lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA and the nucleoplasmic transit of the pre-60S ribosomal subunits. Regulates pre-60S association of the critical remodeling factor MDN1.
Miscellaneous:
MISCELLANEOUS: Present with 7820 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSEEFIAVSTLARNLEIAKGNEFHTILATLRSPVYINEQLLKSELSFLVTKILKLIRSGNDFDLWKGCHTSVVTCAYNPLVLSTHGGQLLAAIYSRLEQKTGFYSSVISSSHGKQLFNTLISSVAIIIDLMKNKPTLSREALVPKLKAIIPTLITLSQYEPELVLPVLQRILKRNTTTFKPFTNKFRTVLINLIISDYASLGTKTQRLVCENFAYLHLLKIQVSDTSDDETQAHHKIYADSNWRTGLMSILSQFKPIIQLCGEILDFEQDNELYKLIKSLPVIDESNNKEEFLPSLKLDFNAPLTLWEIPQRLSLLADMLVAFISLPTPFPIRVPLGGINSLCEVLLGVSNKYLPLKKELRHDNELNGVINTILPQIQFQGIRLWEIMVSKYGKCGLSFFEGILSSIELFIPLKKKSNNEIDFNVVGSLKFEFATVFRLVNMILSHLGHQLNIISVISQLIEVALFLSHDKTLIDSLFKNRKSIMKQQTKTKQSKRSKSAEGAFSDIYTHPELFVCKNSMNWFNEINDFFITALNNWILPSTPHIQILKYSITQSLRLKERFGYIPESFVNLLRCEVLHPGSERVSILPIAISLLKNINDDMFELLCHPKVPVGMVYQLHKPLDLGEDGEVRDDINKKEVETNESSSNANTGLETLKALENLENVTIPEPKHEVPKVVDDTAIFKKRSVEEVIERESTSSHKKVKFVEETTVDNGEELIVKKAVSQTKEEEKPMEDSEDEEQEEFEIPAIELSDDEEEEEEEE
The following text describes a protein:
Function:
Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass type II membrane protein; Intermembrane side.
Domain:
The CHCH domain contains a conserved twin Cys-X(9)-Cys motif which is required for import and stability of MIA40 in mitochondria.
Sequence:
MYRTALRPSQSALRAIRSTTSPSALVSSGARRFASTTSAPKKKSTWKGAAVRWGLAVAAVYYYNTSPIFSDELPETAGTAPSQLTDADLPTVDAIVEEKRRQAAEHAAARKAAQAAAKAAATPATPSESVEEQITKAEAEAEAVPEGDSKPRSESTEGVIPEAGASPEALQEEADAQGAFNPETGEINWDCPCLGGMAHGPCGEEFKAAFSCFVYSTEEPKGMDCIEKFSHMQDCFRKYPEVYGAELADDEEAERASAAAPAAEGTPAKEEPVENKKEEALEPATHDATAANNNKKQQ
The following text describes a protein:
Function:
Splits dipeptides with a prolyl in the C-terminal position and a nonpolar amino acid at the N-terminal position.
Sequence:
MRIERLKEFIAEKELDGVLITHKPNLFYFTGSAPVLGGYLVVTADEELFLVPQLEYEEARESSRVPVEYFKRGAELYERLKAFNLKKLGIEGRTSYSSVQSLKEKAGVEEFAVVDDVIKELRMVKTPEEIEVIKRACQIADKAMLVAIEEVREGVREREVAAKMEYVMKMEGAEKTAFDTIIASGWRSALPHGVASDKRIERGELVVIDEGALFNHYHSDMTRTVVVGSPNEKQREIYEIVLEAQKKGVEEARPGITAKELDTIVRDVIAEYGYGDYFIHSTGHGVGLEIHEWPGINQNDETVLKPGMVITVEPGIYLPKFGGVRIEDTIVITENGAERLTKTERELI
The following text describes a protein:
Function:
Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the phytosphingosine degradation pathway.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
METPAAAAPAGSLFPSFLLLACGTLVAALLGAAHRLGLFYQLLHKVDKASVRHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPIDVLYPYFMVQKEMVPAKPRKGLVGRVVSWYLENYLANLFAGAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENRSAALKKADVIVLAGTVCDFRLSYGRVLSHSSKIIIVNRNREDMLLNSDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKAAMPVAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACSLAYTEYHKAAMGLGARGLLLSRENEDQVVKVLHDAQQQCRDGHPVVVNILIGRTDFRDGSIAV
The following text describes a protein:
Function:
D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Sequence:
MSKRLALAYSKKDPAGSGMAREIKDMMGEEFEISDKRCELIEVDREILYINGSQFEGFDYLAVLSRHSGTPNHPIFTAHVSGNFGRARYGGDHFKLSIAIPSLMKEYLISVSKRAEEIGYWVGFEPTHHGPTLDIPTAFLEIGCDETAWRDERGLRAAAESVLEAIESWKDGKFVAAVAFGGPHINDHFTRVELFTRFAIGHAARKLDAEWVDGEMVKQAVSRNGEPTGVAIVDNKGLKGEDRERIEGALRDLGLEVIRVKKILRDELGEEEGEEI
The following text describes a protein:
Function:
Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Miscellaneous:
MISCELLANEOUS: Displays the following serological isotype: Mgc-, Ke+, and Oz-. Mgc- has Ala-6, Ser-8 and Thr-57; Ke+ has Gly-46 and Oz- has Arg-83.
Subcellular Localization:
Secreted. Cell membrane.
Sequence:
GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVKVAWKADGSPVNTGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPAECS
The following text describes a protein:
Function:
Protein kinase involved in salt tolerance and pH sensitivity, probably by regulating plasma membrane potential and cation influx. Positively controls the TRK1-TRK2 potassium transport system in response to potassium starvation. Stabilizes TRK1 in the plasma membrane by preventing its vacuolar sorting and degradation. Also stabilizes other plasma membrane nutrient transporters like CAN1, FUR4 and HXT1. May itself be subject to regulation by ARL1.
Sequence:
MGDEKLSRHTSLKRARSLSESIKGLFKPSGISGSNNAAAPSSRPGQDQAHSHQTARIITSNVSSPSISPVHSPVLQAAPKHHKLGVPNIAKLSLSPSREPSLNSENEMFSQESFISEKDEDEANLLEREDLQNKKEEKARAKHVRSKEAYVPHHRYTVGSDEVERQPRERLKNFPQNAGSSNPANSNANHVLDQENNFSIDAMLDYDEESKLRRRNSLGVRNHSNRTRSRKNSLSTPRSPPMKNGNGGMNSNATNNVGNGTGNRIYMRGRNHSDSISASSLPKFQEIECKCILDLGHFKVFENGYHEHSLRVLPIITNNKNVDSGDEKDADASVNSGDDGDNDSEANMHKQKSVFSLSGLFKSHKDGNQQQQQQQQQEENGEQINLEKAFSIIPSQRFIKSQTLKKSRTSNLKNGNNDELMKNDGKNIPQIVNPNAAVGVEELKLINALSEKIRKGLKSENTKGNNGEGRSNSNKQEDSDDTEGKAGTTNDDTSHKPCSQKYGKSIGVVGAGAYGVVKICARCKTAKDVLPYSTYSNGKKLFFAVKELKPKPGDQIDKFCTRLTSEFIIGHSLSHPHFEANAMIAGNVSRTTPPKHVFNAPNILKILDLMEYSNSFVEVMEFCASGDLYSLLTRNNISNESNNGSSRLIQTVKEGSGSPLHPLEADCFMKQLLNGVQYMHDHGIAHCDLKPENILFQPNGLLKICDFGTSSVFQTAWEKHVHFQSGAMGSEPYVAPEEFIRDAEYDPRLVDCWSCGIVYCTMVMGQYLWKIAIPEKDSLFKSFLSEIKDDGQFYLFEELRHVSSELNRLRKIALYRTFQVDPTKRITIEQLLQSSWMRKTKCCVVYRHLHTKVSK
The following text describes a protein:
Function:
Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Domain:
The CBM21 domain is known to be involved in the localization to glycogen and is characteristic of some regulatory subunit of phosphatase complexes.
Sequence:
MEPAEEPGQISKDNFLEVPNLSDSVCEDEEVKATFKPGFSPQPSRRGSGSSEDMYLDTPTSASRRVSFADSLGFSLVSVKEFDCWELPSVSTDFDLSGDVFHTDEYVLSPLFDLPSSKEKLMEQLQVQKAVLESAEHLPGSSMKGIIRVLNISFEKLVYVRMSLDDWQTHYDILAEYVPNSCDGETDQFSFKISLVPPYQKEGGKVEFCIRYETSAGTFWSNNNGTNYILVCQKKRKEPEPVKPLEEAPSRQIKGCLKVKSRSKEEPLLAPEENKFETLKFTESYIPTIICSHEDKDDLGANHPNVDDINKKHDEHNGKELDLMINQRLITSQDEKNTFATDTVNFTNKAEGSEKKQAYHEINTDLFMGPLSPSLSAESSLKRDFYHSRSSSPGNEYGHPHSEEIISDMGEKGPSLGDTSSDELMQLELCSKEDLDDNANPANGSGRVCSSFDQRMACGLKNNEAGIKKTGIQDYKYSHGDSTKLEESNASSRDDYAKVDNKKEKQTCLGVNENPSKNFQSVFQTQEGHMGYPKISTEGDKANNQDLTSLLSKDITANTWAVTVDPCPSTNAKRSWREVGSGSNLEPGTSDLSSPRNFSPLTDDHLFQADRENSDSSNPENQNMNTRHRKKWNVLETQSETSETESDIAKHTKEQAEYKDMWEKTDNSRNLKATPTEHLFTCRETECYGLSSLADHGITEKAQAVTAYIIKTTLESTPESASARGKAIIAKLPQETAGNDRPIEVKETAFDPHEGRKDDSHYSLCHGDTAGVIHDNDFERESHLDICNLRVDEMKKEKTTSTCFPQKTYDKEKHGIGSVTSIDEPSQVITGNQKATSKLDLHLGVLPTDRAIFQANADLELLQELSRRTDFNAVPSAFNSDTASASRDSSQVYRHCSKKSVPSYGEEKAVTNTTLQSIPTKSEYNWHPESEVLGHAMSKPEDVFKSSEIMKSGSGGERGGGPILQQKEGSLENSQGPMFFTNEPLENLDEASSENEGLMHSGQSQCYLGDKGLVSSASATVSTQELEAQGRESLLSISTNSKIPYFLLFLIFLATVYYYDLMIGLAFYLFSLYWLYWEGGRQRESVKKK
The following text describes a protein:
Function:
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Subcellular Localization:
Cytoplasm.
Sequence:
MPSTFLTSERTRRNQSDRVIRHRSMMLELQGIPVSPGVAIGPALVLDADGYRIPRCIVPASDVEDEFARLHTAVDLVSAHLEHSRLETTATAGRSTGDIFAAQLQMLHDPRLHSELQRRIGEDRQSAAFAVSGVLHNYASALRRLDNPLLADRAQDVLDIERQLLMQLGAVTRQPLSDLSEPVIVLSHMLTPSETANLDRRFVKGFCTETGGPGGHTAIVAKGLEIPAVVGIGDFLHQIAGSNCVIVDGDRGKLIVDPDDDVLENYRERAEYRRSLAVRLAELSQLPAETTDGVRIQLNANIEFPHETVACIDRGADGIGLYRTEFLYLSSDDEPSEEDHYQAYSEVVQKMDGRPVVIRTLDLGADKMGRGNMAHRENNPFLGLRSIRLSLRNLDVFRPQLRAVLRAAVHGDVRVMFPLITTINELRQARMLLNVVAEDLQESGLPYRSDLPVGMMVEVPAAVMMLEHFASEVDFFSIGTNDLAQYTLAVDRSNEYVADLYQSSDPAVLRLIQHSIDVAAKSQTPVSVCGEMSSNPGRALLLLGMGVRNLSVPPSALPRVKKVIRNVSIDQCKAIAERVMKLEAARDVDLYLLDRLSDLAPELVMQ
The following text describes a protein:
Function:
May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Sequence:
MRILEFDEKRQAVKLHIESEDDLWLLHLILEKDDKVVAKTTRDVGLGKESRRIPMTIILKVDYTEFQEFTNRLRIHGIIEDAPERFGIKGAHHTINLDIGDEIIIIKQQWNKYVLDRLKRQANKRSRIIIALVDFDEYLIAIPFEQGIKILSEKSLRPLNEEEGIIEQNALEIATELAEYVKQYDPDAILLAGPGFFKEEVSKKVNAILKNKKIYIDSVSSATRAGLHEVLKRDIIDKIMTDYEIAIGAKKMEKAMELLAKQPELVTYGLEQVKNAIEMGAVETVLVIEDLLSSDEQERLTIERMLEDIENKRGEVILVPKESPIYFELKNLTGILAILRFRIN
The following text describes a protein:
Function:
May play a role in antibiotic biosynthesis.
Sequence:
MRIFVYGSLRHKQGNSHWMTNAQLLGDFSIDNYQLYSLGHYPGAVPGNGTVHGEVYRIDNATLAELDALRTRGGEYARQLIQTPYGSAWMYVYQRPVDGLKLIESGDWLDRDK
The following text describes a protein:
Function:
Involved in the mineralization and structural organization of enamel.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MAPIGQDNPEDQDQVLPTGQSGMSPATQDTPEDQPPTASGLLDESEVTLPANLQGVSLTTEESTTEEPRGPTLKMENLVLILSLFGTSFAIPVFLQPGGPPGMGSLSLETMRHLGNLNLLPQFSRFGFGKQFNSLWMHGFLPPHSNYPWLSPRDQETQQYEYALPVHPPPRPSQRTLQPQQPKQNAFLPPTVAPSAQGPPAQNGDPQPPILHLQPPLQQEEKPSVQEQVAPPKRPPKPELPALDFTVQLRQSIFPIAQKLISQGPRQKAEQSPLYPELVYVPFGANQQNAAPARLGKVSSEEMPGGGGEPLAYGSIFPGFGSMRPGFGAMQINPALGKDFTLEDDSPTVAGKPPGQGGEVLGSPRDGAIPAGHPNPGLLPERISRLRSGAALTFPSDFIPHRGQGPAGQSKLPPGVTPPPADPLMTPGPSDPLEFFEGDGTTPLGLQREALLDTTMTPDTQSTYMPGNEAQQMQVTQDQWQFQEP
The following text describes a protein:
Function:
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Sequence:
MSVIDPVFFDKKFSASRYMLRYVVGAATDELRDQQLQKVRKFRAMADEQIDGVIDQSFVNFNTSLARFTAISNQLQETRDKVQEVRKRAADGRTILGSKTKNLRELLLQKYEAKKVIDIINDIECIEAAPTKIDALLHQRKFLEAVDEFASALDLVFSEQLVAFHATTGLRNGLMECKQTIEDRLIHELQRAIYLKGAFSNIASKTNQYSLAAIENELNSDAQLDHEFDRLLLQASPSKADATDQSSNDAATVARTNNALKTAVSAVKKLHREREAIGNIKSSIEEELDAVVAELSRLCRGIFNTSSSTSFANAFTEATFGTHDHSSDFGTFLRLLFTVLRRIAQRHYLVAVYFEADGDTWDYGMFEVSTRISGVLELTNFDRRAQRVVGEYLDGVSIPQPVTSDPAESSASDSGELFKLSRNKPSKNQVSDGDESGQLVAKRRHLVCEPSVFHLPEVYQDLERIGKDLQQFFRASNSRSGANSLSGFASFLSTFIIQKWIPKVKAKAQHFLALKARGQTSACRLPIPSDTTYQPPSIDSLLHVIENLREMMVKMPTHASDLASVLETSVLSWLEECAVIVRDIREHTLNHQQLQSKNVTYADLATIFHEYEGYQRAKQGSPIPYHHSKVQPTGSASCGANSTRTSAEETIAAQELELEREMYDPDAWMQGPNGLLMDNARIGMLGYANSACDLIALYLQRVAGGSGGKSNNNSAPPTTSPALTMALQAASWQCSALADECLLFLRREVRLHCCYYLTQLVSQRFDMEEGQSTMAQDSVLTLNLNLSSIENALQPYLASDKMALVFNGADALLSRLLIGNLAQMTDSTFTRGGVQQMLLNIGALRQGLTGTLYSYPRDGASLSSTASMPSSCSSASRLEHAKRYYQLLNLSETQLEMFLLANRGAYSHEAFRALWHVQAPHRPLAKGSVNKLDSLLR
The following text describes a protein:
Function:
Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity).
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein.
Sequence:
MGVVNELRQRTWSGMLNVEVVLNPKLVVQGMPDEQVRCHLRIPRESYLVLHLPFVLNKLRGVLRQEVKDAFHGWWFGMEDVLVHWNHPVGTLYDSLVGLRPQERAAQFQANTLTMWTLTLNYSEDARDGSVPLVGGMQQVEDFWRHQWKQACYIIHGSSKQIMSLSIPDSKTFWDCVLQRDERVFRGIASRITARKGGVKALPVRIHQTTLRELRTLQPTVKPGEWGGGTLGELLRAELPECFKNGSVLRPVVHGIEVSPESQLADLYHLFCSFDGFLHISICSPVALIIPTT
The following text describes a protein:
Function:
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Sequence:
MKQLYGVIGNPIGHSLSPVMHNDAFEHLNMDAHYHAFLVEEELLGEAVRGLKALGISGFNVTTPHKVAIMEYLDEIDPLARKIGAVNTVVHKDGRLIGYNTDGIGFVRALQSISNEPLQGKRILLLGSGGASRAIYFSLADVGVKEIDVANRTVDKAKELIAARTADVNSVALSLEKATEEQGNYDIIIQTTTIGMHPHVEHTPLQICSLKKGTIVSDIIYNPFETKILCEAKEQGAIIQNGIDMFVYQGALAFEMWTGRTPNIERMKQLVIEKLGG
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MAAWRLSLCARSLFAIRGLQAAPLRWKSSSSRAVIARSAAASKKRREEPTIQWMEDPEPEDENVYLKNPNFHGYDDDPNMDVWNMQAVFFFGFSIALVLGTTFVAYVPDYRMLEWAHREAMMLVKYREANGLPLMESNRFDPSKINLLDNK
The following text describes a protein:
Function:
Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases.
Subcellular Localization:
Cytoplasm.
Domain:
The MATH/TRAF domain binds to receptor cytoplasmic domains.
Sequence:
MSIDIKFTINDILFNQESLQKKNKYTCPICFEFIYKKQIYQCKSGHHACKECWEKSLETKKECMTCKSVVNSYNDLSRCLMVERAFDKKECCCIYSFTEQIVQGGTNCSPPDGASDQNQRKLIKDEENGCKEKIEVDQIDSHLINCQYKFVTCSFKGCEKILRMNSLESHQNECGFKLVICDFCKRDDIKKKELETHYKTCPMVPIDCSQGCSVKIERKSIIDHIENDCCNTQIPCKYFEQGCKVEMKRSELQNHLERVNHQTYMGILIDKLTNQVGHSKKTHDELLKKIEDLSLLIIKFSDACLKKQVLPKALDICSNGYRNKWIISNYSSLAKSKLNCKSLSSPILLILSHHFQVCVYPKGDENKEYISLYLRVNNIEEPNSLKVEYSFTLVNVLDKSKSITKRVDKIVFISPKEWGWGKFLLSDLINKENGWLSNDDKLTIEIYIKILNEEYEPLES
The following text describes a protein:
Function:
Substrate-specific adapter of SKP1-containing E3 ubiquitin-protein ligases which mediate the ubiquitination and subsequent proteasomal degradation of host target proteins including CDKN1B. Disappearance of host CDKN1B correlates with cell cycle progression through the G0/G1 checkpoint. Therefore, viruses in infected cells are protected from diverse innate host antiviral responses normally triggered by G0/G1 cell cycle arrest.
Sequence:
MDLYGYVSCTPRIRHDVLDGLLNVYDPDELCSRDTPFRLYLTRYDCTPEGLRLFLTRGADVNGVRGSRTSPLCTVLSNKDLGNEAEALAKQLIDAGADVNAMAPDGRYPLLCLLENDRINTARFVRYMIDRGTSVYVRGTDGYGPVQTYIHSKNVVLDTLRELVRAGATVHDPDKTYGFNVLQCYMIAHVRSSNVQILRFLLRHGVDSSRGLHATVMFNTLERKISHGVFNRKVLDFIFTQISINEQNSLDFTPINYCVIHNDRRTFDYLLERGADPNVVNFLGNSCLDLAVLNGNKYMVHRLLRKTITPDAYTRALNVVNSNIYSIKSYGMSEFVKRHGTLYKALIRSFVKDSDREIFTYVHIYDYFREFVDECIRERDAMKADVLDAVSVFDTAFGLVARPRWKHVRILSKYVRGVYGDRVKKILRSLHKRRFKTDRLVRRIADLCGPDGLWTRLPVEVRYSVVDYLTDDEIHDLFVKIHA
The following text describes a protein:
Function:
Required for the establishment and maintenance of stable cell fate in several lineages including V5.pa, T, Z1/Z4 and QR lineages probably by repressing the expression of cell fate determinants. Required to maintain non-distal tip cell (DTC) fate of somatic gonadal cells through the htz-1-mediated repression of transcription factor ceh-22. Regulates the subnuclear localization of histone variant htz-1 in somatic gonadal cells. Plays a role in the attenuation of the let-60/ras pathway, probably by preventing expression of activators of the pathway. Involved in adult locomotion. Acts together with the sumoylation pathway to prevent muscle myosin depletion in aging adults probably by preventing myoblast growth factor receptor egl-15 overexpression. May play a role in vulva development.
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to granular structures in interphase and co-localizes with chromosomes during metaphase.
Domain:
The BROMO domain 2 is essential for the interaction with smo-1 and E2 enzyme ubc-9.
Sequence:
MSEGSGDQSQQRPWASPRQQPIKGIVQPRVLPPFGKPTRHTNKLDYIMTTVLKEAGKHKHVWPFQKPVDAVALCIPLYHERVARPMDLKTIENRLKSTYYTCAQECIDDIETVFQNCYTFNGKEDDVTIMAQNVHEVIKKSLEQAPREEHDMDVYWGKNKKKPAKSDGGSKSSSSKKNDARGPSEAPSEAGSEVSSVTTASAAAPTVSESASVAAKPERKVAGKKTGKRKAESEDDEKPEPLRAKREVAVVKKEVHQPLLPSMKPCLKLLNDFSTKKYQEFAWPFNEPVDAEQLGLHDYHKIIKEPMDLKSMKAKMESGAYKEPSDFEHDVRLMLRNCFLYNPVGDPVHSFGLRFQEVFDRRWAELGDSSSRASSVAPQSAPIAPTPKVAKSSAPKEPKESRKEHKKETTFEASGAKSEDLMQINNALSMIREREEKLKAELAAAQAIKDKLTSVKNRREDNPNEPFPEKLINETRALCTTQVGQNASSSSASSAALRNGRSKKAASARLYGYEFDSDDEDNKMALTYEEKRNLSNLINNLPNNQLNTIISIIQRRERSALMQQQLDDSEVELDFESLGDMCLREMGAFIKTIPTLNGNGDDEKPKTSSNPTSSGATGSKGSSSLESKNGKKKKNFNMSESSDDETSNSRKRRKRESSESQSSSSSDDDSDDEDRPSIPRKSGQPPSTSREWNQSSAPPPRMGGMGGQPPMSRVPASSSTSVSAIGKNNAAASSNSYQAPKPAPVPAPTSSRPPAAPRPPSKPKKTGGASILDTLLPDTFGASPPQFFQSQPTTSATIRSPTESQPGNGEDEQTRIQRMRMEAKRARQKEDEGSVSLSNQMEMMAAFEFDNTY
The following text describes a protein:
Function:
Catalyzes the formation of rosmarinic acid using caffeoyl-CoA and 3.4-dihydroxyphenyllactate as substrates. Can also use 4-coumaroyl-CoA and 4-hydroxyphenyllactate as substrates. Rosmarinic acid is an ester of caffeic acid and 3,4-dihydroxyphenyllactic acid.
Sequence:
MRIDIKDSTMVKPAAETPGGSVWLTNLDLLSPANYHTLSVHFYHHDGSENFFDAAALKEALSRALVDFYPYAGRLKLKDNRLEIDCNGEGVLLVEAESDGALAELGEFAPRPDLNLIPQVDYAKGISTYPLMLFQLTRFKCGGVGLGVANEHHLSDGVAALHFINTWAHLARGVPAPSPPPVFDRRSLSARNPPKPQFSHAEYQPPPTLPTPLTDTAIAYSKLKVTRDQLGALKAKCLAGDPSGKPRSTFEVLAGHIWRCVCAARGLPEDQETKLHIPFDGRAKLRLPPGYFGNAIFFATPVATCGEIESNSLAHAVKRVGDAIARLDEDYLRSSIDFLELQEDISKLAQGAHSFRCPNLWVISWVRLPVYEPDFGWGKAVYMGPWAAPFEGKSYLLPNPDNDGSLFVAITLHTQHMERFEKLFYEI
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. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1.
Sequence:
MGNFRFPIKTKLPPGFINARILRDNFKRQQFKENEILVKSLKFIARNMNLPTKLRLEAQLKLNALPNYMRSTQIKNRCVDSGHARFVLSDFRLCRYQFRENALKGNLPGVKKGIW
The following text describes a protein:
Function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
Sequence:
MLCIQRRRHVRPGDLAGQDMAMDHLVNSAAKLHYMSGGNISVLIVFRGPNGTALGVGTQHSEVPCISFLVVFNFNGDNADAKGLLKATIKDPNPVGFLENKLLHGQSFPMSDDVLYTCLTLPIGKAKIEKEGRDVKIALFLMVVPLFLLCHFKKTKANSTTLLLFRYGQYFPVSDEVLDPSFTLPIGNAKYSNLHNVPVYNQYRSSVATTSSIVIGGGSEGGRMVGIAVVAATIAAAIIASSSGGKDKQMAKTGMAMVMLHYL
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. POM152 is important for the de novo assembly of NPCs.
Miscellaneous:
MISCELLANEOUS: Present with 3410 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Note=Central core structure of the nuclear pore complex.
Sequence:
MEHRYNVFNDTPRGNHWMGSSVSGSPRPSYSSRPNVNTTRRFQYSDDEPAEKIRPLRSRSFKSTESNISDEKSRISERDSKDRYINGDKKVDIYSLPLISTDVLEISKQRTFAVILFLIIQCYKIYDLVILKSGLPLSGLLFKNYRFNFISKYFIIDSFFLYVLPSFNIPRLTFKPWVVYLQILAMLLLNIFISSDHEFVLISLIMTTWRKLYTKELSVTGSAINHHRIFDSSAHFKGALTIKILPENTAMFNPLHESYCLPMDTNLFKINSIDVPIRINSTEEIEYIELEYRDLYTNSVELRSLSKKDFKIIDNPKSFLKKDQSVLKSHSNDFEEGSTIRYLAVTLQDIGFYQIKKIVDSKKLNLKIHQSHLVVPYCPIASITGTGSNDRCIGDSDNVSFEIQGVPPMKLAYSKIVNGQTFSYVDSSLQPEYFESPLQSSKSKQSFTQGELNDLKWGRNQPVNINLDSSITQDGKFAYKIDKITDGLGNVVDFTSLPEELKKRYDLSYNFNVHEVPRAALEERFDPKSPTKRSIAIVFEEIKNWISDIPYVISLSYTDAQDKSKKIMNVTTDSLTKVLQADLPGSYNLEYIESKFCPGEIVGKSNVLVTMPVAPTMEVKSFPILDQCVGQVGLNFELSFTGAPPYYYNTKIYKLENGERKLYDAKRYTSEGTRNRFSYSPPKEGNYEIVFDTVSNKLFTEPIKLEPVKEYTFKTSMRVKPSASLKLHHDLKLCLGDHSSVPVALKGQGPFTLTYDIIETFSSKRKTFEIKEIKTNEYVIKTPVFTTGGDYILSLVSIKDSTGCVVGLSQPDAKIQVRRDIPSAAFNFFEPIKEAKIKHGSVTEIPLKLSGEGPFTVKFKHMDYDGNIVKEFENKFQNSYKPALKVSKEGLYQLVDIRDSSCQGNVIYRNSLYKVSFLEKPKFAIQDNHHITKVTENLFSKEEVCQGMEGTVDLALFGSPPFILEYDLMAPNGHISTKKIQVATKYASLKLPNQIPGEYITTIKAIFDGNYGESDIHFREHQSELIIKQTVHPIPDVAFADGGKTLRACAANVDQISFLEPINLKFLQGESPFSITFSVYHESTSRTDQYTIDNIDSENFSFEKLYEGMKLGNHAITIDSVVDANGCVNSLISGPRNQILVSITDAPKIHILDPSTEYCVGDYVAYQLNGVAPFMIKYEFNGIPLKSKERSSQFVRLASEPGIISITSLQDSSSQCIVDFTNPKLKSEFDDLSLNIHPIPSVTVSQGNYVTEDIREGDQAEVIFSFEGTPPFSLTYVRTEETDGKHGKRRSQVVETHKVTDIYSHEYKVITSLQGTYEAIEITDAYCFAKNDLFFNN
The following text describes a protein:
Function:
Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Domain:
The selectivity filter, in which calcium ions are arranged in single file, is composed of two acidic rings separated by one helical turn along the central axis of the channel pore.
Sequence:
MASLLVVRNLKHVLCRECNANCSSKVLKQLFNNNFMLRSACSQSKYFSVCSIKVLNFNPKYKQAHHATTTAYYTTSAHESNRDFYVPDKSTIDGYIKLKNEQGLCLIAVPLYSREEVCRIVLKPLMNTLNDLMNNIRIEDAGVQKIRAFTLEGDLISNNTSIADLLKNDFILQMNELNYMVQLNGLDFSSPYIEGDSVKNLVAQLYMAINSDEVFIKRQEKLMERLEGLQLELLPMEKVVSDMKDLAARKTRIMSWVGLSMMGLQFGILARLTWWEYSWDIMEPVTYFVTYGTIMAMFSYYIITNQEYIYPDVHDRQVVRLLHKISKKGEFDLVRYNYLCDEVSKIKYDLRRLRDPIKLQLHPPHIGANVTSLPSL