMMAGGCPVFVTLKPSPAPKGKLGASNDWQLDPAELASKFTPRTKILVLNTPNNPLGKVFSRMELELVANLCQQHDVVCISDEVYQWLVYDGHQHVSIASLPGMWDRTLTIGSAGKSFSATGWKVGWVMGPDNIMKHLRTVHQNSIFHCPTQAQAAVAQCFEREQQHFGQPSSYFLQLPQAMELNRDHMIRSLQSVGLKLWISQGSYFLIADISDFKSKMPDLPGAEDEPYDRRFAKWMIKNMGLVGIPVSTFFSRPHQKDFDHYIRFCFVKDKATLQAMDERLRKWKELQP | Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others . Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond .
Catalytic Activity: 2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate
Sequence Mass (Da): 47873
Sequence Length: 423
Pathway: Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.6.1.7
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A0A0R4IXF6 | MADPAAQSSAQPRLQQAQSSGPTGSNSNPGAGSSDPARPGLSQQQWSSQKKAQVRSFPRAKKLEKLGVFSSCKANDACKCNGWKNPNPPTAARMELQQQAASLTETCRSCGHSLAEHVSHLENVSEEEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMGKPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPKERQTMYELSKMFLLCLNYWKLETPSQFRQRAQKEDAAAYKVDYTRWLCYCHVPQSNDSLPRYETCQVFGRSLLKSIFTVTRRQLLEKFRVEKDKLPPEKRTLILTHFPKFLSMLEEEIYGENSPIWEADFTMPASEGTQLGHQTVLSPVSISGSPHSKGSSASALGVTGLDVASSEPTIGEKRKLPEALTLEDAKRIRVMGDIPMELVNEVMKTITDPAAMLGPETSLLSANAARDETARLEERRGIIEFHVIGNSLSQKSNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHGILYFLTYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIPYTELSHIIKRQKEIIKKLIERKQNQIRKVYPGLTCFKEGVRQIPVESIPGIRETGWKPSAKEKSKELKDPDLLYNMLKNLLAQIKTHPDAWPFMEPVKKSEAPDYYEVIRFPIDLKTMTERLKNRYYVTKKLFIADLQRVITNCREYNPPDSEYCKSANTLEKFFYFKLKEAGLIDK | Function: Protein lysine acyltransferase that can act as a acetyltransferase, glutaryltransferasesucc, succinyltransferase or malonyltransferase, depending on the context (By similarity). Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequency around the transcription start sites of genes (By similarity). Succinylation of histones gives a specific tag for epigenetic transcription activation (By similarity). Association with the 2-oxoglutarate dehydrogenase complex, which provides succinyl-CoA, is required for histone succinylation (By similarity). In different complexes, functions either as an acetyltransferase (HAT) or as a succinyltransferase: in the SAGA and ATAC complexes, acts as a histone acetyltransferase (By similarity). Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles (By similarity). Acetylation of histones gives a specific tag for epigenetic transcription activation (By similarity). Also acetylates non-histone proteins, such as tbx5 . Involved in heart and limb development by mediating acetylation of tbx5 . Together with kat2b, required for growth and differentiation of craniofacial cartilage and bone by regulating acetylation of histone H3 at 'Lys-9' (H3K9ac) . Also acts as a histone glutaryltransferase: catalyzes glutarylation of histone H4 on 'Lys-91' (H4K91glu), a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes (By similarity).
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 90624
Sequence Length: 795
Domain: Loop3 is required for substrate specificity and adopts different structural conformations in succinyl-CoA-bound and acetyl-CoA-bound forms. Tyr-603 has an important role in the selective binding of succinyl-CoA over acetyl-CoA.
Subcellular Location: Nucleus
EC: 2.3.1.48
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Q92830 | MAEPSQAPTPAPAAQPRPLQSPAPAPTPTPAPSPASAPIPTPTPAPAPAPAAAPAGSTGTGGPGVGSGGAGSGGDPARPGLSQQQRASQRKAQVRGLPRAKKLEKLGVFSACKANETCKCNGWKNPKPPTAPRMDLQQPAANLSELCRSCEHPLADHVSHLENVSEDEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMTRPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPRERQTMFELSKMFLLCLNYWKLETPAQFRQRSQAEDVATYKVNYTRWLCYCHVPQSCDSLPRYETTHVFGRSLLRSIFTVTRRQLLEKFRVEKDKLVPEKRTLILTHFPKFLSMLEEEIYGANSPIWESGFTMPPSEGTQLVPRPASVSAAVVPSTPIFSPSMGGGSNSSLSLDSAGAEPMPGEKRTLPENLTLEDAKRLRVMGDIPMELVNEVMLTITDPAAMLGPETSLLSANAARDETARLEERRGIIEFHVIGNSLTPKANRRVLLWLVGLQNVFSHQLPRMPKEYIARLVFDPKHKTLALIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHNILYFLTYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIPYTELSHIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKEGVRQIPVESVPGIRETGWKPLGKEKGKELKDPDQLYTTLKNLLAQIKSHPSAWPFMEPVKKSEAPDYYEVIRFPIDLKTMTERLRSRYYVTRKLFVADLQRVIANCREYNPPDSEYCRCASALEKFFYFKLKEGGLIDK | Function: Protein lysine acyltransferase that can act as a acetyltransferase, glutaryltransferase, succinyltransferase or malonyltransferase, depending on the context . Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequency around the transcription start sites of genes . Succinylation of histones gives a specific tag for epigenetic transcription activation . Association with the 2-oxoglutarate dehydrogenase complex, which provides succinyl-CoA, is required for histone succinylation . In different complexes, functions either as an acetyltransferase (HAT) or as a succinyltransferase: in the SAGA and ATAC complexes, acts as a histone acetyltransferase . Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles . Acetylation of histones gives a specific tag for epigenetic transcription activation . Recruited by the XPC complex at promoters, where it specifically mediates acetylation of histone variant H2A.Z.1/H2A.Z, thereby promoting expression of target genes . Involved in long-term memory consolidation and synaptic plasticity: acts by promoting expression of a hippocampal gene expression network linked to neuroactive receptor signaling (By similarity). Acts as a positive regulator of T-cell activation: upon TCR stimulation, recruited to the IL2 promoter following interaction with NFATC2 and catalyzes acetylation of histone H3 at 'Lys-9' (H3K9ac), leading to promote IL2 expression (By similarity). Required for growth and differentiation of craniofacial cartilage and bone by regulating acetylation of histone H3 at 'Lys-9' (H3K9ac) (By similarity). Regulates embryonic stem cell (ESC) pluripotency and differentiation (By similarity). Also acetylates non-histone proteins, such as CEBPB, PPARGC1A, PLK4 and TBX5 . Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5 . Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4 . Acts as a negative regulator of gluconeogenesis by mediating acetylation and subsequent inactivation of PPARGC1A . Also acts as a histone glutaryltransferase: catalyzes glutarylation of histone H4 on 'Lys-91' (H4K91glu), a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes .
PTM: Acetylated at Lys-549, inhibiting the protein acetyltransferase activity . Deacetylation at Lys-549 by SIRT6 promotes phosphorylation at Ser-307 and Thr-735 and subsequent activation of the protein acetyltransferase activity, leading to acetylation and inactivation of PPARGC1A .
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 93926
Sequence Length: 837
Domain: Loop3 is required for substrate specificity and adopts different structural conformations in succinyl-CoA-bound and acetyl-CoA-bound forms. Tyr-645 has an important role in the selective binding of succinyl-CoA over acetyl-CoA.
Subcellular Location: Nucleus
EC: 2.3.1.48
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Q1LUC3 | MSESTGIPQGSPAVGAAGSAPAAPGVGGTECSGAAVGSARIAVKKAQLRSSPRPKKLEKLGVYSSCKAEGACKCNGWKSQNPPPTPPPPTPPRAEQPTAVSLMEPCRSCSHALGDHVTHLENVSEEEMNRLLGIVLDVEYLYTCVHKEEDPDTKQVYFSLFKLLRKCILQMGRPVVEALESPPFEKPSIEQGVNNFVQYKFSHLPSKERQTIVELAKMFLNQINYWQLETPSQKRQRAPDDDVAGYKVNYTRWLCYCNVPQFCDSLPRYEATQIFGRIFLRSVFTIMRKQLLEQARQEKDKLPPEKRTLILTHFPKFLSMLEEEVYSHNSPIWSENFMIGLSGGQIPTVVSAPPVNRSLYYSSSPAPVELAGGGSVSPARKTASVLEPNPGGEKRKPAEPLSHEDSKRPRVVGDIPMELINEVMSTITDPTAMLGPETSLLSAHSARDEAARLEERRGVIEFHVIGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLSLIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHEILNFLTYADEYAIGYFKKQGFSKDIKVPKSKYVGYIKDYEGATLMGCELNPCIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKEGVRQIAIESIPGIRETGWKPLGKSKELKDPDQLYSTLKNILTQVKSHPNAWPFMEPVKKNEAPGYYQVIRFPMDLKTMSERLKSRYYTTRKLFMADMQRIFTNCREYNPPESEYYKCANLLEKFFYTKIKEAGLIDK | Function: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation (By similarity). Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles (By similarity). Also acetylates non-histone proteins . Involved in heart and limb development by mediating acetylation of tbx5 . Also acetylates spermidine (By similarity). Together with kat2a, required for growth and differentiation of craniofacial cartilage and bone by regulating acetylation of histone H3 at 'Lys-9' (H3K9ac) .
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 90026
Sequence Length: 796
Subcellular Location: Nucleus
EC: 2.3.1.48
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Q92831 | MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK | Function: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation . Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles . Also acetylates non-histone proteins, such as ACLY, MAPRE1/EB1, PLK4, RRP9/U3-55K and TBX5 . Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A . Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-BMAL1 and CLOCK-BMAL1 heterodimers . Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5 . Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4 . Acetylates RRP9/U3-55K, a core subunit of the U3 snoRNP complex, impairing pre-rRNA processing . Acetylates MAPRE1/EB1, promoting dynamic kinetochore-microtubule interactions in early mitosis . Also acetylates spermidine .
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 93013
Sequence Length: 832
Domain: (Microbial infection) The bromodomain mediates binding to HIV-1 Tat.
Subcellular Location: Nucleus
EC: 2.3.1.48
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Q9JHD1 | MAEAGGAGSPALPPAPPHGSPRTLATAAGSSASCGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRGDLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMDRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPSKERQTTIELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTKVFGRTLLRSVFTIMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSPLGIQTVISPPVTGTALFSSNSTSHEQINGGRTSPGCRGSSGLEANPGEKRKMNNSHAPEEAKRSRVMGDIPVELINEVMSTITDPAGMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHEILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPQIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPKDPEQLYSTLKNILQQVKNHPNAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLRNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCASILEKFFFSKIKEAGLIDK | Function: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY, MAPRE1/EB1, PLK4, RRP9/U3-55K and TBX5. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-BMAL1 and CLOCK-BMAL1 heterodimers. Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5. Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4. Acetylates RRP9/U3-55K, a core subunit of the U3 snoRNP complex, impairing pre-rRNA processing. Acetylates MAPRE1/EB1, promoting dynamic kinetochore-microtubule interactions in early mitosis. Also acetylates spermidine.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 91769
Sequence Length: 813
Subcellular Location: Nucleus
EC: 2.3.1.48
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Q5QNI1 | METISNIFHNDPLPPLGARANQSIKLRKFIISPYDSRYRTWETFLLVLVVYSAWICPFELAYLRNLSWKVSLVDNIIDSFFAIDIILTFFLAYLDQKSYLLVDDPKRIVARYFSSWFLFDVCSTIPYQLLGQIFKKHENGLAYRLLSMLRLWRLRRLSELFARLEKDIRLNYYWIRCTKLISVTLFAVHCSGCFNYLIADRYPNPARTWIGAAIPNYRSQNLWVRYVTAIYWSITTLTTTGYGDLHAENQREMLFSICYMLFNLGLTAYLIGNMTNLVVQGSCRTRNFRDTIHAASQFAARNQLPGHIKDEMLSHICLRYKTEGLKQKETLDSLPKGIRSSIACNLFLPVIEKVYLFHGVSFTCMIQLVTEMEAEYYPPREVVILQNEAPRDVYILVSGAVEERVEIDGTEKVQEVLCNGEIFGEIGVICSIPQPCAFHTIKVSQLLRLNTAVLKNIIKENSDDRRVILNNLSQKMNQDHRFSTEVMEKSLQMMHQHFGEYNRCSALNQDNEKNELKANNGHSMALEWKRVTIHMYSQRNKRPEAPLAKVINLPGSLDKLFAIACQKFNNYRLTKLVNPEFAEIDDITVIRDGDHLFFMEI | Function: Probable inward-rectifying potassium channel. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69807
Sequence Length: 601
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids. The pore-forming region H5 is enclosed by the transmembrane segments S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity (By similarity).
Subcellular Location: Membrane
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P92960 | MSTTTTEARSPLPLLLRRGRSSTALSASTAEARSPLSILQFRRRSSKDVRNITSVSSSLLPAFGTFIEDDNPSSKPFIVLHFDRRYRLWELFLVILVGYSAWASLFELAFEKAAEGALLTIDLVVDFFFAVDIILTFFVSYLDNTTYLNVTDHKLIAKRYLKSVAFVMDVASTLPIQFIYKTITGDVGRGQAFGFLNLLRLWRLRRVAELFKRLEKDAHFNYFVIRVIKLLCVTIFWIHLAGCILYWIAYHYPRPTDTWIGSQVEDFKERSVWLGYTYSMYWSIVTLTTVGYGDLHAVNSREKTFNMFYMLFNIGLTSYIIGIMTNLVVHGALRTFAMRSAINDILRYTSKNRLPDTMREQMLAHMQLKFKTAELRQEEVLQDLPKAIRSSINQHLFRSIIEEAYLFKGFPEGLLVQLVSQIQAEYFPPKMEIILQNEIPTDFYVIVSGGVDIIASKGVSEQVLAKLGPGSMAGEIGVVFNIPQPFTVRTRRLSQVIRIGHHKFKEMVQSDNDVDAKMIIANFMTYLKGLNDELKKEIPFLRDLLDDADAQVQETVQSEETPQSNDEEIVTVSRHENGQIEERRREGVPKRVIIHGQAPPNQDNKNNGDSNGRLIILPDSIQLLFDLAEKKLGKRGSTIAMADGAHVEQIDALRENDHLYIF | Function: Probable modulatory (alpha) subunit of inward-rectifying potassium channels. Could mediate potassium uptake from the soil solution by plant roots in association with AKT1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75598
Sequence Length: 662
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids. The pore-forming region H5 is enclosed by the transmembrane segments S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity.
Subcellular Location: Membrane
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Q6YP21 | MFLAQRSLCSLSGRAKFLKTISSSKILGFSTSAKMSLKFTNAKRIEGLDSNVWIEFTKLAADPSVVNLGQGFPDISPPTYVKEELSKIAAIDSLNQYTRGFGHPSLVKALSYLYEKLYQKQIDSNKEILVTVGAYGSLFNTIQALIDEGDEVILIVPFYDCYEPMVRMAGATPVFIPLRSKPVYGKRWSSSDWTLDPQELESKFNSKTKAIILNTPHNPLGKVYNREELQVIADLCIKYDTLCISDEVYEWLVYSGNKHLKIATFPGMWERTITIGSAGKTFSVTGWKLGWSIGPNHLIKHLQTVQQNTIYTCATPLQEALAQAFWIDIKRMDDPECYFNSLPKELEVKRDRMVRLLESVGLKPIVPDGGYFIIADVSLLDPDLSDMKNNEPYDYKFVKWMTKHKKLSAIPVSAFCNSETKSQFEKFVRFCFIKKDSTLDAAEEIIKAWSVQKS | Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others. May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond. Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro).
Catalytic Activity: 2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate
Sequence Mass (Da): 51400
Sequence Length: 454
Pathway: Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2.
EC: 2.6.1.7
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Q71RI9 | MLLAQRRLISLGCRSKPIKTIYSSSKVLGLCTSAKMALKFKNAKRIEGLDSNVWVEFTKLAADPSVVNLGQGFPDISPPSYVKEELSKAAFIDNMNQYTRGFGHPALVKALSCLYGKIYQRQIDPNEEILVAVGAYGSLFNSIQGLVDPGDEVIIMVPFYDCYEPMVRMAGAVPVFIPLRSKPTDGMKWTSSDWTFDPRELESKFSSKTKAIILNTPHNPLGKVYTRQELQVIADLCVKHDTLCISDEVYEWLVYTGHTHVKIATLPGMWERTITIGSAGKTFSVTGWKLGWSIGPAHLIKHLQTVQQNSFYTCATPLQAALAEAFWIDIKRMDDPECYFNSLPKELEVKRDRMVRLLNSVGLKPIVPDGGYFIIADVSSLGADLSDMNSDEPYDYKFVKWMTKHKKLTAIPVSAFCDSKSKPHFEKLVRFCFIKKDSTLDAAEEIFRAWNSQKS | Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others . May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond . Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro) .
Catalytic Activity: 2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-glutamate
Sequence Mass (Da): 51126
Sequence Length: 455
Pathway: Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2.
EC: 2.6.1.7
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Q5JM04 | MPRSSRMNLWPHCFPCFDDGDRSGNRFSTVCNFPDDLLPSLGATAHQPPKLRKYLVSPYDPRYKVWETFLIILVVYSAWICPLEFAFLRYLPSAPFVVDDVVNGFFAVDIMLTFFVPFVDKKSYLLVNDPKKIAVRYLSSWFVFDVCSTVPFHSISLLFNEHGHDLGFKFLNVLRLWRLRRVSSMFARLEKDIRFNYAVIRCTKLISVTLFAIHCAGCINYLIADRYPDPRRTWIGAVMPNFREDGLWIRYVTAMYWSITTLTTTGYGDLHAENAREMLFGICYMLFNLWLTAYLIGNMTNLVVHSTSRTRDFRDVVQAASEFAARNQLPQQIEEQMLNHICLRYKTDGLKQQETLDVLPKAMRSSISHYLFFRVVQGAYLFKGVSSRFIQQLVTEMQAEYFAPKEDIILQNDSPSDLYLLVSGAVDILVFLDGTEQVYRRAAEGELLGEIGVLCNKPQSFTFRTTKLSQILRISRTKLLGIIQENREDGDIIRSNLQQVNV | Function: Probable inward-rectifying potassium channel. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58008
Sequence Length: 502
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids. The pore-forming region H5 is enclosed by the transmembrane segments S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity (By similarity).
Subcellular Location: Membrane
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Q652U9 | MAARSELLRPAFGEASPSLGRFVINPHSCSYRWWHMFLIMLVLYSAWASPFELSMEKAASIALVVTDLVVDVFFAIDIALSFFVAYRDTSTGLLITDRRKITMRYLKRPCFALDVASTIPLQIIYQLVTGKRQGLWGLLNLLRLWRLRRVSKLFARVEKDIRFNYLWTRLIKLLCVTLFALHFAACIYLWMAFNYKIKELTWIGSQIHSFEDRSVWFCYTCAVYWSITTLATVGYGDLHATNIGEMLFSIAFMLFNMGLTSYIIGNITNLVVRETSNTFKMRDMVQRVSEFGRMNRLPEAMREQMLASVQLRFRTDEQLQQEMLSELPKAVRSGVMKHMFKSAIESCYLFQGVSDSLIVQLVAEMKAEFFPPKANVILENETSTDCYIIISGEVEALTTLADGTEKHVKRIGPRGMAGEIGVMFSIPQPFTIRSRRLTQVVRISHIHLLQAVRPNTADGYIVFSNFIQYLESLKVQTKDVAFVSDHLWNGNSMVLRRATEVAVDESKEAAHKMLPCKEPKRVVIHEQLPNATSTALHPSPGKLVLLPDSMQELMKLSEKKFGKAVRGILTVEGAEVEDIEVIRDGDHLLFS | Function: Probable inward-rectifying potassium channel. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67394
Sequence Length: 591
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids. The pore-forming region H5 is enclosed by the transmembrane segments S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity (By similarity).
Subcellular Location: Membrane
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Q92993 | MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGAARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDIVDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW | Function: Catalytic subunit of the NuA4 histone acetyltransferase complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H2A and H4 . Histone acetylation alters nucleosome-DNA interactions and promotes interaction of the modified histones with other proteins which positively regulate transcription . The NuA4 histone acetyltransferase complex is required for the activation of transcriptional programs associated with proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair . The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) by promoting homologous recombination (HR): the complex inhibits TP53BP1 binding to chromatin via MBTD1, which recognizes and binds histone H4 trimethylated at 'Lys-20' (H4K20me), and KAT5 that catalyzes acetylation of 'Lys-15' of histone H2A (H2AK15ac), thereby blocking the ubiquitination mark required for TP53BP1 localization at DNA breaks . Also involved in DSB repair by mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac), promoting NBN/NBS1 assembly at the sites of DNA damage . The NuA4 complex plays a key role in hematopoietic stem cell maintenance and is required to maintain acetylated H2A.Z/H2AZ1 at MYC target genes (By similarity). The NuA4 complex is also required for spermatid development by promoting acetylation of histones: histone hyperacetylation is required for histone replacement during the transition from round to elongating spermatids (By similarity). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome . Also acetylates non-histone proteins, such as BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF, LPIN1, NDC80/HEC1, NR1D2, RAN, SOX4, FOXP3, ULK1 and RUBCNL/Pacer . Directly acetylates and activates ATM . Promotes nucleotide excision repair (NER) by mediating acetylation of ERCC4/XPF, thereby promoting formation of the ERCC4-ERCC1 complex . Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2 . Acts as a regulator of regulatory T-cells (Treg) by catalyzing FOXP3 acetylation, thereby promoting FOXP3 transcriptional repressor activity . Involved in skeletal myoblast differentiation by mediating acetylation of SOX4 . Catalyzes acetylation of APBB1/FE65, increasing its transcription activator activity . Promotes transcription elongation during the activation phase of the circadian cycle by catalyzing acetylation of BMAL1, promoting elongation of circadian transcripts (By similarity). Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer . Acts as a regulator of the cGAS-STING innate antiviral response by catalyzing acetylation the N-terminus of CGAS, thereby promoting CGAS DNA-binding and activation . Also regulates lipid metabolism by mediating acetylation of CHKA or LPIN1 . Promotes lipolysis of lipid droplets following glucose deprivation by mediating acetylation of isoform 1 of CHKA, thereby promoting monomerization of CHKA and its conversion into a tyrosine-protein kinase . Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of LPIN1, thereby promoting the synthesis of diacylglycerol . In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) and 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to mediate protein crotonylation and 2-hydroxyisobutyrylation, respectively . Acts as a key regulator of chromosome segregation and kinetochore-microtubule attachment during mitosis by mediating acetylation or crotonylation of target proteins . Catalyzes acetylation of AURKB at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis . Acetylates RAN during mitosis, promoting microtubule assembly at mitotic chromosomes . Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore-microtubule attachment . Catalyzes crotonylation of MAPRE1/EB1, thereby ensuring accurate spindle positioning in mitosis .
PTM: Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase . The phosphorylated form has a higher activity . Phosphorylation at Ser-90 by CDK1 or CDK9 is a prerequisite for phosphorylation at Ser-86 by GSK3 . Phosphorylation at Ser-86 by GSK3 (GSK3A or GSK3B) activates acetyltransferase and acyltransferase activities . Phosphorylation at Ser-90 by CDK9 promotes KAT5 recruitment to chromatin . Phosphorylation by VRK1 following DNA damage promotes KAT5 association with chromatin and histone acetyltransferase activity .
Catalytic Activity: acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]
Sequence Mass (Da): 58582
Sequence Length: 513
Subcellular Location: Nucleus
EC: 2.3.1.48
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Q9NYS0 | MGKGCKVVVCGLLSVGKTAILEQLLYGNHTIGMEDCETMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLASKLSQPQSKSSFPLPGRKNKGNSNSEN | Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB.
Sequence Mass (Da): 21643
Sequence Length: 192
Domain: In contrast to other members of the Ras family, the members of the KappaB-Ras subfamily do not contain the conserved Gly and Gln residues in positions 13 and 65, which are replaced by Leu residues, and are therefore similar to the constitutively active forms of oncogenic forms of Ras. This suggests that members of this family are clearly different from other small GTPases proteins.
Subcellular Location: Cytoplasm
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Q8CEC5 | MGKGCKVVICGLLSVGKTAILEQLLYGNHTIGMEDCETLEDVYMASVETDRGVKEQLHLYDTRGLQKGVELPKHYFSFADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKLDLSEQRQVDADVAQQWARSEKVKLWEVTVTDRRTLIEPFTLLASKLSQPQSKSSFPLPGRKNKGNSNPEN | Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity).
Sequence Mass (Da): 21662
Sequence Length: 192
Domain: In contrast to other members of the Ras family, the members of the KappaB-Ras subfamily do not contain the conserved Gly and Gln residues in positions 13 and 65, which are replaced by Leu residues, and are therefore similar to the constitutively active forms of oncogenic forms of Ras. This suggests that members of this family are clearly different from other small GTPases proteins.
Subcellular Location: Cytoplasm
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Q6DGL2 | MGKSCKVVVCGQGSVGKTAVLEQLLYANHVVGSETMETLEDIYIGSVETDRGTREQVRFYDTRGLRDGQEFPRHYFTFADGFVLVYSIDSRESFKRVEALKKEIDRCRDKKEVTIVVVGNKLDLQDQRRVDSSAAQQWARQEKVRLWEISVTDRRTLIEPFVHLASKMTQPQSKSTFPLSRNKNKTSGSLDS | Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation.
Sequence Mass (Da): 21913
Sequence Length: 192
Domain: In contrast to other members of the Ras family, the members of the KappaB-Ras subfamily do not contain the conserved Gln residues in position and 65, which is replaced by a Leu residue, and are therefore similar to the constitutively active forms of oncogenic forms of Ras. This suggests that members of this family are clearly different from other small GTPases proteins.
Subcellular Location: Cytoplasm
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Q9NYR9 | MGKSCKVVVCGQASVGKTSILEQLLYGNHVVGSEMIETQEDIYVGSIETDRGVREQVRFYDTRGLRDGAELPRHCFSCTDGYVLVYSTDSRESFQRVELLKKEIDKSKDKKEVTIVVLGNKCDLQEQRRVDPDVAQHWAKSEKVKLWEVSVADRRSLLEPFVYLASKMTQPQSKSAFPLSRKNKGSGSLDG | Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity).
Sequence Mass (Da): 21508
Sequence Length: 191
Domain: In contrast to other members of the Ras family, the members of the KappaB-Ras subfamily do not contain the conserved Gly and Gln residues in positions 13 and 65, which are replaced by Ala and Leu residues, respectively, and are therefore similar to the constitutively active forms of oncogenic forms of Ras. This suggests that members of this family are clearly different from other small GTPases proteins.
Subcellular Location: Cytoplasm
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Q32NS2 | MGKSCKVVICGQHGVGKTSILEQLLYGNHVVGSDMIETQEDIYIGSVETDRGVREQVRFYDTRGLKDGLELPKHCFCGTDGYVLVYSVDNKDSFKRVEALKKEIDRSKDKKEVTIVVLGNKSDMKDQRRVDHEAAQQWAKAEKILLRNGPTHGSANWNLHPDH | Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation.
Sequence Mass (Da): 18398
Sequence Length: 163
Domain: In contrast to other members of the Ras family, the members of the KappaB-Ras subfamily do not contain the conserved Gly and Gln residues in positions 13 and 65, which are replaced by His and Leu residues, respectively, and are therefore similar to the constitutively active forms of oncogenic forms of Ras. This suggests that members of this family are clearly different from other small GTPases proteins.
Subcellular Location: Cytoplasm
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B0VHH0 | MEPLILTAAITGAETTRADQPNLPITPEEQAKEAKACFEAGARVIHLHIREDDGRPSQRLDRFQEAISAIREVVPEIIIQISTGGAVGESFDKRLAPLALKPEMATLNAGTLNFGDDIFINHPADIIRLAEAFKQYNVVPEVEVYESGMVDAVARLIKKGIITQNPLHIQFVLGVPGGMSGKPKNLMYMMEHLKEEIPTATWAVAGIGRWHIPTSLIAMVTGGHIRCGFEDNIFYHKGVIAESNAQLVARLARIAKEIGRPLATPEQAREILALNK | Function: Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminohexanoate (KAH) and acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. The reaction involves the deprotonation of KAH, the nucleophilic addition onto acetyl-CoA and the intramolecular transfer of the CoA moiety.
Catalytic Activity: (5S)-5-amino-3-oxohexanoate + acetyl-CoA = (3S)-3-aminobutanoyl-CoA + acetoacetate
Sequence Mass (Da): 30222
Sequence Length: 276
Pathway: Amino-acid degradation; L-lysine degradation via acetate pathway.
EC: 2.3.1.247
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Q8RHX2 | MMEKLIITAAICGAEVTKEHNPAVPYTVEEIAREAESAYKAGASIIHLHVREDDGTPTQDKERFRKCIEAIREKCPDVIIQPSTGGAVGMTDLERLQPTELHPEMATLDCGTCNFGGDEIFVNTENTIKNFGKILIERGVKPEIEVFDKGMIDYAIRYQKQGFIQKPMHFDFVLGVQMSASARDLVFMSESIPEGSTWTVAGVGRHQFQMAALAIVMGGHVRVGFEDNVYIDKGILAKSNGELVERVVRLAKELGREIATPDEARQILSLKK | Function: Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminohexanoate (KAH) and acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. The reaction involves the deprotonation of KAH, the nucleophilic addition onto acetyl-CoA and the intramolecular transfer of the CoA moiety. It can also use beta-alanyl-CoA as substrate.
Catalytic Activity: (5S)-5-amino-3-oxohexanoate + acetyl-CoA = (3S)-3-aminobutanoyl-CoA + acetoacetate
Sequence Mass (Da): 30137
Sequence Length: 272
Pathway: Amino-acid degradation; L-lysine degradation via acetate pathway.
EC: 2.3.1.247
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P47114 | MFNHDWKYSINSKTFADLNIELFRNHKFKTVLNYIIGVVGWNGLKLALFVSDIYTCIKLLAFNSWSNNIIKPYLPFKISKWLFSGCILASIVLLIWEAIAGMRIYKTGNISLTYVNNFSRNLNSVLNYSKFCVYNMIERKGFRQKMTFFTFFQLKDCIRLIFTDTPRQVINGLTLWSVLVTVNKNEDLGDLESFTGLINKIKNIGQTNHEEAVILSLMLFSFIIWALFVFKFLLAVICSIFVYYKIINDQEYSGLREYICVTVSENVDELVERQRKKENDDTIYKTGLLESQTFDDFKEVENKIETSFNDTSYASNNDSMIELIERRPEYKSQDVCGPIPTMKKTETMESFVDNGNPQYTTRFSAILDSPYINSYESNDIKKAKIQSRSVNTPKYEDLSSSDIFNKIHSAGQLKSTTSMEFHGPLDSMPNTTNNIRNFNSNSSRPRPPPLQTKSSINSKADSNDNGRIYTPMKAYFREPDLPRKGLLEDEDRTYNYT | Function: Low affinity potassium transporter that, with PRM6/KCH2, participates in high-affinity Ca(2+) influx system (HACS) activation during the response to mating pheromone . Directly promotes K(+) influx and HACS may electrochemically respond to this K(+) influx . KCH1 and KCH2 act at the apex of the calcium signaling pathway that is used for survival during prolonged exposures to mating pheromones .
Catalytic Activity: K(+)(in) = K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57517
Sequence Length: 497
Subcellular Location: Vacuole membrane
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P31069 | MSHWATFKQTATNLWVTLRHDILALAVFLNGLLIFKTIYGMSVNLLDIFHIKAFSELDLSLLANAPLFMLGVFLVLNSIGLLFRAKLAWAISIILLLIALIYTLHFYPWLKFSIGFCIFTLVFLLILRKDFSHSSAAAGTIFAFISFTTLLFYSTYGALYLSEGFNPRIESLMTAFYFSIETMSTVGYGDIVPVSESARLFTISVIISGITVFATSMTSIFGPLIRGGFNKLVKGNNHTMHRKDHFIVCGHSILAINTILQLNQRGQNVTVISNLPEDDIKQLEQRLGDNADVIPGDSNDSSVLKKAGIDRCRAILALSDNDADNAFVVLSAKDMSSDVKTVLAVSDSKNLNKIKMVHPDIILSPQLFGSEILARVLNGEEINNDMLVSMLLNSGHGIFSDNDELETKADSKESAQK | Function: K(+)-specific ion channel. May play a role in the defense against osmotic shock.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46063
Sequence Length: 417
Subcellular Location: Cell inner membrane
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Q9JJ57 | MGAVMGTFSSLQTKQRRPSKDIAWWYYQYQRDKIEDELEMTMVCHRPEGLEQLEAQTNFTKRELQVLYRGFKNECPSGVVNEETFKQIYAQFFPHGDASTYAHYLFNAFDTTQTGSVKFEDFVTALSILLRGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKAIYDMMGKYTYPVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESCQEDDNIMRSLQLFQNVM | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. Modulates KCND2/Kv4.2 currents . In vitro, modulates KCND1/Kv4.1 currents (By similarity). Increases the presence of KCND2 at the cell surface.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26831
Sequence Length: 227
Subcellular Location: Cell membrane
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Q8R426 | MGAVMGTFSSLQTKQRRPSKDIAWWYYQYQRDKIEDDLEMTMVCHRPEGLEQLEAQTNFTKRELQVLYRGFKNECPSGVVNEETFKQIYAQFFPHGDASTYAHYLFNAFDTTQTGSVKFEDFVTALSILLRGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKAIYDMMGKYTYPVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESCQEDDNIMRSLQLFQNVM | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels . Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner . Modulates KCND2/Kv4.2 currents . In vitro, modulates KCND1/Kv4.1 currents (By similarity). Increases the presence of KCND2 at the cell surface .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26817
Sequence Length: 227
Subcellular Location: Cell membrane
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Q9NS61 | MRGQGRKESLSDSRDLDGSYDQLTGHPPGPTKKALKQRFLKLLPCCGPQALPSVSETLAAPASLRPHRPRLLDPDSVDDEFELSTVCHRPEGLEQLQEQTKFTRKELQVLYRGFKNECPSGIVNEENFKQIYSQFFPQGDSSTYATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTVDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIYDMMGKYTYPALREEAPREHVESFFQKMDRNKDGVVTIEEFIESCQKDENIMRSMQLFDNVI | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3 trafficking to the cell surface. May be required for the expression of I(To) currents in the heart (By similarity).
PTM: Palmitoylated. Palmitoylation enhances association with the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 30907
Sequence Length: 270
Subcellular Location: Cell membrane
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Q9JM59 | MRGQGRKESLSESRDLDGSYDQLTGHPPGPSKKALKQRFLKLLPCCGPQALPSVSETLAAPASLRPHRPRPLDPDSVEDEFELSTVCHRPEGLEQLQEQTKFTRRELQVLYRGFKNECPSGIVNEENFKQIYSQFFPQGDSSNYATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLSWAFNLYDLNKDGCITKEEMLDIMKSIYDMMGKYTYPALREEAPREHVESFFQKMDRNKDGVVTIEEFIESCQQDENIMRSMQLFDNVI | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner . In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3 trafficking to the cell surface. Essential for the expression of I(To) currents in the heart (By similarity). Required for normal protein levels of KCND2 in the heart ventricle (By similarity).
PTM: Palmitoylated. Palmitoylation enhances association with the plasma membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 30933
Sequence Length: 270
Subcellular Location: Cell membrane
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Q6PIL6 | MNVRRVESISAQLEEASSTGGFLYAQNSTKRSIKERLMKLLPCSAAKTSSPAIQNSVEDELEMATVRHRPEALELLEAQSKFTKKELQILYRGFKNECPSGVVNEETFKEIYSQFFPQGDSTTYAHFLFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIYDMMGKCTYPVLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIESCQKDENIMRSMQLFENVI | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates KCND2 channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner . Modulates KCND3/Kv4.3 currents . Isoform 4 does not increase KCND2 expression at the cell membrane . Isoform 4 retains KCND3 in the endoplasmic reticulum and negatively regulates its expression at the cell membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28729
Sequence Length: 250
Domain: The KIS (K-channel inactivation suppressor) domain is required for converting A-type Kv4 current to a slowly inactivating delayed rectifier potassium current.
Subcellular Location: Cell membrane
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Q6PHZ8 | MNVRRVESISAQLEEASSTGGFLYAQNNTKRSIKERLMKLLPCSAAKTSSPAIQNSVEDELEMATVRHRPEALELLEAQSKFTKKELQILYRGFKNECPSGVVNEETFKEIYSQFFPQGDSTTYAHFLFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIYDMMGKCTYPVLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIESCQKDENIMRSMQLFENVI | Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels, such as KCND2/Kv4.2 and KCND3/Kv4.3 . Modulates channel expression at the cell membrane, gating characteristics, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28756
Sequence Length: 250
Domain: The KIS (K-channel inactivation suppressor) domain is required for converting A-type Kv4 current to a slowly inactivating delayed rectifier potassium current.
Subcellular Location: Cell membrane
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Q8NCM2 | MPGGKRGLVAPQNTFLENIVRRSSESSFLLGNAQIVDWPVVYSNDGFCKLSGYHRADVMQKSSTCSFMYGELTDKKTIEKVRQTFDNYESNCFEVLLYKKNRTPVWFYMQIAPIRNEHEKVVLFLCTFKDITLFKQPIEDDSTKGWTKFARLTRALTNSRSVLQQLTPMNKTEVVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCAFKTTWDWVILILTFYTAIMVPYNVSFKTKQNNIAWLVLDSVVDVIFLVDIVLNFHTTFVGPGGEVISDPKLIRMNYLKTWFVIDLLSCLPYDIINAFENVDEGISSLFSSLKVVRLLRLGRVARKLDHYLEYGAAVLVLLVCVFGLVAHWLACIWYSIGDYEVIDEVTNTIQIDSWLYQLALSIGTPYRYNTSAGIWEGGPSKDSLYVSSLYFTMTSLTTIGFGNIAPTTDVEKMFSVAMMMVGSLLYATIFGNVTTIFQQMYANTNRYHEMLNNVRDFLKLYQVPKGLSERVMDYIVSTWSMSKGIDTEKVLSICPKDMRADICVHLNRKVFNEHPAFRLASDGCLRALAVEFQTIHCAPGDLIYHAGESVDALCFVVSGSLEVIQDDEVVAILGKGDVFGDIFWKETTLAHACANVRALTYCDLHIIKREALLKVLDFYTAFANSFSRNLTLTCNLRKRIIFRKISDVKKEEEERLRQKNEVTLSIPVDHPVRKLFQKFKQQKELRNQGSTQGDPERNQLQVESRSLQNGASITGTSVVTVSQITPIQTSLAYVKTSESLKQNNRDAMELKPNGGADQKCLKVNSPIRMKNGNGKGWLRLKNNMGAHEEKKEDWNNVTKAESMGLLSEDPKSSDSENSVTKNPLRKTDSCDSGITKSDLRLDKAGEARSPLEHSPIQADAKHPFYPIPEQALQTTLQEVKHELKEDIQLLSCRMTALEKQVAEILKILSEKSVPQASSPKSQMPLQVPPQIPCQDIFSVSRPESPESDKDEIHF | Function: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a non-inactivating outward rectifying current. Channel properties may be modulated by cAMP and subunit assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 111877
Sequence Length: 988
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: Membrane
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O54853 | MPVRRGHVAPQNTYLDTIIRKFEGQSRKFLIANAQMENCAIIYCNDGFCELFGYSRVEVMQRPCTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDGAVIMFILNFEDLAQLLAKSSSRSLTQRLLSHSFLGSEGSHSRPSGQGPGPGRGKYRTVSQIPQFTLNFVEFNLEKHRSGSTTEIEIIAPHKVVERTQNVTEKVTQVLSLGADVLPEYKLQAPRIHRGTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLSDQDESQRGTCGYTCSPLTVVDLIVDIMFVVDIVINFRTTYVNTNDEVVSHPRRIAVHYFKGWFLIDMVAAIPFDLLIFRTGSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNVERPYLEPKIGWLDSLGAQLGKQYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFGNVSPNTNSEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLHRALLQHCPAFRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDDVVVAILGKNDIFGEPASLHARPGKSSADVRALTYCDLHKIHRADLLEVLDMYPAFADTFWNKLEVTFNLRDADGGLQSTPRQAPGHQDPQGFFLNDSQSGAAPSLSISDTSALWPELLQQMPPSPPNPRQDLDCWHRELGFKLEQLQAQMNRLESRVSSDLSRILQLLQHPQGRPSYILGASASSDLASFPETSVTRSSESTLLVGHVPSAQTLSYGDLDDHIQTPRNFSPRTPHVAMAMDKTLVPSSEQEQPGGLLSPLASPLRPLEVPGLGGSRFPSLPEHLSSVPKQLEFQRHGSDPGFTRS | Function: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, rectifying current. Channel properties may be modulated by cAMP and subunit assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105706
Sequence Length: 950
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: Membrane
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P48048 | MNASSRNVFDTLIRVLTESMFKHLRKWVVTRFFGHSRQRARLVSKDGRCNIEFGNVEAQSRFIFFVDIWTTVLDLKWRYKMTIFITAFLGSWFFFGLLWYAVAYIHKDLPEFHPSANHTPCVENINGLTSAFLFSLETQVTIGYGFRCVTEQCATAIFLLIFQSILGVIINSFMCGAILAKISRPKKRAKTITFSKNAVISKRGGKLCLLIRVANLRKSLLIGSHIYGKLLKTTVTPEGETIILDQININFVVDAGNENLFFISPLTIYHVIDHNSPFFHMAAETLLQQDFELVVFLDGTVESTSATCQVRTSYVPEEVLWGYRFAPIVSKTKEGKYRVDFHNFSKTVEVETPHCAMCLYNEKDVRARMKRGYDNPNFILSEVNETDDTKM | Function: In the kidney, probably plays a major role in potassium homeostasis. 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 channel is activated by internal ATP and can be blocked by external barium.
PTM: Phosphorylation at Ser-44 by SGK1 is necessary for its expression at the cell membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44795
Sequence Length: 391
Subcellular Location: Cell membrane
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P63252 | MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKEGKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEDDSENGVPESTSTDTPPDIDLHNQASVPLEPRPLRRESEI | Function: 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 . Can be blocked by extracellular barium or cesium .
PTM: S-nitrosylation increases the open probability and inward rectifying currents.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48288
Sequence Length: 427
Subcellular Location: Membrane
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O15554 | MGGDLVLGLGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFLVKCTISISTFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPAPVRGPPCVQDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIQYTKEMKESAARVLQEAWMFYKHTRRKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMVDISKMHMILYDLQQNLSSSHRALEKQIDTLAGKLDALTELLSTALGPRQLPEPSQQSK | Function: Forms a voltage-independent potassium channel that is activated by intracellular calcium . Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells . Plays a role in the late stages of EGF-induced macropinocytosis .
PTM: Phosphorylation at His-358 by NDKB activates the channel, and conversely it's dephosphorylation by PHPT1 inhibits the channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47696
Sequence Length: 427
Subcellular Location: Cell membrane
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Q7KVW5 | MSIQKLNDTTNSGYVSSEETDSLLVSSSNPSKGGGRTALLRQVKSNSTNGPTTGASTSSSGSVSGGGGGSGSGGGSASGSAAGASKPTLMRQDRTSTYLTSPQQSQHARMGSEESMRGGASGAAGHDEDVEQGLVRSSIVPDIEVHEEDQEQHSQQLNATTMATMTNNQQQQQPTISIMNLSLKPGDSHSHSSSPGSHPNLGTSSYQNLASSIPPSVPSRCRACRNCSRRASTTPTTLIDRSASRDSVKSAFQQGNLSGSMAICISNSALPQQQQLQQQYHLQQQQQQHYQLQQHHLHQQQLQQSQQQVPPVLITSSPTNGSRIIRQSSQPESSSTAICCGPHSACVGHAHSHSHTVPNVSLKQLRESSGDGIAGIAADSLRINGGMRPFKQLRKPASTLSIPGSMKTPSIANREQISSGCNEEAAEALVGIHSDYPRYEMYMEERALTGGNTSRKPSTNSAKHKPNVGYRLGKRKALFEKRKRISDYALVMGMFGIIVMVIENELSSAGVYTKASFYSTALKTLISVSTVILLGLIVAYHALEVQLFMIDNCADDWRIAMTWQRISQIGLELFICAIHPIPGEYYFQWTTKLANKNKTIGTEMVPYDVALSLPMFLRLYLICRVMLLHSKLFTDASSRSIGALNRINFNTRFVLKTLMTICPGTVLLVFMVSLWIIASWTLRQCERFHDEEHANLLNSMWLTAITFLCVGYGDIVPNTYCGRGITLTCGMVGAGCTALLVAVVSRKLELTRAEKHVHNFMMDTQLTKRLKNAAANVLRETWLIYKHTRLVKRVNPGRVRTHQRKFLLAIYALRKVKMDQRKLMDNANTITDMAKTQNTVYEIISDMSSRQDAIEERLTNLEDKMQSIQEHMESLPDLLSRCLTQHQERIEQRRNFLHPDTAAVAPIQAPTPQSMFNAAPMLFPHSS | Function: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101868
Sequence Length: 927
Subcellular Location: Membrane
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P51787 | MAAASSPPRAERKRWGWGRLPGARRGSAGLAKKCPFSLELAEGGPAGGALYAPIAPGAPGPAPPASPAAPAAPPVASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGWKCFVYHFAVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKKKKFKLDKDNGVTPGEKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFMRTNSFAEDLDLEGETLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVTQLDQRLALITDMLHQLLSLHGGSTPGSGGPPREGGAHITQPCGSGGSVDPELFLPSNTLPTYEQLTVPRRGPDEGS | Function: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon . Associates with KCNE beta subunits that modulates current kinetics . Induces a voltage-dependent current by rapidly activating and slowly deactivating potassium-selective outward current . Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity) . Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current . When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions . This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity). When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current . When associated with KCNE4, inhibits voltage-gated potassium channel activity . When associated with KCNE5, this complex only conducts current upon strong and continued depolarization . Also forms a heterotetramer with KCNQ5; has a voltage-gated potassium channel activity . Binds with phosphatidylinositol 4,5-bisphosphate . KCNQ1-KCNE2 channel associates with Na(+)-coupled myo-inositol symporter in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability.
PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74699
Sequence Length: 676
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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P97414 | MDTASSPPSAERKRAGWSRLLGARRGSAVVKKCPFSLELAEGGPEGSTVYAPIAPTGAPGLAPPMSTPVSPAPAPADLGPRPRVSLDPRVSIYSARRPLLARTHIQGRVYNFLERPTGWKCFVYHFTVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGIWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRIEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSATWKIYVRKPARSHTLLSPSPKPKKSVMVKKKKFKLDKDNGMSPGEKMFNVPHITYDPPEDRRPDHFSIDGYDSSVRKSPTLLEVSTPHFLRTNSFAEDLDLEGETLLTPITHVSQLRDHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFIPISEKSKDRGSNTIGARLNRVEDKVTQLDQRLVIITDMLHQLLSMQQGGPTCNSRSQVVASNEGGSINPELFLPSNSLPTYEQLTVPQTGPDEGS | Function: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity) . Associates with KCNE beta subunits that modulates current kinetics (By similarity) . Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity) . Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity) . Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion . Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion . When associated with KCNE2, forms an heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity). Also forms a heterotetramer with KCNQ5; has a voltage-gated potassium channel activity (By similarity). Binds with phosphatidylinositol 4,5-bisphosphate (By similarity). KCNQ1-KCNE2 channel associates with Na(+)-coupled myo-inositol symporter in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability.
PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74514
Sequence Length: 668
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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Q9MYS6 | MAAASTPPRAERKRXSWSRLPGAQRESAGLAKKCPFSLELAESGPPSSALYAPVSPPSAPEPAPPASPASPAPPAADQGPQPPVSLDPRVSIYSVRRPLLARTHIQGRVYNFLERPTGWKCFAYHFTVFLIVLVCLIFSVLSTIEQYATLATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSATWKIYIRKPTRGHALLSPSPKPKKSAMVKKKKFKLDKDNGVSPGEKTLPVPQITCEPPEERRPDHFPVDSHDGSVRKSPALLEVSTPQFLRTNSFAEDLDLEGETLLAPITHVSQLREHHRATVKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFVPISEKSKDRGSNSIGARLNRVEDKVTQLDQRLVLIADMLQQLLALHQGRCHGGAHPAQARDGDPADPELFLPTYEQLTVPRRDPEEGS | Function: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity). When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity). Also forms a heterotetramer with KCNQ5 that has a voltage-gated potassium channel activity (By similarity). Binds with phosphatidylinositol 4,5-bisphosphate (By similarity). KCNQ1-KCNE2 channel associates with Na(+)-coupled myo-inositol symporter in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability.
PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73636
Sequence Length: 661
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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O73925 | MSSEVKSRWSGSGSQKSGTARKPTMLEMAENAASRHYEPVPLPLQRSNSPDSSTDKNPESRAADSRAEVIINPDIPPKAIALPLSRYRGRNPFFSKVNIQGRTYNFLERPTGWKCFIYHFTVFLIVLVCLIFSVMSTIEQYHYFANRALVWMEIVLVVFFGTEYIVRLWSAGCRSKYVGFWGRLRFARKPISIIDLIVVVASVIVLCVGSNGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVDDSGSQQFGSYADALWWGVVTVTTIGYGDKVPQTWIGRTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTSWRCHAAENHESATWKMYVRQPTKFYVASPSPKTKKSVGKRKKLKTDKDNGLNSEKSLNVPNITYDHVVDKDDRKFENSNIDGYDSSVKKSLGILDVNSGALSRANSYADDLDFIEGEPVLAPITHVSQLRESHRVTVKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSLGKPTMFLSVSEKSQDRGKNTIGARLNRVEEKFVHMDQKLNTITDMLHHLVAHQQGHPHPQTQPQAQGTVVQAVASTHSSLPSYEQLTVRRKDQDNQPDL | Function: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74687
Sequence Length: 660
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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Q9Z351 | MVQKSRNGGVYPGTSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSVLSKPRTGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRPKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPMYRLIPPLNQLELLRNLKSKSGLTFRKEPQPEPSPSQKVSLKDRVFSSPRGMAAKGKGSPQAQTVRRSPSADQSLDDSPSKVPKSWSFGDRSRTRQAFRIKGAASRQNSEEASLPGEDIVEDNKSCNCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRIDMIVGPPPPSTPRDKKYPTKGPTAPSRESPQYSPRVDHIVGRGPTITDKDRTKGPAETELPEDPSMMGRLGKVEKQVLSMEKKLDFLVSIYTQRMGIPPAETEAYFGAKEPEPAPPYHSPEDSRDHADKHGCIIKIVRSTSSTGQRNYAAPPAIPPAQCPPSTSWQQSHQRHGTSPVGDHGSLVLRLERSAGMMSCH | Function: Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability . KCNQ2-KCNQ3 channel is selectively permeable to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). Associates with Na(+)-coupled myo-inositol symporter SLC5A3 forming a coregulatory complex that alters ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation (By similarity).
PTM: KCNQ2/KCNQ3 heteromeric current can be increased by intracellular cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the N-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84450
Sequence Length: 759
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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Q8K3F6 | MGLKARRAAGAAGGGGGEGGGGGGGAANPAGGDSAVAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGREEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEMDAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQEQHRQKHFEKRRKPAAELIQAAWRYYATNPNRLDLVATWRFYESVVSFPFFRKEQLEAAASQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDAGTGDPMAEDRGYGNDFLIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTYPSQQSPRNEPYVARAATSETEDQSMMGKFVKVERQVHDMGKKLDFLVDMHMQHMERLQVHVTEYYPTKGASSPAEGEKKEDNRYSDLKTIICNYSETGPPDPPYSFHQVPIDRVGPYGFFAHDPVKLTRGGPSSTKAQANLPSSGSTYAERPTVLPILTLLDSCVSYHSQTELQGPYSDHISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPSGGSSWMREKRYLAEGETDTDTDPFTPSGSMPMSSTGDGISDSIWTPSNKPT | Function: Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. KCNQ2-KCNQ3 channel is selectively permeable to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). Associates with Na(+)-coupled myo-inositol symporter SLC5A3 forming a coregulatory complex that alters ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation.
PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is inhibited by USP36.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96852
Sequence Length: 873
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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Q88M04 | MNSMAPVITIDGPSGSGKGTVAGLIARELGWKLLDSGALYRLLAFNASNHGVDLTNEELLTKLAAHLDVQFIAAEPGKLQQIILEGEDVSNVIRTETVGAGASMVASLPAVRDALLVRQREFREVPGLIADGRDMGTVVFPDAPLKVFLTASAEERARRRYLQLKGKGEDVSLSSLLDEIRARDERDTQRAVAPLKPAADAIQLDSTELSIEQVLQRIRSEIAQRDLI | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24691
Sequence Length: 228
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q885T2 | MKIKAPVITIDGPSGSGKGTVAGLLAKKLGWCLLDSGALYRLLAFAARNHGVDLTNEEALKLLAAHLDVQFETTAAGQGQRIILEGEDVTQAIRNEQIGSGASQVASLPAVRDALLMRQRAFQEEPGLVADGRDMGTVVFPDAPLKVFLTASAEERARRRYLQLKAKGDDVSLSSLLDEICARDERDTQRAVAPLKPAHDAIQLDSTELSIEQVLERILSEIALRDIAG | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24634
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q8ZTJ1 | MVVIAVSGQPGSGKTTIAREIARVLGLPLVSSGLLFREMAARMGMDFIEFHKYAETNPDIDKKVDSLAIERAKAGDVVLEGHLTAWIVRPYADVCIYLKASLETRARRVALRDGKSLQDALREVAEREELNRRRYLSIYGIDINDLSIFDLVLDTSHLSVNDAVRISLDYTCTSLSFKYSRKIC | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 20611
Sequence Length: 184
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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A1RRJ5 | MVVIAISGQPGSGKTTVAREVARVLNLPLVSSGSLFRELAAKMGIDFIEFHKYAEKNPDIDKVVDSMAIERAKAGNVVLEGHLAAWIVRPYADICIYLKASSEIRARRISIRDKKSFEDALREVREREELNRRRYLSLYNIDINDLSVFDLVLDTSYLSINDAIRISLDYICTVLGFKYSRKFC | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 20895
Sequence Length: 184
Subcellular Location: Cytoplasm
EC: 2.7.4.25
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Q8Y0Y5 | MSDVAAFTAYPVIAIDGPTASGKGTVAHQIADLLGFHYLDSGSLYRLVAFVSIRENIDDHDVNSLVRIASELDVRFKADHIWLKGEDVSLALRHESVGNQASAIAVHGPVREALRARQRAFLEAPGLVADGRDMGTVIFPEAVLKVFLTASVQARAERRYKQLIAKGFSATVESLSRDLEARDLRDRTRSVAPLRPAEAARLLDSSDMSVDEVVAQVLDWYRQVQGVKAR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25221
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q67NU0 | MTDGTRELVIAMDGPAGAGKSTVARIVANRLGYLYIDTGAMYRALALKALRLGIPETDAAALADLADATEVELQRAPDGGNRVLLDGEDVTAEIRSPAVSAVVSQVSAVPRLRQRLIEVQRSMARAGGVVMDGRDIGSYVLPHADRKFYITASLQERARRRVAQLRAEGHEADLAAVEAEIARRDEQDMNKGVHSLVQLPESIVIDTTGKRVDEVVEEILRHCRRT | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24562
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
A0LK48 | MNNATIIAIDGPAGAGKSTVSRLLAKELGYTYLDSGAMYRALAWALQREGVDLEAEAHVARALPELPLEFSTRGGSLLIHCGGKALEDELRNPEMAAYASRISQMRAVRTFLTEWQRKLAEAGKVVAEGRDTATVVFPHAGVKVFLTADPAARAGRRHAEYLAKGIRVDYAVLERQIRERDEADSTRCLAPLRPADGAVILDTSDLDISEVMSRLMDLIREKSRG | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24577
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q9HIT3 | MRITIAGKIGSGKSTVSSELSRITGYTVYSSGTFFRETARKMNMSIEDFNVYSESHPEADYYTDETQKAFMQANDNIIVEGRLAGWISYLNGINAFRIFLYATYYTRLVRFAGRENIDIDSARDLMEKREKSEKERYRKLYGIDVDDLSIYDIVVNTEFMKPPEIAVYIANRIDEMSRKDIFTPRILR | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 21864
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q5JJE3 | MPKGCLVITVSGLAGSGTTTLCRNLAKHYGFKHIYAGLIFRQMAKEMGMTLEEFQKYVELHPEIDREIDRRQIEAAKECNVVIEGRLAGWMVKNADLKIWLDAPIMERAKRVAKREGISVEEAFVKIAEREKQNRKRYLNLYGIDIEDKSIYDLIINTAHWGPDGVFAIVKAAIDHLSPSGDAGEDEKEKEVG | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 21790
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
Q9X1F6 | MGFQIAIDGPAASGKSTIAKLLAEKLGFDHLNTGATYRAVAVYLHEKGLSSSSAEEEIENVLKDLKIDYVNGRVYINGEDYTEKIQSPEAGVLASNFARLEVVRRHLVRIQREICDDKNIVVEGRDIGTVVLPNAHLKIFLTASLEARVERKLKEYQKRGLKVTKEEVERELISRDEQDSKRNVAPLKPAEDAVIIDTTSMSVEEVLDRILKLVRERMNT | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 24702
Sequence Length: 220
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
B5YH69 | MKKVVAIDGPSGAGKSTVSKEIAKALGFQYLDTGALYRAVAYYFSIKFNYIDDFSLLTEQEIEEELKNIKIHYKNGRVFLSGEDVSDFIRDPKIGEITSQLSTQKVVRDFLMPLQRSFAEKVDIVAEGRDMTTVVFPDAWKKFYLDASPQVRAKRRFEQLIQSGKKISFEEALRDVIERDKRDCSRENAPLRLSKDAFYIDTSELTLQEVISIVLKKVAEDA | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25338
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
O83362 | MRIAVSGASGCGNTTVSALLAERLGLPLVNYTFRNIARELGISLSEVLERARTDNHFDKAVDARQLCLAMRSSCVVGSRLAIWLVKDAALKVYLLASLKERVKRVLQREGGDVQDVERFTSMRDAEDMSRYKKLYRIDNTNYSFADLVLNTEGCDQETVVSIIIEMLRARGIAW | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 19505
Sequence Length: 174
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
B5ZBF2 | MKKYINVAIDGPSGSGKSTAAKGLANKLGFLYINTGLMYRAYAYFLNENNLDINTNETACIEAIKNARFIFNGDDVKIDDQDVSDILRSNDVAMLASVVAANAKIRNLATNEQRKIASENNVVMDGRDIGSIVLVDADLKFYLNTSIQTRAKRRLAQNKDIEKLDYESIYNDIKERDYRDMTRDIAPLKKAIDAIEIFNDNMNLDQCVAHLYEIYLNKIKKS | Catalytic Activity: ATP + CMP = ADP + CDP
Sequence Mass (Da): 25063
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 2.7.4.25
|
O86224 | MHQFQQDNQYFIFNFDRTFEQATEFFQAEFWQKQERVIGSAKGRGITYFLQTEDWFGVNCALRHYYRGGLWGKLNKDRYRFSALETTRSFAEFHLLQRLYEAGLPVPKPIAARIQKGKLGICYQADILTEKIENAQDLTALLQTQTLPKETWMQIGRLIRKLHDLQICHTDLNAHNILLQQTEQGQKCWLLDFDKCGEKSADFWKVQNLNRLKRSFEKEVGRMNIQFTEQNWADLTSAYHQ | Function: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position. To a lesser extent, can use GTP instead of ATP as substrate.
Catalytic Activity: an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28569
Sequence Length: 241
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.1.166
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P58551 | MQIIQTKQQYICYNPELLTETPEMAFSSEFWQQQNKIIGSAQGRGTTWFVQGEKLAMALRHYRRGGLFGKLVADSYLFSGWDKTRSVAEFSLLNHLIAHQVNVPKPVAARAVRLGWFRYQADILVEKIANSRDLVGILGQETLSQQVWFDVGAMIKRMHDAGVCHTDLNCHNIILDDHKTVWIIDFDKCYRLEGANWQEKNLARLHRSFIKEQGKRGILFNEDNWQWLCKVIRVNGNKGQ | Function: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position.
Catalytic Activity: an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27780
Sequence Length: 240
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.1.166
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Q9KVB9 | MIQTFNDAQQKVWFDDALLHEDPSQCCNPEFWQQNGKVLGSATGRGTTWFVQLQQTQGALRHYRRGGLFGKLVADSYWFTGWEKTRSYQEFMLLNHLRDAGVNVPRPIAARVQKHGLLYKADLLSEKVPNARDLVSILQESPISDELYRKIGREIRKMHDAQVNHTDLNIHNILIDDQEKVWIIDFDKCYVQIGDSWKQGNLKRLKRSFEKEVCKRGINWSLEAFAIISSYKHEE | Function: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position.
Catalytic Activity: an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27408
Sequence Length: 235
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.1.166
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Q7NN41 | MAFEGVLQIVATLVLMVAIVPFFGTYMARVFQGESTWLDRVLGPIENLVYRLGGVRPELTMDWWSYARAVLASNAAMFVPVFAVLLLQGSLPLNPNGISGMSWDLALHTAISFLTNTNQQHYSGETGASHLAQMVCFQFLMFTSAATGLAVGIAFIRGLLGKPLGNFYVDLTRSVSRILMPISIAFAVVLLSQGVPQSLGGTTEAQLVDPYRTEQDGKREQVTAQKLVSGPFASMESIKELGENGGGSYGINSAHPYENPNPFTNLLEILLLLAVPTSLIYTFGVLANNKKQGWVLFGTIFVLFVGLVGVAALGEYWGNPTVNALLGSANPNFEGQEVRFGWAQSALFATATTGTMTGAVNAMHDSLTPLAGLVTLFNLCLQVIWGGQGTGIAYILVFLIIAVFLTGLMVGRTPEIFGRKLEKREVALASIIFLVHPVIILVPTAIALAIPGLAGNSNPGFHGLTQVVYEYASAAANNGSGFEGLGDATPWWNLSTSVVLLLGRYAPIVALLALAGGLQRKQPVPETPGTLRTDTVLFGSVTAGTILILGALTFFPVFALGPIAEWIANLAGKTL | 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 binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61127
Sequence Length: 575
Subcellular Location: Cell inner membrane
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B0R9L9 | MASPPPIVEYAVFFTILAVLVFVAGEYLAWVYREQANSDHRPPGYLSWFERLDEIFTPIENGLYRLSGINPRREMTWKGYLKAVLVFNVCIWVLLFVVLMFQDALPMNFVGVGGESWDLAFHTASSFTSNTNQQHYSGETLSVFTHTFGIGIAMFLTPATGLALMPAFARAFTNKEDPRLGNFYENVVRGLVRFLLPISLLIAIILMAEGSVQTILGGQLTANTFTMGIQNIRIGPHAGIEAIKMFGTNGGGINAANAATAFENPTPLSNLVLTLAMPIGTFSAIYAWGAWVGNRSHGVAIVAAFFVIYMALTGVAVVGETGTNAGMVVTGNGLHVDQTVGNMEGKETRFGPTASAIWGLSTTGTTNGGVNSMHNSWTALGAFSLLFAFATNNISNGVGTGLLNILMFVILTAFIGALMIGRRPQYLGKKLEWQEMRYVFVVILVLPILVLIPQAAAVVYQGAIDSMNNPGFRGFSEVLYEFFSASANNGSGFEGLGDGTLFFNLVNGVQVLLARYVPITAQLAIAGYLANKKVSPESKGSLDTDTPAFVGLLIGVIIIVSALVFLPALVFGPIGELLSGGI | 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 binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel (By similarity). The Kdp system is essential for growth under K(+) limitation, and for survival under desiccation and salt crystal inclusion .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62353
Sequence Length: 582
Subcellular Location: Cell membrane
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B4U8E3 | MNIFLDIFSFILFFGILTIISPILGKYMADIYEGRVHPSLKPIRYVEKTIYKILGIDESKEMNWKEYLYALLSFNFLGFLVLFLTLLFQKYLPLNQYHIPNMSWDLAFNTAVSFVTNTNWQAYAGETQATYFSQITGLALQNFLSAASGIVVALVLIRAFARKNTIYLGNFYVDFTRTILYVLLPVAFFSALFLVSQGVIQNFSHYKTIELLEPYKDSKNIITTQTLPMGPVASQEAIKLLGTNGGGFFNANSAHPFENPTPLSNVFEAFLIILIPASLVFTFGYMIKDKRQGWFLYSVMLFVLMLFMGIQYYFEWFGNPIVKKLGIEGPYLIGKELRFGIGGTVLFSSITTATSCGAVNSMLDSFTPLGGLVPMSLISLGEIIFGGVGSGLYGMIAMVIIAVFVAGLMIGRTPEYLNKKIESREMWSSVVITLVSGITALLLTTLALYTKWGLSSMSNPGPHGLSEVLYAYISTSNNSGSAFAGLNANTVFYNITTGLAMLIGRFIPIIAVFYMASSLSLKKHVPPSPGTLPTHTLVFGVWLVFIIIVVGALTFLPAFSLGPILEHMLMLEGVTL | 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 binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63652
Sequence Length: 576
Subcellular Location: Cell inner membrane
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Q8F1M1 | MVTEWIQLLIFLFALLIFSPLFGLGLYKVYLYKTSGFEKFLYKICGIDPNRNMDWKEYALSLLVFNFFGFLLLFLILFFQNYLPLNPENFPGLVWDLAFNTAVSFATNTNWQAYSGESTLSFFSQMAGLTTQNFLSATTGLCVLLALSRGISVNYNVFALGNFWKDMIRGTLYVLLPLSFIFALFLVGFGVVQTFSESVSAITLEGNTQIIPLGPVASQVAIKQLGTNGGGYFGVNASHPFENPSPISNFLQMFSILILPGACVFLYGRITGSIRHAWAIFSVMFTILCVGILIVWTFESSWNPISGTLGFWEGKEIRFGILNSSIWEVATTVASNGSVNSMHDSFSPIGGLVGILNIQLREIVFGGVGAGMYGMILFVLLTVFLSGIMVGRSPEYLGKKIEKREIQMSILGILLPSTIILLFTAISVSVSDALSSLTNRGPHGLSEILYAFSSGAGNNGSAFAGLNANTTYYNVMIAIAMILGRFGVILPVLVIAGSLAQKKRSEIVSEGSFSTEGGTFYILLLSVIIIVGALTFFPVLTIGPILEHFIMFQNLTF | 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 binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60877
Sequence Length: 557
Subcellular Location: Cell inner membrane
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B3DWJ8 | MKIFSLLILSLKITFLLTLLLGGLYPLAVFIVGKIFFPYQSEGSLIKDATGNVIGSALIGQKFDSPWYFHSRPSASDYDGLSSGGSNLAPSSLALIDTLRERTLRYRKENALSPTTPVPSDAVCASASGLDPHISFENGLLQVPRVAHERKADPKSIEELLRKHTEAPTWGILGERVVNVLLLNLELDKRYPKKIGY | 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): 21653
Sequence Length: 197
Subcellular Location: Cell inner membrane
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B8GER0 | MTLRASLRAAVVLFGGCLLVLGLLYPLAMTGIAGVVFPVQAHGSLMYDVNGSVSGSELIARPVTDPRYFQPRPSAVSYNASASGGSNLGPTNPVFLDQVNTSIASLRDAGVTGPIPAELVMASASGLDPDLSVEAALVQAPAVAAARNSSVDEIRALVIAHRVTDLMPFHPEYVNVNTLNQALDGR | 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): 19282
Sequence Length: 186
Subcellular Location: Cell membrane
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P65212 | MRRQLLPALTMLLVFTVITGIVYPLAVTGVGQLFFGDQANGALLERDGQVIGSAHIGQQFTAAKYFHPRPSSAGDGYDAAASSGSNLGPTNEKLLAAVAERVTAYRKENNLPADTLVPVDAVTGSGSGLDPAISVVNAKLQAPRVAQARNISIRQVERLIEDHTDARGLGFLGERAVNVLRLNLALDRL | 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): 20028
Sequence Length: 189
Subcellular Location: Cell membrane
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Q1DFX4 | MFSTFLTALRTCVVTMVLTGLLYPLAVTGLAQLLFPGEANGSWVKDGRGRVVGSALIGQGFTRAGYFHPRPSAAGAGYDGAASSGSNLGPTSLKLKERAAAELERLRRENPDAAGPVPAELVTTSASGLDPHLSPEAARWQAARVARARGVALERVLDVVDARVEGRTFGVLGEPRVNVLLLNLALDRRFGPLPDAAPGVGGRASPGQGAP | 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): 21860
Sequence Length: 211
Subcellular Location: Cell inner membrane
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Q1QJ48 | MLKELRPAIVILVALTIITGLIYPLAMTGAAQVLFPYQAQGSLIEQGGKTIGSALIGQSFTADRYFHGRPSATTAPDPKDASKTVPAPYNAVNSMGSNLGPTSKALADRLRQDVATLKAQNPSAAVPVDLVTASGSGLDPDISPQAARFQVPRVAKARNLPEAEVETLIDSRTEGRDLGFLGEPRVNVLKLNLALDRMAASGQPR | 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): 21584
Sequence Length: 205
Subcellular Location: Cell inner membrane
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C5BAD7 | MSFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLAEVVELCGFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAAIPWDRERFAVSQSQIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVDVALQAPGTGVDTPEDLDCVRAILASQGQN | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27669
Sequence Length: 253
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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B2KD62 | MGDTIIVIPARYGSTRLKAKVLEQLDGKSIVEHVWRAAKAAGEGKVLIATESPVIVEHCAKFGAQAVLTSEACQSGTDRIYEAVKNGSEDYVLNLQGDEPFVKPQTIKGVIKLLKKDSKIDIATACYPTFNDDIYKNPNAVKAVLTKDMRALYFSRSAIPYKRELTEETKKAPYYIHCGIYGYKKTALERFVNLPPSNLEKLEKLEQLRALEDGMVIKSILIEAAGPAIDTAEDLNEARKYIRNN | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27239
Sequence Length: 245
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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A6GYA2 | MKIIAVIPARYASTRFPAKLMQDLGGKTVILRTYQAAVETNLFDDVFVVTDSELIYNEIITNAGKAIMSIKEHESGSDRIAEAIQNLEVDIVVNVQGDEPFINKEPLEEVIQVFRNDTHKKVDLASLMRNITHKNDIQNPNNVKVIVDQKGFALYFSRSVIPYPREENVGVRYMQHIGIYAFRKQALLDFYHLPMLSLEASEKLEQLRYLEYGKRIKMIETTHVGIGIDTLEDLEKARSML | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 27573
Sequence Length: 241
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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B0U168 | MVNIHVVIPARLKSTRLPGKMLADIAGKPMIQRVYEQVAKSKFKSIIIATDSQEIKEVAENFGAKVILTRDDHESGTDRIAEAVTKLGFADEDIVVNVQGDEPLIPVENIEQAAQLLIEKPEAVVSTLCERITEAEDIYNPNNVKVVFDKNNYALYFSRASIPFERGFSENHQVSISEFFRHIGIYTYRVGFLKHYAELAISPIEKYEALEQLRVLYNGYKIAIEQSAKPTPAGVDTLQDLEKVRKLFDV | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28199
Sequence Length: 250
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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Q8RFA8 | MKFLGIIPARYSSTRLEGKPLKMIEGHTMIEWVYKRAKKSNLDSLIVATDDERIYNEVINFGGQAIMTSKNHTNGTSRIAEVCEKMTEYDTIINIQGDEPLIEYEMINSLIETFKENKDLKMATLKHKLLNKEEIKNPNNVKVVCDKNDYAIYFSRSVIPYPRKNGNISYFKHIGIYGYKRDFVIEYSKMLATPLEEIESLEQLRVLENGYKIKVLETTHSLIGVDTQENLEQVINYIKENNIKI | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28426
Sequence Length: 245
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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Q01T78 | MPRKILGVIPARFSSTRFPGKVLAQIANKTMLQHVYERAGLATYLTSTIIATDDERVYTAAKSFGARVRMTRADHLSGTDRVAEVASAENAEIIVNIQGDEPLIDPAAIDAAVLPLVHEPDVLMGTLKKRIEDPREIVDPNVVKVVTDHAGDAIYFSRCPIPFDRDRSADTPYFKHVGLYVYQRDFLLSYSTLPVGPLERSERLEQLRALENGYRIRVVETEYESLGVDTPEDLERVSRLFKASILQGMGNG | Function: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Catalytic Activity: 3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-beta-D-manno-octulosonate + diphosphate
Sequence Mass (Da): 28087
Sequence Length: 252
Pathway: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.38
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