lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Sequence:
MEDDSPLPSSQEFLLQRLAFVGVPKECCSKRGLVEFVRASHQSMISELVSALLPTDEDVNAGLKEAMEKFRKPTMKKRLRESMNWLQWLMFRDEPGVSLKDLAKLNVDQRGVCGSVWGHNDIAYRCRTCENDPTCAICVPCFENGDHSSHDYSIIYTGGGCCDCGDETAWKREGFCSKHKGSEQIQPLSGDLADSVGPVLDALFACWNSKLLSAESIRDARSNDASSAVLQKMSNELTFVVVEMLLEFCKSSESLLSFVSRRIISSSGLLDILVKAERFLDQDAMKKLHDLFLKLIADPVFKSEFAKAFVSYYPLVISEAVKQGDDNAFRKYPLLSTFSVQIFTVPTLTPFLVKEMNLLAMLLGCLSEIFLSCSGEDGVVQATKWERVCKTSDRVIDDLKFVLSHAAVSKYATHEHRELSRSWLILLAFAQGMNPLKRETGIHIEEENEYMNLFFVLGHSIAVIHSLLVTGTYSAASDEEIENERITKVGLDTCDGDGERYAKVGRLSHEDSVCTAMESSSSSDSSMASAVHKIDPFCALLPSSATWLIRECLKVLETCLGDDEGVSKFLCKLCSPSGRNIPGSKISWPSRKLLKVEIGRSVSSGLAGSSRDPSTGLSPLCGDIHTDPSLDNVGGFNGEVQTDVTAYSRRVSCNSSDQAKKASEIHILGLCDWPDIHYDVSSQAISIHLPIHRLLSLLIQKALGMCYGESALQHGANVSHEIPHADFFSYVLGDCHPHGFSALVMEHVVRLRVFCAQVTAGMWKKNGDSALVSCEWYRSVRSVRWSEQGLELDLFLLQCCGALAPADSYVNKLLSRFGLSSYLSLNPDTTNEYEAVLVQEMLALLIQILQERRFCGLSTTESLRREIIFNLATKDFTHSQLVKSLPRDLSKSDELQEVLDDVSVFSNPSGMNQGKYSLRASCWKELDLYHPRWNSRELQSAEERFSRYCGVSALTTQLPRWKMIYQPLKGLARIGTCKATFQIICAALYYALQSGTSIKSRAPDGVLISALHLLSLSLDICTQQRESNRQACYVEDSIPILELAGLEIIGTNQGMGKQSLLSLLVSVMRKRKDDGLHQFSEAGSCNISSWIRDLLKKFSAIDSVCMNLLQSLAPEAVRQSEFDKVTSGSTSDEKRKAKARERQAAILAKMKAEQSKFLSTLSSSMDGDDPVSETEKSDFVMEHDSEISVREVCSLCHDPDSKDPVSFLIFLQKSKVLSFVDRGPPSWDQCPQFEKTIPVSGSTNVLQLSDDATSESRTDSVLEALTARLIGNGQKEKRSSDGRGKDELDMESLEMAMYQTVRRKVEMINQSHAHVDHQRHDDAESSSERSSVGALPILQVRLPDSGPKQTSRHPDVSFDGFHPTDCDGVYLSSCGHAVHQICLERYLKSLKERSERRNVFEGAHIVDLAQGEFLCPACRRLANSVLPACPGDLCSVSKLQESLFAKLGGSDAQMPSLWLSEALCLLQSAADAIEDGDIVKNVSLQGDERRRKDLESVSNKLWNFYFAKRQDKPPGTSWQPQSILMWDTLKYSLISVEIITRCAKNSMCPVYCIGSLYEELNTSKGTALSLLLRVVQSTRTKSALHVRQRFMGMRHLAESICSGFSSSSSSSIFGSEGTVGSMKHINLLWNRASDPVLAHDPFSSLMWALFCLPSPFITCEESLLSLVHLFHSVSLVQTVIAYCAGRLCDLSELDFEENLLRDISIALRESGGWGYFRSNHMDLSCDIKETIRKYSLPFLRRCALLWRLLKTSPGKFHQEVDMFDVPSDSTNDSMDFMYGPKSELNHVHELEKMFKIPPIDTILSDELLRSSTQKWLRHFQKEYSVNRVKGPLCITPVVPFQLMKLPNLYQDLIQRCVKKPCSNCTKVIEEPALCLLCGRLCSPIWNPCCRESSCQTHAVTCGAGTGVYLLIRRTTILLQRFARQSPWPSPYLDTFGEEDIEMIRGKPLYLNEERYAALTYMVGSYGLDHISKVLNQTTIGGAFFT
The following text describes a protein:
Function:
Polarity-determining protein which forms a conjugate with the ubiquitin-like modifier HUB1. Involved in bud site selection and cellular morphogenesis during conjugation. Required for survival during stationary phase.
Subcellular Localization:
Cytoplasm.
Sequence:
MNMNESISKDGQGEEEQNNFSFGGKPGSYDSNSDSAQRKKSFSTTKPTEYNLPKEQPESTSKNLETKAKNILLPWRKKHNKDSETPHEDTEADANRRANVTSDVNPVSADTKSSSGPNATITTHGYSYVKTTTPAATSEQSKVKTSPPTSHEHSNIKASPTAHRHSKGDAGHPSIATTHNHSTSKAATSPVTHTHGHSSATTSPVTHTHGHASVKTTSPTNTHEHSKANTGPSATATTHGHINVKTTHPVSHGHSGSSTGPKSTAAAQDHSSTKTNPSVTHGHTSVKDNSSATKGYSNTDSNSDRDVIPGSFRGMTGTDVNPVDPSVYTSTGPKSNVSSGMNAVDPSVYTDTSSKSADRRKYSGNTATGPPQDTIKEIAQNVKMDESEQTGLKNDQVSGSDAIQQQTMEPEPKAAVGTSGFVSQQPSYHDSNKNIQHPEKNKVDNKNISERAAEKFNIERDDILESADDYQQKNIKSKTDSNWGPIEYSSSAGKNKNLQDVVIPSSMKEKFDSGTSGSQNMPKAGTELGHMKYNDNGRDNLQYVAGSQAGSQNTNNNIDMSPRHEAEWSGLSNDATTRNNVVSPAMKDEDMNEDSTKPHQYGLDYLDDVEDYHENDIDDYSNAKKNDLYSKKAYQGKPSDYNYEQREKIPGTFEPDTLSKSVQKQDEDPLSPRQTTNRAGMETARDESLGNYEYSNTSGNKKLSDLSKNKSGPTPTRSNFIDQIEPRRAKTTQDIASDAKDFTNNPETGTTGNVDTTGRMGAKSKTFSSNPFDDSKNTDTHLENANVAAFDNSRSGDTTYSKSGDAETAAYDNIKNADPTYAKSQDITGMTHDQEPSSEQKASYGSGGNSQNQEYSSDDNIDVNKNAKVLEEDAPGYKREVDLKNKRRTDLGGADASNAYAAEVGNFPSLIDPHVPTYGFKDTNTSSSQKPSEGTYPETTSYSIHNETTSQGRKVSVGSMGSGKSKHHHNHHRHSRQNSSKGSDYDYNNSTHSAEHTPRHHQYGSDEGEQDYHDDEQGEEQAGKQSFMGRVRKSISGGTFGFRSEI
The following text describes a protein:
Function:
Has specific phosphohydrolase activity towards sphingoid base 1-phosphates. Has high phosphohydrolase activity against dihydrosphingosine-1-phosphate and sphingosine-1-phosphate (S1P) in vitro. Sphingosine-1-phosphate phosphatase activity is needed for efficient recycling of sphingosine into the sphingolipid synthesis pathway (By similarity). May play a role in attenuating intracellular sphingosine 1-phosphate (S1P) signaling. May play a role in pro-inflammatory signaling. Plays a role in the regulation of pancreatic islet beta-cell endoplasmic reticulum stress and proliferation (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAELLRSLQDSQLVARFQRRCGLFPAPDEGPRENGADPTERAARVPGVEHLPAANGKGGEAPANGLRRAAAPEAYVQKYVVKNYFYYYLFQFSAALGQEVFYITFLPFTHWNIDPYLSRRLIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLISTMDRYQYPFVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTYPAWTFIDCLDSASPLFPVCVIVVPFFLCYNYPVSDYYSPTRADTTTILAAGAGVTIGFWINHFFQLVSKPAESLPVIQNIPPLTTYMLVLGLTKFAVGIVLILLVRQLVQNLSLQVLYSWFKVVTRNKEARRRLEIEVPYKFVTYTSVGICATTFVPMLHRFLGLP
The following text describes a protein:
Function:
Probably involved in thiamine biosynthesis.
Sequence:
MKTIIRYFSFVMGLMLTLPSFAKEKISIMLDWYVNPDHAAIIVAQQKGFFEKNNLEVEIIEPADPALPPKLAAAEKVDLAVSYQPQLYQQVAEGLPLVRVGSLISNPLNSVVVLKKSNLKSLADLKGKKVGYSVSGFEDGLLDTMLHSIGLSNKDVELVNVNWSLSPSLLTGQVDAVIGAFRNFELNQLALEKQEGIAFFPEQYGVPAYDELILVANKNSVTDKKTSAFLTALEQATSYLQAHPNEAWQAFVSYKPNELNTPLNQLAWKDTLPFLANKPRQLDAKRYQQMAEFMQQKGLIPKALALKEYAVEIE
The following text describes a protein:
Function:
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MNNEPTNNDKNYLKNIFNCTDKKIILFKSYLKNKLDIDSFTLGEYCFKHDEKFQRSVLSNILKEQIISKKDKNKLHLINEIIIDTSFFKENYDFQYFLENVLLLEDLVLKKLDNKLNDEDFIFKENKKVSINNWKECYSHIKKKLNIKGMDEKSKIYNNSILLFNSTKFSYDDINCCDSFYGLKVWDILFNYVSFDFLNYLLSNTLIFISDYFFINTNNNFKTYVKSSYFIKIAEIQLNYQDAQNIERNIFSKKKNLYYKNTKLVKLTYQKKSIKDSTTPNLTIQKKKKKKKKKKFSKNINTNEHINININNYIYNTLNQNNEVNQYNVNHLNMDKNITYKEKESQNYTINNNLLNDQLLYYNKTYQNNVNTHIYSNDNKTPIIANQCIDIHNRVSDPTRKNIFYHSINSLSYEASLNIFHYNNLTQHTTYIDTPNKSQTCINSPMQHEIDEHSNNELKNQKCTQYEYVDNVCTTNKNISNDNISDKCITTKNIPLKYHINKKYKYLLKKKYHTMYTNNDHSYGKYLYLVQCSGRILKNDFFKDMKQIQEERKKYTSNIKINSEYTNNIIINNNNNNNNNNNNNNNNVHGFGHINNLFSSNEFPSSNISSCTNYTEKNDKLTHIRETSLLITENSSKKDKLLPEIDFFSEDRKEKSSSVGYDIKKKNDSNIKRFHNKINRTKEEKKKKWNKIIINRNNILQHNTTNKCKTFLFNKHIIFDKIENNNIPLFIYDLLNYIFKSDQTYFYHNNFIDEYKQKICKQIKCSTKKNDISHIITSRKENHLFHVQKLENNYKHPNINKQLRKTKILKYVYNYFKEFINNVINTKFGKIYRKFFPRKHILNKIHKIFKIIRLQIIKKYRIINIRMNRKFIKQKVYDTFFKNYDFLSFSFKTYKIINFMVYITKKCIPIKLLGSKHNFKIFLKNVKKFLLFNYKESFSLNQVMKNIKVKNIFQKKISKYNIKNRILLKNIFDNNYENKILHRNNKEIITNINDNIKIYNKKNDNLNNSFKIKTTLFNKLRRKYFNKIKKINIAIQKRHLMNRLIYFLFNYFIMPLIRRFFFLTKSEQTLHKTIFFDRKIWNHFTKISNFCLYHQIFRNKKLKKRNEPKMDYVQNMFNVKKKGEKIKTNKYIFIKKMKKKSTNKCINNKFSKKCIPKKKKKNLYNITRHNNIFIKKDMEKKSKTNNLINKSIDNLYKLKEINKKSVRPYIKKFYYKIKKKYFALKKMYIHMRMAKEEKSNIKLERAFKHFFIFAQEKEHILKYFSSHFFQNRKINYGKRFNKLIHRIKNIIIKQNSGIVKNKDKTFLHLIKNKSNKNNNNKKKNKNNYNNNNINNNNNNNNNNNINNNNNNKCKLSNSKRYNIRNNNNNKKAKNNEKNNIDDSNLEKKKKKIYIYKIKNIIEKRNFMLKLNSINHFISKKLRINWIPKKKGLRPLINLSTLNVPEIVKQRIFEILKSKKSSEFYFHNILNNLEREKKDKNIKKRKKYNKKNFNPVSLNNICNFSLKCLGNMRHNNNSLFKNTLTKTGEIELKLKKWLHYLKNWFYKKKRMKKYIKNKLKNNKKIYAYICIGDFSNCYEHINHNYLFKILKNFFDNINNFEFIYLFKRSFRLYNKNLNNSFLSYYPVNVKSFGLHYIRNLRELIIKSHLNDNHHFLLNQMFKTKSKSDLYIFADSYKSLQVDKRDIFMTIITVIRYYYLNIYFSIKEFKLNRKNIFYFQIFQENQMKGVYLSVRDKKRVENIKKWYLNSMKKINHDEILESLKNSSININNKNFMICTNHEQDTEEKGNTQNKEKHDIYIGPIYNNSFDSTTTTHSSNNYKGNNIHVSGDYKNDGLLHKGNNSMNECYVKDIKCNNNNNNNNNNNNNNINNSYNKLNCVTNNSKNDIIKYHKTIDTDNSKNHTYFKNKFLNFLDKKIISNIYGLPQGFSLSNILCSLYYAYLDKNEEFQNLLYSEKQINNKYFLANGTCNYFNLNSLILRFIDDFLFITLNKKNIKIFKNLLLKKKIWGSNINSSKTKIFKIPLIYKNDLLIYNFQNKYQQKKKYKIKNKKKIQSVRNKRIHNQLVNANKKKHTSVQKDKINKYINLIHPTIQKNDSVLSSNSIMNFERIYNKESHKSNSSIRTDIPNSVVNDDIEYNQKSDNNSYSTNNLYNNINMTQNGDNNNVNIFKHVQNDSFQCFNSNNLYIEKDIKENNISQINRKLCSKRNFTKKSRKINTLTYLQIDKVIKILKCKKKYIKHIKKMKYMNNFQNFKKLKKLQKFHNASFELKINKINKNIRRLNKLKKRKNHSINITPVTSIEWLNNSYTFDFINNSIQSTSYPWKNKCDATIRNHLHLHNVIIDKNNKTYFMKNLVENRIVRNIISKQKKCQSLYKNKQNVYFCYKNNFSLLKSSILKFICCIKTLKKMFNAFTNSTYNTKFILFLISYMNKMLIKNKKLKFVKLFLIQTAIEAFRYARIFNQQDSFYPCLQHFRKIKKRLINKYKIGHNKNLLREFFFLFNFIKKELYNSWPYMFKIKN
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC).
Subcellular Localization:
Nucleus, nuclear pore complex.
Sequence:
MEEVDEDPSVTLIPGVNSDKKQLCFAWGPGEMLMCETLFRSAENQDKSPGCPYVYIIRKDQDVYSQTLRKLFNESHGIFVGLQKDEKEKAGKSRTAQLVRVSKNYRSVIRACMEDSHQMAISTRDPAMHLHHSTQVSILSAMELIWNLCEIMFIEAAPAGPLLCHLLDWVRLHVCDVDNMVCEVLRNESPTKHENFWNVVTIFVLQGRMDEARQLLSKEANANPTSVNMCKILDELMKKMPVPSLNSIQTLTELELKWQHWHEECQRFLKDGTFASNPHMETLCKILLGDEKTILEKKDLMTTWYHFLVTRLLYCHPTVKHVELHVYAQSSLDLFLGGESSPEPLDSILLAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCNLLQSHNLYFGSNMREYLLLEYASGLFSHHSLWQLAVDYFDHCPEYGRAYLEHHIERIPLDTERKALKVLRICEQRMMSEQVRSICKIMAMKAVRNNRLGSALSWSIRAKDAAFATLISDRFLKEYCERGTFSDLDLIDNLGPSMLLSDRLTFLGKYREFHRMYGEKQFFAAAKLLLMLMTARIAPCSFWMTLLTDALPLLEQKEVIFSADQTYELMKCLEDVTATESKKQKFQDDDAEMMKVEMLRLAMARNLAKAIVKEGTVEES
The following text describes a protein:
Function:
Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP4 may act as a sperm receptor.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Zona pellucida.
Sequence:
MAMTMRLIHFCLLAVTLHNLADGQGDKVGQPPHYPQYPQQPQHPQQPQQPQYPSKPQQPQYPQNPQQPQYPSKPQQPHQPQNPQQPQYPSKPQNPQQPQYPQNPQQPQYPSKPQQPHQPQNPQQPQYPSKPQNPQQPQYPSKPQQPHQPQNPQQPQYPSKPQNPQQPQYPQQPQYPSKPQQPQNPQQPQYPSKPQQPQYPQNPKQPQYPSKHQNDQQPQYPQNPKQPQQPQNPQQPQYPSKSQNPQTPPSTFHSCEVDEYYKIPCGSSNITASECDAINCCYDGHTCYYGKYVTLQCTKDGQFIIVIAKDATLPHIDLESVSFLGSGAECHPAGASSAFAIYQFPVTSCGTIMRDEPGVLVYENRMSSFYEVAIGPRGAITRDSHFELSVQCRYIGTSVEALVTEVDLVPPPGPVAAPGILRVELRLGNGQCQVKGCYEEDVAYTSYYNDADYPVTKVLRDNVYVEVRMLERTDPNLVLTLGRCWATTSSFSNSVPQWDLLINGCPNIDDRYLTTLVPVDPSSGLPFPTHYRRFIFKMFTFVGNGPTSPSDPSKKAPSDAPNLPLKEHVYIHCDVSVCQPTLSNNCEPLCPLRKARDVSGSTRKAYREETVVVSSDEIVFTAASP
The following text describes a protein:
Function:
Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis. Also functions as a guanyl-nucleotide exchange factor/GEF for the MFN1 and MFN2 mitofusins thereby regulating mitochondrial fusion. By regulating both mitochondrial dynamics and bioenergetic function, it contributes to cell survival following oxidative stress.
Sequence:
MWPAPFAALRVNGVAFSRLPRLRPTRGKNMAKSKFEYVRAFEADDTCLPHCWVVIRLDGRNFHRFADQHNFAKPNDDRALHLMNKCAQVVMQELEDIVIAYGQSDEYSFVFKKMSNWFKRRASKFMTHVASQFASSYVFYWKDYFKDQPLLYPPGFDGRVVLYPSNQNLKDYLSWRQADCHINNLYNTVFWMLVQRSGLTPVQAQERLKGTLAADKNEILFSEFNINYNNESPMYRKGTVLIWQKVSEVTTKESKQPEDKEEQKVEVTRTRTKVVPLHCDIIGDAFWKEHQEILADDS
The following text describes a protein:
Function:
M-factor is a mating pheromone produced by M-type mating cells. All three mfm genes contribute to the production of M-factor.
Subcellular Localization:
Secreted.
Sequence:
MDSIATNTHSSSIVNAYNNNPTDVVKTQNIKNYTPKVPYMCVIA
The following text describes a protein:
Function:
May be part of a complex that binds ubiquitinated proteins and that is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome.
Sequence:
MIIAVRSPSGTTKINVSDTAIVKDLYVKLKENNVDIDGKSITKTPRDPPLEVGDKLSSLGIKSGDLLHLVGNNNNNNNDNKASSGSNNNNNNNNISKKEISYDEKLPNGLTPRCKHAVGDKCVFCSDAQGMKRCDHPENATCPNCQNKKFKGKRLKWLCNHPAGGKCSNCLRVGKNVSYKCNHGSTATCVNCMDKDDEDQDDNEEDNKDNKDNSEIKKSGFVPKVAIKNEVKTKCLHGPNQKCINCLPKDDPNSIEVPKRRCKNHGINGSCVECIEWRESLKMRLKSQDNPHAPGALVDFQSANIFQQYIANSKYEQQRIGFLFGNFLSDGSVVVDSIYEPPQECKDKQTPTLLPDPLADKIESMASMLGLTRVGWIFSHPSRKYTMSSTEIIQAASYQNKYGPSFVTLILSVNSDGQSNMEAFQVSDQALKLEKTGEFLPTQPDPTKCKLKSPVFEEGTETINADTHFFIVTVPLKAREDKSIFNISFPVENRIPVNTLSDLASYKLEHKDVSPLKFFSDFHFLIFLLENQFLDFQSDFPIICENIRSRSSENLIGYLEIINYQIGDIIGHDQFN
The following text describes a protein:
Function:
Fallaxidin-1.1 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction; Fallaxidin-1.2 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction; Fallaxidin-1.3 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction.
Subcellular Localization:
Secreted.
Sequence:
MASLKKSFFLVLFLGLVSLSMCEEKKRENEDDAEDGNHEEESEEKRGLVDFAKHVIGIASKLGKRSEEKRYHPFGKRSEEKRYFPIPFGKRSEEKRYFPIPIGKRSEEKRYFPIPIGKRSEEKRYFPIPIGK
The following text describes a protein:
Function:
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Subcellular Localization:
Cytoplasm.
Sequence:
MYCLKSIFKIGLTGGIGAGKSTISEMIKEKNIPVIDADKISREVLKLYPEILIRVKEVFGKEFLDDNGDLKRREFGSYIFKNKNKRMEYENIIMPYITKETFKRIKLLEENKESICVLDAPTLIEQGLYKYMDINILVWVDKDTQINRVVKRDGLNRSEVMNRINSQMSMEEKKKFVEYIIDNSKDIENTKSELDKIFMEVMIKARQKGGVL
The following text describes a protein:
Function:
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.
Subcellular Localization:
Nucleus.
Sequence:
MGTENQFDSNENGVNIDETAVTIHTFLEKTGLDEKPILENESDHEKIDSSLQQLKRYKEQLLKRLWLLTKFQDLNALFSGEDTFSEAQLKDWTSFVANNVKGKFQPETLNEIEQEPALSTPQLDALVKRQEEDIASTEQIPEAVEQKVSETHEASAESKETTAPELMAVSEVVPETIPTESADESVTAPQPQIVEPKLPEVKEISEQTSIVIEGKASEEMRDTSVSSNLESPKTAHLSPSPVLPVEPEPEALPKEASLIIDDTAHSPTVTETEISQKPAAKEEVVAITETVEKASAEPQPETVASTSVPISPKHVTSESEQESVKKEASPQGDFFPPLTLKTEESTEGTVYTAPAVVKIDAVHSPPSTQPLDIPQEQPTEISAAVEVEKEKVTETVQATVEPEPEPESSMPVEPVTEEQLSVPETQVEETLRQLPPSELDLRVTLPSTLIAPEPVINRTRDGSVESWLLRTEMQPLQPLVELAHKCVRTEQWMHVNKENILRHVLLRVKALKDKQQWSFCQPIRAKSLPRKKSHHDFLLEEMQWLSMDFSQERQWKMVMAKRLAYWVLDYHNAEDKKSLCVKRNSPASASLSEPSTSKSLDTSSEAITAEPDIAGDAVRLFEAASSDEPLVTISNPQIMFALNSVPLYAPPDPSNDSYINTVDQFPFVPLSRFSLAKTKLKSECNLLPRKRSQHLPELHSKQFRGEVIESEEFNEHRRKRIHFILTIRPPCPPFKRDSSEASWSPEEDELLLSLLNRYSYNWDFVSRLLTPSGLYITAKERRTAWSCFERWVQIDPQAANAQLVGTYARLAQQRLDELTSSNTNSERHINNAIKDYLSANTKASSLLLPSVSRNYQQSLIFDAMRKVIKKRELAKKAALSRKVISRPKANTENPPPVPSPLELSRLKSEREAQLQQVQAQRNAALLMQYHAQGRTPHRGMSSPTVPLSRQQMQQFSSLQSSGGVPRQKNIMSDVP
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular Localization:
Nucleus.
Sequence:
MSATPKAGAPSVMNKFLGLLRNYRESAEGGSGYEQLPDVINALLTEGKIKIFKKGSVLSYGIVDAEEAERIRGLTLEQRLVLQEIERADNKGIWTRDIKSHTNIPQQIVTKTLRMLETRRLVKSVKSISSKNKKLYMLFDLVPSTEITGGPWYNEQEFDHVFIDTLSTFVYEVIKASGMSTLNAITDKVHASGISKVALGPEEIRSIIQTLMYDGRVEEVRSVRLTPGASHEVKYKVSQQITTFNYLSETPCGVCPVFDQCQEGNVISPRSCLYMTKWLGLKELDF
The following text describes a protein:
Function:
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. Gliotoxin contributes to pathogenesis during invasive aspergillosis. In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MDQVYLPQSVRTAVAVSFGVGLLYWVYRLLLQKTKSLKALDLPVLQSVGDQDIVKTLEEGHAKYPDTPFALGVPGQQLVVLPVSEIDTVKALPENQLSIKKHHYNQFLGEYSYMGTKADEFDDAMRYLLVRNTPAVLASFTAEIDYAMSTVLQVPPNSWTRVKPRSIMPKVATILSGRAFVGLPLSREPDWIESNVNYTQDVSRAWMVLRFYPHWIRPLVAPFLREVKTLEQNKALIGRKIAKLLADQEAQKLSPAQEKIPGGDMIDWFKSRYQAQGKTATAQQLTRDQLLATFASIYNLSNALTYVMFDLAANPAAVDELREELDQVLGPNVGAESIDKTALPRLIKLDSFVRESQRLSPTSLVNIPRIVTDPNGLRLKTGHVIPPGYLVMVRAQPINQSPTLYPNPERFDAFRFARLRQQGGANENRWQHTSTGADNINFGHGIWACPGRFFASAEIKVVVAYVIRHYDLRLIEGRPHPKPKYGGLAIFPDAGAEVELKPRV
The following text describes a protein:
Function:
Plasma membrane t-SNARE that mediates docking of transport vesicles. Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane. In neurons, recruited at neurite tips to membrane domains rich in the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) which promotes neurite tip surface expression of the dopamine transporter SLC6A3/DAT by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane. Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones. Required for normal hearing.
Subcellular Localization:
Cell membrane; Single-pass type IV membrane protein. Cell projection, neuron projection. Cell projection, stereocilium.
Sequence:
MRDRTHELRQGDDSSDDEGKERVALVVHPGTAKLGNPDEEFFQKVRGIRQTMTRLENKVKELEKQQITILATPLPEESMKQDLQNLREEIKQLGKEIRTQLKTIDPQKEEADENCNSVNIRMRKTQHGILSQQFVDLINKCNTMQSEYREKNVERIQRQLKITNAGMVSDEELEQMLESGQSEVFVSNILKDTQMTRQALNEISTRHGEIQQLERSIKELHEIFTFLATEVEMQGEMIDRIEKNILSSADFVERGQEHVKSALESQKKARKKKVAIAICVTIAVLVLALIIGLSVGT
The following text describes a protein:
Function:
Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins.
Subcellular Localization:
Cytoplasm, P-body.
Domain:
Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs; The N-terminal zinc finger binds to poly(A) RNA; The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2.
Sequence:
MQHDSGYDQLNPGSRLHKYLGAASPSRPVPATTSMSPMSVNVPAFIPNFARLQLENGGGNGGAVGPPQQTSSQFQANAEEFVPQDHGGTVYFYRGGGQSAYESSGGGGSTGGLGSPIEQSDSSVLVELMNRQLAMKAKPEAALYPELPQAIEHMRDIVPLEAGSIKPSTGYQQSVYKATSARDGVHYVLRRVHAFRPINAKAFAPAESWKKLQAAHVVQLRECFATRAFGDNSLIFVYDYHPLSESLKERHFGRNGGVTMVDTMTGAKIMSSYSGSAGGAGLTGSGVPELLLWQYVVQLTAALRSIHATGLAARSIDISKVILMGKCKLLLSSCGVQDLVAPDHQQIQQQQSDDMVALGRLVLALATGNQNAGRREIVQQGLSIVGAHYSQDMKNLVTCLIGPSPRKTIADVMPMIGARFYHHIEALQSRVDLLENETARELENGRLFRLLCKMNTIVERPEHNMDSSWSETGDRFLIKLFRDYVFHQVTDQGKPWMDMAHIVSCMNKLDAGVAEKIELVSRDQDSVIIVSFGDLRRCIDAAFAELSATTVTARGTPNNQRHH
The following text describes a protein:
Function:
Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol; Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Required for auditory function. Component of the cochlear hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein; Extracellular side. Endoplasmic reticulum.
Sequence:
MSPAIALAFLPLVVTLLVRYRHYFRLLVRTVLLRSLRDCLSGLRMEERAFSYVLTHALPGDPGHILTTLDHWSSHCEYLSHMGPAKGQILMRLVEEKAPASALELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDEHTVELIVGRSEEVIPRLRTQYQLSRADLVLLAHRPRCYLRDLQLLEGHALLPAGATVLADHVLFPGAPRFLQYAKSCGRYRCRLHHTGLPDFPAIKDGIAQLTYAGPG
The following text describes a protein:
Function:
Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. Not required for SLC2A4 membrane fusion upon an initial stimulus, but rather is necessary for proper protein recycling during prolonged insulin stimulation.
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Endomembrane system; Single-pass membrane protein. Cytoplasm, perinuclear region. Note=Shifts from low-density microsome vesicles to the cell membrane upon insulin stimulation.
Sequence:
MANPAQPPLQDPGSTSPLELPEMEKLLTKVENKDDQALNLSKSLSGALDLEQNGHSLPFKVISEGHRQPSLSGSPSRVSSRRASSVITTSYAQDQEAPKDYLVLAIASCFCPVWPLNLIPLIFSIMSRSSVQQGDLDGARRLGRLARLLSITFIILGIVIIIVAVTVNFTVPK
The following text describes a protein:
Function:
Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs. Binds the APUM-binding elements (APBEs) in the 3'-UTR mRNA sequence of CLV1, PNH, WUS and FAS2.
Subcellular Localization:
Cytoplasm.
Sequence:
METPIRFAENIGGGTWPPNDESRSQHLHGVERDKIPCRSVSAPPSMERSLSVLANFRGSHESSLHDRMLSTNNNEVHVLEEQLRSDPSYVTYYSSNINLNPRLPPLINHDNYYLMHKINHSWENEKLASFDEIERESCFMFTQASFPTHKERAEEDRSTLADSNFRFLPTEYSSSLEDQCKTIVDPISIQEKFPWIPSPLFNDQARLSSHVSGELVDSLDQGNTLANSSIITNKLPELGVLAINSIPNILTVKSIQNPDLSENSVLNMSPSETRNFLSLDVKQKEGLNMERKSSVTDVSGLNYHGNQHYPEQNIQQGSLYSWTQESATRFHDSQTNTLPQSYGTHFPSAVYRMPLYDGSSGYMESENPNFQQSSLFTSQHSMRDYAINASNITALFYGHHPPGTIPIAVENQINLNNNISGINVELGTYLHQLHKLSGQHGMSLQLAPTEYLCYPYYQLPFFDMFGASIQYYEPRINPSVEVCEFSPHLRSGINISSLVEGRFSSPNYYIFEVSDIVGHIAEYCTDQYGSRCIQLKVENCNENEKAQIFNEIIPCAFMLMTDVFGNYVIQKFFEHGNAEQRKVLANKLVGYILPLSLQLCGCRVIQKALEVIELDQKIQLVQELDTHVMQCVEDYNGNHVIQKCIECVPNENIQFILYSLKGRVGHLSLHQYGCRVIQRLLEHWTSKLQSQFIVHEILQSVCILAQDQYGNYVLQYVVERGEPEERHHIISELALQIVEMSQNKYASKVIEKCLVHADSLEKELLIEELIGHTEENEKLLIMMTDKYANYVIQKILETCSNKQRAILLGQVKVHLPALKNYSYGKYIVPQIERLYSEDIQ