lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Sequence:
MNDVFSEISRCIKMDIPKFIELIDEYILPENIKSPIDHKSYYQTAAPYPSCTYVWEDDSLVAICRECSVSPMSVICLDCFEHSDHHNHLTFLVRSEYGFCDCGKASNMKVQAFCTHHHDPKIPTSQIPENEKEKFRQVIDLIVSNIPFYCSCDTNSAVSLLKWINGWIRASYLHMKVVADVFIEKFNLTNFLLRSGKMDLRIIDEFVTTLIFLHSCEDFNLYLLKQCISLFPNCVSILLELASVISHSPDLLTTTPPFPQFHKVTQTFLFCIKNDLLQKVIHTMDWINPFLDSIKLIFDRGLNDYDKNNSCARIAISMLFSLTELMQHIIKNLNQEELIQFIRKYVDAVLPLEGQFVFDSSIGDFVPGTGRIAYVQITELEFTSFNIINLRKCVVPDIIEIFITKFLNNLSSNNYETIEDKIVYHRFFDDEHVKTSLSLGLHSFALDQLLLQNDLKKSFETLSKTHNYSYDDLAIYWALLPLRFIGLSQLNSFKLVTMDQILSRYIDINQNWANIHLRFKQCFIIVQTMLGLARDKDAFLKMICYTCGLDADYCTDYEIGIMEFNVLMIICGLIFDRYLVKNDERMIRKLSFISRMTSGPQSINELLTGMQTPDFFQKEIIEDVLEVARQIAGTDKFVVRNASEWNVVAPWVPNNLIHGAVLSKLSSGTRFFPFPEWEDPIRPEIDLKPCLNSRVLFALIFQIISNTVHFSGYTDPVTANVCSGLLVRMGELFPDPPKEMPKVCSPPKAKTLEDLIKVLPNNLYAFVRFQVAYRGSEATCVLQMLECLGKVSERIFHVLDPDRVKTPCSPRQETEQKVLIASAKKQAIDFIRNTPLPFDSHKVKNANYSKCNICGKKDNLWLPVYAYKNGLPKFIGLDVDTVLSLFACPHCVHISCVPKNTCYLCKNDNFKANCFVPMNPTPENAQIFLSALFPNEPAEKWPALGINTLTYEVHAIEMRHRMNPFALDNANQRILLEKTFLCIQSFDDIDSNCLVHDPVASLFMLLMDDYDFSVFLDIIRTLSIDLSPKDLYVFLRCCRIIARFLYNKAARDWDDEMSAEKLKIFFGIDNVKEIVLEKFKFKDLDQNLMYMILKSGVKETDLFGSTYYDLLTGDIILGSHDHLEPIKQLRQHVKDKWNSSFSILVPLQGGKHAIIIDGNETIYYLMPLYYNPYRTEMGILECPYVLSRDVNDYLIDCILSGYWLVLSK
The following text describes a protein:
Function:
Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Miscellaneous:
MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MNNQPQGTNSVPNSIGNIFSNIGTPSFNMAQIPQQLYQSLTPQQLQMIQQRHQQLLRSRLQQQQQQQQQTSPPPQTHQSPPPPPQQSQPIANQSATSTPPPPPAPHNLHPQIGQVPLAPAPINLPPQIAQLPLATQQQVLNKLRQQAIAKNNPQVVNAITVAQQQVQRQIEQQKGQQTAQTQLEQQRQLLVQQQQQQQLRNQIQRQQQQQFRHHVQIQQQQQKQQQQQQQHQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQGQIPQSQQVPQVRSMSGQPPTNVQPTIGQLPQLPKLNLPKYQTIQYDPPETKLPYPTYWSDKKADTDTLLYEQIIQRDKINKYSLIRETNGYDPFSIYGFSNKEYISRLWHTLKYYQDLKNTRMKSITSTSQKIPSASIWGNGYSGYGNGITNTTTRVIPQVEVGNRKHYLEDKLKVYKQAMNETSEQLVPIRLEFDQDRDRFFLRDTLLWNKNDKLIKIEDFVDDMLRDYRFEDATREQHIDTICQSIQEQIQEFQGNPYIELNQDRLGGDDLRIRIKLDIVVGQNQLIDQFEWDISNSDNCPEEFAESMCQELELPGEFVTAIAHSIREQVHMYHKSLALLGYNFDGSAIEDDDIRSRMLPTITLDDVYRPAAESKIFTPNLLQISAAELERLDKDKDRDTRRKRRQGRSNRRGMLALSGTSASNTSMNGVHNTVAAGNASSLPPGEILLPDIADIPRTFRTPVPSTLMPGGVDVGPSVESYELRNTTTYKSRPDRPKPVSPPCYIIDHIPGHSLLLSIKLPGKVNTKEEFAAAPNDTSSGTNAMLPSPESLKTKLNSNIRAGVTIPSIPNPIANHTVTNSPNPTLQPVIPGGAASKSVPTPSLPIAPPVAPHDSEATLLTNSNNGSSNNNTQNT
The following text describes a protein:
Function:
Voltage-gated chloride channel. Chloride channels may have several functions including the regulation of cell volume, membrane potential stabilization and signal transduction (By similarity).
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSTSKYSKMISSKHGYKKTRIKNNTSDSDLFNLVMPKADVVGFKSKQGGISRQAISWAKFARLNNFYIWLFLAAVGLLGSIYLVAVDLIFKYVVFSWREAFMSLTENYFLQYLSFIAWTVALATGSCFIIKKICPAAVGSGIPDLKSIFSGFWNPFVVAPMVLLWKTIGLLLSYGSGLSIGKEGPYIHISATLANTLLSIKPFKSIAQNDTQRSQLLAACCALGVAATFGSPIGGVLFSIEATGTFYLISNYWRAFFTATVGAVGIKILLSNPSNDLLESFRTHFADLNLASAQLIAFIILGVLCGLLASLFISLYTKIYNWKKHNAELFKKITPFGEVIIVAAATAILSFPLKFLRLDHATAVHTMFTATPDSDNSEVLSELAVWTDSMPFNHGIILACFLYVVVKLVLTAVSITLPIPYGIYIPLFAIGSAVGRFVGELMLVLFPNSKEIYPTGYAVVGAAALCGGATRTVSSAMIILELTNDLTYMVPVLLGVVLSCGIGNLLNHSIYDCFLKNKNLPYLPFYKAKSDSLIARDVMKRDLYYVCQNTTLSQISNLLKRVDEHSIPVVSSDNDLQLIGTISTTTLEEVIAYHERLHSYSKSPLSLSDNGIDINDNDNNDNINNNQNNNNNNNNNNNNNNSNNQNNSLVSEAIEMNVLSDSDNDENNNLIPNIPINDNNIIIQNNIRNNNNNNFSDNNNNYNNNNYNNNNNNNNDNNTNNDNNINNNSNDINESISEETTIDLVQMELQNPWVVIDSSPFQIQETMPVRKIVFMFMMLGGNILYVTNKGKLTGVVAKTELVHQNNNKH
The following text describes a protein:
Function:
Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90. Dephosphorylation positively regulates the Hsp90 chaperone machinery.
Subcellular Localization:
Nucleus.
Domain:
The TPR repeats mediate protein-protein interactions with substrate proteins, but also autoinhibit PPT phosphatase activity.
Sequence:
MASSDLEAATALKVQGNKAFGQHEWPTAVDFYTQAIAKYDREPSFFSNRAQAHIKLEAYGFAIADATKALELDPAYTKAYWRRALANTAILNYKDALRDFKVVAKREPNNRDAKVKLADCEKLVRRMEFEKAIEVGDPPSAFEDLDIDAIAVDDSYDGVRLEKEMTQEFIDDMIERFKNGKKIHRKYAFQIVKAVKDIVYAEPTMVEIGVDQGTKLTVCGDTHGQFFDLLEIFRLNGYPSEKHAYLFNGDFVDRGSWSTEIALLLYAYKWLRPNGIFLNRGNHETDDMNKVYGFEGECKAKYNERMFKVFSESFSALPLATLIGNKYLVLHGGLFSDDNTSLDDIRKLDRHNQRQPGQQGLMMEMLWTDPQTEPGRGPSKRGVGLQFGPDVTKRFCEKNGLEAIIRSHEVRMEGYEVEHDGRCITVFSAPKYCDTTENKGAFINVGPELKLDFQVFEAVPHPDIKPMAYAQNSIMSMM
The following text describes a protein:
Function:
Plasma membrane reductase that uses cytoplasmic ascorbate as an electron donor to reduce extracellular Fe(3+) into Fe(2+). Probably functions in dietary iron absorption at the brush border of duodenal enterocytes by producing Fe(2+), the divalent form of iron that can be transported into enterocytes. It is also able to reduce extracellular monodehydro-L-ascorbate and may be involved in extracellular ascorbate regeneration by erythrocytes in blood. May also act as a ferrireductase in airway epithelial cells (By similarity). May also function as a cupric transmembrane reductase (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Note=Localized at the brush border of duodenal cells.
Sequence:
MAMEGYWRFLALLGSALLVGFLSVIFTLVWVLHYREGLGWDGSALEFNWHPVLMVTGFVFIQGIAIIVYRLSWTWKCSKLLMKSIHAGLNAVAAILAVISVVAVFENHNVNNIANMYSLHSWVGLIAVICYLLQLLAGFSVFLLPWAPLSLRAFLMPIHVYSGIVIFGTVIATALMGVTEKLIFSLRDPAYSTFPPEGVFFVNTLGLLILVFGALIFWIVTRPQWKRPKEPDSTILHPSGGTEQGARGSMPAYSGNNMDKSDSELNNEVAARKRNLALDEAGQRSTM
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC).
Subcellular Localization:
Nucleus, nuclear pore complex.
Sequence:
MTFSGRGTLISSTNSFNPSGSPFASTPQKPLFAQQRAQKRSGAPSTRGPLQPSKLGQAVMYNDDEDEREPNQQETKANRSGTFGLPFDDTYDLDDSSILMSGAPGGDLEMRDDDSDLMMLNTPAATERVRKEAAGIFRASVAQSGPRIRDLRFAALAKDVYTHMGTASLLEPGELIVNTERLITRLYDEGVGEEEDEEKLDEALAHVAGELTDLWKRAISDFPQPDEEHTVEIGPGPNTSPLEKATYLANLALHVHHERYEDNTGRTRPTPLPETLFKWLDEYHNVYSGQTEEILRYKPSPASHALFWQAIFVALLRGKVDDAAKLLRQAGWDKVRKDNGENKYINRALESVQLATAETVAMLENCPGYNEDWDIWNSDWTLWRVRTRGALDHLRRFAEGRDTMLGDSTFSDFSASVTSTRNRESMAGLARRAESQVPWEIYEKLNIIFDIVLGSKNAILDAAQDWCEATIGLTAWWDDRRADKFGNPLSMARSQALTLASQSATTDSYLDRLNNAFHVAVEEDFYLNPHNPVEVGIACIFEDNVKGLIGLLRGWSLPIASAVAEIASLGGWLPQHQPGAFFMEGLDQDDLDVLGVDPTAPDEIDGIKDSTLIQYAQKLTDDEDIGTIADHLGESRDGWELAIHVLGRMDSQERSEEMIGILVRHIVDSLHVDSNEVVDKTWSLLNELGMIPYAEEVVETYAEILARDSHRYGEAMWYFALAHKPHKVREVMNLLISYSLIQSTAFPPNEELDDWLHRLLNERNETLEQCAKQDLEAAELLGKMLSGYASLRQYFVIRDDEAVLPNATPYARKQQAATALVNVIASSDDNIRGGLLDPTRDGIVSEDFLLALLGEALAFVTNPDNTNVHLGQQALPILNLDQIDIILKAVEDLQAVSDRVRNTCEEFLQIVLASAPGGLKGTTPADLLKKNASGSLVLAGSTMVATQLKNSLSGGLVGSGAKMNPVKRGWDWRADMPAKTTGDDVMQRLRLGVAKDLAGLWLADADNALW
The following text describes a protein:
Function:
Golgi membrane protein involved in vesicular trafficking.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MFTSLDRNLYVDNHITLTKMDYQNTETIAEQERNASRLPQMFQMSSHPVALFFFLLFRTGAIVAYILGMFFTSSFMLLFIVIFTLLAVDLWTVKNVSGRLLVGLRWRNETGVDGESIWIFESADPSRPRNAVDQKTFWYALYLYPFIWIILGIVAIIRFEFLWLALVAVAIGLTSVNTAAYSRCDKDAKRRWATELADSNSSGFVSRFLSRAFIKRFIG
The following text describes a protein:
Function:
Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein bound to a number of target proteins.
Sequence:
MAAEKCAEEFGDSSAASLKIVPKDYAYPLLEDPQGALTTPTEGGRTLVTRGGFNYFHYGCDGHQDAGWGCGYRTLQSAISWIQRRQGSSGHVPSIREIQQILVAIGDKGPEFVGSRDWIGTLEEFYVIDVLHQVPCKILHAKELSSDEILGELRSYFEKYQGFVAMGGLSDTASKAITGYHCSARGRIFLQVVDPHFVGVPSSRQHLIDLGYVRWVPVDEFAGSTYNLCLILQP
The following text describes a protein:
Function:
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Miscellaneous:
MISCELLANEOUS: Present with 10100 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MPQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDNIEVSK
The following text describes a protein:
Function:
Required for the activity of the bacterial periplasmic transport system of putrescine.
Subcellular Localization:
Periplasm.
Sequence:
MKLFNKMTTLALVTAGTLASVAVQAEEVVRMYNWSDYIAEDTLENFKKETGIRVIYDVFDSNEVVEAKLLSGRSGYDIVVPSNHFLAKQIKAGAFKPLDRSKLTNFKNLNADLMKLLEKADPGNQYAVPYLWGTNGIGYNINKVKAAVGEDAPPFNSMELIFNPKYAEKISKCGFAMLDSADDMVPQAMIYLGLDPNSTKAEDYEKAGELLEKIRPYVTYFHSSRYISDLANGDICVAYGFSGDVFQAAARADEAGNGNKIGYSIPKEGANLWFDMLAIPADATNVENAHKLINYLLRPEVIAPISNYVAYANPNDLAQPLVDEAIRNDPAIYPPKEVLDKLYIGEIRPLKIQRVLTRVWTKVKSGQ
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.
Domain:
Lacks the C-terminal regulatory region which is replaced by HisZ.
Sequence:
MLKLAIPKGRLEEKVMTYLKKTGVIFERESSILREGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETSLIQPFFIPTNISRMVLAGPKGRGIPEGEKRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETGRTLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQEVIEHDSNEQSRG
The following text describes a protein:
Function:
Might be involved in the organization and polarity of the actin cytoskeleton. Interacts with the barbed end of actin filaments and nucleates actin-filament polymerization in vitro. Seems to play a role in cytokinesis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MVGMIRGGMGDQNWSRLVFWLILFSGLLVITLEENPEKDEIFLSQFMAPSTGQVNEHMEETSWAQRCWQDSDCVKEAVAEFNLCFPGSKDSRELFGLNHTNLKQTLLDCIQEKGKLNGHNPKYLELLSSMLDIPRRNLATKPGSSPSPSPSRPPKRSRGPPRPPTRPKSPPPRKSSFPPSRSPPPPPAKKNASKNSTSAPVSPAKKKEDHEKTIIIAVVVTAVSTFLLAALFFLCCSRVCGNGSGGRKNDERPLLSLSSSDYSVGSSINYGGSVKGDKQGHQSFNIYSNQGKMSSFDGSNSDTSDSLEERLSHEGLRNNSITNHGLPPLKPPPGRTASVLSGKSFSGKVEPLPPEPPKFLKVSSKKASAPPPPVPAPQMPSSAGPPRPPPPAPPPGSGGPKPPPPPGPKGPRPPPPMSLGPKAPRPPSGPADALDDDAPKTKLKPFFWDKVQANPEHSMVWNDIRSGSFQFNEEMIESLFGYAAADKNKNDKKGSSGQAALPQFVQILEPKKGQNLSILLRALNATTEEVCDALREGNELPVEFIQTLLKMAPTPEEELKLRLYCGEIAQLGSAERFLKAVVDIPFAFKRLEALLFMCTLHEEMAFVKESFQKLEVACKELRGSRLFLKLLEAVLKTGNRMNDGTFRGGAQAFKLDTLLKLADVKGTDGKTTLLHFVVQEIIRTEGVRAARTIRESQSFSSVKTEDLLVEETSEESEENYRNLGLEKVSGLSSELEHVKKSANIDADGLTGTVLKMGHALSKARDFVNSEMKSSGEESGFREALEDFIQNAEGSIMSILEEEKRIMALVKSTGDYFHGKAGKDEGLRLFVIVRDFLIILDKSCKEVREARGRPVRMARKQGSTASASSETPRQTPSLDPRQKLFPAITERRVDQSSSDSD
The following text describes a protein:
Function:
NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide.
Domain:
The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
Sequence:
MSANDRAIETLRREIAKLQTDGAAIARKDAGIRAKLASAMAAQAKAKTAPALRLKQAEASRLEKELMATSKSQADIATKIAKKQSSLSAKLVVQANEAKKADAKAKKNQERVSKTQEEATRKLEAGYRKLTLENQSLEQRLQRELSAMKPTAGPTTNADLTSAPPHDIFISHAWEDKADFVEALAHTLRAAGAEVWYDDFSLRPGDSLRRSIDKGLGSSRFGIVVLSTHFFKKEWPQKELDGLFQLESSGRSRILPIWHKVSKDEVASFSPTMADKLAFNTSTKSVDEIVADLMAIIRD
The following text describes a protein:
Function:
As a component of the mitochondrial large ribosomal subunit, plays a role in mitochondrial translation. When present in mitochondria as a free protein not associated with the ribosome, associates with mitochondrial RNA polymerase POLRMT to activate transcription. Required for POLRMT stability.
Subcellular Localization:
Mitochondrion.
Sequence:
MFPVARCCVKFQAVASTVRRLEISTVRLLRTTSELRNLSPLPSPPLDNAPKDYPPKIHQLVDQIASLTLLEVSELNELLRRTLKIQDVGMMPMGSMMPGASATPSQDAEESEAPAKKEKTNFTVKLTEVNATDKVKLIKEVKNCIQGLNLVQAKKLVEALPQEIKANVSKDEAEKIKTALEAAGGKVVLE
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC).
Subcellular Localization:
Nucleus, nuclear pore complex.
Sequence:
MQQEEMRVVLCESRLIFLNVQSEFGTGRHEDMAEKMRSNKLLAYSRQYRSTIKACTIHLQSLLRFSKDDNHNRIMIGQLELMEMTELLWSLAEIIFIDQLGHQSGRYIVSQLMDWFQMKFYDGDNKVNRVIKSELYDKHHLYWDALYSLVCLARIEEARHLLSLHSSSHTEPFRTMDLLLSKMPIYKHGQYSQQEFSLKWRQWHLVCEEQDEDGTFSVDDKLSDLCKLLAGQDQMFTKLRDSLGTWYCMLICRLFYQSPLCEATDLKMHVQFCIDQYGGNLGLTDWDNIILSIIMMDIREALCIASTTFPNWWFVCHLTDLLQHSGHIDDKPAGFGSNLREFFILEYASSLVSCPSLRDTAIGYYSSCPAYGKAHIGDLVLRDSLESTLKVEKLLHTCNKYQLESDANIICRSFSLKWLQKKQYANALIWAVRSKDTNFTASIVKKLLAIDAITMGNILERWEVIADIGGTVHFNIQLTILTKLVEYKRLLDDGNLGGAINILIVLLKEAVIHHEFFQLLLGETMSLLEKDDIQLTSDELFKLNEYVQEYRDALRFRRIKADVKLLGRMNDSFEKVHQRLTNQIAACYLR
The following text describes a protein:
Function:
Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle. Note=Colocalizes with SHCBP1L at spindle during the meiosis process.
Sequence:
VEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRVQSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKSTAGDTHLGGEDFDNRMVSHLAEEFKRARFEELNADLFRLDKGQIQEIVLVGGSTRLLQDFFNGKELNKITITNDKGRMVQEAERYKGKISEQDK
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MSLTDWGSPEPQPEMLQINIKEEEADREDHVTLSDGGNCLTNEENRCPKPARAQLGIRSPPVTDGSMLAQTRDSAQFRSCSASAKEPGFICNKSGEMFSDNSDVSTHHFACTLYDSQSRDLASAGEFHCTECGKSFACKVSLEEHVKLHTEEKPFPCTDGGKLFAGKSSLQNHQRIHCGAKLFHCAECGKRFSQKVTLHLHQSVHTGEKPFTCKECGRSFSKKDNLRRHKKVHIMEKTCAQCGKCFTQTRPLDRATSLKLFTCPECEKRNHIRELPFRCALCGDGFYGKSYLTMHQKVHEREKPFRRKDCGTTFPEKIHMSVGSPEPQPEMLQIKIKEEEADREDHVTLSDGGNCLTNEENRCPKPARAQLGIRSPPVTDGSMLAQTRDSAQFRSCSASAKEPGFICNKSGEMFSDNSDVSTHHFAGTLYDSQSRDLASAGEFHCTECGKSFACKVSLEEHVKLHTEEKPFPCTDCGKLFAGKSSLQNHQRIHCGAKLFHCAECGKRFSQKVTLHLHQSVHTGEKPFTCKECGRSFSKKDNLRRHKKVHIMEKTCAQCGKCFTQTRPLDRATSLKLFTCPECEKRNHIRELPFRCALCGDGFYGKSYLTMHQKVHEREKPCRRKDCGTTFPEKNKLRKHQEIHNKEAEEGWVSETDRLLVL
The following text describes a protein:
Function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKHILDSQEVEIVWTILPAVI
The following text describes a protein:
Function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side.
Sequence:
MFLLYEYDIFWAFLIISSLIPILVFFISGFLAPSSKGPEKLSSYESGIEPIGDAWLQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGVSVFVEALIFVLILIVGLIVMNSIEFPLFHRTTQNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAIIDAITKLRKKISREIYPDRIMSQRENRCFTTNHKFQVGHSIHTGNYDQGFLYQPPSTSEIPPETFFKYKSSVSSHELVN
The following text describes a protein:
Function:
Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular Localization:
Cytoplasm, cytosol. Rough endoplasmic reticulum.
Sequence:
MGHQQLYWSHPRKFGQGSRSCRICSNWHGLIRKYGLNICHQCFRQYAKDIGFIKLD
The following text describes a protein:
Function:
Essential for filament assembly. May act as a facilitator of flagellin (hag) secretion. Antagonizes translational repressor CsrA indirectly.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MAIQNPYTAYQQNSVNTATPGELTLMLYNGCLKFIRLAAQAIENDDMERKNENLIKAQNIIQELNFTLNRNIELSASMGAMYDYMYRRLVQANIKNDTGMLAEVEGYVTDFRDAWKQAIQSERKDRHGSGGIA
The following text describes a protein:
Function:
Component of the intraflagellar transport complex B (IFT-B) involved in flagellar assembly (Probable).
Subcellular Localization:
Cell projection, cilium, flagellum. Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton, flagellum basal body. Note=Localizes to the cytoplasmic and membrane-bound portions of each of the eight axonemes, localizing particularly at the flagellar pores and at the distal flagellar tips. Localizes to the basal bodies.
Sequence:
MLHNRMTTAFERSKEQEHEAAKNEIPSFQVFIERRDFLGAITVLKFLKSTRNTAEVGNADLWIAYCNFHLGRHEEALEIYTALKKSKNPPLDAHTLDLYRAICMLYLGQMGDARELATTLPPTPLSNRLLFHACSRLLDEESLVTYHTKLRNVSADQMALAAVHFLRTHYQQALECYEEVLQVQPECFAIYMHMALCYYKLGDYLKSEEFLMLYRENAEDSLTSLNLYAATKFRQGKMAEALKILEELQNDETIVGLPIFKHNKCLYTEMNAAVHILPPLVGIVSEARQNLVKLYIEKGQYEDAYKVVQSFEPAVSAEYTLKAAAYAYYGQTVQDMAVLQYAQAAYSTVGQSDADRDTVLGRRAMAAAYFLTGEFEEASMYLESIADIPKESEDSFMLNYSLCLAATCKVTEALERLMSVMGSTNFTPVHRTWLGRLLIRAQRSAEAFDLYRDAEKNSLQTILLMKVIANECFAAGEYQYAERAAAILVDLDKASKDHYIMIQKACIAAMELIRRGKTITPPELVYETE
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a 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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular Localization:
Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MSFFGLKRYSTPILKPMLPFFLGGAIVFYGTVKLRDAMMDSAEYRNDPRNPKAGKYGSDH
The following text describes a protein:
Function:
Required for autophagic breakdown of peroxisomes, called pexophagy, through linking peroxisomes to the autophagy apparatus. Involved in regulation of the glyoxylate cycle.
Subcellular Localization:
Peroxisome. Note=Recruited to peroxisomes by PEX3.
Sequence:
MASVNNYQVDCGSRSARIQPRINNGIHDEESLFEVLELSEEEFELDFHRLKSFNDVRVINNPDLSPECTNTAISRDETLESASSAFEVPSDEIAILSISSDSNKNSPPSEQPAPALRNIRSSSNSDRIDEWCLGSHLFNELHQNVPQSSDGVNHGFPVYSFKERELYTSAKLKKLTNAQRIAVQKLSRDLYPILRTCYREKTRRQLLTYHHERIFDDIPSFFPQRDFIFNYYSMPLEFDRLSDVDIDSSSRSRFTDESTGETLNRSPSAASSSLENTSWFGWTLLSRFLDREW
The following text describes a protein:
Function:
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain. In presence of high levels of lactate, also acts as a protein lactyltransferase that mediates lactylation of lysine residues in target proteins, such as TEAD1, TP53/p53 and YAP1. Protein lactylation takes place in a two-step reaction: lactate is first activated by ATP to form lactate-AMP and then transferred to lysine residues of target proteins. Acts as an inhibitor of TP53/p53 activity by catalyzing lactylation of TP53/p53. Acts as a positive regulator of the Hippo pathway by mediating lactylation of TEAD1 and YAP1.
Domain:
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence:
MDSTLTASEIRQRFIDFFKRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPSHPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALELLTQEFGIPIERLYVTYFGGDEAAGLEADLECKQIWQNLGLDDTKILPGNMKDNFWEMGDTGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNRAQVPDHTLGKLVLRMPMGLTWPTGCWLTTLGPSLWHWLMVAGLTTQGVVFASYRYVLRRILRRAVRYAHEKLNASRGFFATLVDVVVQSLGDAFPELKKDPDMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDSKTIPGDTAWLLYDTYGFPVDLTGLIAEEKGLVVDMDGFEEERKLAQLKSQGKGAGGEDLIMLDIYAIEELRARGLEVTDDSPKYNYHLDSSGSYVFENTVATVMALRREKMFVEEVSTGQECGVVLDKTCFYAEQGGQIYDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGDLKVGDQVWLFIDEPRRRPIMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIANEMIEAAKAVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPSGPAGSLTSVEFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKAESLKKCLSVMEAKVKAQTAPNKDVQREIADLGEALATAVIPQWQKDELRETLKSLKKVMDDLDRASKADVQKRVLEKTKQFIDSNPNQPLVILEMESGASAKALNEALKLFKMHSPQTSAMLFTVDNEAGKITCLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDVSAQATGKNVGCLQEALQLATSFAQLRLGDVKN