lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
Subcellular Localization:
Nucleus.
Sequence:
MSLYSSRFSIASFDPECVKYYDNIGRVLLESTDDPDVFLTLDYNLELYPKLNKNARSLEVQILSSISYQDFNVSADSPNYDPKLSEILHDAYPDLDYAMHGTVFEFRAVGDKVDMFISFGGLIAKLQAPAFRLERFKFGMKLYLLCCNTM
The following text describes a protein:
Function:
Component of the gamma-tubulin ring complex (gTuRC) which mediates microtubule nucleation.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center.
Sequence:
MEAAASSLSTLLSTLRVDGPWTPPGTWESAIPESGAARVTDLGGRLQPIYELASVTDDALIHLALHALYGVKSSLDEIEELSVLFSSNPADRTSNRVTNVWLRSSSTISVGSILKSLRSTGLVVFFLCKFVHFYLVQSREMNCASREVHEHEHPGDKDTEQHRPYSLVNQAFAAAVSKVLEGVSSDITDEFTLFPLKGRNHVSAPCFLKEICHPVLRTGQQLRVLMNLLKSCKLSATGGDGYPSCNIINMEGVLPWFNTPIESSMNSFTFSKSSVEAVTCKRDAMYKLMMEKLQRFFSNVEVIPFDTASNILHKRTNLLDTSVSDAELFNGDSDAALPCNMSADEKDNDISFSSEDSSDKEDPLESSECSSYTSMDDTEVKSSTACEKISSSMFSLYCTSTGEAKCPLVTMKLLSSQSSSVYHGINWAVPIDECEKDDSLSCKHVPVHSQNAEHTAVLDGLELDYQYSQFSPFDRFMKRTSCSSEDMNSVEFLYTDHKRSVEKVSHGNAVNALHSESGPTKLSNGKNYEKFGNINQPWYTSIPYNLSLNPILKNAACYCTESDVQQKSKNQSLASFDFESVMDPCEVYCARSTSCLVEFVNGATIIQPSTHPCERLDCSPKLLQAQTRSQASLTSSGEMSTRDSLQKNVYGGAFWERSLLYNDKSKEKPAVDFSSQFDMPLDIVINKCIMEEVLLQYKYVSSFTMKLLEEGFDLCAHLLALRRYHFMEIADWADSFIALIYNKKWSFVKSEQKRSEIQGLMDFALQRSSCDSDPYKERLFIYIREPPVDSFDASACDLDLLDDILLGYKAEWPVNIVITEDTLKIYAEIFCYLLQVRFAVFSLTEVWRFLKELTQFISRSSHRGSDVLKKLNVVMKVRHKLHHFLSTLQQYLHCHLSDISWRRFQHSLKNQVRDILDLEYVHMCYITDALDICFLSDESKQVATIIKSMLQLALELRSCFQSIGDTCDLPVNQLSNLQYLINFSQVDVIRTKFEGNIKDLYVLHSKSSKYGELGLSRFWGYQNYNEYHSMKVSKDMGSFCF
The following text describes a protein:
Function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Sequence:
MNADAKELAASFDLEKLTPEFYDNPYPTYRALRENEPVKRLPNGTVFLTRYDDLVTTYKNTKSFSSDKKREFAPKYGNTPLYEHHTTSLVFNDPPAHTRVRRLIMGALSPRAIAGMEADLIKLVDGLLDAIAAKGSCELIEDFAASIPIEVIGNLLDVPHDERTPLRDWSLAILGALEPVVSPEAAARGNKAVKDFLSYLETLVARRRGKPGNPERDVLTRLIQGEGNGEENGERLTEKELLHNCIFLLNAGHETTTNLIGNGLVALDRHPDQKQRLIDHPDMIKTAVEEMLRYESSNQLGNRMTTERVELGGVMLDAGTSVTLCIGAANRDPAQFPDPESFDIARTPNRHLAFATGAHQCAGMALARLEVAIAISRFLARFPNYAVNGRPVRGGRVRFRGFLSVPCAIG
The following text describes a protein:
Function:
Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides. Involved in lifespan determination in a ubiquinone-independent manner.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MLAFRPQSAPLRLLTRSVSSKCKIEEIIRVDHAGELGADVIYAGQMAVLGSTSKGPIIKHMWDQEKGHRAKFEELIRKHRVRPTVMTPIWKVAGFALGAGTALLGDKAAMACTVAVETVIVDHYNDQLRELMEDPEANKELLETITRFRDEEQEHHDCGIDHGAEQAPFYKALTEAIKLGCKGAIAISKVI
The following text describes a protein:
Function:
Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.
Sequence:
MKPYESFVFPELPLDIREKLFQKDNAMVVVGVLGKSNEAHCNKLLEFNMLHSHPSLTDEAGIDCRVKFYFRTEGQTLFLHFDAPFDNFVLLHLAERMMVEKTDESPLHFIEFNSAIRTRFARVLLLALQVCHILVVVEPSISFDMSYLSIFKSLKIIREKYVLKFLPKMLKNANVGSFMGKECRLCSPRLLFMFNLPDNGEPHSLDEIDMLETKVEDYINKTLRNEFIITNNSAMSLFSLPKMKQFVFFNEAKPCNQDPLMDSIDMLSMYLAKQQQNSAGTLPESEEQQILEQAKPYDCFGFPSNFKFELKDPIEEDERSIFSLVQDHVEDALDTGFDESENPGRQRIRTHFVLPSTHAWYEMFKYMHQLFIENPNDPYYDAYDSDYKAYLQNFHDIVDIDERFFGEICEQGLDLATLKYKDMLPPHYSASFHETKYHEALNLLLEYARGPELKPSIQKLKEYCDAIWQSGKQQCEYPSLRGNPCVLGKHKSIDLAEHSSGVIYVSSCNCGRTQGHREDPYTIRQANYEFYQMIAKSCSNCNRLERVQFPVFEPSSSDFRAAEFINKNFSNLMSFDSTGRTASDFGPNVRAIPGHSPFLSGSQRSQNSSASLSFNIASDGEEDEEEGNIGKKGEGRSNRREQDPAEERNDTDQCDQMDDGRLNDDDDDDEDDDQLASNNEEMNEIVIKLGALKHGSDASPGEIGHPAAPARLPSTTEYLPGMLHIASPAGLLPRFPSWSLVCLGSSSIYTHNTGLPEHVQSGFLSGSNFLLPWDVSVRLEHAQCWAASYEKIRNRKKGNPHSSKSFEHNKTFTLKIFIGVEYECLRGHRFIMNAPDSILRCGSEIVRNSGSKVVFNDMPIYFPCPCRNTINNTAQLMRVHIITPKAPVNVIIDPKVKLFQNNMQNSITFTTGMTEPIKLTQSSYWILRLPFVYEGDSGPLMAPTDVNPASAIMHGVLLAGMYGIRENELNEETIGISNPSG
The following text describes a protein:
Function:
Bifunctional growth regulator. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage by bone during endochondral bone development. Plays a role as antiangiogenic factor in cardiac valves to suppress neovascularization (By similarity).
Subcellular Localization:
[Chondromodulin-1]: Secreted, extracellular space, extracellular matrix. Note=Accumulated in the inter-territorial matrix of cartilage; [Chondrosurfactant protein]: Endomembrane system; Single-pass membrane protein.
Sequence:
MEETAEKTPVEAYSTLKPKGLMKMKKTALVAFIAGAALLLFGGVGAFYLWKVTEKEAISAHLGRNIDIKIENDSDSAEGTIVEVQDFKAGITAVKFPGKEKCFIKSQARTELSEDEAGVKAEVASLVWITSEEPLKDSSFLSPEILRFCADLPIYWHHPANSRALRKRRSATRMRRQTSAGVNRQPARRRNSTASARDERPTGPEYNPENPYHQNQGSEGTMVFDPMLDHRGICCTECHRSYTHCERVCEPLGGYWPWPYNYHGCRPVCRLIMPCRWWAARVLGLV
The following text describes a protein:
Function:
Skin-specific kinase that plays a key role in glycerol metabolism, catalyzing its phosphorylation to produce sn-glycerol 3-phosphate. Involved in skin-specific regulation of sterol regulatory element-binding protein (SREBP) processing and lipid biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MIYPSQDSSSFVPLLGECSKKSPEKRHHSTHPTHIIAVDIGTTTIRSCLFRVNGCERIGEFPDNVEVDYDESDGKAEIDPDNLWGKFVSVVKRAQAAAPKGSTIALSFCTQRNSFLTYDKSNLEPTTKIILWNDKRAKAECENKNRSPLLKGLNTVAAILHYFLRLPRLRAAMVLRFIGSMVSFRVVKAINDNPVNKTLLSSGRLAYACLDTWIMLKLTGGRHLATEPSNVSATGLYDPFITDYNMAVLRWMVHFPRQLLVPITESAVTGSPHCMTDPSIFGESLPLHAVLADQQSALFGCGGLRRGDTTISMGTGIFIQKNLEDKPHASMKGLYPLVAWKVDGRTTFLAEGQQHQSAACIEWAKEQGYFSDVAQTSSIASSVSDSNGVTYVPAIGGLQTPYDDDRAIEKMFETRPETTTNAHRLRAVLEGLSFRVHEIFGTMEREIVSKEKSAVRICGGISANDFVCQTIATLINRPVERITDSTYAAARGVALMAGISLGAWKMEDVSSMVSIEKTFMPKSDERCRLMETFSQWQKHVQKCLGKRE
The following text describes a protein:
Function:
Involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Activates the wis1 MAP kinase kinase by phosphorylation.
Sequence:
MENILDPSVVNSHILENGSRRSSINPILDSELRDKTFEKAHRRSLTLLSSFTSSMLELPNNGKEENHRRPSVARSSSDRSKASAKEDLFSEAFRMAEQPPAEALTISTPVDPINIDELDRAYAVSPSDTSNLLHPPTSSSSIPIPIKNAGHSNLDHPIRPSLQSSISSNRIIKSPGIKEDDYMHRGRSISSPMIDVEHINSTAVPSKTKNLPEKPKRSHKLRNSITFAKIEDHPERKSQLRRLSSSLKCFDPEYDYNDPSLSIRRDSSTYYFSNVNETYDEEDSDLDSETSTVNWVQSVLNLPSLLSDDLMANPKNKERFEWQYMLTSVLTGDIVRSEKLRLRKIASSREGRNSDYSDNLWMEIWCWLTHRSVDSYRENLKHLRTGMVDVLLAIMNFHWDESNELTPIVAVDNMLQKLDKYERLYPSRRSILQEHSLYASESFQHKLDVLTAYSNVTHALEIQVNIIRSWVGNEEMDITKNTTNSINNVSQISNGPFVERFYRETGLIRAFEQRIMTNMNSVLSKVCNTIVTYADDLKSYGLPLIADDYMRLLSFPFRLIKEFLNLRLSCAENITSISLFTIDSLLDDLRNTMKVAVHIIQQHTVLIKPFRDDSKFVDENQSLNNILVASLKFYFNLLHRKVRNGCALLHFKETEILEGEWDFLLAVCPHIEHGFQIMSKSLSSLVGEILTNINRYLKDQLQGPDTDDSALITSFYIKVLDCVRIRFRKLMSFTRILKAHLENSCEYVIKENSLSLLIQRLEESNHVLTYTASIEHEGAYVIVPGHLVDSPNILREVLSMTFNKGDNNFESVPPYAVVLAPDSSICWNGHVTDLDIPEVSISIAPNCVRLVTLATANQLSVIEDYFISIVGDTVSLVDSAKANSSKINKQMTKIKRNSLKLALSLLDVIQTIRTRYHGMNCQNLIHYSFSYAIEFAQRLMRLSILDASSIGLIRRKMIQLAISWVGFIYEDCSPTDRNTFRWTVTALEFAMIMTYGSNILMIDKKSFEELKEKVGKCVALLLLHFDVMGTKHAGRSMDQQAGDIPARLVRNNSDRSRLSDNELASFVKEEVMHRIIELESNRRDRLYKSQLIGRVLDDTTKENRLLKELASSKSNITIRWQQGGLIGSGSFGTVYRAVNLDTGDLMAVKEVALHKPRISRPMIKRIKGEMLVLELFDHPNVVSYYGIEVHREKVNIFMELCQGSSLFEFLRYGRIEDELVIQVYVLQLLEGLAYIHSCGVSHQDVKPENILFDHNGIMKFTDFGSAKMSGSASTKIFEQLTQQEEEEFEKDSEFLQHLDQNRGYSLTGTPTYMAPELILGNPSERVGAMDIWSLGCVIVEMATGSPPWPRLDNHFSLMYHIAAHNPPIIPADDQLSPLGQNFLKRCFVSDPNQRATAAELLMDPWVYPLRAGTEFDLMNSSVVESAPSTNGAPLEL
The following text describes a protein:
Function:
Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). May be able to store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization.
Subcellular Localization:
Mitochondrion.
Sequence:
MLSTILRNNFVRRSFSSRIFSQNEYETAADSTLERLSDYFDQIADSFPVSEQFDVSHAMGVLTVNVSKSVGTYVINKQSPNKQIWLSSPMSGPKRYDLEEEGKWTYAHDGEQLDSLLNREFRKILADDRIDFSRHV
The following text describes a protein:
Function:
Acts as an E3 ligase mediating SUMO/Smt3 attachment to other proteins. Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis.
Subcellular Localization:
Nucleus.
Sequence:
MSEAQLKTSLEALSQNLLPGNQNHCSFDFQLKEIDDSIKQVIKCALVAAEIKNNECLDMLDSGIRELLDAKQRLLLMQQSVDTLANKTSENISDFENKSLLDIYTQIFKELIQEYEEKSDYGKYGTQGEYIEFKKTIWHEQNTDGSDFPSMKTFFNVMNTEEQEADEVMVYSATFDNRCPLTLQPIVHPILSTACNHFYEKDAILSLLNPTCVCPVVGCEARLQRSLLKEDEILERRLRRAQEISNLKEA
The following text describes a protein:
Function:
Catalyzes the production of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent manner. Glutathione (gamma-glutamylcysteinylglycine, GSH) is the most abundant intracellular thiol in living aerobic cells and is required for numerous processes including the protection of cells against oxidative damage, amino acid transport, the detoxification of foreign compounds, the maintenance of protein sulfhydryl groups in a reduced state and acts as a cofactor for a number of enzymes. Participates in ophthalmate biosynthesis in hepatocytes.
Sequence:
MTTLWKDILRNVQLIQYVAPIAVDAALLEGVLMRTKDDPNASDAVNYAPFTLLPSAVPSDLLEQAYSVQQNFNLLVDRVSQDTEFLERTLASTVKVDEFTAQLFNIYKQVLKEGVTQTVFLGINRSDYMFDYGTGGSPALKQIEINTIAASFGGLTSRTTAVHRLVLNVLGKSKEASKLLTNNPSKGIAMGIAKAWELYGSDRAVVMFLVEEVQRNIFDQRCIENELWRRNIRVIRRRFKDVFEKASLDNDKRLYIDGDEVAVVYYREGYVPKNYNKQNWEARLLLERSRAVKCPDIATQLAGTKKVQQELSRPGSLERFLPNKPEAVDQLRATFTGLYSLEMDEEGDKMVAMAIADPDRFVLKPQREGGGNNLYSDELKQVLEKIKDSPERTSYILMDKIKPLPAMNYLLRAHSELKISECVSELGIFGVYVRQGQDLVVNKHVGHLLRTKAVEHADGGVAAGVAVLDTPYVT
The following text describes a protein:
Function:
Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline.
Miscellaneous:
MISCELLANEOUS: Present with 10400 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MKDANESKSYTIVIKLGSSSLVDEKTKEPKLAIMSLIVETVVKLRRMGHKVIIVSSGGIAVGLRTMRMNKRPKHLAEVQAIAAIGQGRLIGRWDLLFSQFDQRIAQILLTRNDILDWTQYKNAQNTINELLNMGVIPIVNENDTLSVREIKFGDNDTLSAITSALIHADYLFLLTDVDCLYTDNPRTNPDAMPILVVPDLSKGLPGVNTAGGSGSDVGTGGMETKLVAADLATNAGVHTLIMKSDTPANIGRIVEYMQTLELDDENKVKQAYNGDLTDLQKREFEKLKALNVPLHTKFIANDNKHHLKNREFWILHGLVSKGAVVIDQGAYAALTRKNKAGLLPAGVIDVQGTFHELECVDIKVGKKLPDGTLDPDFPLQTVGKARCNYTSSELTKIKGLHSDQIEEELGYNDSEYVAHRENLAFPPR
The following text describes a protein:
Function:
Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates. Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity. May also hydrolyze long chain retinyl esters such as retinyl palmitate. May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border.
Subcellular Localization:
Apical cell membrane; Single-pass type I membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MDPSSMFGRASPSSKIARFALLGPFSYLLTFSGFDLNNSICGSRRPRSRALFSTLVYSLAVILFTARTILVGSRDAPEAQVIQTRKMLILGGCLGAVFIGITVVASVKRSVYRNSYENSTEPLIHHHFLSRYNIWGVEIVIGIWMALCTVLAIASYIFMHIAAKEECTKFKEDLDEAAKAEKLVSRLDQFSHRHIAILKLVSLITERTNTFVSFSTICVFIAHINVFYVISAVGAPNAFGTASCVLWGISTIALLPFILSPPGTIQIMLEKSMATLANHEQLIGHPEKLAMAQLMEDRNRETPTRMAIMKAIKVNAQTPHLGRLEWTPQMQASLLTATFYGSLATISFTGSIADRFGPKYIFSAACCVYVIVTMATPFLAELSFRAYFAARLIMGLAEGFIVPCIGSMAGRWFPPLERSTMAGIYTSGNQLGASSSSVISAALCGSPLGWPSIFYLFGAIGIIWIIAFMTLSSNSPSSNRFITEGEAKFLMAEITRKKAFLPTYFRDELMIPLSMNGLYTTIPFVVQIFMKTFCSIVADALKRKVSVFKDKNENDSWMNTQGILAPTTAAKVFQTMCALGIATSLISLAFLPSCDRPWIAALCLASYGISYSFGIPGYFTALMSIAPQYTGTLTSMTMLAATFANISSPMLTSLMMTLKTEHMWKVVFTITGLLNLTGGIIFLIFGDADIQEWARVEKKSSSVVEEKKKHKIDDEKMERIQVEFSCENYLIVLQVGTTDLATVVQAFYFSVRITRPTRLLLILVQTFSSVNVFEMYHLSVLFSSILVLVNSALFKDYGIPGWACEPQVMKRSAQVPSSVHSLRFADIDIIGALGDSLTAGNGAGALNQNVQAVLQTENRGLVFSVGGDSDLNQHVSLANILKKFNPKLYGFSLGSGPVYDFGSAQFNAAVPGAKAINLTSQAIDLVDIAKSWKLVHIFIGGNDACDWCANPQDETADLFERRIIDAIKILKENLPRTIVVITGMMDITILRDLGDKNEMCSVMHDKLCPCVQNKNFTTEQLRGLCKDYIIQNSGLFDGSDDFTVVVLPFLEDNNRAPLLVNGSVDLSLFAPDCFHFSAYGHAVVGKNLWNNLLQTIPHKPRTVDLTTVASPLYCPNPECPFIRTTKNSFNCGKYWTSITLSPLMKVPPRVDYGDEREKDQPAPPSLVKITWANSQGGKVEFISTARDLAPYHDNYSSTVLIAHSSVTNMRFADVCSISHRRNEMMAIVAMVDVRNFREFWNTVDFDPTVFNETVRVDIDGGYTGTLLWIPPMQAIIFSGTFYGSLLTVFFTGKAIERLGAKAILAASIFVSMAATVATPILAESSFVALFVARMFMGAAESFVMPSIGVMASRWISPSERFAMMEMISSGNQLAASFSAVVTAALCLSPMGWQSVYYFYGLIASLWLVAWILLAANSPDKCRIVSESEAEFLSKTIPVKPSSSERIPWRSILTSRPFITCLFCQFAFVYSGTIMQGFLPTFLRAQLRIPLKMNGLFTLIPFGTMLIMKTLFSLLTRRFNSTKLSTPTGRAKLFQSLSSIGCILAMISMVFFANPNQLWIAIISLAVFGVSLAAAIPGFALSTQSLSPQHSLAINQISAVTGVVAAICAPMIMWLIMTLKVNGVVESIWKTAFSVACALNLIAGVMFILFGDGFSVSLCPKKYDLVRNGECYRQKEKGLEVDAGNGPSNAVYECGNDNAMPVIIRNQEDQDYWWSVAKKDKEKYGDLILGIVCDKRHELHWADGSDIDFRPEKYDADLDEPCHDNGYHFCMFNIDAKTGAWKAQCNIDVTINIYCTIVPPSPSLQPDDDCAEFEHDDDDNVCYQVGASPANWTEANSWCKSFGSSVASIHNDQENSFIRRLAASKGLLNGIMLGGIATNNNNKWIDGSVWDYNNFAPATDRDPTCDGTVRKEGEIIYSPGFPFNSSAACDFILMADSGKLVEVEILLLEANSCCDHLILTEGTLGGAVLADLTGDKNDGMKIRTKTQNSMRVSWQPNGATNVRGMMLMAASSYTSREEGTT
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion.
Sequence:
MPGNFINPYGHVPVDTTAFEEAAGVKEKIDPELAGILKDIKRGDLGVPSHVLKASAFQYANECNEVNKEFMLCREEEMDPRKCLKYNIKVSDCAENFFRKMTTACADEIVAFGKCLERDHKRSFVYCRDEQVKFDRCMFEKLGIDKKYNAVELDQTVKTDRPAPKNPFKLKNYDHPSPLMPDWNRPLPKIED
The following text describes a protein:
Function:
Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA thiolase activity.
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane. Mitochondrion outer membrane. Endoplasmic reticulum. Note=Protein stability and association with membranes require HADHA.
Sequence:
MTTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
The following text describes a protein:
Function:
Irreversibly catalyzes the reduction of fumarate to succinate. Together with the second isozyme of soluble fumarate reductase (OSM1), essential for anaerobic growth. Involved in maintaining redox balance. Reduction of fumarate is the main source of succinate during fermentation, and under anaerobic conditions, the formation of succinate is strictly required for the reoxidation of FADH(2).
Miscellaneous:
MISCELLANEOUS: Present with 7620 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSLSPVVVIGTGLAGLAAANELVNKYNIPVTILEKASSIGGNSIKASSGINGACTETQRHFHIEDSPRLFEDDTIKSAKGKGVQELMAKLANDSPLAIEWLKNEFDLKLDLLAQLGGHSVARTHRSSGKLPPGFEIVSALSNNLKKLAETKPELVKINLDSKVVDIHEKDGSISAVVYEDKNGEKHMVSANDVVFCSGGFGFSKEMLKEYAPELVNLPTTNGQQTTGDGQRLLQKLGADLIDMDQIQVHPTGFIDPNDRSSSWKFLAAESLRGLGGILLNPITGRRFVNELTTRDVVTAAIQKVCPQEDNRALLVMGEKMYTDLKNNLDFYMFKKLVQKLTLSQVVSEYNLPITVAQLCEELQTYSSFTTKADPLGRTVILNEFGSDVTPETVVFIGEVTPVVHFTMGGARINVKAQVIGKNDERLLKGLYAAGEVSGGVHGANRLGGSSLLECVVFGRTAAESIANDRK
The following text describes a protein:
Function:
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis and membrane trafficking in synapses. In response to high synaptic activity at neuromuscular junctions, stabilizes Pldn protein levels and, together with Pldn, plays a role in promoting efficient synaptic vesicle recycling and re-formation through early endosomes.
Sequence:
MLTSMVKEHHKEQAKRKQEQEVRRKEAIEASNELTQSLVDTLNVGVAQAYLNQKRLDAEAKQLHLGATNFAKQTHQWLQLIDQFSTALKDLGDVENWARSIEGDMHTINQTLELAYKASRATQTSSGAGTSLEASTSASASANPSAT
The following text describes a protein:
Function:
Catalyzes the formation of pyruvate in the last step of glycolysis, it is irreversible under physiological conditions. The reaction is critical for the control of metabolic flux in the second part of glycolysis.
Sequence:
MSRRLRRTKIVTTLGPATDRDNNLEKVIAAGANVVRMNFSHGSPEDHKMRADKVREIAAKLGRHVAILGDLQGPKIRVSTFKEGKVFLNIGDKFLLDANLGKGEGDKEKVGIDYKGLPADVVPGDILLLDDGRVQLKVLEVQGMKVFTEVTVGGPLSNNKGINKLGGGLSAEALTEKDKADIQTAALIGVDYLAVSFPRCGEDLNYARRLARDAGCDAKIVAKVERAEAVCDQNAMDDIILASDVVMVARGDLGVEIGDPELVGIQKALIRRARQLNRAVITATQMMESMITNPMPTRAEVMDVANAVLDGTDAVMLSAETAAGQYPSETVAAMARVCLGAEKIPSINVSKHRLDVQFDNVEEAIAMSAMYAANHLKGVTAIITMTESGRTALMTSRISSGLPIFAMSRHERTLNLTALYRGVTPVHFDSAADGVVAAHEAVNLLRDKGYLVSGDLVIVTQGDVMSTVGSTNTTRILTVE
The following text describes a protein:
Function:
Involved in the regulation of neurogenesis. Negatively regulates neurite outgrowth. Involved in the morphogenesis of basket cells in the somatosensory cortex during embryogenesis. Involved in the positive regulation of oligodendrocyte differentiation during postnatal growth. Involved in dendritic arborization, morphogenesis of spine density dendrite, and establishment of postsynaptic dendrite density in cortical pyramidal neurons (By similarity). Involved in homologous recombination (HR) repair pathway. Required for proper resolution of DNA double-strand breaks (DSBs) by HR. Is required for recovery of stalled replication forks, and directly contributes to genomic stability. Interacts with PARP1 and mediates MRE11-dependent DNA end resection during replication fork recovery. Contributes to genomic stability by preventing telomere dysfunction.
Miscellaneous:
MISCELLANEOUS: Cells silencing ZNF365 display delayed mitotic progression and exit, due to increased replication stress, and ultimately leading to cytokinesis failure, re-duplication of centrosomes and increased aneuploidy.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=localizes to the centrosome at all stages of the cell cycle.
Sequence:
MQQKAFEESRYPWQESFENVAVCLPLRCPRCGDHTRFRSLSSLRAHLEFSHSYEERTLLTKCSLFPSLKDTDLVTSSELLKPGKLQSSGNVVKQKPSYVNLYSISHEHSKDRKPFEVVAERPVSYVQTYTAMDLHADSLDGTRSGPGLPTSDTKASFEAHVREKFNRMVEAVDRTIEKRIDKLTKELAQKTAELLEVRAAFVQLTQKKQEVQRRERALNRQVDVAVEMIAVLRQRLTESEEELLRKEEEVVTFNHFLEAAAEKEVQGKARLQDFIENLLQRVELAEKQLEYYQSQQASGFVRDLSGHVLTDISSNRKPKCLSRGHPHSVCNHPDLKAHFHPKGRNHLKKAKDDRASMQPAKAIHEQAESSRDLCRPPKKGELLGFGRKGNIRPKMAKKKPTAIVNII
The following text describes a protein:
Function:
ATP-dependent RNA helicase required for ribosome biogenesis. Involved in the release of U14 snoRNA in pre-ribosomal complexes. Required for pre-rRNA cleavage at site A2; RNA helicase.
Subcellular Localization:
Nucleus, nucleolus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MRAARDDAEDMRRAKAQAKQQRWQERQERSKDSREEIDKLQLRCADMHRELKDIAESNEANTSTEHEYSKFTELPISQRTQMGLERGHYTILTPVQKGTLHLALAGLDVLGAAKTGSGKTLCFVIPVLERLYRERWSSDMGVGALLLSPTRELALQIFKVMQLVGYKHVLSAALLTGGRDVQEERKRLHAISIIVGTPGRVLHHLQDDAELVLDNLQLFCMDEADRLLDMGFREAITSILAYLPPQRQSLLFSATQTTDVQMLAQMSLKNPRYVSTQAITAAPTPMTLCQNFVVVELHKKLDALLMFLKRHPNDKIVVFVSTCNQVKFMHLAFSKILKKMRIPSMCLTSKMKQFRREEVFLTFCRCKSAVLFCTDVASRGLDFPLVHWVVQYDCPESAQTYIHRAGRTARAGARGVSLLFLTPRETPMLSYLHHKHVPLREIAIKPDFLTSSQEIFVALVVQGLKYEAQKAFIAYLRSVYFASNKNVFEVAAVDVEAFAKSLGLPVVPDMSELQNLQRSAKNLPWDVVNFIAQRGGSGADKAGSTLTRKEKHLQATDMYRVMEQKQRFANKKGALHGDGASRGDSSSGDAGSDDDDFLVKKEPAGASGCGASVSAKAGTVIADSNPLHLTVEERLAGLSKNKRRKLIENADIRVRDLRLNQRIIFHDDDDESDEEADAMGNGGRSGAKGNAAHSSRSDDDADEENDTTVAGLLKHAVLRHREQGCRDVDSDNDDADDADFTATLQTRVQANKADDLERAKKMRRLRRLQRQGRVSRKSTVDESGIKTASGGPRPANSDDNADDGSGDYYDEHVDGSDAESTGSISRLLKAARGELYSDDDTDEDGEEEESLCGSSSAARKRTRGNCTYHGIDSSDDNGSEGDADEVASPPPPLKRSRQRR
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.
Sequence:
MLASFQLLAANPQVEFETNRGNFVVELYPDKAPRTVENFLRYVQSGFYSGTIFHRTIQKFVIQGGGLTEKLEQKHTFDPIPNESTNGLSNDYGTLAMARGYGPNTATSQFYINLEDNKFLNFYRQEAGLEGYTVFGKVVRGIDIVKRISESQTTKIGKLEHVPNDPVVISGAHQLDNPVMAESYGAPQPETINKPIQIAKKGKKRG
The following text describes a protein:
Function:
Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).
Sequence:
MSNEEARSAGDLRNTGLSLRHDRTWDYELDRIVDEVERKDAEKVGLQFPEGLKRRGPAVADDLRARLDDTRIMLSGQPCYGACDLDTYLMRRTDVFVHFGHSPMKESDSIIYVPLFSNVDVEPIMQEARDELHDGDVGLVTTAQHMNQFEEMRTWLEERGYTVHTRRGDDRLTNEGQVLGCNYASADIDADQVLYVGGGKFHPLGLAMEHPEKNVVIADPVNNAVSIADAEQFLKERYASVHKAMDAEQWGVIFCTKIGQGRFDQAEEIVENNDNAYLITMDEVTPDRLMNFDMDAFVNTGCPRITTDDGPQFHKPMLTPGEYEIAVGNKPLEDLSFDTFHGTW