lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.
Sequence:
MRRQSRIVASLLVLACASSGAFAHRKFNVHDDLLAYPQFRIKFPDGFILESQARAFLEQAPYSSPDLNDISEQTPLKDESEESIRDGSSGEKAKFSYEELSLEGQRYLCQIPVVEDGDSNRTKVEVNEEEERKELARATDRGLELLREMEGKCLYYISGWWSYSFCYMNQIKQFHALPSGGGVPNYPPMEDHTTHSFILGRFPQEEGQDEGKGAKSGKSSTELAELQTKGGSRYLVQRLESGDQCDLTGKNRKIEVQFHCNPQSTDRIAWIKELYTCSYLMLIYTPRLCNDVAFLPPQQEEVHTIECREILTPEEVTGWQAMHEYQLSQQLVESAEAPKHQVIGGIEVGAQRLVGTEGKRIEKGRVASIGEEKVDVVAKRVNGEVQLLSAEELKKFDLDEAKIEELRKKLEEWAKGKDWTLEIVTGNGAYLRGVVDTDEDEEDGYENEEGETDKREQRENTQETTGQPGQPGHQEETESGQAGHPMDDRSEDGEDPDVDGSEEIFKDEL
The following text describes a protein:
Function:
Catalyzes the first step of the osmoprotectant glycine betaine synthesis.
Subcellular Localization:
Cytoplasm, cytosol. Plastid, chloroplast stroma.
Sequence:
MAEEVVLLDFWPSMFGIRSRIALAEKGIKYEYKEEDLWNKSALLLQTKPVHKKIPVLIHNGKLVCESLIQVQYIDEVWHDKAPLLPSDPYQKATARFWADYVDKKDFGLVPIKVATWGPFVLLNMDNEILQKDNIDTDNVTSEWLGSSSELFSLNGVDTTLTYVCRREYIIECNWKDDKAFIERSLADSEKVQENTQMEDIRLCEGVQKGIESPAYSTGRYAPNVEKAMHHFHCLLYDNLINFFCLLNAFLNCCLASIGTAQGTPTPMFQFSSHSYWIPACKWHNTSPLYLLSSSYDGKVMLWDLRTALFYVLNGGKWNRKNQLH
The following text describes a protein:
Function:
This is a receptor for the anterior pituitary hormone prolactin.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Domain:
The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding; The box 1 motif is required for JAK interaction and/or activation.
Sequence:
MMKNDGGVRLFWLLLLFLLYTRGKSYSVPGKPTLTRCRSPEKETFTCWWEPGSDGGLPTTYKLFYRKEGSEKEYQCTDYHTGGKNSCFFNKNDTSIWVNYNITVVATNALGQALSDPLNIDVYYIVEPNPPENLKVTIQNDKGWPFLRASWDPPTKADTRSGWITLIYELRIKLEEEDEWEIHHVGQQKVFNIFGLQSEGTYVIQIRCKPDHGFWSEWSEDVQVVVPNYFPNKRSTWVLVMVFSGMVFLILSWLLHINSRNLKHCILPPVPGPKIKGFDQKLHKSGKSVDAFKSLDVPDFPHHTFSKSEDLLVEYIEVYVPEEQELMLEKSNNLHNGCLKSENSVSDCDSGRGSCDSHTLLLDKSGQQTDTQESQTDEQRHGEALQGENLAYTHQDMVSPDMSAGRVKTWPSVFSPLPQNRSTEDQTSSLEIAKQHCLSDSLLPSDFLTPYHSPPGHCTREHLGSNYWEFDFGNKRPHLTQPQTEVCHQIQAHSEININTGVKAEPAAQKFPTPRSNEYVEVQRINEEDSVVLRPVASNYDKLFEMQQGEDYSRVKGVDSDSVLLLLQKEAMEEEMNMCSCEQLTDTTDAHYTTFATSPEKPTACTHPTPQPLEERVVNGYVDTATMFTMPPY
The following text describes a protein:
Function:
Catalyzes the epimerization of beta-D-mannuronate to alpha-L-guluronate during the synthesis of the linear polysaccharide alginate. In addition, is part of a periplasmic protein complex that protects alginate from degradation by AlgL by channeling the newly formed alginate polymer through a scaffold that transfers the alginate polymer through the periplasmic space to the outer membrane secretin AlgE.
Subcellular Localization:
Periplasm.
Domain:
The C-terminal region contains a right-handed beta-helix (RHbetaH) fold, which is common among proteins that bind and cleave long-chain linear polysaccharides.
Sequence:
MPDISLSIPRRRLPRLRPLAAAVLGAVLLHGQAWAAQPVEKPQPVPAQAGNEPGLTQGLKETGNYTVTTAPAEPLHLDPPKLPDLSGYTAAAVEAKIVRKPGGRASVQRMVQQQPLKEFTGGSNRLAEWVKRQRQMPQAIFIEGGYVNLAQLAGKLPASALEQVEPGVFVARLPIVVSQGATLDIDKQVKELRLSQERGAFLVNDGMLFVRDSKVTGWSESKKEPAWFKTPNEFRPFLISWGGAEVYLSNSTFTSFGYNASKAYGISISQYSPGMDKQMKRPRPKGWVIDSTIVDSWYGFYCYEADDLVVKGNTYRDNIVYGIDPHDRSHRLIIADNTVHGTRKKHGIIVSREVNDSFIFNNRSYENKLSGIVLDRNSEGNLVAYNEVYRNHSDGITLYESGDNLLWGNQVLANRRHGIRVRNSVNIRLYENLAAGNQLIGVYGHIKDLTNTDRNIALDPFDTKVSLIVVGGKLAGNGSGPLSVDSPLSLELYRVAMLAPTKSSGISLPGVLGEKQDQILDLLVRQDKAVLIDPVESQAELQD
The following text describes a protein:
Function:
Probably involved in translation.
Sequence:
MLDLSETVIPASFDPFAEADVEDSGVGSKGSGYVHVRVQQRNGRKSLTTVQGLKKEFNYNKILKDLKKEFCCNGVVVQDPELGQVIQLQGDQRKNVSNFLVQAGIVKKDLIKIHGF
The following text describes a protein:
Function:
The GINS complex plays an essential role in the initiation of DNA replication.
Subcellular Localization:
Nucleus.
Sequence:
MGYYDLDDILADSSKFACRFNYELPGLGYLEGNPGKPVGKHSKVELPLWLASVLATVTGEQEHVDEEALPFVEFLPPEMFSARVVNAIKADAPTLDVHSINGHFYALGTRWAALFSDAGLAGMLAGMVLERALEVQRHAASAAVEATAPTDATARMLQTLDEWERQLYRRAHAASRDAKLWAARR
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 membrane; Multi-pass membrane protein.
Sequence:
MATVTILSPKSIPKVTDSKFGARVSDQIVNVVKCGKSGRRLKLAKLVSAAGLSQIEPDINEDPIGQFETNSIEMEDFKYGYYDGAHTYYEGEVQKGTFWGAIADDIAAVDQTNGFQGLISCMFLPAIALGMYFDAPGEYLFIGAALFTVVFCIIEMDKPDQPHNFEPQIYKLERGARDKLINDYNTMSIWDFNDKYGDVWDFTIEKDDIATR
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MLRSFSHFLQIGSRRQPTYFRCFHKTTVHLNSFKNDPKKELNSNLNEKSVEESSKNETKEQFNSSSIPRESESEGKTASNTSPLSPKKVENLSKLFNDINEDVSIEELKSRFKDHLPFYENYIRNHPLAIEALQKSTAPRQTGLKLNYVSKLDKYVTPLDGYSHLGSEESNGEIPDKWEDFKDDLTFEISSKFSPFDFGDAGKSTSDAEFLSDISGIPKSDLRALMFVPLVRRRVVNQTRKGKIASMYVLTVVGNRNGVAGFGEGKAESYSLAYKQSCGRAVKNMVYIPRYDKRTVYGVIHKKFHAVRLTLRSRPAGFGLRCNPILHEICRCAGIKDISGEILGSKNGMNTVKAMFEALQSQRLPEDIAMERGQKFVDVQREYYKQT
The following text describes a protein:
Function:
Rho GTPase-activating protein involved in the signal transduction pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MQKENLSIIEMWKKNRFEERRIEIVQYKNRPFIQIDKRPRIDLTKAIVSRTIEMEIPIEESKKSLCFEVVYDKQFVFFCKDDDMVRYWVNKMALVSKTFGVFGYPLSCAVKKSSWRFPIPVFRSLQYLLTHEGKELEGIFRTNASHVSLSRIKTILDCDQDVDMESFDDCRVAAAILKDYLRQLPEPLIPYEYYKQFIELPLKTTDPKLFMESLPKMNQDTLWYLCSFLYEIQLNEEKTRMNASNLATCIGLTVCRPPPFEGVDELIHTKNAISAFEFVLNNYEPIFFSIKQRNEKEGLIPPEYPCVIPHQKIPFCRLTGMIKTTIKKDSDLPQATPQVRTKAKLSKCNSETNLTPALGIDKNKNIRVSEVPSSPKEELNIEKLDEGTEKEKELEHCESPISDGTTPKIKKEKKEKKGRKGSIEGNINTLIAKGWSKMKFERKTNTTSSSTTTESKEDKKKDESKEKDTKPPRSPRGSLLPSTFKKLSQEKDHKRNETTELTDEQILTQHITEVQINLIEDLKKELVKLNDELNKVKAERDYLKRKYEPESFVETNKYGIPTDNQFAFTQTQFTEEKHEEIHVPSFTDYEHNEKHNEKYNEIKDSSESKEENKEENKEENKEENKESSNEEKNEEKNEESSLLKEKNVIIESDIESHENKKEEEPKVILSNSGSTHLSDEDSEISNNEVKTNND
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors.
Miscellaneous:
MISCELLANEOUS: Present with 4420 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Sequence:
MYSTPLKKRIDYDRETFTASASLGGNRLRNRPRDDQNNGKPNLSSRSFLSERKTRKDVLNKYGEAGNTIESELRDVTTHVKISGLTSSEPLQLASEFVQDLSFRDRNTPILDNPDYYSKGLDYNFSDEVGGLGAFTPFQRQQVTNIPDEVLSQVSNTEIKSDMGIFLELNYCWITSDNKLILWNINNSSEYHCIDEIEHTILKVKLVKPSPNTFVSSVENLLIVATLFDIYILTISFNDRTHELNIFNTGLKVNVTGFNVSNIISYERTGQIFFTGATDGVNVWELQYNCSENLFNSKSNKICLTKSNLANLLPTKLIPSIPGGKLIQKVLEGDAGTEEETISQLEVDQSRGVLHTLSTKSIVRSYLITSNGLVGPVLIDAAHIRRGMNALGVKNSPLLSNRAFKIAKIVSISMCENNDLFLAVITTTGVRLYFKGSISRRSIGSLKLDSVKFPPTSISSSLEQNKSFIIGHHPLNTHDTGPLSTQKASSTYINTTCASTIISPGIYFTCVRKRANSGELSKGITNKALLENKEEHKLYVSAPDYGILKNYGKYVENTALLDTTDEIKEIVPLTRSFNYTSTPQGYANVFASQYSAEPLKVAVLTSNALEIYCYRTPDEVFESLIENPLPFIHSYGLSEACSTALYLACKFNKSEHIKSSALAFFSAGIPGVVEIKPKSSRESGSVPPISQNLFDKSGECDGIVLSPRFYGSALLITRLFSQIWEERVFVFKRASKTEKMDAFGISITRPQVEYYLSSISVLADFFNIHRPSFVSFVPPKGSNAITASDAESIAMNALILLINSIKDALSLINVFYEDIDAFKSLLNTLMGAGGVYDSKTREYFFDLKFHDLFTPNAKTKQLIKEILIEVVNANIASGTSADYIVNVLKERFGSFCHSADILCYRAGEHLEAAQKFEMIDSKISRNHLDTAIDLYERCAENIELCELRRVVDIMVKLNYQPKTVGFLLRFADKIDKGNQAQEYVSRGCNTADPRKVFYDKRINVYTLIFEIVKSVDDYTSIEQSPSIANISIFSPASSLKKRVYSVIMNSNNRFFHYCFYDWLVANKRQDYLLRLDSQFVLPYLKERAEKSLEISNLLWFYLFKEEHFLEAADVLYALASSDFDLKLSERIECLARANGLCDSSTSFDQKPALVQLSENIHELFDIASIQDDLLNLVRNETRIDEDYRKQLTLKLNGRVLPLSDLFNDCADPLDYYEIKLRIFKVSQFKDEKVIQGEWNRLLDSMKNAPSPDVGSVGQESFLSSISNTLIRIGKTTRDTDVVFPVHFLMNKILESFIDKSSAADGSVCSMFLLAGVSHLKLYYILSRIIENSEGNVELAKKEMVWLIKDWYQSDSDLRGSIAPEQIKKLEKYDPNTDPVQDYVKDRHHGLK
The following text describes a protein:
Function:
Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.
Subcellular Localization:
Nucleus matrix. Nucleus speckle.
Sequence:
MCSGSGRRRSSLSPTMRPGTGAERGGLMMGHPGMHYAPMGMHPMGQRANMPPVPHGMMPQMMPPMGGPPMGQMPGMMSSVMPGMMMSHMSQASMQPALPPGVNNMDVAAGTTSGAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEGYQNTIVAGSLITKSNLHAMIKAEESSKQEECTTTSAAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANASASTSASSTVSGTVPVVPEPEVTSIVATVVDNENTVTISTEEQAQLTSTPSVQDQSEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAISERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPVFSLGSTALDLFKFYVEDLKARYHDEKKIIKDILKDKGFVVEVNTTFEDFVAIISSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQATPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMHVLEHECQHHHSKNKKHSKKSKKHHRKRSRSRSGSDSDDDDSHSKKKRQRSESRSASEHSSSAESERSYKKSKKHKKKSKKRRHKSDSPESDAEREKDKKEKDREGEKDRTRQRSESKHKSPKKKTGKDSGNWDTSGSELSEGELEKRRRTLLEQLDDDQ
The following text describes a protein:
Function:
May play a role in sperm motility, especially in the regulation of flagellar function.
Sequence:
MDITSIKKTLGSQYRVVFFLGQGSYGRVRLAWHRRTQALVAIKTVEISKDTIRGILSEMTTLESLNHPNIISLYEVLITGTGVHFILQYAPGGNLGKLISEEGPLPEEKAKKMFGQVVSAIRYCHSLDIVHRDIKPQNILIDGEGNIKLIDFGQAIKCKPGTLLSRHCGTRDFNAPELVLREPYDGKSSDVWSLGVVLYFFTTGYLPFRGKTINDVEERITTGTYTIPTHLSGQLENLIHQILRVSPDMRPSVEEIENHPWIKKCEFKILPKTDPDYKIIEMLCAMGYKAKDILESLQKKRYDEPMGAYLSLKDHVSKGFDVGYITPAKPGDPCPPPPPSPAHPSVFGLPLRRRASEPIFGLHHRPPSREQNPLDLILSGLKMSRCVSMPPIAVYYPKKERSTSTRALHSTPVACPCVSNNMSEVEIILPPKQDIEMNTSSPPQRMGWFKRLRKGIRDCFSRLCCLPRAPKKKTQHRSSKRVAPLKKAASSTI
The following text describes a protein:
Function:
Over-expression suppresses AP1, CREB, NFAT, and NF-kB transcriptional activation, and delays cell cycle progression at S phase.
Sequence:
MAAVLKPVLLGLRDAPVHGSPTGPGAWTASKLGGIPDALPTVAAPRPVCQRCGQPLALVVQVYCPLEGSPFHRLLHVFACACPGCSTGGARSWKVFRSQCLQVPEREAQDAQKQGNSLAAEDWCEGADDWGSDTEEGPSPQFTLDFGNDASSAKDVDWTARLQDLRLQDAVLGAAHPVPPGLPLFLPYYICVADEDDYRDFVNLDHAHSLLRDYQQREGIAMDQLLSQSLPNDGDEKYEKTIIKSGDQTFYKFMKRIAACQEQILRYSWSGEPLFLTCPTSEVTELPACSQCGGQRIFEFQLMPALVSMLKSANLGLSVEFGTILVYTCEKSCWPPNHQTPMEEFCIIQEDPDELLFK
The following text describes a protein:
Function:
Required for normal beta-1,6-glucan synthesis.
Miscellaneous:
MISCELLANEOUS: Present with 3460 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MQTVLKYLLLIMCGSFCASEELQNQTNVPAIFFSYKLTPGILKYQEDYDRAVTLPRDTFIEAAEKFLGVCNADTYVFINQPGLRKLDFLEFETEFVSLQRYIRRSSTAIKFEKVDLLPQDLYYDLAEFVKEYCNVDQVLNLRGNNTEDFQPFIDSEKRVIIIEYPKLPEDTNERKEAFRHYDKYLRTILAQIPSPEQNVIYTSLNPGTTLAHESIIPIQIFPDIFDIKSRVGEVEQNNRVLDVPRLSFNDYTPRFSEPPSEYVSIFDSQLIENNRGLLQLIFTILVGYILIQFFFTKKTIVDEKITNKKDNVKQTSPQLLKKVQEIQKKPSQQVS
The following text describes a protein:
Function:
In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity.
Sequence:
MARLFLFDGTALAYRAYYALDRSLSTSTGIPTNATYGVARMLVRFIKDHIIVGKDYVAVAFDKKAATFRHKLLETYKAQRPKTPDLLIQQLPYIKKLVEALGMKVLEVEGYEADDIIATLAVKGLPLFDEIFIVTGDKDMLQLVNEKIKVWRIVKGISDLELYDAQKVKEKYGVEPQQIPDLLALTGDEIDNIPGVTGIGEKTAVQLLEKYKDLEDILNHVRELPQKVRKALLRDRENAILSKKLAILETNVPIEINWEELRYQGYDREKLLPLLKELEFASIMKELQLYEESEPVGYRIVKDLVEFEKLIEKLRESPSFAIDLETSSLDPFDCDIVGISVSFKPKEAYYIPLHHRNAQNLDEKEVLKKLKEILEDPGAKIVGQNLKFDYKVLMVKGVEPVPPYFDTMIAAYLLEPNEKKFNLDDLALKFLGYKMTSYQELMSFSFPLFGFSFADVPVEKAANYSCEDADITYRLYKTLSLKLHEADLENVFYKIEMPLVNVLARMELNGVYVDTEFLKKLSEEYGKKLEELAEEIYRIAGEPFNINSPKQVSRILFEKLGIKPRGKTTKTGDYSTRIEVLEELAGEHEIIPLILEYRKIQKLKSTYIDALPKMVNPKTGRIHASFNQTGTATGRLSSSDPNLQNLPTKSEEGKEIRKAIVPQDPNWWIVSADYSQIELRILAHLSGDENLLRAFEEGIDVHTLTASRIFNVKPEEVTEEMRRAGKMVNFSIIYGVTPYGLSVRLGVPVKEAEKMIVNYFVLYPKVRDYIQRVVSEAKEKGYVRTLFGRKRDIPQLMARDRNTQAEGERIAINTPIQGTAADIIKLAMIEIDRELKERKMRSKMIIQVHDELVFEVPNEEKDALVELVKDRMTNVVKLSVPLEVDVTIGKTWS
The following text describes a protein:
Function:
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function.
Subcellular Localization:
Cytoplasm, perinuclear region. Nucleus.
Sequence:
MEAKWFLSIIQDDFRSGRINLDRTMKLLEKLKIPCDYAHVKHIFKANDREKTGKITIEEFRAIYRTLAHKEEILEIFNAYSANRKILPKPKLMEFLQREQFIMDMVSQVACAIIDQYEPIEEVRGKKEMTFEGFSRFMDSQDCLLFKKDYRKVYQDMTRPLRDYFISSSHNTYLVSDQLIGRSDLWGYISALLKGCRCLEIDCWDGYQNQPVVYHGHTLTSKIMFKTVIQVINMYAFMASEYPVVLSLENHCSPKQQEVMADDLESILGEKLLSETLCDFPDELPSPEALKFKILVKNKKIGTLRETVLRRGTDRHGQVGECEEVEDDEEDGEEEEEEAAAEKKESQTLLRDRASKKLTEDRKIWGRRKFSSTKGDKIRKIKIAMELSDLVIYTKSQKFRSFEHSRATQKFYENNSIGETRARKLAKMAAREFISHTGKFITRIYPKGTRTDSSNYNPQEFWNLGCQMVALNFQTPGLPMDLQNGRFLDNGGCGYILKPEILRNSKLSFNPTGPSTNDSPVTFSIRVGTTCYGRIERNLCRKLISGFQLPPSNFSASNKADPRVIIEIHGVPEDQCKQQTRVIKKNALCPRWNETFTFTIQVPDLALVRFVVEDQVSLASNEFLGQYTLPFYCMDKGYRRVPLFSKLGDSLDPASLFVYIWYY
The following text describes a protein:
Function:
Involved in the biogenesis of rRNA. Required for the formation of 18S and 5.8S rRNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAQKKDSQVSKDKSSKKTQNESSSTAPRPAPAFTSTLQNDETDFPRGGGSSLTAFEFKQVREEGRREAENEAKHQASKGEKRKRQMSDRQAKRLKKNEDAKKKEERDKDNIRVEILNYKRLVPGTHVLARVHTILPLHLILSLPNNLLAHVPITEISNTLTQLLTAEEAMAVDEGEEESDDESSAPDLAQLFVPGQYVHAKVLTLYPTASQSFISQYPITETTKLASRVELTLIPEKVNSEVAKKDLETGYFLVGEVKSEEDKGWIVGVGLNTQGGSSVEGFVSKDEVAKFVPAQALIPGQLLPATISSIAAGGRVAHLSLNQQDITRSQISEVSTVGSIVPGHSVNALITAVVPSGLNVKVAGFFDGTIDLAHLPLGEDDIENKYKIGKKIRARVIYDNLAANPHSFALSALPHVLNFTSPTQEGDNTPLELAIPIGKVYQSVKVTRVLNDWGVMVRTQDGLEGFVHISHLADERIPVLSNATPQFKAGTLHRARVIGHSPMDGVLLLSFEQSVLSQLFMQVDELKVGQQLKGTIRRLTDKMLFVNVHGNVDGIVHPTHYADIRLKHPQKRFKPEGSVKARVLYLEPTRNRVVLTLKKTFLESDLAVPQGFEDLKVGEVTLGSVLKIVDKGVIVELFAGLKAFMPHSECSQTHIKNLSEAFYIGKPLTVRVITVDASASRIVVSAKQAAPTAPATAAEKLEVGEAVSGTVSQVHTEQVVVKLDGNGLTALLSLSNLSNQRHTGIEELRRSLKEGEKIDDLVVVSKNPVSGLIIVNIKKTITAKKEKAKKEDKAPSGISAHVKAIDAIEVGQIITGTVQEQTSQGYMVQLPNNLRGRVHPCDSSDDLALAAGHGPLTVGEEVKCYVLDVNRSKRAIDLSTRLSRVQGKENVVDREINTVDDLKEGESVRGLVKNIAGHGVFVSLGRNVTARIMIKELFDEYVKDWKSRFEINQLVSGKILSINPGSNSIEMTLRKNPSKSAKKTALLSLSDFEEGQKVVAVVRKVEAYGMFLKIEGSNVSGLCHKSEITDNRKADVAQALKGFREGDQVKAKIVSIDTEKGKISFGIKASYFGEEFEGGEKSEDEDDEVDEENDERFNEGDQEMESDAGESGEGQEHEDEEALEIDGGEEEATSDEEDNAPQNFKPAPKTALNLGAGFDWTGEAPAAAPESDDESDSDEEAVAPAKSKGKSKAVDLTATAPSSRPSSTGEYERALLASPNSSFLWIQYMSFHLQLHEIEKARKIGRQALEKISYREEEEKLNVWMALINLEIAFGTVSATEKVFEEAAQYNDKRTVYMRYAEALQVAGKDEALEELFKKIVKKFSAYPESWTRFAEFYLNKGDVEAARALLPRSMKSLDKSKHVETIEKMALLEFKQGDAERGKTLFEGLVDRFPKRLDLWGVYIDQVAKVGDIQGVRGLMDRALEQKLTSKKAKFLFKKWLTIEQRIGDAAGQDKAKTRAREWVEANAKKPAQDEEEDSNDEE
The following text describes a protein:
Function:
Ubiquitin-like protein involved in autophagic vesicle formation.
Sequence:
MVEEPQSMLQLPPSSATGEEGLTEVSPETTTLEPPSSAAVSPGTEEPAGDTKKKIDILLKAVGDTPIMKTKKWAFLKLVASEQLFIYVNQSFAPSPDQEVGTLSECFGSDGKLVLHYCKSQAWG
The following text describes a protein:
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.
Sequence:
MFQQLIDGISYCHNKGIFHRDLKLENVLLDENGHIKITDFGVRAVPQHFREDGLLHTTCGSPNYVAPEVLANKGYDGAASDIWSCGVILYVILTGCLPFDDTNLAVLCRKIVKGDSPIPRWLSPGAKTMIKRMLDPNPVTRMTVASIMAND
The following text describes a protein:
Function:
Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Sequence:
MAQTFVDAQIRDNKVVMFSKTFCPYCKMAKDSLASAGLKDYKVVELENHNMCAEIQDYLNKLTGARSVPRVFIGGKCIGGGSETKALQESGKLTTMLQQNGAM
The following text describes a protein:
Function:
Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion. Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events. Overexpression induces the formation of mitochondrial networks. Membrane clustering requires GTPase activity and may involve a major rearrangement of the coiled coil domains (Probable). Plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes (By similarity). Plays an important role in the regulation of vascular smooth muscle cell proliferation (By similarity). Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). Is required for PRKN recruitment to dysfunctional mitochondria. Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress (By similarity). Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions (By similarity).
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=Colocalizes with BAX during apoptosis.
Domain:
A helix bundle is formed by helices from the N-terminal and the C-terminal part of the protein. The GTPase domain cannot be expressed by itself, without the helix bundle. Rearrangement of the helix bundle and/or of the coiled coil domains may bring membranes from adjacent mitochondria into close contact, and thereby play a role in mitochondrial fusion.
Sequence:
MSLLFSRCNSIVTVKKNKRHMAEVNASPLKHFVTAKKKINGIFEQLGAYIQESATFLEDTYRNAELDPVTTEEQVLDVKGYLSKVRGISEVLARRHMKVAFFGRTSNGKSTVINAMLWDKVLPSGIGHTTNCFLRVEGTDGHEAFLLTEGSEEKRSAKTVNQLAHALHQDKQLHAGSLVSVMWPNSKCPLLKDDLVLMDSPGIDVTTELDSWIDKFCLDADVFVLVANSESTLMQTEKHFFHKVSERLSRPNIFILNNRWDASASEPEYMEEVRRQHMERCTSFLVDELGVVDRSQAGDRIFFVSAKEVLNARIQKAQGMPEGGGALAEGFQVRMFEFQNFERRFEECISQSAVKTKFEQHTVRAKQIAEAVRLIMDSLHMAAREQQVYCEEMREERQDRLKFIDKQLELLAQDYKLRIKQITEEVERQVSTAMAEEIRRLSVLVDDYQMDFHPSPVVLKVYKNELHRHIEEGLGRNMSDRCSTAITNSLQTMQQDMIDGLKPLLPVSVRSQIDMLVPRQCFSLNYDLNCDKLCADFQEDIEFHFSLGWTMLVNRFLGPKNSRRALMGYNDQVQRPIPLTPANPSMPPLPQGSLTQEEFMVSMVTGLASLTSRTSMGILVVGGVVWKAVGWRLIALSFGLYGLLYVYERLTWTTKAKERAFKRQFVEHASEKLQLVISYTGSNCSHQVQQELSGTFAHLCQQVDVTRENLEQEIAAMNKKIEVLDSLQSKAKLLRNKAGWLDSELNMFTHQYLQPSR
The following text describes a protein:
Function:
May contribute to UTP accumulation needed for blast transformation and proliferation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSLPVCPGAGVPGCWEFGRHSSHSLLPPVAPGHSPRRRTTSQCKSEPPLLRTSRRTIYTAGRPPWYNEHGAQSKEAFVIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDAFYKVLTQEQQEQAARNDFNFDHPDAFDFELIISTLGKLKQGKSVKIPTYDFTTHSRHKEWKTLYGANVIIFEGIMAFAHTELLKLLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVLKQYHAFVKPAFDQYIQPTMRLADIVVPRGSGNAVAIDLIVQHVHSQLEERKLRWDMAALASAHQSQPLPRTLSVLKETPQVRVMHTIIRDRETSRDEFIFYSRRLMRLLIEYASSFLPFRCCTVQTPQGHDYQGRMYDGKRITGVSILRAGETMEPALRAVCKDVRIGTILIQTNPSTGEPELHYLRLPKDISEDHVILMDCTVSTGAAAMMAIRVLLDHEVPEEKIFLLSLLMAELGVHSVAYAFPRVQILTTAVDKKVNDMFRIIPGIGNFGDRYFGTDAPADWSEDDDDDDDEDPV
The following text describes a protein:
Function:
Toxic component of a type II toxin-antitoxin (TA) system, first identified by mutations that increase production of persister cells, a fraction of cells that are phenotypic variants not killed by antibiotics, which lead to multidrug tolerance. Persistence may be ultimately due to global remodeling of the persister cell's ribosomes. Phosphorylates Glu-tRNA-ligase (AC P04805, gltX, on 'Ser-239') in vivo. Phosphorylation of GltX prevents it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to persistence and multidrug resistance. Once the level of HipA exceeds a threshold cells become dormant, and the length of dormancy is determined by how much HipA levels exceed the threshold. The hipA7 mutation (a double G22S D291A mutation) leads to increased generation of persister cells (cells that survive antibiotic treatment) probably by entering into a dormant state, as well as cold-sensitivity. Wild-type cells produce persisters at a frequency of 10(-6) to 10(-5) whereas hipA7 cells produce about 100-fold more persisters. hipA7 decreases the affinity for antitoxin HipB, leading to increased HipA levels and persistence; depending on the protein level, can be toxic enough to reduce cell growth or even kill cells. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. Also neutralized by overexpression of gltX. With HipB acts as a corepressor for transcription of the hipBA promoter; binding of HipA-HipB to DNA induces a 70 degree bend. This brings together and dimerizes 2 HipA molecules, which distorts the promoter region, preventing sigma-factor binding; additionally HipA and HipB would physically prevent RNA core polymerase from contacting the -35 promoter box. May play a role in biofilm formation.
Miscellaneous:
MISCELLANEOUS: The hipA7 allele (G22S and D291A) as well as a P86L mutation have been identified in E.coli isolates from human patients with urinary tract infections, showing the mutations may be clinically relevant.
Sequence:
MPKLVTWMNNQRVGELTKLANGAHTFKYAPEWLASRYARPLSLSLPLQRGNITSDAVFNFFDNLLPDSPIVRDRIVKRYHAKSRQPFDLLSEIGRDSVGAVTLIPEDETVTHPIMAWEKLTEARLEEVLTAYKADIPLGMIREENDFRISVAGAQEKTALLRIGNDWCIPKGITPTTHIIKLPIGEIRQPNATLDLSQSVDNEYYCLLLAKELGLNVPDAEIIKAGNVRALAVERFDRRWNAERTVLLRLPQEDMCQTFGLPSSVKYESDGGPGIARIMAFLMGSSEALKDRYDFMKFQVFQWLIGATDGHAKNFSVFIQAGGSYRLTPFYDIISAFPVLGGTGIHISDLKLAMGLNASKGKKTAIDKIYPRHFLATAKVLRFPEVQMHEILSDFARMIPAALDNVKTSLPTDFPENVVTAVESNVLRLHGRLSREYGSK