ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9D7F7 | MSKLGKFFKGTRSSRARAAPSAQEALARLRETEEMLAKKQEYLENRIQRELALAKKHGSQNKRAALQALKRKKRFEKQLTQVDGTLSTIEFQREALENSHTNTEVLRNMGFAAKAMKAVHDNMDLNKIDDLMQDITEQQDIAQEISEAFSQRVQFADGFDEAELLAELEELEQEELNKKMTSLELPNVPSSSLPAQPSRKASMPSSVHRSRAASSRRAEEDDDFKQLAAWAT | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
P30577 | KMLTSRTLHGVMQNIRDIVNLKKSEFWNKGGPAWQKIAVCLVFDGIDPCDKDTLDVLATIGIYQDGVMKKDVDGKETIAHIFEYTTQLSVTANQQLIRPHDDGPSTLPPVQMMFCLKQKNSKKINSHRWLFNAFGRILNPEICILLDAGTKPGHKSLLALWEAFYNDKDLGGSCGEIHAMLGKGWKNLINPLVA | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
P30582 | EIGFTRTLHGVMQNITHLCSRSKSRTWGKDGWKKIVVCIIADGRKKVHPRTLNALAALGVYQEGIAKNVVNQKQVNAHVYEYTTQVSLDPDLKFKGAEKGIMPCQVLFCLKEHNKKKLNSHRWFFNAFGRALQPNICILLDVGTKPAPTALYHLWKAFDQNSNVAGAAGEIKAGKGKGMLGLLNPLVAS | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
P30572 | MSYNNPNNSNSHLRPHAYNNSRRDDSDGDESSIEFLNQRSNTPLTQGTYNYHNTSTNSLNFQQPEPIYRNQTRTSLSDSYYDHPIFDTSQTQIQPPHDNPFTESYEMTDTSYQGNDHHYRTGQPNHLMNPTYNQAFIPHVYDEEDNDEQEYDQRIQYNQFQGDHFDLAAISYADDESQSQLDYVPTERVIPEGEEEEEEGETSFEKEPGSETISGPFGEERSFEEPPPQQEVRSKKLTRATGLNGHLVLDCPVADELLSKFPDYNPAEKSGGLSREFAFMRYTAVTCGPSNFYRDAYILRPVHYPIPRQTELMIVITMYN... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
J9VQ06 | MAYHYSHDSDRRQPHGGYNYPSNYSNPSQYSIPDSVYSGHSTNTPRVPSPGGYHQQPSPTTRAVNPAYYQPQPTASSMTSHDLMYGRPSPGPNQYGAAPADVVRGPGATTVPLSQQAPYQPYPSHTDYSDEDKSFASTTHLVSPQKEWGVGSVVPVTTIPPVNQLPYQPYQAYPPRPSPSPITHRGGTSHWHAMRKQLLERRVIKQIPLHNGNLVMDVPVPKGVIPSTKGLGVMDGEMDSMRYSAATCDPDDFMGSKFSLRQYLYGRKTELFIVMTMYNENSELLLRTLNAVIKNIAHLTTRTRSKTWGPDSWKKVVVCI... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
P30601 | MAYNRLGSPQRDGPYSPSAQPQYDSRSPSPGRPLQPYIHPDEAYARQQPLHLQMPTASDDRLAMQPTYSVENVHNPQAYGQQYGQHLPDSGDMGYGRNDYIVSPEEHHDAYYTQPYSPHPQGDYALDPYPSHDEPYRPDTDNVPILQPDSAYGPDPHTQPGMDYDDYQEEPRPTPSPAPIRRWKTVKEVQLFNGNLVLDCPVPPKLLANVPHAKPPERDEFTHMRYSAATCDPSDFHNERFTLRQRLFAKPRQTELFIVVTMYNEDEFLFARTMIGVFKNIEFMCNRSSSKTWGKEAWKKIVVCIVSDGRAKINPRTRAV... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
Q8H4L3 | MVTSTVKLEEVRRMQRAEGMAAVLAIGTATPANCVYQTDYPDYYFRVTNSEHLTNLKERFQRMCESSQIRKRYTHLTEEILQENPSMCVFTAPSLDARQDMVVAEVPKLGKAAAEEAIKEWGQPMSRITHLVFCTTNGVDMPGADYQVAKMLGLPTSVKRLMMYQQGCFAGGTVLRVAKDLAENNRGARVLVVCSEIMAMAFRGPSESHLDSLVGHALFGDGAAAVIVGSDPDEAADERPLFQIVSASQTILPGTEDAIVGHLREVGLTFHLPKDVPEFISDSVEGALTDAFMPLGVHDWNSIFWVVHPGGPAILDQVEE... | Function: The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Catalytic Activity: 4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA
Sequen... |
O53547 | MKLTESNRSPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVVDEIGAAAADAGAKAVAVAGDISQRATADELLASAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRDKAKDAEGGSVFGRLVNTSSEAGLVGPVGQANYAAAKAGITALTLSAARALGRYGVCANVICPRARTAMTADVFGAAPDVEAGQIDPLSPQHVVSLVQFLASPAAAEVNGQVFIVYGPQVTLVSPPHMERRFSADGTSWDPTELTATLRDYFAGRDPEQSFSATDLMRQ | Function: A reversible dehydrogenase involved in cholesterol side-chain degradation. Catalyzes the oxidation of hydroxyl-cholesterol-CoA ester metabolic intermediate (22S)-HOCO-CoA (3-oxo-chol-4-ene-(22S)-hydroxy-24-oyl-CoA), the product of ChsH3, has no activity on (22R)-HOCO-CoA (the product of EchA19). Also acts on ... |
Q00757 | MAYHGSGPQSPGEHTYDDGHQLRDLSHSNTSYEEEASHGLLSSQQSPFAGPFDDPHQQRGLTASPVQRPTSGYSLTESYAPDAAYHDPYSANQSVYSGHSENPAAAFGVPGRVASPYARSETSSTEAWRQRQAGAAGGGNGLRRYATRKVKLVQGSVLSVDYPVPSAIQNAIQAKYRNDLEGGSEEFTHMRYTAATCDPNEFTLHNGYNLRPAMYNRHTELLIAITYYNEDKTLTARTLHGVMQNIRDIVNLKKSEFWNKGGPAWQKIVVCLVFDGIDPCDKDTLDVLATVGIYQDGVMKRDVDGKETVAHIFEYTTQLS... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
P48398 | MSTTVTVLTDTWSRRAKRLEGDAKILAIGTATPASWVDQTTYPDFYFRITNSQHLLEHKEKFRRICNKSKIRKRHLVLTEELLKKNPNLCTYNETSLNTRQDILVSEVPKLGKEAAMKAIKEWGRPISEITHLVFCTTSGVDMPGADFQLTKLLGLNSSVKRLMMYQQGCNAGAAMLRLAKDLAESNKGGRVLVVCAEITINIFRGPSLEQDDNLLAQCLFGDGAAAMIVAADPRPGLETPLFELVSSAQTIVPNTDSHLKLHLREMGLTFHCSKAVPSVLAENVEDCLVKAFEPYGISDWNSIFWVFHPGGNAIVDRVE... | Function: The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Catalytic Activity: 4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA
Sequen... |
P22924 | MKVENGQLQGWWAQRAEGPAKILAIGTATPFHWVDQNSYPDYYFRVTNSQHLVDLKEKFRRICSKTMIKKRHMFLTEELLRKNPTLCSHNEPSLDIRQDILVSEIPKLGKEAALKAIGEWGQPKSTITHLVFCTRSGVDMPGADCQLVKLLGLSPSVQRLMMYQQGCFAGGTMLRLAKDLAENNKGARVLVVCAESSAIGFRGPSEANVDNLIAQALFGDGAAALIIGSDPKPGLERPVFEIFSAAQTFVPNGDCHLALHLREMGLTFHCTKDVPPTIAKNVESCLIKAFEPLGISDWNSLFWILHPGGNAIVDQVESTL... | Function: The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Catalytic Activity: 4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA
Sequen... |
P30583 | MSYNRLGDPYGDDRDARSPIMNPSSLSNRSPSPGRPLDGYQLSDAPYGHHHHIEMPSSDRLAEQPTYSVERIPQSYGHNEAYEAQHQHYPGYEYSVDPEAHHDAYYTQPYQPTVTPGHDDYDLGQYPGHQHSYQDDEPILQPEDPFQAQNPYSDDYQEDMTIAPTPSPAPLRRWKTVKEVQLFQGNLVLDCPIAPKLLNQIPHAENGQRDEFTHMRYSAATCDPKDFFEERFTLRQKLFAKPRHTELFIVVTMYNEDDFLFARTMVGVFKNIEHMCSRTRSKTWGKDAWKKIVVCVISDGRAKINPRTRAVLAGLGCYQD... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
P78746 | MIVLFTLLRWAPISPVFSMRTMHANLAHRGIFLPVMIVTLPLPVHLRRRFPAQMVLMLQWFAFGMFSVLLIIPWLLCVYRLVTHSPGRTKRIKQVLDDRTAPKTVVVMPVYKEAPETLIRAIDSVVDCDYPANCIHVFLSYDGCLIDESYLRLIEHLGIPITLESYPQSIDVTYKDARITVSRFKHGGKRHCQKQTFRLIDMVYADYLERHDNLFVLFIDSDCILDRVCLQNFMYDMELKPGSKHDMLAMTGVITSTTDRGSLLTLLQDMEYVHGQLFERSVESSCGAVTCLPGALTMLRFSAFRKMAKYYFADKAEQCE... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
Q9SA37 | MDPKMLFCLPEGDALFNPLNTMFIQMACILVFSQFFYLFLKPCGQAGPVAQILAGIVLSLLTIIRKVHEFFLQKDSASYYIFFSFLLRTAFVFLIGLEIDLDFMKRNLKNSIVITLGSLVISGIIWLPFLWFLIRFMQIKGDFLTFYLAFLITLSNTAAPVVIRSIIDWKLHTSEIGRLAISCGLFIEITNIFIYTIVLSFISGTMTADIFIYSFATGVIILTNRFLASWLPKRNPKEKYLSKAETLAFIILILIIALTIESSNLNSTLFVFIIGLMFPREGKTYRTLIQRLSYPIHEFVLPVYFGYIGFRFSVNSLTKR... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88909
Sequence Length: 785
Subcellular Location: Membrane
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Q9M353 | MPFNITSVKTSSNGVWQGDNPLNFAFPLLIVQTALIIAVSRFLAVLFKPLRQPKVIAEIVGGILLGPSALGRNMAYMDRIFPKWSMPILESVASIGLLFFLFLVGLELDLSSIRRSGKRAFGIAVAGITLPFIAGVGVAFVIRNTLYTAADKPGYAEFLVFMGVALSITAFPVLARILAELKLLTTQIGETAMAAAAFNDVAAWILLALAVALAGNGGEGGGEKKSPLVSLWVLLSGAGFVVFMLVVIRPGMKWVAKRGSPENDVVRESYVCLTLAGVMVSGFATDLIGIHSIFGAFVFGLTIPKDGEFGQRLIERIEDF... | Function: Operates as a K(+)/H(+) antiporter that maintains K(+) homeostasis in guard cells and could regulate pH. Plays a critical role in osmoregulation through the control of stomates opening.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91553
Sequence Length: 842
Subcellular Location: Endomemb... |
Q8VYD4 | MSSGAPLNVTNPNYDIEESRFGKIVCYDQSLLFEKREQKGWESGSTLASSLPFFITQLFVANLSYRVLYYLTRPLYLPPFVAQILCGLLFSPSVLGNTRFIIAHVFPYRFTMVLETFANLALVYNIFLLGLGMDLRMVRITELKPVIIAFTGLLVALPVGAFLYYLPGNGHPDKIISGCVFWSVALACTNFPDLARILADLKLLRSDMGRTAMCAAIVTDLCTWVLLVFGFASFSKSGTWNKMMPFVIITTAIFVLLCIFVIRPGIAWIFAKTVKAGHVGDTHVWFILGGVVLCGLITDACGVHSITGAFLFGLSIPHDH... | Function: Operates as a K(+)/H(+) antiporter or Na(+)/H(+) antiporter of the chloroplast envelope that functions in pH homeostasis and chloroplast development. Monovalent cation transporter with a preference for Cs(+), K(+) and Rb(+) relative to Na(+) or Li(+). Required for pollen tube guidance, but not for normal poll... |
Q1HDT2 | MVRHFPINDQSLLPAHFGFWPGNSTTPGEVSNRVFSPKIPVVCRKLHSKQPFGMFKGENAMNYAFSTFLIEAIIIIFFIKVVSIALRPFRQPRIVSEIIGGMMIGPSMFGGIRNFNYYLFPPIANYICANIGLMGFFYFLFLTAAKTDVGAIGKAPRKHKYIAAIGVIVPIICVGSVGMAMRDQMDENLQKPSSIGGVVFALSFTSFPVIYTVLRDMNLLNSEVGKFAMSVALLGDMAGVYVIVIFEAMTHADVGGAYSVFWFLVSVVIFAAFMLLVVRRAFDWIVSQTPEGTLVNQNYIVMILMGVLASCFLTDMFGLS... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96681
Sequence Length: 859
Subcellular Location: Membrane
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Q9FGH6 | MVRSFPSDGWSALPTRFGFWPENPTTAGVVSSRVFSARLPEVCRQVHDKQPFGMFKGENGMNYTFSTFLIEAILIIFFIKIVYVLLRPLRQPRIVCEIIGGMMIGPSMLGRNRNFNYYLFPPIANYICANIGLMGFFYFFFLTAAKTDVAEIFKAPRKHKYIAAVSVLVPIACVGSTGAALKHKMDIRLQKPSSIGGVTFALGFTSFPVIYTVLRDMNLLNSEIGKFAMSVTLLGDMVGVYVLVLFEAMAQADGGGGAYSVIWFLISAAIMAACLLLVVKRSFEWIVAKTPEGGLVNQNYIVNILMGVLVSCFLTDMFGM... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95833
Sequence Length: 857
Subcellular Location: Membrane
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Q9M008 | MNNSVTSNGTHEFVCEAWLGSSSGGLLRGDDPLKYSTPLLLLLISLVSSLSSVFQALLRPLANVDFVTQILAGIFLGPSALGQNIDLVKKLFNTRSYFIIESFEAISFMFISYISTAQVDMGVIKRGGKLAIINGLSLFLFPYVVGAIACTVITSNIRGTVAKNNPEQLHNLLTNQSVVYFQVAYSVLSNLKMLNSEPGRLALSSIMVANCFGWGFFLLLITFDSFLHQNYSKTTYLPTFTKVLLLVGIVVVCRPIFNWIVKRTPEGKKLKASHLCTICVMLCTATFLSETVGFPYVVGSVALGLVTPKTPPFGTGLTDK... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87038
Sequence Length: 784
Subcellular Location: Membrane
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Q9M007 | MENITKTFQYGGVDWLCEPWVGAGSLGIGRGENPLKFALPLLLLQISVFSIFSVSFQFLLRPFGKFAFLTQMLAGICLGPSVIGRNKQYMATFFYARSVYIIESFEAICFLFICYITTCQVDTRMIKRVGKLAFINGILLFLIPFVWGQFAAILISKRLKSGPAGIPPVEFHHVAIVQSTMFFQVVYGVLSSLKMLNTEPGRLALASMMVHDCLSWCFFMLNIAIKLNVDLPNKNRAAFLSVLQMIMILVIAYVFRPLMLWMKNRTPEGHSLKASYLSVICVLLFISCLWAEFVGLPYFFGAVVLGLATPKRPPLGTGLS... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86991
Sequence Length: 767
Subcellular Location: Membrane
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Q8L709 | MNSTTTKNVCGDKWYLNLDRPEEALKILVFIAIFVVRTLLHYLMKPLGQPYLTTDFAIGLILGNIPRFRGAFSGPYSITLNNIIEFGMICHMFVMGLEMNPSVLLRPPTKDAFIAYTSMITTFVLAFVTTPFLHYTKTSPYIFSLALSLMASSTGSPILTRVIANLKIRKSDLGKLASAAGVHTDMISTLLYCFGFIFFPTEKPLARPLHRFFRALLMFCLFLAQVTFTSIVSPIFLNWVNNENPEGKPLKGSHLVMSLAFVVLICSFPTWPPESMYNPILSAFTAGLFLPNKGRMSKWIINKINYLLSTVFYPIFFFWV... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88710
Sequence Length: 801
Subcellular Location: Membrane
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Q9FYC1 | MEFNGDRIPYLRDTWRDANMICGILPINPSSSGLWPSPKLPDPQANIEFWNYMFPHVQIIFLIVTILWQFFHFFLRRLGMIRFTSHMLTGILLSKSFLKENTPARKFLSTEDYKETLFGLVGACSYMMFWFLMGVKMDLSLIRSTGRKAVAIGLSSVLLSITVCALIFFLILRDVGTKKGEPVMSFFEIIFIYLIQCLSSFPVIGNLLFELRLQNSELGRLAMSSAVISDFSTSILSAVLVFLKELKDDKSRLGSVFIGDVIVGNRPMKRAGTVVLFVCFAIYIFRPLMFFIIKRTPSGRPVKKFYIYAIIILVFGSAIL... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92008
Sequence Length: 817
Subcellular Location: Membrane
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Q3EDG3 | MESRNEAYEGAYNATFWGDFSYHGYGFSEDGSKFCEQIPILVNSFGVWEKLDLPIRGMKIWDYSLPHLESVIVLVLCLWQFFYLSLKKIGLPVPKITSMMIAGAALSQTNLLPNDWTIQHILFPDDTRPKVPETLGGFAFVFYWFIEGVKMDVGMVRKTGTKVIVTGIATVILPIIAANMVFGKLRETGGKYLTGMEYRTILFMQSISAFTGISRLLRDLRINHSEFGRIVISTAMVADGTGFGVNLFALVAWMDWRVSALQGVGIIGYVIFMVWVVRPAMFWVIKRTPQERPVKECFIYIILILAFGGYYFLKEIHMFP... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91606
Sequence Length: 815
Subcellular Location: Membrane
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Q8GX92 | MATEEIDMSYWDVSWGEFNEDKNSSIFCESHPHIVNSHGIWEVMTFKRGMNFWEYPLPNLEILIFSTFFIWRLLDISFNKIGLRVPRFTYMMIAGIILGQTCHFSNKSWIHDIFFPDDNRPKVAETLGAFGFVLYWFLKGVTMDAELPFRTEKRSSVIGFITVIIPLICGSLTFRYRERRGDSSILRMEYRLIIFLQSISAFTSIDTLLKDLQIKHSEFGRIALSGAMVTDMLAFGVTFFNAIYYEKLYGFMQTVGFCLFVVVMICVVRPAMYWVIKQTPEGRPVKDFYLYSIFGIAFACFTFFNKVIHLFGPAGSFVFG... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93395
Sequence Length: 818
Subcellular Location: Membrane
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P0CG16 | MDAENATWRKEFMWNNDEKRAEMGTKMFCDVSPHIMLNSHGVAEKMASGSKGMDFWEYPLPQLEIIILSIFLLWRLFDMLFKKLGVPIPKFTSMMLVGAVLSEMFGSMQIPCLKHIFIHYNQYMTKVPDTIGAFAFVLDWFLRGVTTDVGIMKKSGTKSVVIGITSMIIPWQIGKLLYSSREKSSILTMTEMEYTVMTFTMSMTPFTCVNMLLTDLKIVHTDFGQIAQSAGMVTDLLAFFLTVSAYVSRDETQGVKMGLAFMAFFIFVYLVRQFMLWVIRHTPEGAPVKNVYLYIGLLLAYLSYLYWSRFLFFGPLGAFA... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90112
Sequence Length: 796
Subcellular Location: Membrane
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Q9ZUV9 | MDPFNASWWTNMAWHGYSLSEDGTKFCEMLPTKINSFGLSEKILHKSVGLYFWEYPLPNLELIILSVFFFWQFFEILFKMSNIPIPKMPSMMLGCVVINLFSYTRPGSLLHRMFFPDDGRPKVAETGGAFGFVMYWFLKGVSIDVGMLRKTEPRAALIGFNTLVIPYISGYILMRTRKHFGKLAMTELQYQEIILLQSLSSFAGVNGLLTDLKINHSEFGRMVQSCAAVTDLVIFIMVSGTVLLKGQKGLPHGIVIVLVIGFLVYIVWPVMLWIIKQTPEGRLVKDVYIYLVMATAYFVYMFWLNFFQFSTYGWFIIGLA... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90990
Sequence Length: 801
Subcellular Location: Membrane
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Q58P71 | MGGGDISHMSPEVKWIFEMAWYGETVRYDGLICEEHPPKLSSDGIWEKLIIKSAGLYFWQYRLPKLEIVILLVFFLWQGFNILFKKLGLSIPKLSSMMLAGLLLNVLVTLSGENSIIADILVTKNRIDVAGCLGSFGFLIFWFLKGVRMDVKRIFKAEAKARVTGVAAVTFPIVVGFLLFNLKSAKNRPLTFQEYDVMLLMESITSFSGIARLLRDLGMNHSSIGRVALSSALVSDIVGLLLLIANVSRSSATLADGLAILTEITLFLVIAFAVVRPIMFKIIKRKGEGRPIEDKYIHGVLVLVCLSCMYWEDLSQFPPL... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90956
Sequence Length: 816
Subcellular Location: Membrane
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Q9FFB7 | MTDSQALVPGPSPPHSKAEICYGATFFNISSYGIMEKYETPTVIFGYALPLLELQIILIFVCIVLSHMFLRRIGIPRFVSNILAGLILGPQLLDLLEYSSDRLSLDIPGNVALEGVARLGLVMFTFLMGVKTNKRAVYQIGKRPIVIAVSSFFVTMISGLAFRNFRLDKVDPLYMPLRLAPTERSVIVSIQAVTLLPVITHLVYELKMSNSELGRIAISTAAVSDFLGFLTLVCISYVGTYRYVSPGIANRDIVALIILVLVILFIFKPMAQRIVDMTPEGKPVPKVYLYVTILTAIAASIYLSVFNQMYILGALLVGLA... | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89060
Sequence Length: 800
Subcellular Location: Membrane
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Q5EK40 | MYLTFYLEKVMKKMLLIAGATVISSMAHPTFAVEDELNIFDECRSPCSLTPEPGKPIQSKLSIPSDVVLDEGVLYYSMTINDEQNDIKDEDKGESIITIGEFATVRATRHYVNQDAPFGVIHLDITTENGTKTYSYNRKEGEFAINWLVPIGEDSPASIKISVDELDQQRNIIEVPKLYSIDLDNQTLEQWKTQGNVSFSVTRPEHNIAISWPSVSYKAAQKEGSRHKRWAHWHTGLALCWLVPMDAIYNYITQQNCTLGDNWFGGSYETVAGTPKVITVKQGIEQKPVEQRIHFSKGNAMSALAAHRVCGVPLETLARS... | Function: An NAD-dependent ADP-ribosyltransferase (ADPRT), it catalyzes the transfer of the ADP-ribosyl moiety of oxidized NAD onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. It probably uses the eukaryotic prolow-density lipoprotein receptor-related protein 1 (LRP1) to enter mouse cells, ... |
Q5HL70 | MEKAKFVIKLILQLALIMLITFIGTEVQKLLHIPLAGSIVGLMLFFLLLQFKIVPESWINVGADFLLKTMVFFFIPSVVGIMDVASNITMNYILFFIVIIIGTCLVALSSGYIAEKMLEKSNTRKGTDHS | Function: Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics... |
P60639 | MNDYVQALLMILLTVVLYYFAKRLQQKYPNPFLNPALIASLGIIFVLLIFGISYNGYMKGGSWINHILNATVVCLAYPLYKNREKIKDNVSIIFASVLTGVMLNFMLVFLTLKAFGYSKDVIVTLLPRSITAAVGIEVSHELGGTDTMTVLFIITTGLIGSILGSMLLRFGRFESSIAKGLTYGNASHAFGTAKALEMDIESGAFSSIGMILTAVISSVLIPVLILLFY | Function: Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics... |
A3B529 | MEERSVLMERYVIGRQLGQGTFGKVYYARNLSSGQSVAIKMIDKEKILKVGLMEQIKREISIMRLVRHPNVLQLFEVMATKSNIYFALEYAKGGELFHKMARAKLNEESARNYFQQLISAMDYCHSRGVYHRDLKPENLLLDENETLKVSDFGLSALAESRRQDGLLHTACGTPAYVAPEVLSRKGYSGSKADVWSCGVILFVLVANYLPFHDRNIIQMYRKIAKAEYRCPRHFSAELKELLYGILDPDPSTRMSISRIKRSAWYRKPIAISALNNETGKKSCTSEAPFSGPTICISSERNQEPPNLHNLNAFDIISLST... | Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Seq... |
Q7XIW5 | MPPSTGSVPPAASTPAAGDEATAAGRVLLGRYELGGLLGRGASAKVYLARDLLTGRDVAIKSFPNPRHGGGLRGGEEDVLLRPAPIEREAAILPRLRHRHVMRLREILATRKKVHFVLDLAAGGELFSLLDASGRMTEDLARHYFRQLISAVRYCHSRGVYHRDIKPENLLLDDAGDLKVADFGLGAVADGALHHTLCGTPAYVAPEILSRKGYNPAKVDIWSCGVVLFVLAAGYLPFNDASLVNMYRKIYAGKFRCPAWFSPELRCLVRRILDPNPATRIDTEEIITHPWFRQDASHFAMAQLMQHGHDEEAKFKTEFK... | Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Seq... |
Q5JLQ9 | MAMETTSQDSQVIMGRYKLGRLLGRGTFAKVYKAYKLATGEAVAIKVFDKEAVQRSGTVEQVKREVDVMRRVHHRHVIRLHEVMATRSRIYFVMEYASGGELFTRLSRSPRFPEPVARRYFQQLITAVEFCHSRGVYHRDLKPENLLLDARGDLKVTDFGLSALDGGLRGDGLLHTTCGTPAYVAPEVLLKRGYDGAKADIWSCGVILFVLLAGYLPFNETNLVILYRNITESNYRCPPWFSVEARKLLARLLDPNPKTRITISKIMDRPWFQQATCPLGDMSLVASAPSVLLARKEASQQHDDEEDDGFAREKKKRSNV... | Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Seq... |
Q6X4A2 | MYRAKRAALSPKVKRRVGKYELGRTIGEGTFAKVRFAKNTENDEPVAIKILDKEKVQKHRLVEQIRREICTMKLVKHPNVVRLFEVMGSKARIFIVLEYVTGGELFEIIATNGRLKEEEARKYFQQLINAVDYCHSRGVYHRDLKLENLLLDASGNLKVSDFGLSALTEQVKADGLLHTTCGTPNYVAPEVIEDRGYDGAAADIWSCGVILYVLLAGFLPFEDDNIIALYKKISEAQFTCPSWFSTGAKKLITRILDPNPTTRITISQILEDPWFKKGYKPPVFDEKYETSFDDVDAAFGDSEDRHVKEETEDQPTSMNA... | Function: Involved in cold stress tolerance. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ... |
Q86X95 | MGKSFANFMCKKDFHPASKSNIKKVWMAEQKISYDKKKQEELMQQYLKEQESYDNRLLMGDERVKNGLNFMYEAPPGAKKENKEKEETEGETEYKFEWQKGAPREKYAKDDMNIRDQPFGIQVRNVRCIKCHKWGHVNTDRECPLFGLSGINASSVPTDGSGPSMHPSELIAEMRNSGFALKRNVLGRNLTANDPSQEYVASEGEEDPEVEFLKSLTTKQKQKLLRKLDRLEKKKKKKDRKKKKFQKSRSKHKKHKSSSSSSSSSSSSSSTETSESSSESESNNKEKKIQRKKRKKNKCSGHNNSDSEEKDKSKKRKLHE... | Function: May modulate splice site selection during alternative splicing of pre-mRNAs (By similarity). Regulates transcription and acts as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC). Required for RBPJ-mediated repression of transcription.
PTM: Phosphorylated by NEK6.
Sequence Mas... |
Q9DA19 | MGKSFANFMCKKDFHPASKSNIKKVWMAEQKISYDKKKQEELMQQYLKEQESYDNRLLMGDERVKNGLNFMYEAPPGVKKENKEKEETEGETEYKFEWQKGAPREKYAKDDMNIRDQPFGIQVRNVRCIKCHKWGHVNTDRECPLFGLSGINASSVPTDGSGPSMHPSELIAEMRNSGFALKRNVLGRNLTANDPSQDYVASDCEEDPEVEFLKSLTTKQKQKLLRKLDRLEKKKKKKKSDKKKKKLQKSKNKHKKRKNKSPSSSSSSSSSSSSSSSSSSSSSSSSETSDSSSESDNKEKKREKEKRKKKKKTKCSESKS... | Function: Regulates transcription and acts as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC). Required for RBPJ-mediated repression of transcription (By similarity). May modulate splice site selection during alternative splicing of pre-mRNAs.
PTM: Phosphorylated by NEK6.
Sequence Mas... |
P17315 | MFRLNPFVRVGLCLSAISCAWPVLAVDDDGETMVVTASSVEQNLKDAPASISVITQEDLQRKPVQNLKDVLKEVPGVQLTNEGDNRKGVSIRGLDSSYTLILVDGKRVNSRNAVFRHNDFDLNWIPVDSIERIEVVRGPMSSLYGSDALGGVVNIITKKIGQKWSGTVTVDTTIQEHRDRGDTYNGQFFTSGPLIDGVLGMKAYGSLAKREKDDPQNSTTTDTGETPRIEGFSSRDGNVEFAWTPNQNHDFTAGYGFDRQDRDSDSLDKNRLERQNYSVSHNGRWDYGTSELKYYGEKVENKNPGNSSPITSESNTVDGK... | Function: Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73896
Sequence Length: 663
Subcellular Location: Cell outer membrane
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Q9DED4 | MSDEGKLFIGGLNFDTNEESLEQVFSKYGQISEVVVVKDRETKRSRGFGFVTFENPDDAKDAMMAMNGKAVDGRQIRVDQAGKSSGDRRGGYRGGSSGGRGFFRGGRGRGGGDRGYGSSRFDNRSGGYGGSSGSRDYYSSGRSQGSYGDRAGGSYRDSYDSYATHE | Function: Cold-inducible mRNA binding protein. Acts cooperatively with elavl1/elrA to stabilize AU-rich element (ARE)-containing mRNAs by binding to them and inhibiting their deadenylation. Essential for embryonic gastrulation and neural development, acting to maintain the expression of a set of adhesion molecules, and... |
Q14011 | MASDEGKLFVGGLSFDTNEQSLEQVFSKYGQISEVVVVKDRETQRSRGFGFVTFENIDDAKDAMMAMNGKSVDGRQIRVDQAGKSSDNRSRGYRGGSAGGRGFFRGGRGRGRGFSRGGGDRGYGGNRFESRSGGYGGSRDYYSSRSQSGGYSDRSSGGSYRDSYDSYATHNE | Function: Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Acts as a translational activator. Seems to play an essential role in cold-induced suppression of cell proliferation. Binds specifically to the 3'-un... |
P45410 | MTLILKRVQLLKDKPRREAIDRFLRQHQLSLEADCEMAIIAEYQQRLVGCGAIAGNVLKCIAIDPSLQGEGLSLKLLTELLTLAYELGRSELFLFTKPCNAALFSGAGFWPIAQAGDRAVLMENSRERLTRYCRQLAMYRQPGRKIGAIVMNANPFTLGHRWLVEQAASQCDWLHLFVVKEDASCFSYHDRFKLIEQGITGIDKVTLHPGSAYLISRATFPGYFLKEQGVVDDCHSQIDLQLFRERLAPALQITHRFVGTEPLCPLTRNYNQRMKSLLEAPGDAPPIEVVELARIEKNGGPVSASRVRELYRQRNWQAVA... | Function: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
Catalytic Activity: acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate lyase ACP] + AMP + diphosphate
Sequence Mass (Da): 38477
Sequence Length: 342
EC: 6.2.1.22
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O53076 | MRRDWQNFLMACGIKNFDDSELNPLDITIAVYENEEIIGTGSIAGDVIKYVAVQETTMSGHSTLFNQLMTKLENFMAVEGRFHQFVLRNQFTKKVLNTLASKRWLSVNKEFCWKKDYQILRNTCQQFPSQTPIDKVASVVINANPFTNGHRFLIEEASRNNELVYVFVLNQEASLFHTDERIALVKAGVQDLSNVIVVNGGAYIISYLTFPAYFLKHNDSAIDYQTTIDVRLFKYKIASALGITSRYVGSEPLSHTTNLYNQKLISELNPQIEVHVIQRKLAAGDLGVISARTVREAIDKGDEAVWQKMVTETTQHFISN... | Function: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
Catalytic Activity: acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate lyase ACP] + AMP + diphosphate
Sequence Mass (Da): 38460
Sequence Length: 338
EC: 6.2.1.22
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A0A142PTM2 | MATVKVIDFIQTPFDFLIVGGGTAGLVLAARLSEEPGIQVGVIEAGSLRLGDPKVDLPTGPGQMLGDPGYDWNFESIPQAGANAKAYHIPRGRMLGGSSGINFMSYNRPSAEDIDDWANKLGVKGWTWSELLPYFKRSENLEPIEPSASCPVSPKVHGTGGPIHTSIGPWQAPIEESLLAAFDEAARLQRPAEPYSGAHLGFYRSLFTLDRTSTPVRSYAVSGYYAPVMGRPNLKVLENAQVCRILLSDASDGIPVAEGVELHHAGARYAVSARREVILSAGSVQSPQLLELSGIGDPSVLEGAGIACRVANTDVGSNLQ... | Function: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III . The pathway begins with the synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT) from successive condensatio... |
P55069 | MLAILGFLMMLVFMALIMTKRLSVLTALVLTPIVFALIAGFGFTEVGDMMISGIQQVAPTAVMIMFAILYFGIMIDTGLFDPMVGKILSMVKGDPLKIVVGTAVLTMLVALDGDGSTTYMITTSAMLPLYLLLGIRPIILAGIAGVGMGIMNTIPWGGATPRAASALGVDPAELTGPMIPVIASGMLCMVAVAYVLGKAERKRLGVIELKQPANANEPAAAVEDEWKRPKLWWFNLLLTLSLIGCLVSGKVSLTVLFVIAFCIALIVNYPNLEHQRQRIAAHSSNVLAIGSMIFAAGVFTGILTGTKMVDEMAISLVSMI... | Function: Proton motive force-driven secondary transporter that mediates the transport of citrate complexed to Mg(2+). Cotransports at least two protons per Mg(2+)-citrate complex. Can also transport citrate in complex with Ni(2+), Mn(2+), Co(2+), and Zn(2+).
Location Topology: Multi-pass membrane protein
Sequence Mass... |
P31602 | MTNMSQPPATEKKGVSDLLGFKIFGMPLPLYAFALITLLLSHFYNALPTDIVGGFAIMFIIGAIFGEIGKRLPIFNKYIGGAPVMIFLVAAYFVYAGIFTQKEIDAISNVMDKSNFLNLFIAVLITGAILSVNRRLLLKSLLGYIPTILMGIVGASIFGIAIGLVFGIPVDRIMMLYVLPIMGGGNGAGAVPLSEIYHSVTGRSREEYYSTAIAILTIANIFAIVFAAVLDIIGKKHTWLSGEGELVRKASFKVEEDEKTGQITHRETAVGLVLSTTCFLLAYVVAKKILPSIGGVAIHYFAWMVLIVAALNASGLCSPE... | Function: Uptake of citrate across the boundary membrane with the concomitant uptake of a sodium ion (symport system).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47558
Sequence Length: 446
Subcellular Location: Cell membrane
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P21608 | MMNHPHSSHIGTTNVKEEIGKLDRIRISGIGLIAYAFMAVLLIIAISTKTLPNTMIGAIFALVLMGHVFYYLGAHLPIFRSYLGGGSVFTILLTAILVATNVIPKYVVTTASGFINGMDFLGLYIVSLIASSLFKMDRKMLLKAAVRFLPVAFISMALTAVVIGIVGVIIGVGFNYAILYIAMPIMAGGVGAGIVPLSGIYAHAMGVGSAGILSKLFPTVILGNLLAIISAGLISRIFKDSKGNGHGEILRGEREKSAAAEEIKPDYVQLGVGLIIAVMFFMIGTMLNKVFPGINAYAFIILSIVLTKAFGLLPKYYEDS... | Function: Uptake of citrate across the boundary membrane with the concomitant uptake of a sodium ion (symport system).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46629
Sequence Length: 442
Subcellular Location: Cell membrane
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Q07065 | MPSAKQRGSKGGHGAASPSEKGAHPSGGADDVAKKPPPAPQQPPPPPAPHPQQHPQQHPQNQAHGKGGHRGGGGGGGKSSSSSSASAAAAAAAASSSASCSRRLGRALNFLFYLALVAAAAFSGWCVHHVLEEVQQVRRSHQDFSRQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASLEESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESD... | Function: Mediates the anchoring of the endoplasmic reticulum to microtubules.
PTM: Reversibly palmitoylated. Palmitoylation at Cys-100 by ZDHHC2 is required for its trafficking from the ER to the plasma membrane and for its perinuclear localization. Palmitoylation by ZDHHC2 is also required for its function in APF-med... |
P25859 | MEKYEKLEKVGEGTYGKVYKAMEKGTGKLVALKKTRLEMDEEGIPPTALREISLLQMLSTSIYVVRLLCVEHVHQPSTKSQSTKSNLYLVFEYLDTDLKKFIDSYRKGPNPKPLEPFLIQKLMFQLCKGVAHCHSHGVLHRDLKPQNLLLVKDKELLKIADLGLGRAFTVPLKSYTHEIVTLWYRAPEVLLGSTHYSTGVDMWSVGCIFAEMVRRQALFPGDSEFQQLLHIFRLLGTPTEQQWPGVSTLRDWHVYPKWEPQDLTLAVPSLSPQGVDLLTKMLKYNPAERISAKTALDHPYFDSLDKSQF | Function: May control G2/M (mitosis) phase progression. Plays a role in regulating seedling growth in darkness via regulation of hypocotyl cell elongation and cotyledon cell development. Plays a role in stomatal development. Required to suppress endoreduplication. Together with CDKB1-2, promotes both the last division ... |
Q2V419 | MEKYEKLEKVGEGTYGKVYKAMEKTTGKLVALKKTRLEMDEEGIPPTALREISLLQMLSQSIYIVRLLCVEHVIQSKDSTVSHSPKSNLYLVFEYLDTDLKKFIDSHRKGSNPRPLEASLVQRFMFQLFKGVAHCHSHGVLHRDLKPQNLLLDKDKGILKIADLGLSRAFTVPLKAYTHEIVTLWYRAPEVLLGSTHYSTAVDIWSVGCIFAEMIRRQALFPGDSEFQQLLHIFRLLGTPTEQQWPGVMALRDWHVYPKWEPQDLSRAVPSLSPEGIDLLTQMLKYNPAERISAKAALDHPYFDSLDKSQF | Function: Together with CDKB1-1, promotes both the last division in the stomatal cell lineage as well as the number of stomata . In collaboration with MYB124 and MYB88, restrict the G1/S transition and chloroplast and nuclear number during stomatal formation, and normally maintain fate and developmental progression thr... |
Q0J4I1 | MAALHHQAAAAPVTTTTDGGELRAMDLYEKLEKVGEGTYGKVYKAREKATGRIVALKKTRLPEDDEGVPPTALREVSLLRMLSQDSHVVRLLDLKQGQNKEGQTILYLVFEYMDTDLKKFIRAHRQNLQKIPVPTVKILMYQLCKGVAFCHGRGVLHRDLKPHNLLMDRKTMALKIADLGLSRSFTVPLKKYTHEILTLWYRAPEVLLGAAHYSTPVDIWSVGCIFAELATNQPLFAGDSEVQQLLHIFKLLGTPNEQVWPGVSKLPNWHEYPQWNPSKVSDLVHGLDADALDLLEKMLQYEPSKRISAKKAMEHPYFND... | Function: Forms a complex with CYCB2-1 or CYCB2-2 that activates CDK kinase in tobacco BY2 cells during G2/M (mitosis) phases. May be involved in the regulation of the cell cycle at the G2/M transition.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 36977
Sequ... |
P46559 | MTAIEKFFTEKSPDSEQVLLKVIELGIDFLGGEWKNVDKSQVNVSRVHGGQSNHMFHVTSSTSATPYLLRIHRQPPSQVFTDTVNLAIFSERGLGPKLYGFFEGGRMEEFLPSKTFDVNDVLVPENSRKIGAIFPLYHSINVPVSKSRRCVHLMREWLNGYESLGGGDYEILPTTVNYSDHPKSVSIKDLNHEIDNFEKWSTEIFEHTLVFSHNDLASTNILELNSTKELVLIDWEFGTYNWRGFDLAMHLSETAIDYRVPFPPGIKMNGDLIDNPPNIQIFCEAYVEADKKLKNRSPSDPTAEVKALIQECQFFWPLTN... | Cofactor: Less efficient with Mn(2+).
Function: Catalyzes the first step in phosphatidylcholine biosynthesis. Phosphorylates choline.
Catalytic Activity: ATP + choline = ADP + H(+) + phosphocholine
Sequence Mass (Da): 42264
Sequence Length: 369
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phospho... |
Q8CFC7 | MWHEARKHERKLRGMMVDYKKRAERRREYYEKIKKDPAQFLQVHGRACKVHLDSAVALAAESPVNMMPWQGDTNNMIDRFDVRAHLDHIPDYTPPLLTTISPEQESDERKCNYERYRGLVQNDFAGISEEQCLYQIYIDELYGGLQRPSEDEKKKLAEKKASIGYTYEDSTVAEVEKVAEKPEEEESPAEEESNSDEDEVIPDIDVEVDVDELNQEQVADLNKQATTYGMADGDFVRMLRKDKEEAEAIKHAKALEEEKAMYSGRRSRRQRREFREKRLRGRKISPPSYARRDSPTYDPYKRSPSESSSESRSRSRSPSP... | Function: Probably functions as an alternative splicing regulator. May regulate the mRNA splicing of genes such as CLK1. May act by regulating members of the CLK kinase family.
PTM: Phosphorylated in vitro by CLK4.
Sequence Mass (Da): 76825
Sequence Length: 668
Subcellular Location: Nucleus
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Q5HZB6 | MWHEARKHERKLRGMMVDYKKRAERRREYYEKIKKDPAQFLQVHGRACKVHLDSAVALAAESPVNMMPWQGDTNNMIDRFDVRAHLDHIPDYTPPLLTTISPEQESDERKCNYERYRGLVQNDFAGISEEQCLYQIYIDELYGGLQRPSEDEKKKLAEKKASIGYTYEDSTVAEVEKVAEKPEEEESPAEEESNSDEDEVIPDIDVEVDVDELNQEQVADLNKQATTYGMADGDFVRMLRKDKEEAEAIKHAKALEEEKAMYSGRRSRRQRREFREKRLRGRKISPPSYARRDSPTYDPYKRSPSESSSESRSRSRSPSP... | Function: Probably functions as an alternative splicing regulator. May regulate the mRNA splicing of genes such as CLK1. May act by regulating members of the CLK kinase family (By similarity).
PTM: Phosphorylated in vitro by CLK4.
Sequence Mass (Da): 76807
Sequence Length: 668
Subcellular Location: Nucleus
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P32756 | MEKEKVDELPPNDNWYETALPKPPVPSLEATLDRYLEYAAVVAVGQKASLATTHDAAHKFVRQATPLQEQLLEIAEKSPNWATKFWLPEMYMRVRMPTPVNSNPGYIFPKVKFETKEDHIKYTALLTRGLLEYKNLIDTKQVCREKSTGAQKLQMCMEQYDRVLSCYREPGVGEDTQIRKQKTNDGNEHVLVMCRNQTFLLHSRINGALVSYADVEYQLAQIEEISKINQNNTANIGASGVGPRDNAALFWQDMLTVEQNSKSYEWVKSALFVVCLDMEDPIDYGKNDTMSISEKEKEFVARGYSTLTGHGSSKFGLNRW... | Function: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses (By similarity). Required in SIA sublateral cholinergic motor neurons for a left-right turning behavior that occurs during the lethargus phase of the normal sleep process called 'flipping' . During 'f... |
B2ZGJ1 | MPVSKREQSKDTGDPCALPKLPIPPLKQTLDMYLTCMGHLVPEDQFRKTKAVVEKFGAPGGVGETLQKKLLERSEQKANWVYDYWLEDMYLNNRLALPVNSSPVMVFHKQNFKGQSDVLRFAANLISGVLEYKALIDGRALPVEHARGQLAGTPLCMDQYNKVFTSYRLPGTKTDTLVAQKSTVMPEPEHIIVACKNQFFVLDVMVNFRRLNEKDLYTQLERIRKMADIEEERQPPIGLLTSDGRTQWAEARNILIKDSTNRDSLDMIERCLCLVCLDEETATELNDSNRALLMLHGGGTDKNGGNRWYDKPMQFVIGAD... | Function: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
Catalytic Activity: acetyl-CoA + choline = acetylcholine + CoA
Sequence Mass (Da): 71840
Sequence Length: 637
EC: 2.3.1.6
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P51798 | MANVSKKVSWSGRDRDDEEAAPLLRRTARPGGGTPLLNGAGPGAARQSPRSALFRVGHMSSVELDDELLDPDMDPPHPFPKEIPHNEKLLSLKYESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKGNIDKFTEKGGLSFSLLLWATLNAAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWN... | Function: Slowly voltage-gated channel mediating the exchange of chloride ions against protons . Functions as antiporter and contributes to the acidification of the lysosome lumen and may be involved in maintaining lysosomal pH . The CLC channel family contains both chloride channels and proton-coupled anion transporte... |
P0DM29 | MNPKLLIVIGLLLATGVCSFAKALDEESLRKECNHLNEPCDSDGDCCTSSEQCISTGSKYFCKGKQGP | Function: Cell penetrating peptide (CPP) that increases intracellular calcium release through the activation of nuclear inositol 1,4,5-trisphosphate receptors (ITPR) of cardiomyocytes, thereby causing an increase in the contraction frequency of these cells . In vivo, this toxin is not lethal to mice, hovewer anti-CPP s... |
Q8MN58 | MSDPFGEENVEITEEFVEGDINENDLIDGNVEYVDGNGISFETTTFDNSNNNNNNNNHNNNSYNSGFDGDLSSVDGDMKPKETAPAMREYLEKHEKEMQEKKKKSEEKRQKKIAEAKQSLDNFYSEREAKKKTALKNNRDHNKSLETDSTSGNTTHTWESVVSMIDLQAKPNPANKDTSRMREILIRLKNQPIV | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22137
Sequence Length: 194
Subcellular Location: Cytoplasmic vesicle membrane
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Q9VWA1 | MDFGDDFAAKEDVDPAAEFLAREQSALGDLEAEITGGSASAPPAASTDEGLGELLGGTASEGDLLSAGGTGGLESSTGSFEVIGGESNEPVGISGPPPSREEPEKIRKWREEQKQRLEEKDIEEERKKEELRQQSKKELDDWLRQIGESISKTKLASRNAEKQAATLENGTIEPGTEWERIAKLCDFNPKVNKAGKDVSRMRSIYLHLKQNPIQVQKST | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23840
Sequence Length: 219
Subcellular Location: Cytoplasmic vesicle membrane
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Q5E9L0 | MASTASEIIAFMVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYWANLWKTCVTDSTGVSNCKDFPSMLALDGYIQACRGLMIAAVSLGFFGSIFALIGMKCTKVGGSDKAKAKIACLAGIVFILSGLCSMTGCSLYANKITTEFFDPLFVEQKYELGAALFIGWAGASLCLIGGVIFCFSISDNNKAPRMGYTYNGATSVMSSRTKYHGREGDLKTPNPSKQFDKNAYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in the regulation of paracellular epithelia permeability to ions in multiple organs. It acts as a paracellular ion channel probably forming permselective pores; i... |
P78369 | MASTASEIIAFMVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYWANLWKACVTDSTGVSNCKDFPSMLALDGYIQACRGLMIAAVSLGFFGSIFALFGMKCTKVGGSDKAKAKIACLAGIVFILSGLCSMTGCSLYANKITTEFFDPLFVEQKYELGAALFIGWAGASLCIIGGVIFCFSISDNNKTPRYTYNGATSVMSSRTKYHGGEDFKTTNPSKQFDKNAYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in the regulation of paracellular epithelia permeability to ions in multiple organs. It acts as a paracellular ion channel probably forming permselective pores; i... |
Q9Z0S6 | MASTALEIVAFVVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYFANLWKICVTDSTGVANCKEFPSMLALDGYIQACRGLMIAAVSLGFFGSIFALFGMKCTKVGGSDQAKAKIACLAGIVFILSGLCSMTGCSLYANKITTEFFDPLYMEQKYELGAALFIGWAGASLCIIGGVIFCFSISDNNKTPRMGYTYNGPTSAMSSRTKYQGGEGDFKTTGPSKQFDKNAYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in the regulation of paracellular epithelia permeability to ions in multiple organs. It acts as a paracellular ion channel probably forming permselective pores; i... |
O75508 | MVATCLQVVGFVTSFVGWIGVIVTTSTNDWVVTCGYTIPTCRKLDELGSKGLWADCVMATGLYHCKPLVDILILPGYVQACRALMIAASVLGLPAILLLLTVLPCIRMGQEPGVAKYRRAQLAGVLLILLALCALVATIWFPVCAHRETTIVSFGYSLYAGWIGAVLCLVGGCVILCCAGDAQAFGENRFYYTAGSSSPTHAKSAHV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21993
Sequence Length: 207
Subcellular Location: Cell junction
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Q5REK8 | MVATCLQVVGFVTSFVGWIGVIVTTSTNDWVVTCGYTIPTCRKLDELGSKGLWADCVMATGLYHCKPLVDILPCRALMIAASVLGLPAILLLLTVLPCIRMGQEPGVAKYRRAQLAGVLLILLALCAIVATIWFPVCAHRETTIVSFGYSLYAGWIGAVLCLVGGCVILCCAGDAQAFGENRFYYTAGSSSPTHAKSAHV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21248
Sequence Length: 200
Subcellular Location: Cell junction
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Q0IIL2 | MGCRDVHAATVLSFLCGIASVAGLFAGTLLPNWRKLRLITFNRNEKNLTVYTGLWVKCARYDGGNDCLMYDAAWYSSVDQLDLRVLQFALPLSILIAMGALLLCLIGMCNTAFRSSVPNIKLAKCLVNSAGCHLVAGLLFFLAGTVSLSPSIWVIFYNIHLNRKFEPVFAFDYAVYVTVASAGGLFMTALLLFIWYCACKSLPSPFWQPLYSHPPGMHTYSQPYSARSRLSAIEIDIPVVSHTT | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26951
Sequence Length: 244
Subcellular Location: Cell junction
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P56749 | MGCRDVHAATVLSFLCGIASVAGLFAGTLLPNWRKLRLITFNRNEKNLTVYTGLWVKCARYDGSSDCLMYDTTWYSSVDQLDLRVLQFALPLSMLIAMGALLLCLIGMCNTAFRSSVPNIKLAKCLVNSAGCHLVAGLLFFLAGTVSLSPSIWVIFYNIHLNKKFEPVFSFDYAVYVTIASAGGLFMTSLILFIWYCTCKSLPSPFWQPLYSHPPSMHTYSQPYSARSRLSAIEIDIPVVSHTT | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27110
Sequence Length: 244
Subcellular Location: Cell junction
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Q2G015 | MNMKKKEKHAIRKKSIGVASVLVGTLIGFGLLSSKEADASENSVTQSDSASNESKSNDSSSVSAAPKTDDTNVSDTKTSSNTNNGETSVAQNPAQQETTQSSSTNATTEETPVTGEATTTTTNQANTPATTQSSNTNAEELVNQTSNETTSNDTNTVSSVNSPQNSTNAENVSTTQDTSTEATPSNNESAPQSTDASNKDVVNQAVNTSAPRMRAFSLAAVAADAPVAGTDITNQLTNVTVGIDSGTTVYPHQAGYVKLNYGFSVPNSAVKGDTFKITVPKELNLNGVTSTAKVPPIMAGDQVLANGVIDSDGNVIYTFT... | Function: Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decre... |
Q8GHB1 | MSKALANMPGDDYFRHPPVFDTYAEHRAYLKFRHAVALRHFARLGFDQDGLAGLITVADPEHADTYWANPLAHPFSTITPADLIRVDGDSTETVDGQRRVNIAAFNIHAEIHRARPDVQAVIHLHTVYGRAFSAFARKLPPLTQDACPFFEDHEVFDDYTGLVLAKDDGRRIAKQLRGHKAILLKNHGLVTVGETLDAAAWWFTLLDTCCHVQLLADAAGGAEPIPAEVARLTGQQLGSHLLGWNSYQPLHEATLARNPDLAAMAPALPPQTPALAR | Function: Involved in the biosynthesis of ring A of the aminocoumarin antibiotic clorobiocin . Catalyzes two consecutive oxidative decarboxylations of 3-dimethylallyl-4-hydroxyphenylpyruvate (3DMA-4HPP) to yield 3-dimethylallyl-4-hydroxybenzoate (3DMA-4HB) via the 3-dimethylallyl-4-hydroxymandelic acid (3DMA-4HMA) inte... |
P09870 | MLRRKVSTLLMTALITTSFLNSKPVYANPVTKSKDNNLKEVQQVTSKSNKNKNQKVTIMYYCDADNNLEGSLLNDIEEMKTGYKDSPNLNLIALVDRSPRYSSDEKVLGEDFSDTRLYKIEHNKANRLDGKNEFPEISTTSKYEANMGDPEVLKKFIDYCKSNYEADKYVLIMANHGGGAREKSNPRLNRAICWDDSNLDKNGEADCLYMGEISDHLTEKQSVDLLAFDACLMGTAEVAYQYRPGNGGFSADTLVASSPVVWGPGFKYDKIFDRIKAGGGTNNEDDLTLGGKEQNFDPATITNEQLGALFVEEQRDSTHA... | Function: Cysteine endopeptidase with strict specificity.
Catalytic Activity: Preferential cleavage: Arg-|-Xaa, including Arg-|-Pro bond, but not Lys-|-Xaa.
Sequence Mass (Da): 59733
Sequence Length: 526
EC: 3.4.22.8
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Q5ZKJ0 | MLSRSSFTSLAVGVFAVYVAHTCWVMYGIVYTRPCPSGGAAACVWPYLARRPKLQLSVYTTTRSNIGAESNIDLVLNVEDFDIESKFERTVNVSVPKKTRNNGTLYAYIFLHHAGVLPWHDGKQVHIVSPLTTYMVPKPEEINLLTGESTTQQIEAEKQTSALDEPVSHWRSRLTLNVMVEDFVFDGSSLPADVHRYMKMVQLGKTVHYLPILFIDQLSNRVKDLMVINRSTTELPLTVSYDKISLGKLRFWIHMQDAVYSLQQFGFSEKDADEVKGIFVDTNLYFLALTFFVAAFHLLFDFLAFKNDISFWKKKRSMIG... | Function: Scramblase that mediates the translocation of glucosaminylphosphatidylinositol (alpha-D-GlcN-(1-6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol, GlcN-PI) across the endoplasmic reticulum (ER) membrane, from the cytosolic leaflet to the luminal leaflet of the ER membrane, where it participates in the bios... |
Q6DHU1 | MFPKTSFTSLIVGVFLLYVLHTCWVMYGIVYTKPCEKRRAESCISPYLAAKPRLQLSVYTALRPNADGGHSLIHREEEFDVNTKFEKLVNVSLPKKTRKNGTLYAMVFLHQAGVSPWQDPHQVHLVTQLTTYMLPKPPEISLITGQDEPEKPDQQKQSSDSELDRPVSHWRSRLTLNVVSENFLFDREALPGDVHRYMRVYQSGKKMIYLPLLFVDELSNRVKDLMEINSSSTELPLTITYDSIALGKLRFWIHMQDAVYSLQQFGFTEKDADEIKGIFVDTNLYFLALTFFVAAFHLLFDFLAFKNDISFWKHKKSMVG... | Function: Scramblase that mediates the translocation of glucosaminylphosphatidylinositol (alpha-D-GlcN-(1-6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol, GlcN-PI) across the endoplasmic reticulum (ER) membrane, from the cytosolic leaflet to the luminal leaflet of the ER membrane, where it participates in the bios... |
Q96KA5 | MWSGRSSFTSLVVGVFVVYVVHTCWVMYGIVYTRPCSGDANCIQPYLARRPKLQLSVYTTTRSHLGAENNIDLVLNVEDFDVESKFERTVNVSVPKKTRNNGTLYAYIFLHHAGVLPWHDGKQVHLVSPLTTYMVPKPEEINLLTGESDTQQIEAEKKPTSALDEPVSHWRPRLALNVMADNFVFDGSSLPADVHRYMKMIQLGKTVHYLPILFIDQLSNRVKDLMVINRSTTELPLTVSYDKVSLGRLRFWIHMQDAVYSLQQFGFSEKDADEVKGIFVDTNLYFLALTFFVAAFHLLFDFLAFKNDISFWKKKKSMIG... | Function: Scramblase that mediates the translocation of glucosaminylphosphatidylinositol (alpha-D-GlcN-(1-6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol, GlcN-PI) across the endoplasmic reticulum (ER) membrane, from the cytosolic leaflet to the luminal leaflet of the ER membrane, where it participates in the bios... |
Q8KG79 | MNTADTRQRLLDIEKQIASLREEQATVKAQWEAEKELIHTSRRLKEELEDLRVQAENYERSGDYGKVAEIRYGKIAEIEKALEENNRKIEARQASGDLIMKEEIDAGDIADIVSRWTGIPVSKMLQSERQKLLGIESELHRRVVGQDEAVRAVSDAVKRSRAGMGDEKRPIGSFIFLGPTGVGKTELARTLAEYLFDDEDALIRIDMSEYMEAHTVSRLVGAPPGYVGYEEGGQLTEAVRRKPFSVVLLDEIEKAHPDVFNILLQILDDGRLTDSKGRTVNFKNTIIIMTSNIGAQLIQSEMEHLEGRDADAALAGLKEK... | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein... |
Q7U637 | MQPTAEQFTEQAWAAIVAAQQLAQASRHQQLETEHLLLALLRQNGLAGRILSKTGVDVTTFEASVEGHLQRLPSLGSAPDSVFLGRSLNKALDRAEQRRDGFGDSFIAIEHLLLALAEDDRCGRQLLSQAGVTTNTLKEAITAVRGNQTVTDQNPEATYESLAKYGRDLTAAARDGQLDPVIGRDEEIRRTIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPQALQNRQLITLDMGALIAGAKYRGEFEERLKAVLKEVTTSDGQIVLFIDEIHTVVGAGASGGAMDASNLLKPMLARGELRCIGATTLDEH... | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein... |
P53533 | MQPTNPNQFTEKAWEAIVRTTDVAKQAQHQQIESEHLFLALLQEPGLALNILKKAGLEAAQLQQFTERFIARQPKVSGGNQSVYLGRSLDQLLDQADQFRKDFGDEFISVEHLILSFPRDSRFGRLLSQEFKVDEKQLRQIIQQIRGSQKVTDQNPEGKYEALEKYGRDLTEMARRGKLDPVIGRDDEIRRTIQILSRRTKNNPVLIGEPGVGKTAIAEGLAQRIINGDVPQSLKDRRLIALDMGALIAGAKFRGEFEERLKAVLKEVTDSEGIIILFIDEIHTVVGAGAVQGSMDAGNLLKPMLARGELRCIGATTLDE... | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein... |
Q8KA87 | MHFDPNKFTVKAQEALQAASMLASSKQNQQIEPEHLLSVMLGDHDNIACQIARKLETPVDTLLSVVDREIDRIPKVTGASATGQYISSDLGKVFDTALKEAEQLKDEYISSEHLFIAMSEAGVKVSKLLKDAGIDRNAILKVLTSFRGSQRVTSQNAEESYQSLKKYSRNLNDLVIKGKLDPVIGRDDEIRRVLQILSRRTKNNPVLIGEPGVGKTAIVEGIAQRIVGGDVPENLKSKQIAALDIAALVAGTKFRGEFEERLKALVKEVQASDGEVILFIDELHLLVGAGSAEGSMDAANILKPALARGELRCIGATTLD... | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein... |
Q7U3T3 | MTGTPASRGSLTHEPDRFSDPAWELLLAGQDMARRWRHDQLDVEHLIQVLFSDSSFRRWVEPLPLRSDDLLDRLEDVLADQPPARGDQLFIGEDLEQLLETADQVRGRWGDRSIDVPQLIVAVGADPRIGAELFAAQGLAVDRLESLLRQPSVSPAPAPPPVPTAASAPAPTPRSAPAPRVMAPEPEPMVELEREPSALEAYGRDLTEEAEAGSLDPVIGRDSEIRNLIKVLSRRSKNNPVLIGEPGVGKTAIAELLAQRIVAGEVPDSLQGLRLIALDLGALIAGAKFRGQFEERLRSVLEEVSRSDSGVVLFIDELHT... | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein... |
Q7NEW2 | MPIGIPKVPYRLPGGQSQWIDIFNRLALDRIIFLGREVDDEIANAIIASMLYLDSEDPEKDIFLYINSPGGSVSAGLAIYDTMQHVRADVATMCVGLAASMGSFLLTAGAKGKRTSLPHSRIMIHQPLGGAQGQATDIGIQAKEILYTKDRLNQILSERTGQPLERIERDTDRDFFMSAEDAKQYGLIDQVVQHRPV | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q5FUR3 | MTIRDRDPLEVFSNSLVPMVVEQTARGERSFDIFSRLLQERIIFLTGPVYDQVSSLICAQLLYLESVNPTKEISFYINSPGGVVSAGLAIYDTMQYIRCPVSTVCIGQAASMGSLLLAGGEKGHRYALPNARVMVHQPSGGAQGQASDIEIQAREILIIRQRLNEIYREHTGQTLEQIEQKLERDSYLSANEAREFGLIDKVVERNPHETTPDPS | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q5Z0M4 | MSTYTIPNVIAQHPRGGERITDIYSHLLAERIVYLGTPIDSGVANALIAQLLHLESESPDQEINFYINCEGGDLPSMLAVYDTMQHIGAPVHTTCVGQAIAVGAVLLAGGAPGQRAMLPHARVVLHQPAARGQGPIPDLILQADELVRMRSEIEAILSRHTGRSPEQLREDTDRDRVFTATAALEYGLIDTVLSPRG | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q8YXH5 | MTIPIVIEQSGRGERAFDIYSRLLRERIVFLGQQVDSNLANLIVAQLLFLDAEDPEKDIYLYINSPGGSVTAGMGIFDTMKHIRPDVCTICTGLAASMGAFLLSAGAKGKRMSLPHSRIMIHQPLGGAQGQATDIEIQAREILYHKRRLNDYLAEHTGQPIERIAEDTERDFFMSPDEAKDYGLIDQVIDRHAAGSRPVAMVGQ | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q928C4 | MNLIPTVIEQTSRGERAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLDAQDPEKDIFLYINSPGGSISAGMAIYDTMNFVKADVQTIGMGMAASMGSFLLTAGANGKRFALPNAEIMIHQPLGGAQGQATEIEIAARHILKIKERMNTIMAEKTGQPYEVIARDTDRDNFMTAQEAKDYGLIDDIIVNKSGLKG | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
P26567 | MPIGVPKVPYRIPGDEEATWVDLYNVMYRERTLFLGQEIRCEITNHITGLMVYLSIEDGNSDIFLFINSLGGWLISGMAIFDTMQTVTPDIYTICLGIAASMASFILLGGEPTKRIAFPHARIMLHQPASAYYRARTPEFLLEVEELHKVREMITRVYALRTGKPFWVVSEDMERDVFMSADEAKAYGLVDIVGDEMIDEHCDTDPVWFPEMFKDW | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q65RF6 | MALIPMVVEQTSRGERSYDIYSRLLKERVIFLSGEVEDNMANLIVAQLLFLESENPEKDINLYINSPGGSVTAGMAIYDTMQFIKPDVRTLCVGQACSMGAFLLAGGAAGKRAALPHARVMIHQPLGGFRGQASDIQIHAQEILKIKQTLNERLAFHTGQPFEVIERDTDRDNFMSAEDAKNYGLIDSVLVKR | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q9MUV8 | MPIGIPKVAYRIPGEAVSTYVDVYNRLYRERILFLGEDLDDEVANQLIGVMVFLNSEDDTKGIFFYINSPGGSMNAGLGVYDMIQHVNVDVTTICMGLAASMASFILAGGTPGQRLMFPHARVMLHQPMGGNGGKAKYMVEESVEVKRLRELIAHLYVKRTGQSLEKIRKDMNRDNFMRPRQAKEYGLIDHMVTNVNELDELDKQSNDLKKLGKVNLTNIETSNKSELK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
B7V5T6 | MAATGVDKDRPRAMTSTTYLGLLLVGIQVLGFVAAIHAVLTVRTAQGAIAWATSLVFMPYLTLLPYLVFGRSRFDAYIEARRQANREMHLAAAELDWRPWVEEALAARQVSGYKGLKALVRMTRTPTLANNRVRLLVNGEASFEAMFKAISAARQVILVQFFIVRDDALGQRLQQLLLERAANGVEVFFLYDAIGSHALPHRYVERLRQGGVQMHGFSTGSGMLNRFQVNFRNHRKVVVVDGECGFVGGHNVGVEYLGEKPPLAPWRDTHMELRGPAVACLQESFAEDWYWATHSLPPLILPPQYDSEGALCQVVASGPA... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
Location Topology: Multi-pass membrane protei... |
A0A345BJN2 | MAGDLWLVGDCTNHGGLSDAIIVSPDYRLLPEATGADIFDDVEAFWNWLHTSLPSLAQSYSWQAQPDLTRILCVGQSGGGSMAVHSALLHPEYSIKVIVSLYAPLYHNVPNLTVPRPRRILGTMPPPPRKAEGLIRSYIKQSKGSVRTGGNPFDMWELLLCLLQQGRLISLMNIKPDSRLDTPFLLRQVGKLPPLWLIHGEDDSVVGPSTICVHRVIF | Function: Probable carboxylesterase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8-dioxobicyclic[3.2.... |
A0A345BJN3 | MVQRSHRSLVLETGGIQDRNSAKPFQVRRLYCTPIFHAFSFPEMVVNTIRLGFPSFYMRRFDESFADKIHEFGITETMAAPAMLLKIIQWTEKHEEKRFKLQGLRTILCAGAALASRLRASFLQLFDSASVRIVQVWGMTEGGWFATFWYPEHDDTGSIGRPLPTCQIRVSEVSRAELPDGRQVGELLVKGPQLLTAYKGHPDATKEALHDGWLRTGDIGYCADGKIYIIDRAKDIIKVNGWTISPAELETVLHQIPGIVDAAALSYGTGTKEHVAMFVVAEGPSLLVADIKHHLLQQVARFKVATCEIHLVDSLPRSPS... | Function: Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8-dioxobicyclic[3.2.1]octane-3... |
A0A345BJP6 | MATATLPATVGVIGLWDGTTDGKEGFMDYATGDTNVKQPKEYEIEVHDIRKLDPQPTLLNNGYELVDIPTVVTEEQFSESGKSEKGKAYIKDVYFAECKRIIQEVAGGVDTIIPVSFRMREQKGEKESTTKKLGNIESRYAPRPVAHLDRDTPTAITVLEETVGKEKAQELLSKHKRNPATMWPLCFLNHDRIPTWNYDTHVGHVWSLNDPRVSDRGEKTYDCVVKYDERYDYHYVSDLKPEECLVFCSFDSIPKYAMPHSAFWDNNVPADAPNRRSIEVRSLVFF | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8-dioxobicyclic[3.2.1]octane-3,... |
A0A345BJP7 | MSTTTTTLHTTTGTVYVADGTTDGKIGYYNHTDDSTNVIRKPIPIQVEDARTLSKSPTTKEEGYQLVDFHTKLPEGHFLDSKSPENKKVIEQVYFDECRRLVQEVTGAAEAYPYVYRVRNQEQNAKASNKSNFHTDFVPVVHVDRDDITAPQRLRASLGAEKAEMLLSKYKSYGSINVWRPVKNVVQKWPLMLVDHKSIENWDYSTHMFTLHSSNDERVATRGAKDHETILTHDKRYRYIYASDMTPDEAWLFFAFHSDPALGIPHGAFWDDSTKEEALTRCSIEVRIWVFFD | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8-dioxobicyclic[3.2.1]octane-3,... |
A0A345BJP9 | MNVDTTSPQAPLAGVESKQDGASNEATAKAESTTHDQNESSSFDERPVHSALSERQRSALLAVASFAAAISPASTTTYYPAITTLANDLDVSITQINLSLPAYQIFQGLAPTVAAAFSDRFGRRPVYLVSLSINMAANLGLALQKNYASLMVLRCLQSSSSGGTVALGQAVMDDLITSEERGRYMAYLTLGLVMGPALGPLIGGLLSQYLGWRAIFWFLMILGGFFFLMVLTFFRETNRSIVGDGSVPPQKWNRSLVQIFRKDKLIANPESLAKKRISVNPLASIQILRNKENFIVCMYGALLFGGYASVISIFATQLEE... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS).
Location Topology: Multi-pass membrane protein
Seq... |
A0A345BJQ0 | MVSTRGVLYYLLRPKELRPILQWKALHGLGHQRDEKNESPDVKACYQYLALTSRSFAAVCQQLDRELLMPICIFYLILRGLDTIEDDMTLSKEVKEPLLRNFYTTIYDQTWTFNDSGTDEKDRELLVHFDCVAREFHKIKDEYKIIITDITKQMGNGMADFVVSGDLTGIQKIKDYELYCHYVAGVVGDGLTRLFVEANVADPSLLKNPRLIESMGQFLQQTNIIRDVREDHDEVRHFWPKEVWSKYAQDFDHLVSPKPQDRKKALQCSSEMVLMALNRADDCLNYMAGVREQTVFNFVAIPQSMAIATLELCFQNPAIF... | Function: Squalene synthase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . Catalyzes the condensation of 2 two farnesyl pyropho... |
A0A345BJP2 | MPSISTDFDVRPYEDVPAQTIALSVPDAAAPKHCPIQLLFWPVDGKSSFTRGYENLKEGLSRLLSDVPVLAGKLERGWKGDSRYLAVNISSDASVEFVYEDVSAEDIIPSYDNLAQNGFPTTGFRDILSPKMSLGPMVEGSPMMCAKLNMIKGGAILAYGFSHVLADGWANSELGRLWALHAAQVSQGIEFKKHKDATPDEDIRRRLSTLPEYDTDVPLDAFLQITPSEEATNFLHKDVLSAEKAKKKAREKMMATLLAAGEVPELPRFTFWRFTPEKLKELKQAAAGSDPDKWISTMDALAGLFWSRIALIQGQSSNGH... | Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8-dioxobicyclic[3.2.1]octane-3... |
A0A345BJN8 | MAASTKPTTKLSTEEDDVSRRDSESSADFMKSNEELQATMIPEDDGANPATGQPTWTILSDTEIKSVLVVASFAAAISPFSTSTYYPVVTAIARDLGVSVSKINLTMSSYQIFQGVAPTITAAFADTYGRRPMFLVCFVTYFVANVGLALQNDFTTLLVLRCLQSTGSSGTFALAQAVTADITTRAERGRYLIYATLGSTLGPFIGPVIGGLLVKFLGWRSVFWFLLCMGTVFALLIFIFFGETARPIVGDGSIPPQSWNRSYLQMRSKGVSNLKPNLASLERRKSRPNPLTSLALLWDRENFILSVSGGLLYAGYSSVT... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS).
Location Topology: Multi-pass membrane protein
Seq... |
P0DQV5 | CCSALCSRYHCLPCC | Function: Slowly and reversibly inhibits human nicotinic acetylcholine receptors (nAChR) alpha-7/CHRNA7 (IC(50)=45.7 uM). It is unknown whether it inhibits nAChRs by a competitive or a non-competitive mechanism.
PTM: Has a free C-terminus.
Sequence Mass (Da): 1662
Sequence Length: 15
Domain: The cysteine framework is I... |
P0C1T9 | GRCCDVPNACSGRWCRDHAQCC | Function: Mu-conotoxins block voltage-gated sodium channels (Nav). This synthetic toxin moderately blocks rNav1.1/SCN1A, rNav1.2/SCN2A, rNav1.3/SCN3A, rNav1.4/SCN4A, rNav1.5/SCN5A, and mNav1.6/SCN8A . This block is very slowly reversible . Causes seizures when injected intracranially into mice.
Sequence Mass (Da): 2441... |
P01523 | MMSKLGVLLTICLLLFPLTALPMDGDEPANRPVERMQDNISSEQYPLFEKRRDCCTPPKKCKDRQCKPQRCCAGR | Function: Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin potently blocks rat Nav1.4/SCN4A (IC(50)= 19-110 nM) . It also moderately blocks rNav1.1/SCN1A (Kd=260 nM), rNav1.2/SCN2A (IC(50)=2.7-17.8 uM), and mNav1.6/SCN8A (IC(50)=680 nM) . The inhibition is reversible. In vivo, induces paralysis to an... |
P85017 | KCCMRPICTCPCCIGP | PTM: Reg12e and reg3e are conotoxins with identical sequences, but different post-translational modifications. Reg12e is C-terminally amidated, while reg3e is not.
Sequence Mass (Da): 1728
Sequence Length: 16
Domain: The cysteine framework is III (CC-C-C-CC). Classified in the M-1 branch, since 1 residue stands between... |
O85728 | MLVVAFKPGHDGAVAAIDDRRLLYSLESEKDSRPRYSTLLPTTFLDIAERLGAIPDVVALGGWADLRPRGVVYTGAGYEGTQEPTVTTSRFFGKEVKFFTSTHERSHIYMALGMAPKDGAPLKSVLVWEGDVGAFYLVDSEHRIIRTIPVMTGPGARYSFLFGLADPTFPDTGGKPRLNDAGKLMALAAFGDSADASPDIRHVVERVLKQDSMYPAPKAEYRDSVLHNAGVESEECKIAAALLTERLFETFAEVARRELPEGTPLYISGGCGLNCDWNSQWAQLGHFSSVFVAPCTNDSGSALGTAIDALTTFTGDPHID... | Function: Catalyzes the carbamoylation reaction in the cephamycin biosynthesis.
Sequence Mass (Da): 57370
Sequence Length: 521
Pathway: Antibiotic biosynthesis; cephamycin C biosynthesis.
EC: 2.1.3.-
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Q04733 | MTSVRGASKTGRTSKTSTATTALVLACTAHFLVVFDTSVITVALPSVRADLGFAPASLQWVVNSYTLAFAGLLLFGGRLADIHGHRRVFLGGLAVFTLTSLIGGLATSPASLIAARAGQGAGAAVLAPLAVTMLTTSFAEGPRRTRALTISTAVALVGGASGNLLGGVFTEFLSWRSVLLVNVPIGIPVLFLAARVLAGPRKRPWGRVRLDLPGAVLATAGLTLLTLGVSQTHEHGWGEAAVAVPLAGGLLALLAFVVVEARFAASPLIPPRLFGLPGVGWGNLAMLLAGASQVPVWFFLTLSMQHVLGYSAAQAGLGFV... | Function: Involved in cephamycin export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49325
Sequence Length: 486
Subcellular Location: Cell membrane
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