lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase Ran in its active GTP-bound form. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus, nucleoplasm. Nucleus, Cajal body. Nucleus, nucleolus. Note=Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm (By similarity).
Sequence:
MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFDFSSGQITQVKAKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFETLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHGQLLEKRLNLREALMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDIPPRRQLYLTVLSKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTEIIMTKKLQNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPAQFKLVLDSIIWAFKHTMRNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISTPLNPGSPVSNQMFIQDYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEERETALRQAQEEKHKLQMSVPGILNPHEIPEEMCD
The following text describes a protein:
Function:
Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. Has preference for C-18-CoA substrates compared to C-16-CoA substrates.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence:
MKIPAALVFIPVGVLFLISGLIVNIIQLVFFIIVRPFSRSLYRRINKNVAELLWLQLIWLFDWWACIKINLYVDAETLELIGKEHALVLSNHRSDIDWLIGWVMAQRVGCLGSSLAIMKKEAKYLPIIGWSMWFSDYIFLERSWAKDENTLKAGFKRLEDFPMTFWLALFVEGTRFTQEKLEAAQEYASIRSLPSPRNVLIPRTKGFVSAVSEIRSFVPAIYDCTLTVHNNQPTPTLLRMFSGQSSEINLQMRRHKMSELPETDDGIAQWCQDLFITKDAQLEKYFTKDVFSDLEVHQINRPIKPLIVVIIWLGFLVFGGFKLLQWLSIVASWKIILLFVFFLVIATITMQILIQSSESQRSTPAKRPLQEQLISA
The following text describes a protein:
Function:
Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by precluding channel closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that positively regulates synaptic transmission mediated by AMPA-type glutamate receptors. Plays a role in suppressing the production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK pathway (By similarity).
Subcellular Localization:
Secreted. Synapse. Cytoplasm; [Isoform 1]: Cytoplasm. Golgi apparatus. Secreted; [Isoform 2]: Cytoplasm. Endoplasmic reticulum.
Sequence:
MESESSRRMGNACIPLKRIAYFLCLFSVVLLTEGKKPAKPKCPAVCTCSKDNALCENARSIPRTVPPDVISLSFVRSGFTEISEGSFLFTPSLQLLLFTSNSFDVISDDAFIGLPHLEYLFIENNNIKSISRHTFRGLKSLIHLSLANNNLQTLPKDIFKGLDSLTNVDLRGNAFNCDCKLKWLVEWLGHTNATVEDIYCEGPPEYKKRKINSLSPKDFDCIITEFAKSQDLPYQSLSIDTFSYLNDEYVVIAQPFTGKCIFLEWDHVEKTFRNYDNITGTSTVVCKPIVIDTQLYVIVAQLFGGSHIYKRDGFANKFIKIQDIEVLKIRKPNDIETFKIEDNWYFVVADSSKAGFTTIYKWNGNGFYSHQSLHAWYRDTDVEYLEIARPPLALRTPHLILSSSSQRPVIYQWSKATQLFTNQTDIPNMEDVYAVKHFSVKGDVYICLTRFIGDSKVMKWGGSSFQDIQRMPSRGSMVFQPLQINNYQYAILGSDYSFTQVYNWDAEKAKFVKFQELNVQAPRSFTHVSINKRNFLFASSFKGNTQIYKHVIVDLSA
The following text describes a protein:
Function:
Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome. May do so by stabilizing the catalytic center or the position of the RNA substrate (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSYNGIGLPTPRGSGTNGYVMRNLSHVKKYDKNTNLQSNRNAKALEKRVQDPSISEHECRRQIESKLLLYREQLLEEVSSQHSTDAAASDSNTNFGTENPKPPKAIIKDEQSQSKTKSLDEADVEILVQKYREQLLKELQLQKSTEKGKNFESILQPQKRKETRGFHSKNDDDGRLEERDDLRSSVDDDYYDYPRYSERKSLNSKRHVDNYNENRRRHYDSYSSYDELERRRSSNESYSRRSELPRRDYNRHDERERYSYHRRRERSNSPSYTKNESIPVVDRDSSPEGGEIV
The following text describes a protein:
Function:
Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.
Subcellular Localization:
Cell junction, focal adhesion. Cell junction, tight junction. Cell projection, filopodium membrane. Cell projection, lamellipodium membrane. Cytoplasm, cytoskeleton.
Sequence:
MSESSICQARATVMIYDDGSKKWVPAGTGPQAFSRVQIYHNPTNNAFRVVGRKMQTDQQVVINCPIVKGLKYNQATPNFHQWRDARQVWGLNFGSKEDAALFANGMMHALDVLSSIPDGGYSARPVSNGPSPEELEQQRRLEQQRLEQQERERLERERQERERQERERQERERQERERQERERPVASVVIPPAPPLAPGGPPAPPGPPPPPGPPPSGPPPPPGPPPSGGGAPPPPAPPLPSSGGSDGGGGPGGGGGLAAALAAAKLRKVPKDDAGGGGGVASAAASVAAPKADSGRNSVSMPSGGGGGGGGGGGGGGLMGEMSAILARRRKAADKGEKPPPKAEEPANDDSDTQGPGDFRRPWEKSATMPRTNSAPRSLESPSSSSPLARMKPVSQSAEAESGEGESEMERIKQELLEEVRKELQKVKNEIIGAFIQELQKRGST
The following text describes a protein:
Function:
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Sequence:
MSPSVASPKTLYDKVWDSHVVDLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKDMKDIASFIHQPDSRTQVLALENNIKEFGLTYYGMNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRPLAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAHVKDNVRAASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKDAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREFFGDVSNGSPSIITNKNYDPSHDVEGDIGLSVDDATDAVTDADGIATNVAGSVSSGSAGIPKFTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRYDADGKEIPDFVLNREPYRHATVLVAHDNFGCGSSREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDMMKAAENQVKFSVDLVNQTITYGDKQVKFDVEPFRKHCLVNGLDDIGLTLQKETMIDAFEAAREENFPWMNIKRSRARLSPVKSNKQSSSRNDW
The following text describes a protein:
Function:
Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the blocking of the phosphorylation of rhodopsin.
Miscellaneous:
MISCELLANEOUS: Probably binds two or three calcium ions.
Sequence:
MGNSRSSALSREVLQELRASTRYTEEELSRWYEGFQRQCPDGRIRCDEFERIYGNFFPNSEPQGYARHVFRSFDTNDDGTLDFREYIIALHLTSSGKTHLKLEWAFSLFDVDRNGEVSKSEVLEIITAIFKMIPEEERLQLPEDENSPQKRADKLWAYFNKGENDKIAEGEFIDGVMKNDAIMRLIQYEPKK
The following text describes a protein:
Function:
Acts as a co-chaperone and mediates the association of the chaperones HSP70 and HSP90 probably facilitating substrate transfer from HSP70 to HSP90. Stimulates HSP70 ATPase activity and, in contrast, inhibits HSP90 ATPase activity.
Subcellular Localization:
Cytoplasm.
Sequence:
MTETAAEWKAKGNAALSAGNAQEAVHCYTQAIELNPSDHVFYSNRSAAYLSLDDAAHALEDAELCIQTKPDWAKAYSRKGAALHALKRYDEATDAYSDGLKVDATNAACLSGVEEVKKAQAAATQSFNPLANAFGPDMFGKIATNPRLAPLLGDPQFVQVLQEIQRDPSKINEHIKDSRVMTVLGELMGLNINMDGAEDEEMPAAASTPAPKAEPTPVPEPTPMDEDLTDEEKAERAAKKAADEAKQRGNAFYKQKKFSEAIECYNEAVEKDATNMSYYSNLAAVKLEMGQFDACIEDCKKAIEVGRANRADYALIAKAYVRIGNAHLKKGETEENLSAAIDSYEGAQMENRTKDVERKIKTLQVKLRKAKDLAYIDPEKALAAKNEGNEFFKNGEFPQAVERYTEAIKRDPSCAVYYANRAAAYTKLTSFNEAKKDCEKAIELDPKYVKAYSRMGAIQCFMKEFHKARESYEKGLALDPNHQECIDGLRNVMYKIQSGDTDEERARHGMADPEIQAILRDPVMQNVLNDFQTDPSSAQRHLQNPGIMAKIEKLIAAGVLQTK
The following text describes a protein:
Function:
Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 20 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA (Probable). Binds to erythroid progenitor cells expressing high levels of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region. The additional N-terminal region of isoform Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus.
Miscellaneous:
MISCELLANEOUS: [Isoform Minor capsid protein VP1]: Minor splicing isoform; MISCELLANEOUS: [Isoform Major capsid protein VP2]: Major splicing isoform produced by deletion of the initiating AUG for VP1 and downstream translation of VP2.
Subcellular Localization:
[Isoform Minor capsid protein VP1]: Virion. Host nucleus. Host cytoplasm; [Isoform Major capsid protein VP2]: Virion. Host nucleus. Host cytoplasm.
Domain:
The N-terminus of Isoform Minor capsid protein VP1, VP1u, contains a phospholipase A2-like region. VP1u is necessary and sufficient for host cell binding and internalization; A nuclear localization signal is present in the C-terminus and can be recognized by cellular nuclear import molecules. After assembly, it is hidden because it is on the inner capsid surface.
Sequence:
MSKESGKWWESDDKFAKAVYQQFVEFYEKVTGTDLELIQILKDHYNISLDNPLENPSSLFDLVARIKNNLKNSPDLYSHHFQSHGQLSDHPHALSSSSSHAEPRGENAVLSSEDLHKPGQVSVQLPGTNYVGPGNELQAGPPQSAVDSAARIHDFRYSQLAKLGINPYTHWTVADEELLKNIKNETGFQAQVVKDYFTLKGAAAPVAHFQGSLPEVPAYNASEKYPSMTSVNSAEASTGAGGGGSNPVKSMWSEGATFSANSVTCTFSRQFLIPYDPEHHYKVFSPAASSCHNASGKEAKVCTISPIMGYSTPWRYLDFNALNLFFSPLEFQHLIENYGSIAPDALTVTISEIAVKDVTDKTGGGVQVTDSTTGRLSMLVDHEYKYPYVLGQGQDTLAPELPIWVYFPPQYAYLTVGDVNTQGISGDSKKLASEESAFYVLEHSSFQLLGTGGTATMSYKFPPVPPENLEGCSQHFYEMYNPLYGSRLGVPDTLGGDPKFRSLTHEDHAIQPQNFMPGPLVNSVSTKEGDSSNTGAGKALTGLSTGTSQNTRISLRPGPVSQPYHHWDTDKYVPGINAISHGQTTYGNAEDKEYQQGVGRFPNEKEQLKQLQGLNMHTYFPNKGTQQYTDQIERPLMVGSVWNRRALHYESQLWSKIPNLDDSFKTQFAALGGWGLHQPPPQIFLKILPQSGPIGGIKSMGITTLVQYAVGIMTVTMTFKLGPRKATGRWNPQPGVYPPHAAGHLPYVLYDPTATDAKQHHRHGYEKPEELWTAKSRVHPL
The following text describes a protein:
Function:
Involved in the biosynthesis of galactosamine-containing minor teichoic acid, a non-essential cell wall polymer in B.subtilis 168.
Sequence:
MNEKSFNYDFSVIMPIYNVELYLTEAIESIINQTIGFENIQLILVNDDSPDKSEIICKEYAQKYPNNIVYAKKQNGGVSSARNYGLKYAEGRYIQFLDPDDLVSEGTFENVLNFFDEHKNEIDIVAIPIFFAEGRTGEHNLNNKFSSTRILDVEKEPHHILTHCCSTFIKKDALKNIRFDENCKIGEDAKLVNLIISQKKKYGLVKEAKYHYRVREDGSSAMQTAKANKNWFNHSLITFSKNLIDIIKNHEQKIPLFLQYMVMHDLKWKLLIKDISETPLDENEYSEFLTLIREVLSYIDDDVIIETKSVSHFYLYHALKIKHGENYSRYVYERETEQDYYLYREGKIVSKLSDQTLTIEILEENEDSIHIEGFWSSLFNSKGFKFYAKIGETKIKAKNIKRQHNDYISLGEVIKKYPGFSIDIPKGHLADNHHIEFFITKGKKRKLTKLRFFKYSGLSNDLYNTYVAKKDYIFYYNYKKLMFKKNNFKNRFIKEFRFLKSLHKSGEKSKKRKSAIKKALMARMVHHVFTIFNRKPVWLFIDRQDKADDNAEHLFKYAINKNDGVKKYFIIKKDSKDYDRIKKYGKVIPYRSFRHKILTLSSSKVISTHADIWVVNPFFNMEIYFRDLFNFEFIFLQHGITMADHSEWLNKYNKNIKLLVTSAKPEYRSIVKGNYNYKKENILLGGFPRYDNLKKSEGEKQLLIMPTWRKDIVLPKDQAKGVRPYNPKFKDSEYFSRYNALINDERLIEFAKKNNYKITFFPHPDIQQQIVDFEKHDYVEFADYNSSYQMLFNSSNIMITDFSSVAFDFAYEKKPVIYYQYEKSYHFKLDYYDYKKMGFGDVLENHNSLVDKVIYYMKNNSRMEDKYRKRVDNFFAYTDKNNRNRIYNAILELDNNKVAK
The following text describes a protein:
Function:
Putative transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MNTVEENNTKITDNNNNNNNNNNNNNNNNNNNKNNDGENLSQQLIDSNNKKLRSPIQVYFDSDVSSCSLQSQSSPQQLPTQQPIQQQINNIFNHFLPQNQAPLLQAQNQQPINNINQVSNFQIQPIPLTFQLPNNINTNTNNTNMINNVQQFQNNFLNNNDFSLTDPVPSPFVLFNNNNNNNNNNNNNNNNNINNFHHNNINNNFDNNNSNYNTINTHPNNTNNNSSNINQIQSNIYPQQNLHNPFLPIHNNNNINNNNINKNNNNYNNNNNNKNNNNNNNNNNNNNNPQLFSMEPPNGFNHSTTDNTSSVSSVPSNKKKSSKTKQKSKPLTIQQQQQHKSNYHQQPNQNSQHLQSKPNSPILISSPLNSQQNSSPPQPSPTQSFLSPPQYSQSPQNNNFNNNNNNISNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNSTNNNNNNSNTNNNTNTNTNNNNNKNNNNNNNNEIENNNNEELILLWYNSIIKNIIVDENHFKIENQFNKENGYLVFKQLFKNHFGSIGTIGKEMAEYIQLHCEVMNEITELSKFHFQSIDNFYNNYIRIINGYSLIPAKDSGATIKARPKKGAKLSKESKDILENWIKNHIAHPYPTNDEKEQLQRQTGLTPNQISNWFINTRRRKVPTLCDEAGIITNSNVMPQMTINNNNNNGGNSNFKNNNNNTITTTSTSNNNNNNNNNNHNEMECDDGENEESSEYDD
The following text describes a protein:
Function:
Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide.
Subcellular Localization:
Cytoplasm.
Sequence:
MLNIVLFEPEIPPNTGNIIRLCANTGFRLHIIEPMGFTWDDKRLRRAGLDYHEFAAVQRHHDYAAFVAAENPQRLFALTTKGTPAHSAVSYQDGDYLMFGPETRGLPASILDALPKEQKIRIPMMPDSRSMNLSNAVSVVVYEAWRQLGYPGAVLRS
The following text describes a protein:
Function:
Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA interference via its interaction with Ars2 and is required for primary microRNAs (miRNAs) processing. Also involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. In the CBC complex, Cbp80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of Cbp20 and lock the CBC into a high affinity cap-binding state with the cap structure.
Subcellular Localization:
Nucleus.
Sequence:
MGRRKREDSSDEEGDDCRQKRTAETTVKTVEQLMRELSFPGHTPLELKLGNLGYLLGKGMSVDLKENLINELVICLGYYPGQASAYATLVGLINVADFEFGSECLLFMAHKVGESVHIRDWNRCRGVVHCMVDLYHCQVLPSSYILKLLAAFLKDCEALKDPDDLVGVTPQIRRDFLAYCVLSAMPLIGRDLEGETAFDKLIVSLQIYIKKRSALHTNMLSVWPDFNQRDYLELLWQQVDGMRQNHWAEPEHQLIPRPYKSFSETLSHGRIHQLRDYDLAAHEERCRYPLPRVCFRIFSCDSVGEIPNMPPPVSIERHLLEAHILDILISFHKERKICADSLLMYAASKPQLPVYYCIVEVILGEMLRLPTANWSTIAYGSILVELCKRQPDKIPQVVAQALDIIYNRLNSMSVACFDRLVNWVSHHISNFGFNCQWSKWAQGLPSPIDPSATNLQPKVVFLRELLKKCFRLSYHQRIKDVVPDILADFLPPPVLPHFKFVDETLPGAILSKDLLEAMRSPQASPEMISEIIKSSTGIGPLLKINVFTQNCLHLGSKSFSHTFGILRKYHSVFKDLVAGDPERQAAVLNGIFDVWVASDQYKFVVTEKLVTGLIIEPISVVRWIFGPSMRKELTKIYIWELLHSALRHLKRVQQKIEVVDVDDPSACDPVVKGILFTIVQRFVKTLCGAPFADEGTEEHYWFQWVLGRLEETLFIYADDFRVINNKLIKMSEDASDLRPEISKTIAAFVACVM
The following text describes a protein:
Function:
Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue. The DNA-protein cross-link is then reversed: able to catalyze the reversal of the thiazolidine cross-link and cycle between a cross-link and a non-cross-linked state depending on DNA context: mediates self-reversal of the thiazolidine cross-link in double stranded DNA. Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine.
Subcellular Localization:
Chromosome. Note=Localizes to replication forks.
Domain:
The N-terminal catalytic Cys-2 residue forms a thiazolidine linkage to a ring-opened DNA abasic site (By similarity). Glu-132 catalyzes reversal of the thiazolidine linkage; self-reversal is favoured by duplex DNA formation (By similarity).
Sequence:
MCGRFALAYDSGDLPQLLRDWNLPVNTPKDASSNSQHPHDEEDTKDQPTVSKDIFKASYNISPTNYSAVYRPDTKAIQFMRWGLVPFWTKDVSQFKTYRTFNARLENLQESKMWMRPCEKKRCAVLMSGYFEWKTVGKKKTPYFISRRDGRLMFVAGMYDYVEKDDLYTFTIITAQGPRELEWLHERMPCVLEPGTESWDAWMDVDKTTWSTEELVKLLKPDYDESKLQFYQVTDDVGKTTNTGERLIKPLLKEDSDMFSVKREKEEALLENDNEQGIDNRGVKGDKSLKGEDVFNQKKSLKRNSYDGLKKNEEQEETTLPEEGSIGDRVKREEANLSPKREGNREKRNIVNMLGNQKDSRGKKKIKK
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. LAGE3 functions as a dimerization module for the complex.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MMPQIANKPNESIIRVPFETPRLAEIAYKVLGVDQEPRRNFVKKTLSLENDVLVVHFQSDQVKSLRTAITSFFECLLLCQDTINQFGDSKKEKLIPESNDNAGTHSSSDSP
The following text describes a protein:
Function:
Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA.
Subcellular Localization:
Nucleus.
Sequence:
MKDSTCKDGGKQSSKRDSTRVSTHTTSTDQISTKCYGETALKLVKEAVRSRDMSTLAVYKDDLVRDILLETKHLQSQLAIFESTIQGLRPKDVSVKPLAAIVPLETACTLHTLALARNKRCVLAYQRQRLDRLVEMLWNAPGGASTASTLSDQVTQCMSGHEAQFVNGYKTLASEFRGYFLDLDLGMGLIPPNAVFVEIRVIRDCGEIATDDGTLRLDPGAQLFVRRCDVEDFILSGDVKEIVS
The following text describes a protein:
Function:
Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). UME6 controls the level and duration of gene expression in the filamentous growth program such as HGC1; and is specifically important for hyphal elongation and germ tube formation. Promotes filamentous biofilms and is required for adherence to surfaces such as plastic. Plays an important role in virulence.
Subcellular Localization:
Nucleus.
Sequence:
MITHMVTPDSTSSAPNSPYGEDTIKLNSSVISSSSPVRSTSYLQNLQLQQQFSQLQFLQLQQQQQQQDQQLALQQQQQQQQSQSQQAQPYANPYFQTPIDQLFQFDNNPNSSFNPTRPPNIHTNQPYVSPYLHSAPLTNHSDLQPQPPPASLSDSELGLGLVKQQQDSLPPQQQAQSQPTPLLNQQHPFYNEYINDMPSTQHPYLIFNNTNAAHSTTSLPNLDAANPSSILPQSALNQSEYYKVTNGSMSNDPQPSTFLYNLHNHSADLVMNNDLEFSNASFDSIGGVSVSAAATGAGAGAGDYSHTNITSNFAQTNLHSSSQQSGVLPPPPSLPPPPTSLPSQQSQNQYLDVVPPQQLTNNALKTEANSPLITDSANFTTSQPQFENTILEQSPIFSNNTILSGIDEPSKEKSPNMLNSTLPLSKSTPHHIYQPSSSSSSHVRHNKITKKSSLSRLNTSSKKNLRANLVHSLSTPTELDDANNNNNDIVTPPKTLSPLLRKKTSFINVKKENDIDDSHDINCKNFSIDIDDMDDEDVLSDFSQPPPPIGGVSNDTMRSLAPVGGVGLGSSGNITGYRSLSNASSTSSHGSHHGLPVMNIFRHNPDSTKPSTPSPILSTASSSSTLSNKKVVKKLRGRKSKTKMNKSSIKTEQVVNEEPQVKNYKDDNDNDNDNGHGHDHDDENGGVSSDVGTGSNSTPSTTTKGKKMKLNVDLNNGGGSGTGSGSCSDENTSGNGTNTNTDSTSTSNPMVKKKHTRRRLLPRSKKGCWICRIKHLKCDEVTPICGGCAKFGLQCDYSSEKPAYVTDKILRQKKLTEVSLIRKRNQAKTKISRKKSSNDITND
The following text describes a protein:
Function:
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MRIFQSRTGGDFIAYILTGDHVIEENNQLLTIKSPAQVKRSRFTLACFARSLEDLYKKHELLCLRSAALSLSDTHSQSFVRSNSNRSNMFLTRTEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIKTKDGVVLAVEKRITSPLLEPSSVEKIMEIDAHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVESTTQALCDLALRFGEGDEESMSRPFGVSLLIAGHDENGPSLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQYNKDLTLQEAETIALSILKQVMEEKVTPNNVDIAKVAPTYHLYTPSEVEAVITRL
The following text describes a protein:
Function:
Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MALQGVCGWQDPASARPRLPGPEEGWAVPPGWDPSSFLGTPGLDLAHGTTTLAFRFRHGVIAAADTRSSCGQYVACPASLKVIPVHRHLLGTTSGTSADCAAWFRVLQRELRLRALREGRLPSVAGAARLLAGMLHRYQGLDLCVATVLCGWDRSGPALFYVYSDGTLLPGTVFSVGSGSPYAYGVLDRGYRYDMEPHEAYALARQAVAHAARRDAYSGGSVDLYHVRESGWEHVSRQDACVLYRGLQETPGPAPPGPEPPPADEADPGEGPLSTPGKPGEDPGDLGEEGAPRAD
The following text describes a protein:
Function:
Required for maturation of 30S ribosomal subunits.
Subcellular Localization:
Cytoplasm.
Sequence:
MSKVLEQVEAIVAPITDELQLELVDIAFEKEGPNWFLRIFIDKDGGVDIDECAAVSEKVSEKMDENDPITQNYFLEVSSPGAERPLKKEQDFENAVSKYVHVTSYEPIDGRKMWEGTLVSYDGTTLVITITDKTRKITCEIPKDKVAKARLAIQF
The following text describes a protein:
Function:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGRIAVAAIVSVWVIPISILVNRIVPDPYMDEIFHIPQAQQYCNGNFRSWDPMITTPPGLYYLSLVHVAALFPGNYFLQLASSFPEVCSTAALRSLNGVLAVLCSILVYEIITHLRPALDDRKATLFAAVLALYPLHWFFTFFYYTDVASLTAVLAMYLACLKKKYLFSALLGAMAVVIRQTNIIWMLFVTCSGVIDITLAHQRDSAKVYNLKANKGISPSTLITSVNVSSNLRKRKSRGNSEANKHSFYRTNTSSTSQTSGLLYEIQAIVFTAWRIKWELLVSFSPFFFVLLAFVGFLICNGSVVLGAKEAHTVSPHFAQIMYFSIVSALFAAPLHFTIGQALDLFWSFWKNRLLGFFLGFLALIASLLSVHFFSIAHPYLLADNRHYTFYLWRKIINFHWSMKYLLVPVYVYSWFSIFHLLDKTQRRIWVLVYFLATSAVLVPAPLIEFRYYTIPFYFYMLHTGINDCQSLLLMGILYTVLNVFTMRMFLFRPFHWDHEPGVQRFIW
The following text describes a protein:
Function:
Histone methyltransferase that monomethylates 'Lys-5', 'Lys-8' and 'Lys-12' of histone H4 (H4K5me1, H4K8me1 and H4K12me1, respectively), thereby controlling gene expression and remodeling chromatin structures. Functions together with the chromatin-modifying complexes COMPASS and NuA4 to regulate cell growth and stress responses; (Microbial infection) Acts as a virus host factor involved in the replication of positive-strand RNA viruses like the MBV.
Miscellaneous:
MISCELLANEOUS: Present with 5000 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Chromosome. Cytoplasm.
Sequence:
MTLTIKIGTLNDSDQSAVHNGTENGSDFRKITPTEEEICDDVVLLWKEEPGTEDATIQHLYDRITERNQSWKLSASRFRKILNEHHLYDTDLETVSLYKDKIHFPKALDSDAKVEVKFIDDEHGRGLFAKRDFSKGQIILKENKPIVYIPPLDKLFLISNGKACARCGKALYDLTQHKIMVHYLDCEVCKAIWCSEKCKKAHASLHELLYHSWRSNRIDILHAGNWKRFVNYCEKYCFTAAFSVGLIYGSMLLDTTGEVKEQWQKLASISQRERIKLRDASGIGSTFSLLNGTTVHTEEESDNGTKKGVEKNIDDETVWEKCYELFCGAFPKASEEIDFEKFLTMIGTFNINQYNGQVYHWISFINHDCEPNAYIEQVEEHEELRLHARKPIKKGEQIRITYVNPLHGVRLRRRELRVNWGFLCQCDRCQNELSTFERVPNLEKKNADANLGVEKIDSNDSSEDGSKKSTGNRKSSMREAQPDLKEILKNGKEFELDIPETVDTQGNVRKTSVRFDSNVSVAVDER