lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Sequence:
MAQDLSSLPTALFTQEQVRDAELLAVSEGKTTLYQLVERAGRAAFDCLATQIARQPRLESMPLLVLAGSGNNGADALVCARLALEAGHKVMVFLLKTKGTPEFEQALSAYLNQGGIADSPNIDAILQAPMLIDGLLGTGVHGGVREEVAALIQAINQSDAWVLSLDLPSGIVADTGVVAQAAVMADLTLCFGGLKQGLLTSKARHYCGDLDFADLGLTPFFKTPNATRVGGEILKSYFAARARDSHKGQSGKVTLIGGDFGMAGAIRLASEACLRAGAGLVTVISRPEHQLTVNVSRPELMFWGCELVDMEVYLRLGWAQVVVLGPGLGKHDWGYNLFKAAGLSDKPCVLDADALNLLSNEPRRQTNWVLTPHPGEAARLLGCNVAEIEQDRFAAVRALQQKYGGVVLLKGAGTVIFDGKQMVVAPVGNPGLASGGCGDVLSGIIGALMAQGMDNMQATVVGVVVHGCAADLAAVQGERGMLASDLMPFIRQLVNSDLL
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MAAVEKPAEANPSPQVGIKELAEPAPVIGKDNAKESPMENLLEKLRAKASQYKPWGDMAKALRMALMEKHHLVDSADRNRLQKCLDTIQKLIFTTGPDGQECFISSDMFYVEVLLETSGEVKDVKIAHHGDPVSCPELTQVLLKGDFAEFTSHLEGLASIYQLNADNLPSFAALSNLNSTTLPASFVLKLPQPIPMALALVRKIHAITSIECADTTCCQSLLSLIITQASEGKLNGSSDRGLNVTLPDQHHCYYLSGSPDLQGVLVSGVQFTHPTHVPQILVFLRQQLLFNSLIASCVRPASRQNAESSHMFEVSTTSISNISISFEHPLDESLATVDLNLNEITSVKCRIYTLNSDISICSDEYASKVMQRCLSIPVTMRAVIRKAQGQRMRMSNQTDSYYSALNSNGPSYLPHLPGYGGGAGGGAFGSGGPDFASGTPPPKRGGTLGSLLGQGGGGAGFQQPGGGPGKQSAQPNMMLMSMLSDVPSASSSPSPSQQSSYPFLSQAKPRKQRKRKATSSDGRSPKRKAGVEDDGGGGTPTPADLEDSTSISLTSFEGRQTPSGDAPSFGKGDGGHTLPGEPFLEADAGQKKAALLNPAESSSVEEFHQRRPLQSPSESFRGFLSEGPPGDATGDDCKPGTKALPASQRPLAAPPQCRKIKRVKSEEGRGEELKLEREGSRSQDSGPKNLLPGGDSERLLASSLGGSVASAAGKSHSVSPPVIATSFKIEKSGDGLKISKAEGRQSSTKGRDPKGRDNRKERKRKRAESVDLSSSHGAKLAFDTSSLDSVLQATLLPLESGDGALHAFNLTMKPQGSVSPALGQAAPARVMGKKSGSQGSLPSGGNGKSDKPSKPLSGAKTNEVDGRLATSPTKLLKHKPSPGPPKSGTGTPGRPACYAGQPSLVGPNTSPSKPSSKSASAAPPGSTLKLKHLNLPSSTTITPVAPKVQPAQLPSPSSSSAASITIVPTGGASSNNLNKPPKSRKGSLSAVIAKLTNTAAPSLPPVDPSSGPPRLEGGVKSSEKRDSPTLGKESKDKEALLKNSEGKMKYSSSDQFTVKQSSGIKLTVTKTSGTYKSSSSKAKMGMSSSKASAGVSSSSKAKGTGSLGSASRPPGAPGGLAKKPSSLSSSSLSGLGRAPSKPSQKSSSPNTTNPAISQNPLNPSSALRSKTPTSGSTPKRPDEFPGAEENDPDRALRLLLSQPKAMESTQPLEQWQPLSLKSQTPPSVDSSVKPDFEDKTPWVSSSTDVKPNNSIATVVAKAPLENGPDSALTPTDLSSSSPRFELISSTLEEGANTTTPSFKALPLLLSASAPSKLPAKTKPTSDEDSSPEDGLVIDFPESIDSKKGSSSLSSSRAQSPKDGSGGGGGSQESGTSLKAAVSPGPALSAKSPYFTAQSPSLKSPQVGSPPSNHSVSSSISRPSPCVIDDDLMDEAIMGLGK
The following text describes a protein:
Function:
Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively.
Sequence:
MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANEQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFWSDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIALKSL
The following text describes a protein:
Function:
May be involved in constitutive endocytosis of a-factor receptor STE3.
Miscellaneous:
MISCELLANEOUS: Present with 815 molecules/cell in log phase SD medium.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
The DHHC domain is required for palmitoyltransferase activity.
Sequence:
MTSMSIIDDENVKKTSNGAAVVTDVAQHAVSDSDNNKAQLLGDGSNTEYVVDIFIEAAKDGDLKVVKDVVESGAVDINNDRIDELSGLHWACINNRFSVAKFLLLRGANPNQAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLYFVVNNNDNVDIDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQRVICDLILSGANFYERNNQKQDCFDLAEGMGTKSLFEQALQHHGYDRLGNQKDKLFKKSSHAQFTIFLSPFLLMVYIYLISLVLSPVLAIMLSLLVTVVMVNTLKKFVLPCLPRKNTYKVSLTRTPFFSGLFLSTFCFLIYIWTKKLYPYSVSDYTMKNVQFLVTSFLTVVLFLRLVRSDPGCLKTDDSLTSIQETIKQLIDLGKFDRENFCVETLERKPLRSKYSFFSGALVARYDHYCPWIYNDVGLKNHKLFVFFAVTVQYHMFLFMWLCLAYFKKTNYIYEQVEEYARCALLKNETLCKGSNYDPSTFFLFIWISVNFIWLGAMLIVQFFQILKGITTPELFILIKEEHKAKFINLIPFENSIYTSESKGVEDSDMIPEGPSATTITHTISIDGLEPRNRRRAILSACFSMMGINQWLVTIKEIVGITHILHGQVPQQHHSSLLRSFLVTNHWKTNLTDFWLNSDVTAPLWQRFFYSSDTSKAMLGGTEVDYYELYEYPAREGEVLRPN
The following text describes a protein:
Function:
Involved in floral organogenesis. May play a protective role in flowers by protecting the reproductive organs from potential pathogen attack.
Subcellular Localization:
Secreted, cell wall. Vacuole. Note=Possibly the cell wall or vacuole.
Sequence:
MARSLCFMAFAILAMMLFVAYEVQARECKTESNTFPGICITKPPCRKACISEKFTDGHCSKLLRRCLCTKPCVFDEKMIKTGAETLVEEAKTLAAALLEEEIMDN
The following text describes a protein:
Function:
Sugar-phosphate phosphohydrolase that catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate. Also catalyzes the dephosphorylation of 2-deoxyglucose 6-phosphate (2dGlu6P); this is a biologically important activity in vivo since it contributes to the elimination of this toxic compound and plays an important role in the resistance of E.coli to 2-deoxyglucose.
Sequence:
MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRRNELPDTLGLRIDMVVDLWYARQPWNGPSRQEVVERVIARAISLVEETRPLLPGVREAVALCKEQGLLVGLASASPLHMLEKVLTMFDLRDSFDALASAEKLPYSKPHPQVYLDCAAKLGVDPLTCVALEDSVNGMIASKAARMRSIVVPAPEAQNDPRFVLANVKLSSLTELTAKDLLG
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MSAEESKIKNVAVASSIDTPSSEEEKEEIKSETGTDLGFSLDILSLGPKKKLLVIPLGGLIVRRAHVRERFTLPKNRRPNLSYGKFMIYKRRYCEGFLKFCFERFEVGLWSSAMEHNIQAVLNHVTGDVKTKFLFTMDQKECTDTGFTCLKNKNKPLFLKQLKYIWEKKYPNGEYSASNTLLITDPEKAILNPPNTAIFLKEYDVKKKDGDFLGPDGELRAFLDGVAEAKDVQSYVKEHPFGEPAITPSHSDWDYYSKIIRFFDKKDK
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MSGYESLADVTLRPWPAAKKEELSPQDLLLQIEQLGTERGHLRDVTEKSLQEDMAAGKGASEEAAGSLEQKKKKKDATSREERLQEVLKAQHEMCMHMEWAKFAATNTVDLISLILSADPNRRSLANFSHSMQMQGLQQGLPFGAFGLGKESHVHHDRKHDEQDVLKEYAHRQELVSKGARMEALDRATDDILKAARKLEKEVRRETKYWQEIVSISDKGWPIQRHRIKADVWTASNHFKARGLAPLRMDKDGSIILDPALASKPKSLRVRIRQDGNVTGTSHLPTAVGESDTTIEKTIQRTRNSLFEEELFHEMSLEARQLMAHGVDYRDSIIHIDASGSAGQQRSMTLLIDCIPLEGPNPASQEHANDWLAQNIVEGLRLLLTHEQSMRLYRRTQVPPPLTGQKREKQSPSLLRTLLAIFHHLQGVDSLYGYLNTVAETLKNAGLPIELDTTREVSWARLANTLRSSPKKGISAADQLLDIFSKPFDGRATLTLPALGGTPSESITLSTRTVIGQPTFGSEHRLTLPSTLAADLGLFPQHKFSSVEETVSYLDWVLSLNIAHRQLKNHFSTRAAIKGDDARVTIRGKNTKKTAIADSDILIQMQDGKLRATATIAESEEGAEEAEQSYTWIGKEASMSLTERIKSWVG
The following text describes a protein:
Function:
Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity).
Miscellaneous:
MISCELLANEOUS: Most taste cells may be activated by a limited number of bitter compounds; individual taste cells can discriminate among bitter stimuli.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MNGDHMVLGSSVTDQKAIILVIILLLLCLVAIAGNGFITAALGVEWVLRGTLLPCDKLLVSLRASRFCLQWVVMGKTIYVLLYPTAFPYNPVLQFLAFQWDFLNAATLWFSSWLSVFYCVKIATFTHPVFLWLKHKLSEWVPWMFFSSVGLSSFTTILFFIGNHSIYQNYLRNHLQPWNVTGNSIWSYCEKFYLFPVKMITWTMPTAVFFICMILLITSLGRHMEKALLTTSGFREPSVQAHVKALLALLSLAMLFISYFLSLVLSAAGIFPPLDFKFWVGESVIYLCAGVHPIILLFSNRRLRAVLERCRSSRCRTP
The following text describes a protein:
Function:
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Peripheral membrane protein.
Sequence:
MASLISFSLLPKPKAVRSSISAPQTQTINTEKLEDKFGRKGIKFSESNNIPMVELKVRNGSSLKLSLSDAHVLSYKPKVYWKDEGFEEVLYTVDGDESRGGVGVVIVNGEEPKGGSSVISGCDWSVKDTDSDAIDALQIELSCTAGVLDITYIVSLYPVSMATALVVKNNGRKPVTLKPGIMSYLRFKKRSGAGIQGLKGCSYCPNPPLSSPFELLSPSEAMKAESSGWFGSEEGEKPGIWAVEDSVITLLEKKMSRIYGAPPAERLKAVYNTPPSKFETIDQGRGLFFRMIRIGFEEMYVGSPGSMWDKYGKQHYFVCTGPTSMLVPVDVASGETWRGAMVIEHDNL
The following text describes a protein:
Function:
Involved in DNA recombination repair and meiotic chromosome segregation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSQTINSELNENATSQCKEDLKVSLSESDLRDSQGQLGIENPPKCNNSGNHSDNLGFIEQSETVHPENEKALTPDLRDTKIHTSLPITTPFSKKRAREAKNILLKPFKSPLRQTASPQVADTNLKPSLAVTNLNSDETNTSSEPVTSPLRTTPNSIKRQKRLFKSPISNCLNPKSDPEITQLLSRRLKLEKEVRNLQEQLITAETARKVEAKNEDKDLQTLIQKWKNAAQQAAEVLFKPMAERIRLAGGVTQSFRIEEGENKGQIQEVRTEFTMSMFLNQFGVPVHLMSFDEENGDWKS
The following text describes a protein:
Function:
Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane. In a functional T2SS this subunit helps assemble the outer membrane channel.
Miscellaneous:
MISCELLANEOUS: In many other E.coli strains this gene is part of a type II secretion system, but in MG1655 the locus is missing a number of genes.
Subcellular Localization:
Cell outer membrane; Lipid-anchor.
Sequence:
MSIKQMPGRVLISLLLSVTGLLSGCASHNENASLLAKKQAQNISQNLPIKSAGYTLVLAQSSGTTVKMTIISEAGTQTTQTPDAFLTSYQRQMCADPTVKLMITEGINYSITINDTRTGNQYQRKLDRTTCGIVKA
The following text describes a protein:
Function:
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins.
Subcellular Localization:
Cytoplasm. Nucleus. Chromosome, centromere, kinetochore.
Sequence:
MAASSSSSSAGGVSGSSVTGSGFSVSDLAPPRKALFTCPKAAGEMLEADGSERFLCESVFSYQVASTLKQVKHDQQVSRMEKLAGLVEELEADEWRYTPIEQLLGFTPSSGGK
The following text describes a protein:
Function:
Probable transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MKKVKLSLIANERSRKTSFIKRKDGIFKKLHELSTLCGVQACALIYSPFIPVPESWPSREGAKKVASRFLEMPPTARTKKMMDQETYLMERITKAKEQLKNLAAENRELQVRRFMFDCVEGKMSQYHYDAKDLQDLQSCINLYLDQLNGRIESIKENGESLLSSVSPFPTRIGVDEIGDESFSDSPIHATTGVVDTLNATNPHVLTGDMTPFLDADATAVTASSRFFDHIPYENMNMSQNLHEPFQHLVPTNVCDFFQNQNMNQVQYQAPNNLFNQIQREFYNINLNLNLNLNSNQYLNQQQSFMNPMVEQHMNHVGGRESIPFVDGNCYNYHQLPSNQLPAVDHASTSYMPSTTGVYDPYINNNL
The following text describes a protein:
Function:
Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine (acp3U) at position 20 in the D-loop of several cytoplasmic tRNAs (acp3U(20)).
Subcellular Localization:
Nucleus.
Sequence:
MANPKSLEARQAYIDQNPFEGFKIDDNSILGKLSGRHACPKCNKSRKYFCYSCYVPISELEGVLPTVKLPIKIDIIKHKHEIDGKSTAGHAAVLAPSDVSIYTYPEIPDYSGENVVLIFPSQHAISISQLVKQENYDCVKNSNNSPLEAVPKGFNPGTLMKNVLKCGDSITVDNSNKLPITKAIFIDSTWNQSKGIYKMKGSENPLCGDPKSHFTFWSTKAVXL
The following text describes a protein:
Function:
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Subcellular Localization:
Cytoplasm.
Domain:
The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Sequence:
MKDYYSILGVSRDASQEEIKKAFRRLARKYHPDLNQGDKSAEEKFKEINEAYACLGDPVRRANYDRYGTAEGPTGNGFGFETYTTFTDIFEDIFEGFFGSFGFRKNKPTKGADLRYDITITLEEAARGVEKTIKFPRWEICGTCNGSGIKPGSEPIICSSCGGSGYIRYNQGFFSVSKTCSKCGGTGRIIRDPCFDCAGNGKIKVEHELTIKIPPGVDSGSKLKVSGEGEIGEFGGPRGDLYIFVNVKEHEFFKREGINLYCSIPISFVRAVFGGEVEVPTLDGKEKIEIPAGTPSGRVFKLRGKGLPRVGGTHRGDQIVTVYIDVPKKLNERQRELLEEFARISGEEIKKGSKGLKDKLKDIFSM
The following text describes a protein:
Function:
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
Miscellaneous:
MISCELLANEOUS: In the transfer reaction, the free carboxyl group of lipoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Subcellular Localization:
Cytoplasm.
Sequence:
MTKTRILLSDSTDPWFNLAVEDTIFRSMPADQRVLFLWRNADTVVIGRAQNPWRECKTDRMEQDKVKLARRQTGGGAVFHDLGNTNFTFMAGKPEYDKEVSTKIVLAGLQKLGIHGVANGRNDLVLEDEQGIRKFSGSAYRETLDRGFHHGTLLLSADLNRLADYLNPDLKKLQAKGITSVKSRVINLNTVKADIEHQQVCEAIMQAYCEHYQQQVEPELISPQSFFDLPGFEQKFAQQSSWDWNFGQTPPFTHHMDERFSWGGVEVYLEVERGTIVQATIFSDMLDPYPMEQLALRLSGLTYNKTALEPCLAQLMQELPQYQLPLEEFQRWFIDQID
The following text describes a protein:
Function:
Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin.
Subcellular Localization:
Secreted, extracellular space.
Sequence:
MNWHLPLFLLASVTLPSICSHFNPLSLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIVSKKNKDIVTVANAVFVKNASEIEVPFVIRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDLWYNFIELPYHGESISMLIALPTESSTPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITRSENLHVSHILQKAKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP
The following text describes a protein:
Function:
RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tRNAs. Requires a tRNA-binding adapter protein for full tRNA acetyltransferase activity but not for 18S rRNA acetylation.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVRKKLDERIRTLFSHCLRTNQRALLLLVGDHGKDQIPNLHQIMDRTANMSKSERLGSINNGNSSVLWCYKKELGFSTHRKKRMEKIKRDKKRGLAKSSSSNNAAATAAAEQMDNFELFLNNTNITWCYYKDSHRVLGTTHSILVLQDFEALTPNIMARTIETVQGGGLVVFLLRTVKSLRQLYAMTMDVHSRYRTESSGDVVPRFNERFILSLGGCANCLVCDDELNILPLSKKTLARLTKMGTSPTAYDDDGEEQQQVVTYKTDDDVQLEQLKQTLQDTPHVGKLVELTKTLDQARAVLTFLEASGKSTTVSLTAPRGRGKSAALGLCLAGAISFGFNSVVVTAPEPENLVSVFQFLIEGLKALKYQEHYDYTIGYNYGMDSNEGNNRGEKAGRDNIKCIVSVEIHGRGTQRQTVRYVKPSDVDKFVGAELVAVDEAAAIPLPIVRKLMQLTFLSSTINGYEGTGRALSLKLIKELRDSNSKRRSGRWAAEAAAAKGAVSSSGSATGPLKELELSHPIRYALGDPVEKWLNNLLCLDYTLALRGGAPAPAECELYHVNRDALFSYHRLSESFLQKLWGLYTSAHYKNTPNDLQMLSDAPAHNVFVLLGPTAESDGDEDALPDILAIVQTSLEGKLSRKTIQAQLARGHRSAGDLIPWTMSQQFGDGNFAQLSGARVVRVAVHPAVQGLGYGSRAMELLFRYYNGEMVSLNGGIEETSDSENETPSESESEDEPASNALIHKEALKPRKKLPPLLLPLSTIPTPRLDWLGTSFGLTPSLHNFWQRKVGMTLLYLRQTSNELTGEHSAIMIRALPRRSGWDDAWLPAFGVDARRRIGRLLGGSFRGMDVSLAVSLMGDVAALQEVKKRSGTQSTKLTSSELHYHLTPHDLQRLELYSRNLCDHHLVSDLIPSLSQLYFTSRMGHSFRLSSVQAALLCGLGLQQKSVEDLTKELGLPINQVLAMFNKAVKKMSLAFNQILVEEESKSLLGGDAMRKAETKVNKMRDVVGQTLEEDADEGAAVAMEALKKGNAENSRKSVIMKYALKGTDEEWATALKDKEGVDGATVQIKLKTPKKRKADGGDVLESILKHEKEAQSGKKEKGGKKKSKKKSRKTM
The following text describes a protein:
Function:
ppGpp hydrolyzing enzyme involved in starvation response.
Sequence:
MPNSVSINSSPTTTNVLLNPPLRSPSYSEVELIRTPPARSFTPTPPVSRSLSANGSPTASTPGRLHGESDLSLLLRTLDFAARKHSCQRRKDVDQSPYINHPISVANYLSSTGITDVHVLQAAILHDTVEDTCTTIEEIADQFGIDVARIVEECTDNTALDGLQRKVEQLRAAPSKSKQAQQVKLADKLHNLESIRRSPPVGWGMKRVQAYFIWAKRVTDICAPAHPPLAERLQRLYETAHTRVNGTYFPCHPEVCGPLTEEEKELVDKRLRELKEGDTMCPEPLFF
The following text describes a protein:
Function:
Protects DRG2 from proteolytic degradation.
Sequence:
MTDYGEEQRNELEALESIYPDSFTVLSENPPSFTITVTSEAGENDETVQTTLKFTYSEKYPDEAPLYEIFSQENLEDNDVSDILKLLALQAEENLGMVMIFTLVTAVQEKLNEIVDQIKTRREEEKKQKEKEAEEAEKQLFHGTPVTIENFLNWKAKFDAELLEIKKKRMKEEEQAGKNKLSGKQLFETDHNLDTSDIQFLEDAGNNVEVDESLFQEMDDLELEDDEDDPDYNPADPESDSAD
The following text describes a protein:
Function:
Transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MMLSNISQTKAELLSGLGSSLTSSPGNVSAATMKLEAVMENLQRQHQQRMMEQHKNDDVISNDVRCDDFSDGGERQRSYSGSPKEDSDEDRNDMTSPMMRDDDDVMQSDGRSPEPDKTSLITQQMAFAAALAQRSSPDGSLSSLVPQAMMQHFGQFPASFDASQLPQGFRELAMLQHQHVAQRMAMEAQKRMQQDHNIQQSTNHIPTPSSASSHTSSGSVTSQTNSCNGSQQEWTYEEQFKQLYEIDDDIKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYQLYRLVVEKGGLVEVINKKIWREITKGLNLPSSITSAAFTLRTQYMKYLYPFECEREKLSVPSELQAAIEGNRREGRRPSYSSHMFSYSPNTSANMLTPPKFPFAHHNGLAQLSQMAAAKYGQPDERCLPTSPTQQLIAQQQQLLQSANAQHVAAMAALETIQNQAKARQAAQQAAHHAAQQAAQHQMSLKKEIDSDYSEGEPPEKKLSFDDSVRRLTPDNQRRSSTSSLKISMGDRGRHNEMSDVTNADSINICVEVNGITYQGVLFAHSPNHPPVKHVTLDHPTS
The following text describes a protein:
Function:
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
Subcellular Localization:
Endosome membrane; Peripheral membrane protein; Cytoplasmic side.
Domain:
The FYVE domain is involved in the binding to phosphatidylinositol 3-phosphate (PtdIns(3)P) which is required for the association to endosomal membranes; Both IUM domains are necessary for efficient binding to ubiquitin.
Sequence:
MSWFGRATSDAPVATISQVELDNKIVEATSESIPNGEIDLSIAFEITDLIRSKKISNKIAMRSLKKRLTLIYLNPNLLLSSLKLIDLCIKNCGFGFLIEISSKEFMDYLIDFIFKIHYNTKELTYGHGGGDVGNKIKIGEMILKYLQNWKIIFENQQQLQYVEKKYQELKNQGFEFPDNNNNSGENDDFNDQVTQLNSKFVVDSEVPPDWVDNEECMICYSPFSMLNRKHHCRACGGVFCQTHSSNNIPLVNLGIMEPVRVCDNCFAKYDKSKKHSRNTSSSGDYNHQSRSIQNDYGGTHGSRRQGNNNDDDNDEEEQIRKAIELSLKESGAGGSGSGGPNSIPSQSRPSAQPPIDREPESETGNADDDEDAEMKAAIAASLKEYETEKSRQSQYQQIQPVQSTQSTQPESDLYNISFPTFSSTSNYPQPQFTASQPPPQQQQQQQAQQQAPSQDLSQAEEEQINLFITLMNSIKNDSRKQKDIMYDTNLNELYGKVIKLRPKLNKSLRNSIEKYETFLEMNNKISTITRLYDQFLEQKLNMAYGNHHISTQFTGVPQQQQEGQFTGSQQQQQQQQPHLPAQGTGYPRYGGSDTNVAQQQQQPPISPNEFYNNLPQHTGFQNYPSYPQNQGTAPDNSYLSQQPSGASTRQKQQQPPIQTYPNQLQPSEPDFEDDDNEEPVNTPQIRVAHNRTSSGSCPLYPTNDIIPDPYSANTNKSTTPNSDDHNYVAVSLPHYPPPEDLSNELPPQQHYVRRASSSLPPNAYEDASLKYPTLENVEHDYDKKKNQEQQQSVNESDFPDVSKVSQFNNRGEEDEGRRNSGASGASSNKKFVVEPEPLIEL
The following text describes a protein:
Function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Sequence:
MSKKGGKKGQKPQMEDDDEQMAFLMAAAAANKAKIEEKIKESQIPDEVFKDLPEPPMNTHKDKPFEERYTIKYPDEMLAKIQIDHAAEERLTELKETLPYFREGGIVHNSVSEWALNSGIIAPGVNLNDMCARIEEGVRRMVNFEPPVRGLAFPCGCSINNCAAHYSPLPGDTRVLQKDDVMKIDYGVAINGYIIDSAFTVCFDPRFDSLIEASKKATETAVKMAGPEARISEIADAIEEVITSYSLELNGKTIPLKPVYNLTGHQLGQYVIHCGKSIPICKNSGSTDKMLPGEVFACETFATTGNGIVFDDGVTSHFMTNKKPPKPKNGSAQKLLTLLQDNYKTMAFCQRFIERAGDRSYTLTLNELVKEKVVDPYPPLSDVVGSYVSQHEHTFCLLEDHKEVLSCPVNKMF
The following text describes a protein:
Function:
Transfers N-acetylgalactosamine onto globotriaosylceramide. Plays a critical role in preimplantation stage embryonic development.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MAPAVLTAIPNRMSLRSLKWSLLLLSLLSFLVIWYLSLPHYNVIERVNWMYFYEYEPIYRQDFQFTLREHSNCSQQNPFLVILVTSRPSDVKARQAIRVTWGEKKTWWGHEVLTFFLLGQEAEREDKVLALSLEDEHALYGDIIRQDFLDTYNNLTLKTIMAFRWVIEFCPNAKYVMKTDTDVFINTGNLVKYLLNLNHSEKFFTGYPLIENYSYRGFFHKNHISYQEYPFKVFPPYCSGLGYIMSGDLVPKIYEMMGHVKPIKFEDVYVGICLNLLKVDIHIPEDTNLFFLFRIHLDVCQLRRVIAAHGFSSKEIITFWQVMLRNTTCHY
The following text describes a protein:
Function:
Negatively regulates vacuolar (H+)-ATPase (V-ATPase) activity by interacting with members of V-ATPase V0 complex and hence inhibiting V1-V0 assembly. Required for multinucleation during osteoclast differentiation.
Subcellular Localization:
Lysosome membrane; Multi-pass membrane protein. Cytoplasm, cytoskeleton. Cell projection, filopodium. Note=In osteoclasts, localizes not only to the actin ring, but also to the filopodia, the stretched structures for searching cells to fuse, and the fusopod, the cytoplasmic bridge for contacting other osteoclasts to fuse.
Sequence:
MLSFSRVVNCSRTCSRFLGLSLGTASLCAAGANIALLFPNWDVTYLMRGLIGKHAMLGSGLWGGGLMVLLAATLISMTGSFSKSAPCLQVLIALLSSGLALLGAVICFVTSGVALKDGPFCMFDVSSFNQTQAWKFGYPFKDLHNRNYLYDRSLWTSVCLEPSKAVVWHVAFFSILLCISLLQLLLVAIHLVNSILGLFCSFCEKH
The following text describes a protein:
Function:
Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MANGSQHLLIFQKINGQSYLFSTLSPNLQSRNTSVHSLSNAYVNGGLQTSLLPANNGNGLTCPLYHPCLPSLLKLLRRKVQKVFMIDFLIGRVSIVVSKSVAAPIERVKLLIQNRDEIIKAAMLSELYKGITDCFARPIKNEDVFSL
The following text describes a protein:
Function:
Interacts with OSBPL11 to function as lipid transfer proteins. Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex.
Sequence:
MASIMEGPLSKWTNVMKGWQYRWFVLDYNAGLLSYYTSKDKMMRGSRRGCVRLRGAVIGIDDEDDSTFTITVDQKTFHFQARDADEREKWIHALEETILRHTLQLQGVDSGFVPTVQDFDKKLTEADAYLQILIDQLKLFDEKLQNCKDDDQRKKIENLKETTSSMVESIKHCIVLLQIAKSTINPVDAIYQPTLLESSVISTMPTQTVLSPEPAQLCKSEQRPSSLAVGPAVTLLGNHQTPTPNSTGSGQSVPSSSLTSPSHVNLSPNTVPDFSYSSSEDEFYDADEFYQSSSSPKRCLDPSGTGTILTRSSTGNSMKRPDTTESLNSSMSNGTNDADLFDPIDDRDDDNEGESVEEHKSVIMHLLSQVRLGMDLTKVVLPTFILERRSLLEMYADFFAHPDLFVSISDQKDPKDRMVQVVRWYLSAFHAGRKGSVAKKPYNPILGEIFRCHWVLPGMDQEDNTESVADGPLPWVAQDNVSFVAEQVSHHPPISAFYAECPSKKIQFNAHIWTKSKFLGMSIGVHNIGQGCVSCLDYDEHYILTFPNGYGRSILTVPWIELGGECSISCSKTGFNASITFHTKPFYGGKKHRITAEIFSPNEKKAFCSVEGEWNGVMYAKHATGENVVFIDTKKMPIIKKKVRKPEDQEEYESRCLWKDVTYNLKIRDIDAATDAKHRLEERQRAEARARKEKEIPWETRVHTVLIQPVDLLQISLVPTEAAKCIFFSYSCSMKMENAGFTMSHYSSDLLPVNTKWAIPWLSGTNYNFQVLFFWRACLLQLQFLISGILDFLMQRTIKAGRALTV