lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.
Subcellular Localization:
Preautophagosomal structure membrane; Multi-pass membrane protein.
Sequence:
MDESLLSSNDDHLVGAEEEDELLWNELKDDHRAPPFGSTSSQDAALGSHTGSSSHGGAPLPSLRVNAHLPAISTLFREVLDTAKAALPGAQRHGNAQNAVSASRRVSPVPDRFGNMPSLDAFLITLYNYYYHKGFWSIVVVELVGLATGLFSVVLSSFLLGCVQWGPLLECHRHPETGGCAQEMEHYITCRADNNGLLGLVGAFYFAMFLVYWVSRAFQLVGTLRDTREMEVFYKERLHIDERQVQTIAWDEVVTRVLDLVNGANAPVNMRQLSSYKLQIDPALLSSPHDFARRIMRRDNYLIAFMNHALFQSKNLLPTSLQFLSTSHIMCSRNLEANLNICLLDQMFDTDLNLAPTVIHNVEMLKKRFVIAGVLNFVLAPFILLYRLSRFFFLAAQEWQTNHVHYLGTRRWSSYAIWRFREYNELPHVLDARMARSYSLADRYLGMFPAGSLAIIAGGVSFCASSLMAVLVLVSLLEESILLETTLMGHELLWYLTVATGVFALSRSFTTSTSPFLINGDCEEAMMQVSAETHYFPKEWRGQCHSFEVRDAFTVLFPYKAVLFAEECVSVLLAPYILCVSLPRLAREILLFLRSHSLVHPSTGAVCRFAEFDFKEYGNDAKMESSFINFKQNHPKWVGAREGEALMQRLGKLKEEEMEKSMRMGDTMMYSSHMSMSQQLMQSQAIQNAMGGGRMSGYMPQDNEFYWLEKLHQQGRLGDLDLEMKGNPADSISISSLGSP
The following text describes a protein:
Function:
Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling.
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum.
Sequence:
MTEEVIVIAKWDYTAQQDQELDIRKNERLWLLDDSKTWWRVRNAANRTGYVPSNYVERKNSLKKGSLVKNLKDTLGLGKTRRKPSARDASPTPSTDAEYPANGSGADRIYDLNIPAFVKFAYVAEREDELSLVKGSRVTVMEKCSDGWWRGSFNGQIGWFPSNYVLEEADEAAAEAPSFLSLRRGTALSNGQGARVLHVVQTLYPFSSVTEEELSFEKGETMEVIEKPENDPEWWKCKNARGQVGLVPKNYVVVLSDGPALHPAHTPQISYTGPSASGRFAGREWYYGNVTRHQAECALNERGVEGDFLIRDSESSPSDFSVSLKASGRNKHFKVQLVDSVYCIGQRRFHSMDELVEHYKKAPIFTSEHGEKLYLVRALQ
The following text describes a protein:
Function:
Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates. Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity. May also hydrolyze long chain retinyl esters such as retinyl palmitate. May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border.
Subcellular Localization:
Apical cell membrane; Single-pass type I membrane protein.
Sequence:
MADIPQAEVVEVFCNKPTARSDGKTDGLLEEQGKLKALGSFQFSCGHVTSPETPSSSVHALRPADIKVVTAIGSLQTPLGSSIYHEDLLQSTGRSLPEVTVEILAALISSFNPSVLHQSPLPGTMGAASDGQTTSLLDQAGEIVKLMKENQMMDFQNDWKLITVFFSAENPCSSCASTQPKNCILDNLEKLQEVLDFLYKEVPKAFVNLVDSTEMTTSFLMCHDPQNASNSTGNQCNCIHKHSMLNYNILRWSYQDAWEKLLKSKRYDQKDNFTVVLQPSLQETNLLLSLSRDGFFSTSKTQVETLEEDYTFMALSLWKNMLEPVGQKKPYDFTELHQVQCPSQENPYLFTYRNSNYSLFQEISNTKETLQERSYGTNVPCFNQGPSDTVPDSVHKLRPADIRVIAALGDSITAGNGAASNPHDVLDVLTQYRGISWSVGGNENISTVTTLANILREFNPSLIGYSTGTGTQTTENAALNQAVAGAQAEDVPAQVRRLVDRMMNDSRINMQSDWKLITLFIGGNDLCKFCEDPIRYSPENYTYNIQVALDMLHKEVPRAFVNLVTILSITSLRELYAEKNVSCPRLLMRILCPCVLDYDENSSEYKQLIYFNKRYQERTRELVESGRYDTREDFTVVVQPFLTHISMPKTQEGFPDNSYFAPDCFHFSQKSHSQAARGLWNNMVEPVGKKTDDQQMENEIVLKCPSEAEPFLRTYKNSNYTYPNQTPNYGSQLLCEDRSPSSPSPTSVHSLKPADVNIIAALGDSLTAGTGIASYSLMDLATQFRGLSWSIGGDDSLENVTTLPNIFREFNAKIEGYSTGTGSENDPNAFLNQAVPGAQAEHLPAQARALLKLMKTDSRIDFSADWKIITVHIGGNDLCNYCKDPDHYSAVNFTSRIQETLDILHEQVPRALVSLVGVMDILHMRQIFVDTEVQCPTYMSDYLCSCVLTGEENSENLTMVREATKAYQLGIQRLVESGRYDTHDNFTVVIQTSFQNPKIPLDQDGHPDISYFAPDCFHPSQKGHSQLAKALWNAMLQPVGQKSDSFDFTADIVLSCPTQNNSFLSTNKNSNNANPPVLPTSEPTENWGSDLSCSEKTPSSRVPTSVHELQPSDIKVIGALGDSLTTAAGACTTDPQVDWRGCSWSIGGDGTLETQTTLPNILKKFSPNLFGFSTGSSKEAAGFNVAERGATSGNMPTQARELVELMRSSSKINFKEDWKLITIFIGGNDLCQYCLDKEAYSVQNYVKHLQDTLDIFYTELPRVFINMVEILEISGLRQVAASSSECVLTEENLCPCFLNPKENSSDLQEIKRVNRDFQAEALQLVNSGRYEQREDFAVVVQPFFRNTILPLDSNGKPDLSFFAADCFHFSEKGYAEMAVALWNNMMEPVGEKQTYNNFTYDRSKLKCPNSEKPFLSTLRNSGFRNSALNLEKTEPSVPYWAVIVAAVAGVLVGSLFLWAMSGRRARRHRCEVDAEKNMKTTSL
The following text describes a protein:
Function:
Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has exodeubiquitinase activity and has a preference for long polyubiquitin chains. May play a regulatory role at the level of protein turnover.
Sequence:
MEQPQTENPAPSKATSAETVESENHEALSGPEKHPQDKDGADADGAAGEQEPGDQTLPPAQDGENLECPPPEASSSPPGPACGTSPKVETAEVCSRPQELPQSPRIQQPELDFYCVKWIPWKGERTPIITQSTNGPCPLLAIMNILFLQWKVKLPPQKEVITSDELLTHLGNCLLSIKPQEKSEGLQLNFQQNVDDAMTVLPKLATGLDVNVRFTGVSDFEYTPECSIFDLLGIPLYHGWLVDPQSPEAVSAVGKLSYNQLVEKIITCKHSSDSNLVTEGLVAEQFLETTAAQLTYHGLCELTAAATEDELSVFFRNNHFSTMTKHKSHLYLLVTDQGFLQEEQVVWESLHNVDGDSCFCDSDFHLSHSLGKSHGAEGGGGSPEKQLQVDQDYLIALSLQQQQQPQGTLGLSDLELAQQLQQEEYQQQQAVQPVRTRAPSPQGRGATSGRPAGERRQRSKTESDCVLL
The following text describes a protein:
Function:
Required for the synthesis of amylose. Destroyed as it is released from the starch granules during the night. The circadian expression is controlled by CCA1 and LHY transcription factors.
Subcellular Localization:
Plastid, chloroplast. Note=Exclusively bound to starch granules and found in the soluble fraction only if PTST is absent.
Sequence:
MATVTASSNFVSRTSLFNNHGASSCSDVAQITLKGQSLTHCGLRSFNMVDNLQRRSQAKPVSAKSSKRSSKVKTAGKIVCEKGMSVIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYDQYKDAWDTCVVVQIKVGDKVENVRFFHCYKRGVDRVFVDHPIFLAKVVGKTGSKIYGPITGVDYNDNQLRFSLLCQAALEAPQVLNLNSSKYFSGPYGEDVVFVANDWHTALLPCYLKSMYQSRGVYMNAKVVFCIHNIAYQGRFAFDDYSLLNLPISFKSSFDFMDGYEKPVKGRKINWMKAAILEAHRVLTVSPYYAQELISGVDRGVELHKYLRMKTVSGIINGMDVQEWNPSTDKYIDIKYDITTVTDAKPLIKEALQAAVGLPVDRDVPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTGKKKMEAQILELEEKFPGKAVGVAKFNVPLAHMITAGADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGYTGFHIGRFNVKCEVVDPDDVIATAKAVTRAVAVYGTSAMQEMVKNCMDQDFSWKGPARLWEKVLLSLNVAGSEAGTEGEEIAPLAKENVATP
The following text describes a protein:
Function:
Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis (By similarity). Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro-inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP (By similarity). Seems to play a role in establishing neuronal contact sites and axonal maintenance (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type III membrane protein; Cytoplasmic side.
Sequence:
MPSTDLLTLKAFEPYLEILEVYSTKAKNYVNGHCTKYEPWQLIAWSVVWTLLIVWGYEFVFQPESLWSRFKKKCFKLTRKMPIIGRKIQDKLNKTKDDISKNMSFLKVDKEYVKALPSQGLSSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTELLVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEKGIKTSEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLTVFMEKAGYPLEHPFDFRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVDTDWQGGIYASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIALGSRDFDIYRLSNLMTAKGWNLNQLQFPPSIHFCITLLHARKRVAIQFLKDIRESVTQIMKNPKAKTTGMGAIYGMAQTTVDRNMVAELSSVFLDSLYSTDTVTQGSQMNGSPKPH
The following text describes a protein:
Function:
Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. May have a role in synapse differentiation and growth.
Sequence:
MPPLKISKCMSDVAQARIDNLFLTKLPSETSHNTQHTCRSYVSKVLNNLNELRRHNRFCDVEIIAEDKIFQAHRAVLAASSPYFQAMFTGGLCEKDQQSVELHGITSYVFEILLNFIYSGEVNITQNNVQELMVAADMVGLSEIVLGCTEFLIKELHPLNAIGIYRFADDHNWTELKTAAVQYIENNFPKVCKEDEVYDLHKDTIIKFLSSENLKIDSEFQVFQAALRWINHDILGRRQYVFDILKNVRLPLLPLGLLERAITQCNDSSLRVALKSIHADLLNRKGCLVPLNVTPRKCAKKDIYVIGGSKRELHSVWDRGLEMNYVSVEKFNTFSREWHKVPDMTVNRLVPGVASLNGHIYVVGGEEGSSILSSCERFEPQSNQWTQVASMVVSRCEFGLCALDGYLYAMGGWVDTDISGSIERYDPKIDEWRLVGSLPEPRFSMGLVSYEGLIYMVGGCSLNQRNLQDLMSYNPFSGEWKKLPSMSVARFQMGVAVLDDYLYVVGGTNRQQVLNSVERYSFKTNKWSMVPPMSVERSGPAVAAMDGLLYVIGGAQTHATPFYRAQCTISSVECFDPITNSWAECPPLSETRAEAGAVVI
The following text describes a protein:
Function:
Probable RNA-binding protein that may be involved in salt and oxidative stress tolerance.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MAALARIGGRHLKSVCLINSSASCFFTQRRGVASKLFIGGLSFCTTEQGLSEAFSKCGQVVEAQIVMDRVSDRSKGFGFVTFASADEAQKALMEFNGQQLNGRTIFVDYAKAKQSLGGGGGYPIARGPPDPAVIAATRTTETSKSD
The following text describes a protein:
Function:
Part of the spliceosome which catalyzes two sequential transesterification reactions, first the excision of the non-coding intron from pre-mRNA and then the ligation of the coding exons to form the mature mRNA. Plays a role in stabilizing the structure of the spliceosome catalytic core and docking of the branch helix into the active site, producing 5'-exon and lariat intron-3'-intermediates.
Subcellular Localization:
Nucleus.
Sequence:
MSDRKGINKYYPPDFDPSKLERRAKKVSDSKSATMPTVRLMVPFSMRCTACGEYIYKSKKFNARKQVTDEVYLDVKIIRFFIRCPRCSGEIRFKTDPKNSDYQTEYGAVRNYEPWRDEKKVEETLDERLDRLEKEEKELEELKKQGKAMPDPSKLGTAVSTDGDVMAEIEARQKANIDEQEGIERLEELKERTARLNKIGRDVDVLEELRKRDDKESGVSEQDLRDDEMAKEVFRNAQGEKIKRVEVAKVDASVKKVSKPVVKMKKRMKGIVRK
The following text describes a protein:
Function:
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator.
Subcellular Localization:
Cytoplasm.
Sequence:
MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM
The following text describes a protein:
Function:
DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Sequence:
MDKKEKVLEIIKRLDKRYPNVKTALNFNSALDLVVATILSAQTTDINVNKVTENLFKKYQTADDYANVSLTELENDIKSINFYKNKAKYIKNLAKKLIEEFNGQVPKTMNELVTLPGVGRKTANIVLWNVFGINEGIAVDTHVKRISKLLGLTENTDPDKIEQDLMEITPRKYWGKLSHLLIMLGREICKAKAPNHKICPLSDICPSSTT
The following text describes a protein:
Function:
Protein 1A functions as a suppressor of RNA-mediated gene silencing, an antiviral defense mechanism of insect cells. Binds to long dsRNA and to a lesser extent, to siRNA; RNA-directed RNA polymerase replicates genomic and antigenomic RNA.
Sequence:
MESDKSMACLNRILMNKMMFVEDKISTLKMVADYYQKEVKYDFDAVESPREAPVFRCTCRFLGYTIMTQGIGKKNPKQEAARQMLLLLSGDVETNPGPVQSRPVYYRYNDPRYTRLEKAIERRDDKIKTLIKELRRQIKNRKIYSQGMFDKLTKQISDGIKDGVGSEQMNGNLTRICDFLENTLPGLQANIQATVIDTTDKYVSLKEDIMKIVLVILLVRLLMVWKKYRASLCVILIFIFKFYGFDQKLIDLIMDLKNKIFSQGALEDTVEEVVYHPWFHTCGKIIFAVMAFLTIKKIPGKQDWDSYITRLDRIPKSIEGAKKITDYCSEYFNIANDQIKMMVLGKTKEELQRANGLYGEIQAWAQEVRQYLELDQRNKIDLDTETANRVEQLWIKGLKFKSEPLLSKEMSALVHTTLLPAKQLYEYVSCSPVKGGGPRMRPICLWLVGESGVGKTEMVYPLCIDVLREMGMIKKDDFHHQVYGRQVETEFWDGYKGQKIVIYDDAFQKKDDKTAANPEIFEVIRSCNTFPQHLHMAALHDKNTFSAAELLLYTTNDYNVKLESITFPDAFFNRMGDMAYKVSPKKEYGIETEKGNSGKTYLKLDKSKLDKTKAIDLSVYEFQKIVRDEKSDAGWIDSGSPLDYEDFAKLVCSKWKEAKQSSMNKLKFLEEYAIRAQVGSEENSEYGDCIDFVDDIAKRLQKGETLEEIEFDYASDPEMFTQYYHFKSTIKPASRWQKYKDRMDICLSDCKTYLAKKYEEIKKILAEHPILTILGMIGVALSALAMYYWFSKSLDPVEAEVAPSGDAKTVRLPRKLVEIGASGDVKTQKIVKPVVETEWHRNNKGEIEISCDECGMHRMSAFNNMTDEEFDNCTYEDLNKDQKRELAQWSTKDSWLGRFFLSRDRKNKVGIWAEVGQSGDVKTNKAQIKRVEAGAEELVTVALTQGCSDDAAHNLMIDVFQKNTYRMSYFRGDKRYQLGNCTFVRGWSFIMPYHFVQAVFARRLPPNTIISLSQQMSEDLMQIPLSHFFSAGVDNFYLTDNCVRLPFKNGDFRDCVMVNLHSRMCTPHRDLVRHFILTSDQGKLKGSFSGAMATFHVNNMGLYRVYNWLNAVRPCDKKIEIFHPEDGFEYPEESYIQRDCYEYNAPTRTGDCGSIIGLYNKYLERKIIGMHIAGNDAEEHGYACPLTQECLETAFSALVNKNKKNISSQFYYEIPNMVDPLGDSSVPEGKFYALGKSSIRVGQAVNSSIIPSRIYGKLSVPTMKPALLKPTILNNKVHNPLLSGLKKCGVDTAVLSDDEVLSASQDVCRVMLNQYNKNLNKTKYQRILTYEEAIRGTQDDEFMCAINRTTSPGFPYAQMKRNAPGKQQWMGFGEEFDFTSNYALALRKDVEQLIEDCASGKISNVIFVDTLKDERRDIAKVNVGKTRVFSAGPQHFVVAFRQYFLPFAAWLMHNRISNEVAVGTNVYSSDWERIAKRLKTKGSHVIAGDFGNFDGSLVAQILWAIFWEIFVVWLKQFIDIENSEGKRILCICLGLWSHLVHSVHIYEDNVYMWTHSQPSGNPFTVIINCLYNSIIMRLSWIRVMEKFQPRLKSMKWFNEYVALITYGDDNVLNIDAKVVEWFNQINISEVMTEMRHEYTDEAKTGDIVKSRKLEDIFFLKRKFRFSPELQRHVAPLKIEVIYEMLNWSRRSIDPDEILMSNIETAFREVVYHGKEEYDKLRSAVLALKVPQELPENPQILTYNQYLHDIEYLADPLYDF
The following text describes a protein:
Function:
Epithelial intermediate filament protein.
Subcellular Localization:
Cytoplasm.
Sequence:
TSKISTTYEEEGRQSKIQPRAFVITRSGPTSRSSSYSARQSYGSRSSITPGVYQQLSSSGITDFRGTREKEKREMQNLNERLAGYIEKVHFLDAQVKKLEAENXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMDYAEFWKSELSKCVRDIQSAYDEKIDIIXXXXXXXXXXXXXXXXXXXXXXXMQLQHVQEEVKKLRTQAGEKNAAYAEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMELEIACYRKLLEGEESRVGLRSLVEQAIGVQGRGTASLKDTIQQSTASGSMTVQRSSKGPIAFNSVDQSGSNIVIENTTSGARAKTQSLKGWRVDKTVAGRVAASIELKNYDLPPNTKYTIWAKGAKDRATADNEQIADMFSLGVG
The following text describes a protein:
Function:
Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
MGQRSHRFVYYVPCLVALSVVGCLLVLFRERPYLASYRGRDSRGKVASPSAPTPEVTASPRREPVKLVMVTCGDHLNITLVSLKSAVAFSKAPLHLLLFASDASIQPLREQSVLPEEDAVLYVDADVIFVHPPEDLWSLFGAMNDSQLAALVPESEDYATNWYRRFARHPFFEPLGVNSGVMLMNLTRMRAFGWESLMGPLLTKYERNISWGDQDLINIVFHDHPDKLLVLSCKWNFRTDHCMYGPNCLGATAALLHGNRNVFQTSKEPAFRAVYLAMQQARAPSSWPACPIECFLSLPKTYQLGSSLLTGFLDPLEKGLRKARTTRCGQELLGHLAQWRERQLL
The following text describes a protein:
Function:
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Subcellular Localization:
Cytoplasm.
Sequence:
MDFLKINGAHGEGGGQIIRSAITLSCITKQPIHIENIRKNRKVSGLKPQHLTAIKILKKISDCKVIGDEIGSTELKFIPGEIKSSKLSEDVGTAGSISLILQVLIPIVAISQKNLEISIKGGTDVQWSPTMFYTQHILREVYSRMGINFSFELKKRGYYPKGNGEVNLEINPSNVKAISLSKRKTNRVKILCTFSKIPNEKIESEIKKIKEKLNESFVVDVEIKEEALDSGASLLVYSIDENSIIGIDSLFDKKIESFDVDLDGFLEDIAVDENLADMIVVPASVAKGKTIFQVKKITKHLETNLFVTSKISGCKYGIGKLPNGFEVIIEGTSYSSIK
The following text describes a protein:
Function:
Plays a role in primary ciliogenesis by modulating actin polymerization.
Subcellular Localization:
Cell membrane. Cytoplasm, cytoskeleton. Nucleus.
Sequence:
METTGYRPGSSSMSRKVQPTAPRAQEHQLSAQESRPPPEANAEAVRFLRSLRQEELQMLFFSETLVMVSDSGEPQGELTIEVQRGRYKDDFGLMSHCVLVHAFSRGLMDKMLCGNSLLGHLSWNLELMEQHSQEFIKFHILPMERKTSLLKQDDQLVMTRSIKEGQEVKTEVAFFPWHSITGFISEAANLVLLRVMAWRQTVPSNARFLALDTEGKLCYSTYQALGSQAIQVGHQQVEVFTVEQTVHSEEGIPMSCQFYLLPDGHVAKRVQVGSPGCCMITKMPILREEDEIEPRPAFEKKPLVWEEDVELYSRFMERKEELRLSHNSYLRQHPEAHALISDFLLFLLLRQPADVVTFAADFFGPFAVRRRPTPSLRSSNRPSPFRSLDPECSPSEG
The following text describes a protein:
Function:
Prokaryotic-type aspartate aminotransferase. Also has a prenate transaminase activity. Involved in the aromatic amino acids biosynthesis pathway via the arogenate route. Required for the transamination of prephenate into arogenate. Can use 2-oxoglutarate, oxaloacetate and prephenate as substrates, but not phenylpyruvate or 4-hydroxyphenylpyruvate.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MAATTTTSSSSRIAYSRHNIPGLHSDSLNPKSISFSSNLHTFSLKSSGSRRQLYSRRTGAVVIMQSMDKVEVDISLSPRVNSVKPSKTVAITDQATALVQAGVPVIRLAAGEPDFDTPAPIVEAGINAIREGHTRYTPNAGTMELRSAISHKLKEENGLSYTPDQILVSNGAKQSIIQAVLAVCSPGDEVLIPAPYWVSYPEMARLADATPVILPTSISEDFLLDPKLLESKLTEKSRLLILCSPSNPTGSVYPRKLLEQIAEIVARHPRLLVISDEIYEHIIYAPATHTSFASLPGMWDRTLTVNGFSKAFAMTGWRLGYIAGPKHFIAACNKIQSQFTSGASSISQKAAVAALGLGYAGGELVATMVKSFRERRDYLVKSFGEIEGVKISEPRGAFYLFIDLSSYYGVEVDGFGSINNSESLCRYLLDKAQVALVPGDAFGDDTCIRISYAASLSTLQAAVERIKKALVTIKPPVPV
The following text describes a protein:
Function:
Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Sequence:
MNNKFIIVIFGGLGDLAQNKLYPVIYSLYKKYRLLNCTKIISTGRRPNVDKEEFLKILEKSIKTHDDSFFSLFDFVKFDLEKEEEYNHLKNMLSNFKEEEFIFYLATPPTTFETIIKNLGEFLKSFPNKRKIVIEKPFGYNLYSAQKLNQLIKIYFKEEEVYRIDHFLGKETVQNIFGLRFSNIIFEGIWNRNFIDHIQISALEDIGVEGRLGYYDKVGALRDMIQNHLIQILSIVAMEPPCCINEKEIRDEKIKVLKSIREIKREDVPLYAVRGQYEGYLIDENLSQSNTETYAAVKLFIENLRWDGVPFYLRTGKKLKRKETSIIIVFKKIPGLFSKILDCMPQEDIIGFKIAPENKIILSFQLRPLGGSMLSCPVSTSMEWTGPNIEAYETLFMDIIEGDQSLFIRKDEIEKSWEIVQPILDFWKDDPNIPIYPQGSWGPKEAEELIRRDGREWRYIDG
The following text describes a protein:
Function:
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase.
Miscellaneous:
MISCELLANEOUS: Present with 2540 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Chromosome. Note=Nuclear throughout the cell cycle. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. At anaphase, it is enriched at rDNA. Dissociation from chromosomes is observed in late telophase.
Sequence:
MSGFSLSEYLTKFQTTDRESYPRLQDPSRELNVIIDQLAVSPEQIDASPDSLEALIDLCHDFPHLTPKLQTQLSYLISSSLSNLSKDIKANLSSNVNFTEIGGLIPQWKRHLEEYGYLIQVLLTFLQDELHKVSSQSTNLNRSAKNSKNDSANVELFKRDCNQMENLLESITKLLEINLSKIFQTTPEKDLFIGLFTRPLFVLLEIEPVTKVSSLKMFIQRILAMCVKNHGQSSSIQSSLMTNLTYFLHLSVFNAELLKLLNDEYNYPQLTEDILKEISTRVFNAKDTTGPKAISNFLIKLSELSPGIMLRQMNLVITLLNNSSITLRCSVVEACGNIVAELAQDPQTMEHYKQQIAVLIELLEERFQDSNPYVRTKAIQGCSKICDLSSKFNKSKAKFTSLAVRSLQDRSSLVRRNSVKLLSKLLLKHPFKAIHGSQLRLSEWEEYLKGSESQLNSTLKKVESQETLNDTIERSLIEEEVEQDEGQCRTELEGSFNKSAELSRIENEVENINATNTSVLMKLKLMIVYYKDAISFIKEIHKSIELISNLLFSKNRNEVLESMDFLVLADAFDIELSEFGIKKMLHLVWMKGTNDEGTSISVHLIECYKQLFLTAPDSCNMQEKAAHIAKNLINLSIGASIADLASLEQLLGMMYEQKLIDQHVINILWAIYNSASKASMQKEQNVNNRDSEKGFSKEQIHGSIIILGMLSLADNEIALKGLESLLNIGLGAVGLKDLTLCRYSCLALERMVPKRSTIITKAINQELEDVAVKKLYAIIINYTKDNEYYPMCEQALSALFTISSKPDILATDLIREKTMMTFGKPEEEDSILSLEQSSRVVSLSQLLFIVGQVAIKTLVYLEKCEAEFKKRKIEAETRNGKVKNQGADVTNTTQDNGGDKELEMIGGTNEDDFTDAIQFVKENELLFGEKSILGKFCPIVEEIVSNSSRFSDPMLQRTATLCLEKLMCLSSKYCEKSLPLLITVMEKSPDPTIRSNAVLGLGDMAVCFNNLVDENTDYLYRRLHDENLMVQRTCLMTVTFLILAGQVKVKGQLGEMAKCLDNPDQGISDMCRLFFTELASKDNAIYNGFIDIFSNLSSDDLLGKESFKKIIKFLLTFIDKERHQKQLNEKLVGRLRKCETQKQWDDIAFVLNNLPYKNEDVTALLEQGFKVVSAKE
The following text describes a protein:
Function:
Involved in pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MADKTEAQDDSKKMPEPEIAPVVGESVPETEDVKPAPADPKAALAARMARFKALQSQKESGRKATEKEVRDAEDRSARLAQISKLQDAHDKASYKLLKSEDPDFERKRNWDYTVEESESWDKRMAKKARSRDNVAFADYTKEANKVYKRQIKQMDKVDLDSYAAQKAEKLQRQVQSGLLQLIESPEGDLYTVNPLNNQINTPAEEGYSHDHKPSQEAIDKLVGDLDKGERARLKARAARGIRDENDAGDVTYINQKNKQFNDKLTRFYNKYTTEIRESFERGTAI
The following text describes a protein:
Function:
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Subcellular Localization:
Cytoplasm.
Sequence:
MIHYSGNPISKVGRPGIYIHYPYCIQKCEYCDFYSVGNGKNQIPDETGLFQRYKEEIATRISDNPFISDLEFDTIFFGGGTPSRAEVSKISDLIFFLRNNIKFSKYSEITMECNPEDITPDFLKSIEQAGINRISVGIQSFHPEKLQFLGRYYDPDRYENVLETVKNSGISNFSADLIYGIPGQTVQEILQDIQKVLSAGGKHISLYALTVEKGTEYSRKVMDKISPSPEEEIQEKILKLLPDLLSPYELFQYEVSNFSKPGFFSKHNLKYWTMEYYLGIGPGAHGFLPSGRYSNPRNVDTYKRKNFSKEYTKPNFYEELILSLFRLFQPILMESFYELIPDQSQTLDLQLKKFQESGLCEFSNGIFQWKPEAVLFLDSKILELTSFD
The following text describes a protein:
Function:
Responsible for the hydrolysis of the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol phosphorylceramide (M(IP)2C). Regulates sphingolipid metabolism in mitochondria, especially the formation of alpha-hydroxylated very long chain phytoceramides. The generated ceramides contribute to the normal function of mitochondria. Also active on sphingomyelin (SM), but this activity is probably not physiologically relevant.
Miscellaneous:
MISCELLANEOUS: Present with 2170 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein. Note=Localization is regulated in a growth-dependent manner. Predominantly in the ER during early growth and becomes associated with mitochondria in late logarithmic growth.
Sequence:
MYNRKDRDVHERKEDGQSEFEALNGTNAIMSDNSKAYSIKFLTFNTWGLKYVSKHRKERLRAIADKLAGHSMLTPISDELLPNGGDSNENEDYDVIALQEIWCVEDWKYLASACASKYPYQRLFHSGILTGPGLAILSKVPIESTFLYRFPINGRPSAVFRGDWYVGKSIAITVLNTGTRPIAIMNSHMHAPYAKQGDAAYLCHRSCQAWDFSRLIKLYRQAGYAVIVVGDLNSRPGSLPHKFLTQEAGLVDSWEQLHGKQDLAVIARLSPLQQLLKGCTTCDSLLNTWRAQRQPDEACRLDYALIDPDFLQTVDAGVRFTERIPHLDCSVSDHFAYSCTLNIVPQGTESRPSTSVKRAKTHDRELILQRYSNYETMIECIHTYLKTAQRQKFFRGLHFWASILLLIASLVVTTFTANKAGWSSIFWVLFAIAVSISGTIDGAISFLFGRSEIRALIEVEQEVLDAEHHLQTFLSEK
The following text describes a protein:
Function:
Appears to regulate regional development of specific tissues. Can rescue axis polarity in UV-radiated Xenopus embryos.
Subcellular Localization:
Nucleus.
Sequence:
MVETNSPPAGYTLKRSPSDLGEQQQPPRQISRSPGNTAAYHLTTAMLLNSQQCGYLGQRLQSVLQQQHAQHQQSQSQTPSSDDGSQSGVTILEEERRGGAAAASLFTIDSILGSRQQGGGTAPSQGSHISSNGNQNGLTSNGISLGLKRSGAESPASPNSNSSSSAAASPIRPQRVPAMLQHPGLHLGHLAAAAASGFAASPSDFLVAYPNFYPNYMHAAAVAHVAAAQMQAHVSGAAAGLSGHGHHPHHPHGHPHHPHLGAHHHGQHHLSHLGHGPPPKRKRRHRTIFTEEQLEQLEATFDKTHYPDVVLREQLALKVDLKEERVEVWFKNRRAKWRKQKREEQERLRKLQEEQCGSTTNGTTNSSSGTTSSTGNGSLTVKCPGSDHYSAQLVHIKSDANGYSDADESSDLEVA
The following text describes a protein:
Function:
Required for normal chemotaxis in response to cAMP and folate. Required for the heterodimerization of the G protein beta and gamma subunits gpbA and gpgA, which is itself thought to be necessary for prenylation of the gamma subunit gpgA and its association with plasma membranes.
Subcellular Localization:
Cytoplasm.
Sequence:
MEQNILNSILDKFGDGDQERSDIRHNDSGDENDNHSDHEGNHGNNECCEGNEDGDKEYEVDVEDMTDEQYAQFIQEQQEPKIKSGGNTGVKGVLSDYAEHREKQKQKYLQKKYETQKMLEKMCFTTRDQPPPTEEENQLDSDDDDLERIRKARMEQWKSKQQITSDVKKPEKKVFGYFKQIDSSQYIHEIDNEPPNVFVIIHLFQNYIPECVLLNQQLGQLAVKYRYIKFLKILSKEAKENYHDEALPSLLVYIGGKLLVSFVPLTEELGRNFDQEDLELLLSSYDIIPNPMKAKNSNWETSLSRKRPESDDDNDD
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.
Subcellular Localization:
Cytoplasm.
Sequence:
MVLLQPDPFLNELTTMFEQTTEEGTVWVTLKRSSQKCKAHRNKMITDGEPIEYRCLIRATNGKRTISTSVGAKDHQRFQSSYATILKAHMTSLKKRERKDKKKAAGEDKKEAVTTKAKRA