lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MIILLKIAAEAFRSLVFSPQPQNPAAQQNSDGRATTVFRAETRNSRPSQLLIIQAQNLINFRQINIYHDSYGAAATGQHIGSTVVFLLFSAGVFAYQKITAETTHHSAGEEETLSEPIAAAAAVTFTCEICADEKPLTSFRILACNHWYCSDCITKYISSQLLENNAAAISCIAAGCDEHLDPYQLRSILPENVFVRWCDALCEASIEEEDKYYCLYKDCSAFLINDSESRKEIIAQAKCPACGRCFCVTCKVQWHEGFLCEEFQKLRVDERSNEDLMLMNLAKENKWKRCPLCQIFVDRSEGCLFMKCRCGYTFCYNCGAPLKQHYCTNCKH
The following text describes a protein:
Function:
Component of the ESCRT-I complex, a regulator of vesicular trafficking process.
Subcellular Localization:
Cytoplasm. Endosome. Late endosome membrane; Peripheral membrane protein.
Sequence:
MNINNSNNNFGEPPPPYSFNNSPLSSSPLGPPTLNNSNTNNNNNNNSTNNNNNNNNNNNNNNSNKQFENMINLKSQNSFQNIKEVKLFNNNIEREMYENLAELYSIIKVTEHLEKAYIRDDVSPKDYTTACSKLIAQFKSSQTLLKDQVSNVGQFMKDYDLNCKAAFDRLVIKGFPSTLEHNTNESSTDSAMAKNVAEAVQLFITTMDSIRLKLVSVDGIYPLLSDLMESLNKNQWLGPTFEGKEKIKNWISILNQMKATDELDDDQSRQLLFDLDNSYNIFYKAIKS
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Sequence:
MVIPAELIQKALKQQSGWGFTEGLVLGQLSVIITVIIILKFVIFAENKSPKKGNDMTAVSAKDKEAEHVAMGGQTANGVKTSGVRRNKSSTNLRNRLATGAAGASISRPGSSRVSMVRSTSGAVPVLGQNGGATPRGMAGSSVAGSTSNLAVPVPTTPTIAEGIEPENDSTLQDDSAIIDLDLDLDLSPVDEILHKTCYQLSSHAPESLDWFNVLVAQIITQLRFDAKANNNLNLLNSLDAAFNSKRPDFIDRINVTEINLGDDYPILSNCKITHKGTGPAGSGAASGNNMPNNAEYDDSRLEAQMDIDLSDTITLGIETRLNLNQPKILSPFLSLSTSLPVSLSVTIVRFTARLNISLYQQIEQTEEDEKDKRDTILSINFEPDYKLQLSVKSLVGSRSRLQNVPTLESLVDSKIQKWFRDHYVEPHQMIFILPSLWPRKKRSATAGAAGTATGADTASGSS
The following text describes a protein:
Function:
High-affinity potassium transporter that plays a role in K(+) acquisition. May operate as a K(+)/H(+) symporter.
Miscellaneous:
MISCELLANEOUS: K(+) uptake enhanced by a proton electrochemical gradient (acidic outside). Not affected by specific inhibitors of voltage-gated K(+) channels.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MELSMFGREDTNSSQWGEVHGPFMLEEIVCQAQNMLTSRGIFMKSNPLKYALPLLLLQMSVIIVTSRLIFRVLQPLKQGMISAQVLTGVVLGPSFLGHNVIYMNMFLPAGGKIIIQTLSNVGFVIHLFLLGLKIDGSIIRKAGSKAILIGTASYAFPFSLGNLTIMFISKTMGLPSDVISCTSSAISLSSMTSFPVTTTVLAELNILNSELGRLATHCSMVCEVCSWFVALAFNLYTRDRTMTSLYALSMIIGLLLVIYFVFRPIIVWLTQRKTKSMDKKDVVPFFPVLLLLSIASLSGEAMGVHAAFGAFWLGVSLPDGPPLGTELAAKLEMFASNLFLPCFIAISGLQTNFFEITESHEHHVVMIEIILLITYGCKFLGTAAASAYCQTQIGDALCLAFLMCCQGIIEVYTTIVWKDAQVVDTECFNLVIITILFVTGISRFLVVYLYDPSKRYKSKSKRTILNTRQHNLQLRLLLGLYNVENVPSMVNLLEATYPTRFNPISFFTLHLVELKGRAHALLTPHHQMNKLDPNTAQSTHIVNAFQRFEQKYQGALMAQHFTAAAPYSSINNDICTLALDKKATLIVIPFHKQYAIDGTVGQVNGPIRTINLNVLDAAPCSVAIFIDRGETEGRRSVLMTNTWQNVAMLFIGGKDDAEALALCMRMAEKPDLNVTMIHFRHKSALQDEDYSDMSEYNLISDFKSYAANKGKIHYVEEIVRDGVETTQVISSLGDAYDMVLVGRDHDLESSVLYGLTDWSECPELGVIGDMLTSPDFHFSVLVVHQQQGDDLLAMDDSYKLPNVEHQKIGDTGIQQRFSAEEGFTTIDLGKR
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the 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:
MECVVQGIIETQHVDALEVLLQGLSGVPKERVRVHELCLKSGPNLGVVPSEVRLLCDLAQSTPSWTIRHVGGAMRGAGAEQISVLVRSIVESKASNNVLRYFYGIGYKLDHEVLKGGFAFRFHRGAQITVTVTSVSKMTKLHATNEAVPITPAIQLVEITAPAAADNYNDVVSAVTSFCEYLAPLLHLSKPGNSTGIVPTAGAAAASLMSSGGGGGGKTL
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the 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. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MQTLHQSQLLQNPAEAANNQSESDAPPKQVAQAMERLNQAARVIADIRLGADRILEAMFVASQPRHTDMPLQLFLREDASMRQHLQDLRLIGKKLEESGVLTESLRSRSNSWGLHMPLVCPDGAVVAYAWKRQLAGQAGASAVDRTRLALKAFTDQKRRFFPHIDDGLKMEPSSKKHRASHLLLENGREEPVDYKTLPDIQSRLEKLVPSVKVSTYGRLNWLKRANSLPGSGSDDPTEASKPIFQSSSKLRSGLQTEVVDKIAVIELSFPSLFRAIVSLSPAGSVDPDAVAFFSPDEGGSYLHARGFSVYHVYKHITEHAATALQYFLGFGTGTALYSLLLWICSFESVFSKPCTKCGRLLAMDKKSALILPPLHRAYQELPLALNLDVCEAYHSSCSQDDT
The following text describes a protein:
Function:
Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MLTLWSLLLYTFIPLIQCTGYLELRLTSPYVRVLNVSVELAIGSEKSFYKVPLSPYYELAITNVPIEFDQPASIIIRSGPVKEIGLTDFVVSPKIFSTRKMSIVPPKAGLPFSGFRIDIKCDTNYFGAHCEHFCDEEQARSMGRRCNILGNIGCPIGVRGSKCDIELPIDSGICKCMNGGKCVNSFDSKLTADFPICECLNGFEGAACEKQMKIFEPKISTRLFESTARFHDLANVSVKNQLYDDKMDIYSKHVAPSFHVLQQGALNGKALRAPKKQKNTIIFDPVTLSFHPTKPISTPYFPKGRPVRLNSQS
The following text describes a protein:
Function:
Involved in cellular response to chemical stress and may contribute to resistance toward antimicrobial natural compounds as well as drugs (Probable). Catalyzes the methylation and detoxification of the P.aeruginosa toxin 2-heptyl-1-hydroxy-4(1H)-quinolinone (HQNO) to 2-heptyl-1-methoxy-4(1H)-quinolinone (HMOQ). Can also methylate 3-bromo-2-heptyl-1-hydroxy-4(1H)-quinolinone, and shows much lower activity with 1-hydroxyquinolin-4(1H)-one, quercetin, 4-hydroxyquinolin-2(1H)-one (DHQ) and 4-hydroxyisoquinolin-1(2H)-one. In addition, N-methylates and abolishes the mycobactericidal activity of 3-methyl-1-oxo-2-[3-oxo-3-(pyrrolidin-1-yl)propyl]-1,5-dihydrobenzo[4,5]imidazo[1,2-a]pyridine-4-carbonitrile (compound 14), an inhibitor of DprE1. Also methylates and reduces the inhibitory effect of TPSA (2-[5-(2-{[4-(2-thienyl)-2-pyrimidinyl]sulfanyl}acetyl)-2-thienyl]acetic acid), an inhibitor of GlmU acetyltransferase.
Miscellaneous:
MISCELLANEOUS: Is dispensable under in vitro conditions in both axenic and macrophage culture.
Subcellular Localization:
Cytoplasm.
Sequence:
MSTVLTYIRAVDIYEHMTESLDLEFESAYRGESVAFGEGVRPPWSIGEPQPELAALIVQGKFRGDVLDVGCGEAAISLALAERGHTTVGLDLSPAAVELARHEAAKRGLANASFEVADASSFTGYDGRFDTIVDSTLFHSMPVESREGYLQSIVRAAAPGASYFVLVFDRAAIPEGPINAVTEDELRAAVSKYWIIDEIKPARLYARFPAGFAGMPALLDIREEPNGLQSIGGWLLSAHLG
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 inner membrane; Single-pass membrane protein; Matrix side.
Sequence:
MVYLLVHWVHIFIPMGSAIRYYLNKKNDEKLFSFWNNSSLFKREPKLNEEITLKFFQEQIKFFLRLLL
The following text describes a protein:
Function:
Functions as a positive regulator of TNF-induced NF-kappaB signaling. Regulates angiogenesis and cellular metabolism through interaction with PKM.
Subcellular Localization:
Endoplasmic reticulum lumen. Cytoplasm.
Sequence:
MAAAGRFGLLLLIVLWTMVTVVLPASGEGGWKQSRLGTEAAVMEEERCTVERRAHLTYSEFMQHYAFLKPVILQGLTDNSKFRALCSRENLLASFGDNVVRLSTANTYSYQKVDLPFQEYVEQLLHPQDPESLGNDTLYFFGDNNFTEWAPLFQHYRPPPFRLLGTTPAYSFGIAGAGSGVPFHWHGPGFSEVIYGRKRWFLYPPEKTPEFHPNKTTLAWLLEIYPSLAPSARPLECTIQAGEALYFPDRWWHATLNLDTSVFISTFLG
The following text describes a protein:
Function:
Aldehyde dehydrogenase able to oxidize various aldehydes such as formaldehyde, glyceraldehyde, butyraldehyde, glutaraldehyde and benzaldehyde (in vitro). Is likely involved in the oxidative D-xylose degradation pathway, catalyzing the oxidation step of 2-oxoglutarate semialdehyde to 2-oxoglutarate. Is able to use both NAD(+) and NADP(+); however, shows a preference for NADP(+). Does not display succinate semialdehyde dehydrogenase activity.
Sequence:
MAIATIDPTTGITLKTFDAHTPEEVENRIARAEAAFRSLQNTSFEERARWMHKAADILESEADEVARLIATEMGKTLTTAKYEALKSATGMRHFADHAQRYLSPETPVPASEVNASNLHVQFDPLGVVLAVMPWNYPLWQAVRFAAPALMAGNTGLLKHASNVPQCALYLGDLFARGGFPEGAFQTLLVEGKDVIPLVDDARIRAVTLTGSVAAGSAIAEAAGRNIKRSVLELGGMDVFIVMPSADIEKAAAQAVIARLQNSGQSCIAAKRFYVHEDVYDRFEHLFVTGMAEAVAGDPLDESTSFGPLATERGRQDVHELVRDAREKGAAVQCGGEIPEGEGWYYPATVLTGVTEDMRIYREECFGPVACLYKVSSLQEAIALSNDSDFGLSSSVWTNDETEATEAARSIEAGGVFINGLTASFPAVPFGGLKDSGYGRELSAYGIREFVNIKTVWTS
The following text describes a protein:
Function:
Assembles to form an icosahedral capsid of 66 nm, with a T=7 laevo symmetry. Responsible for its self-assembly into a procapsid. The phage does not need to encode a separate scaffolfing protein because its capsid protein contains the delta domain that carries that function.
Subcellular Localization:
[Major capsid protein]: Virion. Note=Forms the icosahedral capsid shell which contains 420 major capsid proteins.
Domain:
[Scaffolding domain delta]: The scaffolding domain delta has a role of scaffold allowing the self-assembly of the capsid protein (By similarity). In prohead I, the scaffold domain forms rigid helix-turn-strand structures on the interior surfaces of all capsomers and, around the portal, forms trimeric coiled-coil towers, 2 per surrounding capsomer.
Sequence:
MSELALIQKAIEESQQKMTQLFDAQKAEIESTGQVSKQLQSDLMKVQEELTKSGTRLFDLEQKLASGAENPGEKKSFSERAAEELIKSWDGKQGTFGAKTFNKSLGSDADSAGSLIQPMQIPGIIMPGLRRLTIRDLLAQGRTSSNALEYVREEVFTNNADVVAEKALKPESDITFSKQTANVKTIAHWVQASRQVMDDAPMLQSYINNRLMYGLALKEEGQLLNGDGTGDNLEGLNKVATAYDTSLNATGDTRADIIAHAIYQVTESEFSASGIVLNPRDWHNIALLKDNEGRYIFGGPQAFTSNIMWGLPVVPTKAQAAGTFTVGGFDMASQVWDRMDATVEVSREDRDNFVKNMLTILCEERLALAHYRPTAIIKGTFSSGS
The following text describes a protein:
Function:
Reversibly phosphorolyzes beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine to form alpha-D-galactopyranose 1-phosphate and acetyl-D-glucosamine. Active towards galacto-N-biose and lacto-N-biose. Does not phosphorolyze galacto-N-tetraose or lacto-N-tetraose. In the reverse reaction has activity toward N-acetyl-D-glucosamine and N-acetyl-D-galactosamine, but not L-rhamnose, D-glucose or D-galactose.
Sequence:
MKKDTMLAGRVTIPTDVDVVPETMELLNRWGADAIRDCDGTDYPEELKAVQAKVYSTYYTTRKDNAWAKAHPEEVQQCYIMTSFYTATETTLRIPLLKGIAKELMMVNNYDDKVRWWEVIDRSTAMVVSTDTWSYDKETGEVIITNCEPFHNYTVSFLAYLIWDPVHMYNAVVNGWQGVEHQITFDVRQPKTREYSMVRLRKFIEEHPYVDVIRYTTFFHQFTLVFDEMMREKYVDWYGYSASVSPYILEQFEKEVGYRFRPEFIIDQGYYNNQYRIPSKEFKDFQAFQRREVAKLAKEMVDITHEYGKEAMMFLGDHWIGTEPFMEEFKTIGLDAVVGSVGNGSTLRLISDIPGVKYTEGRFLPYFFPDTFHEGGDPVKEAKVNWVTARRAILRKPIDRIGYGGYLKLACQFPEFIDYVESVCNEFRELYENIKGTTPFCIKRVAVLNSWGKMRAWGAHMVHHALYQKQNYSYAGVIESLSGTPFEVSFISFDDIKKDKNILKNIDVIINVGDGDTAHTGGLVWEDADISSAIHQFVYEGGGLIGIGEPTGHQYQGRYIQLANVFGIEKETGFTLNYDKYNWDAVESHFITEDCTKEVDFGEGKKNMYALEGTTILVQMEKEVQMAVNEFGKGRSVYLSGLPYSFENSRVLYRSILWSAHEEENLHKWYSSNFNVEVHAYVKNNKYCVVNNTYEPQNTTIYRGDSSSFDLELEANEIIWYEI
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 complex plays an important role in the uptake of multiple carbon sources present in different host niches.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MALSKTVYNLLFRRSSTFAVTVVVGAVFFERLFDQGGNALFESINRGKLWKHIKHNYEQKEE
The following text describes a protein:
Function:
Transcriptional activator of glycolytic gene expression, such as enolase genes (ENO1 and ENO2), glyceraldehyde-3-phosphate dehydrogenase gene (TDH), phosphoglycerate kinase (PGK1), phosphoglycerate mutase (PGM1), pyruvate kinase (PYK1) and triosephosphate isomerase (TPI1) genes. Binds DNA on E-box motifs: 5'-CANNTG-3'. In response to adenylic nucleotide reduction, activates Ty1 mRNA transcription, possibly by controlling Ty1 antisense transcription. Acts as a cell cycle transcription factor. Its function may also be linked to sulfur metabolism and the cross-regulation between phosphate and sulfate metabolism.
Miscellaneous:
MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MNSILDRNVRSSETTLIKPESEFDNWLSDENDGASHINVNKDSSSVLSASSSTWFEPLENIISSASSSSIGSPIEDQFISSNNEESALFPTDQFFSNPSSYSHSPEVSSSIKREEDDNALSLADFEPASLQLMPNMINTDNNDDSTPLKNEIELNDSFIKTNLDAKETKKRAPRKRLTPFQKQAHNKIEKRYRININTKIARLQQIIPWVASEQTAFEVGDSVKKQDEDGAETAATTPLPSAAATSTKLNKSMILEKAVDYILYLQNNERLYEMEVQRLKSEIDTLKQDQK
The following text describes a protein:
Function:
Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall. Chr5 shows acceptor substrate promiscuity and is also able to cross-link chitin to chitin.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor. Secreted, cell wall.
Sequence:
MYFKYTAAALAAVLPLCSAQTWSKCNPLEKTCPPNKGLAASTYTADFTSASALDQWEVTAGKVPVGPQGAEFTVAKQGDAPTIDTDFYFFFGKAEVVMKAAPGTGVVSSIVLESDDLDEVDWEVLGGDTTQVQTNYFGKGDTTTYDRGTYVPVATPQETFHTYTIDWTKDAVTWSIDGAVVRTLTYNDAKGGTRFPQTPMRLRLGSWAGGDPSNPKGTIEWAGGLTDYSAGPYTMYVKSVRIENANPAESYTYSDNSGSWQSIKFDGSVDISSSSSVTSSTTSTASSASSTSSKTPSTSTLATSTKATPTPSGTSSGSNSSSSAEPTTTGGTGSSNTGSGSGSGSGSGSSSSTGSSTSAGASATPELSQGAAGSIKGSVTACALVFGAVAAVLAF
The following text describes a protein:
Function:
Involved in the synthesis of glycan chains within amylopectin in leaves. May play a regulatory role in the control of starch accumulation in plastids.
Subcellular Localization:
Plastid, chloroplast. Plastid, amyloplast.
Sequence:
MISYFLNQDFSRKKQGRMAASGPKSSGPRGFGRRTTVGSAQKRTQKKNGEKDSNATSTATNEVSGISKLPAAKVDVQKQSSVVLNERNVLDRSDIEDGSDRLDKKTTDDDDLLEQKLKLERENLRRKEIETLAAENLARGDRMFVYPVIVKPDEDIEVFLNRNLSTLNNEPDVLIMGAFNEWRWKSFTRRLEKTWIHEDWLSCLLHIPKEAYKMDFVFFNGQSVYDNNDSKDFCVEIKGGMDKVDFENFLLEEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAENVWYIEPSDFKAEDTVKLYYNKRSGPLTNSKELWLHGGFNNWVDGLSIVVKLVNAELKDVDPKSGNWWFAEVVVPGGALVIDWVFADGPPKGAFLYDNNGYQDFHALVPQKLPEELYWLEEENMIFRKLQEDRRLKEEVMRAKMEKTARLKAETKERTLKKFLLSQKDVVYTEPLEIQAGNPVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMEATDDESSHVKTTAKVPLDAYMMDFVFSEKEDGGIFDNKNGLDYHLPVVGGISKEPPLHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRSYHWGGTEIKVWHGKVEGLSVYFLDPQNGLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKTRIVFTIHNLEFGANAIGKAMTFADKATTVSPTYAKEVAGNSVISAHLYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEELQNRLGLKSADFPVVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGLFDTVFDVDHDKERAQAQVLEPNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPALEYLELYHSARK
The following text describes a protein:
Function:
Transcriptional activator. Binds DNA on GT-box consensus sequence 5'-TTGGTT-3'. Plays a role in spermiogenesis.
Subcellular Localization:
Nucleus.
Sequence:
MSGVMVGSHADMAPASTAEGAGEKPGPAAPAPAAQYECGECGKSFRWSSRLLHHQRTHTGERPYKCPDCPKAFKGSSALLYHQRGHTGERPYQCPDCPKAFKRSSLLQIHRSVHTGLRAFICGQCGLAFKWSSHYQYHLRQHTGERPYPCPDCPKAFKNSSSLRRHRHVHTGERPYTCGVCGKSFTQSTNLRQHQRVHTGERPFRCPLCPKTFTHSSNLLLHQRTHGAAPAPGTASAAPPPQSREPGKVFVCDAYLQRHLQPHSPPAPPAPPPPPPPVVPELFLAAAETTVELVYRCDGCEQGFSSEELLLEHQPCPGPDAAPQPQEAPAEAPKADQPPSPLPQPPPPAAAPAPGFACLPCGKSFRTVAGLSRHQHSHGAAGGQAFRCGSCDGSFPQLASLLAHQQCHVEEAAAGRPPPQAEAAEVTCPQEPLAPAAPVPPPPPSAPASAERPYKCAECGKSFKGSSGLRYHLRDHTGERPYQCGECGKAFKRSSLLAIHQRVHTGLRAFTCGQCGLTFKWSSHYQYHLRLHSGERPYACGECGKAFRNTSCLRRHRHVHTGERPHACGVCGKSFAQTSNLRQHQRVHTGERPFRCPLCPKTFTHSSNLLLHQRTHSAERPFTCPICGRGFVMAAYLQRHLRTHAPANTPPSTTAPAAGPQPPAPLAAARAPPATQDVHVLPHLQATLSLEVAGGTAQAPSLGPAAPNSQTFLLVQTAQGLQLIPSSVQPPTPPPPPAPPKLILLPSSSAGAGGGRARQGPRAVGKAGQGAGVVWLPGPGGLGVQGAASAGASGTGQSLIVLQNVGGGEAGPQEMSGVQLQPLRPAPEVTTVQLQPAQEVTTVQLQPAQEVTTVQLQPAQEVTTVQLQPVAGQLSNSSGGAVATEAPNLLVVQSGAAEELLTGPGPGEAGDGEASTGVVQDVLFETLQTDEGLQSVLVLSGADGEQTRLCVQEVETLPPGLTEPPATGPPGQKLLIIRSAPATELLDSSNTGGGTATLQLLAPPPSGPASGPAGLPGAPASQMVQVVPAGAGPGVMTPQGLPSIQIVQTLPAVQLVHTF
The following text describes a protein:
Function:
Probably involved in the organization of the actin cytoskeleton.
Subcellular Localization:
Endomembrane system; Peripheral membrane protein. Cytoplasm, cytoskeleton.
Sequence:
MSTKVPIYLKRGSRKGKKEKLRDLLSSDMISPPLGDFRHTIHIGSGGGSDMFGDISFLQGKFHLLPGTAVEGPEEDGTFDLPFQFTRTATLYGQELPDGPSPLLKNAISLPVIGGPQALTLPTTQAPPKPPRLHLETPQSSPQPSPQEAGSVDIWRIPEAGSAHNGLTPESGAEEPFLSHASSLLSLHVDLGPSILDDVLQIMDQDLGHMQIPT
The following text describes a protein:
Function:
Transcription factor that binds to the DNA sequence 5'-AACAAT-3'. Acts as a transcriptional activator (By similarity). Plays a role together with nlk in neural induction during early embryogenesis.
Subcellular Localization:
Nucleus.
Sequence:
MVQRADMDSSQHTEPDTEEGEFMACSPAALDESDPDWCKTATGHIKRPMNAFMVWSKIERRKIMEQSPDMHNAEISKRLGKRWKMLNDSEKIPFIREAERLRLKHMADYPDYKYRPRKKPKVDPTASKSPTLAQSPEKSPKSRSAGKKCPKLKPSHSGNSSKSLSIKSEYGVGGDYVFGSPKSSGKAAVMKCVFMDEDDEEEEEDEEEEEDELQIRIKQEEDDESLRLYNVAKVPASPTLSSSSAESVEGASMYEDIRNGTRLYYNFKNITKQSTIPQATITLAPRPLLATTSPAGSHELLFDLSLNFTQQNPQLPDPNSGNVSLSLVDKDLDSCSEGSLGSHFDFPDYCTPELSEMIAGDWLEANFSDLVFTY
The following text describes a protein:
Function:
Essential for the control of the cell cycle at the G2/M (mitosis) transition.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Sequence:
MALRVTRNTKINTENKAKVSMAGAKRVPVAVAASKPLLRSRTALGDIGNKVSEQSRIPLKKETKKLGSGTVTVKALPKPVDKVPVCEPEVELDEPEPEPVMEVKHSPEPILVDTPSPSPMETSGCAPAEEYLCQAFSDVILAVSDVDADDGGDPNLCSEYVKDIYAYLRQLEEEQSVRPKYLLGREVTGNMRAILIDWLIQVQMKFRLLQETMYMTVSIIDRFMQDSCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTNNTYTKHQIRQMEMKILRVLNFSLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELSMLDYDMVHFAPSQIAAGAFCLALKILDNGEWTPTLQHYLSHTEESLLPVMQHLAKNIVMVNRGLTKHMTIKNKYATSKHAKISTLAQLNCTLVQNLSKAVTKA
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 Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Subcellular Localization:
Cytoplasm.
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:
MQTHEIRKRFLDHFVKAGHTEVPSASVILDDPNLLFVNAGMVQFVPFFLGQRTPPYPTATSIQKCIRTPDIDEVGITTRHNTFFQMAGNFSFGDYFKRGAIELAWALLTNSLAAGGYGLDPERIWTTVYFDDDEAVRLWQEVAGLPAERIQRRGMADNYWSMGIPGPCGPSSEIYYDRGPEFGPAGGPIVSEDRYLEVWNLVFMQNERGEGTTKEDYQILGPLPRKNIDTGMGVERIALVLQDVHNVYETDLLRPVIDTVARVAARAYDVGNHEDDVRYRIIADHSRTAAILIGDGVSPGNDGRGYVLRRLLRRVIRSAKLLGIDAAIVGDLMATVRNAMGPSYPELVADFERISRIAVAEETAFNRTLASGSRLFEEVASSTKKSGATVLSGSDAFTLHDTYGFPIELTLEMAAETGLQVDEIGFRELMAEQRRRAKADAAARKHAHADLSAYRELVDAGATEFTGFDELRSQARILGIFVDGKRVPVVAHGVAGGAGEGQRVELVLDRTPLYAESGGQIADEGTISGTGSSEAARAAVTDVQKIAKTLWVHRVNVESGEFVEGDTVIAAVDPGWRRGATQGHSGTHMVHAALRQVLGPNAVQAGSLNRPGYLRFDFNWQGPLTDDQRTQVEEVTNEAVQADFEVRTFTEQLDKAKAMGAIALFGESYPDEVRVVEMGGPFSLELCGGTHVSNTAQIGPVTILGESSIGSGVRRVEAYVGLDSFRHLAKERALMAGLASSLKVPSEEVPARVANLVERLRAAEKELERVRMASARAAATNAAAGAQRIGNVRLVAQRMSGGMTAADLRSLIGDIRGKLGSEPAVVALIAEGESQTVPYAVAANPAAQDLGIRANDLVKQLAVAVEGRGGGKADLAQGSGKNPTGIDAALDAVRSEIAVIARVG
The following text describes a protein:
Function:
Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates.
Subcellular Localization:
Secreted, extracellular space. Lysosome. Melanosome. Note=While its intracellular location is primarily the lysosome, most of the enzyme activity is secreted. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Sequence:
MASPGCLLCVLGLLLCGAASLELSRPHGDTAKKPIIGILMQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLISGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPIYTGNISSFQQCYIFD
The following text describes a protein:
Function:
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Subcellular Localization:
Cytoplasm.
Sequence:
MKLAELKDHMQKSVEATQRSFNTIRTGRANASLLDRITVEYYGAETPLKSLATIGTPDASTIVIQPFDMGSIGTIEKAISLSDLGLTPNNDGKVIRLNIPPLTAERRKELVKVAGKLAEEGKVAIRNIRRDAVDEVRKQEKNSDISEDEARDLQEEIQKLTDQSTKRIDELLAAKEKDITTV
The following text describes a protein:
Function:
Centriole-enriched microtubule-binding protein involved in centriole biogenesis. In collaboration with CEP295 and POC1B, is required for the centriole-to-centrosome conversion by ensuring the formation of bona fide centriole wall. Functions as a linker component that maintains centrosome cohesion. Associates with CROCC and regulates its stability and localization to the centrosome.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, spindle pole. Midbody.
Sequence:
MATGDLKGNLRKIEQGLRHLNYPNDVDYTGLAKGDPSVFLPIISYCFTSFSTRITELLVESGVELTAKNDFRFIEAVYKLLRDEFQYKPILSKQQFLHYGFAERKIQIVCDIISLVYKRHKELSNMKSQAKKRASSIKPQQYANFSNQLEFTTVYATDFQQGVSLTKEPEERSRNLISTCIFEDGFREVLEEGKTEAVCMGNGLDPVADMLDSVYEQDAPLTKNPEIECSSSLTCACIRGDNVREVSEEGGNKAVCVAYSLNSGADRLGKECEQNMKDNSNMEKLKSQIVELEEKLNKLKWVEDKLQALEEKLQGRIIVDEKDWNNLLSRVLLLETQLLLHCKKVDLSRDLNNTDEKDISANNVTSVSPDRKKEDLPDSLHQSSGYSSQLSAEPSPKATVINNHGLLESSKDTTIQRMERISKMIEETSELLKTSSNTS
The following text describes a protein:
Function:
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Miscellaneous:
MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Subcellular Localization:
Cytoplasm.
Sequence:
MGLELGFRELGEVPYEPTWHAMQRFVAERDKSVMDEAWLLQHPAVFTQGQAGKAEHVLFPGDIPVIQVDRGGQVTYHGPGQLVTYLLLDVRRLGLGVRELVSRIEQSLIGLLASYDVQAVAKPDAPGVYVDGAKIASLGLRIRNGCSFHGLALNLDMDLRPFQRINPCGYAGMPMTQLRDLVGPVDFAEVCTRLRAELVSRLGYAEQKTLTGGIELT