lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MLLWLVLLAFCAGLMPIVALLCICIYISAYRSCSHSSNSKPCLGRSAAVVVLGDIGRSPRMCLHVESLANEGWKVAIVGYAGSTLPPALQRSSIKQHHLRSPPSWIARMPRAAFIAVAPFKLLVQAVSLFVELTTQVHPPPELILVQTPPALPTLLVVKAAAALVKSRVVIDWHNLAYTILALRLGEKSKLVRLAEWLEKWSGRKAFAHLFVTEAMKNHLDLNWKLQGDKLVLHDRPPAHFRRATLEETHSLMCKVLPQIVPSIGDDWLPSCNLPDSTPFTQRTDGGELQWSQDRPALVVSSTSWTADEDFGLLLRAAKLYEYRARLLAIQSSLPPHSRSSSTAETVSATLSPVSASSCSSASTTSHFSYTDIADPIRTSKERRRPSIGALRTPTLPNEPASSLPKLLIIVTGKGELKARYLAEIAHLEATEAWQFVRIRTAWLESQDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMLGCGLPVCALDFACLDELVCERWNGVVFRDAEGLARQWESLLANHPLPNWLSTGGGMQEPFDPPARSVLTPKTGWLCEPGNTSAPPMSPNPSLTLVPSPGFAPWSNETATNKAKKSPRSTWPGNWKHVMRPLLDPRTDMDEHDENTVDDYLSHTSAIKLNAISAGILQRRAVSKQGYVAAATSPASSDTQRGSASKRKNSTDPQIDHDDQIATRSAPWNGFGFVSQAAVISDGESQKGLRQRKSVSKPSTDLTQQQHAFNLTLLDDALHDNRSTTDSQDQSSIPAIQVSKPPSPP
The following text describes a protein:
Function:
DNA ligase involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair.
Subcellular Localization:
Nucleus.
Sequence:
MADEGGLETGAHDELKGTEEQAVNFAPSPDFLWLCEQLFAKIDHVQFERANNLLTKPVTARYYEVISNFTTLWRTTVGNNIYPALRLILPYRDRRVFNIKDYTLIKAICAFLKLPKDSSTEKKLINWKQDAGRSVRLSKFCVEEIKKRRSEPQIDRNERITIDDLNGYLDQLAIERTEQGRSFKNLANSDIMNKCLTSMTFLEMQYFFDILLKNRPLGGHEHKLLNCWHPDAQDYLSVVSDLETVAKRLWDPSQRLGNQDLKINIGLAFAPQLATKLHVSYQKIGEKLGWDFFIEEKMDGERIQMHYTNFGSDIKFYSRRATDYTYLYGNNLKTGTLANFINLNKNVKDCVLDCEVVTFDSNNKIVLPFGMVKSSAKNMLSQDGIDTQGFHPLLMVFDVLYLNGATLVDLPYYKRREYLKQILTPTAHRIEIIKSIRANDEQMIKKSLEKALSVGSEGIILKRYDSRYVIASRSDDWIKIKPEYLEQFGENMDLVLMGRDPSKKDSLMLGLLDYEEVIQDSPIMVNSQSSEENSQRFRGFVSLCIIANGISNEEYKEIDRKTKGLWNDSEKIPPLEYMKFGSKVPRQWIDPKKSLILEIKARSLDNTRSSERKFAAGCTLFGGYCRQIREDKNWKTCYTLQEFERAKSGNNWRKRGSSKPQKVISKKRRYNIISSVNKALEDFAELEHRSDIFDGMYFYVLSDYFDGVKRKRIKKSEIQKVIVANGGQLVQNVITRNYNLNDLRIISSRNTVECNSLIVRGYDIISPKWVFDCLLSGKIMKLEPSHCFNFSKQLMDYAYKRIDQYGDPYERDINKYEWSSLTSEKICTTAKQQPDVQFDNSLMDVPHFLFHGRIVFLLSDNNNIQKESFMVDAYGGKVTNELSSANLVIVVGAVTQRRINDIRKQISSEVIKQDHPPRIPDMVSEGWLYDCIKQNTQVAEDNYRLP
The following text describes a protein:
Function:
Involved in cytoskeletal organization and cellular growth. May exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins such as profilin or proteins possessing SH3 domains. Plays a role in actin patch assembly by enhancing the ability of myo1 to stimulate actin polymerization by the Arp2/3 complex.
Subcellular Localization:
Cytoplasm, cytoskeleton. Note=Localized to patches at the tips of growing interphase cells. These patches form prior to patches of myo1, but in cells lacking myo1, they are less intense and may be short lived. Detected in the medial region of mitotic cells, and this requires cdc15.
Sequence:
MAPAPPPPPPAPAPAAAAPAPPLMTGDRSALLNSIQKGKKLKKATTNDRSAPVVGGGVVGERKSNTPKSFAAPPVPTGAPSLPTSSNNTQQAEERPSMPALGGLFAGGMPKLRHIGKSSASAAPPSAPAPPTPQSELRPPTSAPPRPSIPPPSPASAPPIPSKAPPIPSSLPPPAQPAAPVKSPPSAPSLPSAVPPMPPKVPPPPLSQAPVANTSSRPSSFAPPAGHAPNVTSESPKFPNRGPSIPSASVPPVPPSSYVLQQRPNRVDDHGRFHFKDDSYLPIPHPFLGVPKVYRGGSGTTVPLNLSSF
The following text describes a protein:
Function:
Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin. Active against linseed rhamnogalacturonan.
Subcellular Localization:
Secreted.
Sequence:
MRLGVCFSLAAAASVARAALTATENDTSIVLENDRLRATFDKGRGSIIDLYLDGQDFLGPQSGSTGIGPYLDCYCTPSGFYTAGSTNPVTELVQGTDSTGTKYAGIILNDTYTPTGQEFQQYWFLRDGETGFHMFSRLAYYNETTPFLRNLQELRTLFRPNTDLWTHLTSSDLQTAPLPSDEAIAEQIVVQDATWRLNNTPDDAYYQQFSEYFTKYTFSNHWRDNDVHGLYADGSTSDGTTYGAWLVMNTKDTYYGGPLHSDLTVDGIIYNYIVSNHHGEGTPNITNGFDRTFGPQFYLFNGGGSSSLEELRDEARSLASPSWNADFYDSIAKHVIGYVPSSQRGSVKGTIKLPKNAKSPIAVLTVDGHYFQDNSAVPSSHQYWADIDKNGRFSIDRVVAGKYRLTVYADGIFGDFTRDGIVVKARKSTSIKETWKPESAGTEIWRLGTPDKSSGEFRHGAARDPTHPRHPPEYLIYWGAYDWQSDFPGGIDYMIGESDPATDFNTVHWAVFGPTPDNPVAESNTTHDWRIRFDLSAKQLHARKTATLTIQLAGAKAASGNTDVYNASEPYANLPLRSYINEQEEPLTMVIGYDQSSSCIVRSAVSCYQVREKWEFPASWLKEGSNLLRLSLPTNGTNYESAVLPTSVYVQYDALRLELK
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
MTEQLASMPEESTIGFTAPCRPRTSYHELIQAVPVSGSPIRWSLPNSQSGRNGLSSYSSSGASNSCPSNNSGNSSGTISVSAAIVDNGELTRIAHQMVNDGYIWHTVQAFDDASSAPAAFKHGGGVRGHALENWFLELDIDWVLQIDDEHGLRRLLRDKPVTTQELIDKWVRALTVIVASITETEYEFAFHRTPAVALFGKASITEMLNVVDVIVTALEAKKLQAVLDMFTCVCGTSHMIRPVMISREAQSIFKELGNSLEREGIRLSEIISNSTKEVRTLVEEDDSWAIEILRGRGEVHKNTRFIMDCIVSMTIARTSMHNSAPSNNSENLDGLIDIEYLEDLLLRKSWLLLDPSLRYLFLLNNSYFVAHVVSESSGSFIPDDPWDLTPKLTPECKKYMDSYLDFSWGHVLSCIPKSRSLGLIHRLVNTPSLAKFQSAFHETYQAQKFWKVPDPRLREALRRAIIERVITGYRNYLEEHPELEKHVGRQSSSPQVLEEMLGELYEG
The following text describes a protein:
Function:
Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MTDVQQTSNQKKSDLAQDIADAEISRTLRKAKVSAAFRYIVLIIVGLLMLYPLLWMFSAAFKPNNEIFTTLGLWPEHPTSDGFINGWKTGTEYNFGHYMLNTFKYVIPKVILTIISSTIVAYGFARFEIPWKKFWFTTLITTMLLPSTVLLIPQYIMFREMGMLNSYLPLYLPLAFATQGFFVFMLIQFLRGVPRDMEEAAQIDGCNSFQVLWYVVVPILKPAIISVALFQFMWSMNDFIGPLIYVYSVDKYPIALALKMSIDVTEGAPWNEILAMASISILPSIIVFFLAQRYFVQGVTSSGIKG
The following text describes a protein:
Function:
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Subcellular Localization:
Cytoplasm.
Domain:
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Sequence:
MNILIFGPPGSGKSTHSRTIMEKYGLVYISSGDLIRREIERKSSLGREMEAYLSRGDLIPDTIVNTLIISKLRRQRENFILDGYPRTPEQVISLENYLFDHGIKLDLALEIFIDEDTSVERISGRRICPNCGAVYHVKYNPPKVPGICDVCGSELIQRADDREEVVRKRYRIYSKNMEPIIKFYRAKGIYVRVDGDGPISEVWKRIQPLLDYIHSREEKRKEHE
The following text describes a protein:
Function:
Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the first outer-core glucose from UDP-glucose to the inner-core heptose II. Cannot use other sugar donors, such as UDP-galactose, UDP-glucuronic acid, UDP-galacuronic acid, GDP-mannose, ADP-glucose and GDP-glucose. In the absence of a lipid acceptor, can slowly hydrolyze UDP-glucose.
Miscellaneous:
MISCELLANEOUS: For the in vitro assay, an inner core analog, heptose2-1-dephosphorylated-Kdo2-lipid A (Hep2-1-deP-KLA), was prepared and used as the acceptor substrate.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=Binds membranes via electrostatic interactions. Interaction with the membrane is conferred at least in part by the N-terminal positively charged and largely alpha-helical membrane-interacting region (MIR-WaaG).
Sequence:
MIVAFCLYKYFPFGGLQRDFMRIASTVAARGHHVRVYTQSWEGDCPKAFELIQVPVKSHTNHGRNAEYYAWVQNHLKEHPADRVVGFNKMPGLDVYFAADVCYAEKVAQEKGFLYRLTSRYRHYAAFERATFEQGKSTKLMMLTDKQIADFQKHYQTEPERFQILPPGIYPDRKYSEQIPNSREIYRQKNGIKEQQNLLLQVGSDFGRKGVDRSIEALASLPESLRHNTLLFVVGQDKPRKFEALAEKLGVRSNVHFFSGRNDVSELMAAADLLLHPAYQEAAGIVLLEAITAGLPVLTTAVCGYAHYIADANCGTVIAEPFSQEQLNEVLRKALTQSPLRMAWAENARHYADTQDLYSLPEKAADIITGGLDG
The following text describes a protein:
Function:
Component of a multiprotein complex equivalent of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MSPPVAGAASSGDGPPGRPPRELYTIPASSGWFQWDEIHETERRALPEFFGGAGGSGFGTASRNPRIYREYRDYIISRYREDTSRRLTFTEVRKALVGDVTLLRKLFAFLDSSGLINFSASPSRPEAQQQQRQTEAEAVVEAPVGLQVTPRPPPSYFAEEKGGGGNENGFRLPPLTSYSDVFGEWAPGMAPICGLCGMECRDGNAQILKDGFKVCSKCYANNDNKGEANIHPGDKKERIDNHSSSAWTDAETLLLLEGVLKHGDDWDLIAQHVRTKNKSECIARLIQLPFGEHMLGTVNGKLDNRLHKIQTTDGKVNKSTVKESSSQPTETVDDMQIDGNEDGADKSVEEHPTKHRRLFSSIDITVSLMEQLAHLTTSTSPDVVAAAADAAIKALGNENPQARRAFQLSEKEYQTRAFSSNHARQSDDVGGGDRDVEMHGHPDKKQGKMFISTTYQVRAAVATSIGVAAARAKMLADQEEREMELLMASIIETQLKKIQYKIKHFEELELIMDQEYATLQQMKSSLVDEWQKVLKRAFETGVPISRDEVLIKLFQNKPNL
The following text describes a protein:
Function:
Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. May play a role in wound healing.
Subcellular Localization:
Secreted.
Sequence:
MWKWILTHCASAFPHLPGCCCCFLLLFLVSSVPVTCQALGQDMVSPEATNSSSSSSSSSSSSSFSSPSSAGRHVRSYNHLQGDVRWRKLFSFTKYFLKIEKNGKVSGTKKENCPYSILEITSVEIGVVAVKAINSNYYLAMNKKGKLYGSKEFNNDCKLKERIEENGYNTYASFNWQHNGRQMYVALNGKGAPRRGQKTRRKNTSAHFLPMVVHS
The following text describes a protein:
Function:
Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for a distribution of the CatSper complex in linear quadrilateral nanodomains along the flagellum, maximizing fertilization inside the mammalian female reproductive tract. Together with EFCAB9, associates with the CatSper channel pore and is required for the two-row structure of each single CatSper channel.
Subcellular Localization:
Cell projection, cilium, flagellum membrane; Peripheral membrane protein. Note=Specifically located in the principal piece of sperm tail. Although it does not contain a transmembrane domain, localizes with the CatSper complex at the flagellum membrane.
Sequence:
MEESVKPVPKHANHRRSSVRSSLYGDVRDLWSTATMSTANVSVSDVCEDFDEEGKSVRNRIRKYSQTISIRDSLNLEPEEIQQQARRELELCHGRSLEHGEDHEESETSLASSTSESLIFSLWKPHRTYWTEQQNRLPLPLMELMETEVLDILKKALITYRSTIGRNHFMTKELQGYIEGIRKRRNKRLYFLDQ
The following text describes a protein:
Function:
Part of the ecpRABCDE operon, which encodes the E.coli common pilus (ECP). ECP is found in both commensal and pathogenic strains and plays a dual role in early-stage biofilm development and host cell recognition (By similarity). Positively regulates the expression of the ecp operon by binding to two TTCCT boxes.
Subcellular Localization:
Cytoplasm.
Sequence:
MTWQNDYSRDYEVKNHMECQNRSDKYIWSPHDAYFYKGLSELIVDIDRLIYLSLEKIRKDFVFINLNTDSLTEFINRDNEWLSAVKGKQVVLIAARKSEALANYWYYNSNIRGVVYAGLSRDIRKELAYVINGRFLRKDIKKDKITDREMEIIRMTAQGMLPKSIARIENCSVKTVYTHRRNAEAKLYSKLYKLVQ
The following text describes a protein:
Function:
Involved in non-homologous end joining (NHEJ). Facilitates the transport of LIF1 into the nucleus, where it can interact with DNA ligase DNL4 to repair double-strand breaks (DSB). Mediates mating-type regulation of NHEJ. Prevents chromosome circularisation by NHEJ in absence of telomerase.
Miscellaneous:
MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus membrane; Multi-pass membrane protein.
Sequence:
MDSELKGQQLSDAEWCVKKINGEGNCLLLFLPMSSPTTIVMIVLVSLERLVPYVFKLSQTQLSQQCQSQGFTDSISLNLIKLKLMDILQAPQEINQIGLVDSNLVFSFDVSADITVSINSVPSHVTKDMFYMILQSLCMLLLKLVNLSTQYHYVQRDILNEKQKCLDFLLISLRDLDGGSKVISQWAPENSKNYESLQQCTDDDIIKKLLHKGKFQHQEFLADSLKTLLSLRNKFQDVSRFEESGELNKKERVRFPAVNHFYNDDFELQADPTNEARPNSRGKIKPKTDFKPKSRESSTSSQLRLENFSESEATPEKTKSSSSLVEEYPQKKRKFGKVRIKN
The following text describes a protein:
Function:
Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress conditions. Key activator of the integrated stress response (ISR) required for adaptation to various stress, such as heme deficiency, oxidative stress, osmotic shock, mitochondrial dysfunction and heat shock (By similarity). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming (By similarity). Acts as a key sensor of heme-deficiency: in normal conditions, binds hemin via a cysteine thiolate and histidine nitrogenous coordination, leading to inhibit the protein kinase activity (By similarity). This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell: heme depletion relieves inhibition and stimulates kinase activity, activating the ISR (By similarity). Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions (By similarity). In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties (By similarity). It thereby plays an essential protective role for RBC survival in anemias of iron deficiency (By similarity). Iron deficiency also triggers activation by full-length DELE1 (By similarity). Also activates the ISR in response to mitochondrial dysfunction: HRI/EIF2AK1 protein kinase activity is activated upon binding to the processed form of DELE1 (S-DELE1), thereby promoting the ATF4-mediated reprogramming (By similarity). Also acts as an activator of mitophagy in response to mitochondrial damage: catalyzes phosphorylation of eIF-2-alpha (EIF2S1) following activation by S-DELE1, thereby promoting mitochondrial localization of EIF2S1, triggering PRKN-independent mitophagy (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MLGGSAGTRGGEAEGDGAGAVGAVAPPPAIDFPAEVSDPKYDESDVPAELQVLKEPLQQPAFPFAVANQLLLVSLLEHLSHVHEPNPLRSRQVFKLLCQTFIKMGLLSSFTCSDEFSSLRLHHNRAITHLMRSARERVRQDPCADNSHIQKIRSREVALEAQTSRYLNEFEELSILGKGGYGRVYKVRNKLDGQYYAIKKILIKGATKTDCMKVLREVKVLAGLQHPNIVGYHTAWIEHVHVHVQADRVPIQLPSLEVLSDQEEDRDQYGVKNDASSSSSIIFAEFSPEKEKSSDECAVESQNNKLVNYTTNLVVRDTGEFESSTERQENGSIVERQLLFGHNSDVEEDFTSAEESSEEDLSALRHTEVQYHLMLHIQMQLCELSLWDWIAERNRRSRECVDESACPYVMVSVATKIFQELVEGVFYIHNMGIVHRDLKPRNIFLHGPDQQVKIGDFGLACADIIQKNAARTSRNGERAPTHTSRVGTCLYASPEQLEGSEYDAKSDMYSVGVILLELFQPFGTEMERAEVLTGVRAGRIPDSLSKRCPAQAKYVQLLTRRNASQRPSALQLLQSELFQNSAHVNLTLQMKIIEQEREIEELKKQLSLLSQARGVRSDRRDGELPA
The following text describes a protein:
Function:
Plays a key role in early steps of protein N-linked glycosylation by being involved in the conversion of polyprenol into dolichol (By similarity). Acts as a polyprenal reductase that mediates the reduction of polyprenal into dolichal in a NADP-dependent mechanism (By similarity). Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAPPENGILEVLENLLDRYKINLLQMMFGTFIATIVFFGGLMTFVEKYLPNSIRQSFRYGKHSFKGETDPLVAWLEVPKSWFKHFYTFALFWSWLAFYVLVSTVREQKEAPEYVLQFLDIMGGGRSHRKVEIDSTTACVGAFMLTLQCTRRFYETNFVQIFSKKSKINLSHYAVGYVHYFGAVIALLSNTSGFVRGSKPMEFSLDKLTSQQILYLGVFFLAWQQQYASNMILVNLRKDPRTGSVKTEKHLLPKGGLFNLLSSPHMFLEVVMYFCIADLYMPVRIWRLIFLWVASNQTINALLTHKWYQETFREYPKNRRAIIPFLL
The following text describes a protein:
Function:
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins.
Subcellular Localization:
Nucleus.
Sequence:
MSEKKQPVDLGLLEEDDEFEEFPGEDWAGLDEDEDAHVWEDNWDDDNEEDDFSNQLRAELEKHGYMMETS
The following text describes a protein:
Function:
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGRPKLNPPKVGRRPISDKIFKVGATVAGVYVLVVIVLLAFQLISESAPIWDEYGLSFIVKSEWNAIDDRQDFGVLPYIFGTLVTSALAMVIGVPLSIGIAMFISDAPSKIGGPLGFLVELLAAVPSVIYGLWGLFVFRVYFVDWVEKPLHNTFGDSIWLFSGTPFGLDILTASVILAIMIIPTVSAVSREVMKAVPQQQKEAAYMLGATKWEMFKLAVFPYSKTGLIGASILGLGRAVGETMAVTMLIGNATGPNAFADSLFDPSQTMSSIIANEFNEASLGTLHLPALIGVAVVLLLIAIAINVVAHILVTRMLKVKEGAINN
The following text describes a protein:
Function:
Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton. Modulates the expression of IL2. Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2. May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells.
Subcellular Localization:
Cell junction. Cytoplasm.
Sequence:
MDGKADVKSLMAKFNTGGNLTEEVSVGNRPFKVGGHSSPSGIQARKSVFTNQGNASPPPGPNNSSKFGTPRPLLGVKSSFEEKTDKDPKPPYLKPTGAGQRFGTPASSASREPEGKVGFLKPVGPKPFDQPKEDAKPVFPRPSGNKPLLHAVNQENDVKTPSPKSVFNAPAQENEPKPVFPKLAAAKGKFTSPQDHDSKPPFTKPAIGQKPSANTDTSHEDQSPSKSTFPQKGPAFAPPSKPKISTPKPGKEDTENKDHATDLPNMPFPGVTLKPAASRGTPGSSLNLPKNTEEKKEERKIDAAKNVFMSKMNQDDSGSGAPPPKFSKPPSKLVVGGPWNQSQEKEKGEKNSTAPKQKPLPALFTLGPAPQKPNRPPTIDLARFRKASPANSPSKGTAPYSGATSPPPPPPPPAHPTTQPVAPVPPVPYPTQPPVPSLPPRNIKIPPDPKSLTNEENYDDVDMQSNDLGNPDEDQESDGETYEDIEATKEREKKKDKEEKKRLEQEKKEQKEKEKKEQEIKKKFKLTGPIQVLHQAKACCDVKGGKNELSVKQGEEIEIIRITDNPEGKWLGRTSRGTYGYIKTTAVEIDYDSLKRKKNSMSTLPSKLMEDDQELYDDVAEHGSVSSHSQSGSGGVFPNQGDEIYDGIEDDDDNGSTLQVDDEKSNPWTWGILKMLKGKDDKKKSIRKKSKDTESDSNEDVAFPSPPKQLGLDVGDEVYDDVDSSDFPAPPIEISAGVNFGKGRLEEKDLKKLKKQEKEEKEFKKKFKFDGEIRVLYTTQVVPTLTSKKWGTRDLQLKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSCLVDNEGEIYDDIADGCIYDND
The following text describes a protein:
Function:
Acts as a component of the core factor (CF) complex which is essential for the initiation of rDNA transcription by RNA polymerase I. After binding of UAF (upstream activation factor) to an upstream element of the promoter, CF is recruited in a SPT15/TBP-dependent manner to form a preinitiation complex.
Miscellaneous:
MISCELLANEOUS: Present with 237 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MSEGQIPSSDVLGSQLGVGVQGASLYCPQENYTTKKQEKPQWLRPVDDTLAEDALDLHIVVKSLLCDTAIRYISDDKVLQESDADDDLITSDIDEDTDNQGDTSIVVNPVIPVVPKDVHFFKKVDVGNDSMFGVNCDTPVSFQDYIPSDLLRNLDDTLQESTNSSRPMQDAFFWDPTVANRLDSQYIQTASDLRNYRDGTEIIAYASGKTGSVLNIAVLTRQNTLHLNRHNNVTSIELHSPIKSIKIPGASESIGRRSNLVGIITENSFQIFRIESVHSRSCDVMVSSSEPLYFVEIDDLQVVDFAFNPWDLQQFAIIDIKGNWSIGRIPKNFNNNNKRKLQLIDNLHGTIFDPEELSSWKRIEWFSHFQKILVFDRSKMIEIDFMNNWQTEVVQAKAWSNIRDYKRIDDKNGILLTSREIIIVGASESNDPVRRISWKHDLDPDDTTLRITVQKVKKPDHILLVAFVYSMRHKRIYMHVFSHRKANLFQSLGCSTVLEIPGGTPTGIETILTLDHIDDESRREEDADENFELVVDFLVKLRNSSEVYYYALSNTQNSEPNKQETPIIVDHPEWASLFNNADEREKESIGALVSQIKLKERERISRVQNLIEHENSHDEDKYLQDLGYRLSIATNELLESWQKTKDESILSGSLSHSKLKNLLENSDSFASIPEFSSLLDQFFQYYQDQDVTFIGFEKLLHLFLHEDVPGLDIFYNKLLQCWVLVSPQAELLTKEIVKDIIWSLARLEKPSLFEPIQNEISRSLSGPYQDIISSWDMDDINEEDESNEFNFDSQFSAPFNGRPPFNLNSQSQIPTIKSSQSSGLARRKRILKTQSQKATPLSQSTQNLSVLPDSMTPAFTLMQPPSSQISFVNDSQPRNSQKAKKKKKRIRGFG
The following text describes a protein:
Function:
Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. Acts as a negative growth regulator (By similarity).
Subcellular Localization:
Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Late endosome membrane; Peripheral membrane protein.
Domain:
The UEV domain is required for the interaction of the complex with ubiquitin.
Sequence:
MYGHHGYPMHAHQQQMVNPTLAIVDNKMHTLSTFLNYIRAYRDPLRISKDLKETFHLFPNLSPFYENIPNRVNLICIKGTIPICFKGINYYLPIIVWVPLNYPQEFPTMVLDPTPEMRIVKNHHHVNLQGLVYHPYISSWSSNSTMETRVSQQQQPQPPQNNISPPPYGSSPTNNNVAAQQQQPPPPYGSSPSTSNSSSYTQPPPSYDSIKNKTNNTSSLPPPKQPQTSPPPPPTQQQQQQQNNNIIPPPQQPSPPPAYTEPTAAKQQQQQTSPSVKPLPPLPPQPVIDKKSEMVDQCTIKLQELLSKFYDTTSLEIKDFEAHNKSLEELSKKKLLEKEELSNQLATYNSQIDQLNENIEQLEKWINENDKSDSNIDIDQILGPKDSLSKQLLKLVSDDSTIEDLLYYLDKALHSNRISLEEYLKNVRSLSRDQFIIRATVKKVQFIIRQNQQQLQQQQQQQNSPQRQQYNQQQYFSK
The following text describes a protein:
Function:
Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MAHLPLTCLLVLASAHAVFSSGMFELKIHSFHTAQRICRRHRDCHIFFRICLKHPEDVISAEPPCTFGTGHTNVIRADHTSISSSAPIRVPFHFKWPGTFSLIIEAWNAESPTEYTDNQNNLVSRLATRRRLAIGEDWSQDVHFGEQSELRYSYHVFCDEYYFGDGCADYCRPRDDTLGHYTCDEEGSRVCLEGWKGNYCSEPICSADCSERNGYCEAPGGCTCRMGWQGPSCTECVRYPGCLHGTCGQPWQCNCQEGWGGLFCDQDLNYCTNHKPCANGATCSNTGQGSYTCTCRPGFGGTNCELETNECDSNPCKNGGSCNDLENDYSCTCPQGFYGKNCEIIAMTCADGPCFNGGTCVETMTGGYTCRCPPSYTGSNCEKKLDRCSNRPCLNGGQCLDLGHGILCRCQAGFSGANCQVNVDDCASSPCQNAGTCQDGVNDYTCSCTLGYTGKNCSVRSDACGARPCQNGGTCFTHFTGPVCQCPKGFMGPSCEFTLQPSFKPALRQAPQSSSTTVTVSCFLAILVLVLIAAILFLRRRKRRMDGRKQLSDIAVYNDLETVNNLGGSEREAFLFPNGPFKISNSTARLSLSLCPDSRSGFRHNPVESRADRQDYMWREEAMLGSGAGLR
The following text describes a protein:
Function:
Transcription factor that binds to the VHRE consensus sequence in promoters of VHT1 and BIO5, and regulates their biotin-dependent expression.
Miscellaneous:
MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MNGPPTFTQYRINKFSGNGATHKIRELLNFNDEKKWKQFSSRRLELIDKFQLSQYKASEQDQNIKQIATILRTEFGYPVSCSKEFEKLVTAAVQSVRRNRKRSKKRYALSIANGSGGNVNNSISSNSTSDDEISPSIYQRSNSDFLPSSNYAADFQFSNKFQPLMSHQSHNGTIFPTVGTQNDSSPSVTSTQQKYNDIVTMLVHDLVTNVVPLSEQALKDPYTGPNLSHFATSSLSQQPNITTNIPIDSTVPFFLREKLLLQIQRSRTCQDISQAAGSIDIYANLEILGEMSIRMSIAFVIERFFSNLVSSSMKYITAKTCSPENLALLSQRLFGAATRHNLSHFPAAQVQLRLLYLVIGGIVKDFGFDPTLYPLSEIIHHIVMVQYPLASSCASEPPSSSPNKRVKRSPPVVSSDVMLNNNNTLSNRATLLTTLPMKPQSANKDVNRRVIIRFNDREQAFTFHQLSNGPPTVSEVLENCKNLFNIINKNKNFGIFHNDNLLNDESLAKLFDSFSTSEIHLVIKDISTIPLQDAKIPVPITLPKMSCIGENPSMPSIPLVPQEKDDPKKSSLTAFDNILNRISKSPMNEENSNTTLNTGTSTSNTNNNDHNESVPAPYVTKNKNSFQNGNLPQPVFQPLL
The following text describes a protein:
Function:
Involved in mRNA splicing. Helps to stabilize the U1 snRNP-5' splice site interaction.
Subcellular Localization:
Nucleus.
Sequence:
MEKKVICQDIFWSCDGTSFVSVHNDFGIRQYLVPEESNTDKLNRNLLLPFTRFFRNQSIVSCAIDPFYTLYNENSDRLAGDRIVVGGKNFPLQLYSLMDGQCILSYDTMNKINGEYETVYSVKIDVESRVYTGSCRNKVAIYDKSRRDAVWMNQSTKKASKGRQSIISCFEEQPMGGQALSRGSLLCGSYANEMFQVDCRHQRLERLNYTRTVAGGIVQILTSDNGRYVYVVRRNSDAISIYDRRNLQHELNVLRLPFRIHHNSAKLKAYIDTAYGLSMGTPQGTILNWGRDLVEFGGVPSHNSVEDPLITSIPPESEWRTNLDSTIPATVVKNCPGDPELFALSHGGTISLCRFGG
The following text describes a protein:
Function:
Plays an essential role in chain termination during de novo fatty acid synthesis.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MVAMAASTYFFLNSFSYHDMTRNNLRGTPGPKVAHGIIKKNDGSSRSLLAKDLTKVNATEVRANKASFLKPIMMLGQNKNYLDMIPDLGFGSMLSDGFVFRQNFQIRSYEVGSDQAVTIETLMNLLQETSINHLKAIGVWGGGSGLTREMCKIKNLIWVMSKLQVAVDRYPIWFQMGVLNSYDVWSRPPWMNAVKKVYSRMVKALRKKTIETSLKVNNEHSIMLCFPQSLTDARRTKSEVYEGFRMCIVMNCLMLLSKR
The following text describes a protein:
Function:
Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature.
Subcellular Localization:
Cytoplasm. Note=Membrane-associated.
Sequence:
MTASTANTASLEALRRCHFAVDLGAARTRVYVKGAGLVVDQPSAAAVNTRTGALIAVGDFAEKMTGRTPGYIRVVRPVSGGTVVDIEMAQRMLRHLLGDRVRRALRRKPRLRAAVCTPHDADPLSQRAAIETLVGLGARRVELVDTLIAAAVGCGLPVEQPEATMIMVCGAHATQVAVLSLGSIVTAVRVPVGGEAVDHAIVQLLRHQHELVLPSQSVRPLQLALSGNGLTPQGPSSTEIHGRDVATGLARSVRVDTATVRNAIQTPLTAVLDGIGKVLRDCPPDLVADLADRGIMMVGGSALLPGFDQMLRQATGMPVHIAERPDVCAVQGLGSMLEGRVEPLVLHPTTAGSDSHADSD