lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Specifically demethylates trimethylated H3 'Lys-4'. Required for the correct regulation of homeotic genes during development. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. Regulates the expression of clock-controlled genes including tim, per and cry.
Subcellular Localization:
Nucleus.
Sequence:
MSAKTEADNTTAANSGGGGVGSGTSSGGGASANGTATPARRLRTRNSTGNGTNSGSESVKKSNANDEPSTPVTPAGATGSHTHAPPGISPAVMERPMPSVPMNHASSSVSASKKYHNSCPHPTPTPAPTGHKKSVHTQPHSSNKFDQGKNEEFHFDTPPECPVFRPTTEEFKNPLAYISKIRSIAEKCGIAKILPPATWSPPFAVDVDKLRFVPRVQRLNELEAKTRVKLNFLDQIAKFWELQGSSLKIPMVERKALDLYTLHRIVQEEGGMEQTTKDRKWAKVANRMQYPSSKSVGATLKAHYERILHPFEVYTSGKVLGPTPTSSGSGSTPVKLEDGGGTDYKAHEIPTRQQIAPPNETNTRRSKRFGNSNASCGLSGVTPTTKPSAGVFVKTETKEEFKRDLLSSFNAVNSGGSPLATGTTANTRGASQKKGGEPPALIVDPLMKYICHICNRGDVEESMLLCDGCDDSYHTFCLLPPLTSIPKGEWLCPRCVVEEVSKPQEAFGFEQAEREYTLQQFGQMADQFKQEYFRKPVHLVPTEMVEREFWRIVSSIDEDVTVEYGADLHTMDHGSGFPTKSSLYLLPGDQEYAESSWNLNNLPLLEDSILGHINADISGMNAPWMYVGMCFAAFCWHNEDHWSYSINYLHWGEPKTWYGVPGSCAEQFEETMKQAAPELFSSQPDLLHQLVTIMNPNILMNNRVPVFRTDQHAGEFVITFPRAYHAGFNQGYNFAEAVNFAPADWLKMGRECVNHYSMLRRFCVFSHDELVCKMALEPAKLTFGIATACYIDMAEMVDTEKKLRKSLLEWGVTRAERRAFELVNDDERHCQECNTTCFLSAVACECNDKLIVCLRHYTVLCGCAPEKHTLIYRYTLDEMPLMLQKLKVKAHSFERWLSRCRDIVDAHTPTSVTLQELQELCKEAETKKFPSSLLIDRLNAAAVEAEKCVTVIQQLGINKVRTRSDHNQEAAQYKLTMEELELFVQEIDNLCCIIDEGASVRELLVLGKQFVERSESQLQLSLESLEESELETLINEGSSLRIELQQLDLLQKRLKQCKWYKRSQGLRETSSKLTYQDVKNLLHIAAADLDPTDPYVDKEMRKLQQIGADIEAWESQAAKYFRRLTQQHELGEIEQFLKSASDINGQVPSHGLLKDALRKAREWLRAVEQLQQNNHVTYCHTLEAMIERGLNIPIQLEELSRMQGHLNSAHQWKDNTACAFLKKGTFYTLLEVLMPRSDAINIDSDLKPRFQDDFLKEKNPAEIVASFKHAEEQELLDMRELRRQNMNKNPMRDMFCLCKSEFRNLMFNCQLCRDWFHEDCVPPPSATNQNGIVNGGSGPGTNRPKWLCPSCVRSKRPRLETILPLLVQLQQLPIRLPEDEALRCLAERAMNWQDRARKALSSPDVSAAQEAIMAQQQQKRRSEGGAGVGNISSPRKPRRRGSLTKEASGSTESDADDDDDEDECRLRIVEDNFSNDEDEPRTAPATSTVNSDLLKLLSDSEIENLLDLMMEGDLLEVSLDETQELWRILETMPPTLLQAEAMERVVQYMQRQRQQHTNPLPTSGAEDSNDSLMVQNSPNSNSNSGGATGSASNSGRNKKRRSNDTGGNSAVPRKKQSTPKQTPGKKGSAAAARKSDAKASPAASTTPGADADAENKQANGGNTNSSTGSGGGNSATTTPTPGSTHKKRKRTSTTATNNNNNNNNNSTNNSNSSTNLNSNTTSGQGAATGGNNATGGQKKHAQRSQQAAQEDDEEECRAENCHKPTGREVDWVQCDGGCNEWFHMYCVGLNRSQIKPDDDYICIRCTKTVAIGTQGSGHSMSVASTTTPGKQRAVQSAR
The following text describes a protein:
Function:
Binds specifically both D-ribose and D-allose, with affinities in the lower micromolar range.
Subcellular Localization:
Periplasm.
Sequence:
MKRVASRRLLAAVVLTACSSFLPLSAVHAETPEKPRIALVMKSLANEFFLTMEDGAKAYQKEHADRFELVSNGIKDETDTSSQIRIVEQMIVSGVDALVIAPADSKALVPVVKKALDAGIVVVNIDNRFDPQVLQAKKIGVPFVGPDNRKGARLVGEYLAKRLKVGDEVGIIEGVSTTTNAQQRTAGFKDAMDAAGMKIVSLQSGNWEIEKGNAVASAMLNEHPDLKALLAGNDSMALGAVSAVRAAGRAGQVKVVGYDNIQAIKPMLKDGRVLATADQFAAKQAVFGIQTALKLLAGQTPEHEKDGVVETPVELVTAP
The following text describes a protein:
Function:
Possesses antifungal activity against phytopathogenic fungi such as P.oryzae, R.solani and B.cinerea but not against phytopathogenic bacteria. Shows weak activity against the insect pathogenic fungus B.bassiana and against S.aureus. Binds chitin.
Subcellular Localization:
Secreted.
Sequence:
MKTLTFYTLLLCAALYSNFFDCKAVADAELPKLPDDKVLIRSRSNCPKGKVWNGFDCKSPFAFSKK
The following text describes a protein:
Function:
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
Subcellular Localization:
Peroxisome membrane; Multi-pass membrane protein.
Sequence:
MSNQELAHAVSGAVGGALALGITYPLITLSTIAQTAAKKKEAEEASTTEDGKKPQPTVSLTTLEKIAHVIQNNAAYIAAKEILKEKGPLGLYSGLESALYGITLTNFIYYYFYELTSNVFLRANGKKRNGLSTIQSIITGAIAGAFTCVGSNPFWVANTRMMTEKKKEKTATAGDAADAKEENDNSSNSTFKALVNIVEQDGVGALFAGVLPALVLVINPIIQYTIFEQIKNIIIAKDGPKAFTAVKAFFIGAFGKLIATSLTYPYITLKSRMHIKRKKLNIDNQQQDEEKQLSMIQEIRKIVKEEGLEGLYAGLAVKLTQSIATAAFLFYFKEELFSGSVKLIEILRVFSFKKSLKSPVVQV
The following text describes a protein:
Function:
Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components.
Sequence:
MSTDSDWYLIYTKPRQERIAEENLERQGYRIYLPFIQVNRRRSGCYQLITEPLFPRYLFILLNIDKDNWGPIRSTRGVSALVRFGGIPAKVPPDFVQFLKNNETSASVPPKVSLFQKGQRVQIIDGVMAGYEGVFEMHSGAKRVTLLLDMVGKVTRVEVPLDSVTGT
The following text describes a protein:
Function:
Acts as a negative regulator of the GCN2 kinase activity by disrupting the GCN1-GCN2 interaction in amino acid-starved cells.
Miscellaneous:
MISCELLANEOUS: Present with 10300 molecules/cell in log phase SD medium.
Sequence:
MDYKEEQKQELEVLESIYPDELRIINDEYPKIKFEVAIKLELDTGDSTSVLTKEHTIIAEFKLPENYPDEPCLISLEAQEVALNDNEEDNEEDEDEVEYDDHGNKVLKKFENLPDLISFKGYLPELTVQLESQIETDMLLGMQMCFALISSIKERCEQWYSEQLNKLEKQYELEAQEREKKEQAKFHGTKVTRESYLEWRSKFRQELKLDERDQVRRMKAHHGKLTGKQMFEQGVVGTGDEYMEEDDASVDDVAKGLAKTEIANQ
The following text describes a protein:
Function:
Cytosolic inhibitor of vacuolar proteinase B (yscB), probably regulating protease B activity during limited proteolysis. PBI2 is a component of the LMA1 complex, which is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi.
Sequence:
MSSLLYKRLLSTTRHLKMPDQKYIILLKDDSDAAKVKDVKDKVSSIGGKVTHEYDLINGFAADIPADHVSTFESDPNIKSIEKDQEVSIN
The following text describes a protein:
Function:
May regulate neuronal differentiation, polarization and axon guidance.
Subcellular Localization:
Secreted.
Sequence:
MEFILGIFCVIFCLRAGAGFGVDPSLQIDIFEDFQLGEATPGVQQVQGFHNRSKAFLFQDTSRSIKASAETAERIFTKLRNKHEFTILVTLKQAMLNSGVILSIHHADHRYLELESSGHRNEVRLHYRSGSHRSQTEVFPYILADDKWHRFSIAISASHLVLHIDCNKIYERIVEKTFMDVPPGTALWVGQRNNVHGYFKGIMQDLQIVVMPQGFISQCPDLNRTCPTCNDFHGLVQKIMELQDILAKTSAKLSRAEQRMNRLDQCYCERSCTVKGNIYRELESWMDGCKKCTCTNGTAQCETLTCSVPNCLSGFAPAYVPGKCCKECQPVCMYQGQMYFEGEQEAVQSSSGACVLFQCKSNTMQRIESPECLPLNCPQSQHITLRSGCCKVCKGHDFCSEGHNCVEYSICKNLNDKAVCICRDGFRALREDSAYCEDIDECTEGRHYCRENTVCVNTPGSFMCVCQTGYLKIDDYSCTEHNECATNQHSCDENAVCYNTVGGHNCVCQPGYTGNGTVCKAFCTDGCRNGGTCIAPNICACPQGFTGPSCEADIDECTEGFVQCDSRANCINLPGWYHCECRDGYHDNGMFSLSGESCEDIDECATGRHSCSNDTVCFNLDGGFDCRCPHGKNCSGDCTHEGKIKHNGQIWVLENDRCSVCSCQVGLVMCRRMVCDCENPTVDLFCCPECDPRLSSQCLHQSGELTYKSGDTWVQNCQQCRCLQGEVDCWPLPCPEIDCEFSVVPESECCPRCISDPCQADIIRNDITKTCVDETNVVRFTGSSWIKHGTECTLCQCKNGHMCCSVDPQCLQEL
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MRPVPVRLRTERQEKPGALKKLKGNKLIRHYHVLLKRKEQLKQRKANPKEIQKVQSELDMLGIDAYQKASQNGQNKRRGGDSSVILVEYVKSQKYPKTVYPIDLLEIGCVSIDNKCSTSKLFRVDRIDLHSTHPLIKQQDILERTPSEGMYGCISCSLVLNFAPPETRGDILLHCTRLLKPPTEQMKSLFFLVLPAPCVLNSRYMSLETISKMMEDLGLFTVYTKTTAKIVYLIYEYRKEPKSVIVWKKKELFKGATRNNFFIPLNTTEATRRPVNKDEQ
The following text describes a protein:
Function:
Histone methyltransferase specifically required for trimethylation of 'Lys-4' of histone H3 (H3K4me3) and is crucial for both sporophyte and gametophyte development. Function as a diurnal 'writer' to counteract the nocturne 'eraser' demethylase activity of JMJ14 thus orchestrating the circadian rhythm of histone modifications (e.g. H3K4me3) and modulating the rhythmic expression of diurnal target genes; this mechanism relies also on the circadian clock oscillators CCA1 and LHY.
Subcellular Localization:
Nucleus.
Sequence:
MSDGGVACMPLLNIMEKLPIVEKTTLCGGNESKTAATTENGHTSIATKVPESQPANKPSASSQPVKKKRIVKVIRKVVKRRPKQPQKQADEQLKDQPPSQVVQLPAESQLQIKEQDKKSEFKGGTSGVKEVENGGDSGFKDEVEEGELGTLKLHEDLENGEISPVKSLQKSEIEKGEIVGESWKKDEPTKGEFSHLKYHKGYVERRDFSADKNWKGGKEEREFRSWRDPSDEIEKGEFIPDRWQKMDTGKDDHSYIRSRRNGVDREKTWKYEYEYERTPPGGRFVNEDIYHQREFRSGLDRTTRISSKIVIEENLHKNEYNNSSNFVKEYSSTGNRLKRHGAEPDSIERKHSYADYGDYGSSKCRKLSDDCSRSLHSDHYSQHSAERLYRDSYPSKNSSLEKYPRKHQDASFPAKAFSDKHGHSPSRSDWSPHDRSRYHENRDRSPYARERSPYIFEKSSHARKRSPRDRRHHDYRRSPSYSEWSPHDRSRPSDRRDYIPNFMEDTQSDRNRRNGHREISRKSGVRERRDCQTGTELEIKHKYKESNGKESTSSSKELQGKNILYNNSLLVEKNSVCDSSKIPVPCATGKEPVQVGEAPTEELPSMEVDMDICDTPPHEPMASDSSLGKWFYLDYYGTEHGPARLSDLKALMEQGILFSDHMIKHSDNNRWLVNPPEAPGNLLEDIADTTEAVCIEQGAGDSLPELVSVRTLPDGKEIFVENREDFQIDMRVENLLDGRTITPGREFETLGEALKVNVEFEETRRCVTSEGVVGMFRPMKRAIEEFKSDDAYGSESDEIGSWFSGRWSCKGGDWIRQDEASQDRYYKKKIVLNDGFPLCLMQKSGHEDPRWHHKDDLYYPLSSSRLELPLWAFSVVDERNQTRGVKASLLSVVRLNSLVVNDQVPPIPDPRAKVRSKERCPSRPARPSPASSDSKRESVESHSQSTASTGQDSQGLWKTDTSVNTPRDRLCTVDDLQLHIGDWFYTDGAGQEQGPLSFSELQKLVEKGFIKSHSSVFRKSDKIWVPVTSITKSPETIAMLRGKTPALPSACQGLVVSETQDFKYSEMDTSLNSFHGVHPQFLGYFRGKLHQLVMKTFKSRDFSAAINDVVDSWIHARQPKKESEKYMYQSSELNSCYTKRARLMAGESGEDSEMEDTQMFQKDELTFEDLCGDLTFNIEGNRSAGTVGIYWGLLDGHALARVFHMLRYDVKSLAFASMTCRHWKATINSYKDISRQVDLSSLGPSCTDSRLRSIMNTYNKEKIDSIILVGCTNVTASMLEEILRLHPRISSVDITGCSQFGDLTVNYKNVSWLRCQNTRSGELHSRIRSLKQTTDVAKSKGLGGDTDDFGNLKDYFDRVEKRDSANQLFRRSLYKRSKLYDARRSSAILSRDARIRRWAIKKSEHGYKRVEEFLASSLRGIMKQNTFDFFALKVSQIEEKMKNGYYVSHGLRSVKEDISRMCREAIKDELMKSWQDGSGLSSATKYNKKLSKTVAEKKYMSRTSDTFGVNGASDYGEYASDREIKRRLSKLNRKSFSSESDTSSELSDNGKSDNYSSASASESESDIRSEGRSQDLRIEKYFTADDSFDSVTEEREWGARMTKASLVPPVTRKYEVIEKYAIVADEEEVQRKMRVSLPEDYGEKLNAQRNGIEELDMELPEVKEYKPRKLLGDEVLEQEVYGIDPYTHNLLLDSMPGELDWSLQDKHSFIEDVVLRTLNRQVRLFTGSGSTPMVFPLRPVIEELKESAREECDIRTMKMCQGVLKEIESRSDDKYVSYRKGLGVVCNKEGGFGEEDFVVEFLGEVYPVWKWFEKQDGIRSLQENKTDPAPEFYNIYLERPKGDADGYDLVVVDAMHMANYASRICHSCRPNCEAKVTAVDGHYQIGIYSVRAIEYGEEITFDYNSVTESKEEYEASVCLCGSQVCRGSYLNLTGEGAFQKVLKDWHGLLERHRLMLEACVLNSVSEEDYLELGRAGLGSCLLGGLPDWMIAYSARLVRFINFERTKLPEEILKHNLEEKRKYFSDIHLDVEKSDAEVQAEGVYNQRLQNLAVTLDKVRYVMRHVFGDPKNAPPPLERLTPEETVSFVWNGDGSLVDELLQSLSPHLEEGPLNELRSKIHGHDPSGSADVLKELQRSLLWLRDEIRDLPCTYKCRNDAAADLIHIYAYTKCFFKVREYQSFISSPVHISPLDLGAKYADKLGESIKEYRKTYGENYCLGQLIYWYNQTNTDPDLTLVKATRGCLSLPDVASFYAKAQKPSKHRVYGPKTVKTMVSQMSKQPQRPWPKDKIWTFKSTPRVFGSPMFDAVLNNSSSLDRELLQWLRNRRHVFQATWDS
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane. Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes. Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA. SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER. Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA. Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development.
Sequence:
HKQENSLFEEMLEDNIIYVMDASIGQSCEAQEKAFKDNIDVASVIVTKLYGHEKGGGALSAVAATKMALNHLKQPFISKFLGMGDIKGLIDKVNELKLDYNEIMKMGPFSQILGMIPGFGTDFMSKGNEQESMARLRKLMTIMDSMNDQELDSTDGAKVFSKQPGRIQRVARATPVAPDTHTHTQKTHTQYTKFAQMVKKMGGVEGLFKSGDMSKNINPSQMAKLNQQMAKTMDPRVLHHMGGMAGLQSMMGQFQPPSKKNAGNKTNLCTWHSLTLQRHSTQ
The following text describes a protein:
Function:
Glutathione S-transferase-like protein; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC. The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC. The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone. The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin. Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin. Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin. Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death. The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway.
Sequence:
MPDIQPITVYGKGGPNPPRVAIILAELDLPHKVIEVPLSKVKEPDYVAINPNGRIPAIYDPNTDLTLWESGAIVEYLVSHYDPDHRISFPAGSNLAALATQWLFFQASGQGPYYGQASWFKKFHHEKVPSAIERYVKEINRVTGVLEGHLSRQKVAADGDGPWLVGGKCSFADLAWIPWQVIVTAIIQPEDGYTVEDYPHVKNWLDRMMARPGVQKGMADIFPST
The following text describes a protein:
Function:
DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Regulator of UV-induced DNA damage response: required to protect genome stability during DNA replication, possibly via recruitment of vcp/p97 (cdc-48.1 or cdc-48.2) recruitment.
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to nuclear foci following UV treatment.
Sequence:
MSRSSLVDPSFELSDPCPDIHALFIQFDARFFGGSLACCEVKWSPRMYACAGICSYEIRGGRGGLCSIRLSKPLLTLRPRSDLVETLLHEMIHAYLFVKERNRDRDGHGPQFQAHMHRINQAGGTNITIYHSFHDEVRLYKQHWWRCSGPCRDRRPFFGYVKRSCNRAPGPNDRWWSQHQQSCGGNFLKVKEPEGYGQGKGSKRTNDKNKSGGPALKKTITPPRVTLDDFFKKDGKNSSDNSTSKSPTKPSTSLFTGSGQKLGGSSSTSSLLNSYPKATQNSGGNRLGGTSGGVSRLLPPVNFTSPSSAPVAEQVIDLGDSDDDDFQDMDDDALEISFVASDNSVICPSCNTEVMENLIHGHLDYCLG
The following text describes a protein:
Function:
Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. Sarcoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MEKVQHLTRSALRRASNIEMPPQARQNLQELFVNFCLILICLLLICIIVMLL
The following text describes a protein:
Function:
Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that binds both ligands with similar high affinity. Mediates calcineurin-dependent activation of NF-AT, as well as activation of NF-kappa-B and AP-1. Involved in the stimulation of B- and T-cell function and the regulation of humoral immunity.
Subcellular Localization:
Membrane; Single-pass type III membrane protein.
Sequence:
MSGLGRRGQGGRGLAGQEEPTPQGPRRGVAMEPCPEEQYWDSLLNTCVSCKPICSSQIPRTCAAFCKSLSCRQEQGRYYDLLLRDCVSCASICGRHPKQCTHYCEKTLRSQVSLLPEVRRQRAGEAPTRADTLGRHQVPEHRGLDAGPAPAGLKLSADQLALVYSTLGLCLCAIVCCFLLAVACFLKRRGVQVSFPTRPRPCPTQAKTSKDHWMEAGCVAGTPPEPVETCSFCFPECRAPTQESAGAPPTPGSERTGRRARQGQSTAGQPCVRAANGGIEVVYTPAQEGGLAT
The following text describes a protein:
Function:
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Sequence:
MADGGSERADGRIVKMEVDYSATVDQRLPECEKLAKEGRLQEVIETLLSLEKQTRTASDMVSTSRILVAVVKMCYEAKEWDLLNENIMLLSKRRSQLKQAVAKMVQQCCTYVEEITDLPVKLRLIDTLRMVTEGKVSFCWRDFLLQSVETYGSMEKKERVEFILEQMRLCLAVKDYIRTQIISKKINTKFFQEENTEKLKLKYYNLMIQLDQHEGSYLSICKHYRAIYDTPCIQAESDKWQQALKSVVLYVILAPFDNEQSDLVHRISSDKKLEEIPKYKDLLKLFTTMELMRWSTLVEDYGVELRKGSSETPATDVFSSTEEGEKRWKDLKNRVVEHNIRIMAKYYTRITMKRMAQLLDLSVDESEAFLSNLVVNKTIFAKVDRLAGVINFQRPKDPNNLLNDWSQKLNSLMSLVNKTTHLIAKEEMIHNLQ
The following text describes a protein:
Function:
Aquaglyceroporin that may modulate the water content and osmolytes during anhydrobiosis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MGNPPFPFFKKFVTTNQAVREFLAEFFGTFILYIFGGASFAHYLFTDNKDVFAVTFCWGIGVMLGIQTGAGVSGGHVNPIVTTSFASVGKLPWRKVPHYLLGQHLGAFLAAAILYFNYIDLLDKFDGGARQIFGTNGTGILLSTYPHPDVHLSVCVFDTV
The following text describes a protein:
Function:
Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MKTVAISRCVWHFAQSTALLCSQKLNIVKINSSQFLLINRSLSTIPQKKSSESTVHHVLKTAYSSDSWTNVSPSVLSKIEHRLHLQQNHPLAILKTKIEDYMLHSQPSIYKIIDSMVPVVSPKQNFDDLLIGPDHPGRLPTDTYYLNRDNILRTHTSAHQSTVLASKSSEGYLLTADVYRRDEVDQTHYPVFHQMEGIRTFDRRQFSSSQHTAAEAATAIGISENKIQSMHTPAEVMALSRHLKDTLENLIRCVFADEPNLQWRWNEDYFPFTSPSWELEVFYNGKWLELFGCGVVRQEIMNNSGNSDRVAWAFGLGLERIAMPLFNIPDIRLFWSTDPRFTSQFMSGKMSKFKPFSKYPSCYKDISFWIPSWFHENDFFEVVRDVAGDLAEEVKLVDEFKHPKTSRTSHCYRINYRSMDKTCTNAEIDITQEKLRIAVVQQCGVELR
The following text describes a protein:
Function:
Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Cell projection, microvillus. Secreted. Note=Colocalizes with actin in membrane protrusions at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli.
Domain:
The lectin-like LINK domain is responsible for hyaluronan binding.
Sequence:
MDTFWWRAAWGLCLVQLSLAQIDLNITCRYAGVFHVEKNGRYSISKTEAADLCKAFNSTLPTMAQMEAARNIGFETCRYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTICFNASAPPGEDCTSVTDLPNAFEGPITITIVNRDGTRYTKKGEYRTNPEDINPSVVSPSSPPDDEMSSGSPSERSTSGGYSIFHTHLPTVHPSRPRRPWSQRAENTSDTRDYGSSHDPSGRSYTTHASESAGHSSGSEEHGANTTSGPMRKPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINNGNGTMEERKPSGLNGEASKSQEMVHLVNKGSSETPDQFMTADETRNLQNVDMKIGV
The following text describes a protein:
Function:
Transcription factor that plays a key role in sex determination and differentiation by controlling gonad development and germ cell proliferation. Acts both as a transcription repressor and activator (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSEEEQTNGSLSIRKPSRMPKCSRCRNHGFVSPLKGHKRFCNWRDCQCQKCRLIAERQRVMAAQVALRRQQAQEEEMGICSPINLSGSDTLVKNEAVGENVFTLSSGPPSPASSSATASPTNLGSRSMLSLSPAMSSRGHTDCTSDLMVDASYYNLYQPTPYSSYYSNLYNYQQYQMPSGNGRLSSHNVSPQYRTHSYYSSYLSQGLGAACVQPSTCPEPKAAAFSDGAQDSVSISSMINAENKLECESSSESGSFSVDSIIEGATK
The following text describes a protein:
Function:
Involved in chlorophyll degradation. Specific for the pheophorbides of the dihydroporphyrin and tetrahydroporphyrin types. Chlorophyllide a, pheophytin a and the nonfluorescent chlorophyll catabolite (NCC) are not used as substrates.
Miscellaneous:
MISCELLANEOUS: An additional type 1 isoform with the same enzymatic activity seems to exist.
Subcellular Localization:
Cytoplasm.
Sequence:
MGGEGGADDSVVHFVFVHGASHGAWCWYKLTTLLVAAGFKATSVDLTGAGINLTDSNTVFDFDHYNRPLFSLLSDLPSHHKIVLVGHSIGGGSVTEALCKFTDKISMVVYLAADMVQPGSTSSTHDSIMTVGEEDIWEYIYGEGADKPPTGVLMKEEFRRHYYYSQSPLEDVSLASKLLRPAPVRALGGADKLSPNPEAEKVPRVYIKTAKDNLFDPLRQDRLVEKWPPSQLYILEESDHSAFFSVPTTLFAYLLRAVSFLQL
The following text describes a protein:
Function:
Has an organic peroxide-dependent peroxidase activity.
Sequence:
MAESPNDAATPASIVDALKAVAGNPPKVRASFAKGWCVRGTYTPSDRAEEITRSQSFTRPSRVLARFSVGGGNPNVADTNNLVLRGFSFKLGDDDHRSDILVESAPVHFARTLDQMLAFLKARIPGPDGKPDMAKVKAFSAANPETLNQANYIAARALPGSFAGTTYWGVHAFPATNEQGETRFIKFKVVPARGEITLSEDEARTKPADFLHDDLGTRIAAGNVRFNVMALLDRPGDPTMDVTIRWPDEDQRDEVRLGTIVITGFEPDQACDVTIFNPANLAEGIGHPPDEIFAARRAAYMISLAKRR
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MIRCSSALVMWTNVFKIGGLHQVSWFQYLPNESDPNISDRSAKLNQRDFAAQLVLSSHLQLQKDGFLSTWGNSFVGPWDPSQGLHNPDEKIKLWLFIPGRHSSPNDKAKAIVSKLRVLASGVWLAPGDSEEVAAALSQALRNCIERALVNLSYMRFGDVFSRYHPSSQGESFRRGRPMLEFIFTATEEAVFVHVIISAKHVRALSNGDMEAILKRTSSHSSDRLPVIASPHGMRGRLTGFCPGDLVKQLYFSSGKFKASNGIVGLPNQMSQTSGCQLRGQKCYLEVTLGCESVKNEKPLPSNSTKNFSKHHSTENEKGPTFWLQNWMGPSLSGSSFSMQCDALSSMDGSWHDASIRCQQGYNSSGNSNSSSISTSSSSDSDYRMTAETGDLEADADSLSCIKSGLTSADQMHIDASKMGSKRSRPGMTESYGQAGAVINDFGSMEVNNEQGGSQWDWDDDDRGMGMDIQALLSEFGDFGDFFENDALPFGEPPGTEESQTQTPMFSATDGGDASSSPFTGMMDASDQIIIPLGFSSFESFNPPSTVVEESISKNQELTKETVSSGSMNYNPPANNTEFDYVIKAEAMMTFAPEYSAVETPGNDLLLTVIKTPYVPKSRTTESANSSTNNYIYSSIPPKHDLSDDKSGANLNDKNYYTHVESGKLKDKKDVKDEKLSFRDSFGFGEDVANANASGFSSLSTASRSKILEGGLGMENFVLSSKTGVANELECVMFQAFMCRIRHTLLASNRLSGNNNNNNNNNNNNNNNNNNTILYQMHSESNVLGDNMSSKYDIKKKETIPVRIAGGDMDTGLLDGPLNSPVGVWRTVGVAKGSKAMSMTQNMESFGNIPHNSFTEEGMLLSYGQRQPLLELLDGMSLLFQQALTFVDVTLDSDCGDGPYGWLAMQEQWRRGFSCGPALVHAGCGGVLAASHSLDIAGVELADPLSADVPASYAITLLQSDIKLALKSAFGNFDGPLSVMDWCKGRNGQIDGFSAESSASINDCRDSSSTPTSPSQSAGGSTSCLSKDGNRIDDVSERRSNQDESEQQLGLRPALLVLPIPAILVGYQDDWLKTSASSLQHWEKAPFEPYAMQKHMNYCVVCPDIDPLTTAAADFFQQLDTVYETCKLGTHSPQNLGNQTSKDSVKWSTSGFVLLDCPQSMKIEGDSASLVGSISDYFLSLSNGWDLTSFLKSLSKVLKTLKLNSIFAPNSKEGNTTPCTVIYVVCPFPEPVSILKTVVESCVAIGSAMCPPSDKERRSALQNQVGKALSCTTAVDEASISNIVTISGFSVPKLVLQIITVDSIFRVTTPSLNEPVILKEIAFTVYNKARRISRGNGIADSIPSVRSQSQSHSGMMQMNSNSPIPGMWKDSIAPRMVGPREGEWDNNSWQMSNRVTGEYFLQDELKYMFEPLFILADSPERGIPPESLKVLSDDGTSSDTGDGLDDGYGSTHKPPPSLHCCYGWTEDWKWLVCIWTDSRGELLDSYTFPFGGISSRQDTKGLQFLFVQILQQGCQILQACSPETTTARPRDFVITRIGCFFELECQEWQKALYSIGGSEVKKWSLQLRRSVPDGIPASSNGGSEMGMIQDRNLAAHGKGGGFMKGGGMGQAASRKQILSGGGGGGHMGMDNSKGLLQWVQSITFVSVSVDHSLQLVYQADSSPGTTQGSGIMGQSVYTEGFTPVKSLGSTSASYIFIPSPTMRFLPPNPLQLPTCLTSESPPLAHLLHSKGSAIPISTGFVVSKAVPSMRKDSRTNSKEEWPSVLSVALFDYYGGNNNNNSNNNNNNNNNNNNNNNEKTSKNMGKSMENHVILDRVAAELHALSWMTVSPGYLERRTSLPFHCDMVLRLRRLLHFADKQLSQISVKSEV
The following text describes a protein:
Function:
Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MDTGMEASSHAMLYKASGLQDPDQEFKITRRKTISWFSPYSYSLESLTMYRMPPNIFARQSSEIDWCEGNYLHSEYVAEYYNTVSNVVFLLVGPLMMYLLHPYACTRSLAVHLVWLMFIAVGIFSMYYHMTLSYMGQLLDELSILWVIAVGYSIWFPRPCFPYFIKNRNHFGTVIFTLAAISTMLSFVKPAVNAYALNCITFHILYIIVKEMRKCSNHRILNLALVSFCLWVVAISCWLSDRLFCSFWRRINFCYLHSIWHVFICITVVYSNTLFAYFDAMYEIPESQPQVDYWPLKSLRIGLPYLSITKHDIQRKIC