lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
[Isoform 1]: Mitochondrial scaffold protein, of the core iron-sulfur cluster (ISC) assembly complex, that provides the structural architecture on which the [2Fe-2S] clusters are assembled. The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (Probable). Exists as two slow interchanging conformational states, a structured (S) and disordered (D) form. May modulate NFS1 desulfurase activity in a zinc-dependent manner. Modulates the interaction between FXN and the cysteine desulfurase complex; [Isoform 2]: Cytoplasmic scaffold protein, of the cytoplasmic core iron-sulfur cluster (ISC) assembly complex that provides the structural architecture on which the Fe-S clusters are assembled and may be involved in the cytoplasmic iron-sulfur protein biogenesis.
Subcellular Localization:
[Isoform 1]: Mitochondrion; [Isoform 2]: Cytoplasm. Nucleus.
Sequence:
MAAAGAFRLRRAASALLLRSPRLPARELSAPARLYHKKVVDHYENPRNVGSLDKTSKNVGTGLVGAPACGDVMKLQIQVDEKGKIVDARFKTFGCGSAIASSSLATEWVKGKTVEEALTIKNTDIAKELCLPPVKLHCSMLAEDAIKAALADYKLKQEPKKGEAEKK
The following text describes a protein:
Function:
Transfers electrons from cytochrome c551 to cytochrome oxidase.
Subcellular Localization:
Periplasm.
Sequence:
MFAKAVAVSLLTLASAQVFAADCKVTVDSTDQMSFNTKAIEIDKSCKTFTVELTHSGNLPKNVMGHNLVISKEADMQPIATDGLSAGIDKDYLKEGDDRVIAHTKVIGAGEKDSVTFDVSKLKADEKYGFFCSFPGHISMMKGTVTLK
The following text describes a protein:
Function:
Subunit e, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Part of the complex F(0) domain.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MVPPVAVSPLIKTARWSALLIGVIYGKQRFNYLKPIAEEERKVEEAEKKAREEQERINKQLAEANSDTILK
The following text describes a protein:
Function:
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTLRAKVFLVILVVLAGLLVSFYLIYQSVSGAVVETVKKNATVQIQVLSNYFAEKLNKYVERAVALTQSMEAQLLDTYSMASNMVKLVKEASNTLIAGITIEEMTGSGYIAKADGLEQIDSSSTIYQKYMDLVKNSQNPYLVTSDVFEGKPALVVLAPLGAFGAGTLGAVGYVIDLSQNKNFWRTVAEGGKLGESGYGLLVTSDGKVLIHKDMGNFMKDVKELGGFEKAFEEAKKGGEKYVEYEYNGEKKYTVWEKVPGYDFYIFSTGYLDELLAEGRKATLGTIVTYVVFGGVIFAVLFVSMMPVVKRMRQQVEKVKRFGEGDLTVEFEAKGEDELTQIEESLKEAVLSLKEMIVSIIEAAKELSGASEEIKVLSEESHKMSENLHEEAKKILDEANNMSSALTEVTSGVEEVAASAQNISKITQDLTERSEAVTKAAREGTERVEAVGGVINKLKGSAERQRDYLRELVDSAKTIGEIVDTISSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEIRKLAEESQRATEDIAKMLSSLRTTIEHVENGSKEMFEGVDEIAVMGEEVTKRFREILGRIEEINSMIENTAATAQEQGAAAEEMASAMDNVTKIVEGVVESLNRMESLIEDQTTSAAKVSQAAERLSELSEQLSTLVQKFKV
The following text describes a protein:
Function:
Involved in translocation of long-chain fatty acids across the outer membrane. FadL may form a specific channel (By similarity).
Subcellular Localization:
Cell outer membrane; Multi-pass membrane protein.
Sequence:
MSQKTLFTKSALAVAVAIISTQAWSAGFQLNEFSSSGLGRAYSGEGAIADDAGNVSRNPALITMFDRPTFSAGAVYIDPDVNISGTSPSRRTLDADNIAPTAWVPNVHFVAPINDQFGWGASITSNYGLATEFNDTYAGGSVGGTTDLETMNLNLSGAYRLNEAWSFGLGFDAVYARAKIERFAGDLGQLVAAQNPALAPVAGQIPSDTKIAHLNGNQWGFGWNAGILYELDKNNRYALTYRSEVKIDFKGNYSSDLPIAINRFNLPIPTATGGATQSGYLTLNLPEMWEVSGYNRVAPQWAIHYSLAYTSWSQFQELKAKSTAGDTLFEKHEGFKDAYRIALGTTYYYDDNWTFRTGIAFDDSPVPAQNRSISIPDQDRFWLSAGTTYAFNKDASVDVGVSYMHGQSVKINEGPYQFESEGKAWLFGTNFNYAF
The following text describes a protein:
Function:
Metalloprotease.
Sequence:
MEDDLLSDDGSNALLDSTAYTCMDTANLVCLRVINGSRVEVKGHRIESQVAMKARGRTWICLQNLEVVPGGGDAGSPAPQSPNESPETLIDGMLDIIAENEGIDGENNHLGDHGHLIDADIYEEIEGLEEDETRRKRRNALRDRESLWPGGAVPYVIDGYYNINHKKQILAGMQRFHEKTCIRFVPRTIERDYIFFTQNLGCWSMVGRTGGRQKISLSGTCRGSRGVIMHELMHAIGFRHEHNRPDRDGYIDVYWQNIKAGFTTNFRKYSNDQVQTLGTGYDFMSLMHYPLTAFSNDGKSVTIGPRYPTYQIGDVGNQNDFSHIDIYRINLLYKCGQCEDSDKYYCPIWAMMGECSANKEWMTKYCPFSCDRCTIALRKGDGLACIDTTSNCKRWAKIGECERNPAYMLQNCRRSCKQCKAIDTETGQEDELACQDDNTLCYDWATLGECRTNSKFMKAHCRRSCHVCTGGDGRIIIDTDSDDCQDTTMDCALWAAQNMCKDRQEWMSERCRRTCLWCSHRIVTITDQPDESRVDSEGGIITDETTRAGDEVNRVDDEMGVLGDENSRVGGGETRGRKGEIGASEGEDFGDRTNDEKSSDSDGGSNVEGNPRVESQIHAEGELYGGSVNSTGWIKPQGCVDEHDTCSSWASEGDCISNPEWMAIKCPVSCGLCGDTDIEPACVDRHRNCSYWAMIGECDEYPDWMHVKCPQSCGLCGPQPTAEEIEACADNHLFCKHWAKTGSCDSGHVWLRVHCKKSCDFCSLPKLNPTCMDSQQRCRELALKGECRSNRGWMAYQCPHSCDTCKKQNRFEECRDKTRRCQQYAADGQCHTRQLFMEDVCPYSCGFCRVGKTLRSGRYRTFDPALLGGMQTQTEQNGAGAGNELLPASKRRPHQSLRSRLRLSSTRVNSNNNVNTNENSNNNVSTNANSNTNVSTNDNSNNSVSTNQNRRGRFLTSSGQNNSRECRDRNPQCPTWAKTTRCLVNQGYMQENCQLSCKWCPPVETCVDIDAGCEKWARGGHCLTNEEGLRDKCQKSCGHCGEVEECRDVHRKCREWKKGGWCTRSPLFMRKFCAPSCGLCDENRQGNQNVTVVQPVPETAPVKGKKTKQTKQPRLTKQQKLEQQEQEAEQQRVEQQIRERQRQDDGYIALGLEEVQRLLLNTDGDLTAKQIKSLKRARKAIKQRQQREKELRAIQKKAKLNNLNRETEPIIDRLDEAAVRE
The following text describes a protein:
Function:
Sugar-phosphate phosphohydrolase that appears to contribute to butanol tolerance. Catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate. Is also able to dephosphorylate other sugar phosphates in vitro including ribose-5-phosphate (Rib5P), 2-deoxyribose-5-phosphate, fructose-1-phosphate (Fru1P), fructose-6-phosphate (Fru6P), and glucose-6-phosphate (Glu6P). Selectively hydrolyzes beta-D-glucose-1-phosphate (bGlu1P) and has no activity with the alpha form.
Sequence:
MRCKGFLFDLDGTLVDSLPAVERAWSNWARRHGLAPEEVLAFIHGKQAITSLRHFMAGKSEADIAAEFTRLEHIEATETEGITALPGAIALLSHLNKAGIPWAIVTSGSMPVARARHKIAGLPAPEVFVTAERVKRGKPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAVNAPADTPRLNEVDLVLHSLEQITVTKQPNGDVIIQ
The following text describes a protein:
Function:
Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains. Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MTMHEKMKLPSCSCSAFKCGKKDRWLNMERPIPFLLIGLTTILSVFILYTLNPLKFVIEHNIDQKLLLIKPHKEEDKCDLFNGNWVPDFEGSIYTNSSCATIPTSKNCFRNGRKDQDFLNWRWKPERCDLPRFDATAYLDIVRGKTLAFIGDSVARNHIESLLCLLSQKEVPVDAYLDSEDRNRIWHFPVHNFTLKMLWTKFLVHGEERVINGSSSGIFDLYLDKVDENWARDLHSLDYVVISDAHWFFRQVYLHRGSNVVACVYCNEANVTDRGVAFALRMAFRAAFSQINHCNKCKGIVTLLRTFSPSHFENGFWNTGGSCNRTSPYNDQKINFGAYEWEIRSMQVEEIERAEKRGKKGKSFGVLDVTMAMLMRPDGHPGAFWGNQWMKGYNDCVHWCLPGPIDVWNDLLLAVLRRLD
The following text describes a protein:
Function:
Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein.
Sequence:
MILFPVNGGWSPWSPWTECRCPGATLSSGKMSTRTCTHPPPSNGGLPCQGLSVRKTKDCITCPQVEPARWSQWSEWSHCNSDCLKTRRRQCIPGNGQGRRTCNGKDTQTTSCTSEQCRSMELSRVREANLENTKNDIAIYIGVTVAVFFVSMLSFFLTRMYWKKNRHQSLYNMASNDYHPEFFPEQDKKSLSLQPDLTQTVPPCYEYPYTTPATSVTRSVSEHHYDVPHLTSGSDIQMSPATSSTLESSSGKRSQLSGFTNNSDSTYEVATESVTLPLPTAYAVTPTTSGNYTSATVTHSGAFLNLLESGVSLVVPEGAISRTKKQELFLSILNEDCFRPKLAENLTQLSPVVSCGPNISLNKSVVLRIPHCAELSRNNWSISVLQSDCSDSQWQNAVTLGQETINTSVFCQLDKDAGYLVTDCLSRFVIVGQSTNGMALKRLKLAVFAPKLCFQSSVDYSIRVYVLEDTDSSMETVFGQEKRLGGYLLDEPRSIVFQDGGNNLCLTLDSLSEGWKTKPCSNYQEIPFRHLWQASSNSLHCSFTLESYEISRCLNFKIRVNQKGFEYHQTFDITCRDDSDVSVSKTSSGKVVPKIAIQSEAKKVVDFGHSPKSAKFKEEVKMAKNLLVTDRGVSTCDDFNFRLSRQLRKQLCQCLDPPTPRGNDWRMLAHALSVDRYINFFATKPSPTDCILDLWEARNRQSNALTELKQIFSDMERFDAVNILDNCLGPNWL
The following text describes a protein:
Function:
Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
Sequence:
MPKNKGKGGKNRKRGKNEADDEKRELVFKEDGQEYAQVLRMLGNGRCEAACIDGMKRLCHIRGKMHKKVWIAAGDIVLVGLRDYQDDKADVILKYMPDEARLLKAYGELPENTRLNEGIAGGLDEEEDGAGDDYIEFEDEDIDKI
The following text describes a protein:
Function:
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MLVVEVANGRSLVWGAEAVQALRERLGVGGRTVGALPRGPRQNSRLGLPLLLMPEEARLLAEIGAVTLVSAPRPDSRHHSLALTSFKRQQEESFQEQSALAAEARETRRQELLEKITEGQAAKKQKLEQASGASSSQEAGSSQAAKEDETSDGQASGEQEEAGPSSSQAGPSNGVAPLPRSALLVQLATARPRPVKARPLDWRVQSKDWPHAGRPAHELRYSIYRDLWERGFFLSAAGKFGGDFLVYPGDPLRFHAHYIAQCWAPEDTIPLQDLVAAGRLGTSVRKTLLLCSPQPDGFKSQEVSINLVYKCS
The following text describes a protein:
Function:
Required for the correct organization of the nucleolus during development.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVVTRARTRRLSLLETDSRPSTPQLDTVAELGTASPRATRRTRLNSSTLDVRTPTRTRRASLARGETPEPTTPSSVKRTARTPAKNTRSVRQQLTLTEEPEENEVKQEKPSPSPSPVPKEGKGKAQRKPSVSPSPGRTLTPNQQSDEKRVTRSMSQTPPMPTRSSSNTPRDLNDSPKVEQKAKPNIKTTPKVAVRLEKLSMDKFSGKKMEKAKPLIVPDELKDNGVVEEQNKSITEAHSQAPETHESAQPDKDAGKQSFLKSFTTLSKIQGSSKALHPDESADTITKITPTSTSKKIEENMDDVFETLRVESPKVERKIETLQKVHTVGTPEIKEKDEPVGVDNEIKTKTETPQKIEPPIIESKVETQQLIDHPQIEKKRDTPQNVSTVDLMDTSPEKDESMEDQEFLDAEDSIVQLEPQTDEPVEKPKELEFVDLDDDEPVFPSEAPKYVEDSKEVHPDDSMDDDKQNKIDVTEVIHLPSIRARAVRSPAVEQKKSVDFNNDTDDLEVEKKRFPKTPGREKVPVCRILTPKPETPLKLALQKGRNSSTPILKDQERGLSNSTEELHPAPPQIDAIKPFDELESKNAKDEMVEQSPMSKQKAENKILARLESFEEDVEDHGNEEENEEEHEEDKSISEFVDLEAEDAGKDYMSGDSMDSSLRREMEENEIPIDGESVGSKDTEESTPEESDGDDSFIVSDNEDEEDLGQLCYSSGEDEIEDAEESEQAERSSVKRRRIIIASPSDEEHDGKVQSNDDSSENKTEKPKNQSNCSSNASKLSEAAQLLNVSEEKSSISETELERSRQVALNELNKSERFNKTETQLDISVMEVDSSDHDEEEKTEKVGAKNNRSLYEIVDSDDGEEQDQDQSDADKPAESENHSEIKKSTSFMDQMSGAKGNKSVYEIMDSYETEDPKEAGKNEESDKDKPAENGKSDKDKQAETEMSDEDKPSEIKSPSTIKKSIISTADEEALLAELASSDLSHLEKMFNPLQKSRRQSLHVPSPELAAKNPKLRRRSERVEVGNDFCPSQSFVDMVAEKKRQKNKRKRLSKSLSGAPEDLEEMEIKHERKRLKSSHGASTDSMEEDNENETMTVAEEHHSDGEVSNGEVPIEEKPTTSSEKPSASELPEEEETVAVEELLMEKPKTCDSPRSEERPTEIVTSKPKGMAPVKVEKTAEYYLAYCHNLLEAANEAKLKEKKEHLASGAKQKKPKRIAAQAPSKLLGTIGSESETNTAKSSKQPPALKKDVKRLQAARQAVSHAVNLLAPPKATEAEPRTLSRKLSPQPPVVDKKSAKQKKGKKKQKPQEASPLKSSDEENHGHRIRTNAGYVTVVDEPPTKVPKIELIKTSSGMVRVEPCTPKQKYFRELPPTPKMHGFREEPGPSGMSRKRAKHAAPKVEHNSAKQAALRFKEQIFARRS
The following text describes a protein:
Function:
Receptor for hyaluronic acid (HA). Involved in cell motility. When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including the PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity. May act as a regulator of adipogenesis.
Subcellular Localization:
Cell surface. Cytoplasm. Cytoplasm, cytoskeleton, spindle.
Sequence:
MSFPKAPLKRFNDPSGCAPSPGAYDVKTSEATKGPVSFQKSQRFKNQRESQQNLNIDKDTTLLASAKKAKKSVSKKDSQKNDKDVKRLEKEIRALLQERGTQDKRIQDMESELEKTEAKLNAAVREKTSLSASNASLEKRLTELTRANELLKAKFSEDGHQKNMRALSLELMKLRNKRETKMRSMMVKQEGMELKLQATQKDLTESKGKIVQLEGKLVSIEKEKIDEKCETEKLLEYIQEISCASDQVEKCKVDIAQLEEDLKEKDREILSLKQSLEENITFSKQIEDLTVKCQLLETERDNLVSKDRERAETLSAEMQILTERLALERQEYEKLQQKELQSQSLLQQEKELSARLQQQLCSFQEEMTSEKNVFKEELKLALAELDAVQQKEEQSERLVKQLEEETKSTAEQLTRLDNLLREKEVELEKHIAAHAQAILIAQEKYNDTAQSLRDVTAQLESVQEKYNDTAQSLRDVTAQLESEQEKYNDTAQSLRDVTAQLESEQEKYNDTAQSLRDVTAQLESVQEKYNDTAQSLRDVTAQLESYKSSTLKEIEDLKLENLTLQEKVAMAEKSVEDVQQQILTAESTNQEYARMVQDLQNRSTLKEEEIKEITSSFLEKITDLKNQLRQQDEDFRKQLEEKGKRTAEKENVMTELTMEINKWRLLYEELYEKTKPFQQQLDAFEAEKQALLNEHGATQEQLNKIRDSYAQLLGHQNLKQKIKHVVKLKDENSQLKSEVSKLRSQLVKRKQNELRLQGELDKALGIRHFDPSKAFCHASKENFTPLKEGNPNCC
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.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Endoplasmic reticulum membrane.
Sequence:
MAIYDSQLTVVALYSLIIIAIYSAKFITPLNELLQYGKTVSQDVREHARLENNLIKQTIGFISKYFVVPKAWFVHFYITLFALSSLIFLASFNEPISSDPEKFKNLILIHRLLWVQGIRRLTECLTITNFSKTSKMNVSHYVVGLSHYILVTWATYLGLSKYGSHQVPNNYTVFDIVLIIGFAICSLLQFQAHYHLSTLVKYTLPDFKFVSSPHYFYEILIYTILLSFAIKDGFDMVSVTFFTAWLFVISNLSISSLETFSYYQKKYKEEFKLKWAVLPGIL
The following text describes a protein:
Function:
Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.
Subcellular Localization:
Cytoplasm, Stress granule. Nucleus, nucleolus.
Sequence:
MARGKRRNPSNRNQDYMAPSEPNSPIKTNMEYPNTPEKQDLVPKSFLIMMLEDFKKDVKNSLREQVEAYREESQKCLKESQKSLKEFQENINKQVQAHREETQKSLKEFQENINKQVQAHREETQKSLKEFQENTIKQLKELKMEIEALNKEHMETTLDIENQKKRQGAVDTSFTNRIQEMEERISGAEDSIEIIDSTVKDNVKRKKLLVQNIQEIQDSMRRSNLRIIGIEESEDSQLKGPVNIFNKIIEENFPNLKKEIPIDIQEAYRTPNRLDQKRNTSRHKIVKTPNAQNKERILKAVREKGQVTYKGRSIRITPDFSPETMKARRSWTDVIQTLREHKCQPRLLYPAKLSINIDGETKIFHDKTKFTQYLSTNPALQRIINGKAQHKEASYTLEEARN
The following text describes a protein:
Function:
Enhances the tyrosine carboxypeptidase activity of vash1 and vash2, thereby promoting the removal of the C-terminal tyrosine residue of alpha-tubulin. Also required to enhance the solubility and secretion of vash1 and vash2. May play a role in axon and excitatory synapse formation (By similarity).
Subcellular Localization:
Cytoplasm. Secreted. Cytoplasm, cytoskeleton. Note=Detected both intracellularly and extracellularly. Within cells, localizes mainly to the apical part of the cell.
Sequence:
MDPGAGARKERPKPREPAARLEKAKQRSAQQELKQRQRAEIYALNRVMTELEQQQFDSFCKQMQGSGE
The following text describes a protein:
Function:
Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Domain:
The LID domain is a solvent-exposed domain that closes over the site of phosphoryl transfer upon ATP binding.
Sequence:
MLIAIEGVDGAGKRTLVEKLSGAFRAAGRSVATLAFPRYGQSVAADIAAEALHGEHGDLASSVYAMATLFALDRAGAVHTIQGLCRGYDVVILDRYVASNAAYSAARLHENAAGKAAAWVQRIEFARLGLPKPDWQVLLAVSAELAGERSRGRAQRDPGRARDNYERDAELQQRTGAVYAELAAQGWGGRWLVVGADVDPGRLAATLAPPDVPS
The following text describes a protein:
Function:
Functions in the biosynthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the addition of L-lysine to the cyano group of 7-cyano-7-deazaguanine (preQ0)-modified tRNAs at position 15, to generate q0kN15-tRNA, a q0N lysine adduct identified as 7-N-[(5S)-5-amino-5-carboxypentyl]formamidino-7-deazaguanosine.
Sequence:
MTQYFEIENRDGAARIGKLLLFPEIRTPCALHTAALGDLENPGPIVDAGSLWIADQKELEARIKEIREKTGKGTLIILPHQTYPPAVPAESTGKVEAFTATGDENAEAEGPTGSLLRAEGEVRKSDLYIMEGAGTLENNARRFLETLIDLKNRIPPDTALYAPKLALPENAAMLAYVGIDVMDDTRAEIAAYSDIYLTAAGSFYLDSLVEFPCRCRVCAATTPAELRALPKADRVELLSAHNRDALDAELALVREKIRTGNLREYVEGQCRVRPWLTALLRLGDFEYSYIEEKVPAFRQSQLLADTSEALSRIEVVRFARRIQERYAPPDLDVLLLLPCAARKPYSTSQSHQKFILALGKYRKFVHEVIITSPLGIVPRELELTYPAAHYDTAVTGHWDEEEKAWVSGCLESYLSKHMYKAVVAHVEGAYREICERVAEKLGIDVVYTAGESLASYESLTNLKNTVEAICTSKDFSRKSQNAEKEKKNFIKAVAGYQFGEGAGHLFSEEVGDPLVKGRFPKYQLFAGKKQLATLIPQYGMLALSPEGAELVLKSEKYVVKIDDFVPRGSILAPGVLDAGPEIRPNDEVIVLGKKALCVGRAMMSGREMKESGRGVAVDVRHVKKL
The following text describes a protein:
Function:
Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Localization:
Cell projection, cilium membrane; Multi-pass membrane protein.
Sequence:
MVTKQFQTNRAAMALLTFYSTPLVREYQSTLISRACFFACLCFLVCVFAPLLVAYSSHGFWVKHNVHREQPDVRFKYQALLLARSPSSDVTWSTFTEYNSLTSQYLHFPSITVMEKDEDDDGLLDGLDLSLELETNQTIHFIQLFLIFSYRLKDISSITMESLAVIQYNSGIPLTGLHYVGDLQWLQKRMLNYRQSDNRYNQTVMGQFEISDLLRAYNERDYGTETRNGHYSPIYGPSDGLLRVHSYIRYTEAVLEYTPGLWNVLKWAWIQYASILLIFSYVVGIFKNVVFGQQMIPTWNEKCIKTVSHNFK
The following text describes a protein:
Function:
Potential regulator protein for the acrEF/envCD genes.
Sequence:
MAKRTKAEALKTRQELIETAIAQFAQHGVSKTTLNDIADAANVTRGAIYWHFENKTQLFNEMWLQQPSLRELIQEHLTAGLEHDPFQQLREKLIVGLQYIAKIPRQQALLKILYHKCEFNDEMLAEGVIREKMGFNPQTLREVLQACQQQGCVANNLDLDVVMIIIDGAFSGIVQNWLMNMAGYDLYKQAPALVDNVLRMFMPDENITKLIHQTNELSVM
The following text describes a protein:
Function:
Master regulator of recycling and plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Associates with both constitutive and IFNG-induced PD-L1/CD274 at recycling endosomes, where it protects PD-L1/CD274 from being targeted for lysosomal degradation, likely by preventing its ubiquitination. May stabilize PD-L1/CD274 expression on antigen presenting cells and potentiates inhibitory signaling by PDCD1/CD279, its receptor on T-cells, ultimately triggering T-cell anergy.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Recycling endosome membrane. Note=Co-localizes with PD-L1/CD274 in the plasma membrane and in recycling endosomes.
Sequence:
MENGAVYSPTTEAAPGTGRGARSGLAAYFVLGRLPWHRRILKGLQLLLSLLAFICEEVVSECGLCGGLYFFEFVSCSAFLLSLLLLIVYCTPVHDRVDTGKVKSSDFYITLGTGCVFLLASIIFVSTHSGTSAEIAAIVFGFLASSMFLLDFVVMLCEKLRESPLRKPENNAKVEALTEPLNA
The following text describes a protein:
Function:
Cationic peptide that possesses multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage-gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism.
Subcellular Localization:
Secreted.
Sequence:
YKRCHKKGGHCFPKEKICTPPSSDFGKMDCRWKWKCCKKGSVN
The following text describes a protein:
Function:
Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MRPLTEEETKKLFDKLAQYIGPNTAHLLQQKGTKSAGVAPFNNGKTTGNNGSNDDDDGDDGEEQNSQQTYVFRLHKNRIWYMPLRLAKLASCVAKSNLMGIGVLFAKVTHHGHVRLQVTALEYIAQYSLFKVWLKPSQEQKFLYGGHVTRAGLGRITEATPRHQKVAVFSMGDVPLGFGVAALGTLECRRCEMNSTVLFHEADVGEYLRNEARLT
The following text describes a protein:
Function:
Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization (By similarity).
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, actin patch. Note=Cytoplasmic and cortical actin patches.
Sequence:
MYGYQGTGGQQPLGAQPTGFGFGNTPVQQQQQPMQPMQQSQPTGYQAPGGFQNYQPTGFAQQQQQQQPQQTGFQSMQPPMQQTGFQSQPNVSMYQGGGGQGYQSAPMLHQQTMQTGYQPQQQQPGFTGFQPQQQQQQQQTGFTGFQQQPQQQQPGFTGFQSQPTGYNANASAPAATPAAPLQQQKTGNARDPFAPTLPARPPLTSQPTGGGNKSVVDGVYIPNVRLSFLTADDQRNFENLFRQALPKGEQALSGDKARDILFRSGLPPITLSAIWNLADTTRSGALLFPEFAVAMYLCGQAVKGQTVPNNLSENIKNEVSSMVDIISFNIPDAGSRPSSSGQSVPQSQPQQQQQQSSASMLAGLNLGQPTGYQQQQATGYQPMQQQSTGYPMQAMQPQITGGMPLQQQRTGPMQPLQQQSTGYAPLQSQLTGGAPLQSQLTGGAPLQSQLTGGAPLQSQLTGGAPLQQQSTGYAPLQQQSTGYAPLQQQSTGYMPQQQTGMQPQSTGYGSMQPLTAMPTGKPGQWGFINTPSQGLPGIETMQQRLMPQATGAPVQQLPPMQLQQSATVNWAIAKEEKQIYDGIFMAWDKKRAGAIDGDTAIKIFTQSGLNRADLEAIWTLSDPSNKGRLDRDEFAVAMHLIYRHLNGYPIPSRLPPELVPPSSKNFSDSVNQVKSYLKAGGGRTGGSKLKSRSFTGDSTIKKDATVFKNDDSDFGYTSRNRRGGSSSTASSNGSSGNDISLSGKGSSISELKKLIREKQILLDAIDAEDSDMSRDSNLERRDQEAVADLKRRIQNVQRDIDVAPHSAISTDVGASADAKRNLMRKLDHLGDRLPQLASNVRRIEDKIANAKMELFRLKNPTSLVGTGPGGAITEADRIKARSKAKLQARMAALTGKGTTTGADASEEEDYEHRLLTHTSEVERSKAQNYEMIHDIEDSVKSLQRDLSSKLRETQEEVSEDRQRRRWEEAVGVEDDVRQFIYSLRSTRSSRPAPATASSSAPATGSPATAAPISATSTGASTPSAPAAGVDRKAQLKAEAERKMNERLAALGIKRKEKAQAHGFAPPDAKPAEASPAASPAVASPAVASPAATPAVSSPAPVSRGVPAPAAATPATDPATTPAVPVSAPADDSDSDDEEYEKLMAQKREQEERFKKQQEADKKKEEEKKQKKAAKEERMRKLREEMEANEAREKAWKESQSKEAEADEAEGDVGAAALAAFSNKATAPSTTPTAVAATPPVATSTPSPAAPTVPAADDNNPFHRLNNGGDAAAAAPAAGGEDNNPFLRPGTNQPIAAPSPASFSEAPKEAPKPVDPVKISNQRANQRAAKNDDDDWGMSSDEDDDQDYHRGNAAELASQLFRTMAPPIQRQPTGGAPITATPTGSAPAAPPAAPPVAPAAVEVAVAASEATPGPESAPPAPPMPEINIPPATEAPSAPAATEAPPAPPSAPTTIETTHLPPPVDTHNDMSSSEFDFETPEGSPTQQTFAEAAPPVAAPPPPPPTAAAAAPTGIPPPPPSAPGFGAPEAPSGIPPPPPPAPGFGAPPPPPGPAPSFDAPGGAPPPPPPGPPPPMFGAPAPPSMTGPSAGDLPERPPAATGGITALLGEITGGKTLRRVDDKDKKISSNPSAGAVLN
The following text describes a protein:
Function:
Positively regulates the expression of 5 genes involved in the catabolism of certain amides (amdS), omega amino acids (gatA and gabA), and lactams (lamA and lamB) in the presence of omega amino acid inducers.
Subcellular Localization:
Nucleus.
Sequence:
MSSTAHPTNLAPSGNGSAACVHCHRRKVRCDARLVGLPCSNCRSAGKTDCQIHEKKKKLAVRSILDPVPIRCRPPNPEEAPKPISSLSPSSEPPNAFTTALRAVQSDITAPSGVANRVAHIRSRSSQYDTKGTRSNNNSGNNTQYQNVLPEPDSPPYSRPAASDPSEGESRADIEKRLVNLIDGEASDSRAIQRGVRAIYVGHELSNMSFLIRQQRDTGDDVYHFAGNEIPRRQLRTGHDQLLMDALTLPEPALADELVHAYFAQVNPGYPIVEEELFMSQYRNRDPADAPPILLLQTILLVGAHVTRPKSERDTLKDIFFRRAKWLFDNRIERNRDILVQAALLLTWHSDLADDDVSANAHYWIGIAARIATGLGMHRNPVCSRFVPRDRRMWRRLWYILVQFDVMVSLSYGRPQALNLEDSDVSPLTFSDFEGCGARVQADFVIHFSELCTMISYIVRERFGLRISAERRKAALLEADEALANWSLRLPDRLRLRASDMDPWSAMLHLTYNNFLILLHRPHPRASAYSDDYGPHDAEICSAAAGVIASIFEELRIHDRLKQVWYSGVHTLFTAMIQVRVELRFSNPVLAINALRRFDSASYSLRELAQYWSHASTILRLFEESRRLQEDLRTTTSDRPRRFSNLSNNSTNSPASQQKNTSGIPHLANINSSDATPPSAPSIPPLQPSSQLSYEVPTTESAHHNPRSQPTLSAHTHTYTTQPFDTWIPSNNLTPMDTVDNSREMLDWRQLFSFTDLEGPVLPSTMEGITELEDEWRQIYWQETPMSDLLQDGGWMHG