lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells; Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1, C4 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.
Subcellular Localization:
Secreted.
Sequence:
MGSYKDICLLLLFFCTVQGDILDSYVKTDGAWILGQNKKFYRTLNKEECAAKCEAETTFTCRSFLFALKDQQCITLADNTKSTVVFRRADVALFEKRIYLLECRRGNGHDYRGTESKTQGGVACQKWADKNPHVPNFSPESHPNESLEENYCRNPDDDEKGPWCYTTDPEKRYDYCSIPECEEQCMYCSGENYQGKISQTESGLQCQPWASQEPHAHGYIPTNFPEKNLRSNYCRNPDGEPRPWCFTTSPTKRWEFCNIPRCTTPAPVSIVERECLEGNGENYRGKISVTVSGKACQSWSAQTPHKHMRIPENYPCKGLEENYCRNPDGESRPWCYTTDSNTRWEYCDIANCNAPAVVTAAAPVLVPQAPAVEDCYEGTGTSYRGTMALTVSGKKCQAWSSMRPHSHSKTPSQFPNADLRNNYCRNPDGDMAPWCYTTDPHTRWEFCNLQKCANLVQQRPQSTTPTNLGSDCRSGKGEDYRGHIASTASGKTCQEWRSQTPHRHDSFTPQTHPRAGLEKNYCRNPDGDVNGPWCYTTDLSKAWDYCDVPKCPPPEYECGKPKYKPLNCIGRIVGGCVSNPHSWPWQISLRTSFNMHFCGGTLIDPEWVLTATHCLERSSRPSSYRVAAGLHTERASEASAQHRNVQRLFKEPSGADIALLKLSSPLLITDQVIPACLPPANSMVAGGSECYVTGWGETKGTGGDGLLKETGFPVIENKVCNRPELLNGRVRNSELCAGNVDGGTDSCQGDSGGPLVCSEQGKYVLQGVTSWGLGCAQPMKPGVYVRVSRFIPWMERTMKEN
The following text describes a protein:
Function:
May be a specific regulator of miRNA biogenesis. Binds to microRNAs MIR7-1, MIR16-2 and MIR29A hairpins recognizing the 'ATA(A/T)' motif in the apical loop.
Subcellular Localization:
Nucleus. Note=Nuclear localization seems to be depleted upon rotavirus A infection.
Sequence:
MERQKRKADIEKGLQFIQSTLPLKQEEYEAFLLKLVQNLFAEGNDLFREKDYKQALVQYMEGLNVADYAASDQVALPRELLCKLHVNRAACYFTMGLYEKALEDSEKALGLDSESIRALFRKARALNELGRHKEAYECSSRCSLALPHDESVTQLGQELAQKLGLRVRKAYKRPQELETFSLLSNGTAAGVADQGTSNGLGSIDDIETDCYVDPRGSPALLPSTPTMPLFPHVLDLLAPLDSSRTLPSTDSLDDFSDGDVFGPELDTLLDSLSLVQGGLSGSGVPSELPQLIPVFPGGTPLLPPVVGGSIPVSSPLPPASFGLVMDPSKKLAASVLDALDPPGPTLDPLDLLPYSETRLDALDSFGSTRGSLDKPDSFMEETNSQDHRPPSGAQKPAPSPEPCMPNTALLIKNPLAATHEFKQACQLCYPKTGPRAGDYTYREGLEHKCKRDILLGRLRSSEDQTWKRIRPRPTKTSFVGSYYLCKDMINKQDCKYGDNCTFAYHQEEIDVWTEERKGTLNRDLLFDPLGGVKRGSLTIAKLLKEHQGIFTFLCEICFDSKPRIISKGTKDSPSVCSNLAAKHSFYNNKCLVHIVRSTSLKYSKIRQFQEHFQFDVCRHEVRYGCLREDSCHFAHSFIELKVWLLQQYSGMTHEDIVQESKKYWQQMEAHAGKASSSMGAPRTHGPSTFDLQMKFVCGQCWRNGQVVEPDKDLKYCSAKARHCWTKERRVLLVMSKAKRKWVSVRPLPSIRNFPQQYDLCIHAQNGRKCQYVGNCSFAHSPEERDMWTFMKENKILDMQQTYDMWLKKHNPGKPGEGTPISSREGEKQIQMPTDYADIMMGYHCWLCGKNSNSKKQWQQHIQSEKHKEKVFTSDSDASGWAFRFPMGEFRLCDRLQKGKACPDGDKCRCAHGQEELNEWLDRREVLKQKLAKARKDMLLCPRDDDFGKYNFLLQEDGDLAGATPEAPAAAATATTGE
The following text describes a protein:
Function:
TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors.
Subcellular Localization:
Nucleus.
Sequence:
MSESQPMMDIASPGSTGKEKKTPKAKENKEKKTTTPKEPKVTKTKEPKQPKEPKQTKEPKQPKQSKESKEPKVSKEKKTPATPKEPKDQKDTKEQKPKKLTKKQLAAQQSVTTVAPPLGTPPPPTTATTTTTTATTSTSSTSTSNSQPSTPSILDLPSPSQSTKKQRISTPSTASANKKPTVNKTSKKIEQSEDDESADNDDDEDEDDDDDDNNSKNKKKNNNNNNDEEDEDEDEDEESESDSDFEKSNRKRKKIFQKNKNRGRLQSDDDDEDGSGSGSDEDSDEDSDDSDSDESDSDDSDSDSDSDSDSDSDSDSSEGEGNDDDDDESTFNLSEMQVRENTQMNTLIKHFSEDQQTRFEYYKRSSFQRANIKKVMQSVLSAPVNQTSAIVMGGIAKVFVGEIVELARSIMEEWRETGPIRPRHIREAYRRLKESNSIPYYKKSVPKSMK
The following text describes a protein:
Function:
Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation.
Sequence:
MRSILVSRRFAHVLTSTHAAPSTSNIPTTDSHHLTHPSVHRQHTNSYIHGTSNIPLRNETLGQTLRNTTERVPDKEFCVFSKYPIRKTYEEFYHDVRQMAASLYTLGLEKGDRVGVWGPNYYEWVVLQYACAFAGVIQVNVNPHYLHEELRFVMRKTGMKVLFAPKRHKHSNYVHTMLEAMPEMRRGQPGVGHIKSHDIPELRHIVLYGDDVPVHGAWVYSDLIHAAGSAERAKLEDMDRKLRPDEPVNMQFTSGTTGHPKGATLTHFGLNNNAYFAGIRLGWDREDHRICIPNPLYHCFGCAVGVINAVNHGQTVVFPSKSYHVPDIFEAIQNEKCTTMFGTPTMFIDVLKSPLMKQFDISSLRGGVIGGAPCPMALCEKMVKEMRMTDFSVIYGSTETSPLVTMSELHVDPFERIKSVGSVMPHQELAIVDEFGVPVPTGAKGELWSRGYSTMLGYWADHDKTNLAITRDRWYKSGDTATMNEDGTINIVGRTRDMIVKGGENVYPTEIEQFLHKLDYVADAHVVGVPDDRYGENICAWVRLRVEDEGKITAEHIKKACKRGMAHYKVPKYVLIKKESEFPLTISGKVKKFEIQKISKELLGLGTVKSHFTEAVDN
The following text describes a protein:
Function:
Transcriptional activator. Plays a role in ventral mesoderm specification and acts together with nog during muscle differentiation. Mediates posterior pattern formation of the embryo, including specification of posterior mesoderm, via activation of the Wnt and Fgf signaling pathways.
Subcellular Localization:
Nucleus.
Sequence:
MYHSELFQQYGTSYTMRPPHALAPTYPSAGGHHDSYRYSELDVPSQRFDGLFPALEPSQRILGAPPLTPLSLPPGPALGFGQVQPPCETPQLPGNVKMKLENKELWKQFHSIGTEMIITKSGRRMFPQCKVSVSGLEADGKYLLLADLLPVDNSRYKWQEDHWEASGRAEPRLPERVYIHPDSPAPGSHWMKQPISFHKIKLTNNTLDQMGHIILHSMHKYQPRFHIVRAQDVFSRRWGGCSSFTFPETLFLTVTAYQNEKITQLKIQTNPFAKGFREDGMKSKRDRSIRGKRKVISVEQEQEEEEQFQPEGECKRPPLYSGPCDSTLSEELDIGRSLGIPSPNCSFHPITPPTQTPPSTETPNPSLPANQEQGAPLQMSSQTPGTFLQTYPEPPRGASSLYSCSPTDAAQNQTLRPSAQRLPPGYQESPHISHSQGELKIYGTEMGPPGNFNPPSCAVTPSVRLSDEPMGRGFSMNFPHFLPNNKIGLQISGAQLQRMYNGGGWM
The following text describes a protein:
Function:
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination.
Subcellular Localization:
Nucleus. Note=Accumulates to chromatin.
Sequence:
MQRTSRLKRELSLLAAEPPPGITCWQDGDRMEDLRAQILGGANTPYEKGVFKLEVHIPERYPFEPPQIRFLTPIYHPNIDSAGRICLDVLKLPPKGAWRPSLNIATLLTSIQQLMAEPNPDDPLMADISSEFKYNKPVFFKNARQWTEKHARQKTDEEGMPGSLPEVGGSEGPSAAQKRKAGQLSSGGKRFCPDV
The following text describes a protein:
Function:
Involved in transepithelial sodium transport. Regulates aldosterone-induced and epithelial sodium channel (ENaC)-mediated sodium transport through regulation of ENaC cell surface expression. Acts as a scaffold protein coordinating the assembly of an ENaC-regulatory complex (ERC).
Subcellular Localization:
Cytoplasm. Apical cell membrane; Peripheral membrane protein.
Domain:
The PDZ domain is required for interaction with ENaC and SGK1, but not for interaction with NEDDL4 and RAF1.
Sequence:
MEPVTKWSPKQVVDWTRGLDDCLQPYVHKFEREKIDGEQLLKISHQDLEELGVTRIGHQELVLEAVDLLCALNYGLETDTMKNLVLKLRASSHNLQNYISSRRKSPAYDGNTSRKPPNEFLTSVVELIGAAKALLAWLDRAPFTGITDLSVTKNKIIQLCLDLTTAVQKDCLIAEMEDKVLNVVKVLNGICDKTMRSTTDPVMSQCACLEEVHLPNVRPGEGLGMYIKSTYDGLHVITGTTENSPADRSQKIHAGDEVIQVNRQTVVGWQLKNLVRKLRENPTGVVLLLKKRPTGSFSFTPAPLKNLRWKPPLVQTSPPPTTTQSPESTMDASLKKEKPAILDLYIPPPPAVPYSPRDENVSFGYRGHSKSKQPLPVRKGSESPNSFLDQESQRRRFTIADSDQLPGYSVETNVLPTKMRGKTPSYGKPRPLSMPADGNWMGIVDPFAKPRGNGRKGEDALCRYFSNERITPITEESASPMYRFSRPLTERHLVRGADYIRGSRCYINSDLHSSATIPFQEEGSKKKSASSSAKASSGEPSLLVSWLTRLKLLTH
The following text describes a protein:
Function:
Component of the integrator complex, a multiprotein complex that terminates RNA polymerase II (Pol II) transcription in the promoter-proximal region of genes. The integrator complex provides a quality checkpoint during transcription elongation by driving premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation: the complex terminates transcription by (1) catalyzing dephosphorylation of the C-terminal domain (CTD) of Pol II subunit polr2a, (2) degrading the exiting nascent RNA transcript via endonuclease activity and (3) promoting the release of Pol II from bound DNA. The integrator complex is also involved in terminating the synthesis of non-coding Pol II transcripts, such as enhancer RNAs (eRNAs), small nuclear RNAs (snRNAs), telomerase RNAs and long non-coding RNAs (lncRNAs); Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. The SOSS complex is required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. In the SOSS complex, it is required for the assembly of the complex and for stabilization of the complex at DNA damage sites.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MMNQQQQQQQPPTTSPTQQQQLTQLQTHQYFQNKFKLFYKRELDEADPLEIYWRECYDKIELLLLNSSEAEINNYLIEKSASVESSGNNDQSNKFHTEVTIGFLYAILLGSPQNIALSHQYFKSLTFFTKDSLALFCSLLKKLIADKFQKLNDTPRQQVVWIINELIATNHQDCESVTSIILRHIYGGNFTSKNLSLSHSMLNMFLTHRQWLNSRPLLIPTILYNFLRLIQDHISRPQGLHNPTHLKDEINFCLDLLKNKFQECLVIGRDLIRLLQYLSTKTIEFEQLWKDLNSKPTTFAPGYYDIIQSMKTPTPKHFLQSRLSPEMELQVLYILKEVKFGNQKRYQQWFVTKYLVTPESESLIPDIIRYICCVYHPPNHVLCSDIVPRWAIIGWLLKHCKSDAWRNYSKLSLFLDWLYFEPKIDSIMNIEPAILLMAGSVKKYADMTIDLVEFIVGTLLDSYDIQRKDAIRQGIHNSFATVLEKGVVQSLSHVFPPDSLGPSLFEKVKHYFHQFLTNSPIHQLHSQQQQLQQQQLQQPQQPQQQQQPPQYKPYPQQPINKQLPLQMSPQQQSQQQLQQQQLQQQLQQQQQQQQPPQQPPPQQQPQQQPPQQQPQQQPQQQQPQLNISTGNLPNIQQPMVKSPPLSSNTLVSPTSSSSPTSSNLPTNNSRVLNKSGVDIHHVSNLSPQVISQKPQSQQTPSLHSSSQSVLQQKSPPLKETSLFEQQQPSQQLPSQIVKNSPPNLSMTNENISNPPPPPHAKISSDHASPLINSSNSNITTPNPDSQSQIPIPPPISQSPSTKNIDVIMSELNDEPPKLSKSSPTQSNIIVPPPTHKPPQTTISSSSPLLQPQTQPQPQTQPQPQTLQQSTTPSLSSSSTPTIPISPPLLPTQLEIDIQPPPPPPSSQPLQPPPPPPPSQNIKDETLNSLIELNSSIKLDEEIKMEIPDILLTIGSKPQFQPTNITITLGSILSNFNEKISKQPNITLQNELTDSLTQYLSQVLKPELQIDLSTTPSLLSLFCNFQVIHHIFRATFSPTDNSITTTTTTTAAATTTTTTTPTIVKPMFNILKELYKIYPSIGFKIMIWSIITSPGGLNITNNGCTYIYPDIECDNSFSNSDDNESTNNNNNGVEQKPQQQQQQQQQQQINENTHNNNNNNNNNNNNNNNNNNENNITNNSQNITIKEESIFKIEKLLESVQDSNGNRNILGNYLNFHSNLLGGQPPPPPPPQQPNKIVEQIISDCIEANNVGAFNYLVPILYKSFSNLLVGNSDFLYLVLSCINPRQHFRICNKISMGEFRVFGNEMKSLISQSFKWESFEQNYLWQMLIAEDSVYSGMIVKEYPFIISKLDPYNNSEVLQNLTITLKETKFYDFNIFSETLLLNDYFYTFVFCLFSFWLKNNTTQTFNYINQIFDFYLSNNNNNNNNNRKLVERILYFYNIFLKKYGEERIKWSDMIDSDRVSKVLQRSTNSNLFQKYSNLGSLVLPSQSSNIKNDNNPTLSKHQNSDDDSNPKKRFRKE
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
Sequence:
MAKESKSANEISPEQINQWIKEHQENKNTDAQDKLVKHYQKLIESLAYKYSKGQSHHEDLVQVGMVGLIGAINRFDMSFERKFEAFLVPTVIGEIKRYLRDKTWSVHVPRRIKEIGPRIKKVSDELTAELERSPSISEIADRLEVSEEEVLEAMEMGQSYNALSVDHSIEADKDGSTVTLLDIMGQQDDHYDLTEKRMILEKILPILSDREREIIQCTFIEGLSQKETGERIGLSQMHVSRLQRTAIKKLQEAAHQ
The following text describes a protein:
Function:
Part of the ABC transporter complex GsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MRLFNWRRQAVLNAMPLVKPDQVRTPWHEFWRRFRRQHMAMTAALFVILLIVVAIFARWIAPYDAENYFDYDNLNNGPSLQHWFGVDSLGRDIFSRVLVGAQISLAAGVFAVFIGAAIGTLLGLLAGYYEGWWDRLIMRICDVLFAFPGILLAIAVVAVLGSGIANVIIAVAIFSIPAFARLVRGNTLVLKQQTFIESARSIGASDMTVLLRHILPGTVSSIVVFFTMRIGTSIISAASLSFLGLGAQPPTPEWGAMLNEARADMVIAPHVAVFPALAIFLTVLAFNLLGDGLRDALDPKIKG
The following text describes a protein:
Function:
Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. TdcB also dehydrates serine to yield pyruvate via analogous enamine/imine intermediates.
Sequence:
MHITYDLPVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDQYIQNRKTVSIISGGNIDLSRVSQITGFVDA
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a 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; This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MAEFATIARPYAKALFGLAQEKNQIESWLGGLEKLAAVVQEGKVASLIDRPETNASEKADILIDLVGLKDKELKNFVIVLAGQKRLSILPEVYAQYQDLTLSFNHIKSAVIYSAYPLTDKQVGELVQMLNKRFDSELKISVEIEPELIGGIKVEVGDQVLDLSVQGKLSALYTTMTN
The following text describes a protein:
Function:
Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MANETALDPKQQQGRILASTPPSKRRSRRDIYYWLESLAVFSHSVSLSFTASMYSICWTFLSLWPLLLIYLVWMIIDKAFVSGRIRTQMWLRKLAPYNWFCNYFPIRLHKTAELDPNGSYIFGYHPHGILSLGAFGAFGTEGAHFSELFPGLSMSVLTLNSNFYVPLYRDYLLALGVMSVSRSSCVNLLKRGNGSSVLIVIGGAQEKSACSSWHQQAYIYDQVDNNPRSRIYRCQAIIKRVAGFTIPLFYGQGFFNRTFGLMPWRKPINIVVGEPLKLPKKDNPTYEELDTAHTEYIRRLRNIWDTYKDEFLPDRNAELELAF
The following text describes a protein:
Function:
Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis.
Sequence:
MSGYSKPLKSKSIAIVIFGATGDLSMRMLLPSLESIHSYDPFNEASLIIGVARNEYKDSEIKEKISGSIEKYSRTHNEKEEQNLNDFLKHVKFISGDFTDPATYEKLKALLDQHQLEGVLVYFATPPSLIQKISDNLYNAGLSTNKDRWVRIVIEKPFGSSYETALALNDSLHEKFNEEDIYRIDHYLAKETVMNIFTFRWGNTIWEPLWNRNYISHVEILVAESVDVGNRTGYYDGVSVIRDMIQNHLLQMLAIVAMEPPSEMTAKSIRDEKVKVLRAIRSIKKQDVILGQYLGYKEHKGVSKDSTTPTFAYIRFFIDNWRWKDVPFYICSGKALAEKKSCIKLVFHEVPHAIFGDSTINKPNVLEIKVQPHEGIILKQHVKVPGVGLSTAKIPLSFYYKDKFGENALQGAYERVILDAIHGDQSFFPRSDEIEQCWKIVEPILKDSYPEIIPYAQKMDITTGTTKRNRVNQATLAVFRDAQELVQSVTERLTRLIVDTVEKKGTCTIALSGGLAPRPIYSLLATAPYTSRIDFSKVHIFFVAERCVPPTDIHSNYNMINEMFLKYLKIPEGNIHRMKGELDYKVGAKDYEEEIKKYFNSENPEFDIILLGLGFEGHTASLFPGTDAINDHQSLIIGNIVPHDNLSRITMGAKIINNANNIIMINTEAENKDIIDLVFNAPFVPAMIPAQLIQPTHGKLTWFTIN
The following text describes a protein:
Function:
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Subcellular Localization:
Cytoplasm.
Sequence:
MKRCYITTPIYYASGKPHIGHAFTTILADVIKRFKIQNGYEAFLLVGSDEHGNKIESKAKSLNLDPKTFVDINAQAFKLMWKTLNISFDHFIRTTDEIHKQQVQKTFQDLYDKKLIYQSEWKGAYCVECEQNYFTFNKQTMLCEIGHNLSLVQEPCWFISFSSTKNWIETTIGKNQLNIIPKSRASELKNNFINNGLNDLALTRKNVTWGIKVPFDPNQTIYVWFDALFSYITNLGFRNGDPNFIKWWNNDNKEREVIHLISREITRFHCIYWPIFLHLLDIKLPTQFLSHGWIVDGEGRKMSKSLNNVISPEQLIDQFGVDGTRYCLLKEMRLDKDNRCSVSILKEIYNADLANSFGNHVSRTFGMIKKYLNGKLEYQIITDNALQKIMILIDESIVQFDHYFNSYEFYRAINLLLKIVFELSKLIDDFKPWELFKNQEFSLLKQLLFTCVRCVQVCYVLLTPILVNTASKVFHLFNFADDACRKDQLRDATLLKKIIISNSMEVLFKRVD
The following text describes a protein:
Function:
Involved in the transposition of the insertion sequence.
Sequence:
MGNVSLPLDYVVIDFETTGFNPYNDKIIQVAAVKYRNHELVDQFVSYVNPERPIPDRITSLTGITNYRVSDAPTIEEVLPLFLAFLHTNVIVAHNASFDMRFLKSNVNMLGLPEPKNKVIDTVFLAKKYMKHATNHKLETLKRMLGIRLSSHNAFDDCITCAAVYQKCAAIEEEGKRKVNKAMLDETAVYEAVKEILACNKRNVEWLRCMNVGSYLDIKAFYPVMRVKVKGRKKYVLTEILEEDVKEICTSLKCEPALKSEVGNTRIMLNSLEDVMRLESYILEQYDFVLQALHDYKENEMNADEKLKEYLNIMV
The following text describes a protein:
Function:
Polyglycylase which modifies both tubulin and non-tubulin proteins, generating polyglycine side chains of variable lengths on the gamma-carboxyl groups of specific glutamate residues of target proteins. Involved in the elongation step rather than the initiation step of the polyglycylation reaction. Polyglycylates alpha-tubulin and beta-tubulin. Polyglycylates non-tubulin proteins such as nucleosome assembly protein NAP1.
Subcellular Localization:
Cytoplasm, cytoskeleton. Cell projection, cilium. Cytoplasm, cytoskeleton, cilium axoneme.
Domain:
Gln-310 is the main determinant for regioselectivity, which segregates between initiases and elongases in all tubulin--tyrosine ligase family. A glutamine residue at this position is found in elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-chain elongation, whereas an arginine residue is found in initiases TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
Sequence:
MPLHPPARRPHGHRRNGSEAQTEATTQDTGRLSCPRRVGAAVCPIQGLGHRAARRPRRGVGTTSASRAPRPGALMPATRNRPRFIHYRVQPPRTHVSFKRPKRSRTHQSHTKVPGWTHEKRMGSSVEEGLRPELSQLEQDADNLGEEEAARLPVTSLNGLLMEGDRHPNPGQGPFFYIGGTNGASIISNYCESKGWQRTQDSRCEDYKLKWCEIKCRDNYCSFREGQQLLFQLPNNKLLTTKIGLLSALREHARTLSKARLMPSTQAKVLKMDEFFPETYRLDIRDERQAFFTLFDETQMWICKPTASNQGKGIFLIRSQEEAAALQAKTQSIEDDPIYRKMPFRAPQARVVQRYVQNPLLLDGKKFDVRSYMLIACAMPYMVFFGHGYARLTLSLYNPHSSDLSGHLTNQFMQKKSPLYMLLKDSTVWSMEHLNRYINDKFRKSKGLPRDWVFTTFTKRMQQIMSHCFLAVKSKLECKLGYFDLIGCDFLIDENFKVWLLEMNSNPALHTNCEVLKEVIPGVVMETLDLALETCQKSLHSQKMLPLQSQRRFVLLYNGETTDLWPRLGSSRPPIRLPYANSNHARSTCEISSSSLTSTRVTIADRPAARKSMSSRTAPICASRKSRLSDSGGVSIEESETSVCSGLPEGSRDAAREPSLGPTEEEREEEQRSTSHRGS
The following text describes a protein:
Function:
Probably functions as a holin together with holin-like protein 26. Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space. Determines the precise timing of host cell lysis.
Subcellular Localization:
Host cell inner membrane; Single-pass membrane protein.
Sequence:
MEQMRQDIIELKQNDKSQEQRISLLERTSDRHDQQIQAVTESLSKIHENTTWIKRTITGAIISTLSTVVVGGILTIVWNLVKN
The following text describes a protein:
Function:
Transcription activator involved in oxidative stress response and redox homeostasis. Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways, including thioredoxin peroxidase (aspF3), cytochrome peroxidase, and the protein AFUA_3G00730, which appears to belong to the glutathione S-transferase family. Proteins of the protein degradation pathway are also regulated by yap1, as well the p-nitroreductase family protein AFUA_5G09910. May be involved in antifungal resistance to voriconazole.
Subcellular Localization:
Nucleus. Cytoplasm. Note=The nuclear localization is oxidative stress-dependent and oxidized yap1 is found predominantly in the nucleus, while reduced yap1 is continuously exported to the cytoplasm.
Domain:
Contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD and c-CRD, respectively. A nuclear export signal is embedded in the c-CRD, with which the nuclear export proteins interact only in the absence of disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or between the c-CRD and the n-CRD.
Sequence:
MADYNTLYQQGLYLSPDQQDLLLAALSSNNPTQKQQTVTHNSEANQNLNHTPGHASSGSFSVSPPSGLDGSVNQSTTFGYEDSPYLDLNPDFDLDFLGNESLIGDLPPSLPSTEDYEPGDKRKDIDGQVNDKEDSGKKRRESDEKAAKKPGRKPLTSEPTSKRKAQNRAAQRAFRERKEKHLKDLEAKVEELQKASDNANQENGLLRAQVERLQLELKEYRKRLSWVTSTSGLSPVNAIPGAYSKGMYGLNNNEFMFDFPKFGDLPGSHLFTNTQTSKSNQNKAKDNPTATPRSEAQVPGVLNRNDLKISSPNGLSNGPSPAKSTPSGQTPNSQTSTRPGSGTLNGAVDNNGAARGYQVNSSYSASTKQATHDTPSSDSPSSSSDSHQSQLLSSNGTSPEPSLHSPAVKATESSTPHACTYTTINGEESFCAQLSMACGNINNPIPAVRQNSESASNTPSHANSSDKALGLDFFAQQNGGQFDPVLFGDWREPQDAILSQDFGTFFDDAFPLPDLGSPSHNFSEATKQPAAPKKDLIAEIDSKLDEDEEVVPGEDKSQMLTCNKIWDRLQSMEKFRNGEIDVDNLCSELRTKARCSEGGVVVNQKDVEDIMGRVK
The following text describes a protein:
Function:
Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MSTEAKRRRNQKKKQKQKQKKAAEKMQEQASLESTLGSPIDVSIFEQQQYGGAEDAEAAGAAAARESADESRGASVESSGSTDNAIGDDRAGSAPSPYVAVGDSAAVSTAVEVSAPLQDEAFSAVDVEATESPASALPAASVEESEHVSIATPAEPSAAPVAPEAAASEENVVQMAGENGTNPEADVPIEDESNFLFGDSPHSPLPWDDGGASDPEQRPEMTEERPELPTFEEERTQHTSLLPSTSNEHKTPQEALSSEEDQAAEPEQNIGVCDGHAEDSTVDVEWEQHTSSSELFGEEHDTPHSPLPWEEQEAAAPEENRSRMEEHKESISGDERDQDVPITEDSAKTGSLPEDTVPGENTPGDIPETATSAKNVDFDSANGTGNVPVESQAHSTTHTPEEYAADSNSLFALEDDGGDFLAELSNGHDVSSQSAADMLPIDDNVPRTTFDGADALAGPAETYEPGDLFADEDTAEEPPWAQNTNPNVDTSQQLPVSRSSAELSSSQAAKETPGIEVPPPMFWDEESDSIEASNDQLAFTPVAQRGKVTLPDKKFSFLDNDDDLLNDDEEEEANAGDQPENDQENCDDDSFLDSDEEPPLLPPKAGKTTYTPSTQVLGQDRSSYDAHNLSSSMAVSPAVAAVTGQQQFLPGPPVPEKPKVGKYALPKQPNPPPQTNKGYYAPTLGGVGLEATDKPPVLSVNDESVRRLEEEKKKSDAYDFPLELVKSKPKPAKPVPVPSIPSIVTASQPASRSFSPSDAQPVFSPEKAGITPLKPTVPPVKNPYQPNFDGNYLSLVDAVNSRTSSVQQNPYAPPPVNVGPQVTSEKPYAAYEGAASGSQSQHPFPPQPLGAYGTNAPKPPLNSYNLAAAQMDSPKERRPAAYVNTSRTRAISNASVGSSGSYNSHQLPAGPTVVPPRFAFPPPQAHISPTIPALQTVGIAGAPPAVSSPGTQRRTHARSHSSVYAPANAPHASKYAPTVHPSVQQKYPSVAGPSKRSLAGNGVPDGVSNRVLPPTIQEVPVDGHALNFRQFPLFNWSQTSKIVYGLSLPIDTGNYMLGKPFPVSGIHVRNSESILVPNVILKDFPGPLIKGKTRTKDLEKWLELSIAYQRESLPGRDLTLWYVLKHKLSTSGSLRELSKILYDSDQLIPYMGQMHSHGRPTLLSHKLDPNSQMQILAHLQVGSPGAALDLALAQKDYALALVLSSLIGKDKWSEVVDTYLREEFSVSAGNNQFSVYLLALIFQVFVGNSNRVLQELTANPLKRDWAIQDWNIILAAVLNNIPKDVDPRQLPPVVMEFLVGFGVFLVQSGKLAAGAVCFVIANVPLSQNELLPHSGVKFECLGSINSLDAVLLSEVYEYYYTTINDNCPFFASLLLMKTVHASALLDYGLPTTVPKYLDVITGLLRNAPKNSAIAVSLTHQLESINLRLSGVTTAWIGKPTLSSVWGQLDKSFNKFIGGDADDFSKQPEKTVFDSFTPSASRNASMVDLNHGVTPMRPSAIKNSGVNRSHTDLPVSNKGGYAPLNAPGSNVFSVSRSNNHPHGTEHGNSMSNLHGDSQHLTHKTNYTPHRASNLISPKYPEEPQNSHLPNQQSNLPSPANGHSRNPSIPSVATPPPIFSAPPKRARGKYAATASGAVSVDQLYSDAGHSNTPTKVKSVPTCPEIAETPAALATRQATDSMTDFFAPPLLQAGLQQDRRSSAYSASSQGILPSSRRSSNISDVMLPPKKSGSGKPYRKTTVNYTPIDMEASSLAPSSVSLSQSTGDTTTEVKRARNSGEASNSSATEVADSTVLHKSPESVDTSEYSFPDESVQSWEENAEDDQDPLHTVSAISNTEVPVDKRDGERGSQNTLTKAAPYSDLAPYEHEGNAPSTESPAIKGSRVQVQVQVTPPEDFAHIQSQVVSPEKEASPTVEKGANANESSPDLHERQPYAGLGVSYNPNTGGPRPFASHQYLPRAPAVPAYSPIEENAAEEGRTDNQTKAVEKQEHAVLKRTVSGPVIGSEKLMSPALAHPIPRTSRFEPIKEIIQNDEDTFRKDKVPVIRASSNPNFNPYTPVASEQYYDDVVEDESDDSEEESERKRQEKEKEEERKREAAEKEKRKNEGGGSSRWFGWLKKDTNEKKPIKAKLGQKNNFYYDEKLKRWVNKDATEEEKQKVSTPPPPPPVVKRKMNTTPEIKPRSGSVVGGPAIRTQGAVAPVNPQDPQPCQAVVGASSALQKQASPVKPRDPAINLTSKKANGLDDLISLTAGPSNAVSRRKKKPGRGYVNVLNNL
The following text describes a protein:
Function:
Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia.
Subcellular Localization:
Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Sequence:
MASLGLQLLGYVLGLMGLVGTLVAMLLPSWRTGSYVGASIVTAVGFSKGLWMECATQSTGITQCDIYSTLLGLPTDIQAAQGMMVASSAISSLACIISVVGMRCTVFCKDSPAKDRVAVVGGVLFLLGGLLGFIPVVWNLHGILRDFHSPLVPDSMKFEIGEAPLLGIISSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
The following text describes a protein:
Function:
Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MLDQLVGLAMLVAASVVFLYYTIWTLLMPFVDSDHPLQNVFPPRVWAIRIPVILILMASAVVGSFLSVVMIRSNRKKAAKAKATLKKKA