lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II.
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MHVSNDTTVLESRKEGKSFLELVAKRISEPDLAAELISAAARLVVASASAHGKENTPVTAATYAVAAPSDASLLVKFPGLSLVAPRGKFDVGFSPEALVLSNAKSSVVVPVAAITHVAILDQIPQDTKKRCLMFVVLERNGPAVMNGKQRLEAVIIQTLETEELRAVTSKGEALDGPAAAVLCEALALVKPGFEEFIAPDPDLFRTAKGHLGVSAYVKASPGHLFPLRGGLLFAERPPMFLPLADVLAVEYRRPQSATFDLVLHVRPREGGSGSSSSSSVQQLEFSQVDKAEMGRLQSYFATCKIKLYDPAAPPRLDGGAAAAGAQAAAAAAGGSSGGAYGEDAEGDDDESDEDDEDFDPSELQRLESGRATKRQRTGASGSAGAGPSTSKAAAAAAEDEDEDDEAEADDEDAESDEDEEEEDSYDEDEELADLTDEEDMAAEAVRRAARRGGQAAGAEEEDDDEDDDEDD
The following text describes a protein:
Function:
This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited.
Subcellular Localization:
Cytoplasm.
Sequence:
MRYNSEILRTNEFISVRKIKLLIIEDEIAIRDMVRFSLPDEFELLDAEDTAKAIKQLAAQIPDLILLDWMLPGKSGIEFIEWIKQKEIWQDIPIVLLTAKAEEENKVRGLMSGADDYITKPFSPDELIARIRAILRRGPLISSNQEIKIGDIKINTAKHLVTVKDEHIALSPTEYKMLHFFMKHPNKTYSRDQLITYIWGGNIYIDDRTVDVQVRRLRDKLKKYDHHHLIKTIRGAGYQLSTDDTKNA
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Sequence:
MEKESQPADHWLEPEEPEPVASPGAAAAAAGPIYDVYMDDEEEAYLEGLDVPAAPVVLDADTEEAVAAAVEAERQAAMAADEEMAHALHMQDLVGAEEWELRDLDLEQPLGDYPNSSRAGVGFGARATADNFLERQTGTFESIHEVESGTVFLGNSRIPEPLECLESLPGPSTAGVAASPARQTQTILSQDAAGSSSSQQVPGHAVAATVPSVTPPAGFVPSARRCGALCAIAPRARPIGPFDDPVSVKRRALLADAASSVMFPAMQEGHDNGWYEAIVLDDADKLELAEKQRLLESLQLCLPRSDEPCKPAVAAAGEEEEEEGGFSLPKFCQRWGVSPSDLEPDAPGPSTTKVPPLADNEVPTFDCGICMDTLPILDLFHGLPCKHKFCATCMTIYVEGRIRASELPIPCPDAACKGKENTVLHPEKCKKAIDYGAFGDWGARLTESALPPDRRAYCPNRRCGVILETSGQAEPAMAPCPACKHLLCATCGMEWSPDGAAGEHDCAKGPDAALVRSLAQERRWKQCPSCRMIVERSYGCNRMTCRCGFVFCYQCGRPMNRGQPGVAGLLEPCRCLDAGLAFAFAHHHQAHHIELDVPPPPLLEHEEAAAVEAAVAMNMLPVWDAEPEPRVPADGPPRRLEEDDGIHQPGPQDDPDVEMENFFY
The following text describes a protein:
Function:
Functions as a guanine nucleotide exchange factor (GEF) that promotes the exchange of GDP to GTP, converting inactive GDP-bound small GTPases into their active GTP-bound form. Involved in regulation of adherens junction between cells. Plays a role in cell migration; Has a higher guanine nucleotide exchange factor activity compared to other isoforms.
Subcellular Localization:
Cell membrane. Cytoplasm, cytosol.
Sequence:
MIVFIYSLSFFTVIASFRGTVPYGLSLEIGDTVQILEKCDGWYRGFALKNPNIKGIFPSTYVHLKNACVKNKGQFEMVIPTEDSVITEMTSTLRDWGTMWKQLYVRNEGDLFHRLWHIMNEILDLRRQVLVGHLTHDRMKDVKRHITARLDWGNEQLGLDLVPRKEYAMVDPEDISITELYRLMEHRHRKKDTPVQASSHHLFVQMKSLMCSNLGEELEVIFSLFDSKENRPISERFFLRLNRNGLPKAPDKPERHCSLFVDLGSSELRKDIYITVHIIRIGRMGAGEKKNACSVQYRRPFGCAVLSIADLLTGETKDDLILKVYMCNTESEWYQIHENIIKKLNARYNLTGSNAGLAVSLQLLHGDIEQIRREYSSVFSHGVSITRKLGFSNIIMPGEMRNDLYITIERGEFEKGGKSVARNVEVTMFIVDSSGQTLKDFISFGSGEPPASEYHSFVLYHNNSPRWSELLKLPIPVDKFRGAHIRFEFRHCSTKEKGEKKLFGFSFVPLMQEDGRTLPDGTHELIVHKCEENTNLQDTTRYLKLPFSKGIFLGNNNQAMKATKESFCITSFLCSTKLTQNGDMLDLLKWRTHPDKITGCLSKLKEIDGSEIVKFLQDTLDTLFGILDENSQKYGSKVFDSLVHIINLLQDSKFHHFKPVMDTYIESHFAGALAYRDLIKVLKWYVDRITEAERQEHIQEVLKAQEYIFKYIVQSRRLFSLATGGQNEEEFRCCIQELLMSVRFFLSQESKGSGALSQSQAVFLSSFPAVYSELLKLFDVREVANLVQDTLGSLPTILHVDDSLQAIKLQCIGKTVESQLYTNPDSRYILLPVVLHHLHIHLQEQKDLIMCARILSNVFCLIKKNSSEKSVLEEIDVIVASLLDILLRTILEITSRPQPSSSAMRFQFQDVTGRKTCLVALLKMHLTRHGTSCLPRQEDHLSPGDFLLQIFTVFRILIRPEMFPKDWTVMRLVANNVIITTVLYLSDALRKNFLNENFDYKIWDSYFYLAVIFINQLCLQLEMFTPSKKKKVLEKYGDMRVTMGCEIFSMWQNLGEHKLHFIPALIGPFLEVTLIPQPDLRNVMIPIFHDMMDWEQRRSGNFKQVEAKLIDKLDSLMSEGKGDETYRELFNSIIPLFGPYPSLLKKIERETWRESGVSLIATVTRLMERLLDYRDCMKMGEVDGKKIGCTVSLLNFYKTELNKEEMYIRYIHKLYDLHLKAQNFTEAAYTLLLYDELLEWSDRPLREFLTYPMQTEWQRKEHLHLTIIQNFDRGKCWENGIILCRKIAEQYESYYDYRNLSKMRMMEASLYDKIMDQQRLEPEFFRVGFYGKKFPFFLRNKEFVCRGHDYERLEAFQQRMLNEFPHAIAMQHANQPDETIFQAEAQYLQIYAVTPIPESQEVLQREGVPDNIKSFYKVNHIWKFRYDRPFHKGTKDKENEFKSLWVERTSLYLVQSLPGISRWFEVEKREVVEMSPLENAIEVLENKNQQLKTLISQCQTRQMQNINPLTMCLNGVIDAAVNGGVSRYQEAFFVKEYILSHPEDGEKIARLRELMLEQAQILEFGLAVHEKFVPQDMRPLHKKLVDQFFVMKSSLGIQEFSACMQASPVHFPNGSPRVCRNSAPASVSPDGTRVIPRRSPLSYPAVNRYSSSSLSSQASAEVSNITGQSESSDEVFNMQPSPSTSSLSSTHSASPNVTSSAPSSARASPLLSDKHKHSRENSCLSPRERPCSAIYPTPVEPSQRMLFNHIGDGALPRSDPNLSAPEKAVNPTPSSWSLDSGKEAKNMSDSGKLISPPVPPRPTQTASPARHTASVSPSPAGRSPLKGSVQSFTPSPVEYHSPGLISNSPVLSGSYSSGISSLSRCSTSETSGFENQVNEQSAPLPVPVPVPVPSYGGEEPVRKESKTPPPYSVYERTLRRPVPLPHSLSIPVTSEPPALPPKPLAARSSHLENGARRTDPGPRPRPLPRKVSQL
The following text describes a protein:
Function:
Cytochrome P450 monooxygenase involved in the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. During pathogen-host interaction, ABA plays a dual role in disease severity by increasing plant susceptibility and accelerating pathogenesis in the fungus itself. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase ABA3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (By similarity). The cytochrome P450 monooxygenase ABA1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (By similarity). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase ABA2 and the short-chain dehydrogenase/reductase ABA4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (By similarity). ABA2 is responsible for the hydroxylation of carbon atom C-1' and ABA4 might be involved in the oxidation of the C-4' carbon atom (By similarity).
Sequence:
MYGTNLLETMGKPTAGHLGMAVTFTPKAYRELHEKYAAPFTNRALLQQQDILRVHVDKLITALRAKARNKESVNMGEWSPHTQPDTYTTFDIIGDICFAEPFGCLDGGESNEWARAIINIFKAATWDQAIRRVAGTGTLLHKALVKIIIPAEAAQWRTIHFSNSKAKTLARLADPDRQHPDLIKHILDSEDSRAALSPTEIILNMVLFISAGSETTANTMTGWTYFMLRHPEARARATAEVRAAFASPRDIKWETVRALPYLNATLEEALRLFSPAPSNQPRVVPACGAVVAGCPLPSGTTVSVAPWAAVFSARNFADPERFAPERWLDEGGADPRYAADRRGASQPFSTGPRGCMGKNLAYFELRLVLAHLLWHFDLEPTDSAAGRECMRRWEQTDMDTYQTWMKPDLWVDLKEAQR
The following text describes a protein:
Function:
Has a role in the proper organization of the interphase microtubule cytoskeleton. Required for equatorial microtubule organizing center (eMTOC) disassembly into satellites, contributing to the dynamic redistribution of MTOC components for organization of interphase microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton. Nucleus. Note=Associates with the microtubule bundles.
Sequence:
MARTAFHDEFVDYYTILGAESTSSYVEIRQQYLKLVLRYHPDRNPGREAEVLPQFQLIQKAHEVLKDPKLRELFDQRRLLEAGRPDGVLRFRPKKSGPKNDISTKVASKVSVTMATKFAEKKKKQDRENVDSKDNNITNFSLHRSFSASGKMEKNNSFKEVSTSKSYISSGYLHPKTSPIFKKNGYATENVVDPISSSPRFKGPNYNKFNAKLYLESLREKRRTYTPLSEISNGLNSNGVENSSITKSSPRSSSSSNNERFKDTSEESIIFTSPNTPEHPSVYQTDITPEIKLEHSDNNSPSKPEIPFRHPTSKPLPPKPLSRSKSSSLSRNQTRSQLNDLSAENDSTSNSTEYDDQLQSILRSLAIEGDDDEVAKVLPKPPSVPTIQAPIPPEAPRNLTNASVDSYLNSFEMYQRRWSSYSIIYTQYAFQWQIFKNKCFQLDLMNTPGQSRLIDNWKEGSQAIQLFYAYEQMHLRALEELQSLKESLFASFGI
The following text describes a protein:
Function:
Transcriptional regulator which is involved in the sex determination and X chromosome dosage compensation pathways. Directly binds to five 5'-A(G/C)(G/T)(T/G)C(A/G)-3' sites in the promoter of sex-determining factor xol-1 to negatively regulate its expression and promote hermaphrodite development. Together with fox-1 is involved in making the distinction between one and two X-chromosomes. Plays a role in the fox-1-mediated repression of the functionally active isoform (isoform b) of the sex-determining factor xol-1 gene to promote hermaphrodite development. Plays a role in the association of the dosage compensation complex proteins dpy-27 and sdc-3 with the hermaphrodite X chromosomes.
Subcellular Localization:
Nucleus.
Sequence:
MSFETKPNYLLLTNPDTPLSVCTSPYYSPSGKTASIPSSEASKPEGTNGQWSHLPTGATYVTDEFSSEFQIQNGSTAAQSGNANNYADPLSHRRYFNNVNGYNHHQFYDTASQASVSSPATSVTSSLSPPDSLSNGHTTQRHHIGKAISFCKVCGDKASGYHYGVTSCEGCKGFFRRSIQRKIDYRCLKQQVCEIKRESRNRCQYCRFKKCLDSGMSKDSVRQMKFRNAMRDDKSPDSVFVPEISTLERQEEVDAVYEAVLRAHTTFSFYTDIKIRSIVARPFNVRINEDSKMNRLNAWQIYAHEIDVDIKEVVNFVKEIPKFNFINGNDKAVLLRKNAFPLYLLRIVRGMSNRGLMLRDGRLIDFKSLQLLYGSLADEMLAFANHIITIGCTDGDIALFIVLILCQPLTTEQQFSTNFKSQLQLLEMFDFYKKVLFQKMTCRIDGCDTYKQLMKCIHELNRLNELHKQQLNILRENLSFLNLPPLVVEMFQLSTLPLPVNHNNQENQYTPAPEHQSPQPQQPTPNQQQTPVHC
The following text describes a protein:
Function:
Mitochondrial and nuclear transcriptional activator required for respiratory growth.
Subcellular Localization:
Cytoplasm. Nucleus. Mitochondrion.
Sequence:
MKDLNPEMGKFATTKGPPQDNRGMVDIATLPNFPANRSGTPREEMYLAPNKMETPRILNMNMVPDYLQKENFSPDFSSATVSAKSSPVNVTHDESLPLGTIESNSTKDSKYAVQRQQQQVVDFIENNMQLLSSETLNFRSDIMKTLELPIPKRRDIKGNHLSKLLFAKSPLTINTYCQFYDRRTKRICNQEMIWKDKNSREKHGSRKYQRHLSKVHDVQLTPNNFTEFFDHNSPLFQECYDYQSRLMRDLLVEPDAKFKEKKKKKKGDVNGNHPETGSSLINHQVQQQNVRELQSKIAMNDLIEILIDLNIPFSVLDYQPMRNWLIKYSIISTDTLPDEVYFKTDPGVNELEHNSSNLNNSNSGTPHNHNQNQHTN
The following text describes a protein:
Function:
Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are released from the procapsid (Probable).
Sequence:
MSLKEQLGEELYGQVLAKLGEGAKLVDISDGSFIPKEKFDAVNSEKKSLEQQLTDRDQQLQELSTKATGHDELSAKIADLQKANEEAKQAFEAEKQQLKYEHALETALRDSGAKNPKAVKALLDTESIKLDGDKLLGFEDQIKALKEQEDYLFKGTEPNGGVQGTPPPGKGADLGGLPTKKNPFKQGPDFNLTEQGILFRENPELAKKLQAEAQ
The following text describes a protein:
Function:
Component of cullin-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. In association with ddb-1 directs ubiquitination of cdt-1 during S phase and is required for restraining DNA rereplication. Probably is involved in ubiquitination of cki-1.
Sequence:
MTSGAPPTISTEKSRSKQLRKSSKRTASTVEGTEAKQMRGDTENRSDGEMDDVSTSSEIRHGNGFIENFRSQTGNSSRTTATNERIKKKLVIKNFKANANQNDVAMGDTNIDSTDGSVGRDWAVLSDNVFAILEDRKTVTTLEGLFSKVRSVCDKNQSKVLYDRLVAIVVQFAKSLKESLNAVEQVPLAEDNCEQYLEKFGQIWQAYPVKINLIRNIFLHLDRIALGATDTEILPLWECFMQIFQKTFFPNIFKEFKATKLFNALYMAMQKIMQRYPVDSPLRSLVDMLQTVHVSEEFAKFLISQLREHYNNERIDKVPKMNCNDYMEYCEDQINRYSQLVKVNFDEPSALKDVQATVTNCLIQQAIPEILTHDFDDLIDSDNISDIGRMFNLCRQCVGGEDEVRTQFSKYLKKRGEKLIATCPDEDLVSELLAFKKKVDFIMTGSFKSANDPVKMRQCLSDAFESFVNKQVDRSAELISKHFHTLLHSSNKNVSDDTTLDQMVDEAIVLFRYLRGKDVFEAYYKRGLAKRLFLERSASVDAEKMVLCKLKTECGSAFTYKLEGMFKDMDASENYGRLFNQYLEHMNKEKANFTARVITPEYWPTYDTYEINIPKEMRDTLTDYQDFYRVQHGNRNVKWHHGLASAVISASFRPGCKKELIATMYQTVILLLFNKCETWTVAEIVEHTKILEIEVVKNVLALLGGRDKPKVLQRVEGGGSEKKEGTVENLKNEKFVVNSKFTEKRCRVRIAQVNIKTAVEETKEVKEEVNSDRQYKIDAAVVRIMKARKQLNHQTLMTELLQQLRFPVSTADIKKRLESLIEREYISRDPEEASSYNYVA
The following text describes a protein:
Function:
Part of a checkpoint which monitors spindle integrity and prevents premature exit from mitosis. This cell-cycle arrest depends upon inhibition of the G-protein TEM1 by the BFA1/BUB2 complex.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle pole.
Sequence:
MTPTNQSSGTTNASVEVLSEDGPMPINVMMQEGVKALTKILSNQLQDRQAFQNAPHAMQFVIRNGGKALSNARLEELKDALPKMDSLSLEDELAKIDGQSAYHIDSAEEKETFESKIGQIASRNSADFIIEEDLQNILDDDLKDSELNLDGEEAEIIFDYESQELDTPDGIGEKISQMIESVLPGGFGSEEQGGLRTVTNVEDLDVAEEVTDIDHDTVDAARLHGDGQHSISSRKHSRSKNSKKNGHVRRHDFYDESRDHKSCCPHHHYENLSKLRNYYYHDFEYISRTENRVPDFSVLVNESSPMCLFCEYYMVFGEPPRNMIKWYNRTFGYNRMPNPPRDEQDSRKRNR
The following text describes a protein:
Function:
No E.coli strains have been observed to have an arylsulfatase activity. A 'latent' activity has been observed by heterologous expression of a genomic region linked to tynA, but it does not map near aslA.
Subcellular Localization:
Periplasm.
Sequence:
MEFSFSPKRLVVAVAAALPLMASAADTPSTATARKGFAGYDHPNQYLVKPATTIADNMMPVMQHPAQDKETQQKLAELEKKTGKKPNVVVFLLDDVGWMDVGFNGGGVAVGNPTPDIDAVASQGLILTSAYSQPSSSPTRATILTGQYSIHHGILMPPMYGQPGGLQGLTTLPQLLHDQGYVTQAIGKWHMGENKESQPQNVGFDDFRGFNSVSDMYTEWRDVHVNPEVALSPDRSEYIKQLPFSKDDVHAVRGGEQQAIADITPKYMEDLDQRWMDYGVKFLDKMAKSDKPFFLYYGTRGCHFDNYPNAKYAGSSPARTSYGDCMVEMNDVFANLYKTLEKNGQLDNTLIVFTSDNGPEAEVPPHGRTPFRGAKGSTWEGGVRVPTFVYWKGMIQPRKSDGIVDLADLFPTALDLAGHPGAKVANLVPKTTFIDGVDQTSFFLGTNGQSNRKAEHYFLNGKLAAVRMDEFKYHVLIQQPYAYTQSGYQGGFTGTVMQTAGSSVFNLYTDPQESDSIGVRHIPMGVPLQTEMHAYMEILKKYPPRAQIKSD
The following text describes a protein:
Function:
Cooperates with PPP2CA to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Has a crucial role in protecting REC8 at centromeres from cleavage by separase. During meiosis, protects centromeric cohesion complexes until metaphase II/anaphase II transition, preventing premature release of meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is thus essential for an accurate gametogenesis. May act by targeting PPP2CA to centromeres, thus leading to cohesin dephosphorylation (By similarity). Essential for recruiting KIF2C to the inner centromere and for correcting defective kinetochore attachments. Involved in centromeric enrichment of AUKRB in prometaphase.
Miscellaneous:
MISCELLANEOUS: Shugoshin is Japanese for guardian spirit (as it is known to be a protector of centromeric cohesin).
Subcellular Localization:
Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore. Note=During meiosis I, accumulates at centromeres during diplotene, and colocalizes differentially with the cohesin subunits RAD21 and REC8 at metaphase I centromeres (By similarity). SGO2 and RAD21 change their relative distributions during telophase I when sister-kinetochore association is lost (By similarity). During meiosis II, it shows a striking tension-dependent redistribution within centromeres throughout chromosome congression during prometaphase II, as it does during mitosis (By similarity). In Hela cells, localizes at centromeres throughout prophase until metaphase and disappears at anaphase. Centromeric localization requires the presence of BUB1 and AUKRB.
Sequence:
MECPVMETGSLFTSGIKRHLKDKRISKTTKLNVSLASKIKTKILNNSSIFKISLKHNNRALAQALSREKENSRRITTEKMLLQKEVEKLNFENTFLRLKLNNLNKKLIDIEALMNNNLITAIEMSSLSEFHQSSFLLSASKKKRISKQCKLMRLPFARVPLTSNDDEDEDKEKMQCDNNIKSKTLPDIPSSGSTTQPLSTQDNSEVLFLKENNQNVYGLDDSEHISSIVDVPPRESHSHSDQSSKTSLMSEMRNAQSIGRRWEKPSPSNVTERKKRGSSWESNNLSADTPCATVLDKQHISSPELNCNNEINGHTNETNTEMQRNKQDLPGLSSESAREPNAECMNQIEDNDDFQLQKTVYDADMDLTASEVSKIVTVSTGIKKKSNKKTNEHGMKTFRKVKDSSSEKKRERSKRQFKNSSDVDIGEKIENRTERSDVLDGKRGAEDPGFIFNNEQLAQMNEQLAQVNELKKMTLQTGFEQGDRENVLCNKKEKRITNEQEETYSLSQSSGKFHQESKFDKGQNSLTCNKSKASRQTFVIHKLEKDNLLPNQKDKVTIYENLDVTNEFHTANLSTKDNGNLCDYGTHNILDLKKYVTDIQPSEQNESNINKLRKKVNRKTEIISGMNHMYEDNDKDVVHGLKKGNFFFKTQEDKEPISENIEVSKELQIPALSTRDNENQCDYRTQNVLGLQKQITNMYPVQQNESKVNKKLRQKVNRKTEIISEVNHLDNDKSIEYTVKSHSLFLTQKDKEIIPGNLEDPSEFETPALSTKDSGNLYDSEIQNVLGVKHGHDMQPACQNDSKIGKKPRLNVCQKSEIIPETNQIYENDNKGVHDLEKDNFFSLTPKDKETISENLQVTNEFQTVDLLIKDNGNLCDYDTQNILELKKYVTDRKSAEQNESKINKLRNKVNWKTEIISEMNQIYEDNDKDAHVQESYTKDLDFKVNKSKQKLECQDIINKHYMEVNSNEKESCDQILDSYKVVKKRKKESSCKAKNILTKAKNKLASQLTESSQTSISLESDLKHITSEADSDPGNPVELCKTQKQSTTTLNKKDLPFVEEIKEGECQVKKVNKMTSKSKKRKTSIDPSPESHEVMERILDSVQGKSTVSEQADKENNLENEKMVKNKPDFYTKAFRSLSEIHSPNIQDSSFDSVREGLVPLSVSSGKNVIIKENFALECSPAFQVSDDEHEKMNKMKFKVNRRTQKSGIGDRPLQDLSNTSFVSNNTAESENKSEDLSSERTSRRRRCTPFYFKEPSLRDKMRR
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MQQTYQIFNNYITFRSDEILNLLQKDDISKSEALQQLISAELDGEQHTDMLMNVISYALPSTDHTVKRLFLMYLSCIKRVDEQGKLLSELVLVINSLQNDLNYPNEYIRALTLKFILTISEKELIQPLTHAVINNINSKSPLVRKHCFSAICHIYRLYPDLVPNASKLICTAVNEESITSVKCSALRALMYVDLSAAVRYVIKKSEQISTYKEDIQLELLHLIKSVSRSTPESSTTYLSICASLIQSPSTAVSLEASLCMLVVSSSPSVVKAAIRSLIDIVVKSSDVNVKISILQRIEQQIHKTPRLMNELEIDMLRGFQCNSSYVRSKVAQIVVKCVTSKTINEVINTLRKELQREEDEQYQLAILQAIKECNNKFTCESIIPVLLDIMQTTNSISVSKEILLFVRNILLNSNNTNNKNSFILQPLYDIIHSIKTPQLLVEIIWILSRFSYTKEEVLTSFNKLYELMFNEEGKSILLEEDKSHILSGTYISSIVKLVLKGNTLFEPTKQHEITAKGLQCLLKLLKTQKGSDLIGKIRQGITCITTKNEKLTEAALAEPEIKKEVIVMKKDIIQVDDEVSFGMFNEESEIPTIAENEEKNLMTFRNIIQLSGYSDPLYVEASLELSQFDIAIDTLIVNQSQSTLQNIMIQLVPRSDGLEVIGQQQPLTLGAGEFTRVTIPVCVTGTSSGLIAGYINYDRVGREITTGSSDNHMVLNNISVEALDSIKPADISQDVFQKKWMGYEWENKIIVETDITDLVQFIEHLCKETHMNCVTPKSLFCSEIGFLSANLYATTVFGDDALANISIEINNGKISGCIRIRAKSQGVALSLGDKILMVQKQQN
The following text describes a protein:
Function:
Acts as a critical modulator of FOXO3-induced autophagy via increased cellular ROS.
Subcellular Localization:
Cytoplasm. Peroxisome. Mitochondrion. Note=May localize to aggresomes.
Sequence:
MRSRLLLSVAHLPTIRETTEEMLLGGPGQEPPPSPSLDDYVRSISRLAQPTSVLDKATAQGQPRPPHRPAQACRKGRPAVSLRDITARFSGQQPTLPMADTVDPLDWLFGESQEKQPSQRDLPRRTGPSAGLWGPHRQMDSSKPMGAPRGRLCEARMPGHSLARPPQDGQQSSDLRSWTFGQSAQAMASRHRPRPSSVLRTLYSHLPVIHEL
The following text describes a protein:
Function:
Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II.
Subcellular Localization:
Cell membrane. Early endosome.
Sequence:
MVLLMSIIAGTEKQSSFNQTNRNTQTEIPFQTIHVSKLSNPASLVEYNGLKFLIFDSPTDDNVDNYISELKRYNVTDVVRCCHPSYDKKKLINNKIAIHELVYQDEGCPSSRIISDFMRIVHAIFPNDQNPLGITLGVHCLSGIGRAPTLVAIALIELGMENTEAMKLVRRKRSGAINVLQSRFIQSYVPQEKRMCNIA
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 mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. 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 deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal zinc finger binds to poly(A) RNA; 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 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:
MNINLDTAKDTLCKNILIYGYCKYENKGCAFSHNRQQPAQQQQATNTSNNSTSVITPNSANSTASSADLSSKKKFNLNTPSFQPSVSNLSNKFSTLSPKLKEIPVFKPENGVSEPDTVDSPTTQRPFTSKRFNVSTPSFTPTNFDFANNSNADGNRGGASTPIGISSAPLVQNQQQQQQQQQQQQKQPLAVPSPLASGAQPPTMQHRILSMGVSQSSPSTNPYFANNLDMSAPTPGSETPGPVLPGSAGAAAAAANQPMYPLQYHLYAPAPPPRLTIPLQPYETNSQAMFIPNDLREYLHKKNEASLQSLSHSNLPEHVNQYHSLVPIDKSYEPVSKLWLGKNSLIFKCLDNIDGNLYVMRKIEPCNEIINEKPFKTIKRWKSIKNANIVGLQDAFTTMAFNGNQSGNTSLCIIYDYYPNSISLLEHHKKGLRVEPVNEALLWNYLIQLINAIMAIHEKGLSASSTIDLSKIIVTNKNRIKLSSVGISDILEFKDDETNQDIKIRQLQDIQKVGKVLMELAILLLPVNMRQSNNIYNSLKASTNLSEEIINNLQELNDLDTASGEFDLNEFSQRLTPKMFNIIDSLQNSSDFIEGQLTSELENARLFRLMTKLNYLIHDNSNSENDKIIKLFLNYVYNCYDSNNKKVINLNKVLINLNKLDCGIDEKILLVNNDECIIISYKELKEIIDTKFRLMRE
The following text describes a protein:
Function:
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Subcellular Localization:
Cytoplasm.
Sequence:
MKTFRGTYTVMITPFTAAGEVDVAALRAFVDWQIAEGIHGLIPLGSTGEFLSLDDDEKALVAEVVIGQAAGRVPVLIGTGAEDTREVVRLSRRAEKLGADGVMIIPPFYSTPTDDELVHHYKTVADAIALPIMVYNNPATANVDLKPQLVARIAEIDNCLYIKESTLEVTRVRDIIRLCGDRMTVFGGILGFESFVEGAQGWVAVASNVVPSEMARIFSLVADEGAIKEARELYLKYLPVIEFVGGQAYVAGSKALLGHMGLAVGGPRPPRLPLPAAQDAAALALVKSFGLAWRGASIAAA
The following text describes a protein:
Function:
Involved in nucleotide metabolism via production of dUMP, the immediate precursor of thymidine nucleotides, and decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Sequence:
MEVENVPSKLQKLHHHDNSDSDGISIPFFHVKKLSEKANLPSRASPLSAGYDLSSAVETKIPARGKALVPTDLSIAIPKGTYARIAPRSGLAWKHSIDVGAGVIDADYRGPIGAILFNHSDVDFEVKVGDRIAQMIIERIVTPDVVEVDDLDDTVRGAGGFGSTGV
The following text describes a protein:
Function:
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Sequence:
MGLPWYRVHTVVLNDPGRLLSVHIMHTALVSGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITNSWGGWSITGGTITNPGLWSYEGVAGAHIVFSGLCFLAAIWHWVYWDLEIFCDERTGKPSLDLPKIFGIHLFLSGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQPVNPAWGVEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVGAGLAENQSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPIFRDKEGRELFVRRMPTFFETFPVVLVDGDGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYSDPATVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHASFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQVEFGTFQKLGDPTTKRQVV
The following text describes a protein:
Function:
Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Subcellular Localization:
Cell membrane.
Sequence:
MIFLYQILTIFLLIFVVPISFLFPSARLFFRKRSADKKKILSKSLDLSGKYTVWLHAASVGELDQCKALALEFRKNDPSAFLIQSVFSDSVRDSQLEAFPADETFHLPIDLPFSYDWIFSRFHPKVLVLMAWDTWPNLVISANRFNTKVVLGSAVIGNRKKGIMGKLTKSVFKHLDGIFPSHESFYDVFRSLVPDQIPVKVLGDTRFDSVLKKIEDNAKIFKKPKNYPYSKIILFASTYEPCENLIVSLYELIRSKNPALLDNFAFWIFPHKTSPDRIISIEHKLQDANIIYQTWTSTPFENLTAQTIVFDVLGVLAFAYQAADFAYVGGALHNRVHNILEPATFGLPLMTGPKIYNSPEAMILEKSGSLFIVSEAEDIFQILNLSENDLETIRKQNWEFVQSGRGAAKRLYEEIRKL