lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation. Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity).
Sequence:
MSHYGGNPRGNSSHQFGRKDFQQSDSKHIPKITGQPLPNEVQIPFDNMIYETRNPPKFEKQAKFISEYCINYDRKLQLGRMRAKKFHDKLPPNNLSLDLGKGFETFDPKEGDEKIIMLLEWINQMAPEGGRLKKVIHEADVVCWRGLITKICSTIYNKEEGWRIDAIKRKGVIFLCEEKTEQAKNRDLNQTDLDKRMSYWGHKFEQYVTLDDDAEQPDTSSPVTTKEEYAVVFRNDLQTDQRLNPEKRSIGIFYSGEVDCLDRHGNMLELKTQKGELGHGFYKYSKSFKWWLQSSLVNVDHIIVGLRTQEGHVKSLTSLRTREIPQRASWNFRAGFEFLSTIFTYILNCLEKDGDACVIEYRSEMGIHKGIQMRRVPVDEFDFVPNEFLEKFC
The following text describes a protein:
Function:
Cell surface receptor for LCN2 (24p3) that plays a key role in iron homeostasis and transport. Able to bind iron-bound LCN2 (holo-24p3), followed by internalization of holo-24p3 and release of iron, thereby increasing intracellular iron concentration and leading to inhibition of apoptosis. Also binds iron-free LCN2 (apo-24p3), followed by internalization of apo-24p3 and its association with an intracellular siderophore, leading to iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration and resulting in apoptosis (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein. Note=Upon LCN2-binding, it is internalized.
Sequence:
MASDPIFTLAPPLHCHYGALPPNASGWEQPPNSSGVSVAGAALAASAASRVVTSTDPSCSGFAPPDFNHCLKDWDYNGLPVLTTNAIGQWDLVCDLGWQVILEQILFILGFASGYLFLGYPADRFGRRGIVLLTLGLVGPCGVGGAAAGSSTGIMTLRFLLGFLLAGVDLGVYLMRLELCDPTQRLRVALAGELVGVGGHFLFLGLALVSKDWRFLQRMITAPCILFLFYGWPGLFLESARWLIVKRQIEEAQSVLRILAERNRPHGQMLGEEAQEALQELENTCPLPTTSTFSFASLLNYRNIWKNLLILGFTNFIAHAIRHCYQPVGGGGSPSDFYLCSLLASGTAALACVFLGVTVDRFGRRGILLLSMTLTGIASLVLLGLWDYLNDAAITTFSVLGLFSSQASAILSTLLAAEVIPTTVRGRGLGLIMALGALGGLSCPAQRLHMGHGAFLQHVVLAACALLCILSIMLLPETKRKLLPEVLRDGELCRRPSLLRQPPPNRCDHVPLLATPNPAL
The following text describes a protein:
Function:
Binds the phosphorylated C-terminal domain (CTD) of the largest subunit of RNA polymerase II and functions as a scaffold for RNA processing machineries. May be involved in pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MLTTCKREDMCSPAILTPVFMCLRRTPGTRFTITDGSDRRLLPELAGFSPHISDRRPLPELTGFSLHISDFHPMPELAGFSHRGRRYRCWNMSNNPPQSSGAQVRKVLEFTLLKFDSKQFDFRAMVPGQQGQQFVPAASQQPFHHPYGHVPPNVQSQFSQQLFPVRPGQPGHIASSSPPVVGFGTSGPPPFSSSYSFTPSSYGQQQPTPQMHASGSVPPAANSWPAPPVIQSTTLVSPVQQTPATPTDPGNLTPQSASDWMEHTSADGRKYYYNKQTKQSSWEKPLELMTPLERADASTVWKEFTTAEGRKYYYNKVTKESKWTIPEDLKLAREQAELASAKRSHSEDESTSLSRITASSSDLAVSTPVTAVVPSTSSTIPGHSTSPIPAGLAVPVTRPPPVASVTPTFAATSDTEATAMYHFVDYKEISVNGKSNMTPAGDKANVEEPMMYATKQEAKAAFKSLLESVNVQSDWTWEQTTKEIVHDKRYGALRTLGERKQAFNEYLGQRKKVEAEERRWRQKKAREEFVKMLEECEELSSSMKWSKALSLFENDERFKAVDRPRDREDLFDNYIVELERKEREKAVAEHRQKMAEYRKFLETCDYIKASTQWRKIQDRLEDDERCSCLEKIDRLIGFEDYINDLEKEEEELKRVEKEHVRRAERKNRDAFRTLLEEHVAAGILTAKTYWLEYCIEVRDLPQYQAVASNLSGSTPKDLFEDITEELDKQYHEDKSRVKDAMKSRKVSMVSSWMFEDFKSALSEDLSSQPVSDINLKLIYNDLVERMKEKEEKEARKFQRLAEEFTNLLRTFKEINAASNWEDVKQLVEESQEYRSIGDDNVSRGLFEEYITSLQEKAKEKERKRDEEKSRKEKDKEEKEKRKDKEKERREKEREREKERSSKREESDGDVDVSEGQKEEKRKGKDRDRKHRRRHHNSDDDVSSDRDDREESKKSSSRKHGNDRKKSRKHANTPESDSESRHKRQKKEQRESSRRGGNDELEDGEVGEDGVVSMISGYTLCKSSGCDKSENEPDAASILEQEGTMIQR
The following text describes a protein:
Function:
Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is still unclear: may act as a protein kinase that mediates phosphorylation of COQ3. According to other reports, acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates. However, the small molecule kinase activity was not confirmed by another publication. Shows an unusual selectivity for binding ADP over ATP.
Subcellular Localization:
Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MSRTGLELLRRTASGVRSAGSPHAGCGSAREQTEPRVHCFHRYSTMSSSPCFPAGSGRSGTGPFLRTWTGELLHGPGRRLNQGGSTVGRLTPEDLEKARKKAEVKKYKQVLSESARERRVPVTRIGRLVNFGGLAFGLGIGAIAEAAKKSFKIKQEGPRQAVLDSNPFLSEANAQRIVRTLCKVRGAALKLGQMLSIQDEAFINPQLAKIFDRVRQSADFMPTKQMMKVISGDLGPNWREELEFFEERPFAAASIGQVHLGRLKDGREVAMKIQYPGIAKSIESDVRNIMTALSLSHALPEGLFPEHLVGVMSRELALECDYLREAQCARNFKQLLKDHPFFCVPDVIEELSGRHVLTTTLVPGFPLDKATDLSQGLRNEICEQILVLCLRELFEFRYMQTDPNWSNFFFDPQTHRVALLDFGATRGFDQSFTDAYIEVIKAAADQDREGVLLRSRAMKFLTGYESKSMEDAHVDAVMILGEAFSSEEPFDFGEQSTTERIHRLIPVMLKERLTPPPEETYSLHRKMGGSFLICSKLKARISCKKMFQDAYGRYWGDRRPGRRP
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:
MDLKNKVALVTGAATGLGRAFSEELLKHGAKVVICDLDSDAGELTVEELEKQYGARVLFCHCDVTDYIQFEEAFEYTVNMFKEVNIVINNAEIMNDNFWELEVDVNLNGAIRGTLLAQKFMDKSKGKGGGVLVNIGSGVSVTPQLSTPIYTATKHAILGLTKACGDPFHHANTNVRAFAYCPGPIENSSSHNKRFMSPAYEKAKELDTAGVQLQRMEHVAKELIPLLKNAPTGSIWLVTGGKPAKEIPYSSI
The following text describes a protein:
Function:
Associates with IFNGR1 to form a receptor for the cytokine interferon gamma (IFNG). Ligand binding stimulates activation of the JAK/STAT signaling pathway. Required for signal transduction in contrast to other receptor subunit responsible for ligand binding.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Cytoplasm. Note=Has low cell surface expression and high cytoplasmic expression in T cells. The bias towards cytoplasmic expression may be due to ligand-independent receptor internalization and recycling.
Sequence:
MRPTLLWSLLLLLGVFAAAAAAPPDPLSQLPAPQHPKIRLYNAEQVLSWEPVALSNSTRPVVYQVQFKYTDSKWFTADIMSIGVNCTQITATECDFTAASPSAGFPMDFNVTLRLRAELGALHSAWVTMPWFQHYRNVTVGPPENIEVTPGEGSLIIRFSSPFDIADTSTAFFCYYVHYWEKGGIQQVKGPFRSNSISLDNLKPSRVYCLQVQAQLLWNKSNIFRVGHLSNISCYETMADASTELQQVILISVGTFSLLSVLAGACFFLVLKYRGLIKYWFHTPPSIPLQIEEYLKDPTQPILEALDKDSSPKDDVWDSVSIISFPEKEQEDVLQTL
The following text describes a protein:
Function:
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Miscellaneous:
MISCELLANEOUS: There are 2 genes for eL43 in S.pombe.
Subcellular Localization:
Cytoplasm.
Sequence:
MTKRTKKVGVTGKYGVRYGASLRRDVRKIEVQQHSRYQCPFCGRLTVKRTAAGIWKCSGKGCSKTLAGGAWTVTTAAATSARSTIRRLREMVEV
The following text describes a protein:
Function:
D-glutamate cyclase that converts D-glutamate to 5-oxo-D-proline.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MPFTVHLRCRLPSAIRSLFLQKKPNIRNTSSMAGELRPASLVVLPRSLAPAFERFCQANTGPLPLLGQSEPEKWMLPPQGAISETRMGHPQFWKYEFGACTGSLASLEQYSEQLKDMVAFFLGCSFSLEEALEKAGLPRRDPAGHSQAGAYKTTVPCVTHAGFCCPLVVTMRPIPKDKLEGLMRACCSLGGEQGQPVHIGDPELLGIKELSKPAYGDAMVCPPGEVPVFWPSPLTSLGAVSSCETPLAFASIPGCTVMTDLKDAKAPPGCLTPERIPEVHHISQDPLHYSIASVSASQKIRELESMIGIDPGNRGIGHLLCKDELLKASLSLSHARSVLITTGFPTHFNHEPPEETDGPPGAVALVAFLQALEKEVAIIVDQRAWNLHQKIVEDAVEQGVLKTQIPILTYQGGSVEAAQAFLCKDGDPQTPRFDHLVAIERAGRAADGNYYNARKMNIKHLVDPIDDLFLAAKKIPGISSTGVGDGGNELGMGKVKEAVRRHIRHGDVIACDVEADFAVIAGVSNWGGYALACALYILYSCAVHSQYLRKAVGPSRAPGDQAWTQALPSVIKEEKMLGILVQHKVRSGVSGIVGMEVDGLPFHNTHAEMIQKLVDVTTAQV
The following text describes a protein:
Function:
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Subcellular Localization:
Cytoplasm. Nucleus. Chromosome, telomere.
Domain:
This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Sequence:
MAASTPLLSRGTLIKQGAEAKVYALPSLFPEPTTYHPGSSSSFSAASPTPVILKHRFTKTYRHPTLDAYLTSQRLTFEARALARAAKAGVTVPKVVWVDEKAGVIGMERIEGWSVREILGGGAEGEVEVIEEQEIEEDVENKAEDSAVREEPEGPESEGLKALKNLGVTQEHLMRSIGAALARLHKTMIIHGDLTTSNMMVRLTPGGSGPYEIVLIDFGLSSQAQFPENYAVDLYVLERAFASTHPRSEKLYAGVLETYAEGLGEKKWKPIQIKLKDVRRRGRKRDMTG
The following text describes a protein:
Function:
Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position. Lacks carboxypeptidase activity. Lacks dipeptidyl-peptidase IV type activity.
Subcellular Localization:
Apical cell membrane; Single-pass type II membrane protein.
Sequence:
ARSKMWKKILLFGLLGAAILTFGILVGHYGIEKSPGWVRDMSRDVDESMIEQFIKEVDNKRIEEYLKELTKVPHMATSSGDEQLVKYILDQWKDPISGLDDAWKDTYKVYLSFPSDTTPNRVTVVSPTDSVLFTSRLKEKNYTEDQLHPDVVQPYAAYAPAGNPKGRLVYANQGKVSDYEFLNKTIDLNGAIAIVRYGGAGRANKAINAAPFGVIGVLVYTDPKDINDGKLSDVNETYPNSWYLPPSGVERGSYNTYFGDLLTPYLAAKDYTYRIKEADIKGIPPIPTQPIGFEDASALICKLGGSDAPSLWQGSFKCTYRLGPGFEPNSIFNNSEVQLNVYNKGELKNSDNVMGVIRGSVEPGVLYVPQTLSHSPVPPDTYTHFTIENKPVLGPSPKLYRRWRPRRSIIFGSWGAEEFGLIGSTEYTEEYYSKLRDRAVAYINVDISVFANATLRVQGSPAAQSVVFTATKQVKTPGSPSTSVYDNWIQYFNRSSPAYGIIPNLGYLTGAGSDYAAFMHFLGITSMDIAYTYDRSKTQARIYPAYHTAYDTFDYAARYIDPGFTSHQTVARTAGNVLLRLADSLVIPFNAVDYAETLEQFLNTSLDSYNTRLMEKGISMEPLKTAVAKFRTAANSLSRLIQDTDLTKETPLRIRRINDQLMFMDRAFVDPMAFPDKYHYRHVIWASRSSGVVTFPGLADAFARAVSTDSASDWDQVHRHLTIVIQTIEGAAHTLEEVI
The following text describes a protein:
Function:
Major structural component of the ciliary rootlet, a cytoskeletal-like structure in ciliated cells which originates from the basal body at the proximal end of a cilium and extends proximally toward the cell nucleus. Required for cilia integrity and function in sensory neurons. Maintains cilia integrity, partly by modulating the assembly and transport of intraflagellar proteins along the ciliary axoneme. Required for normal mating behavior and normal responses to environmental and chemical stimuli.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MKSAASSEDVVRVTEDLSECRNRLDAGIEENRRNRQVIQDINDQLQRFRQRANAESIESFNLTPSPDVTLSSLAHPGLTHLHNQTNISMPSLTIDIPLNSNAMISSSRTPNYAINGLRNRHKSLVGHRYRSTSPIGDYGRHRSSPRVLAHYNLDGADIGVGEENLDELFAKLKEELFKNNTLEEVNEMLREENDAALAANEHLRVDATNLSRQLQQLQQQQHTESMRFRSENTRYRNQTETQHRKLISLWKEFTAVKRQLHELRTTTANDLDRQLTEFTRCATLMRKAIRHAEQKNLDQKEQMKREKDDVLDETLRQLNSVTENYMKSEEKANERQRDLKRKEDECRKLREQNDELSDILEQLSKMAHEMAGGRGRNETPMDVARKMRKLLTTKNGEIDESREAAKQAEKERDRAKKDLEKEEKRRKDDREAERKRSSVYSQREHDLKKLDDELRKASEKIRNLEEQRESQEKLTISVQNSLNEAHRQHKQFIEELMIRHREELKEREDSHEEALRSKDTEERSRFEKERSEREKIRRESDELRETQRSLKGDVAAMKTDLDDKTLRLDMLETERDELKKKLETEREQADQRDLEIAECRAKLDEMAEKEAELRKELAEFQAIITAMEGEGKLNQEQFLESKNELNTLTDQIESLNSEVENKNEEIRNLMATLQEKEVHIQNVRTSSHQLTATYEEANGEIDILKAELTRLHEQVNERTRQISEANEKYDDAARKNDALLEDVATWQEKYEQLKMELEEMNRRGQEKEREEADLRALLDDLRGNFDKLTNELKQKGVTVDSLNEEISSLKEQLNKSEKERKEELLRMEELEQKNEAEMKEEYEVKLQLAEKDRQGVENFGKECEARMNELTKIHEMLMEEHDQLKVDHLHTEEEVERLKEKMRKELEKLNEQNDGDRAEWSNERNRLESSKNEAVTELQERVQKLEDVVKEKEDKEIALRRDLEDSHEKSRDLDDKLRKMELTDEEKEEDRKKEQKTLNEERMKLMEQKEEAMLVATKHATTIDQQTRRISVLEGDVEKLTAGIAERESSINALESNTMELISKLETTEAELEKLKDELAVMLKQNSELKNGKEGLSEKWNEERKKIQDLADQLREANKVVHNMRMKNVNLEEKKNELDQNVTDLTNKVRQLEIQLMDKAAKNEVSGDLLRKMEHDAQSMLKQAQNEQFRLTDLEKVRKALQDENQRLVNDLATVKAAFEVKRETSKSAISDILDKYRSAEEKANKGELDNQRLRSDLATVTLKLERQELKAKDSDNRLRDSQKRFEEVQSKLANLQKSAVESLQNPMSSNSRQNRSIYVDIPRAASSIGLNENSDEVPLRSSPSVRFADSSQNMQRAVDSMDVSSSVGVTLRFLKERIEQLEADNADLSDALEKAKDELRQRNEKLADRQMVIERVERQLVHITEERNTIENRMTSQRQMYLTNEESSRSREHEIRSMKARISTLELHLREKESKLAHLRKEIEVLHGQLHDALESKEKATGLVGVQDSKHRDLEEQLDRANRERELAIGKQRRTLAENENLFRKLEQLEKEREQLMREITDERRLNERNRTSLEELRVSERTWKSAMTTAKKPAEEQERAVQEQRRWEESNHEMTNRNTALTKECDRLRVEMRDQLNRMNGINLRSVDFERKNEELSSKLIVMQNTVTAMKKFEEEWKRLEAEMRAELKILRKEKLMQTAEIEDLKRKSFRSDTEKKEIEGIRVRLEREISALKRHVDALEEEKGKTEKAVRETMNERRAIDKSLASMERENQQLYRNCAQLQAQIQNLERDAGNRSVTKLAKEHSLLEARIAALIEEKRQLQSMLDQKDANYSHKRKLLESQIQLLREQLEAERRKRTKGVVATGPTVSRRGVQHTSAFRHTIERHRSLSQSSERTILQERYLEYVYTGDRTPAIQMINTPPISPLSHSGSFNSDGREARIRRESDNGHLQH
The following text describes a protein:
Function:
Retinol transporter. Accepts retinol from the extracellular retinol-binding protein rbp4, mediates retinol transport across the cell membrane, and then transmits retinol to the cytoplasmic retinol-binding protein rbp1. Required for normal vitamin A homeostasis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Contrary to predictions, contains nine transmembrane helices, with an extracellular N-terminus and a cytoplasmic C-terminus. Besides, contains one long helix that dips into the membrane and then runs more or less parallel to the membrane surface.
Sequence:
MSAETVNNYDYSDWYENAAPTKAPVEVIPPCDPTADEGLFHICIAAISLVVMLVLAILARRQKLSDNQRGLTGLLSPVNFLDHTQHKGLAVAVYGVLFCKLVGMVLSHHPLPFTKEVANKEFWMILALLYYPALYYPLLACGTLHNKVGYVLGSLLSWTHFGILVWQKVDCPKTPQIYKYYALFGSLPQIACLAFLSFQYPLLLFKGLQNTETANASEDLSSSYYRDYVKKILKKKKPTKISSSTSKPKLFDRLRDAVKSYIYTPEDVFRFPLKLAISVVVAFIALYQMALLLISGVLPTLHIVRRGVDENIAFLLAGFNIILSNDRQEVVRIVVYYLWCVEICYVSAVTLSCLVNLLMLMRSMVLHRSNLKGLYRGDSLNVFNCHRSIRPSRPALVCWMGFTSYQAAFLCLGMAIQTLVFFICILFAVFLIIIPILWGTNLMLFHIIGNLWPFWLTLVLAALIQHVASRFLFIRKDGGTRDLNNRGSLFLLSYILFLVNVMIGVVLGIWRVVITALFNIVHLGRLDISLLNRNVEAFDPGYRCYSHYLKIEVSQSHPVMKAFCGLLLQSSGQDGLSAQRIRDAEEGIQLVQQEKKQNKVSNAKRARAHWQLLYTLVNNPSLVGSRKHFQCQSSESFINGALSRTSKEGSKKDGSVNEPSKEAESAAASN
The following text describes a protein:
Function:
Transcriptional activator involved in the hypoxic stress response. Acts as a transcriptional activator via the cis-acting element GCC box. Plays a role in low oxygen signaling and contributes to tolerance to anoxia stress by enhancing anaerobic gene expression and ethanolic fermentation. Invovlved in the modulation of ethylene responses under both normoxia and hypoxia; [Isoform 1]: Is mostly responsible for transactivation of hypoxia-responsive genes; [Isoform 2]: Involved in root development through the regulation of root meristem cell division. Does not act as a transcriptional activator via the cis-acting CRT/DRE element.
Miscellaneous:
MISCELLANEOUS: Seedlings silencing ERF73 exhibit reduced elongation of the primary root. Seedlings overexpressing ERF73 exhibit increased elongation of the primary root. Plants overexpressing ERF73 exhibit increased tolerance to hypoxia treatment; MISCELLANEOUS: [Isoform 2]: Plants overexpressing ERF73 exhibit increase tolerance to submergence.
Subcellular Localization:
Nucleus; [Isoform 2]: Nucleus.
Sequence:
MCGGAVISDYIAPEKIARSSGKSSWRSNGVFDCSIYDFDGNFDELESDEPFVFSSTHKHHASGSASDGKKKQSSRYKGIRRRPWGRWAAEIRDPIKGVRVWLGTFNTAEEAARAYDLEAKRIRGAKAKLNFPNESSGKRKAKAKTVQQVEENHEADLDVAVVSSAPSSSCLDFLWEENNPDTLLIDTQWLEDIIMGDANKKHEPNDSEEANNVDASLLSEELLAFENQTEYFSQMPFTEGNCDSSTSLSSLFDGGNDMGLWS
The following text describes a protein:
Function:
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Subcellular Localization:
Cytoplasm.
Sequence:
MPWAALLAGMHATVSPSRVRGRARAPPSKSYTHRALLAAGYADGETVVRDPLVSADTRATARAVELLGGAAARENGDWVVTGFGSRPAIPDAVIDCANSGTTMRLVTAAAALADGTTVLTGDESLRARPHGPLLDALSGLGGTARSTRGNGQAPLVVDGPVSGGSVALPGDVSSQFVTALLMAGAVTETGIETDLTTELKSAPYVDITLDVLDAFGVGASETAAGYRVRGGQAYAPSGAEYAVPGDFSSASYLLAAGALAAADGAAVVVEGMHPSAQGDAAIVDVLERMGADIDWDTESGVITVQRSELSGVEVGVADTPDLLPTIAVLGAAADGTTRITDAEHVRYKETDRVAAMAESLSKLGASVEERPDELVVRGGDTELSGASVDGRGDHRLVMALAVAGLVADGETTIAGSEHVDVSFPDFFEVLAGLGADTDG
The following text describes a protein:
Function:
Involved in nucleotide metabolism via production of dUMP, the immediate precursor of thymidine nucleotides, and decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Sequence:
MHLKIVCLSDEVREMYKNHKTHHEGDSGLDLFIVKDEVLKPKSTTFVKLGIKAIALQYKSNYYYKCEKSENKKKDDDKSNIVNTSFLLFPRSSISKTPLRLANSIGLIDAGYRGEIIAALDNTSDQEYHIKKNDKLVQLVSFTGEPLSFELVEELDETSRGEGGFGSTSNNKY
The following text describes a protein:
Function:
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Sequence:
MKFNPFVTSDRSKNRKCHFNAPSHIRRKIMSSPLSKELRQKYNVRSMPIRKDDKVQVVRGHYKGQQIGKVVQVYRKKYIIYIERVQREKANGTTVHVGIHPSKVVITRLKLDKDCKKILERKAKSRQVGKEKGKYKEETIEKMQE
The following text describes a protein:
Function:
Involved in the anomeric conversion of L-rhamnose.
Subcellular Localization:
Cytoplasm.
Sequence:
MKREAFKMYLKPGYEAEYEKRHAAIWPELKALLSKNGVSDYSIYWDKETNILFAFQKTEGEGGSQDLGNTEIVQKWWDYMADIMEVNPDNSPVSIPLPEVFHMD
The following text describes a protein:
Function:
Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus; Can promote the transfer of one strand of a double-stranded DNA molecule to a homologous single strand and thus may be involved in recombination.
Miscellaneous:
MISCELLANEOUS: S-II binds to RNA-polymerase II in the absence of transcription; MISCELLANEOUS: Present with 6260 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MDSKEVLVHVKNLEKNKSNDAAVLEILHVLDKEFVPTEKLLRETKVGVEVNKFKKSTNVEISKLVKKMISSWKDAINKNKRSRQAQQHHQDHAPGNAEDKTTVGESVNGVQQPASSQSDAMKQDKYVSTKPRNSKNDGVDTAIYHHKLRDQVLKALYDVLAKESEHPPQSILHTAKAIESEMNKVNNCDTNEAAYKARYRIIYSNVISKNNPDLKHKIANGDITPEFLATCDAKDLAPAPLKQKIEEIAKQNLYNAQGATIERSVTDRFTCGKCKEKKVSYYQLQTRSADEPLTTFCTCEACGNRWKFS
The following text describes a protein:
Function:
Required maternally for early embryonic cell divisions. May have a role in DNA replication.
Sequence:
MASSSTAFYLKDAGFHIRNVPKEWNDWNLFHIFQVFGRVGYCRVAGQSNDMQLGFVNMLSAADAEEVRKNLHDGNLIGDNYSLKVSDHKNIGGALLPMASISVQKLLSSPPAKSGPVHLSSSWLPLNKDIEVEVVDYLPSSSAAKDVFALTILRINDAQSNEKYNAMHEKMNSYAQLVAFDSELQIGYDGVFRESPRSIKRVRRISATKLYLVDFGKIINYEKSKCFQIPKVFQTIPTRVSFCGLDGLTWSEQAIPSFDNIREVVQKWGAMENATLHAVTCGFAGAINMINLFCGNSVLAERLQRKGICEYLPRHQQPRFAYSRDSLLKHTNAGVTAHISNDADVVKDLLKKIDGVKSMLRELDL
The following text describes a protein:
Function:
Part of a potassium transport system.
Sequence:
MQVIIVGAGTVGAPLVDVATGSGNEVVVVEQDGGRANEIADAYDCAVLHADATDESTIQDAGADRADALITTTGRDPTNLFVCLLGAEHDIPTVVSLLQRPAHRHLFAELGVYTVAGLHDLAAESLYRVARQPAVSESMPVAGDAAVFRITVGADAPIADTMLVDARSTGVLPDDVLVVAVRTGDGEAEIARSETTITPGDEVTVYSSRGTTADVTAVFSTDVREDGARGRF
The following text describes a protein:
Function:
Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
Sequence:
MLPATTGHSAELGSSVPIYTPHAVSVSLPTWKDNVDYELGLERVHNKLSTGYPRFFIHLDIQKLAEICRAAHALSPQERCMLFPSEKAANLCRKFVADRALKQAIAEAGLEKRCRLVRFEASSSKPSSPVTTRPEPPLRIFVLFVPDEKIFGLARTFWQHTGLGISSRFAERALRLMGSFPVREAPRAPHSQILNDLPSPPNSPAVAPRRYNVKQSPKFPLPAPPIPTGLETDENTSTYVEERYGRNLPIQHVQGAKLALRRRIADILVETAPSDGSSSPPAANLKRSERGAGQLTESDIYLYPTGMSSIFYAHQLAMSLQVRLHPDQPIGKSICFGFPYTDTLKIIEKWGPGAHFFGHGESDDLQALAQLLEQNQAQGIPPIAALFCEFPSNPLLKSPDLVQLRQLADQYGFLVVIDETIGNFLNVEVLPYADILVSSLTKVFSGDSNVMGGSMIINPSSKHHSTLKGLLDGDQTNPTGIYEDTYFGEDAIFMERNSRDFRTRVAKINGNASGICEYLMSLRDSEENKIIKSIHYPRYTTRENYEMCRRKHPPGGYGGLFSIIFHDAKSCETFYDHLKSYKGPSLGTNFTLSSPYVLLAHFNELEWASQFGVDSNLIRVSVGLEDLACLLQWFQFAFQHANS
The following text describes a protein:
Function:
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Subcellular Localization:
Cytoplasm. Vacuole membrane; Peripheral membrane protein.
Sequence:
MPATNSDEPLVKFELYQLKKCYYIVSENATATIFRILKITQSEDELSISIEEAAKILFRQKLQLYLEKLENESADGKLILVTKAYAILGLFRFTAGYYLYLCTERKVVAVIGGHNVYHVDKTQFIELNPSRRHNTSVERKCMSSIEKVDLARTFYFSYSYDLSQTIQYGFTHPIPQHQVRDMFVWNWNMLRPILDSVGIDSPWCIPLIHGFVDQAKLSVYGKPIIVTLIARRSRHFAGARFLRRGIRDDGYVANEVETEQIVFDGSASSFPISSTTPGIPCYTSYVQHRGSIPLRWSQEFSNITPKPPIGIDFHDPFYASTALHFDRLFGHYGIPCIVLNLVKSSEKVKRESLLLDEFESAIQYLNQFLKDSQKIQYIAWDMSAASKKKVPVTKTLEQMASDIVKKTGFFCTADRFFPGTFQTGVVRTNCVDCLDRTNAAQFVIGKCVLAAQLRALGVLDSPQLDYESDAVRLLAEMYHGHGDAIALQYGGSLLVNTLDTYRKNNQWSSTSRDLIESVKRFYSNSFVDFQRQEAISLFLGNFTVHGKIVVFGEKRLQALTEKFKNGQLVRRDYRYWWTPVYVNQELRCKNAYCDSIQRKGIKFPANYFDNVYTPNSISSFSEVLLPNLISTLNFAPLSLIPLLRKSFLPLSYNGFGIEAPSLNPFIPRRNQPRDMFKTSAEEENEDEDEDDDKFRRVSLYKWLFNNEERPVHKFIRKRLHQIPVSNKVQPRDQKQPDFKIPNTDINVYKIHFQYNNISGLADNYTLLSKHDRAMYNNYADYSPDKIKEIKEKELNTYNDYFNSAISENPTLKSDRSEKVAFYSAWITDYKST