lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probable catalytically inactive kinase. Scaffolding protein that regulates the cytoskeleton to control cell spreading and migration by modulating focal adhesion dynamics. Acts as a scaffold for mediating EGFR signaling.
Subcellular Localization:
Cell junction, focal adhesion. Cytoplasm, cytoskeleton.
Sequence:
MSACSDFAEHVWKPGSCKNCFHPLSAHKTVGVPDGSTPASCLKGSLGGDEEAGVTTPSPYSKPTIAVKPTMMSLDTCEPKDVNMNIEPQEKTKISVEQKNLKILNLTPLYIDSNVCNKAHREAVLQDPENKIDDNRISLSPSFSPKDTVIISNILVSQQEGRVSQSLKKNSNEGSCNNQENGVIPIRTKSAYNGSALNTRTNNETQEAFKEMPSEDKVASSPVQGTNGGSADLSKTPITSSETATHRSPASPPSASVLSKQSSLSDSSSSSYLSSTDSLPEPEGLLGRQERSVSLQDSQSKTGPQSTPNSPNKQEGFEPIYAESTKKKRKPAAHVLQPPPQSPNQTKHTSEVDRFGENQRATITVIAAHTENNKTFYLSSPDSAVSTQCHFSPTARKDPASPVFRWPSPSRSAPSLSMDASLPPALHTKPESSPPIPPKRSSRSPKLGTSSLSQSLSSPFSLPEFPKLGTSSLSSSVSCPVPLPELPMFFLVSAKEGHFKFPDNHNTPSERRPKPNLHGSGWSCRIEEEEEEEERGRKRMEKMKPPASLGTTSSATGSVNGAAVWKEARDTNTHSSPPAMTEPGTAPPTNPNNGAGQRETEGTEEEGKHNRSMPAKKMLHGSSGELLASGRGAATNDPNPPPPPPKKLHRGSIRMSGSNLELDRCSQQRSTETPSSFPGLGSTSLPTASPDNLTANSGSRNAARMSCSSPLPRTPVPSAPCSPNPISCTSLKIQPPPLPEKKIVNRTVSAPDGGKPFVGAYPHLPFTGSESNVCRSVDASSRSSLPSSPVDPRPIFSSNESLCHPLPTRPLRSRTLDEPLKNQGRLGVHCRTSITCSSSPQLSSPFSSTETGSAPNVGSSLQLQTLLSNIDSREGVYSKLGGLYAESLRRLALKCEDHFTRSQKNSLKFDESNWSLFRLTSNKPSCNAGDAVYYSAACALDPCNSYAVKICKSPSIETKQGHLYGLSVQQSIPSHFNLQQDCGHFLACVPQSMLPPDEAALPSAPPPSAHRPTTPVQEGDRDRVVVITPDIPHQTAADFVREWGAFHKKQPEIYERRVCFLLLQLCNGLEHLKEHGVTHRDLCLENLLLVPHQRRSSQFIPPTDVDGGSCKGGASADVQRHLPRLLISNFAKAKRRSPEDVSSTSGDPRIKRDHARLAPEIVSAAQYRKFDEFQTGILIYELLHQPNPFEVSPALKEQDYRSEDLPPVPPLSLYSSGLQRLAHLLLQPDPIKRIHIQEAKRILQSLLWGPRKDLMEQQLERHSQAGSLGDGSRHEGLLNWLDVKRALLMMKFAERSLEPERNAELEDWLCCQYFSSAHPLSLCHTAELLYSLK
The following text describes a protein:
Function:
Represses biofilm formation in M9C glu and LB glu media but not in M9C and LB media. Seems to act as a global regulator of several genes involved in catabolite repression and stress response and regulation of the uptake and export of signaling pathways. Could be involved the regulation of indole as well as uptake and export of AI-2 through a cAMP-dependent pathway.
Sequence:
MFVDRQRIDLLNRLIDARVDLAAYVQLRKAKGYMSVSESNHLRDNFFKLNRELHDKSLRLNLHLDQEEWSALHHAEEALATAAVCLMSGHHDCPTVITVNADKLENCLMSLTLSIQSLQKHAMLEKA
The following text describes a protein:
Function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
EAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNPVVMLENELMYGVAFELPTEAQSKDFLIPIGKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAK
The following text describes a protein:
Function:
Bifunctional protein that catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress. In the presence of high intracellular c-di-GMP levels, and in response to envelope stress, interacts with cell division proteins and halts cell division, without disassembling the Z ring, but by blocking its further progress toward cytokinesis. Part of a network that regulates cell motility by altering levels of c-di-GMP.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Note=Localizes to the midcell in a Z ring-dependent manner in response to cell envelope stress.
Sequence:
MMDNDNSLNKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLAALGQQGQFSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLAVLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQRAEKLVR
The following text describes a protein:
Function:
Covalently binds beta-alanine in an ATP-dependent manner to form a thioester bond with its phosphopantetheine group and transfers it to an, as yet, unknown acceptor. May be required for a post-translational protein modification or for post-transcriptional modification of an RNA.
Sequence:
MIPSDMDLIESTAEQPDKLYNINRIRAFKDVPFLIRRTESKDTIVSYADAADEIQVLMNFLRKNGVPDEAGIALRVTEHTPASSLMILAILNNKCHFFPTDKMMLSQDLYSQMSTAGVDYLVANKHLTVAPLYFTFLGSILVFKEDCRLYRVKLKSADETVQSKKPLPANMCYTISTTGTTGKPKLIHVPYECIAPNIVGLSQKLNVSMADIIYLGTPITFDPFVVEFFLALQNGATLLTSRHSMRDSPSKVLSALFPDNLATPGITVLQMTPSLFRQFGASSIKDRVLSGSSSLRVLLLGGEPFPSNVELVTWMHPSVLMQKHICNIYGITEISCWSLLHIVQSLQSPVPLGTPIEEDTVLRIESEDNETSQQGELFLGSVKRRCYIPEVDDQANASQDDSGICFRATGDLVTRQQDGTLFYSERSNDVVKRAGNRISLGLITRKIQKCLPSSELTTCLWLEDLQKLICCIRTLESKTRVQQRVQTFDILSKVSIAEQPDRFVYLQHFPCNVHGKLDKQQLLKMCIPLAQPAQQILKSYLHDRLECVEEPDDSASKKQRLDDAAPCGYDLSFRQAGGTSFHAITICREIGLQMCIDDEQRHLFEMLLDENIPLRTVLRFLDTAKLVANNIKRKNVETAVVVSACQSGLIIKRIEQPVLKLQIYWKVNFEKCIDSPVTEYEGRFICVGAHSKILRTLNPQTGSEYSVVKLPERIECKVTFLTEQLAMVGCYDGCLYGFNPQTGNIVFRVGIGGLIKSQPMLTADGRRIIVCSYADDYNVYCLSAERQEVLWCLRIGEKPIFASPLELPREQSLIVCTLDGSYSRVAITDGSVEWTQKFREPVFSTPVLLESVSNIFLSAEVAGRVHACHVGNGKILATFSTEGNIFSSLVVKTPPTFMGHSFAIFGCIDQHLYCLRCKTGPGGKSVELELHWKVDVGAPIYATPTLLTVQPNGLLVWCAATDGRVMLINFRNGEIQWSDKLPGQVFSSACFIEDLRRVFVGCRDNFLYCLGI
The following text describes a protein:
Function:
Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDVENEQILNVNPADPDNLSDSLFSGDEENAGTEEIKNEINGNWISASSINEARINAKAKRRLRKNSSRDSGRGDSVSDNGSDALRSGVTVPTSPKGRLLDRRSRSGKGRGLPKKGGAGGKGVWGTPGQVYDVEEVDVKDPNYDDDQENCVYETVVLPLDERAFEKTLTPIIQEYFEHGDTNEVAEMLRDLNLGEMKSGVPVLAVSLALEGKASHREMTSKLLSDLCGTVMSTIDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARAVGDGILCNTYIDSYKGTVDCVQARAALDKATVLLSMSKGGKRKDSVWGSGGGQQSVNHLVKEIDMLLKEYLLSGDISEAEHCLKELEVPHFHHELVYEAIIMVLESTGESTFKMILDLLKSLWKSSTITVDQMKRGYERIYNEIPDINLDVPHSYSVLERFVEECFQAGIISKQLRDLCPSRGRKRFVSEGDGGRLKPESY
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the hrd1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M) (By similarity). Together with ubc7, required for the degradation of the transcription factor sre1 precursor in the absence of its binding partner scp1.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MKFILYVLASLVLFGLSVLLSLYSSANVYSATVMISQSPVHITIGLNVCLCLFFAIANALKTLLFGSLQTFELELLYEQFWITLTEIMLAITVFREAISISFFMLLSTLMFARVFHSICSFRTERLQIQLTDQRFHIFSRLTCAYFVLSILDASLIYLCFTSEHLGDKSTRMLFVCEFSVLLLNLTIEASKLCIYLYEARHLDQVWDEKSTYLFRLEVCRDGLRLLAYSLLFMYQFPYVSVPIYSIRQMYTCFYSLFRRIREHARFRQATRDMNAMYPTATEEQLTNSDRTCTICREEMFHPDHPPENTDEMEPLPRGLDMTPKRLPCGHILHFHCLRNWLERQQTCPICRRSVIGNQSSPTGIPASPNVRATQIATQVPNPQNTPTTTAVPGITNSSNQGDPQASTFNGVPNANSSGFAAHTQDLSSVIPRRIALRDGWTMLPIPGTRRIPTYSQSTSTTNPSATPTTGDPSNSTYGGPQTFPNSGNNPNFNRGIAGIVPPGWRLVSSNTQSLSTNSAMTSLYQNASSADNNLGSSLPNVVPLSRGLTQSNETSNTFPAASSNISSQLRELHTKIDELRETVSNFRADYNSIRTSLNQLEAASGINERIQTTSADSLLNSNGMSGTEGFENTQTSITTNDNQSSILTSSDQTSPFATDEDRQNSRNVQLETVDENF
The following text describes a protein:
Function:
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Subcellular Localization:
Peroxisome membrane; Single-pass membrane protein.
Sequence:
MAATVSEPFLPPAASPTPLAATTLPGSEASNISEAPKNDNWRFIEPQPIREDQVENAVKFLSHPKVKGSPIVYRRSFLEKKGLSREEIDEAFRRVPDPPSDSSTGTLPTAGAQSTPVAIPKQMPAMQPGGGQLAVTQPKSTSWAQMVLALGVLTAAGAGAGILTKRFLLPKFKHWIRYVVLGESAPVETIKPKKLNPVEEATAQAAAAAAAAATAATQMAGAMQEIAHSRAEDRQRLDNIIRAVEAQTQELKNALAGMKDAALSSEITKYPRSVPVSGQANGFDSLDYWKGQTNGSRPSSASEIRGDKAFRAPNSASIPEHANGSYNLGHQARSMTASPTSVPTQAPHSQSYMDVIAMLERGEKPPGIREVNDKPPNPNQPPSNPRLQPRPKPWEKSSSEARPISPIYNSEVEQQPGRHVENRNIANNVGYNSTVRTEAASSSGTGGSSEPWWRKKTEAEVLPSPPTVKITEVDPVTENEVPPVQASVPSPAVYNQGTRSGWVPPSVPQPIYPGAHEAIRRPKSAVGSSSSSQFVGESGYGSGSAPLNSLPPSQNGEAVVEVPAEGATPTEQSMHQPEQHDVVSVEREPDVTETALVDPNRTFKDVVNED
The following text describes a protein:
Function:
Part of the ABC transporter complex AlsBAC involved in D-allose import. Probably responsible for energy coupling to the transport system.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGIIYQELSVIDELTVLENLYIGRHLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWALPQE
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Sequence:
MNISNPVSSEVTGVNFTFLCKDDITKLSVKQVVNPATFETVIPGNVPVPVVGGLYDPALGASDALRQRCLTCHLDYKYCPGHVGHISLPVPVYHPLFFDQMLKMLRSSCLYCFHFRMARAEVNRFECKLKLIQYGLLVEAAELDDIHPNTRGEEEGEEGEFSGSTEMEAFYAKREKFVARAIRRHLRSGGLDEGKVMSVAEERRKVVKEFLSTIQFPRKCNRCQAISPGFRKDGYSKIFEVPLTPKAQSQNVQYGFQRPNAAMMQKKPNRLPETKNHDLNRKGAAGRLLHSMEVLNNLSRLFEKEREILQLLYQPREAISKTPKPLTPEMFFIHAIAVPPTKFRPPQAAGGEISESATNKQLVKILQGCLAIRDYNDKFNNPEIEAGAKTVIISKLMQAFVTLQDDVNSFLDSSKSPLTGAAARTLEEGIKQKLEKKEGLFRMNMMGKRVNFAARSVISPDPNIETREIGVPPVFASKLTYPEPVTEINHQWLMRLRIHLSKTLLTPDALSLSDSKSKRVHRHLLNGDVVLMNRTYDPYALRQL
The following text describes a protein:
Function:
Subunit delta, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. With the central stalk subunit gamma, is essential for the biogenesis of F(1) catalytic part of the ATP synthase complex namely in the formation of F1 assembly intermediate.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MLPAALLRRPGLGRLVRHARAYAEAAAAPAAASGPNQMSFTFASPTQVFFNGANVRQVDVPTLTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSVAVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQAELVGTADEATRAEIQIRIEASEALVKALE
The following text describes a protein:
Function:
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation in mitosis and meiosis and spindle checkpoint activity. The ndc-80 complex synergistically enhances the affinity of the ska-1 complex for microtubules and may allow the ndc-80 complex to track depolymerizing microtubules.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore. Note=Localizes to kinetochores.
Sequence:
MSNVVLIVYDPRMISKYLGQKLHMGLVADDIIKPTAEIAQQIFANFVRLVLNVSESSLTTLPLSANCDYDPELHKKSIPIIILFQCMKAFIKDNSGNKLDLTMCDLVTPAKHEHRFRKLTSFLVDFLKLHELATPAFNEISEEFSDRKFEMEKIREELLEAEKKKNDLLAKQSIRKRHEHELINEQSNAKAELKNVVNEYTETRQINEELDKQKEEAILHIQALEKEMLTGKKTIEHLNEEVLTSPEQLKQEMEERKRHIEELRDCLESSKKGLQAKLEAREICINSEKNVPVIIEKIHQWTEVREVIIDLIDVESENLRKLKEMEEQLDFMMKEMETAQKRLVEQSETHEQLRIEHTQKSEERQRRIEEITEQIANLKTSQPDVSQEIAKKKQELLALKNAHSETISQITNSCQDAVAKFAKLNAMFKETQKVAFEKNTAAAREMERLKSSLTGRLLSDYTFGSSTIDAGENTENCDPQPNDSSFSVFK
The following text describes a protein:
Function:
May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. Positively modulates nuclear export of mRNAs containing the EIF4E sensitivity element (4ESE) by binding simultaneously to both EIF4E and the 4ESE and acting as a platform for assembly for the RNA export complex (By similarity). Also binds to exportin XPO1/CRM1 to engage the nuclear pore and traffic the bound mRNAs to the cytoplasm (By similarity). May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters (By similarity). Binds single-stranded DNA. Required for maintaining mitochondrial potential (By similarity). Suppresses the initiation of basal levels of autophagy and mitophagy by sustaining BCL2 levels (By similarity).
Subcellular Localization:
Mitochondrion. Nucleus. Nucleus, nucleoplasm. Nucleus inner membrane. Nucleus outer membrane.
Sequence:
MAALLRPARWLLGAAAAPRLPLSLRLPAGVPGRLSSVVRVAAVGSRPAAGERLSQARLYAIVAEKRDLQEEPAPVRKNSSQFDWALMRLDNSVRRTGRITKGLLQRVFESTCSSGSPGSNQALLLLRSCGSLLPELSLAERTEFAHKIWDKLQQLGVVYDVSHYNALLKVYLQNEYKFSPTDFLAKMEGANIQPNRVTYQRLIAAYCNVGDIEGASKILGFMKTKDLPITEAVFSALVTGHARAGDMENAENILTVMKQAGIEPGPDTYLALLNAHAERGDIGQVRQILEKVEKSDHYFMDRDFLQVIFSFSKAGYPQYVSEILEKITYERRSIPDAMNLILFLATEKLEDTAFQVLLALPLSKDESSDNFGSFFLRHCVTLDLPPEKLIDYCRRLRDAKLHSSSLQFTLHCALQANRTALAKAVMEALREEGFPIRPHYFWPLLAGHQKTKNVQGIIDILKIMNKVGVDPDQETYINYVFPCFDSAQSVRAALQENECLLASSTFAQAEVKNEAINGNLQNILSFLESNTLPFSFSSLRNSLILGFRRSMNIDLWSKITELLYKDERYCSKPPGPAEAVGYFLYNLIDSMSDSEVQAKEERLRQYFHQLQEMNVKVPENIYKGICNLLNTYHVPELIKDIKVLVDREKVDSQKTSQVTSSDLESTLEKLKAEGQPVGSALKQLLLLLCSEENMQKALEVKAKYESDMVIGGYAALINLCCRHDNAEDAWNLKQEVDRLDASAILDTAKYVALVKVLGKHSRLQDAINILKEMKEKDVVIKDATVLSFFHILNGAALRGEIETVKQLHEAIVTLGLAKPSSNISFPLVTVHLEKGDLPAALEASIACHKKYKVLPRIHDVLCKLVEKGETDLIQKAMDFVSQEQGEMTMLYDLFFAFLQTGNYKEAKKIIETPGIRARPTRLQWFCDRCIASNQVEALEKLVELTEKLFECDRDQMYYNLLKLYKISSDWQRADAAWTKMQEENIIPRERTLRLLAEILKTSNQEVPFDVPELWFGDDRPSLSPSSRSAGEDVTEKTLLSNCKLKKSKDAYNIFLKAEKQNVVFSSETYSTLIGLLLSKDDFTQAMHVKDFAETHIKGFTLNDAANSLLIIRQVRRDYLKGALATLRAALDLKQVPSQIAVTRLIQALALKGDVESIEAIQRMVAGLDTIGLSKMVFINNIALAQMKNNKLDAAIENIEHLLASENQAIEPQYFGLSYLFRKVIEEQMEPALEKLSIMSERMANQFALYKPVTDLFLQLVDSGKVDEARALLERCGAIAEQSSLLSVFCLRTSQKPKKAPVLKTLLELIPELRDNDKVYSCSMKSYALDKDVASAKALYEYLTAKNLKLDDLFLKRYAALLKDVGEPVPFPEPPESFAFYIKQLKEARESPS
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 1-alpha at 'Lys-316'. May play a role in intracellular transport.
Subcellular Localization:
Cytoplasm.
Sequence:
MSLPPSELGTKSHWDSVYSLEVANLDEFSDEGEVWFGEEAEEKIIEWIEEHVAPVSPGSPTAIRVLDVGTGNGHLLCRVAEEFAHLVPDKMMLTGVDYSESAVQLARQVAAKHGLESRVDFFALDFLRDPVPYQGEWDLLLDKGTLDAISLCPDLVDGQPADHVYVRQAAKALGPHGILLVTSCNWTEEELIEKFAPVGLVVHSTVRMPVIEFGGHVGSTTAVVAFHRAA
The following text describes a protein:
Function:
Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MEIIFGRNKKEQLEPLRATVTGSIPAWLQGTLLRNGPGMHTVGDSKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYNANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSIADKGGTKYVMFKIPATAPGSKKKGKNPLKHSEVFCSIPSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMTFCKEDKTYIHIIDQKTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDNSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDDHVYCQPEVLYEGLELPRINYAHNGKPYRYIFAAEVQWSPVPTKILKYDVLTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIISTDPQKLPFLLILDAKSFTELARASVDVDMHLDLHGLFIPDAGWNAVKQTPAKTQEDENSDHPTGLTAPGLGHGENDFTAGHGGKSL
The following text describes a protein:
Function:
May play roles in cilia formation and/or maintenance.
Sequence:
MRMSSQPGEIKWTPSAMSMPSIHPVNAPTAKYNKISEQLRHVTPGHIQCSMFCGGKGCKYENPTKWPAKDQAVKGLYSSWVTDDILAMARPSTEIITKYNIIEQFKEQGIKSVVNLQRPFEHASCGNALEPESGFTYLPQDFMENDIYFYNFGWKDYGVASLGTILDMVKVMSFAMEEGKVAIHCHAGLGRTGVLIGCYLVWAKRLNPHQAIHFVRERRSNAIQTRGQIQCIQEFSQYIRPLRVIFPSKDPTSSPFTFNQYLSRQKRYLHGFEGRELKYIPKIVDVVCKLLAAKANVASTEGSHPGLRRTLSKEEVVEAIKECAPAAFDNTEEKASPDSATISALSLEEVPSELANNLPNVKDSLHPNEGQPRVSRALSHSHIEDILPTRQQEKTDQDDSIKDIMEKESDPFSPPSDNSVVDHAPGGGDATTAKTNTTKASEQQQQILGDESISSDSNYSSTSDLGKDASTSTSSSVESSENGPKPRLKKKKSTLQRLKEDRRKRKSESEEISSEKMEPVTYSPRNLMSAAELVATALAFNMTMDPNLNQEVEVWQAELNEDDAAWERLKVEKSPQVLSCLMWSWLEELKEPVLSDKDISNLVEMADNPNEALEQLEKGHKHTLNYILKTIAKLPNLSPAVEEKILTRLIVAFTKQTNPKQAGGDAVPQTEVTENVKILEFLKRVVLSEKQKLVEKENSAASTNSSKTNDQYADQASSIEGEKLTENGEEDAEETLEEFAVNTQGDKNNDEKETEKEMASDISGGDNEQLVQNKGLESADEDIGCNQDQKQPEVEETLGEMVQEECGEAEEDTTSSSEEIADVSTLTAKTGDEGNLTKNEEED
The following text describes a protein:
Function:
Plays a role in lysosome motility. In neurons, mediates the anterograde axonal long-range transport of presynaptic lysosome-related vesicles required for presynaptic biogenesis and synaptic function (By similarity). May play a role in chromosome segregation (By similarity).
Subcellular Localization:
Late endosome membrane. Lysosome membrane. Cytoplasm, cytoskeleton, spindle. Cell projection, axon. Synapse. Note=Localizes with microtubules at the spindle mid-zone during mitosis.
Sequence:
MLALFNKLLDWFRALFWKEEMELTLVGLQYSGKTTFVNVIASGQFNEDMIPTVGFNMRKITKGNVTIKLWDIGGQPRFRSMWERYCRGVSAIVYMVDAADQEKIEASKNELHNLLDKPQLQGIPVLVLGNKRDLPGALDEKELIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS
The following text describes a protein:
Function:
Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor (By similarity). Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA. Has a preference for arachidonoyl-CoA as a donor (By similarity). Also has a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus envelope.
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:
MGLLAFLKTQFVLHPLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQLVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKVLAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRFTETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSLLGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFKPARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTEIEKGSSYGNQEFKKKE
The following text describes a protein:
Function:
CAHS proteins are cytosolic heat soluble proteins that seem to contribute to the anhydrobiosis in tardigrades, but their specific mechanisms are yet to be identified. It is possible that protection during anhydrobiosis might occur via the stabilization of vitrifying small molecules such as sugars, but not via the direct glass transition of CAHS proteins themselves (Probable).
Miscellaneous:
MISCELLANEOUS: Trehalose, a disaccharide essential for several organisms to survive drying, is detected at low levels or not at all in some tardigrade species, indicating that tardigrades possess potentially novel mechanisms for surviving desiccation involving tardigrade-specific intrinsically disordered proteins (TDPs).
Subcellular Localization:
Cytoplasm.
Domain:
CAHS proteins contain 2 repeats of 19-mer peptides designated as CAHS-motifs that comprise each two octapeptides connected by a tripeptide (By similarity).
Sequence:
MEAMNMNIPRDAMFVPPPESEQNGYHEKSEVQQTSYMQSQVKVPHYNFPTPYFTTSFSAQELLGEGFQASISRISAVTEDMQSMEIPEFVEEARRDYAAKTRENEMLGQQYEKELERKSEAYRKHQEVEADKIRKELEKQHMRDIEFRKEIAELAIENQKRMIDLECRYAKKDMDRERTKVRMMLEQQKFHSDIQVNLDSSAAGTESGGHVVSQSEKFTERNREMKR
The following text describes a protein:
Function:
May contribute to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes; neddylation of cullins play an essential role in the regulation of SCF-type complexes activity (By similarity). Regulates responses to the synthetic auxin 2,4-dichlorophenoxyacetic acid (2,4-D) in roots, probably by modulating the SCF(TIR1) ubiquitin E3 ligase complex-mediated proteolysis.
Subcellular Localization:
Nucleus.
Domain:
The DCUN1 domain, also known as PONY domain, mediates the interaction with different cullins.
Sequence:
MDSSPVSARFDIFEIYRRFCAIRSGQQLCNKKPCDGEESQRFNLSKEAITQLLYLVENKFQARNSIFDELFKLMSRLDLMVDFTEFTCFYDFVFFMCRENGQKNITISRAITAWKLVLAGRFRLLNRWCDFIEKNQRHNISEDTWQQVLAFSRCVHENLEGYDSEGAWPVLIDDFVEHMYSILGPNKDTSLFCKCGDTESESCLYQEDEHHKDYRRPHTGLRNIPGLKRKTSKKNDEEEEDEDEEVLETQNSSSLLNFKRIKTSNSPRCSSKSPCSIERSLSQGFASLLSTGDKP
The following text describes a protein:
Function:
[CLE26p]: Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.
Subcellular Localization:
[CLE26p]: Secreted, extracellular space.
Sequence:
MRNNHSLRLQLWFRTLFTVGVVTLLMIDAFVLQNNKEDDKTKEITTAVNMNNSDAKEIQQELEDGSRNDDLSYVASKRKVPRGPDPIHNRFLLLSRFILSLLTNPYPYLHICVLDVSV
The following text describes a protein:
Function:
Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Subcellular Localization:
Nucleus.
Sequence:
MMKKSEECDFQWIELSKGKDARGQQLYESCMVNDALISSGDYVLINNYDDPENENTAYIAKIVKMFHSEAKRTAPHRATVSWFARLHDMPAHVRNKFPLTPASPPSPSCRLQEIFLNTMNFENNIDLETVLKKIYVTDISREDNTSKTGMNYDSSCNNHFVFKGRVYDGKSITDEKNKENQNDGDDGFNLISRSGRKLKKVVMDLSPDVNLQKNRRASTATDGYRGSCKKSLFASATTPSNSTALSITCTPSARSTRHSSTAPDTPSSKHSNDTPRSTAARRKSTTNLQKSSSAAKAKPKLKVTKNTDDGDDVEYDDLLRDDDGDDDEDDDSDYNFDEADLSGSSTPPPSSPSVSSDGDGGDGRRLPHRRSTRSKKKFTKIKNRKQTSRTNSVYVTRSDGVGEFITGCKLSSISLKDKSNLQLIRERLHLAVVPDDLPCREEEFADIYQFIRNKIIDRSGGCMYISGVPGTGKTATVRQVMSILHDEHLSGDLAMFKYIEVNGMKLVDPHHANVEILKQLTGQKATAEHACNLLDRRFKTEDPHRVPVVLLVDELDLLWTRKQTVMYNLFDWPSYKYSQLIVIAIANTMDLPERMLMSRVASRLGLTRLTFQPYNHHQLQEIVLSRIQGFDAFHEDAVQLVARKVAAVSGDARRALEICRRATELVTGKEQFISMVHVDAAIQEMFSAPCMVAVRTSSFFEKMFLKSLLSEFQRTGIEEAVLANVYTQFVALCRFEGVTSPNLSQVSRMCNKLGGFKLLLTDSSRNDIHQKIRLNMSQDDLSYALKQDNS