lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function (By similarity). Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1 (By similarity). Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2 (By similarity). Dephosphorylate FNIP1, disrupting interaction with HSP90AA1/Hsp90.
Subcellular Localization:
Nucleus. Cytoplasm. Cell membrane. Note=Predominantly nuclear. But also present in the cytoplasm. Translocates from the cytoplasm to the plasma membrane in a RAC1-dependent manner.
Sequence:
MAMAEGERTECAEPPRDEPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQKAFERAIAGDEHKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM
The following text describes a protein:
Function:
Guanine nucleotide exchange factor (GEF) which specifically activates small GTPase CDC42 by exchanging bound GDP for free GTP. Plays a role in actin cytoskeletal remodeling in the late stage of cell-cell junction formation by regulating the contractility of actin filaments, which prompts the conversion from 'open' to 'closed' junctions.
Subcellular Localization:
Basal cell membrane. Cell junction. Nucleus. Cytoplasm. Note=Located at the basal plane of cell-cell junctions. Intracellular Ca(2+) concentration is a key factor in regulating PLEKHG4B localization; it diffusely distributes in the cytoplasm under low Ca(2+) conditions, localizes to the basal membrane under normal Ca(2+) conditions, and accumulates at the cell-cell junction under higher Ca(2+) conditions.
Domain:
Subjects to autoinhibition, mediated by the N-terminal domain.
Sequence:
MGFSTADGGGGPGARDLESLDACIQRTLSALYPPFEATAATVLWQLFSVAERCHGGDGLHCLTSFLLPAKRALQHLQQEACARYRGLVFLHPGWPLCAHEKVVVQLASLHGVRLQPGDFYLQVTSAGKQSARLVLKCLSRLGRGTEEVTVPEAMYGCVFTGAFLEWVNRERRHVPLQTCLLTSGLAVHRAPWSDVTDPVFVPSPGAILQSYSSCTGPERLPSSPSEAPVPTQATAGPHFQGSASCPDTLTSPCRRGHTGSDQLRHLPYPERAELGSPRTLSGSSDRDFEKVSPSEQGPRMPPENCGGSGERPDPMDQEDRPKALTFHTDLGIPSSRRRPPGDPTCVQPRRWFRESYMEALRNPMPLGSSEEALGDLACSSLTGASRDLGTGAVASGTQEETSGPRGDPQQTPSLEKERHTPSRTGPGAAGRTLPRRSRSWERAPRSSRGAQAAACHTSHHSAGSRPGGHLGGQAVGTPNCVPVEGPGCTKEEDVLASSACVSTDGGSLHCHNPSGPSDVPARQPHPEQEGWPPGTGDFPSQVPKQVLDVSQELLQSGVVTLPGTRDRHGRAVVQVRTRSLLWTREHSSCAELTRLLLYFHSIPRKEVRDLGLVVLVDARRSPAAPAVSQALSGLQNNTSPIIHSILLLVDKESAFRPDKDAIIQCEVVSSLKAVHKFVDSCQLTADLDGSFPYSHGDWICFRQRLEHFAANCEEAIIFLQNSFCSLNTHRTPRTAQEVAELIDQHETMMKLVLEDPLLVSLRLEGGTVLARLRREELGTEDSRDTLEAATSLYDRVDEEVHRLVLTSNNRLQQLEHLRELASLLEGNDQQSCQKGLQLAKENPQRTEEMVQDFRRGLSAVVSQAECREGELARWTRSSELCETVSSWMGPLDPEACPSSPVAECLRSCHQEATSVAAEAFPGAGVAVLKPHALGKPWASQQDLWLQYPQTRLRLEEALSEAAPDPSLPPLAQSPPKHERAQEAMRRHQKPPSFPSTDSGGGAWEPAQPLSGLPGRALLCGQDGETLRPGLCALWDPLSLLRGLPGAGATTAHLEDSSACSSEPTQTLASRPRKHPQKKMIKKTQSFEIPQPDSGPRDSCQPDHTSVFSKGLEVTSTVATEKKLPLWQHARSPPVTQSRSLSSPSGLHPAEEDGRQQVGSSRLRHIMAEMIATEREYIRCLGYVIDNYFPEMERMDLPQGLRGKHHVIFGNLEKLHDFHQQHFLRELERCQHCPLAVGRSFLRHEEQFGMYVIYSKNKPQSDALLSSHGNAFFKDKQRELGDKMDLASYLLRPVQRVAKYALLLQDLLKEASCGLAQGQELGELRAAEVVVCFQLRHGNDLLAMDAIRGCDVNLKEQGQLRCRDEFIVCCGRKKYLRHVFLFEDLILFSKTQKVEGSHDVYLYKQSFKTAEIGMTENVGDSGLRFEIWFRRRRKSQDTYILQASSAEVKSAWTDVIGRILWRQALKSRELRIQEMASMGIGNQPFMDVKPRDRTPDCAVISDRAPKCAVMSDRVPDSIVKGTESQMRGSTAVSSSDHAAPFKRPHSTISDSSTSSSSSQSSSILGSLGLLVSSSPAHPGLWSPAHSPWSSDIRACVEEDEPEPELETGTQAAVCEGAPAVLLSRTRQA
The following text describes a protein:
Function:
Modulates blood feeding of female mosquitoes on vertebrate species by binding and sequestering different mediators involved in the host response, such as biogenic amines and eicosanoids. Binds serotonin, histamine, leukotriene B4, leukotriene C4, leukotriene D4, leukotriene E4, adrenaline and noradrenaline. Does not bind tryptamine and U-46619, a stable analog of thromboxane A2. Exhibits vasodilating activity. Inhibits agonist-induced platelet aggregation but not blood clotting. Inhibits noradrenaline-induced smooth muscle contraction. Promotes an influx of host neutrophils at the inoculation site; (Microbial infection) Probably promotes Plasmodium gallinaceum oocyst development in mosquito midgut; (Microbial infection) Exhibits antiviral activity against dengue virus type 2 probably through a direct interaction with dengue virus virions.
Subcellular Localization:
Secreted.
Domain:
Lipids and biogenic amines bind independently through different binding pockets, with lipids binding to the N-terminal pocket and biogenic amines to the C-terminal pocket.
Sequence:
MKLPLLLAIVTTFSVVASTGPFDPEEMLFTFTRCMEDNLEDGPNRLPMLAKWKEWINEPVDSPATQCFGKCVLVRTGLYDPVAQKFDASVIQEQFKAYPSLGEKSKVEAYANAVQQLPSTNNDCAAVFKAYDPVHKAHKDTSKNLFHGNKELTKGLYEKLGKDIRQKKQSYFEFCENKYYPAGSDKRQQLCKIRQYTVLDDALFKEHTDCVMKGIRYITKNNELDAEEVKRDFMQVNKDTKALEKVLNDCKSKEPSNAGEKSWHYYKCLVESSVKDDFKEAFDYREVRSQIYAFNLPKKQVYSKPAVQSQVMEIDGKQCPQ
The following text describes a protein:
Function:
Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton. Plays a role in mediating the organization of F-actin into ordered bundles. Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization.
Sequence:
MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDEAMASSGQIDLLERLKELNLDSSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRGFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRVAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRIRQLLQSQATEAERSSQNKHETGSHDAERQNEGQGVGEINMATSGNGQGSTTRMDHETASVLSSSSTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEPGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSITLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQSLYGDYVFDTNRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLGNYHPATENPGTSSKRGLQISTTAAQIAKVMEEVSAIHTSQEDRSSGSTTELHCVTDERNALRRSSAAHTHSNTYNFTKSENSNRTCSMPYAKLEYKRSSNDSLNSVSSSDGYGKRGQMKPSIESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHIIEDEIKQSEQRQSRNQSTTYPVYTESTDDKHLKFQPHFGQQECVSPYRSRGANGSETNRVGSNHGINQNVSQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEEKRHVDQPIDYSLKYATDIPSSQKQSFSFSKSSSGQSSKTEHMSSSSENTSTPSSNAKRQNQLHPSSAQSRSGQPQKAATCKVSSINQETIQTYCVEDTPICFSRCSSLSSLSSAEDEIGCNQTTQEADSANTLQI
The following text describes a protein:
Function:
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.
Subcellular Localization:
Cytoplasm.
Sequence:
ARDRRIQLKSLKLAKLMKKDSEQLLKTYAFKQGDIYRICTLVQLKVVPDVGITGKEPVERMQSIYTSLIHFKGLFDTISEQQRDLLYPADDTLHSMLIEAQSRIKDLANNLLMTFPKLSVVKGQESSPLANGNYFQQKLFGCSVLKKYTEFLSQVVKEL
The following text describes a protein:
Function:
Enhances sperm motility. Binds to calmodulin and inhibits calcium transport into spermatozoa. May modulate the function of nicotinic acetylcholine receptors.
Subcellular Localization:
Secreted.
Sequence:
MNSVTKISTLLIVILSFLCFVEGLICNSCEKSRDSRCTMSQSRCVAKPGESCSTVSHFVGTKHVYSKQMCSPQCKEKQLNTGKKLIYIMCCEKNLCNSF
The following text describes a protein:
Function:
GTPase-activating protein which accelerates the GTP hydrolysis rate of YPT1 and SEC4. Involved in ER to Golgi trafficking and polarized exocytosis.
Miscellaneous:
MISCELLANEOUS: Present with 1940 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Bud. Bud neck.
Sequence:
MSSDKSIEKNTDTIASEVHEGDNHSNNLGSMEEEIKSTPSDQYEEIAIIPTEPLHSDKELNDKQQSLGHEAPTNVSREEPIGISGDEDTQITEQNVNEQRQETREPSSEIDLNEPLDVEKDVTTDVQAPNGLNIEKEYDAVKENEKVYADTKEVVSSPENREVTGKNSGGEKSSSSKFLDDESGTTTAANANDISISSEVTPERSSENDNNQIHITNEVAAGINLNENKEQKAAIEDGPVTAENLSSETARKVPPIPTQIINEKGDNSSENEVSAIPTTSSPPLPPRQNVATSTSPKLPPRGKQREQPPKTKNAVPPPLEEEMKSEKFRKNFEETKRNSYHHVPLTGSKTAQLESTAEINLIASRYRKTSHHLNKEGEETRESLQEGQSFLKSTFTSFLENLSEYNEVENVNEEDREMFKIDWSFWTQVVNDYATVASNEPENLEAHVTNGIPPQIRGIIWQLMANSKSREMEDIYETLLDTECLHEATIRRDLRRTKFVAEDKMESLYKVIKVYSVYDPDVGYTQGMGFIAAPLLINCENEAESFGLLVGLMKNYGLRELFLPGMPGLMLMLYQFDRLLEEHSPSLYNRLIREGISSTMYATQWFLTFFAYKFPLEFVLRIFDIVFVEGIEVLLKFAVNLMLKNEETLVKLRFDELLDFLKDELFNYYLMGNQDDASVVQMGLSNGNSFKGNDDGTFSYNVDLFVHDAMTGVYITPLTLRRYRGEYVEIHEKEQKKEDHYESLRIQNHQLQREAQKLEHDYSILNKENISAANELIQNRLNMEMLLDEKNDLINTITDIKSQIEEEIRKQNLPNPDASLPKADLREDLERTISRNNEVMRENGQLEERITELQAEIDELININKEQVSTASLLERDSKAKGRKGWTGFKKVFK
The following text describes a protein:
Function:
Involved in the biosynthesis of the O-methyl phosphoramidate (MeOPN) group found on the capsular polysaccharide (CPS) of C.jejuni. Catalyzes the formation of CDP-L-glutamine from CTP and L-glutamine phosphate. In the presence of MnCTP, catalyzes the displacement of pyrophosphate from CTP using phosphoramidate, methyl phosphate, methyl phosphonate, phosphate, arsenate, ethanolamine phosphate, (R/S)-glycerol-1-phosphate, glycerol-2-phosphate, serinol phosphate, L-serine phosphate and 3-phospho-D-glycerate as substrate in addition to L-glutamine phosphate.
Sequence:
MNAIILAAGFGSRLMPLTKDQPKCMVEYKNKKIIDYEIEALKSAGINEIAVVGGYLNDVLKNYLNKYDIEHFFINSKYDKTNMVHTFFCAKDFMLKCIEEKQDLIISYADIVYFQDCVQKLINAKEELAIVVDKSWCKLWSKRFANPLEDAETLKMTNGYIIELGKKANAYDEIEAQYIGLFKFSYQFLSEVIAFYEMLDRDILYDNKNFENMYMTSFLQALIEKYNNAKAVEIDGNWCEIDFMSDLEVQIEK
The following text describes a protein:
Function:
Catalyzes the cyclization of farnesyl diphosphate (FPP) to the sesquiterpene germacrene A.
Domain:
The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Sequence:
MNQLLCPGLYCPFPSQTNKYVDVLEEYSLEWVLRFNLLANESAYKRFCKSKFFFLAASAYPDSKFEELKITHDWLSWVFIWDDQCDLSELKKQPEVLNNFHQRYLEILNGAELTSQDTLFSHALIDLRKRTLQRASIKWFNYFISYLEDYFYGCVQEATNRAKGIVPDLDTYIMIRRSSVGVYAVLALSEFCNQFIIPDVLRNHHLVKKLELITTDIIAWSNDIFSASREIASGDVHNLIFVLHYHKKISLEKAIEQVVKIHNEEVHSLIKVESSLSFFSEELDVEITKYISGMHSWIRGNLDWCYESYRYHNLERLELTEFK
The following text describes a protein:
Function:
Transcription regulator that plays an central role in red blood cell differentiation. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA1 and GATA2. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. Acts as a repressor of red blood cells, probably by modulating activity of GATA1.
Subcellular Localization:
Nucleus.
Domain:
Some of the CCHC FOG-type zinc fingers probably directly bind to GATA-type zinc fingers. The Tyr residue adjacent to the last Cys of the CCHC FOG-type zinc finger is probably essential for the interaction with GATA-type zinc fingers (By similarity).
Sequence:
WNGPDELELEISSTDGVGHIRARNQLHKGFSWGPYKGNFTGSSSSPGPADLNISPSWDVDGDCWLKYVTLVSCEAEANAVLYRKGDLIWCKTSQIVEQDEVIQAFLKAEPQAIPNYTIKEEPGETSQCTSTLPEFQLLPQQAGMAAILATAVVNKDVFPCKDCGIWYRSERNLQAHLMYYCASRQSSTSPSMEEKAKDSYPNERICPFPQCKKSCPSTSSLEIHMRSHSGERPFVCLICLSAFTTKANCERHLKVHTDTLNGVCHGCGFISTTRDILYSHLVTNHMICQPGSKVDVYPVVKAVPAVKSSNPVVSQIASSSLLKCGLCGFLAEDFQVFNHALLHTTNPVPSATHSVKSPPENINEKQNPESQENGNAKSPISSSSSASSRSEETPLKLYIKQEPEGQLSISEAGSTTCEAKDGVALVQSPAIKVKTEMSSPTPGSSPVPNETGAATGGGTVIIPHYVFGHEATAAIVPQASEILAKMSELVHSRLKQGQAVTPAGFSGSAVPKGATCFECEITFNNINNYYVHKRLYCSGRHVSDENSSSARKVKALPARTALASGFSSTEQEASPPQEDAGEESSAPVVAVKLEENSGMDCEGAGSGHVSEGSQSPSSLDDPEEDPNRTVCGACNIRFSRHETYVVHKRYYCASRHDPPLRRREVNKPGPPYTTQPTPRTRKRRKLYEIHGVAPTESTPPSPHTLGRVEAMALMPGLIPAPVMPSPSSSPDAVDGPIDLSKKPRLVAEAPVPSAAATVAPLADYHECTACRISFNSLESYLAHKKFSCPTAPLQQKTIQQLQKVKSPSSATGKLVDDTVKVKVESKAALSPGSVSDTIQPLALPFSTISDPKQLQQYSSVTEASLSATTTCPYCPHNVIIRGDLLEHFRSVHGLILAKPTAGHRLQTTIMEVLVPARGQTSSASENSLPSPPVSSASPLQLPGLRRENSNYKDTTSSSSSVNGSPILTSTPRPLLPTSPAPPSNSLPLAESRREDGLPRVPSQVLLPGDKAMQPPKPSLISPVPNGNHRYCRLCNIKFSSLSTFIAHKKYYCSSHAAEHVK
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MDRLDAMKVFVLAVDEGSLAAAGRKLGRSPAAVSRAIAFLEERVGAELLHRTTRSIKLSEEGERYVAICRRVLTELEEADDIAAGPRAAPRGLLTITAPVVSGEMVLRPILDAFLDAYPTVSAKLLLFDRAVNLIEEGVDIALRIGHLADSAMVAMRIGEISRVVVAAPRYLKQHPRITELGDLAKHQIVAMAHLPNSWTFAPQAGSSAARTVQFTPRLVVNSTYAAVASAVAGRGVARMYSYQVAEQVARGELEIVLAADQDPEMPAHLICPQGRLSVPKVRAFTDFAVPRLKKQFALLKKSINAR
The following text describes a protein:
Function:
Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MPIYQLALPRSVLPRCRAVRYSRLLHSARCYSQDSQPKPGNTILQQLRKKLEPFCNSTKDKLEQTCAQVRYSSMQLRYHLEKARASVQEANKKLVQQEREGENSMLTFNDDLENKSKIVDLPSERERKRRQWSRKLEFYIDSLQETIFTATKALNDVTGYSSIEKLRKSIDMMETQLQETKRKLMQLREAHSDAVAVRNQSQRQVNELLQRKHMWSPGDLESFTRLYKEDADNVRRQEEANASLKAMEAKEEELSNSLHRAILTRYHEEQIWSDKIRRTSTWGTFILMGLNILLFLVVQLLLEPWKRRRLTNSFEDKVKRALEDHSLQHNLVLDRLSDRISEKIDAEMVHGIAPVPLPERTEQPEQPPAATTSGQPLGLREALASVGAAIAAEFGFFQAWIADHVRAIGGPTLSALQGFSGWPVLHIDLYNTVIFTCGMLLGLLVSH
The following text describes a protein:
Function:
Not known. It is a suppressor of protein phosphatase 2A depletion.
Miscellaneous:
MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
Sequence:
MTSALRVLVCGDHPNLILYTSRFQHAKNIEFYLVNNSKNANYEVSSLFYGTERFQIQNHFQSLLDLVDLNNENGGLVFDLIIMSASSLQEIPQVLRDIKPMMNKTTKILFESSGFIYLEPFIKASVDLSLSNIFSIFTDYDIRRLDNGSYKQFTTANAKSFSVSIGQTTSVHENSYSSDIIPILNTFQKLFQKLFPRDVVTLYDHSPSAFLAKEWELALPQICFDPLLIILEEKNPSTLDDHVLAKPLISGLLGESLLIIKKMGIAMNNPNFQNEQTILKHWKNKCEDLPDGPALLYNFIHKASSLNIDLLLLQPILLADDFGVKTPYLECLFTMMTQYQLLNKGDSEWFIRKDENTALTRVDDLQNSIALKDGKIMQLQNSESTLKNEIKELQSQVLSLKQEVSSSKANNGQELEILKKKVQMGDNSLFDRPNSNTNGISPSDNIVDVDLNYERSDQGNNSSGNDSRRQSFFNSTSDTTLSRDETSLKERELEVRMKELELQERELELQRKALQQQQQYQQRPPKQVYSGPSGTPTSGNNNNKSYNPNRKSSYSQPQHVAMMTSRGLHGPSAASSSPVISANNFVDPVSSGTPYSSNSSRFSQQIPSQQYMHTVKPTSRKNRSSVMPNIGYVPGLTNNEYGRKFNGNGMNGTQSRLNSLSNQSTFRSQQGPPITQQKSFQNNGGSMRTNRIPSANYNISNQQSGFVNSISSPNLSNLENRNTVQNSRNADSAPCVNQLNSDSPPQLQSLSQNGTSKVPQINITQPSPIQTNFATSDNPAAVIKLGTPSEDTVSAAATANNISTMGDESRKEDVKEKKKKKFSFFGKRKK
The following text describes a protein:
Function:
Plays a role in the recruitment of the exosome to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Nucleus.
Sequence:
MTDSASTTAEKASENATIPPEVVAKLKTFNDALTALENALEPHLKADFEEHMNRDPTELARIDLMSLFTVNSLSWSLLALKGQDPRKNEALQAELDRTKAYGNRLKIEESRREHSGVNEKVAKALVRNALFDAQEYGDKKKTKK
The following text describes a protein:
Function:
Deamidates N-terminal Asn and Gln. Component of a targeting complex in the N-end rule pathway.
Miscellaneous:
MISCELLANEOUS: Present with 1640 molecules/cell in log phase SD medium.
Sequence:
MLIDAIHGAKMSTKLLVSLKVLVIQLNPQIGQVDQTIKRTWSILDKVTKSATYVKPDIILFPEFALTGYSFHARKDILPYVTKKDEGPSFELAKSISEKFQCYTIIGYPEDDDEQKLYNSALVVNPQGEQIFNYRKTFLYDTEMNWDCEENPEGFQTFPMDFSKCAKLSNEDSYNRDVTLKASIGICMDLSPYKFMAPFNHFEFSSFCVDNNVELILCPMAWLNSTSITDKQTLHNNSLLEAAKNKIAFALKEQGLPLAGSQGIYQLKIGDSQRTPRVPSDDSTSEYKDMDEPDMSNVNYWILRFFPFLYFKSRINWFKNSSLIESILGKTRMPLDHEYYKDGKHKEDTIDLLDSEEVIKDTVLEKTFLGTSLGQPWKFQGKNAILVLANRCGTEDGTTIFAGSSGIYKFNGKKPKGSQDDDESSLDSLNESVELLGNLGKGLEGAILREVQFEVFR
The following text describes a protein:
Function:
Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression.
Subcellular Localization:
Cell projection, filopodium. Cell projection, microvillus. Cell projection, ruffle. Endomembrane system; Peripheral membrane protein.
Sequence:
MSSDLRPKLCVLEKGDTGYGFHLHGEKNKPGQFIRHVEPDSPAAAAGLLAGDKLALVNGENVEDEKHQQVVSRIRDTVGKLELVVLNAETAELLLKHNLKCQKEYVTDGIPIPAGSEPEDEVKNGTSSRESTPVPETNGDMRIDRLSVSSKDSKNELRPRLCHIKKGATGYGFNLHTEKTKPGQYIRAVDEDSPAEKSGLRPQDKIVQVNGISVHTMQHSEVVAAIKAGGDETKLLVVDPEADAFFMSCEILPTEEHLTGPLPEPIPRREAEEQVNGKVVQEEKPKVEMSLSSSSTSSNTSTSAAPAPASAPAPASAPAPASAPAPAMAAAPQEKVKEKASSADAGLALNMSLQQAKERAHQKRSNKRAPQMDWSKRNELFSNL
The following text describes a protein:
Function:
Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif (By similarity).
Sequence:
MSSRLHNGNDVYEKAEEYWSRASQDVNGMLGGFETLHTPDITVSKRFIEGLKKRNLFGSYDYALDCGAGIGRVTKHLLMPLFKKVDMEDLVEELIVSSEQYIGSDPRIGEKFIEGIQTFAPPERRYDLIWIQWVSGHLVDEDLVAFFKRCVKGLKPGGCIVLKDNVTNHEKRLFDDEDHSWTRTEPELMEAFNGADLDMVVKTIQTGFPKEIYPVKIFALKPRRQETSDDN
The following text describes a protein:
Function:
Involved in sporulation and affects the sphingolipid composition of the plasma membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSYKKFVYFINLFFLLGATLLTFFLILAGGRTTGVLKNFYWFQASTSGFNSAPSVTRWYNYNWCGWESRGIAVNCSSKMAAQPFSPRDNFGSSPLMPSTFLNNRNAYYYLSRVGWAMLLIGLFFLLITLVSVIASLIRYNRRTAALATAMSWITLFFITLSACLYTGCYAKAVKAFHHENRDARLGPKNFGLIWTTVFLLIVNAICCTIMVATHKRNEYIYDRSFASTKTVDSQTPTPVPTNGGIPSSVPVTEVQQSQSHQNHRFFKKLRTKKRTVTSAGDEPDRVQEERVYTEQNVPVVS
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP53 may play an important role in cell cycle regulation by inhibiting PSE1 transport functions during mitosis and sequestration of MAD1-MAD2 in a cell cycle-dependent manner. It also seems to play an important role in de novo NPC assembly by associating with nuclear membranes and driving their proliferation.
Miscellaneous:
MISCELLANEOUS: Present with 2060 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Domain:
Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side; The RRM Nup35-type domain might be involved in the control of mitosis.
Sequence:
MADLQKQENSSRFTNVSVIAPESQGQHEQQKQQEQLEQQKQPTGLLKGLNGFPSAPQPLFMEDPPSTVSGELNDNPAWFNNPRKRAIPNSIIKRSNGQSLSPVRSDSADVPAFSNSNGFNNVTFGSKKDPRILKNVSPNDNNSANNNAHSSDLGTVVFDSNEAPPKTSLADWQKEDGIFSSKTDNIEDPNLSSNITFDGKPTATPSPFRPLEKTSRILNFFDKNTKTTPNTASSEASAGSKEGASTNWDDHAIIIFGYPETIANSIILHFANFGEILEDFRVIKDFKKLNSKNMSKSPSLTAQKYPIYTGDGWVKLTYKSELSKSRALQENGIIMNGTLIGCVSYSPAALKQLASLKKSEEIINNKTSSQTSLSSKDLSNYRKTEGIFEKAKAKAVTSKVRNAEFKVSKNSTSFKNPRRLEIKDGRSLFLRNRGKIHSGVLSSIESDLKKREQASKSKKSWLNRLNNWLFGWNDL
The following text describes a protein:
Function:
Transferable epigenetic modifier which forms a prion responsible for the non-Mendelian trait [PIN+]. The native function of the soluble protein is unknown.
Miscellaneous:
MISCELLANEOUS: [PIN+], also known as [RNQ+], is the prion form of RNQ1. [PIN+] is the result of a conformational change of the cellular RNQ1 protein that becomes self-propagating and infectious. This conformational change generates a form of RNQ1 that assembles into amyloid fibrils. [PIN+] promotes de novo [PSI+] formation upon SUP35 overproduction (cross-seeding). [PIN+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PIN+] propagation; MISCELLANEOUS: Present with 1140 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.
Sequence:
MDTDKLISEAESHFSQGNHAEAVAKLTSAAQSNPNDEQMSTIESLIQKIAGYVMDNRSGGSDASQDRAAGGGSSFMNTLMADSKGSSQTQLGKLALLATVMTHSSNKGSSNRGFDVGTVMSMLSGSGGGSQSMGASGLAALASQFFKSGNNSQGQGQGQGQGQGQGQGQGQGSFTALASLASSFMNSNNNNQQGQNQSSGGSSFGALASMASSFMHSNNNQNSNNSQQGYNQSYQNGNQNSQGYNNQQYQGGNGGYQQQQGQSGGAFSSLASMAQSYLGGGQTQSNQQQYNQQGQNNQQQYQQQGQNYQHQQQGQQQQQGHSSSFSALASMASSYLGNNSNSNSSYGGQQQANEYGRPQQNGQQQSNEYGRPQYGGNQNSNGQHESFNFSGNFSQQNNNGNQNRY
The following text describes a protein:
Function:
Involved in the biosynthesis of ent-kaurene diterpenoids natural products. Catalyzes the conversion of ent-copalyl diphosphate to ent-pimara-8(14),15-diene.
Domain:
The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Sequence:
MILPMSSACLGQFLRASPRGMIEQFNRAPPLRVSIRGAAGVEKSLGLGRNAGSQQGMQKNQLQDKIRKQLREVQLSPSSYDTAWVAMVPVQGSHQTPRFPQCIEWILQNQHDDGSWGTNLPGSVVNKDILLCTLACVVALKRWNTGRDHISRGLNFIGKNFWVAMDEQTIAPVGFNITFSGLLNLATGTGLEFPVMQTDIDGIFHMRKIELERDAYGTASSRRAFMAYVSEGLGSLQDWDQVMAYQRKNRSIFNSPSAAAATVIHGHNDSALCYLDSLVSKLDGPVPVMYPQNAYSQLGMVDTLEKMGISNNFSCEISDILDMIYRLWIHNEEELMLDMGTCAMAFRLLRMHGYDISSDGMAQFVEQSSFDDSIHGYLNDTKALLELYRSSQIRCLEDDLILQDIGSWSARVLQEKISSKMTHKSEMLEVEYALKFPVYATLERLEQKRNIEQFKTKEQLKIEGFKLLKSGYRGAITHDEILALAVDEFHSSQSVYQQELQDLNSWVAQTRLDELKFARLMPSITYFSAAATMFPSELSEARIAWTQNCILTTTVDDFFDGDGSKEEMENLVKLIEKWDGHGEIGFSSECVEILFYAIYNTSKQIAEKAVPLQKRNVVDHIAESWWFTVRGMLTEAEWRMDKYVPTTVEEYMSAAVDSFALGPTITSAALFVGPELSEEVFRSKEYIHLMNLANTIGRLLNDMQTYEKEIKMGKVNSVMLHALSHSGGGRGSPEASMEEAKREMRRVLQGSRCDLLRLVTRDGGVVPPPCRKLFWFMSKVLHFVYMEKDGYFTADGMMASANAVILDPLQVTLLPSGLGTL