lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Sequence:
MTTNSESSAPPTANSTANVCLVVLAAGKGTRMNSELPKVLCPVVDRPMIHFVLDAADKAGIQKKIAVVGYEADLVRKELQTRGDDSLTFAEQTEQLGTGHAVQRCRDQLAGHEGLTLVIAGDSPLIQPSSLIKLIEHFQATRPALLLGTLTKDDPTGLGRIVRNESGQFTGIVEHKDATDEQREIREVNMSTYLFNNEDLLESLSKLSNDNAQGEYYLTDCARLLHEAGRPVEALPVLQDCESLSINNPEELQVVDQTMRAMGYA
The following text describes a protein:
Function:
Converts sphingomyelin to ceramide. Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly. However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form; In the lysosomes, converts sphingomyelin to ceramide. Plays an important role in the export of cholesterol from the intraendolysosomal membranes. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol. Modulates stress-induced apoptosis through the production of ceramide; This form is generated following cleavage by CASP7 in the extracellular milieu in response to bacterial infection. It shows increased ability to convert sphingomyelin to ceramide and promotes plasma membrane repair. Plasma membrane repair by ceramide counteracts the action of gasdermin-D (GSDMD) perforin (PRF1) pores that are formed in response to bacterial infection.
Subcellular Localization:
Lipid droplet. Lysosome. Secreted, extracellular space.
Sequence:
MKYLLLATLLVLYLAALAETSVVDRKLRVQQFEKDSDVTEDYELKRKVGLLFLRKILGQGDILRPEKEKELDRLVEQSGMTCTLCKAGVDVIQKLLHSNGGEDVITAIAVEVCELGNIEDRRVCKLAVEEFKQEVFYVLFNLQPDELCYWLLKNQCRKPADFLPNWVVTSSTTPQPPYKPRTNPASGTPTLKFLFFTDMHMDVRYAPGRTAKCREPLCCRDNDALPDQESDAAGMWGDYRHCDMPQNTVESMMSQVANNDGIDFIIFTGDIPAHNVWNQTKEDQIDKLQRWTDLLKKHFPTTPVYAAVGNHESAPVNSYPPHSIFDQPGADTQWLLDTLYDSWSNWIPEEDMGFVKQGAFYTTLIRPGLRVVSLNTNYCSDDSWWLLVGTNAVDPEGQLKWFAGVMQAAEDNDENVLIISHRPTDGCMKPWSDNYYEIINRYQNTIIAQLFGHAHTGQLYNDITQEDRVSAIGLIGPGFTTYSNLNSGYRIYTMEGEYEGSRYSLLDGESYYLNITDANMRGEATWQREYSFVDDYDVINLTPPELKKLVDRFDSDEQLFQSYHNHITKMEDLSDCDVTCKQSTLCDIKTFRADDNSFC
The following text describes a protein:
Function:
Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Sequence:
MPREDRMTWKSNYFKIIQLLDDYPKCFIVGAAMWAPSRRSRSGHLENNPALEKLLRHIWGNVGFAFTKEDLTEIRDMLLASKVPAATCAGPIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGANKATLLNTPNISPSSFALVIQQASDNGSIYNPEVVCDVASVCLQTGYPPVASVPHSIITLALSVETNYTFPLAGKVKAFLADPSAFVAIASVAVATMPQLRLKPRKSWRSRMRIWDLFSLTNHQKTTNSASFIYKTRK
The following text describes a protein:
Function:
Functions as a two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Localization:
Cytoplasm, cytosol. Nucleus.
Domain:
Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer.
Sequence:
MTMAILKGLMQGYLSALLDEGVVNDRFNAIVCLNNTVERRERVVQQIETYFADVDMILTEISLDVDNSAFDFSRLASLARQIEEKSDRNWYINAGKWGRILFDYRTVEALRGIGAEHMRLACPEFIKACDEMNKRMLSRTLLWVKHEFANTKRKLEAFVQMERRIIRLERSNSSN
The following text describes a protein:
Function:
Positively regulates reproductive function by facilitating male gametophyte formation and double fertilization.
Miscellaneous:
MISCELLANEOUS: Transcripts of KPL and ARI14, encoded by adjacent genes organized in a reverse orientation, have the potential to generate natural cis-antisense siRNAs (cis-nat-siRNAs) pair targeting ARI14 in sperm, thus leading to opposite expression levels during male gametophyte development.
Sequence:
MEPNNVERNLQSLRRLYSLLVANARNEYIPEAYKLDDNTQFLLKRLLDFASHEHFVTQSNLLATQLRVFPKTVLHGAKPSNVADSSETTPPAMLSQINGSHITRVSKPLEAKGTLQRDLRVDQIRSNPSKDVLTEEVVDAIEQIDTQLSALSFVSSRVDSDERTRSVKSFVTPPTEECRQNSQASMPCLRSNYMTVSQKSVISGAEVTFPYNDQLVRVTSPPQPLPPRAVSGFKKPNQSNRASQKMPIMKPTLMDQETETFDDDSSETEADQTPSATGSESEDEEVSTSQEYSGETGSSSGSEWETQAENDTESKSESSYPPQNDDSVSEVSTSPPHTDRDTSREPGKQRRNVMGRFKRIKNKIGQIFHHHHHHHHHHHHHDKEKPSAWNKLQSKFHHKHQEKSKERKRPMSESKGLTTHKQQHQGGHFHALVEGLVRHRKHSKKQKHQLKSDAKKTEWWKLLKKRQGGGVKIPKRGRVKLGKKKHYLSKNV
The following text describes a protein:
Function:
Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endomembrane system; Multi-pass membrane protein.
Sequence:
MALAETIVGIIGNIISICLFLAPVKTFRKIIKAKSIMNFKSTPYVCTLLSVLLWSFYGLVKPAVLIVTINGAGTFLEICYLICFLYYADRKARIKTSQSLLLVLAIFGIVVASSLTATKVKDTRVMVAGIVSLIFSIVMYASPLRAMKMVVQTKSVTFMPFTLSAILLLNGTVWSIYALLVKDIYVGIPNGVGMVFGILQILLYVLYMKKSRKIQLEKEAEKSHMHSNGRKSDAPNGDHSIDMEKPPLSSSPHAMEQDMKAAQDTKGLSALQGGTSPRPDAAPEFTNVPLEDKAVQDYRDPQSPTPLPTSNTDQMRPLSATD
The following text describes a protein:
Function:
In association with lipoprotein LprG transports triacylglycerides (TAG) across the inner cell membrane into the periplasm; TAG probably regulates lipid metabolism and growth regulation and plays a structural role in the outer membrane. Mutagenesis and molecular modeling suggests TAG (and maybe other lipids) enters the central cavity of the P55 transporter from within the cell inner membrane via clefts on the cytoplasmic face of P55 between TM5-TM8 and TM2-TM11 (Probable). From there the lipid is probably transferred to the hydrophobic cavity of LprG (Probable). Confers resistance to ethidium bromide, requires LprG lipoprotein for normal function. With LprG maintains cell wall permeability. Probably required with LprG for normal surface localization of lipoarabinomannans (LAM). Overexpression of LprG and Rv1410c leads to increased levels of TAG in the culture medium. Upon expression in L.lactis does not export any tested substrates, does not confer resistance to vancomycin, rifampicin or novobiocin. Probably does not function as a bona fide drug efflux pump, but instead plays a role in outer membrane biogenesis (Probable).
Miscellaneous:
MISCELLANEOUS: Bacterial LAM blocks host cell phagosome-lysosome fusion and is one way in which M.tuberculosis evades the host immune system; MISCELLANEOUS: Triacylglycerides accumulate in lipid droplets in the cytoplasm of M.tuberculosis stationary phase and dormant bacteria, and are used as an energy source during starvation.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
The periplasmic loop between the last 2 transmembrane domains plays an important functional role. Has a canonical major facilitator superfamily fold with two N- and C-terminal domains of 6 transmembrane helices (TM 1-6 and 7-12) and two other transmembrane helices between the domains (TMA and TMB) that form a hairpin. Between TM9-TM10 is a periplasmic beta-hairpin that extends along the membrane plane, TM11 and TM12 helices are extended 20 Angstroms into the periplasm. Asp-22 is a possible protonation/deprotonation site.
Sequence:
MRAGRRVAISAGSLAVLLGALDTYVVVTIMRDIMNSVGIPINQLHRITWIVTMYLLGYIAAMPLLGRASDRFGRKLMLQVSLAGFIIGSVVTALAGHFGDFHMLIAGRTIQGVASGALLPITLALGADLWSQRNRAGVLGGIGAAQELGSVLGPLYGIFIVWLLHDWRDVFWINVPLTAIAMVMIHFSLPSHDRSTEPERVDLVGGLLLALALGLAVIGLYNPNPDGKHVLPDYGAPLLVGALVAAVAFFGWERFARTRLIDPAGVHFRPFLSALGASVAAGAALMVTLVDVELFGQGVLQMDQAQAAGMLLWFLIALPIGAVTGGWIATRAGDRAVAFAGLLIAAYGYWLISHWPVDLLADRHNILGLFTVPAMHTDLVVAGLGLGLVIGPLSSATLRVVPSAQHGIASAAVVVARMTGMLIGVAALSAWGLYRFNQILAGLSAAIPPNASLLERAAAIGARYQQAFALMYGEIFTITAIVCVFGAVLGLLISGRKEHADEPEVQEQPTLAPQVEPL
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNSNTVGAIFSVGKCFLLSPKSPSEKKPSLLKHTFAFILVILYTIAALAHLLCNLPDYRSLSLMQMTFLVMTDVALYCSAIYFPLMMNKITLGWYHLIRNLSQVCGTGANRSYSFAGFFTVSSFVTVFLYVILGRKEGVGFFYYFPYRILAANSINFGMVTGVTVLQMLHQCYHAQKNIVQRRILTKVKSEEIYSLLEPFECGLFTLSDAVSHFNDIFGWNILFSHIIGVCRTLIYIDELVRTQTNFQFSLETGAILGSLLIFWILALYLIVLCDNVLKEFDDILDVLLKIKFNLMKMGKLQEGFLDEIEQIRPVFSAARFYNISRPTIFSLSNAATTFLIVLLQFHIN
The following text describes a protein:
Function:
Mitochondrial transcription factor that confers selective promoter recognition on the core subunit of the yeast mitochondrial RNA polymerase. Interacts with DNA in a non-specific manner.
Miscellaneous:
MISCELLANEOUS: Present with 9380 molecules/cell in log phase SD medium; MISCELLANEOUS: Although strongly related to dimethyladenosine transferase proteins, it lacks the methyltransferase activity. Dimethyladenosine transferase methylates the 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 12S mitochondrial rRNA in most species. This explains why 12S rRNA is not methylated in S.cerevisiae.
Subcellular Localization:
Mitochondrion intermembrane space.
Sequence:
MSVPIPGIKDISKLKFFYGFKYLWNPTVYNKIFDKLDLTKTYKHPEELKVLDLYPGVGIQSAIFYNKYCPRQYSLLEKRSSLYKFLNAKFEGSPLQILKRDPYDWSTYSNLIDEERIFVPEVQSSDHINDKFLTVANVTGEGSEGLIMQWLSCIGNKNWLYRFGKVKMLLWMPSTTARKLLARPGMHSRSKCSVVREAFTDTKLIAISDANELKGFDSQCIEEWDPILFSAAEIWPTKGKPIALVEMDPIDFDFDVDNWDYVTRHLMILKRTPLNTVMDSLGHGGQQYFNSRITDKDLLKKCPIDLTNDEFIYLTKLFMEWPFKPDILMDFVDMYQTEHSG
The following text describes a protein:
Function:
Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.
Sequence:
MLSRRHALSVLSAIALATGSLVTAAPAAELQKASLRLKWLPQAQFAGFYVAAAKGYYKAEGIDLTINPGGPNLLTENLVATGADTFGLSGGTDSVFAARDKGLPIVCIGVSHQITPFIFVTRKDGPVKTIQDFKGKTVTTWFTGANHVLNGMLAKEGIKPDELKIQPQQVSVTPFVDGSVDVVTATYYNEFYTIQSRMPKDSLKTFVAEDYGITFPRDTLIVAEATAKEKPELVKAFLRASLKGWKDAFADPKGAVDTVMAAAPTLDRAQQEFMLTEVKRLMTAGTAAKNGMFWIDADAVKTAHDFFLKYGVISKPLDLAAAYDASFIQSVPLADRLP
The following text describes a protein:
Function:
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Essential for female and male gametophyte development.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
Domain:
The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes.
Sequence:
MSSSTKNIPKPPPLPCITYQRFQSSTRKPSSLMRLVPKEALETWDKLFKEGSGADTYVETDNKSHFPAHSSVLAAASPVIATLLNQSRDKNGNTYLKIHGVPCEAVYMFIRFLYSSCYEEEEMKKFVLHLLVLSHCYSVPSLKRLCVEILDQGWINKENVIDVLQLARNCDVTRICFVCLSMVIKDFKSVSSTEGWKVMKRSNPLLEQELIEAVIESDSRKQERRRKLEEREVYLQLYEAMEALVHICREGCGTIGPRDKALKGSHTVCKFPACKGLEGALRHFLGCKSRASCSHCKRMWQLLQLHSCICDDSNSCKVSLCWNFKEKMKKLSKKEQSKWRLLVENIIRARNSLGPFSSRSSGLI
The following text describes a protein:
Function:
Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. May have a general role in telomere regulation. Promotes in vitro the ability of TERT to elongate telomeres. Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization. Binds to the single-stranded 5'-(GTGTGG)(4)GTGT-3' telomeric DNA, but not to a telomerase RNA template component (TER); Plays a role in nonsense-mediated mRNA decay. Is thought to provide a link to the mRNA degradation machinery as it has endonuclease activity required to initiate NMD, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. Degrades single-stranded RNA (ssRNA), but not ssDNA or dsRNA.
Subcellular Localization:
Chromosome, telomere. Nucleus, nucleolus. Cytoplasm, cytosol.
Domain:
The PINc domain confers endonuclease activity and is expected to bind the catalytic metal ion.
Sequence:
MHQSGPVAKRPWPKTNGEGPGRLRAPCRHRCPRRPPRQQKQSPPRTLASLGLTRPGLTSPHNPGAAPPPPASAHLPDHTSAHAQRPSAPPGCSRWSDRACVRRLSSLCGHRRLGRRAGGGGEKGGRWVSARARRPAVVVSWLRARGAGGVAAAVAAAEKMAEGLERVRISASELRGILATLGPQAGSRENMKEPRQRKDNRRPDLEIYKPGLSRLRNRPKIKEPSGSDESKNEVVNDRDSSAVGNCTQLIKDVCKDNPQQNGPVDSENIQAQESFPGTVGQEDRSLRIIKRTKKPDMQIYQPGRRLQTVSKEATSRVEEEEILNQVEQLRVEEDECRGNVKEEVVNKPDREEAEKSLSGDRVRAAKGEKGKRVERGEGVKKANEDSAQGKPGSAKRYSRSDKRRNRYRTCSTSSAGSNNSAEGAGLTDSGSRRRRQDRTKERPRLKKQVSMSSTDSLDEDRIDEPDGPRRSSERKKHSERSWSGRGEGEQKSNGKENRGTLRVTFDAETMNKDSPVVRSAREEVDRLKPDKGSSGGGKGSEKPESKNLRQELRGRGRGILILPAHTTLSVSSAGSPESTPLGPRLLFGTGSKGSRSWGRGGTTRRLWDPNNPEQKPALKSQTPQLHFLDTDDEVSPTSWGDSRQAQASYYKFQNSDNPYYYPRAPGPASQYPYTGYSPLQYPVGPTNGVYPAPYYPGYPAPSGQYVCSPLPASTMSPEEMEQHMRNMQQQELHRLLRVADNQELQLSNLLSRDRISPEGLEKMAQLRAELLQLYERCILLDIEFSDNQNVDQILWKNAFYQVIEKFRQLLKDPNVENPEQIRNRLLELLDEGSDFFDSLLQKLQVTYKFKLEDYMDGLAIRSKPLRKTVKYALISAQRCMICQGDIARYREQANDTANYGKARSWYLKAQHIAPKNGRPYNQLALLAVYTRRKLDAVYYYMRSLAASNPILTAKESLMSLFEETKRKAEQMEKKQHEELELSPDQWRKGKKSTFRHVGDDTTRLEIWIHPSHPRSSQGTESGKDSEQENGLGSLSPSDLNKRFILSFLHAHGKLFTRIGMETFPAVAEKVLKEFQVLLQHSPSPIGSTRMLQLMTINMFAVHNSQLKDCFSEECRSVIQEQAAALGLAMFSLLVRRCTYLLKESAKAQLSSPEGEEDQDDIKVSSFVPDLKELLPSVKVWSDWMLGYPDTWNPPPTSLELPSQVAVDVWSTLADFCNILTAVNQSEVPLYKDPDDDLTLLILEEDRLLSGFVPLLAAPQDPCYVEKTSDKVIAADCKRVTVLKYFLEALCGQEEPLLAFKGGKYVSVAPVPDTMGKEMGSQEGKQLEDEEEDVVIEDFEEDSEAEGSGGEDDIRELRAKKLALARKIAEQQRRQEKIQAVLEDQSHVRQMELEIRPLFLVPDTNGFIDHLASLAQLLESRNYILVVPLIVINELDGLAKGQETDHRAGGYARVVQEKARKSIEFLERRFESRDSCLRALTSRGNELESIAFRSEDITGQLGNNDDLILSCCLHYCKDKAKDFMPTNKEEPIRLLREVVLLTDDRNLRVKALTRNVPVRDIPAFLTWAQVG
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MGITRNLILGLACLAFVSIAKALPHEPELGSARVVFQTSYGDIEFGFYPTVAPKTVDHIFKLVRLGGYNTNHFFRVDKGFVAQVADVASGRSAPMNEEQRKEAEKKIVGEFSDVKHVRGTLSMGRYDDPNSAQSSFSMLLGNAPHLDRQYAVFGKVTKGDETLSKLEEVPTRREGIFVMPTERITILSTYYYDTKMESCEEERSVLKRRLQASFVEVERQRMKCFP
The following text describes a protein:
Function:
May play a role in the early stages of epithelial differentiation or in apoptosis.
Sequence:
MANEVQVLPSPLKGRYAPAVKAGGMRISKKQEMGVLERHTKKTGLEKTSAITNVAKIQMLDALTDTLDKLNHKFPATVHTAHQKPTPALEKAAPMKRAYIIQQPRKC
The following text describes a protein:
Function:
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Subcellular Localization:
Cytoplasm.
Sequence:
MKKFFIIGTDTEVGKTYISTKLIEVCEHQNIKSLCLKPVASGQSQFSELCEDVESILNAYKHKFTAAEINLISFNQAVAPHIIAAKTKVDISIENLKQFIEDKYNQDLDILFIEGAGGLLTPYSDHTTQLDLIKALQIPVLLVSAIKVGCINHTLLTINELNRHNIKLAGWIANCNDSNIKYIDEQINTIEELSGYKCSAKISRNADYLDFIDLSKILISPEENE
The following text describes a protein:
Function:
Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAEGGDSRPPSADPLDVEGGTANLESTKGSGRPLLRSISAFTQRQFSRPVTQRQYSTASTTVSRPPTAPTSRSFQFRFPKTPRSRKHSTYSSVSNTSRYNTRMSFQFGYPKTPRSRKYSTYSTVSNASRKFAEGTKSFFGIGEDCTHTQKRWSQRRVRHASRRYGKIKEESIQRILEPDPAAIPLPQIVDPLALPHRQRMVPAPYDDIDGATDYTTPTTPGAWSSASSLWRRAAFGALTQQRQKVQRQQSVVSMGWDLLVKMTLQQKREQDVAKPAPLVNSRSFAPVSMEEDDDIDDLDFSFFGRDAHQAATSFSVFLYLQHIGALMFFLLLKLSPSHKEDMYDDEVFFDASPTPQGTLQYDAVQPGRAGMAANVFDMVDGGAAPAEYEIRAGDALDREEREANARMLPTDRGWRTGSKKRIAPPLRGQDVMAARAPRRRNRIGDRVLQMALDNSDRREYGRGLVGKWLKRSYRSSMAMSSDIKHQLDTITDYRPYFTYWVTFVHILITIIALAVYGIAPIGFAETETTALVRTPKLSLENIPKIEKDNFWIGPKDEDLIHLGAKYSPCMRKDPKIIQRIEDQRRKENQTGCCIKTDQSGCYQSVEDDCSKTFAEFWRWSEDNPGPHGRISGAVCGQDPEACKNPVSVAPHEWPDDMTKWPVCKEPVAGSSGGSQDHMACEVTAHPCCIGITGTCEITTREYCEFKHGFFHQEASLCSQVSCMDRICGLLPFMDPEVPDQFYRLWTSLFLHAGLVHLLLSVIFQMTILRDLEKLAGWGRIAIIYILSGIGGNLASAVFLPYQAEVGPAGAHFGVIACLFVEVFQSWQMLQAPWRAILKLSIIVLVLFLLGLLPWIDNFAHITGFICGILLSFSFLPYITFGAFDKNRKRIQIIVSFLLFVAFFSGLVVLFYVRPLTDCQGCEYVNCIPFDKTFCKYQGLDLTPRDETT
The following text describes a protein:
Function:
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MVRNLKIAIPNKGRLQQPTLQFLQSVGIKPLASDDRALIVPTSWEGVQLVMIRTEDIPNIVETGATELGITGHDYVIESSADVEELIKLDFGRSKIVLAVPQTWRENSVDELKGKEFRVATKYYNIAKEYVRRRELNAKVVKISGAAEVMPSLGAAEAIIDVMSTGTTLKLHGLKAIDVIMDSYAVVIGNRNWIKNDEADRINLLLTMMKGAIAAKGKKMIFMNVPDNKLDGVINSLPAMLAPAITRLSRSDIWEVITVAEEDILPEVIAKVKAAGARDIVVIDIEKVVK
The following text describes a protein:
Function:
Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by facilitating the membrane insertion and oligomer formation of the subunit c/ATP5MC3. Participates in the incorporation of the c-ring into vestigial complexes. Additionally influences the incorporation of subunits MT-ATP6, MT-ATP8, ATP5MJ, and ATP5MK in the ATP synthase.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MEASGSGSGESSAVEAPGSQDDRLFLIKGGIFLGSAAAAGMLAGFVTTLSLAKKKSPEWFNKGTMATAALPESGSSLALRALGWGSLYAWCGVGVISFAVWKALGVHSMKDFRSKMQSIFPPIPKNPESADQWEEALKWK
The following text describes a protein:
Function:
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC4 binds to ARE-containing RNAs (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Nucleus. Nucleus, nucleoplasm.
Sequence:
MAGLELLSDQGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRGSRARALPDRALVNCQYSSATFSTGERKRRPHGDRKSCEMGLQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSAGFVDGTALADLSHVEEAAGGPQLALALLPASGQIALLEMDARLHEDHLEQVLEAAARASRDVHTVLDRVVRQHVQEASVLLGD
The following text describes a protein:
Function:
Transcription factor that binds specifically to the RAS-responsive elements (RRE) of gene promoters. Represses the angiotensinogen gene (By similarity). Negatively regulates the transcriptional activity of AR (By similarity). Potentiates the transcriptional activity of NEUROD1 (By similarity). Binds specifically to the allelic variant of the CDKN2A promoter present in Balb/c mice, which leads to a down-regulation of CDKN2A expression in this strain, and, as a consequence, to an elevated susceptibility to pristane-induced tumors. Promotes brown adipocyte differentiation. May be involved in Ras/Raf-mediated cell differentiation by enhancing calcitonin expression (By similarity).
Subcellular Localization:
Nucleus speckle.
Sequence:
MTSNSPIGLEGSDLSSINTMMSAVMSVASVTENGGSPQGIKSPMKPPGPNRIGRRNQETKEEKSSYNCPLCEKICTTQHQLTMHIRQHNTDTGGADHACSICGKSLSSASSLDRHMLVHSGERPYKCTVCGQSFTTNGNMHRHMKIHEKDTNSTTAAAPPSPLKRRRLSSKRKLSHDAESEDPGPAKKMVEDGQSGDLDKMSDEIFHCPVCFKEFVCKYELETHMETHSDNPLRCDICCVTFRTHRGLLRHNALVHKQLPRDAMGRPFIQNNPSIPAGFHDLGFTDFSCRKFPRISQAWCETNLRRCISEQHRFVCDTCDKAFPMLSSLILHRQSHIPADQGREKLQTKTLAAESLEQKAFLALLGLQHTKDVKPAPAEELLPDDNQAIQLQTLKYQLPQEPGCPTVLSVSPLDAASLGGSLTVLPATKENMKHLSLQPFQKGFIIQPDSSIVVKPISGESAIELADIQQILKMAASAPPQISLPPLSKAPATPLQAIFKHMPPLKPKPLVTPRTVVAASTPPPLINAQQASPGCISPSLPPQSLKFLKGSVEAVSNVHLLQSKSGIQPSTTTQLFLQQAGVELPGQPEMKTQLEQESIIEALLPLNMEAKIKQEITEGDLKAIMTGPSGKKTPAMRKVLYPCRFCNQVFAFSGVLRAHVRSHLGISPYQCNICDYIAADKAALIRHIRTHSGERPYICKICHYPFTVKANCERHLRKKHLKATRKDIEKNIEYVSSPTAELVDAFCAPETVCRLCGEDLKHYRALRIHMRTHCSRGLGGCHKGRKPFECKECNAPFVAKRNCIHHILKQHLHVPEKDIESYVLATNSGLGPADTPTDAASRGEEGSCVTFAECKPLATFLEPQNGFLHSSPTQPLPSHISVKLEPASSFAMDFNEPLDFSQKGLALVQVKQENVSSLLTSSSSSALYDCSMEPIDLSIPKSVKKGDKDTVVPSDAKKPEPEAGQAEPLSPRPPPCPTLSVTVEPKGSLETPTGTVVAVTTAAKLEPHTQPLQGSVQLAVPIYSPALVSNTPLLGNSAALLNNPALLRPLRPKPPLLLPKPSMTEELPPLASIAQIISSVSSAPTLLKTKVADPGPSITSSNTVATDSPGSSIPKAAATPTDTTSSKESSEPPPAASSPEEALPTEQGPAATSSSRKRGRKRGLRNRPLPNSSAVDLDSSGEFASIEKMLATTDTNKFSPFLQTAEDDTQEEVAGAPADQHGPADEEQGSPAEDRLLRAKRNSYANCLQKINCPHCPRVFPWASSLQRHMLTHTDSQSDTDTLTTPGEVLDLTAQAKEQPPAEGASEISPASQDLAIKEAKAAAAPSEEEEEKETEENPEPEEECRVEESTGAADAPEEDTASNQSLDLDFATKLMDFKLAESEAGSVDSQGPAQQEPKHACDTCGKNFKFLGTLSRHKKAHSCQEPKEEEAAAPSLENEGVGRAVEGPSPSPEPEEKPAESLAIDPTPGTREASVAKQNEETEGPTDGEGTAEKRGDGDKRPKTDSPKSMASKADKRKKVCSVCNKRFWSLQDLTRHMRSHTGERPYKCQTCERTFTLKHSLVRHQRIHQKARHSKHHGKDSDKDERAEEDSEDESTHSATNPASENEAESAPSTSNHVAVTRSRKESLSTSGKECSPEERAAAEQAAEPSAPKEQASPGETDPQSPAAIVQDLLELCGKRPAPILAATDGASQLLGME
The following text describes a protein:
Function:
Polynucleotide 5'-kinase involved in rRNA processing.
Sequence:
MAKPLPICADLIDCNYAVAGHDGTLSDIDGELFIKPCTDTEIAFYNDTIANHQDFYDFMPEFLGTLQLDENQNKAIEEKAAELIAQHSIPEASYPGRTNGKRIVTNQAVVLMNASHGFVKPNILDVKLGVRLWADDAHQEKKKRFDKVTEQTTHKDFGFRIAGMRVWQGPDAKGDDIDEDGYRIYNKDYGRFELNNGNVHEAFKNFIFTEAAGIDKELGQLISQAFLMDLRRIQDVLESQESRMYSASLLFVFEGDGKALRTAMEEASRTPPPTTIEHASSSSGETQSSFEEEEDEDEDDIEEGSFPKIYALKVIDFAHAQWTPGLGPDENALVGKYLPKFDFEARAAAPAAVSHTNIHELQANSEWRFEVAIGSSIDVKVLSGTAEIFGTELALNHTYTFRGTKSSIYTWHGCRLEPVVTRLALAATSRLQDDVKCRETGMIIDTPGVISQGKGGYELISHIVSEFSVNIILVLGSERLHSDMIRRFSAHKTDSGEAITLVRLDKSGGCVDRDDAFMQQMRDAAIKEYFFGDAKRTLSPHTQVVNYDELSIFKVREAHSMHSAFLPGGEEDAEPTQYEKVEPVPMMLHCIFAVMHASTRDSQDTIRDASVMGFVYVAEVDEKKKRLKILAPLNTRVTDRPLIWGSWPEAPVNLMG
The following text describes a protein:
Function:
Translation regulator forming a complex with MCTS1 to promote translation reinitiation. Translation reinitiation is the process where the small ribosomal subunit remains attached to the mRNA following termination of translation of a regulatory upstream ORF (uORF), and resume scanning on the same mRNA molecule to initiate translation of a downstream ORF, usually the main ORF (mORF). The MCTS1/DENR complex is pivotal to two linked mechanisms essential for translation reinitiation. Firstly, the dissociation of deacylated tRNAs from post-termination 40S ribosomal complexes during ribosome recycling. Secondly, the recruitment in an EIF2-independent manner of aminoacylated initiator tRNA to P site of 40S ribosomes for a new round of translation. This regulatory mechanism governs the translation of more than 150 genes which translation reinitiation is MCTS1/DENR complex-dependent.
Sequence:
MAADISESSGADCKGDSRNSAKLDADYPLRVLYCGVCSLPTEYCEYMPDVAKCRQWLEKNFPNEFAKLTVENSPKQEAGISEGQGTAGEEEEKKKQKRGGRGQIKQKKKTVPQKVTIAKIPRAKKKYVTRVCGLATFEIDLKEAQRFFAQKFSCGASVTGEDEIIIQGDFTDDIIDVIQEKWPEVDDDSIEDLGEVKK