lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May be involved in induction of apoptosis in CD4(+) T-cells, but not CD8(+) T-cells or hepatocytes.
Subcellular Localization:
Secreted. Note=Secreted by hepatocytes.
Sequence:
MAAPRGRAAPWTTALLLLLASQVLSPGSCADEEEVPEEWVLLHVVQGQIGAGNYSYLRLNHEGKIVLRMRSLKGDADLYVSASSLHPSFDDYELQSATCGPDAVSIPAHFRRPVGIGVYGHPSHLESEFEMKVYYDGTVEQHPFGEAAYPADGADAGQKHAGAPEDASQEEESVLWTILISILKLVLEILF
The following text describes a protein:
Function:
Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand-activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane.
Subcellular Localization:
Cell membrane. Late endosome.
Sequence:
TAIKLTDSVTLQNDKEKIDPRGRTPLMLAVRLANLPCVKCLLAAKCNATYEYEGWSIVQEAVCTGDVDILTAIIEVRDLQRHVQRVTHVPKLLQHLLDAPDFYIEMKWEFTSWVPLMSRLCPSDTYKVYKRGANVRIDTTLLGFDNNTWQRGNRSYIFKGAKETATMIEIDHDTNEVMVEEMSSDIGDIVAIPPALGTVRARLNAPVITNNIEMDKISFERNKCGIWGWRSEKSEMINGYNCKVYGASNVEFVTKTRMDHLSEEQIKNKTARTPLHSLLGIADEDYVSPADAAAALKDRTPSPRLEEASNAGVENGGRNSPAPGNQSNGSSAGASGTSTPKSSVTPEEYFTQEFDLHGRDVGGPKNLSTKVQRFRANLWLAEEHPIRLQEQVLPILDLMSTMASPHVSKLRDFITMQLPAGFPVKVEIPLFHVLNACITFGNVFALTTPVDHVATLQEQDRVTCLVDDRCFDIPAHYTNRGSDVRRQIPLDEDDMLQYAIEQSLVETSGACGVDARDDDKVDIWEVLRGQNVVGSDLLPEDDEQLQRVLQESLLGAHANLQSGSPASDEDDDGGFRYVDPDLAMAMRLSQQEQRKFELERQQEQEMIEQALKLSLQEH
The following text describes a protein:
Function:
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
Sequence:
MSLLDFFRSRKSQNSASIAKERLQIIVAHERGQRAQPDYLPQLQKDLLEVIRKYVPIDQEQIQVELENQGNCSILELNITLPDR
The following text describes a protein:
Function:
Probable transcriptional factor. Binds to the promoter of the SQUAMOSA gene.
Subcellular Localization:
Nucleus.
Sequence:
MESWSYVSGGKGFVSEESVSVDDGITPCSWSQQGVKNQQVGSQIRDVFGGEDESSSNHSSSTYSKDSSLIDLKLGRGRFLDAKNFNLSSTKRNRAGGLTSFCQVQGCGKDLTSCKDYHKRHKVCEIHSKTAKVIVNGIQQRFCQQCSRFHLLAEFDDGKRSCRKRLAGHNERRRKPHTGLHSGRAGKHFQPFSGTRFQSSSFATSSFICQDILGGSLLHQPKHDMHDWYKNVKVEHCSNYSPQLTRPFTNKHSQPRPHFTSYHTDKHCPALHDEGITTITRSKNNESSNSYLNDIGGSDFVSRSLFHSTSIGSEVLNVMDSASPFQGISNSGCALSLLSSQSQDTSNYSSVVPPSAHHLITPRSNTHYNMTQTSECFPGASPKGSASTVSNIYNLSEVISAEGHLEQMLRNNCGSLQGSDYVNTRNLLSCEDGTTIDLLQLSSQLHQVEHQRHSMK
The following text describes a protein:
Function:
Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development (By similarity).
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
MASKSWLNFLTFLCGSAIGFFLCSQLLNILLQEQADVQPNMLHNDPHARHSDDSGHNHLKGQMDFNADSSQHKDENTDVAENLYQKVKVLCWVMTSPQNLEKKAKHVKATWAQRCNKVLFMSSEENKDFPTVGLETKEGREQLYWKTIKAFQYVHDHYLEDADWFMKADDDTYVILDNLRWLLSKYNPEQPIYFGRRFKPYVKQGYMSGGAGYVLSKEALRRFVDAFKTEKCTHSSSIEDLALGRCMEIIKVEAGDSRDPTGKETFHPFVPEHHLIKGYLPKTFWYWNYNYYPPVEGPGCCSDIAVSFHYVDSTTMYELEYLVYHLRPYGYLYRYQPALPENILKEINQVNKKEDTKIKLGNP
The following text describes a protein:
Function:
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
VIFNHLIPDHQSDGFQSPYKLIPTNSTLLDKIVDYTLGGFARWDGQYFLHISTLGYTHENCLAFFPAYPLLLRFTSVCLSFLSCHTLTYWNSTLLGSIIINTVCFIIAAYFLFLITDKLFSNSNFALQTWKLFCISPATIFFLAPYSESLFSALTFGGIYNCIEYKFLTASIFFAGSGLTRSNGLVNIGFLLYFAVKKTFSTKWKGVPTLVAQLVISVFITVFPFLCYQYYAFTLFCFHKPHRLPTVIHSYLMERNFTVRGERIPQWCEQSIPFSYSVIQSQYWNVGFLRYFEWKQLPNFLLAAPILSLVFLYSLMYVKQNFQIVSRYNSFTSGQSQISHPIFRPAAGVFAAHSIFLGLFTFFFAHVQISTRLIGSSCPAVYWSVNNFKKINKFNYTIINHKNLSTTGKCVRFYCLSYVVVGTVMFVNHLPWT
The following text describes a protein:
Function:
Involved in intercistronic processing of primary transcripts from chloroplast operons. The endonucleolytic activity of the enzyme depends on the number of phosphates at the 5' end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences.
Sequence:
MQSAFVEIGLQRAAFLHAADIMECHAEEGDIKKERPIQEVLHEGQSIIVQVIKEAIGTKGARLTTEISIAGRFLVYLPYQKHIGVSQRIDIEEEREFLRNRLLGLLPEEREGGYIIRTMSENATDEELLADIEYLRKVWQKIQAESKKVGERSLIFYDLSLPRRILRDVVCTETTSIRVDSREMFERLKEFAELYVSHAVKPLTHYKGERSLFEFYDIESEIEKALSRKVELKSGGYLIFDQTEALTTVDVNTGSFVSGKNLSDTIFKTNLEAAQTIARQLRLRNLGGIIIIDFIDMDEDAQREAVLEELRKAVTLDRARINVNGFSALGLVELTRKRTRESLAHLLCESCQVCQGRGELKTAQTICYEIMREVLRESKQFKSAKEFKILASPEVINMLGDEESQSLASLSDFIKKPLSLHPDTQYGREEFDIVWI
The following text describes a protein:
Function:
Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.
Sequence:
MYYKVAVSGSGKVLNVFSSEELLIGERVWLNWRNGKVKGYVLERSLSHENEATPSERDGKSFLSEGHVEIAKWVSERFFSPLGMVFDLFFPQGIDDYKEEVVVSESPFLDFDRMTLRDFLENFGEKALKEMVKKGLVRVEKNFYVKEPRPRVKKRLFLKKRISEIIREHLTVKQRMVVEYLQFNDGVPLEELLEDLEVSKSVIETLQRKNIVEIVSGDVFPKKRRILRGDFKGNISKENLFFGPTGSGKTEALFELIDVYSRKGTVLFLVPEVSVLTHTLSRLKGAFPDLKIGIYHSYLSRARKNLEWYKAASGKIDVLLGTRSAVFVPVKNLSLLIVDEEHDESFYQHTRPSYDAIVVARKISEVFDVPIILSSATPDLWTYREAKEGRIRTFNFTRRFGSLSVEVVDMRNEEKIGSFAKKTLDRIEETLEEGKRVLIYVRRKGFWGRVQCEVCGYVLKCENCDVSLVYHSDTHSLKCHQCGREYGLVESCPRCGGRLVGRTAGTERVERELKRYFPTRRIARVDREVVDNIMELESYIDKLIRGEIDILVGTRLITKSLSVPEIGLVCIMDVDSLIFNPDYSSSLRTFQLVVQALGRASRGDQGKAIIQTYNPEDTIIRKALEEDVNGFYAEELERRKALGYPPYRHLIQVAVKSKNPEVGKNSLTSLKEFLKGEEVLGPVEHWVFKLRGFYRHHLIVKTEDLERVLPKLEKALRILGIDAIVRVDPPTLEVSD
The following text describes a protein:
Function:
Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes.
Subcellular Localization:
Nucleus. Note=Localizes to centromeric and flanking chromatin.
Sequence:
MSSKIRPSADDKKLQRVLYFFLERVRAAKDVSGQLLSPLIDNASVDTASVSPSSNGRPTTLKSIQSKIDEFQYHDFSEFVSDLAYLFINVKALYEGTQTYSFVQALEEFCIQQLRTFQQQGYIPVITWPNTDSPSATTSSPISRNPEYSVSPPNGSKFVKNEDEAYDSDLYVEEEDSDVKGRSMVGRDGRYKSEDLKRRKLQPSSKPLSSLEARAKVIMRQVRRYRDGSGRQLFAPFERLPDPRMFPEYYQAIEQPMALEVIQKKLSKHRYETIEQFVDDFNLMFDNAKSFNDPSSQVYRDADFLKNYLADVLRLEAGKLDSEFFNYETDSRASPQLPKNDIQPAVSIDGTLLNVGDWVLIRNPADSSKPIVSQIYRIWKSDDDINYVTVCWYLRPEQTVHRADAVFYENEVFKTSLYRDHPVSEIVGRCFVMYITRYIRGRPKGIRSTPVFVCESRYNDDTKQFSKIKSWKACMPQEVSGSEYEMILFDRPITLTKVASPLLHLLASKSQGLPSPATTDSNTHMLPSQGSLLPPSSISETKSFSTKASTPLSTDDIATPLSSAPNPPSVMPTYARKTSSHSERSSHSSYHNSSHVPTAAFNSPIMRTSTKSTSPIPARPFYAQSGSLQSLNTTQHSHQISGGHSGRMNVPYAKLSYTSHNGRHGGSNGNISGAKTPMTNYTINSMPSLPVFPPAFIVPGTHQKLDESSPVPGIDDVTVINTETAKMLDKDEHQNVLWYTVPPLDPIPLENRNGSLTHSVEYVLYKKSKGSQVITEKARSNELSREAKFENLVASLSDALIPP
The following text describes a protein:
Function:
May be involved in the mitochondrial lipid metabolism.
Subcellular Localization:
Nucleus.
Sequence:
MRVKKPTSKRTTTRMREGIKKKAAAKRRKDKKIAKKDVTWKSRKSKDPGIPASFPYKDKIITELEEGRRIEKERREQLKLQKQQERQEALARGEIVEDDDEMDEDDQEEGDGANGLAALLESAQQAAKDYDGEDYEDNENEDMVDSEEDVEYEISDIEDTQDEEFGELEKSRKAYDKIFKTVVDEADVILYVLDARDPESTRSRKVEQAVLQNPGKRLILVLNKVDLIPTHALNQWLNFLKSSFPTVPVKAAPGATNSTSFNKNLTNSMTSDALLKALKSYASKSNLKRSIIVGVIGYPNVGKSSIINALTNRHGNNSKACPVGNQAGVTTSLREVKIDNKLKVLDSPGIVFPDEIVNTKKQSKTQQLAKLALLSAIPPKQIVDPIPAITMLLKKFSKDTEMADGLKNFYQLPPLPSSDLNEFVKHFLIHIARSKGRLGRGGVPNLESAAMSVLNDWRDGRIIGWTLPKASKSAAGVSSEEVDLDAPKSSLRGEKEPPKVEQTTIVSTWAKEFDLDGLLGDNFGLQ
The following text describes a protein:
Function:
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Sequence:
MTRTSLQCRECKKEYETAFKYICDDCFGPLDVKYDFPTVTKDTFSNREHTYWRYFELLPIENKSNIVSIDAGLTPLTKAENLGKALDLNNLYIKNDSVNPTFSFKDRPAGVAISKAKEFGLSAVGCASTGNLASATAAHAAKGGFPCHVFAPSNIEMAKIAQALSYGANYVAVDGTYDDANRIAAQIGDSRGIGIVNINMRSHYVEGSKTLAYEVAEQLDWNVPDQLIVPVGSGAMLNAICKGFEELQQVSLLDDVSNMHMIAAQPHGCAPVVDAFKKNSKDVIPVENPDTVAKSLAIGDPGDGRYVLKRLEQYNGFAEECNNKEILDAILLLAKTEGIFTEPAGGVSVSVLQKMVEQGKIDKNDKVVCYVTGNGLKATESIMEVLEKPNVLKADISEVSAVVN
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:
MDSEMESREVLEEVQQQPLQAQQPGEAQQPGEAQQLEGEDVDMLLDFISDDDTNDDDCDSDDDDDSDDDITISDLEEPLNLMERQKPYKVMNEADIRINLERDISNISDILSISRSEAVILLLHFKWNVNAVPDEWFANGYKLREVLGLPEDPVDDEAESSYKKDMTCGICLVTFSPDLVASPHCGHVFCHTCWADYIGKSLTDGLPSLLLRCPDTSCRSAVTQDMINMLATNDDKEKYARFLMRSYIEFNPKANWCPSPGCDYAVVLVRGKTTKVTCKCLYSFCWKCNKEAHQPIACAAVCKWVMESVVQTVNWKIATTNGCPNCGTSMDMDAPFKRMQCPSCKIHFCKDCRTSWLHNGLWEGDQYIHTCSEGKEMQVETEDAAEEQKKVAKQNLIRYQNCHMRWLTHEMHIQATANEILKLKNGVLKILADKQGLTEAEFSFYQDAWEQIADCKRVLKWTCIYEYYLPSCENEKRSLLNYLLRCAGFAVDQLYQCSAQLLTLFSMEETSDKFPQFRDRLCLKTSVAQYYYDNMAWALENGLSDLNAVRQAMSSRRMRLGIPTTTTTAEEGMTPEEEAAAAEEYKACAHCQFGNETSSLVCVMCYH
The following text describes a protein:
Function:
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca(2+)-dependent manner. Triggers intracellular Ca(2+) oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function.
Subcellular Localization:
Cytoplasm, perinuclear region. Nucleus.
Sequence:
MEFLKKEQYVLEIDKVIANEIIQKYEPIEEVKNQHQMTIEGFLRYMNSNDCLLFKKNCTQVYHDMTRPLSDYFISSSHNTYLISGQLIGPSDLWGYASALVKGCRCIEIDCWDGSQNEPVVYHGYTLTSKILFKTVIQVINKYAFMASEYPVVLSLENHCSPQQQEIMANNMQSILGDTLLSDVLENFPNELPSPEALKFKILVKNKKIGTIEETIERIGTNKQGRIVEYEEEEDEEESEEKDNVTTPMLKENKEKELEEKKSIISNFISYSKKKKIRKVKLSLELSDLVIYTKAEKFKSFHHAQINQKFNENNSIGELRARKLSKQKAREFISHTNSFITRIYPKATRTDSSNYIPQEFWNVGCQMVALNFQTPGVPMDLYNGKFLDNGGCGYLLKPEILRNPKLNFSPSEFKHYNPTILSIRLISGFQLPSTYWNNSLVLIEIYGIPDDQTKQQTHVIRRNAFDPRWNETFTFTIHAPEMALIRFVAESQSTIGANEFLGQYTLPLLCMEKGYRTIPLFSKSDKFLLSAMMSFHYFSLPFKKASQESLTIPLCTYCFTVGA
The following text describes a protein:
Function:
Radical SAM methyltransferase that is responsible for the C(5)-methylation of 'Arg-285' of the methyl-coenzyme M reductase (MCR) subunit alpha McrA. This post-translational methylation, despite being not essential in vivo, plays a role for the stability and structural integrity of MCR.
Sequence:
MEVVVDVGGNPGVDCKGFCKYCYFKKVKDIQPLGCKYCLPFKKGCDYCTRSVKESYSGFKSLQMVLEETANKLYFTSGEVKKFTVSGGGDLSCYPELKSLITFLSQFNTPIHLGYTSGKGFSKPDDALFYIDNGVTEVSFTVFATDPALRAEYMKDPEPEASIQVLRDFCTHCEVYGAIVLLPGINDGEVLEKTLCDLENMGAKGAILMRFANFQENGLILNNSPIIPGITPHTVSEFTEIVRSSAEKHPSIRITGTPLEDPLIGSPFAIRNVPEALLKLPRVSKKATIITGQVAASRLTEIFEALGGTVNVIPVKKDIGCLITIDDFKALDLSEVTETVFIPGRAFVHDMEIKEALRRDGVDRIVRRGPERLSVDGEMSIGMTREEVLELEVENFTELIGQINSLGLPLE
The following text describes a protein:
Function:
Plays a role in mitotic bipolar spindle formation. Binds mRNA. May function in nucleocytoplasmic transport and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle pole. Note=Recruited from interphase nuclei to spindle MTs during mitosis.
Sequence:
MSLFGSTSGFGTGGTSMFGSTTTDNHNPMKDIEVTSSPDDSIGCLSFSPPTLPGNFLIAGSWANDVRCWEVQDSGQTIPKAQQMHTGPVLDVCWSDDGSKVFTASCDKTAKMWDLNSNQAIQIAQHDAPVKTIHWIKAPNYSCVMTGSWDKTLKFWDTRSSNPMMVLQLPERCYCADVIYPMAVVATAERGLIVYQLENQPSEFRRIESPLKHQHRCVAIFKDKQNKPTGFALGSIEGRVAIHYINPPNPAKDNFTFKCHRSNGTNTSAPQDIYAVNGIAFHPVHGTLATVGSDGRFSFWDKDARTKLKTSEQLDQPIAACCFNHNGNIFAYASSYDWSKGHEFYNPQKKNYIFLRNAAEELKPRNKK
The following text describes a protein:
Function:
N-alpha-acetyltransferase that acetylates the amino terminal acidic residue of proteins devoid of initiator methionine. Preferentially acts on proteins starting with Asp-Asp-Asp and Glu-Glu-Glu sequences. In vitro, shows high activity towards N-terminal sequences starting with Met-Asp-Glu-Leu, Met-Glu-Glu-Glu and Met-Asp-Asp-Asp.
Sequence:
MRYIKSEPYYEGLPPFNVSGSPFNVVPIHNYPELMKDTCALINAEWPRSETARMRSLEASCDSLPCSLVLTTEGMCRVIAHLKLSPINSKKKACFVESVVVDKRHRGQGFGKLIMKFAEDYCRVVLDLKTIYLSTIDQDGFYERIGYEYCAPITMYGPRHCELPSLQNAKKKYMKKVL
The following text describes a protein:
Function:
This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system which may play important roles in both hemostasis and host defense mechanisms. Its active form catalyzes the activation of proclotting enzyme. Does not activate the mammalian coagulation factors factor IX, factor X, prothrombin, plasminogen, protein C or prekallikrein. Does not hydrolyze fibrinogen. Does not catalyze the activation of factor C or coagulogen.
Subcellular Localization:
Secreted. Note=Secreted in hemolymph.
Domain:
The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence:
MTWICVITLFALASATLGNKVSRVGVLFPKTRNDNECTARGGLKGSCKSLIDCPSVLATLKDSFPVVCSWNGRFQPIVCCPDAIAPPPVTTTAVTVISTKEPKLPRLHISGCGKRKVKIDITTVGRSGSPILPPISTPQNSTGGRGIIAGGVEAKIGAWPWMAAVFVKNFGIGRFHCAGSIISNKYILSAAHAFLIGGRKLTPTRLAVRVGGHYIKRGQEYPVKDVIIHPHYVEKENYNDIAIIELKEELNFTDLVNPICLPDPETVTDPLKDRIVTAAGWGDLDFSGPRSQVLREVSIPVVPVDKCDQAYEKLNTPSLKNGITNNFLCAGLEEGGKDACQGDSGGPLMLVNNTRWIVVGVVSFGHKCAEEGYPGVYSRVASYLDWIAKVTNSLDHAVTN
The following text describes a protein:
Function:
Involved in protein precursor import into chloroplasts.
Subcellular Localization:
Plastid, chloroplast inner membrane; Multi-pass membrane protein. Plastid, chloroplast membrane; Multi-pass membrane protein.
Sequence:
MVLCQGLSAGHAQLLAFPAAKHNVSFARTSCLGTPAGSWSVKRARLHAERKSFSMGALRVGTGFVQNDMLASFGRDDSIKGIPSLAARHSQHRRLEVGCRASSLASFSYPELTSKPRWWWRTVACVPYLLPLHNMWSYADVIYQLHTYLQGFSLVYTFIDTMTLFPGWLLLVIFMTVYFFVVRRKWSPHFLRFHVILAILLDTGSQAVATMCTWMPSIVYQGTPMQYFWMAIAFIQIFTVLECMRCALAGMYPNVPFISHTAFIHSDLNLFR
The following text describes a protein:
Function:
Acts as a receptor for TNF-cytokine egr. Plays a role in activation of JNK signaling and is required for egr-induced apoptosis, including in wing imaginal discs during development. May also play an egr-independent role in cell proliferation. TNF receptor involved in triggering JNK-dependent proliferation of the enteroblast-enterocyte lineage in response to stress-induced release of egr by intestinal stem cells and enteroblasts. Involved in regulation of insulin production in response to dietary protein shortage keeping systemic growth in check. Activation in brain insulin producing cells through binding of egr released into the hemolymph in response to dietary amino acid shortage, results in JNK-dependent inhibition of insulin production.
Miscellaneous:
MISCELLANEOUS: The name 'grindelwald' comes from the village at the foot of the Eiger mountain in Switzerland after which the TNF gene egr is named.
Subcellular Localization:
Apical cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Note=In wing imaginal discs primarily localizes to the cell membrane but internalizes into intracellular vesicles upon binding egr.
Sequence:
MSVRKLSALSLSIGGVPLIPSVSLVAAANGESRDCHGTICHPVNEFCYVATERCHPCIEVCNNQTHNYDAFLCAKECSAYKTFEPLKAEMLDIQNTQQLILLLLTILLVLIALRCAFQFLRWLIGNRCFQKLMRRLQSKAYPHPATANGKDLNATTIQNLNAINHPGSDLERAQSQIYSVAGAAEGSVVTMTTPVSTRYPAENSTTPTTVMTEIGYGYDNQAMVVTPVSEKPSAATIPVAF
The following text describes a protein:
Function:
Involved in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin and of the nitirle glucosides rhodiocyanoside A and D. Can use L-isoleucine > L-valine as substrate, but not L-leucine, L-phenylalanine or L-tyrosine. Catalyzes multi-step reactions starting with two successive N-hydroxylations using L-isoleucine and, to a lower extent, L-valine as substrates leading to the formation of N,N-dihydroxy-L-valine and N,N-dihydroxy-L-isoleucine, respectively; following spontaneous reactions lead to the production of (E)-2-methylpropanal oxime and (1E,2S)-2-methylbutanal oxime, respectively.
Subcellular Localization:
Microsome membrane; Single-pass type II membrane protein.
Sequence:
MDYSAFAFFRSYFHPLWISFLIATCGFFIIKTLRYHLMSVKSKIAKLPPGPKPWPIVGNLPEMIANNPAPMWIFKVMEDLNTEIACIRLGNVHIIPVTCPTIAREILRKHDADFASRPTTMASGIISSGYLTSAIAPFGEQWKKMKKIIVNDLLSPQRYRWLQDKRNEEADNLIFYVYNKCNNGDLVSVRLASQHYCGNVYRKMYFNTRYFGKGMKDGGPGLEEIEHVDAAFTLLKYIYAFSASDYMPCLRLLDLDGHKGKIKNAMKIMNKYHDSIIEERIKQWNDGSKTVEEDLLDVLISLKDVNNNPVLTKKEIKAQLIELMIATIDNPSNLVEWILAEMLNQPELFQQATNELDKIVGKDRLVQESDIPNLNFLKACAREALRLYPMAPFNIPHVSLNDTVVGNYFIPKGSHVLIKRSGRNPLLWDEPHKFKPERHFKNGESNIVLTEPGLKFISFSTGMRSCPGVKLGTTMTVLLLARLLHGFTWSIPPTTSSISLEKSKDDMFLAEPLVVVAKPRLPTELYNFSTK
The following text describes a protein:
Function:
Plays a key role in early steps of protein N-linked glycosylation by being involved in the conversion of polyprenol into dolichol. Acts as a polyprenal reductase that mediates the reduction of polyprenal into dolichal in a NADP-dependent mechanism. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Also able to convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT).
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Endoplasmic reticulum membrane.
Sequence:
MVPDHYTYILGIPINLMSVLWATMSAVLITTYAVNHLVNAGGVVGSMSKYLTDYGKASTTVRSLDVPKSYFTHYYILASIWNTVCFITISRICFGLMTNNWIASLFLMHSTANASGDKLSLLLCMLMLTVHSMKRLYECLFISVFSNKTKMGIIQYVWGNTYYILLAPTMISECLPLHKLPFGSFQVRHFMGIVVFLIASFYHHQSHIILADLRKKGSIKKDAHGIPQGGLFNLVSCPHYFAEVLVYISITIILGAQCQTWFLVLLYNIFAHANMAMGAHTWYRNTFKNYPPNRKAFIPFVL
The following text describes a protein:
Function:
May be an inorganic phosphate cotransporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MTDTAGVYDSKGVSNRNRSDQEVRMERYASDGQIPRCRKTRFFVVLMLFSGMANAYVMRTNMSVAIVAMVNHTAISHTKSSTQSKERDGDFEWSYKLQGYILSSFFYGYVITQIPFGLMIKYYGARHFLGWGMMINSLAAFFIPISARSGGVVGLCVVRFIQGLGEGPIVPCSHSLLAQWVPPNERSLAGAAVYAGAQFGTIVSMPLSGLLAHYGFDGGWPSIFYIFGLFSTIWCIIFICLVQESPAVSTRISEAERRHIMEAIWQAQPEERSRIPFLGIAKSPPFYAILVAHAGHNYGYETLMTMLPTYMYRVLNVNIRTNGIISSLPYLAMWILAIVFGILADCLIRRNFSITVVRKLMNSLGQYGPAVALISVGFVHHSLWLTSVIFILGMGLNGAIYCGFKINHLDLSPRFAGLLISVTNCVANLVGLMAPMVAGHVIDPKPSVENWRIVFYIAAGVFIFTASFYNVFASGKQQW
The following text describes a protein:
Function:
Required for nuclear membrane fusion during karyogamy.
Subcellular Localization:
Endoplasmic reticulum membrane. Nucleus membrane.
Sequence:
MKLGTLVPSHDAPAEIDLVFFLQSKTQQHDAIFTEAVQLLESMKSSPSCNRVAASRLVASCQSIGGTTDHTEQRTYLTLEHVRSLYAARLAVCELDGAGASIPPPCLPVTLGAPRKKGFFGFSSNHKSTTITADSMPTEILESCLRSLESRPQWWTSYSNSRQNAMVICQATRLETEKEELLELHRSIVESSIKLSHGLEEALEMAYAESSQHQAFIEATAALQAKLRQDLEATETGFKALLGNLMEGIKSAVDSGVTTVTSTLARVHNDAASLETDIRNATNEVSYLRQMLQVVYDEALTREAQSSHALEQKVEKQNELALSLQSRLESLVHGDVARLSQNVETFGASLSWLSERLGLILQQELSLSERLRNFETSLETSQSKAEALRIAQLQQFDALDAQYRLQQYMETNLQISQALLDKAITTTANLQAMIEETTTRYRDSPILGKFIGPYSAWTVCGILLSVIGAHSPRLTLAALAIGAGEYKPHRLAADHARITYFQFTSQ
The following text describes a protein:
Function:
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Subcellular Localization:
Cytoplasm.
Sequence:
MEKVLLAMSGGIDSSVAAYLLREKGMAVEGVFFILFDEPANIELAKQTANFLNIKLHIEDLREKFKADVITPFFEGYKKGITPNPCVICNKKIKFPLLKFLAEKVKANYIATGHYARIVRINNIPLLMKGIDPKKDQSYFLYGIERTLLSHIIFPLGEYTKYKIREIAEKVGIPSKVAEESTEVCFLRDKRYYESIRPTKGGPIIEMSTGKIIGQHRGIHLYTIGQRKRLGIASPHPLYVVKIEPSENAVYVDSKEKAFMREFVVNELNWLCDIEKEEFSCQVKIRYAMNPEKATVTLINKDRANVVFEKPQFAPTPGQSAVFYNGDIVLGGGVIKEIMQGF
The following text describes a protein:
Function:
Scaffold protein of the endoplasmic reticulum-associated degradation (ERAD) (also known as endoplasmic reticulum quality control, ERQC) pathway involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Has multiple functions in ERAD including recruitment of DER1 to the HRD1 ubiquitin ligase, and regulation of HRD1 activity. Involved in oligomerization of HRD1 and in HRD1 autoubiquitination and degradation.
Miscellaneous:
MISCELLANEOUS: Present with 1890 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The ubiquitin-like domain is required for HRD1 trans-ubiquitination and degradation. Reported to be involved in ERAD-M but not ERAD-L function. However, a contradictory report states that it is not required for either ERAD-L or ERAD-M function. Reported to be required for HRD1 oligomer formation. However, a contradictory report does not observe any defects in oligomerization following deletion of the domain.
Sequence:
MSEYLAQTPCKFTIWSSEIDLIRTNLLVNAHPLSTVGRLLQYIHYQIYKQLRAIYQPEEQCTNSEIPHTPLNSINTYFLSYEGRELSATCLLKDITSSSHPDSNHFIRLQLEKRTSPSGSAFDLEYDMEGEFNSMNIQFEINTLSSQRIFNSMEPNLPIGTTLARLEKLALERIKDFEKSAGNLCGIKEDHSVSDLQGFIIKGKQTPMFLNYGSDSDYYKDLNLVDLIGIDFAPAHNSFFTFLFKMNHEQNSHIANDEERFVLEFISDATLSITQMNVKPDTTVKQVKDFICSVYTHSLNLRRNDIKLIYKGQLLHENNFAGNSSKISEYIKEPHEVKVHVQINQEYTESGPGFWNEVFNNPNIFQFMPPDTRSQSPVSFAPTQGRSPAAIRGEERGIPYVTESGNDIVPTDELYRKCIINGDEVVFIPVSELNPQSSYLSVIKGDYGEIKIPISSNDYRINGDNILLSPSAIEQLESALNFKIERPRDSTLLHPSGEHVRAADNTSSANDNNTVENDESAWNRRVVRPLRNSFPLLLVLIRTFYLIGYNSLVPFFIILEFGSFLPWKYIILLSLLFIFRTVWNTQEVWNLWRDYLHLNEIDEVKFSQIKEFINSNSLTLNFYKKCKDTQSAIDLLMIPNLHEQRLSVYSKYDIEYDTNTPDVGQLNLLFIKVLSGEIPKDALDELFKEFFELYETTRNMNTLYPQDSLNELLLMIWKESQKKDINTLPKYRRWFQTLCSQIAEHNVLDVVLRYIIPDPVNDRVITAVIKNFVLFWVTLLPYVKEKLDDIVAQRARDREQPAPSAQQQENEDEALIIPDEEEPTATGAQPHLYIPDED
The following text describes a protein:
Function:
Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
Subcellular Localization:
Nucleus.
Sequence:
MGMGKRRKRKKRSLYDQSSMDTILFPLMLAALAKLDNPFCESLLKKCLKKLQLSLLTQTPNSNIPPSFPQKLSNDFLSFLPALLRSKNPEIASRTAEIVGAATLLSLDMNERVVSDAEILKGLVAALSSGSKRISMAACNAVLDVSTTLIGRTRLCDFCVVEKLMSEFLRVVVSPAKSVSLCRTDTRDSISPRIGLTAGKLPILVLYTAVTLINSCNLKNLSKIPRELRKTFLNYLKELWRNVWAQMLLIDIVDCSQGRYYFSNLRTNHLAESIFRLSIDLDQNPIACIFELVKKSMFGPSNSDFEQFMLCYWEDSPCLLRNHLQTSNDHEDIFNPLVQSLNCKGTVDSLLSSILCNLVSCPPICSDEFDILVFLEEVRDKLGCPMIYGQDIRVIKAVEEIYVLKQGSLKKEVHFFKQCMNSFISGPKLIDAVAIQQCKEAHREGYTISLRGMEFRSEYISAIADSLAALFGQPSVGANLYLTPPQSQGLARHYDDHCVFVCQLLGTKKWTVFSRPTVQLPRLYEPLDCILRSEDDCVESKHMQFLLSEGDILYIPRGCPHEACTVTDNSVSTADDGSTGFSLHLTLGVEVEPPFEWEGFAHVALHCWNHNHKRSPDPSSLMGTLNFISVYMLHVAIRLIGDHDPKFRKACMVAAIPLHSLDLNRKMFSYVINKIDRESRYLEVFNRVQAAIGNNEDIWKQMKWIQHLFLLGEMNDEIEWNYSLTEFRDYISYRHMEVEDAFVQLKSKFCRDISFEDACQSFNKVLEKYKKTRKQYMSGMLSLHCT
The following text describes a protein:
Function:
Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion.
Sequence:
MAGEQTHHWVRAVPERDRHDKVVSVLAIIRDTSDMKRTESLLRRREFEFRTLAHNSPDMIIRYDLECRQAYLNPAFERFTGTALADAWNKTPAEAWNALTPCDDYLSRLKGVMETGKPDQILLEWVMPDQSVSTLLLHAVAEHDEEGNTIGALVIGHNITELKASERHLEESRAQLQMLTYHREEAREGERKRIAREIHDELGQLLSVLRLGISTLDYGYGDTNPDLRNKTAKMGAVVDQAIDMVHTLATRLRPAVLESGIALALEWLVQEFSKSTGIDCELSVPDEDIDFDKERALPVFRIVQESLTNILRHSQADHVEIELTQDQEHLKLSIHDNGQGFEVSKATKKGSFGIIGMHERILMLGGTLEISSSSEQGTEIRLE