lhallee/plat_data huggingface dataset:
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 pre-initiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MNSMTTLKMKLKELEDIEKDVATALQSAGQVCLELSKDKPNAKQVDSNATAFVKTLQNVENSLTKHILYLTQVSTVQPHEGSSYAAQKVFHMALHRLEHARSRMNELERLRHQQQQEQQQQQQQQQQQQQQQQQLQQQQLQQQQQQQQQQASHQDS
The following text describes a protein:
Function:
Co-chaperone that regulates diverse cellular pathways, such as programmed cell death and stress responses.
Sequence:
MMRMKTKTTAMPPMMNDNSAGGRDRAAADNEWEVRPGGMLVQKRNPDAENRPPPPPIRVRVKYGSIYHEINISPQATFGELKKMLTGPTGLHHQDQKLLYKDKERDNNAFLDISGVKDKSKIVVVEDPLCQEKRYLELRKNAKMEKAAKTIADISFEVDRLAGQVSAFESIISKGAKVVEKDLVKVIELLMNQLLKLDGIVAEGDVKLQRKMQVKRVQKYVETLDVLKMKNSAPSRSGNHIPKQESSPSPQQHQRRYSNDQASSPVQNQNGSRRSFANSPTPAKHQEPSRHSASGSVVITTQWETFDPAPGPLLDHDSTTTPSNNNNHASYAQPRFNWDLL
The following text describes a protein:
Function:
Transcription activator involved in multidrug resistance, oxidative stress response, and redox homeostasis. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Involved in the oxidative stress response in via multiple pathways, including the cellular antioxidant defense system, carbohydrate metabolism and energy metabolism, protein degradation, ATP-dependent RNA helicase, and resistance pathways. The ability of the major systemic fungal pathogen of humans to sense and respond to reactive oxygen species, such as H(2)O(2) generated by the host immune system, is required for survival in the host and therefore virulence. Regulates the transcription of COR33, GLR1, GTO1, GTT1, GTT1, TRR1, TRX1, SOD1, CAT1, and the transcription regulator TSA1. Participates in the apoptosis by regulating the expression of the glutathione reductase gene and glutathione content. Also plays a role in the peroxide-mediated induction of MDR1 and other drug response genes such as PDR16, MDR1, FLU1, YCF1, and FCR1. Regulates trehalose accumulation which is important for the oxidative stress tolerance. Recruits ADA2 to its target promoters. Activity of CAP1 is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress induces nuclear accumulation and as a result CAP1 transcriptional activity. Nuclear export is restored when disulfide bonds are reduced by thioredoxin, whose expression is controlled by CAP1, providing a mechanism for negative autoregulation.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Oxidized CAP1 is found predominantly in the nucleus, while reduced CAP1 is continuously exported to the cytoplasm. Caspofungin treatment also induces nuclear translocation.
Domain:
Contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD (Cys-254 and Cys-261) and c-CRD (Cys-446, Cys-468 and Cys-477), respectively. A nuclear export signal is embedded in the c-CRD, with which the nuclear export protein CRM1/exportin 1 interacts only in the absence of disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or between the c-CRD and the n-CRD.
Sequence:
MTDIKRNFSDIASPANLDDTKKLHVDSTATTKVGRKPIDTEPKSKRTAQNRAAQRAYRERKERKMKELEDKVRLLEDANVRALTETDFLRAQVDVLKNELAKYTGGSDFSDLNLPTKVGHLSHPNNHHSNVSTGTPHGSMSSSNSVASLDNDKPSSASSVSNNSPGFAFDNPWSKDNIQKLKHQHQQQQQKVPQGVPDLVSGSSSSSTPLNDNLLVTPESLTGLSTSSKYTGQNNVPTNLDFTNQFDEQVDPFCVKLNEACGTKSNPVPKFKRSGSKANTSVTNNSPLAHLVSPESQQYTNSSNIDFMNDPFFNGVGTDYNFNFDSKNGSIQDPLSFLQDDNFDLALAFGDPSPTGNEAEADPISLLTTEESIYDPLTNNSDKLCSTVKADDVNTDFNFNDFVKNSLPEKQEKGKYEPPSTSKTTNNNEEEDKDEVVPAPPQTLKCSEIWDRITSHPKYTELDIDGLCNELKSKAKCSEKGVVINTADVNQLLERSIKH
The following text describes a protein:
Function:
Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity).
Miscellaneous:
MISCELLANEOUS: Present with 2030 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSDRFVIWAPSMHNEPAAKCGYCHGNKGGNMDQLFALDSWAHRYMNKMDVVKIENCTIGSFVEHMDVATYDRMCNMGFRRSGKFLYKVDPLRNCCRLYTIRTAPQELNMTKELKKCISRFATRITSEDYCPAAVASSDFVGKIVNAEMNSKTFYTRFEPALYSEEKYHLFVKYQEKVHQDYNNSPKSFKRFLCDTPFGPEAVLGTQESWEQLNNWQRMKPGEKLKHMGPVHECYYYEGKLIAITVSDILPSGISSVYFIWDPDYSKWSLGKLSALRDLAIIQRTNLQYYYLGYYIEDCPKMNYKANYGAEVLDVCHSKYIPLKPIQDMISRGKLFVIGEEETKVTKELYLVDSETGRGEGFPTDNVVKYKNIAEEIYGVGGCAFKSANESALELKELYGIPYEEEDLDTIYHLKEHNGHAPNGIPNVVPGLLPLWELLDIMQSGKITDLEGRLFLFEIETEGIRPLINFYSEPPNVKKRICDVIRLFGFETCMKAVILYSEQM
The following text describes a protein:
Function:
Polycomb group (PcG) protein. Catalytic subunit of some PcG multiprotein complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. Required to prevent the proliferation of the central cell of the female gametophyte by repressing target genes before fertilization. After fertilization, it probably also regulates the embryo and endosperm proliferation and anteroposterior organization during seed development. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Interacts with the promoter and repress the transcription of genes such as PHE1 and PHE2, that are paternally active and maternally silenced genes.
Miscellaneous:
MISCELLANEOUS: The MEA locus is imprinted. Maternal inherited gene is expressed in the ovule (the egg and the central cell), while the paternal inherited gene is silenced in the pollen. After fertilization, only the maternal inherited allele is expressed. The paternal repression is dependent on DDM1 protein, which may methylate the paternal locus, while the maternal inherited allele is allowed by the DME protein, which may antagonize or suppress DDM1 dependent methylation, and activates its transcription.
Subcellular Localization:
Nucleus. Note=Excluded from the nucleolus.
Sequence:
MEKENHEDDGEGLPPELNQIKEQIEKERFLHIKRKFELRYIPSVATHASHHQSFDLNQPAAEDDNGGDNKSLLSRMQNPLRHFSASSDYNSYEDQGYVLDEDQDYALEEDVPLFLDEDVPLLPSVKLPIVEKLPRSITWVFTKSSQLMAESDSVIGKRQIYYLNGEALELSSEEDEEDEEEDEEEIKKEKCEFSEDVDRFIWTVGQDYGLDDLVVRRALAKYLEVDVSDILERYNELKLKNDGTAGEASDLTSKTITTAFQDFADRRHCRRCMIFDCHMHEKYEPESRSSEDKSSLFEDEDRQPCSEHCYLKVRSVTEADHVMDNDNSISNKIVVSDPNNTMWTPVEKDLYLKGIEIFGRNSCDVALNILRGLKTCLEIYNYMREQDQCTMSLDLNKTTQRHNQVTKKVSRKSSRSVRKKSRLRKYARYPPALKKTTSGEAKFYKHYTPCTCKSKCGQQCPCLTHENCCEKYCGCSKDCNNRFGGCNCAIGQCTNRQCPCFAANRECDPDLCRSCPLSCGDGTLGETPVQIQCKNMQFLLQTNKKILIGKSDVHGWGAFTWDSLKKNEYLGEYTGELITHDEANERGRIEDRIGSSYLFTLNDQLEIDARRKGNEFKFLNHSARPNCYAKLMIVRGDQRIGLFAERAIEEGEELFFDYCYGPEHADWSRGREPRKTGASKRSKEARPAR
The following text describes a protein:
Function:
Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites. Decreases the levels of the pro-proliferative prostaglandins such as prostaglandin E2 (whose activity is increased in cancer because of an increase in the expression of cyclooxygenase 2) and generates oxo-fatty acid products that can profoundly influence cell function by abrogating pro-inflammatory cytokine expression. Converts resolvins E1, D1 and D2 to their oxo products, which represents a mode of resolvin inactivation. Resolvin E1 plays important roles during the resolution phase of acute inflammation, while resolvins D1 and D2 have a unique role in obesity-induced adipose inflammation.
Sequence:
LLDCFSKTKSKFGGLDIVVNNAGVAGEARWKKIFAINTAVFCGTLLGFKYMGKDNGHKGGHIINVASVAGAYEINVASSHTMAEKLNDISLTAGGTDLHFNRHGVKVNCICPEPMDTPLWWGVSEFCKTKDDTTSFAQDYDKRVQRIEDVAKGVVKIIEDGQNGSALVALHGQDFKYYNFQE
The following text describes a protein:
Function:
Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis. Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (By similarity). Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (By similarity). Binds to 3'-UTR ARE of numerous mRNAs. Also induces the degradation of ARE-containing mRNAs even in absence of poly(A) tail. Required for tubulogenesis during pronephros development (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner.
Sequence:
MSATLLSAFYDIDLLYKNEKALNNLALSTMLDKKAVGSPVSSTNSNLFPGFLRRHSASNLQALSGSTNPAKFCHNNNNNQLNESAASSTALLNRENKFRDRSFSENGERSQHLLHLQQQQQKAGAQVNSTRYKTELCRPFEESGACKYGEKCQFAHGFHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRQAPGAGERPKLHHSLSFSGFPNHSLDSAPLLESPTSRTPPPQSSGSLYCQELLQLNNNNPCANNAFTFSGQELGLITPLAIHTQNSSYFRQPSSSPPLSFQPLRKVSESPVFDAPPSPPDSLSDRDSYLSGSLSSGSLSGSDSPTLDSNRRLPIFSRLSISDD
The following text describes a protein:
Function:
Odorant receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MFLHCGERPAPDEGFGASLSEHSPEGCVSQDGCRLFSWGCIRVPRAVVQSRVPAVPQGLCAGAGTLPPARLSTQLYRMDSMPRNRRCPTAAPSASSSSWRWQTRGSCSSCTSGSSVACDHRLHTPMYFFLLNLALLDLGCISTTLPKAMANALWHTRAISYTGCAAQVFFFLFLFGAEYSLLIVMSYDRYVAICKPLHYGTLMDSRACATMAAAAWGTGLLYSLMHTATIFSLPLCQGNAVDQFFCEIPHILKLSCSDAYLREIWVLGVSACLASGCFAFILFSCVQIFRAVLRMPSEQGRHKAFSTCLPHLAVVSLFLNTAIFANLRPLSLSSQSLNLAMAVLYSVVPPTLNPLIYSMRNQELKDAVRKVISWTHFSRDKLLICLCK
The following text describes a protein:
Function:
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MDPVDIIQKREDENGIRLSFNLWPTNRIDAVSASCPIGALYTPLKKLTPIGKIQRTPLEYEPVLCPNCRGALNCYAQIDFNSKTWVCPLCKTRCPLPSQYSNITKELLPLELHSEVNTVEYLVNQGTVKPPIFVFVVDICSNEKELENLKSVLLQAIAILPENSLVGFITFGSSVKIHELVEIPYPRSYIFSGNKTYNAQELATMLGIQRLANGEVQTTIIVPAKQAEDMLNNLVDRLEVDKLPIPKDERMQRCTGAALSIAVTLLEAVCPLIGGQIFLFTSGPITKGPGTMATLKRGEPVRQHSDIEKGKADLTRASQQFFSEIGKNASTKNIVINYLSACFEEAGLYELEPAILITGGWLISAESWGDVNISQSIVKYFTSILENAGAEVQTQIICSNNFKISGCIGPCSPKETPGPAVSEKQIGIGGTTSWSLGGALPSTTLAFYFDITASKADPVPVGTTAFIQFVTTYRNVLSGQYVRRVTTTAVNFGDMNDRSSFARSFDQECGTILLAKLAMWKCRTEDNLDVIHFIDKTLIRFCRWFGTYNQGDPSSFTFGESFTFFPQFLYHLRRSPFMSTFNSSPDLTASLRHSLLMEDTTNSLFMIQPTLMQYTADFQQSPVFLDMNSLKKDTILLLDTFFRVLVWYGENVASWRNQGLDKNPDYENVKWMLETPLQEAKALISERFPTPLLITCDQDSSLSRYLLARCNPSENNYNGLGGSTNSLSTEEPSLSKFLQKLKDVAVND
The following text describes a protein:
Function:
Central component in molecular interactions underlying sperm crawling. Forms an extensive filament system that extends from sperm villipoda, along the leading edge of the pseudopod.
Sequence:
MSANTPKPKKNVSSEPRTAHQKKRRSREEEKSTPCYISNDGYLWTDINPDLALIEPRILVSVNFNYLAFSRKQERPSESRSLALINHGDYPVAFKIETTDNYSYFVDRRNGIIPPRQTVVNAAVRMPNIVTIEVYHRPHNEYLEEDKQHFYNRPRKDKLFILLAPQMCQTFAPEAIFHNERSYEKLRVMLMYSGVEEKPGEKLLLGGVVGWCTWKEDNGARKEKNDRQIAEFRKIEKTIIQNASKEQCEDNPRMTSIHRKSPAIFRSKTPVLAGPAGQRRPGMSKQFRSPKKLSNEGAATPVARTAASPFKTSLENQKTPANQKKMSGETERKSQEAPVPAASPNHKESLENWATSSKPDANSQ
The following text describes a protein:
Function:
Promotes cell proliferation.
Subcellular Localization:
Cytoplasm. Membrane.
Sequence:
MPEFISVDEFIAETLEDYSSPTTSAFTTKMSSCRNAVNSIEEALDSDRTVLQKMKKGAKAKHASGQDHILHLESYINSMEKLAVNFRNNGEQELASAFNKFAEYSKELLTPMKNALQSMYHNINFSLESLVKGDLKEVKGDLKKPFDRAWKDYENKFTKIEKEKRELAKQYGMVRTEVSGGEIAEELEKERRMFQLQMCEYLIKVNEIKTKKGFDLLQNLIKHYHSQCNFFQECLAATEKLKQYIEALTTGLNSIKHRQDEEKRQLCSLRDQLRLSLQPEQKEDSLSRQAVYSMHQLQGNKQYGTEKTGCLYKKSDGLRKVWQKRKCAVQNCYLTIAHGTPNRPPAKLNLLTCQVKPSQEDKKCFDLISHNRTYHFLADDEAECVAWISVLTNSKQEALNVALDERRPSGENSIEDLTKSIIEDVRRMPGNNVCCDCRAPDPTWLSTNLGILACIECSGIHREMGVHYSRIQSLSLDKLGTSELLLAKNVGNAGFNEIVEANLPSSSLKPSADSDMAVRKDFILSKYMERQFAQHSGGSPGTLRRSLQEAVRSRDIFALLRLYGERLDLSQPLHSPVQEPGEAALHLAVLLADRTSLHMVDFLVHNCNNLDKQTVRGNTALHYCCLHNKTECLKLLLRAKANTHIKNEAGETGLDIARRLKHSHCEELVRQTSFQQIGIGQLCAELNWKRHLAKAHRAAVPCPAQLGPVKKERSCRPFSLYQASSPAGPDRGGHASVGRRLASLVRDPRRETYASPSTQTRSLDPPPPPPSSPAPPLPPRIRAPNVPPPPPPPASPPDARCDSVPGRRKRTALPSLAACEWVFFEPAPVVLPSPSAFRFSFPDYGFPGNSRGYSGPEGVYQKSALGSPKYTVTTLNALPELPEKGTGRADGEGSSPQCIYATPQPSGRARLPSSPPFRADGPEPNGASPALLGPPAPHPLPRKALAKPRVRRVKAIYDCVADHHDELTFSEGEVLVVMAEEDADWWLGYIEGHPHKRGLFPASFVHILSE
The following text describes a protein:
Function:
Probable lipid transfer protein.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MSKIISLVVAMIAVLALPIRGQQQPLSQCTPSMMTTVSPCMGFITNSSSNGTSPSSDCCNSLRSLTTGGMGCLCLIVTGTVPFNIPINRTTAVSLPRACNMPRVPLQCQANIAPAAAPGPAATFGPSMSPGPETDPIVPEPTPAAQTPQSDTTRPFTPSVDGGAPTSDDGGSTSRPSETPSSAYALSPSLLFFSIALVALKFY
The following text describes a protein:
Function:
mRNA splicing factor that regulates the formation of epithelial cell-specific isoforms. Specifically regulates the expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2. Also regulates the splicing of CD44, CTNND1, ENAH, 3 transcripts that undergo changes in splicing during the epithelial-to-mesenchymal transition (EMT). Acts by directly binding specific sequences in mRNAs. Binds the GU-rich sequence motifs in the ISE/ISS-3, a cis-element regulatory region present in the mRNA of FGFR2. Regulates splicing and expression of genes involved in inner ear development, auditory hair cell differentiation, and cell fate specification in the cochlear epithelium.
Subcellular Localization:
Nucleus.
Sequence:
MTASPDYLVVLFGITAGATGAKLGSDEKELILLFWKVVDLANKKVGQLHEVLVRPDQLELTEDCKEETKIDVESLSSASQLDQALRQFNQSVSNELNIGVGTSFCLCTDGQLHVRQILHPEASKKNVLLPECFYSFFDLRKEFKKCCPGSPDIDKLDVATMTEYLNFEKSSSVSRYGASQVEDMGNIILAMISEPYNHRFSDPERVNYKFESGTCSKMELIDDNTVVRARGLPWQSSDQDIARFFKGLNIAKGGAALCLNAQGRRNGEALVRFVSEEHRDLALQRHKHHMGTRYIEVYKATGEDFLKIAGGTSNEVAQFLSKENQVIVRMRGLPFTATAEEVVAFFGQHCPITGGKEGILFVTYPDGRPTGDAFVLFACEEYAQNALRKHKDLLGKRYIELFRSTAAEVQQVLNRFSSAPLIPLPTPPIIPVLPQQFVPPTNVRDCIRLRGLPYAATIEDILDFLGEFATDIRTHGVHMVLNHQGRPSGDAFIQMKSADRAFMAAQKCHKKNMKDRYVEVFQCSAEEMNFVLMGGTLNRNGLSPPPCKLPCLSPPSYTFPAPAAVIPTEAAIYQPSVILNPRALQPSTAYYPAGTQLFMNYTAYYPSPPGSPNSLGYFPTAANLSGVPPQPGTVVRMQGLAYNTGVKEILNFFQGYQYATEDGLIHTNDQARTLPKEWVCI
The following text describes a protein:
Function:
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Localization:
Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MDNPLTSAEVFQLNSVSGGLRPGTISFKTLTLQSDKYVCIRDVQPDGQTSLVIVDLGKRESMRNSIRDAESAIMNPMAKILALRSGRNLQIFDVDAANRLKVVVFNEDVVYWCWIDARTVGIVSNTAVYHWSLDTAADAPPQLVFSRAPEFDASFQVLSYQTDEQKKWLMLCGVMRTAEGMVGKTQLFSVENNSGRVLDGHSGTFISTNTPTDPRSCNLMCLAWNNPSTGGKILIMELPTGSKTDLTVQRRMIDVPFAQGDFPVATHVSPRHKLLTVVTSRGSVVLMDLFTGVVIKTHQLPNNTIFCGTPYTKTGGILCVNNAGSVFHVSPNDNTIVPFVKNQLQNADLALRIAGSANLGGVDDLYRVQLDNQLRAGNIEEAVRTCLRAPNNALRGPDILSRFQLMPPIPGQQPAISTYFKVAVAETTLNAHESAELARAVIPKGGVDYVKQQYAADKLTASEELGDLMSAADPELAIKIYHKAEAHAKVVGVLLQRNETQKAVEYCKRAGFTPNWRVILNNAIHVNPQGAVGLAQVLHRDMGDAPVVDPIEVVDMFVTAQHIQQATEFVLEVLRDNTGENTKDLQTKLLEINLKHSHPSVAEKIFARGVCVHFDAMLLAPLCERASLPQRAIECYVMAQRMDPGIDNLANIRRCFSNAQVLSPDWVIEFFGKLSPGDSMKCLEDLLANHHQNFKIIVQVATKYNEALGADKLINVFLERKLFDILYYYLGAVVPYTRDPEVHFRYIEAAAEVGQVQELERMTRESPCYDPERTKNYLKNKKMTNLWPLINVCDQHNFVDELIRYLIDTNNEALIEQYVQRRNPLKTPAVVGALIDCNVQEDFIKNILNSVGTMCPIAELVDVAEERSRLRLIGPWLEARLAEKKTDTALHNAIAKLLVISGNLPEKFIEENDYYDPVVMGKYCEDRDPNLSYLVYRKAKMSTELVEITSKNGMWKQLARYLVKQQDPALWASVLTESSINRDRLVEAVQQTALPESEVTEEVSTTVKAFMDAELTEELTSILDQIVVRGRFRKNRYLENLLIMSAVRASKAKVMEYVTTLDSYDAKEIAGIATAAELHEEAMTVYDKFEMRMEAATVLLRDLKDLPRGRLYAQRCNLPAVWTVLGEYLLAAGEVREAIEVLIRAKNPNYVDAVTAAAERSNQFGDLVKYLNMARQESTSNDNKIESVLLLTYARTGRLSELEELLQNTHNVQIQPVADKCFEDGYYDSARLLYSMSMNFHKLALTLVRMNNLAEAVDAAQKAQSRSTWDAVNHACIEANDVRLAAICAVPLVLQVESLQDVVNRYEAYGLYDELFAVLKSASTNSGAHMGIFTEMGLQLAKYKPEKLLEHVHMYSKKINAHKLISVCEEYHHWLALRVLHVGNEDWLAAAKTMMCHFADAFDHDVFKDVASHLGASDFVYNAISFYVNTCPQNLCDFLTSMFKVLDPDRVLREVKNVAPIHLILPYLESAQPRNSRLINDALNDLYVEEENFVALRNSVENYNNFDSVELSARLEKMELFEFRKIALFLHRRHKAFDHALAVAKENKLFQEAIDTAVESADPKVVEELLDFFAVERPDSFVSCLYACYDYLSPDVVLEKAWLNNRINIAMPYLIQAIHDFTQRVSRLEKGANDGMQPSKDGSRRGGVPGYAGGNDPLMIQAGPAQPMGVPMHNVNIHPQPGYGGVPGQGYAGGMGNPNMMPY
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC).
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane.
Sequence:
MSGGVGSPPARDTLQSHDSSPQDTPDSGGRQQFRRYRKRRSSIGLFSGADEVKGPLPFGGGFGSPTGERYASPQSLPDASPWERWDSGGEDLKTPIPRKLFGTGEGREVGDLTEGLNVPISHARTPTTREQQRRVTLTATPISSPIILKTVKKEDQLEVTDSAEESFARFAGILDATFQGHFSFPELMLQYEAVCRDLVDLVREEASETHRVTEDRLMRQKALMLHGEAASWSLLWYLFGKSSEEMYLDDDDDTPVTSEEEACEFIASDQNAQLCSRIVQWLETLASKELDYEKKHKGWYAGSYAQKLGVWRHTQSAIRKKTGGIVQHLDPDAPSREQAQLHSEDQKLEESLLEDVWKLLLAGRLEEAQDLCRSAGQAWRAASLGGCGELGPSPTVEAWKRKSRDWSPNAYGRGRDRSLKAVELESGSGHQRRLWKWACFAASNNIGDGPHESKYEAAIFASQCGNVKRMLPVCFTWEAACWAMVRSWLDVEVDLQLSSASILKSPQEINDESTGGPELWPQPVVYQQPRDLHSLFQKLLTGDLVNEAVRRSCKEQQRLVQMDLMLGDITHLLELLRTWIAPSQDTRDSSRPHGHPQMIRFGAHLVLVLRYILNDEMKEQFKEKLWLIGDLILNTYAIFLFTQRKEELVGVYASQLAPHLCVELYVQMIELRENESVPVKYKIFKSAIEYLPFISEDGTKGSFSDIISRVLSKSRDIKSDSRPLAKVEISGQRLQTVRKAHAVQWLCFLPPPSLSSVEVLRAELLARALEYSNVLFREYSLSCLWRTPEMPVGAHVLLGHLAEPLNQPTDALLSLDQLRVQENLQEFEEWREYYACDALYRNWLKIEQGNSVVPSDELSSDEKERAATAAQQALDAASSLLQRNHGMWLAGVDDVAEDDLAPDWIELQCTGMLSSSSGSSLVPDASVCTALVDALYNCGAIQGVQRQLTVDVTVNGKDHSLVDILLRCLPVKGDGLGSNTDYDGGLLASIIAYAVKGELPHFRAGIVLEVLRLDAWYISGDGIQQVQAGYIVQGLCRRCCLPELILRSMQVKAALAAASVEVDDEDCDVLELVASKEYELYQLFSQRQLQELLQFERRARIYSLEVLEASGFFSDTSVPLQNMQET
The following text describes a protein:
Function:
Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors. The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes. Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene. The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Sequence:
MNTLNAPRNPTRHPAMTADTLVDAPALPHQNGSTEEKLKERGSFGKLYTYKRSPRALGIQAVAKSIGLELEQVELQPANGVPDFYWNLNPLGKTPTFVGADGLVLTECMAIALHVTNEDSTTTLLGSSSLDFVQIIRWISFTNTDVVTRMASWVRPLIGYTPYSKEEVLKAQQQTTQAIGVFEDSLRDRKYLVGDRLTLADIMCVSLVSFGFAQIFDKEWREAFPYFSGWYMMVMHLPIMKAVVEEVPFVEEGLPNAPPTEPFRAP
The following text describes a protein:
Function:
Regulates asymmetric cell division (ACD), especially in stomatal-lineage cells, probably by modulating accumulation and subcellular polarization of POLAR and SPCH. Mediates an attenuation of MAPK signaling upon polarization of POLAR and ASK7/BIN2 in stomatal lineage ground cells (SLGCs) undergoing ACD, and relieves BIN2 inhibition of SPCH in the nucleus. When phosphorylated, functions as a scaffold and recruits the MAPKKK YODA, MPK3 and MPK6 to spatially reorganize the MAPK signaling pathway at the cortex of cells undergoing ACD. Cortical polarization leads to elevated nuclear MPK6 signaling and lowered SPCH abundance in one of the two daughter cells, thus differentiating the two daughter cells after ACD.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, cell cortex. Cell membrane; Peripheral membrane protein. Note=Dynamic and highly polarized subcellular localization at the cortical polarity in a phosphorylation status-dependent manner. Polarity is only exhibited by one daughter cell after an asymmetric cell division. ASK7/BIN2-mediated nuclear exclusion. First localized to the nucleus in asymmetric cell division (ACD) precursors. In asymmetrically dividing stomatal-lineage cells, before division, accumulates in a polarized crescent at the cell periphery (e.g. meristemoid mother cells (MMCs)), and, after division, localizes differentially to the nucleus (e.g. in meristemoids) and a peripheral crescent in self-renewing cells and their sisters (e.g. stomatal lineage ground cell (SLGC)). Localized in the cell periphery at a position that minimizes the inverse distance from all points along the new division boundaries.
Sequence:
MASQWTIPKLVTWRVRDWASCFLACKIPLDGDEDGANNNGNTTNNNNLTFKRIKRKIKSTKKKRSERKLSLSPPGTRHHHLHLRSSSVSPTTSGSQHRRLSWPQPPVSEESGFIVFCFDREDGGFDVVKEGKQEKKETESSSEKSPRTVNRKLIYGDQGVGGTEKNNSPETKGTEQDQNDNTSCQGTKDVSSDVTERTKEEEDIDASDKSSGSSHSDEGRGSFAFPILGVEWMGSPAKMPESDDLSPKKQKPVALGFQCCRF
The following text describes a protein:
Function:
Required for microtubule stability. Interacts with CIN4.
Miscellaneous:
MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
Sequence:
MNNIRALLDSIQSGVQTVSPEKHQQTIAAINKFQDDPALLDTILPRCVPLLTKSFFCMSQRDQKLVAELFYNLDKISHSKVLKSLDTSIFRLNEILNYLQDRASPSSFSDVLCVYLNLSWLSVILLSPYAFKDKFNKTLQVSSRFENYPICIPPINKIKAVLYFKNFTDAFDQLPEREQANVPFLNQFLKLFIQSSEKANYYFSNENLRHLQQVALSNDGIKLLPKLFQISFNHGSHDILDAIVEFFHDHLSSNSTDTRFQLAHSFAKIAKFLHQADPASFIELIDYTIENTVSLLQAPCDSIDSNELHTSLLIIAEVALAKILPIDLVDRVLTLIIPKTCHFQKSHFQIIKGHHIRDSTNFIIWSVIRSNRSNSLSPQVLQSLLSHLLINAFFDPELIIRYSSFAALQELLGRSNKSLALNQNDIALILQANWKDLPRSFEENSGLIRRLFNPENTSKSAVCVWKVFRDWSFNWNLLENLHLTTMKLNIDYNLVPLIKSKLSSPALLQEVLNKAGSSVTQNCQILYLYLKLFENDVNCPKISEICIDIYQKKIKFQLTTQAKRQFNDNSPELFQIFVILKYWQLTGQNDFNQELFWKFVDIVSPQKKLNLYNEFIPIIQQIISQCVSLNYTRIVQLIKSDNELTCRSICHMPDQEKMCSLFFSQFPLLSPQSRSLLIGELDHHWDVRISLLPSNSYRKFRNIIINCLDDYTITQQGDVGRLVRIQALKLMQSHPDFLSGDCDSINPKLTRLLAEPVPEIRKLSYQLLASATSQITVLSDSSILNFRHKQGLSEEFWKGYAVSAGAIHFTDSQLTSSIDSFIVYYRSLSPSQQLELCHDLIRIIPSAKQIAESRIRDRNKDPLTGGMRFDTIKFTIHCVKFWTRIMESGLVVLHPNFNFQGVFAKFYNLHLLDCTTLRVSVIKFFPFLAISCYHTMRENADQKNLSNIILKRLLVLVKREYAATKSKFMTDQNVALQGMFQIFLELGVTRQLQALQVACQKHELANILESDITL
The following text describes a protein:
Function:
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Sequence:
MLLEKAYRIKKNADFQRIYKKGHSVANRQFVVYTCNNKEIDHFRLGISVSKKLGNAVLRNKIKRAIRENFKVHKSHILAKDIIVIARQPAKDMTTLQIQNSLEHVLKIAKVFNKKIK