lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Inhibits bovine trypsin and human plasma kallikrein.
Subcellular Localization:
Secreted.
Sequence:
SDAEKVYDIEGYPVFLGSEYYIVSAIIGAGGGGVRPGRTRGSMCPMSIIQEQSDLQMGLPVRFSSPEESQGKIYTDTELEIEFVEKPDCAESSKWVIVKDSGEARVAIGGSEDHPQGELVRGFFKIEKLGSLAYKLVFCPKSSSGSCSDIGINYEGRRSLVLKSSDDSPFRVVFVKPRSGSETES
The following text describes a protein:
Function:
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and 5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2.
Subcellular Localization:
Nucleus, nucleolus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MSFQSINIDKWLKNAVAAQGFKKMTPVQANAIPLFLKNKDLVVEAVTGSGKTLAYLLPCFDKVTRRDTDETGLGALIVAPTRELATQIFNVTKELLAYQPDSLDGGKKLVADMYIGGKGTLTNDLASFREKNPSVVIGTPGRLNEMLSHISSKHLEILILDEADTLIDMGFQRTLQSIISQLPKQRRTGLFSATMNDTVSSFLKIAGLRNSVRVSVTVTSKKIDTRTPSSLAIQSLVIPPIYKVQCMIHLLCTIEYEKAIVFFSSCASVEYFNSLFLTYKLPFEIVALHGQQVQSNRSRNFEKFKKSNKKTVLFTTDIASRGLDIPNVDFVLQLDPPLDPKSFSHRCGRAGRAGRAGVAIVLLNDGREEEYEELLRVRKVPITRIDTPIEALDLSRLKVLTHELRKIVSKDRDLYDKGLRAFVSHVRAYTKHHASFIFRIKDLDLGQLATAYALLHLPKMPELKDTEISENIFKKFDIDYATIPYRDQVREQARRRRLEVEKTEPKKLARPAKIKNEAWSKQKEVKEKRNTRREKRKSKKEFLKAQKNEASNNLKQEIVSKAGAQETENDDLIDEESDALSELEEDYRQLKKSKKRKNQASFGFSM
The following text describes a protein:
Function:
Probable transcription factor involved in oxidative stress response.
Miscellaneous:
MISCELLANEOUS: Plants overexpressing ZAT7 show retarded growth and development, and enhanced tolerance to oxidative stress.
Subcellular Localization:
Nucleus.
Sequence:
MVARSEEIVIVEEDTTAKCLMLLSRVGECGGGCGGDERVFRCKTCLKEFSSFQALGGHRASHKKLINSDNPSLLGSLSNKKTKTSHPCPICGVKFPMGQALGGHMRRHRNEKVSGSLVTRSFLPETTTVTALKKFSSGKRVACLDLDLDSMESLVNWKLELGRTISWS
The following text describes a protein:
Function:
Essential to the formation of horizontal top connectors between outer hair cell stereocilia.
Subcellular Localization:
Cell surface. Cell projection, kinocilium. Cell projection, stereocilium.
Sequence:
MALSLWPLLLLLLLLLLLSFAVTLAPTGPHSLDPGLSFLKSLLSTLDQAPQGSLSRSRFFTFLANISSSFEPGRMGEGPVGEPPPLQPPALRLHDFLVTLRGSPDWEPMLGLLGDMLALLGQEQTPRDFLVHQAGVLGGLVEVLLGALVPGGPPTPTRPPCTRDGPSDCVLAADWLPSLLLLLEGTRWQALVQVQPSVDPTNATGLDGREAAPHFLQGLLGLLTPTGELGSKEALWGGLLRTVGAPLYAAFQEGLLRVTHSLQDEVFSILGQPEPDTNGQCQGGNLQQLLLWGVRHNLSWDVQALGFLSGSPPPPPALLHCLSTGVPLPRASQPSAHISPRQRRAITVEALCENHLGPAPPYSISNFSIHLLCQHTKPATPQPHPSTTAICQTAVWYAVSWAPGAQGWLQACHDQFPDEFLDAICSNLSFSALSGSNRRLVKRLCAGLLPPPTSCPEGLPPVPLTPDIFWGCFLENETLWAERLCGEASLQAVPPSNQAWVQHVCQGPTPDVTASPPCHIGPCGERCPDGGSFLVMVCANDTMYEVLVPFWPWLAGQCRISRGGNDTCFLEGLLGPLLPSLPPLGPSPLCLTPGPFLLGMLSQLPRCQSSVPALAHPTRLHYLLRLLTFLLGPGAGGAEAQGMLGRALLLSSLPDNCSFWDAFRPEGRRSVLRTIGEYLEQDEEQPTPSGFEPTVNPSSGISKMELLACFSPVLWDLLQREKSVWALQILVQAYLHMPPENLQQLVLSAEREAAQGFLTLMLQGKLQGKLQVPPSEEQALGRLTALLLQRYPRLTSQLFIDLSPLIPFLAVSDLMRFPPSLLANDSVLAAIRDYSPGMRPEQKEALAKRLLAPELFGEVPAWPQELLWAVLPLLPHLPLENFLQLSPHQIQALEDSWPAAGLGPGHARHVLRSLVNQSVQDGEEQVRRLGPLACFLSPEELQSLVPLSDPTGPVERGLLECAANGTLSPEGRVAYELLGVLRSSGGAVLSPRELRVWAPLFSQLGLRFLQELSEPQLRAMLPVLQGTSVTPAQAVLLLGRLLPRHDLSLEELCSLHLLLPGLSPQTLQAIPRRVLVGACSCLAPELSRLSACQTAALLQTFRVKDGVKNMGTTGAGPAVCIPGQPIPTTWPDCLLPLLPLKLLQLDSLALLANRRRYWELPWSEQQAQFLWKKMQVPTNLTLRNLQALGTLAGGMSCEFLQQINSMVDFLEVVHMIYQLPTRVRGSLRACIWAELQRRMAMPEPEWTTVGPELNGLDSKLLLDLPIQLMDRLSNESIMLVVELVQRAPEQLLALTPLHQAALAERALQNLAPKETPVSGEVLETLGPLVGFLGTESTRQIPLQILLSHLSQLQGFCLGETFATELGWLLLQESVLGKPELWSQDEVEQAGRLVFTLSTEAISLIPREALGPETLERLLEKQQSWEQSRVGQLCREPQLAAKKAALVAGVVRPAAEDLPEPVPNCADVRGTFPAAWSATQIAEMELSDFEDCLTLFAGDPGLGPEELRAAMGKAKQLWGPPRGFRPEQILQLGRLLIGLGDRELQELILVDWGVLSTLGQIDGWSTTQLRIVVSSFLRQSGRHVSHLDFVHLTALGYTLCGLRPEELQHISSWEFSQAALFLGTLHLQCSEEQLEVLAHLLVLPGGFGPISNWGPEIFTEIGTIAAGIPDLALSALLRGQIQGVTPLAISVIPPPKFAVVFSPIQLSSLTSAQAVAVTPEQMAFLSPEQRRAVAWAQHEGKESPEQQGRSTAWGLQDWSRPSWSLVLTISFLGHLL
The following text describes a protein:
Function:
Involved in endocytosis.
Sequence:
MAARKPGRLELDVEKCRAEGNWTKAMELVRQLERGKHSGLESLVQLVLGETKLELHLQEVPPKEENIAKASRALTEARRHFNDALKGEHKQKWAEEILLLQGKLNYATGNYEEALGCFCKGRLEELSTNIQSNRILRLIAEAYALKAMCLEKVPLKTFSKMKQAEREEEIISLYEHSGDMALLYLQECEKGQKATPTVGGVTINNTDLGHVLETAIYRTPVLHLKNGDLSTGIGRYREMLRAVEARCTQNLRQTLARQLSEVLLRAVCEKTYSPPVSPPSSTTVQKRASVADVKVPGSSTASPSLRPKLYPSEGVFTPTQDTEESLLLLLLSEAIANREVVLSRAPEHKESRVQTVSNASAVYDLLTILLIRRSQPGLLAEILERTMKFGFDEFHLWYQFGLSLLAAGKYARAVRVLKECHTIQPDNPTVCLFVAKLCIEHLHQLEDAVIYSKKVIERDSRNSLDKQRGSKNSVDLQRDSENTLHSSRAFLMLGVAYSMQATEAKLMSARHELQKKALDAFNRSHTLDPDDHLALFHLGLQLAVQRQIVEALQRVQQALQLRPDHLPSLHLLALLLSAGKQHTEAQQLVDAALSEYPENSSLLFTKVKLTVAGGDAEEALVTCKHLLQLWKDTFEPTLKEEERRRGSGLIDKVMADKRSLAQIHITEFSDGDSGLHLTDTGSVYADSMAASKVEKALSEVASSLNSYTPKPGPQQAWAMQVHIWLNIADVYLSMGKVEDARACVQEAHAIFPYSHLVIFKRGCIHEMKHEYPEAKKCFSDATAINPSHVPSLQHLGMANYHLGNLVQGEKALRDAVNIDNTAHEAWANLGKVLEAQGDHLAATDCYFTALELEASSPVVQFSIIPKQLH
The following text describes a protein:
Function:
Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg12 converts mevalonate into 5-phosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8. The diphosphomevalonate decarboxylase mvd1 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSKSLIVSSPGKTILFGEHAVVYGATALAAAVSLRSYCKLQTTNNNEIVIVMSDIGTERRWNLQSLPWQHVTVENVQHPASSPNLDLLQGLGELLKNEENGLIHSAMLCTLYLFTSLSSPSQGCTLTISSQVPLGAGLGSSATISVVVATSLLLAFGNIEPPSSNSLQNNKALALIEAWSFLGECCIHGTPSGIDNAVATNGGLIAFRKATAHQSAMKEFLKPKDTLSVMITDTKQPKSTKKLVQGVFELKERLPTVIDSIIDAIDGISKSAVLALTSESDKNSSAKKLGEFIVLNQKLLECLGVSHYSIDRVLQATKSIGWTKLTGAGGGGCTITLLTPECKEEEFKLCKESLLAHKNSIYDVQLGGPGVSVVTDSDSFFPQYESDFDFKKLNLLSKFNKYYI
The following text describes a protein:
Function:
Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the second glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(1)Man(9)GlcNAc(2)-PP-Dol to produce Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGEVQLVLAVTAILISFKCLLIPAYVSTDFEVHRNWMAVTWQRPLCEWYTEATSEWTLDYPPFFAYFELGLASVAHFFGFDECLVISKTPRFSRRILIFQRFSVIFCDILYIAVCALYSFRSPRLVSRIPKKLQQNGREACFVLLASLQALIICDSIHFQYNSMLTAIFLMSLFFIDTERYLMAALSYSILLNFKHIYVYYALGYVFYYLVNYFQFSGNVLLANTPKAISLAIALLIPFCASIFPFIHASGVQGLQNIATRLFPVSRGLTHAYWAPNFWALYNFADLCLYRVLSLLKIGKFDAPTYTSGLVQEYSHSVLPNVSPMGTLCLVVISSMIVLTGLVIRRKDSADFSLFAVFSAFCFFYFGYHVHEKAIILVTVPMTVFAIKNPKYHSILIHLTCIASFSLFPLLFTPFETLLKYAICVSYFFIQLVFLKRVTLMPLSDLIPTRHVASWLLMGMVEVYNTFLHKWLWTSRLPFAPLMAISILTAIELTGLIGALIWSTFGDGIFEIWWAKATCQIRERLIRDSTYSVQAVEDLDDVKLVAGIDTSAAKLNSDMVYISVSFWTYPDLKHVATISDTRMLELPYIPQYLAVREAEVMADFLKSVITERPELRPDVILCDGFGEFHSRGCGMACHVGALSGIASIGVAKNLTLHHTYETIGMENKSKVDSFVEHCREVYKNNKTSPGFIPFDIVEPVVLNILRMGSSMNGVFVSAGYGIDLELSTEICSQLLLNNTTIEPIRAADLESRRLVRENFDGNEKLE
The following text describes a protein:
Function:
Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Involved in phosphate regulation and polyphosphate accumulation. Required for resistance to salt stress, cell wall integrity, vacuole morphogenesis, and telomere maintenance.
Miscellaneous:
MISCELLANEOUS: Present with 1940 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MDTSHEIHDKIPDTLREQQQHLRQKESEGCITTLKDLNVPETKKLSSVLHGRKASTYLRIFRDDECLADNNNGVDSNNGGSVTCADKITRSEATPKSVPEGLQVSEKKNNPDTLSSSLSSFILSNHEEPAIKPNKHVAHRNNITETGQGSGEDIAKQQSHQPQVLHHQTSLKPIQNVDEGCISPKSTYQESLHGISEDLTLKPVSSATYYPHKSKADSGYEEKDKMENDIDTIQPATINCASGIATLPSSYNRHTFKVKTYSTLSQSLRQENVNNRSNEKKPQQFVPHSESIKEKPNTFEQDKEGEQADEEEDEGDNEHREYPLAVELKPFTNRVGGHTAIFRFSKRAVCKALVNRENRWYENIELCHKELLQFMPRYIGVLNVRQHFQSKDDFLSDLDQENNGKNDTSNENKDIEVNHNNNDDIALNTEPTGTPLTHIHSFPLEHSSRQVLEKEHPEIESVHPHVKRSLSSSNQPSLLPEVVLNDNRHIIPESLWYKYSDSPNSAPNDSYFSSSSSHNSCSFGERGNTNKLKRRDSGSTMINTELKNLVIREVFAPKCFRRKRNSNTTTMGNHNARLGSSPSFLTQKSRASSHDASNTSMKTLGDSSSQASLQMDDSKVNPNLQDPFLKKSLHEKISNALDGSHSVMDLKQFHKNEQIKHKNSFCNSLSPILTATNSRDDGEFATSPNYISNAQDGVFDMDEDTGNETINMDNHGCHLDSGKNMIIKSLAYNVSNDYSHHDIESITFEETSHTIVSKFILLEDLTRNMNKPCALDLKMGTRQYGVDAKRAKQLSQRAKCLKTTSRRLGVRICGLKVWNKDYYITRDKYFGRRVKVGWQFARVLARFLYDGKTIESLIRQIPRLIKQLDTLYSEIFNLKGYRLYGASLLLMYDGDANKSNSKRKKAANVKVNLIDFARCVTKEDAMECMDKFRIPPKSPNIEDKGFLRGVKSLRFYLLLIWNYLTSDMPLIFDEVEMNDMISEEADSNSFTSATGSKINFNSKWDWLDEFDKEDEEMYNDPNSKLRQKWRKYELIFDAEPRYNDDAQVSD
The following text describes a protein:
Function:
Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity.
Subcellular Localization:
Nucleus.
Sequence:
MDCYLRRLKQELSQGYPGSQQQTWIQKVPAHGSPDSMTASPTPPRKLYTLLLGRGLGSCVWGGFREGELEVQMSMKEVGDGLQDQMNCMMGALQELKLLQVQTALERLEISGGDPALGCPESPRTQPEPPRWEGGGGPARPMACSPSTQPSLGSSTKFPSHRNVCGRDWAPLPRTQLPEHHSRAQQGPELVEPDDWTSTLMSRGRNRQPLVLGDNVFADLVGNWLDLPELEKGGEKGETGEAGGQKRERGQPRELGRRFALTANIFRKFLRSVRPDRDRLLKEKPGWVTPTASEPRAGRSQKVKKRSHSKGSGHGPFPGTAEPRRGENPSTSCPKALEPSPSGFDINTAVWV
The following text describes a protein:
Function:
Substrate-recognition component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex, also named CRL5 complex), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DAB1 and IRS1. Specifically recognizes and binds phosphorylated proteins via its SH2 domain, promoting their ubiquitination. The ECS(SOCS7) complex acts as a key regulator of reelin signaling by mediating ubiquitination and degradation of phosphorylated DAB1 in the cortical plate of the developing cerebral cortex, thereby regulating neuron positioning during cortex development. Functions in insulin signaling and glucose homeostasis through IRS1 ubiquitination and subsequent proteasomal degradation. Also inhibits prolactin, growth hormone and leptin signaling by preventing STAT3 and STAT5 activation, sequestering them in the cytoplasm and reducing their binding to DNA.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Nucleus.
Sequence:
MKSGSHREKRNSGADVQMRMPSAKLPASNSRDVREISGRKEATGLMGRMRRTLKRGGSKSPKEDPVGQGLPGGYQKNLVNGVVVNPSVGQGFNGDLQPSRLDNDPERTSLNGRTSHCIYHNGCDIRNGNGLERRDADMDHCVVKHGRGNEHLSGRVSQNGGSSPMQNMDSTINQSSYNGVSVFDKQGARPKTGLYRKKSSAVGKNFELGSVVLNVQANRCGEEGKGNNVDVKLSVGGLMGDESESESTVPLQRKASVRNDISVNIVPSGGLQSNSDVTVNCSVNVHCHFTEMEEDCEEVEQNEGESDADSRTKQQNKILSSAELEPLVIQMGHQPDMEPLNNPRTPHIAEVMMKDSLASLDSESSDRHHRSSSDSLHRESKTQRKGNSEQNGNGDTDRVVKEKLKKEKFEHVVPLPKDSQIVDVFTTQKGSACDESDIRFQYNLPRSVSEGAAILASYRNDESFKENSMYGPAIDRRTKPKSGFGDYAQPEGSPGDDDESPPPIPPRMSMVLDQDPKKAEWETEPTHMCLPALMNGLYSDNTGTSASMRSKSLPRHSSLNDVSIDPSIPRRSKTAHLKNRVSQLFKTPRRKSCAFPDRPLPDVPGSKSGVQSRENRRSQVQRPQSLYCPTDGRNQIVPPPPARPSPQRPSAGPRPPRPGQENMVVIERREGIPTKDEVAKCQGMFASSLRRISECGWYWGPMSWDDAEMRLENTPDGSFLVRDSSDDRHILSLTFRVQGSTHHTRIEHHNGKFSFWSQPTTHGSSSIVEFIEEAMRHSRNGRFLYFLRPRWPGLPPVPLQLLYPISRFQKARSLQHMCRFVIRRNVRLDHIDALPLPRRLKDYLREGQYYTPDDIKP
The following text describes a protein:
Function:
Together with the zinc finger protein ztf-16, plays a role in gonadogenesis, specifically in somatic gonad precursor cell development. This is possibly by regulating tra-1 gene expression; [Isoform a]: Required for proper gonadal primordium assembly and somatic gonad precursor cell morphology.
Subcellular Localization:
Nucleus.
Sequence:
MEKCDICHQKFSNKTNLNRHKVMHSGKKKFECQFCRRPFFRNDRMKEHMMTHIKKGNTFECPITACNSKFNSFTSLQFHVDSEHIIRGSSPAKCKSCIKWFNSSHRLLLHFHTAHLDHTKFFSFKPAPILPKSTTSILNPIKNPDDFDRIFDFFKTEIAPLFPLHSTVSQAPLPQCSRSVKSAKELSPTPSTEIETPEEEELDGPESWYCDYCKIRFDDKVMWYLHSGLHSDDIPFKCSLCGSLCDGKYDFAAHLVYANHNF
The following text describes a protein:
Function:
Selectively catalyzes the addition of fucose in alpha 1-2 linkage to Gal-beta-(1->3)-GalNAc-alpha-R, Gal-beta-(1->3)-(GlcNAc-beta-(1->6))-GalNAc-alpha-R and Gal-beta-(1->3)-GalNAc acceptors but not Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc in vitro.
Subcellular Localization:
Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Sequence:
MRYNSNYLMYFCLVLGIFANIYVIIKITLGSSHILEYFQKNSNLSPKCEINVNNLLSFIENRHFLDLEQKNSQKSQPNYEKTLQLMLFAFPSGGLGNKLFEIISLHGIATSLQRKAVINATNPSFIETLNRNIQPLFPKLADQFTLRIIPDSLVTHQQTNWGRCCVYDDPSRFLNRSDQNLILDGHYFQSFKYFHHIRPQVREWLAPSKLQAMRAEILLPAKFRDDFLICTHVRRGDFQYDGLHRPSDATFTRAATDFLVDLYRKSHERVNVVVLGNDIHFAYTVFEDRVAHFTFLQKPVNNSYDYSLPQISPSYTAILTPTLTPEIDLAFSRLFCDVTLITAPSSTFGWWLSYLAKRTATTYYRDILESKDGVAGEMHPEDFYPPEWIKLKTDLNGKISKY
The following text describes a protein:
Function:
Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover.
Miscellaneous:
MISCELLANEOUS: Present with 3310 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQDENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSVMRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSYYQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIV
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. Involved in gene silencing by neighboring heterochromatin, blockage of the silencing spreading along the chromosome, and required for cell cycle progression through G2/M (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MAAAPPPPAKNQGKAKQHVTGARFRQRKISVKQPLTIYKQRDLPTLDSNELEPSQVHHLNSNASSSSTQQPRDLHAVETGVDKNEEEEVHLQQVINAAQKALLGSKKEEKSSDMYIPTPDASRIWPEAHKYYKDQKFKQPETYIKFSATVEDTVGVEYNMDEVDEKFYRETLCKYYPKKKNKSDENNRKCTELEFETICDKLEKTIEARQPFLSMDPSNILSYEELSSYIVDQFKSAVKTSNPYIVTNGGNLEYISTTALKERLSKEIKYEPFVTIFDKNQMSTSAVRPIPKLFELFGRPVYDHWKERKIERKGKTIQPTLKFEDPNSNEKENDNDPYICFRRREFRQARKTRRADTIGAERIRSMQKSLHRARDLIMSVSEREILKLDNFQAEHELFKARCATKACKRELNIKGDEYLFFPHKKKKIVRTEDEEREKKREKKKQDQELALKQQQALQQQQQQPPQPPQQAPSKQDGTSTSQPYVKLPPAKVPDMDLVTVSLVLKEKNETIKRAVLEKLRKRKEHDKGFINLTDDPYQPFFDISTNRAEELSHIPYSSIAATHYHQFNTSNYMNDQLKKLLEEKKPLPGVKTFLGSNGELVPSKAFPHLSSLLEEKYKATSGYIERLLQSVETQDFSSYTNGFKDVEPKETNEPVMAFPQRIRRRVGRAGRVFLDHQQEYPQPNFQQDTDRVGGIPDVYCKEDAIKRLQSKWKFDTEYKTTEPFSLDPSKLNGISPSTQSIRFGSMLLNRTRK
The following text describes a protein:
Function:
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins.
Subcellular Localization:
Nucleus.
Sequence:
MATEAKAVTEDVKIDLFEDDDEFEEFEINEEWDDMEEGKEVTQQWEDDWDDDDVSDDFSVQLRRELEKTTDKN
The following text describes a protein:
Function:
Part of a membrane-cytoskeletal adapter complex that forms a bridge between the endoplasmic reticulum and the plasma membrane. Associates with microtubules.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Protein storage vacuole membrane; Single-pass type IV membrane protein; Cytoplasmic side. Note=Localizes to immobile punctate structures reminiscent of the ER-plasma membrane contact sites.
Sequence:
MSNIDLIGMSNRDLIGMSNSELLTVEPLDLQFPFELKKQISCSLYLTNKTDNNVAFKVKTTNPKKYCVRPNTGVVLPRSTCEVLVTMQAQKEAPSDMQCKDKFLLQGVIASPGVTAKEVTPEMFSKEAGHRVEETKLRVTYVAPPRPPSPVHEGSEEGSSPRASVSDNGHGSEFSFERFIVDNKAGHQENTSEARALITKLTEEKQSAIQLNNRLQRELDQLRRESKKSQSGGIPFMYVLLVGLIGLILGYIMKRT
The following text describes a protein:
Function:
Promotes K(+)/H(+) antiport activity supporting K(+) efflux to control H(+) homeostasis in chloroplasts. Also able to ensure Ca(2+)/H(+) antiport activity in vitro. Essential for chloroplast pH regulation and optimization of non-photochemical quenching (NPQ), a regulatory mechanism that dissipates excess light energy; acts downstream of PSBS but independently from PGR5 and FLAP1.
Subcellular Localization:
Plastid, chloroplast envelope. Plastid, chloroplast membrane; Multi-pass membrane protein.
Sequence:
MSLMSSSMVLCHCLSFSSQNPDPESSSSSLLRYKPCDSISLWGKRRKKLWRFVPSAEKNNSHTGNNNKRRRSWWQRFFFDDDGNWLGLRDDDIVDETTELAKDDEMSDEEKFETWKRRAEAIVELREGQEEIGDSGVVADVTKKWEDWIVDSDDSFVESWTRDSAGSDDNLELDELTIPDGGLVKMVRDMVLGAEEEDILYEDRIFRYASSKSAKFLAVLILIPWALDFLAHDYLLMPFLDRYVKTVPLAAQTLDVRRNQKLEMVKELNREKARYRLEVEIGKSPPLSDDDLWWEMRGKALELRDEWRLENRKAFANIWSDMVFGISLFVLLYANQGRVALLKFTGYKIINNISDTGKAFLIILITDIFLGYHSESGWETLLEIIMEHYGLEVEQSTITIFICLVPVIMDACVKLWLFKFLPRLSPRVSNIFQEMKRH
The following text describes a protein:
Function:
Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'. Plays a role in hematopoiesis and malignant transformation.
Subcellular Localization:
Nucleus.
Sequence:
MSVRQSMTWVISVQERISYTPPASPVPNFPSSSPLHVPGPRPLRMEEDSIRLPAHLRLQPVSWSRDDVGQWLKWAEKEFSLRPIDNNTFEMNGKALLLLTKEDFRYRCPHSGDVLYELLQHILKQRKTRMLFSPFFHPGNSIHTQPEVLVPQNHELDNCLQRASRPPVESVQHNPPTIELLHRSRSPVTTNHRPSPDPDQRPLRSPLDNMIRRLSPAERVSGPRLHQEGGHQEPYPLCVSPMENNHCPPTSEGPAKPSSPRPESARVIQLMPSPIMHPLILNPRHSVDFKQSRLAEDGLHREGKPINLSHREDLAYVNHIMVSVSPPEDHAVPIGRIADCRLLWDYVYQLLSDSRYENFIRWEDKESKIFRIVDPNGLARLWGNHKNRTNMTYEKMSRALRHYYKLNIIRKEPGQRLLFRFMKTPDEIMSGRTDRLEHLESQELDEQIYQEDEC
The following text describes a protein:
Function:
Metal-responsive transcriptional regulator that represses transcription of the aseR-ydfA operon by binding specifically to its promoter. Binding of arsenite or antimonite causes the repressor to dissociate from the DNA.
Miscellaneous:
MISCELLANEOUS: Can also bind zinc in vitro, but it does not impair DNA binding.
Subcellular Localization:
Cytoplasm.
Sequence:
MTIDVAAMTRCLKTLSDQTRLIMMRLFLEQEYCVCQLVDMFEMSQPAISQHLRKLKNAGFVNEDRRGQWRYYSINGSCPEFDTLQLILHQIDQEDELLNHIKQKKTQACCQ
The following text describes a protein:
Function:
DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. The heterodimer formed by RPA34 and RPA49 stimulates transcript elongation by Pol I. Subunit RPA49 can bind both single-stranded and double-stranded DNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSVKRSVSEIEIESVQDQPSVAVGSFFKGFRAPSDTTFDLYKKKKSEKDEFVLHGENERLEYEGYTDSSSQASNQYVVGLFNPEKKSIQLYKAPVLVSKVVSKSSKNLRGPKIKSKSDTRPSALRNALGEAFGTKKAKKAIADLERNRIDSDKLTDSAIDIVDSVRTASKDLPTRAQLDEITSNDRPTPLANIDATDVEQIYPIESIIPKKELQFIRVSSILKEADKEKKLELFPYQNNSKYVAKKLDSLTQPSQMTKLQLLYYLSLLLGVYENRRVNNKTKLLERLNSPPEILVDGILSRFTVIKPGQFGRSKDRSYFIDPQNEDKILCYILAIIMHLDNFIVEITPLAHELNLKPSKVVSLFRVLGAIVKGATVAQAEAFGIPKSTAASYKIATMKVPFKLPEMTRRGRGPRR
The following text describes a protein:
Function:
Prenyltransferase specific for geranyl diphosphate as prenyl donor and coumarin as prenyl acceptor. Can use umbelliferone and esculetin as substrates, and with a lower activity, 5,7-dihydroxy-coumarin and 5-methoxy-7-hydroxycoumarin. No activity with 5-hydroxy-7-methoxycoumarin, bergaptol, xanthotoxol, p-coumaric acid, caffeic acid, 2,4-dihydroxycinnamic acid, kaempferol, genistein or homogentisate. No activity with dimethylallyl diphosphate, farnesyl diphosphate or geranylgeranyl diphosphate as prenyl donors.
Subcellular Localization:
Plastid, chloroplast membrane; Multi-pass membrane protein.
Sequence:
MLQMHSNSSFSPKCYYPLQHAGCVKTLQLPLTKVHGGLNRSESKNYAIKCTQSDSFYSTNKIRNNENSSSRNCKPFNKYRVAVTLQQQDCASNNEDDINSTSFRDVLLKKLHALYVFTRPFAMIGTIVGITSIAILPLQSFADLTPKYFMEFLKALLSAVLMNNYVGTVNQVADVEIDKVNKPGLPLASGDLSVGTGLAITLILSLTSLAIALSLQSPPLIFGLIVWFLLGTAYSVDLPFLRWKTNPFLAGMCMVIVFGLVYQFSFFIHFQKYVLGRPVVITRPLIFAAAIISTISAVMSLLKDIPDEDGDKQFGYQSISSKLGKENVLRLCVYALFFAYGVAVIVGASSSFQLGKLVSIIGHSTLAFLLWLRAQTVDLSNNASTYSFYMFIWKLFYAEYLLIHFLR
The following text describes a protein:
Function:
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion.
Subcellular Localization:
Golgi apparatus membrane; Lipid-anchor.
Sequence:
MPHRLRQNLLLPQPPTVVLHDPRTHLRHLPPAYSAAQTPLSKERDFGAQVRYYLEAPRKPKFRPCKVIFVGDCSVGKTAIVNRFCYDKFQSNYKATIGVDFELENFSILGHNYSLEMWDTAGQERFRCIAGAYYRNASVIVVTYDMSKKDSLESAKKWLNSALNYNASKRPLVFLVGTKADLLSKEEFVRMERLAGLAAAELQAEYWSVSARSGFKVTELFQRIAALAFEEAVMQEIRSIKNKPQEQATQASVKSQTFDLRNFFGSRLSQQKSGCTC
The following text describes a protein:
Function:
As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair (By similarity). The dpb3-dpb4 dimer associates with histone deacetylases, chromatin remodelers, and histones and plays a crucial role in the inheritance of histone hypoacetylation and H3K9 methylation in heterochromatin. The dpb3-dpb4 dimer is also required for the recruitment of sir2 to heterochromatin.
Subcellular Localization:
Nucleus.
Sequence:
MNQDKSKETSELDDLALPRSIIMRLVKGVLPEKSLVQKEALKAMINSATLFVSFLTSASGEIATNNNRKILMPQDVLNALDEIEYPEFSKTLKKHLEAYELALKEKRLKLPNVSDVDNRKKAKIDAHDTTPLDEEKDELEEERIAEDIAQNEVEQNIDDVEDLEEVNDTLDANAESPQIETIHLTDATGNPIEDSSESDSEESLQLNDSS
The following text describes a protein:
Function:
Involved in the assembly of the cytochrome c oxidase complex.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MGWFGGGSGSSSTPPSKVSIVTEYKPEEKTQQYLEDLPPKFEDSEPIPERQATLMDAAQRIKLSDFTVDRFISMPCFREAMITGFQAMGVLGVVTFLIHKNVQKTMNWSVGGFFLGNIIGWEQCRSLRRKSFQMIEKAQQERDEKNKKKWAEMQQSDDEDLKKFQEFNSRK
The following text describes a protein:
Function:
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Sequence:
MAIAENYDEVLKGKYPAKDHARKVAKWIVDKGGDKKGTIYLEAQKQKLNEDNDGEAPFRQRRYFFYLSGCELPDSYLTYDFPSDKLTLFIPPVEPEEVIWSGLPMSPEEAKAKYDIDDCKTTKEVNPHLASSSETAQSTIYAIPGQISDETTFLSYQNKDLEQLKTAIEYCRVTKSDYEIALIRKANVISTNAHINVMKAAAKAQNECELEAVFLKSCVERNAKNQAYHSIVAAGENGATLHYVHNAAPIKSQNLMLLDAGCEVDCYASDITRTFPIKGTFTDESLAIYKIVLDMQKQCINALKAGVLWDSIHELAHKIAIKGLLELGILKGDVEQIFKARTSVAFFPHGLGHYLGMDTHDTGGNANYADKDRMFRYLRVRGTLPARSVITVEPGIYFCRFIIEPYLKDDQQKQYIDEKVLEKYWSVGGVRIEDNILVTEDGIENLTPTPKEIDEITSLVKSG