lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MTETLLVYALAIVLAWPLGRYLAAVMRGAPMRGDAVFGWIERPLYAALGTRPQQGMSWRGYVAAFLLSNLVVGVLTWGVFMTQAWLPFNPDAIPNMRWDTALHTMVSFLTNTNQQHYSGQAQLSYLAQMTGIVGLQVVTPMMGLALAVATLRALFGGRAVANANDVAATASGPHSTALQDATASLATHETQPSIPAGAPLPDADVGNYWADVIRASVRVLLPLCLLWTLLLGWQGVPSTLQGAATATPLDSSAGMATQTIPVGPVAAMVAVKQLGTNGGGWYGPNSSVALENPTPLSNLLETLALVLLPMSVVFMVGYLTRRKRLTALVFGTMLLMSAASTGLLLWSEAHSVSAASPALMEGKEVRIGADASALWAALTTQTSNGSVNAMHDSLSPLSGLVTLVDMLINAIWGGVGCGLQQFVVYLLLSVFLAGLMTGRTPELFGRKIEAREVQLLALLILLQPLVVLGFTAVALSVPAWTANSNPGFHGISQVFYEYTSAFANNGSGFEGLGDATYWWNLSCAVVLALGRYPALILPLMVAARMATKRRAPESSGSLQIETPTFALTLMAIVLVLTVLQFMPALVLGPIAEHLALAAS
The following text describes a protein:
Function:
Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MEEQEKRTTEPMQEEEIKKKEEEELKKKERNEHRNYPPLLKIYPIENYQIDKKEKLDKLKHQTFGYQMDQLKISVEKNHVPRTSVYGVILVHKNNFPHLLVLQSNLSMDLKDEIHLVGGRLKIGEDDPVEGLKRKLRKKMSMEYITHYEIGELLGTFYRIEYDKNLYPYIPVHVSQVKEIINIYMIHLVEKCDFKIFDTDKLSSIPLFALHNNFEKYNITLCSIPTLVSRYLMIYG
The following text describes a protein:
Function:
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. Specific for fully assembled 70S ribosomes.
Subcellular Localization:
Cytoplasm.
Sequence:
MKLQLVAVGTKMPDWVQTGFTEYLRRFPKDMPFELIEIPAGKRGKNADIKRILDKEGEQMLAAAGKNRIVTLDIPGKPWDTPQLAAELERWKLDGRDVSLLIGGPEGLSPACKAAAEQSWSLSALTLPHPLVRVLVAESLYRAWSITTNHPYHRE
The following text describes a protein:
Function:
Component of the heterodimeric BagAB ATPase complex, whose two subunits are actively involved in ATP hydrolysis. The ATPase activity is required to mediate resistance against nitric oxide (NO) and elevated levels of glycerol.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Domain:
Binds nucleotides asymmetrically. The two ATPase domains of BagAB are spatially separated by the large central cavity and they do not physically interact with each other.
Sequence:
MVATTSSGGSSVGWPSRLSGVRLHLVTGKGGTGKSTIAAALALTLAAGGRKVLLVEVEGRQGIAQLFDVPPLPYQELKIATAERGGQVNALAIDIEAAFLEYLDMFYNLGIAGRAMRRIGAVEFATTIAPGLRDVLLTGKIKETVVRLDKNKLPVYDAIVVDAPPTGRIARFLDVTKAVSDLAKGGPVHAQSEGVVKLLHSNQTAIHLVTLLEALPVQETLEAIEELAQMELPIGSVIVNRNIPAHLEPQDLAKAAEGEVDADSVRAGLLTAGVKLPDADFAGLLTETIQHATRITARAEIAQQLDALQVPRLELPTVSDGVDLGSLYELSESLAQQGVR
The following text describes a protein:
Function:
Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity; Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex); Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
METLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESAHFTRKNLAEYLRSRTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVFKKCIAEIQKRLVVNLKNFTVAVVDKDGVRDLEPISAASLAA
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Sequence:
MARSEARRLRTWRGRSLDKRAESVEIRSASKAYGAVRALDDVSLNVGAGEFVSLLGPSGSGKTTLLGILGGFILPSSGTILFGGRDVTYMPPHKRDIGVVFQNYALFPHMSVGENVAFPLRARHLPKASWPNKVRAALAMVGLAGYEERGIAQLSGGQRQRVALARAMIFEPRLILMDEPLSALDKQLRESMQIELRALHRRIGATIIYVTHDQREALTMSDRVAVMKDGRLIQIDEPARLHDHPADSFVASFIGEATMLPVRRVDASSVALGSALLRSARAIPDGDALMLAVHSEKLLIDDGAQDAACNRLSGTVTDIVYQGESLRIFLALEGGVALSLRQPSYHQAYSRIPPLGGSLTVTLHPEDTIVVPRVGD
The following text describes a protein:
Function:
Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase. Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit.
Sequence:
MAAALFSSNGEEAIGRNIDIGQDDIQSSPEKDLGEFYEIEKTVEFIQRNAAQKVALQFPDDLLLDSVKVARKLEEATGAKTYILGDTSYGSCCVDEVAAEHVKANVLVHYGRACLSPCCRLPVSYVFGRKAVNMDLCAEAFLSHYRDTESHVVVLSDVVYDHALGELAKRIRSAYPNVIFSKLTSCGETASPDEIVKFGRRFSPDLRLWPESYGIFYVGGEGSTLNNLMLTWPRCSFFSFNPFTGEGRTEGLHVNRALMKRFYLIERARDAHVFGILVGTLGVSDYLSALKHLKNIIHLAGKKSYMFSVGKLNPAKLANFPEIDVFVLVACPENSLLDSSEFYKPVVTPDEMEIACNPAREWHGYCITNFRELLPGGSAYVEFPETDPSDAHHTDVSLITGNLRSSHLTVAETLEKDSDTSLVQRNSKTALAQMSSAASYLASRSWQGLDKALGQTPVVKAVEGRKGIAIAYEDEICS
The following text describes a protein:
Function:
Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. May be involved in the regulation of some light-responsive genes (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MNWLPEAEAEDDFKGLLSGDFFDDLINHLDVPLDDIDTTNGEGDWVDRFQDLEPPPMDMFPTLPSDLTSCGSGMAKAPRVDIQRNIPALKQSYSSEALSSTLHQSSAPPEIKVSKLFQSLSPVSVLENSYGSLSTHNNGSQRLAFPVKGMRSKRKRPTTLRLSYLFPSEPRKPEKSTPGKPESECYFSSEQHAKKKRKIHLTTRTVSSTLEASNSDGIVRKCTHCETTKTPQWREGPSGPKTLCNACGVRFRSGRLVPEYRPASSPTFIPAVHSNSHRKIIEMRRKDDEQFDSSMIRAVISRG
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAPSATDTNWSVDFDTIRRHQLFKNPPKDHTAFPSLAAAIRPHLDSFNALFEGSKVIEAGLKDIGIKTFLDGDAETPEERRARKAEGRRPPKRNRLNVRIREIFLEKPAIPATNKFATRNRNIYPSEARERHATYRGKLRARLEYQVNNGDWMESIRELGQVPIMLRTNRCHLEKATPQELVQHKEESEELGGYFIVNGNEKLIRMLVVGKRNFPMAIVRSSFVRRGHTYTKFGIQIRSVRPDQTSQTNVLHYLSDGNVTFRFSWRKNEYLIPVMMIMKALVETNDREIFEGIVGSATSKGVNNTFVTDRVELLLRTYKAYNLHTRSSCRAYLGEKFKPVLGVPADMSNEDAGTEFLRKIVLPHLGNQNVTEIQDYDKFKLIMFMIRKLYALVAGDCAPDNPDAVSNQEILLGGFLYGMILKEQLEEWMRSFGPILRDWSNRNGGAKFTDPAFERDFLSKIVKRTNENIGGKLEYFLSTGNLVSPTGLDLQQVSGYTVMAEKINFYRFISHFRMIHRGSFFAQLKTTTVRKLLPESWGFLCPVHTPDGAPCGLLNHLAHKCLIATSDVNVSHLPKLLVQLGVRSESSVALEDSVTVQLDGRIVGYCSPKQARMIADTVRHWKVSGTHNIPRELEIGYVPNSNGGQYPGIYMFSQAARMYRPVKYLPLDKLDYVGPFEQPFMEIACLPDDLVAGVSTHIEYTPTNILSIVANMTPFSDYNQSPRNMYQCQMSKQTMGTPSTAIEYRTDNKLYRLQTGQTPIVRPPLYNAYGLDNFPNGTNAVVAIISYTGYDMDDAMIINKSSHERGFGYGTIYKTKIHSLDDKDSRRSKSRREITKLFGFAPGGEIRAEWRTTLDEDGLPHVGARVKEGSLIAAWHTVRYDAASDSYVNVDGITHFVKYKDAEEGYIDSIRIMGAETGLEPCQALSVKYRIPRKPVIGDKFSSRHGQKGVCSQLWPAVDMPFSESGIQPDLIINPHAFPSRMTIAQMIESMAGKAGALHGHPQDSTPFQFSEENTAADYFGQQLRKAGYNYYGNEPLYSGITGKEFAADIFIGVVHYQRLRHMVNDKFQVRTTGPVNQLTGQPVKGRAKGGGIRVGEMERDSLIAHGAAFILQDRLMNCSDSQRAWICRDCGSFLSTQVAVSSAGSSKARLAASAAAAAKNAFAQQSGAPGIVRCRRCAREAVFEDSRAVVWEDGDGRRYVGGDNVTIVAVPGVLRYLDVELAAMGIRMKFWVDN
The following text describes a protein:
Function:
Chromatin reader component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. YEATS2 specifically recognizes and binds histone H3 crotonylated at 'Lys-27' (H3K27cr). Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors.
Subcellular Localization:
Nucleus.
Sequence:
MSGIKRKIEDKDPDYEDISVVHENKRQKAVEQNARDATIQKIEAIIKDQFSLELKNKEHEIEVIVQRLNEARRMMDKLRACIVANYYASAGQPKVSEGAKSDPSVFNHPAIKRFLESPSRSSSPLNQGSETPSLVPSETESLTQLSEGLDREGESSWKEPSKQERRPGRNTGKDTFGVSAPQEQDQRFTFLTTGEDSSRLYVKKTIVVGNVSKYIPPDKREENDQSTHKWMVYVRGSRKEPTIDHFVKKVWFFLHPSYKPNDLVEVSEPPFHLTRRGWGEFPVRVQIHFKDPRNKRIDIIHHLKLDRTYTGLQTLGAETVVDVELHRNSLGEDFFPFPCSSSRQPASAQPDTPSSAPQTPGPSAGRSSSPVRLTQDSLSTAEKGFPIKSEAGRSTGYTLLSSERTPTRPKATEKITLGSHGNSAFQPITASCKIVPQGQAPNPAESPGKSFQPITMSCKIVSGSPISTPSHSPLPRTPTSTPVHMKPASSVINNPYIIVDKPGQGIGMASSAAGSPTGKQSSSPQVSQGARSPAPKVHGTSFITSGVKEESLFAAMPPLCPIGSQSKVQSTKPLSGGLGAFTKVIIKQEPGEAPQQQQQQQQQQMLVSTATSQQPAQQFVAVKGGHMIAVSPQKQTSAAGAGATQNKVVGIPVGSALQSAVKQAVAISSGQILVAKSSPAASKVMGQKQVIAQGVAKAIVSGASGTIVGQSVQTVTKAQSSSAGTAKTGGQGSVMATLQLPANNLANLANLPPGTKLYLTTNSKNPSGKGKLLLIPQGAILRASNPSGQQSQSATTTSGGGSQTPTSSSLPQNLSCTSYILKQTPQGTFLVGQPAPQGSGKQGAAGSSGHSVSSPSSITQQAIRVTAGQKAAILAQVVGGTQGPTVKLSDGSVKAAHLSKPGTTTLRMTGGVITAASSAGAPAGLATVPAAQQPPEVGSSSLAAPGAKPVVQHPVLVAASQAAVISVAKSASSSAATVAKSAIPAMVTVAKSVNVPVVSIAKGASSAVVSVPKSASPSLVTAASLVTSGTTVSGKTAATLSGMLKIHSGQSNTQQAVLTIPANQLKQLGVSTATGGVQTILMPVSKVVQSSSVTKVAGAGVGPTAASTPSTVPSGSAQHPPLTSTAQVKTEPGVAGPSTSSAAVPSVTAPMTVKVEQGTEIPHEYINTDHVENLHQLLTAVVKKIPLIVPEKTEDSSAFCAVSLEQYYSWNIGKRRAAELQRAVAVKKAVQEVIEKLPKFSSIAPPKTKQVMQWCRQRGYTPPDLEPRRTEEDSIEDILTQIDNEPECPSTLYGAGELCQRLEELQRLLKTEPEEEEEILDIVSVKEPVKVEIKMEEEELNQESKFYIGASPSAQFIRDCAQQIGVPFQQVEVEKNVYAPAVEEMILKATEQLASEVLREALAVAYKKSPQNRVPREITAMNIHQAVSTIPACDFLTNKHMGVLIKEGHAD
The following text describes a protein:
Function:
Catalyzes the oxidation of sulfite to sulfate, the terminal reaction in the oxidative degradation of sulfur-containing amino acids.
Subcellular Localization:
Mitochondrion intermembrane space.
Sequence:
MLLLRRCHGLTRFGHVHIQSRHHLPPAVLSHAARLCSTHDNTSHRHLSGFSWKHGLAGLLAGAGAVIAFGLHRHEAEHPAAAAAAQTAESSSSLPVFGQEEVSKHRSLSEGVWVTFRGGVYDITDFVAMHPGGEKILLAAGGALEPFWALYAVHNQEHVLEILSEYKVGELCAEDLKKQEPAESSDPYSTDPDRHPVLRVNSLKPFNAEPPPEILTDSYITPSAFFFKRNHLPVPQVDPASYQLQVEGLPGGAVTFSLEDLKTRFPKHDVTATVQCAGNRRSEMDREKQVKGLSWGISAISNAKWSGARLRDVLLAAGFGPDVAQWARHVHFEGLDKDVTGAAYGASIPLNKAVSEEGDVLLAYEMNGEKIPPDHGFPVRVVVPGVVGARSVKWVGKIAVSAEESSSHWQQYDYKGFPPGTDWNTVDYKSAPAIQELPVQSAITSPADGALIDSSDGFLTVKGYAWSGGGREVVRVDVSLDGGQTWQVAKLRSSDEAHEAPPPPGRAWAWKLWELTAPLPPPAQELEIICKAVDSSYNVQPETFPPIWNLRGLLSNAWHRVTVKIIEG
The following text describes a protein:
Function:
Catalyzes the 2-beta-hydroxylation of several biologically active gibberellins (GAs), leading to the homeostatic regulation of their endogenous level. Catabolism of GAs plays a central role in plant development. In vitro, converts GA12 and GA53 to the corresponding 2-beta-hydroxylated products GA110 and GA97, respectively.
Miscellaneous:
MISCELLANEOUS: Plant overexpressing GA2OX5 exhibit an extremely dwarf phenotype.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MEEHDYDSNSNPPLMSTYKHLFVEQHRLDMDMGAIDVDECELPVIDLAGLMEAEQVCRADMVRAASEWGFFQVTNHGVPQALLRELHDAQVAVFRRPFQEKVTERLLGFSPESYRWGTPTAKCLEQLSWSEAYHIPMTTPRPSTSIRARAVIEEVSRAMYELAQKLAEILMRGLPGAGEGETMVTTREETCFLRLNRYPPCAMAMGGFGLCPHTDSDLLTIVHQQQDTVGGLQLLKGGRWVAVKPSPSTLIVNVGDLLQAWSNDVYKSVEHRVMANATLERFSMAFFLCPSYHTLIIPSSSHVHDDDAHYRSFTFGEYRKQIMEDVRSTGRKIGLHRFRTR
The following text describes a protein:
Function:
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MKKINKIVLAVGGTGGHIIPALAARETFIHEDIEVLLLGKGLAHFLGDDSEVAYCDIPSGSPFSLRVNRMFSGAKQLYKGYVAALQKIRDFTPDLAIGFGSYHSLPAMLASIRSRIPLFLHEQNIVPGKVNKLFSRFAKGVGMSFAAAGEHFHCRAEEVFLPIRKLSEQIVFPGASPVICVVGGSQGAKILNDVVPKALARIRESYSNLYVHHIVGPKGDLQAVSQVYQDAGINHTVTAFDHNMLGVLQASDLVISRSGATMLNELLWVQVPAILIPYPGAYGHQEVNAKFFTHTVGGGTMILQKYLTEESLSKQVLLALDPATSENRRKAMLSAQQKKSFKSLYQFICESL
The following text describes a protein:
Function:
Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSDKPDMAVIERFDKWKLKKTETHEKNPLPSKETIEQEKQAGES
The following text describes a protein:
Function:
Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos.
Subcellular Localization:
Nucleus.
Sequence:
CNCPYCQENERLAATGQPVPRRKAQHICHIADCGKVYTKTSHLKAHLRWHSGERPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFVCKVCSKRFMRSDHLSKHMKTHNNPKRGNAA
The following text describes a protein:
Function:
Microtubule-associated protein that mediates the formation of a mesh-like stable and dense network formed by individual microtubules (MT). Confers MT resistance to high concentration of NaCl.
Subcellular Localization:
Nucleus. Cytoplasm. Mitochondrion. Cytoplasm, cytoskeleton, phragmoplast. Note=Associated with mitochondria. Binds to MT in preprophase band, during anaphase, and in phragmoplast.
Sequence:
MLEIGSPNALFFRTNTTCNNLLRELQKIWVEIGETETEKDRMLMELERECLQIYQRKVDEAANSKAKLHQSVASIEAEVASLMAALGVLNINSPIKLDKGSKSLKEKLAAVTPLVEELRIQKEERMKQFSDIKAQIEKISGEISGYSDHLNKAMNISLTLEEQDLTLRNLNEYQTHLRTLQKEKSDRLNKVLGYVNEVHALCGVLGVDFSQTVSAVHPSLHRTDQEQSTNISDSTLEGLEHMIQKLKTERKSRFQKLKDVVASLFELWNLMDTPQEDRTKFGKVTYVVRSSEANITEPGILSTETIEQVSTEVDSLSKLKASRMKELVMKRRSELEDLCRLTHIQPDTSTSAEKSTALIDSGLVDPSELLANIEMQINKIKDEAQSRKDIMDRIDRWLSACEEENWLEEYNLDENRYSAGRGGHVNLKRAERARVTINKIPGMVDTLIKKTLVWEEDMQKSFLYDGVRLVNILEDYKLTRKQQEEEKKRYRDQKKRQDLLLTQRESIYGSKPSPRRSSSFRKPNGFNISNGNGSVPPTPRRGSVGTTTPDVLLTPRSYSGHHRQNGYFKEVRRLSTTPLNYVAMQKEDTVSTTYTSIYSSEPDSPLQG
The following text describes a protein:
Function:
Cell wall formation.
Subcellular Localization:
Cytoplasm.
Sequence:
MAKIAVFFGGSSTEHSISILTGCFICKTLHTMGHSVKPILLTKDGGWVVPSEYRMSIPFEVSNSPDLFQEEFQKRYGVSRTNQIFSLDADIVFLGLHGGQGEDGTIQGFLEILGIPYTGSGVLASAIAMDKTRANQIFLQSGQKVAPFFEIDKLEYLNSTDAVITKLETLGFPQFLKPVEGGSSVSVYKITNREQLKEKLALIFESDSKVMSQSFLTGIEVSCGVLERYRDGKFKKIALPATEIVPGGEFFDFESKYKQGGSHEITPARISEQEMKRVQELAIAAHRSLGCSGYSRTDFIIVNGEPHILETNTLPGMTETSLIPQQAKAAGISMEEVFSDLIEIGLKRSLY
The following text describes a protein:
Function:
Responsible for the transport of C4-dicarboxylates.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MVSVEIIFSSLNEVIIMIWVELAIVLLFIFIGARIGGIGIGLAGGAGVIALSLILGVPTKQAFIPVDVILIIMSVITAIAAMQVAGGMDWLVQLAENFLRKHPERITFYAPIVTFLMTLMAGTGHTAFSTLPVIAEVAKGQGVRPSRPLSIAVVASQIAITASPISAAVVAFAAMLVPFGVDYLTLLAICIPTTFAACMVGAFVANFMGSELKDDPIYQERLAQGLIKLAGTQKREILPTAKTATYIFLTAIILVVCYAAAISNSIGLIENPALGRNEAIMTFMLAAAAGIVLLTKIDAAQIPAASTFRSGMTACVCVLGVAWLGSTFVNAHVDGIKEVAGTLLADYPWMLALVLFFASMLLYSQGATTVALMPAALAIGVAPLTAVASFAAVSALFVLPTYPTLLAAVEMDDTGSTRIGSYVFNHPFFIPGVVTIASAVAFGFLFGSLFI
The following text describes a protein:
Function:
Mediates cotranslational and post-translational transport of certain precursor polypeptides across endoplasmic reticulum (ER). Proposed to play an auxiliary role in recognition of precursors with short and apolar signal peptides. May cooperate with SEC62 and HSPA5/BiP to facilitate targeting of small presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen. Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAGQQFQYDDSGNTFFYFLTSFVGLIVIPATYYLWPRDQNAEQIRLKNIRKVYGRCMWYRLRLLKPQPNIIPTVKKIVLLAGWALFLFLAYKVSKTDREYQEYNPYEVLNLDPGATVAEIKKQYRLLSLKYHPDKGGDEVMFMRIAKAYAALTDEESRKNWEEFGNPDGPQATSFGIALPAWIVDQKNSILVLLVYGLAFMVILPVVVGSWWYRSIRYSGDQILIRTTQIYTYFVYKTRNMDMKRLIMVLAGASEFDPQYNKDATSRPTDNILIPQLIREIGSINLKKNEPPLTCPYSLKARVLLLSHLARMKIPETLEEDQQFMLKKCPALLQEMVNVICQLIIMARSREEREFRAPTLASLENCMKLSQMAVQGLQQFKSPLLQLPHIEEDNLRRVSNHKKYKIKTIQDLVSLKESDRHSLLHFLEDEKYEEVMAVLGSFPYVTMDIKSQVLDDEDSNNITVGSLVTVLVKLTRQTMAEVFEKEQSICAAEEQPAEDGQGDTNKNRTKGGWQQKSKGPKKTAKSKKKKPLKKKPTPVPLPQSKQQKQKQANGIVGSEATVKEDEEEVSDKGSDSEEEETNRESQSEKDDGSDRDSDREQDEKQNKDDEAEWQELQQSIQRKERALLETKSKITHPVYSLYFPEEKQEWWWLYIADRKEQTLISMPYHVCTLKDTEEVELKFPAPGKPGNYQYTVFLRSDSYMGLDQIKPLKLEVHEAKPVPENHPQWDTAIEGDEDQEDSEGFEDSFEEEEEEEEDDD
The following text describes a protein:
Function:
General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
Subcellular Localization:
Nucleus.
Sequence:
MAAAEAAAEAAAALEGSEPVDLVKHPSGIIPTLQNIVSTVNLDCKLDLKAIALQARNAEYNPKRFAAVIMRIREPKTTALIFASGKMVCTGAKSEQQSKLAARKYARIIQKLGFAAKFKDFKIQNIVGSCDVKFPIRLEGLAYSHGAFSSYEPELFPGLIYRMKQPKIVLLIFVSGKIVLTGAKVRDETYTAFENIYPVLTEFRKVQQ
The following text describes a protein:
Function:
Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane protein substrates in or close to their luminal transmembrane domain boundaries. Acts like a sheddase by mediating the proteolytic release and secretion of active site-containing ectodomains of glycan-modifiying glycosidase and glycosyltransferase enzymes such as MGAT5, B4GAT1 and B4GALT1. Plays a role in the regulation of cellular glycosylation processes. Required to link T-cell antigen receptor (TCR) and calcineurin-NFAT signaling cascades in lymphocytes by promoting the association of STIM1 and ORAI1 during store-operated calcium entry (SOCE) in a protease-independent manner.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus. Membrane; Multi-pass membrane protein; Lumenal side.
Domain:
The first transmembrane domain may act as a type I signal anchor. The catalytic loops is exposed toward the lumen. The PAL motif is required for normal active site conformation. The catalytic domains embedded in the membrane are in the opposite orientation to that of the presenilin protein family.
Sequence:
MAEQTYSWAYSLVDSSQVSTFLISILLIVYGSFRSLNMDFENQDKEKDSNSSSGSFNGNSTNNSIQTIDSTQALFLPIGASVSLLVMFFFFDSVQVVFTICTAVLATIAFAFLLLPMCQYLTRPCSPQNKISFGCCGRFTAAELLSFSLSVMLVLIWVLTGHWLLMDALAMGLCVAMIAFVRLPSLKVSCLLLSGLLIYDVFWVFFSAYIFNSNVMVKVATQPADNPLDVLSRKLHLGPNVGRDVPRLSLPGKLVFPSSTGSHFSMLGIGDIVMPGLLLCFVLRYDNYKKQASGDSCGAPGPANISGRMQKVSYFHCTLIGYFVGLLTATVASRIHRAAQPALLYLVPFTLLPLLTMAYLKGDLRRMWSEPFHSKSSSSRFLEV
The following text describes a protein:
Function:
Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. Also plays a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation. Participates as well in T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Note=Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.
Domain:
The coiled-coil domain is required for the induction of autophagy during endoplasmic reticulum (ER) stress; The RING-type zinc finger is required for auto-polyubiquitination; The C-terminal transmembrane domain is indispensable for the localization to the ER.
Sequence:
MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGLLEGNVRNSLWRPSPFKCPTCRKETSATGVNSLQVNYSLKGIVEKYNKIKISPKMPVCKEHLGQPLNIFCVTDMQLICGVCATRGSHTKHVFSSIEDAYTQERDAFEFLFQSFETWRRGDALSRLDTLETNKRKSLQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQTYDPEINKLNSILQEQRMAFNIAEAFKDVSEPIIFLQQMQEFREKIKVIKETPLPPSNLPTSPLMKNFDTSQWEDIKLVDVDKLSLPQDTGVLTSRSPWHPCLLLMAVVLLGLLVFFGPTVFLEWSPLEELATWKDCLSSFNSYLTKSADFVEQSVFYWEQMTDGLFVFSERVKNVSLVALNNVAEFVCKYKLL
The following text describes a protein:
Function:
This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
Subcellular Localization:
Nucleus.
Sequence:
MSVNAIDSNGVIVNLVLRSNNFNSYECPFEQTMGIDLDRMYNVFQLCGHDDSLTLESVRDYAVKLIFTSPDRDTIATAQLNLVSDFLWTDFVIKDTEPYATVRMPSSGLESMCKMLIVASDTIIISVTKEQVKFSIICDTGAIDYTFVQRTVPADKPEDETVIQMHETMEPVSMMVDLEYLKVFTKATLLSKTVTLKFCPDDNLVVVYQIPRFGFLKFCMPKE
The following text describes a protein:
Function:
Probably involved in the RNA silencing pathway and required for the generation of small interfering RNAs (siRNAs).
Sequence:
MVTSSSYLICSNQASLHSEIALSSSVETVLKRIYGKHNHPPIKAETRRRLSSIPNEMALETLSKVFNVDYVKGTLDGFIKYLLDQTVSSVYGSPLQCSGESPVLSPRTPGKKCCRKAIVGAEMSLLDYEVPSPKSMKLEVNGGSSLHIPPQLLALSELEFRKAFLLLSYIPGKHLGQVNITAEEIRQWKDLSMVAYEAAVWDRLGRHSCPSTDRRVSLQWDSGNTHYYQCHVSPDGSYRFKGPLMENTGTHLHNVLGDENVLTVKFADVPGEATYCNDIYSTYKEIAKKGIMLGLRRYQFFVFKDGGKEEKKKDFSGKGVKCYFIRTDSTSSNDMGKPYIFSGKSIHEARMHFMHVHTLPTLAKYMARFSLILSKTRKLEVDTSRIAFQQIDDIHCHDQNNNDVLDKNQKPCIHSDGTGYISEDLARMCPTDIFKGKHVRSDNMQANTYGKEPPMLIQFRMFHYGYAVKGTFLLNKKLPPRTVQVRPSMVKVSEDPALYNFSTFNSLEVVTTSNPPRRTKLSRNLVALLSYGGVPDEFFLDILRSTLEESKTVFDNKRAAVRAARNYGDMDEYNALQMIMSGIPLDEPHLKDHLSILLNTEKNDLKAGKLLVTESYYLMGTVDPTGKLKQNEVCVILESGQISGDVLVYRNPGLHFGDIHVLKATYVKALEEYVGNSKYGVFFPQKGPRSLGDEIAGGDFDGDMYFISRNPKLLEHYKPSEPWVSSSPPSKIYTGRKPSELSPEMLEEELFRLFLKARFHSSNVIGAAADSWLRIMDQFLTLGDDRVKETAERKSKMVKTMLKAIDIYYDALDAPKNGAKVDLPLDLKFDSFPHYMERKNKKIFKSTSILGLIYDTVVSQNEEEPPPCEIKKLQCFEDELVPEFYMEKCSRWYQEYKTEMSQAMDENNKKESASEVILKYKQEFYGAAGFEESKKSLEELYLQALALYNIVYDYAIIKNKVRSCGFVWKVAGPVLCKLYLKKAEEKSIPCSVSVLKELWG
The following text describes a protein:
Function:
Serine/threonine-protein kinase component of the sperm flagellar doublet microtubules. May act as a regulator of sperm motility by mediating phosphorylation of sperm doublet microtubule proteins. Plays a role in DNA condensation during postmeiotic chromatin remodeling and histone-to-protamine transition during spermatogenesis.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme. Nucleus.
Sequence:
MSKSSGGDRWLSELGYKLGQTLGEGSYSKVRVATSAKYKGPLAIKVVDRRRAPPDFVHKFLPRELSILRSIRHPNIVRVFEFIEVCNGKLYIVMEAASTDLLQMVQQLGKLPCTPEARDIFAQVVSAVRYLHDRNLVHRDLKCENVLLAADGRRAKLTDFGFGRESRGYPDLSTTYCGSAAYASPEVLLGIPYDPKKYDVWSLGVVLYVMVTGCMPFDDSHIHSMPRRQKKGVFYPEGLPKLPEPCTSLITQLLQFSPASRPGVGQVAKNSWLKGGNLNRDTSYRQLKGQQLEF