lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transcription factor that binds to GC box promoter elements. Selectively activates mRNA synthesis from genes containing tandem repeats of GC boxes but represses genes with a single GC box. Acts as an epidermal circadian transcription factor regulating keratinocyte proliferation.
Subcellular Localization:
Nucleus.
Sequence:
MSAAAYMDFVAAQCLVSISNRAAVPEHGGAPEAERLRLPEREVTKEHGDPGDTWKDYCTLVTIAKSLLDLNKYRPIQTPSVCSDSLESPDEDIGSDSDVTTESGSSPSHSPEERQDSGSAPSPLSLLHSGVASKGKHASEKRHKCPYSGCGKVYGKSSHLKAHYRVHTGERPFPCTWPDCLKKFSRSDELTRHYRTHTGEKQFRCPLCEKRFMRSDHLTKHARRHTVFHPSMIKRSKKALACPL
The following text describes a protein:
Function:
Regulates cytotoxic granule exocytosis in effector lymphocytes, thus acting as a critical mediator of inflammation in a broad range of infectious and non-infectious diseases. Essential for cytotoxic degranulation of natural killer (NK) cells and CD8(+) T-cells and for the activation of CD4(+) T-cells following infection. Plays a critical role in CD8(+) T-cell and NK cell-mediated cytolysis of target cells and contributes to the cytolytic activity via the perforin/granzyme pathway by enhancing exocytosis of LAMP1-carrying lytic granules. Contributes to NK cell-mediated control of cancer metastasis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cytolytic granule membrane; Multi-pass membrane protein.
Sequence:
MEPCRSLALFAGSLGLTSSLIALTTDFWIVATGPHFSAHSGLWPTSQETQVAGYIHVTQSFCILAVLWGLVSVSFLILSCIPALSAPGRGPLVSTVMAFSAALSILVAMAVYTSMRWSQTPFSQVQTFFSWSFYLGWVSFILFLFAGCLSLGAHCRTRRAEYETL
The following text describes a protein:
Function:
Through its association with the EHMT1-EHMT2/G9A and PRC2/EED-EZH2 histone methyltransferase complexes may function in gene silencing, regulating repressive post-translational methylation of histone tails at promoters of target genes.
Subcellular Localization:
Nucleus.
Sequence:
MLRTTLQTSAAMEDLTRPEDAAVKNGSVSAIEEEKNKVKDLMFKHLREAADVQLFSNGEDSITEHGAPSKTDRQTLKAHCKIQQGAVFSGKILSFGCSVCKDSSTYSPNDLLKHFRAAHKGTLPTYPCDLCDFVTNEFPALQRHRMEHRNTLVTCELCNDNTQYSLLLITRHYMMSHSTNGQFKCDWCEFRTSDAGTFVQHIHRHNDSHWKCSKCRHISLNEEDHQSHMKAHSKTFPFTCQVCGYGATSSEYLRKHRASVHKDMSETTNTWKVAEDALANFSANSKQTFKKSGESLETLRIFNPSCVSSSVQNQTSRSVKPDLPEALHCSEGSPVKKDHRVWSKSPESTEQSATVGLEESQNTDAGCHTNANGLTVLMVKNKISLPPNCTTKVMGFKVVDGKKHLVLKVIPSAKQDLMAKSNCLVSDVSLLPKPVLDRGKVSETKENSDSRSSAVSPRTGSCGSGVHQGDVMAIQVKIEEETSVCSVNVDDQTNGLHSSITTCADTMTSVTKDSCHVCNQIHLNEARCTEERNNLSLVSCVSTAARQISAVLSNSSQISASKVKSVSTPSDLQRAKNLSSGLRKSAENFGAVNLSSQADKTSNFKQNQQNVTDLDSSPWSLQTSLLSNGECASGTGKTIQNTLNQEVFTFHNYSKETFSMSPKPPQDLDCNPNLSDCESKCEPSLFSLTLTESPERLTESSEEDIEVDECVASVADQLNEDHSDSVLQNLNIVKVEEDIVSISATQPELQSCLTSMGCFVEEHSDAIVSQQLHRERRGPSRTSNNSLKQATNSHVLQLPERKQPILLRAAENRFSVPVKVNPSPGFRLLTNSKKSLINVSYIRPGMNKSNNVGVAPTKLQSDENRTTLASVLQPSTNPTQNHYLINRAGFKGPTLVPSSSNTPPEVKMAKTQQTCYLVQRSVPVKSPGGPVLKMASASQENPHPVLAVPVNPAEKPSGRQSFLLRYISPKSGLCLNNQETKTRNLSSQTGENSGNKVIFKIVSPSGSLLTSGSPTSRGQPLFLATRPKTQCFLVSSNKTDAPAYSGAKTLIGLKNSAQKDVKKCDILLSQILPQAQQCEAEKLALAPRSIRPPSQRKRCRKTFEEPATMVHKARRVSNTLQIEKDTPALWIPAAKEVERTLKLAPFSSVQRIKCPRRYQPVVVLNHPDADIPEVANIMKIVNRYRGAVTKVSLCQKTLQALSDLGVPDEDSTLSNEERLRPRLIQTFARERFLLKMKLRRKNKKKYEVVKPSSGCRQSTVLFDCWFCGRIFTNQEDWIGHGQRHLMEATRDWNKLF
The following text describes a protein:
Function:
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Subcellular Localization:
Cytoplasm.
Sequence:
MKSEINIFALATAPFNSALHIIRFSGPDVYEILNKITNKKITRKGMQIQRTWIVDENNKRIDDVLLFKFVSPNSYTGEDLIEISCHGNMLIVNEICALLLKKGGVYAKPGEFTQRSFLNGKMSLQQASAVNKLILSPNLLVKDIVLNNLAGEMDQQLEQIAQQVNQLVMQMEVNIDYPEYLDEQVELSTLNNKVKLIIEKLKRIIENSKQLKKLHDPFKIAIIGETNVGKSSLLNALLNQDKAIVSNIKGSTRDVVEGDFNLNGYLIKILDTAGIRKHKSGLEKAGIKKSFESIKQANLVIYLLDATHPKKDLELISFFKKNKKDFFVFYNKKDLITNKFENSISAKQKDIKELVDLLTKYINEFYKKIDQKIYLIENWQQILIEKIKEQLEQFLKQQKKYLFFDVLVTHLREAQQDILKLLGKDVGFDLVNEIFNNFCLGK
The following text describes a protein:
Function:
Probable serine protease inhibitor.
Domain:
The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable (By similarity).
Sequence:
MEDNAGDCGGMTAFALRLAKRLADVGVSSNKNLVFSPASLYAALALVAAGARGTTLDELLALLGAASLDDLEESVRRAVEVGLADESASGGPRVSDACGVWHDETLELKPAYRAAAAGTYKAVTRAANFQRQPKRSRKKINKWVSKATNKLIPEILPDGSVHVDTALVLVNAIYFKGKWSNPFPRSSTTTGKFHRLDGSSVDVPFMSSREDQYIGFHDGFTVLKLPYHHRTMKNHGDGGDTITNSSITRAILEHYGGENVGLSMYIFLPDERDGLPALVDKMAASSSSSSFLRDHRPTRRREVGDLRVPRFKVSFYSQINGVLQGMGVTAAFDAGEADLSGMAEGVDQRGGGLVVEEVFHRAVVEVNEEGTEAAASTACTIRLLSMSYPEDFVADHPFAFFVVEETSGAVLFAGHVLDPTSSSE
The following text describes a protein:
Function:
Required maternally for proper expression of other homeotic genes involved in pattern formation, such as Ubx.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSSSEPPPRYEPPVEPVNGIVQPPVIPPAERPGRNTNQLQYLIKTVMKVIWKHHFSWPFQQPVDAKKLNLPDYHKIIKQPMDMGTIKKRLENNYYWSAKETIQDFNTMFNNCYVYNKPGEDVVVMAQTLEKVFLQKIESMPKEELELEPVTAKGGKKKQRAPATPKSSSGGAGASTGSGTSSAAVTSGPGSGSTKVSVAASSAQQSGLQGATGAGGGSSSTPGTQPGSGAGGAIAARPVSAMGGTVSSTAGGAPSIPPISTMPPHTVPGSTNTTTTAMAGGVGGPGAAGANPNAAALMASLLNAGQTGAYPGAPGQTAVNSSSLLDGSTAAVAAAAAAAAAAAAAAGGAAGAAGGAGTIPAVAVNAANAVQAYVNAGVSVGVDAVIPPQQPAKIKKGVKRKADTTTPTANAFESPYTQMDSKSAKIATRRESNRQDLTFQGSGYNMSPLGVSGVPGLGGLVAGGVAGVAVAKNKEKLSDALKSCNEILKELFSKKHSGYAWPFYKPVDAEMLGLHDYHDIIKKPMDLGTVKRKMDNREYKSAPEFAADVRLIFTNCYKYNPPDHDVVAMGRKLQDVFEMRYANIPDEPVANAAHHHGHGHGHGHGHGHGHGHGHGHGHGHGYGGSSSLKHDASDSSSEDSSDTENESNSDEERSARLKMLESKLLGLQEEIRKLSEEASAKKKAKKKLKEKKKSIGGGSGSGSASHHCHATGGGANAGGAGGPGSGGHGSVSVPGGVGSLGPGGAGGANLNALLGGSLVGHGGAAVAGGVPNVGALHSQVHDVAMAFSQMAGGGAAAGAGFGAGVTAAGASSGGKAGTLAGALAAGAAAGAGGTTAGSGSSKGAKSKGGRGAKGSGAGGVGASNNAAAGNAAGGAAGAAAGAGSVGGVGGAGAAGGGNASKRAKGSSSAGAGGGVGGANASAGGAGARGSSKKKPSQVMNFDSEEEDTAKPMSYDEKRQLSLDINKLPGDKLGRVVHIIQNREPSLRDSNPDEIEIDFETLKPSTLRELESYVASCLRKKTHKKPSGKSKDEQMAEKKQELEKRLQDVTGQLGASKKTAKKDESASSKVEAVQPANPVSSSSSSSDSSSSSSSDSSSSDSSDSEAGDGDERPPRKKKSRDSNGSNVNNPSINVVMGGNLPSGALSPTTMLMGLDHVVNSNTPTSQMSNMLGNANPLTAAAMLNNNNKTSLPGSNFGGAPAPGNMMHAGAGVPVAGAAVSASTGQQHNKNGPNDLSKVQPGGPINAALPPHSFAGGTATVATSQSSGGIRIASNLHKPSGLGGGDLGEHHAALAAALTSGINSTGTAGGGINNNGGSNNNANPLGGSHGDAMVNASLASLASGLKQIPQFDDPVEQSLASLEFSAGSTGKSGLTDNFLMQQHLMQPAGPQQQQQQQQQQPFGHQQQQQQQQQQQQQQQQHMDYVTELLSKGAENVGGMNGNHLLNFNLDMAAAYQQKHPQQQQQQAHNNGFNVADFGMAGFDGLNMTAASFLDLEPSLQQQQMQQMQLQQQHHQQQQQQTHQQQQQHQQQHHQQQQQQQLTQQQLQQQQQQQQQQQHLQQQQHQQQHHQAANKLLIIPKPIESMMPSPPDKQQLQQHQKVLPPQQSPSDMKLHPNAAAAAAVASAQAKLVQTFKANEQNLKNASSWSSLASANSPQSHTSSSSSSSKAKPAMDSFQQFRNKAKERDRLKLLEAAEKEKKNQKEAAEKEQQRKHHKSSSSSLTSAAVAQAAAIAAATAAAAVTLGAAAAAALASSASNPSGGSSSGGAGSTSQQAITGDRDRDRDRERERERSGSGGGQSGNGNNSSNSANSNGPGSAGSGGSGGGGGSGPASAGGPNSGGGGTANSNSGGGGGGGGPALLNAGSNSNSGVGSGGAASSNSNSSVGGIVGSGGPGSNSQGSSGGGGGGPASGGGMGSGAIDYGQQVAVLTQVAANAQAQHVAAAVAAQAILAASPLGAMESGRKSVHDAQPQISRVEDIKASPGGQGQSSPAQQSPQDRAAAKRAEQRRAEQERRRREALAGQIDMNMQSDLMAAFEETL
The following text describes a protein:
Function:
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Subcellular Localization:
Cytoplasm.
Domain:
A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Sequence:
MIALIQRVSRASVVVDNQTIGAIDKGLLVLLGVEREDNREKMEKLATKVMSYRVFSDENGKMNLNLTQAGGSLLVVSQFTLAADTERGLRPSFSGAGTPEQALGLYEEFVAFCRTKGVNTETGQFAADMKVELVNDGPVTFHLQV
The following text describes a protein:
Function:
Involved in the biogenesis of the 60S ribosomal subunit.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MANPRQRRKSRSGAPKARLSKFANSKLKKVTPRNFPGPLSNAYNPRQTPRQNYERLGLLSGKLAPRLAGGIEKKTDLQNIWLNKYKKKDEFEILRTTSDGEVVDNEEDENDDEETDEDDSEKSDDDGNQATTVNRDPKLSKGEGRIIRDADGKIIKVIIGDESEIELEPTAEDPSKIVIERDLQPSTSTPWGNPLDTPSYEQDPSVTHHPPAPVLQGIGYQNPRQGFVPPKTKFVEELEKISSNRLATYSETIKKKQHLSENQTNWLLKLIEKHGLENTHLMARDLKLNKDQKTEGEIRHLISKLASQ
The following text describes a protein:
Function:
Required for translation of the mitochondrial OLI1 transcript encoding subunit 9 of mitochondrial ATP synthase.
Miscellaneous:
MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion.
Sequence:
MITTVQEISKWRNLCFIRMQSRKWYPVLKKTPLVADGRKIIKHADKVPHPEEIIHPFYQPTAIEQFTACATEYNPSLLDGKKIAPSLIKHPVSLKTILVDSKLKFDDIRGVNKWLMEFVARRQHQRNIVLTPASKSVRSFHVLHLSSTDIAKLRGLENILSEIENTNDLQSRVESVNNELQNIFDRDSKQTRLFCENILAYLIKNYGNSTEKLILLINVTEMQLYSRLDQMKAMNIILYNILCKVEANENPPYSPTLVTALENLLAAINNRFFPGRCENSLHPIVIEQLLSYFIKTGNLNESKNFLGHLIKKGILPEATIINRYLEAIDVHFDKSTKIFDIRSKFAFIADLAPIIENYGTIDLFKFLIPMCRHFDELCSLLNIIRKSNNAKRAVDSTLPIFIKKVLTFTKDPMINSGNLSTVFNIVSPIYGQNVPSEFVEKFILSFALQGNYTMMAHMIDTYKIKLSHKYQLQIIRALKNSERNHALKNTGAVGYNKEFKKYFIEKYLNCTEREALRP
The following text describes a protein:
Function:
Methyltransferase which mediates trimethylation of 'Lys-78' of cytochrome c (CYC1).
Miscellaneous:
MISCELLANEOUS: Present with 2940 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm, cytosol.
Domain:
The SET-like region, although related with the SET domain is not detected by any prediction method.
Sequence:
MEEVFRFYSNSRNIFIHKSLSLKPSTIDDPKSGYGLFVEPSKFKNDELKSETIQLLRIPKRCTFNINTLLALLGDEDEFSSKEEFQRTNDKIKIALREIMAHPNFSVFLTETNLLIIYFMIFQTIRSRYEIPENIQYYLENVLMSIEVETAMDSIENLATDYGHYPQIFGLRETLNLFKELFHDVLNLSDIKHLYSAIISRCLEIPERADTKSEEFTVHSTLVPIVDFANHEGTQKNAYFDIDPSNNDVLLLLDTKAVQSELTKPIEVFISYSPTEDLFSMLVTYGFTPDFRGNSQFWTVSFDRCFLRNYDGPDKTTNLRLFYKWMHINPVVPLVKYEHNGKTRWFLNDTTPEFDMLLLPFIPSIDDGKIARWAYDSTCHLMFTKIHCLINPEANEHALMIAENYRSLIKEKESNGDDFINLPPLAWSLRYKDTENDCVRQRHICSEDAVAVLKQEEMQDSTKTKSQFTSFFRKFLEFRRSKIIRPTSDSKVASILYQQELEIIADLAKAIDSSSTIFFSDLNVTLDTEPERLPPLRFLDDYIEISADKQEPSPICEDLSYYTPSRFTDFFQEEVSQYAAFFQDD
The following text describes a protein:
Function:
Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate which can then be utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. Shows broad substrate specificity and can also accept deoxyuridine and other analogous compounds.
Sequence:
MASVIPASNSSMRSDRNTYVGKRFVHVKNPYLDLMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFALFMHKELGLEEAEEDIKDICAGTDRYCMYKTGPVLAISHGMGIPSISIMLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVILDNIVTRSTELDKELSEELFNCSKEIPNFPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYKAGVRNIEMESTVFAAMCGLCGLKAAVVCVTLLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRRRLGLCD
The following text describes a protein:
Function:
Involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in processing of 18S-E pre-rRNA to the mature 18S rRNA. Required for the recycling of NOB1 and PNO1 from the late 40S precursor. The association with the very late 40S subunit intermediate may involve a translation-like checkpoint point cycle preceeding the binding to the 60S ribosomal subunit. Despite the protein kinase domain is proposed to act predominantly as an ATPase. The catalytic activity regulates its dynamic association with the 40S subunit. In addition to its role in ribosomal biogenesis acts as an adapter protein by recruiting NCL/nucleolin the to PRMT5 complex for its symmetrical methylation.
Subcellular Localization:
Cytoplasm.
Sequence:
MTSPVEDSEEMESYESFLMRKEQASLQEEGATKEDSEDEEQDEDDDWYWDGTYTNFKHYSSTRSSNPQANRNDIQSGSSKTYTVSDKVLQKYENKINLGKINISESVLNKVSEKSRKKESDTYRVKDKSDRATVEQVLDPRTRMILFKMLTRGVISEINGCISTGKEANVYHASTSSGDSRAIKIYKTSILMFKDRDKYVSGEFRFRHGYCKGNPRKMVKTWAEKEMRNLIRLNTAGIPCPEPIMLRNHVLVMEFIGKNDMPAPLLKNAQLSDSKARELYLDIIQYMRRMYQDARLVHADLSEFNMLYHNGKLYIIDVSQSVEHDHPHALEFLRKDSTNINDFFVKYDVAVMTVRELFEFITDPSITKDNMDAYLQKIMEIAAQRTEEERSSQDKVDEEVFKKAYIPRTLNEVKHYERDVDTMQKLKEEDMALNTQQDNILYQTVTGLKKDLSGAETVPALLQSSDHEEQLGSDPDDDEDDSANESASDSDEDIHPKDQGSQPEIDKKERKKQIKEAQREKRKNKVPKHVKKRKEKVAKTKKGK
The following text describes a protein:
Function:
Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for the assembly of the central element of the synaptonemal complex during meiosis, via remodeling of SYCP1 lattice structures and promoting recruitment of SYCE2-TEX12 and SYCE1-SIX60S1 complexes (By similarity). Required for chromosome loading of the central element-specific SCS proteins, and for initiating synapsis between homologous chromosomes. Chromosome loading appears to require SYCP1. Required for fertility and normal testis development. May play a role in apoptosis of spermatogenic cells and pathogenesis of cryptorchidism.
Subcellular Localization:
Nucleus. Chromosome. Note=Colocalizes with SYCE1 in the central elements.
Sequence:
MADSDPGERSYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFLNCKEEMEKNWQELLTETKRKQ
The following text describes a protein:
Function:
Efficiently inhibits forskolin-induced production of cAMP. Acts as a potent negative regulator of gonadotropin synthesis and secretion. Induces secretion of prolactin; Efficiently inhibits forskolin-induced production of cAMP. Blocks morphine-induced analgesia.
Subcellular Localization:
Secreted.
Sequence:
MEIISSKLFVLLTLATSSLLTSNIFCADELMMSNLHSKENYDKYSEPRGYPKGERSLNFEELKDWGPKNVIKMSTPAVNKMPHSFANLPLRFGRNVQEERSAGATANLPLRSGRNMEVSLVRRVPNLPQRFGRTTTAKSVCRMLSDLCQGSMRSPCANDLFYSMTCQHQEIQNPDQKQSRRLLFKKIDDAELKQEK
The following text describes a protein:
Function:
Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumor cells. In NK-cells, the presence of CD8A homodimers at the cell surface provides a survival mechanism allowing conjugation and lysis of multiple target cells. CD8A homodimer molecules also promote the survival and differentiation of activated lymphocytes into memory CD8 T-cells.
Subcellular Localization:
[Isoform 1]: Cell membrane; Single-pass type I membrane protein. Note=CD8A localizes to lipid rafts only when associated with its partner CD8B; [Isoform 2]: Secreted.
Sequence:
MALPVTALLLPLALLLHAARPSQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKAAEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV
The following text describes a protein:
Function:
Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II.
Subcellular Localization:
Cell membrane. Early endosome.
Sequence:
LCHLRQGVNSPQFSGVLRQAFVDFLKELKRNGVTIIVRVCEATYNTAILEKEGIQVLDWPFDDGAPPPRHIVEKWLKLIKQKFRQDPGSCIAVHCAAGLGRAPVLVAIALIEGGMKSEDAVQFIRQKRRGAFNSKQLLYLEKYRPTMCFRLRNSRCNCFVQ
The following text describes a protein:
Function:
Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MMSNLSRHQANCTSLSTALSPTPTFARIVKNRSTEKFSSTPYVASVFSNAIWLLYGLVTPNSLFVITISSVLVIIYGTYCALFWKHAVTFETRVATERLLFGAALVISVTAAITWGAVPEDRRTLLLGLFGDVLSVIQARISFVFGNRMHVWNVAAPLSVLGMVFRTKSAEYLPLPLCVNNLINNTVWGVYAILKADVFVGAPCIPAVLLALASVALIFHYGDGSKTAAGARAAASGTADVTYVGGGSMHGGVSVHRGASQRGRPNKLDMGAPLLERIDSMPESPTGTNGNELHSAVFVISDEEEVHGARNFHTPTQSGPQNTKGGETEGRGTPTATATREEAVADVASRRAAEKLTEASQGQSGARMPASFRTSVSRRSSFSQQEGL
The following text describes a protein:
Function:
Acetyltransferase enzyme. Acetylates histones, giving a specific tag for transcriptional activation.
Subcellular Localization:
Nucleus.
Sequence:
MDNSHAFVGDFGMNLNGDNRFMNQFNLGGNGNVSSGGMDLSGGLDFSSGMNLMTDSSMMLGGGSSSSTAGLIDFPDELNSPTTTANSGPSSRSMVGSSGSMMTAASAPMTSTADAIPFPASLAAESLTSGGTSASSSGSLDVMNFMNTTTTSSGMGNNGNGMGLDMNMGMNMNMGMGVNNMGMDMSGSNGFGMNDANQMMFNNMQHMNMMNPQGSYYVPQQQMQQQHYMQMMQQQRQLNLQRQQQQQQQQKALLERQRLAQQQAQKNNNNQQTQQQQAAQQKQQQMLASGQVPPQMSAQRQLSGGNPSVNSNVNAARSQPQASSQVAGSVSGATRPTWQSSADQALRKEMLNHIMRVLQNQRSNAPANWLQKLPEMAHRLEDECYRIAASREEYANTSTLQSRLRSIVRSAQTHQRSVGGNAMRQPGAPNQASPGDIRSASTVPTGAPIPFPGANAVGPTTNRANADVNNLAAQAIQMPPELQDPPSQVSTPVKTEVSRMQSSSSLIDSVMSNRSSMSGPGISPLAGQNGVQTTPGSSPNASGNASGMGTTPGSGSTSANSPGSATAARNKSAQIIWQFKAKAQQVTSALDKNQTTEYHNKLRLMVREDVKTAGSKEVLQRQQQRLLLLRHAMWCKSPEGSCTTTPSCGEMKRLWAHMGACRQTNACSYSHCISSKYVLSHFQQCTNAKCLVCQVVRYPVEVKEKNGALMLDADRALQQIIAASQRRQRMIAIKKQQEMQQQQQQLQQPQQSQQPMPLAMPAHLQQPQNNGNVAMGFQQQQQQHNAGPVGANANAMGMAMPNVDNRSVPMPTVQANGTTTGANGVVGQQVPVKAENPGAPTNLVPDDQRQLQLIKQKLSSRSLEQLTAHCLKLEKWVEEIRARMNAIMNECRQLLHLSNSTQDPMQKTQYEAQVQEKRVMLKQLDVKFKQCRSQRNIVKHVIDERNASGAMLTQNGGAQSHPGMNSTTNAMQPIPMPTQIQQQNPHQLQQGSTVSSMQMKPSPDDLLGEEDMDVPSKVDSSLAVAGKPLEMPMDLQESTATPVSVAAPLNTLAGSAPMNGPSVNHSQSQGTAHGQMQGYVMSNLSSAASGGVTVKEEVHGASLQSSSSAGSAPTQTFVKKEEVAINPLTMNNSKLNAMMVEHRRMDASKDLQLPAGAVATSTAMMASDANSCSAVATPPAPPASSEVPMSVLSELSNEDLASHVDSLVTYYNATVSPLNLKKKLEALLKGMMEHKFGWVFNTPVDPVALNIPNYFKIIRKPMDLGTVKKKLELGIYNHMEEFAHDVRTTFQNAMQYNSEDQDVFSLAKDMLSDFNGEMRKLAAEIDVDEKAARAKESSCRLCGIERMVFEPAVLYCNGECNSRIRRNCYYYTSADNKYHCCHQCHGSLPDTIKHNEGRQYHKSELTRKKNDEVHEEPWVQCDKCERWVHQICALFNGKIDSEKKPQLVKTESGQSTDSGDASASSSGSNPTTTVTTTTVVKSSASSGSKGTVHSITTSPGSEFLCPECLLEHRKSEPEKYKVGRHAFSAKDLPRTKLSDFLERRIIQSLKAEREDEAKWTQRDVNDVETAEGLTVRLVSNIEKQLMVRDKMFQRYKDSHKYTSEHRFKSKCICMFQELDGVSVLLFGMYVHEFDEQEADCNSRRVYISYLDSVNYFKPAHLRTKVYHEMLIAYFDFVKQRGFHTAHLWACPPLKGDDYILYCHPEAQKTPKSDRLRAWYVDMLVKAEEEGVVWQITNMYDDYWRDHNTPCALPYCEGDYWVGLVEDLIEKLDAEKPKKIVNKRGSKSHKRKNSDTKKAANKKSKSKKPKRRKTASGGEGSGDEDDDEGDGHEETAGSNRTLTVKSLDTPDWKLTDPLMHKLGEVIEPMKDDFLVVKLVPCCRVCNTSVVQGTLWLDPSVKTEHGLNPKVVQTALCDGCYQKLKVVSVAGSSAAHHRLQTRLNVLIKETVALPERCTDPDEINDSEFFDTRQAFLSLCQGNHYQFDELRRAKHSSMMALYHLGNPNPNAYVYECNACTRDIVSGNRWHCHTCPDFDVCDACYAKEKHEHPLEMVPTSGVGTAGSGPGGSTGPGAPGTGALTAEQRRLREQRAKNVRLHMQLLVHSSSCADGNCGSSNCEKMKELMRHGAQCKQRAYGGCTICRRVWALLQLHARQCRQYECKVPRCHDLREHVRKLQLQQQLMDDRRRAAVTQQYRQMQSERQQEQQSRAQGDEPMQQA
The following text describes a protein:
Function:
This is one of the three pore-forming subunits of the heterotrimeric epithelial sodium channel (ENaC), a critical regulator of sodium balance and fluid homeostasis. ENaC operates in epithelial tissues, where it mediates the electrodiffusion of sodium ions from extracellular fluid through the apical membrane of cells, with water following osmotically.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein. Cell projection, cilium, flagellum. Cytoplasmic granule. Cytoplasmic vesicle, secretory vesicle, acrosome.
Sequence:
MGTASRVSPARGGSVKAEKMPEGEKTRQCKQETEQQQKEDEREGLIEFYGSYQELFQFFCSNTTIHGAIRLVCSKKNKMKTAFWSVLFILTFGLMYWQFGILYREYFSYPVNLNLNLNSDRLTFPAVTLCTLNPYRYSAIRKKLDELDQITHQTLLDLYDYNMSLARSDGSAQFSHRRTSRSLLHHVQRHPLRRQKRDNLVSLPENSPSVDKNDWKIGFVLCSENNEDCFHQTYSSGVDAVREWYSFHYINILAQMPDAKDLDESDFENFIYACRFNEATCDKANYTHFHHPLYGNCYTFNDNSSSLWTSSLPGINNGLSLVVRTEQNDFIPLLSTVTGARVMVHDQNEPAFMDDGGFNVRPGIETSISMRKEMTERLGGSYSDCTEDGSDVPVQNLYSSRYTEQVCIRSCFQLNMVKRCSCAYYFYPLPDGAEYCDYTKHVAWGYCYYKLLAEFKADVLGCFHKCRKPCKMTEYQLSAGYSRWPSAVSEDWVFYMLSQQNKYNITSKRNGVAKVNIFFEEWNYKTNGESPAFTVVTLLSQLGNQWSLWFGSSVLSVMELAELILDFTVITFILAFRWFRSKQWHSSPAPPPNSHDNTAFQDEASGLDAPHRFTVEAVVTTLPSYNSLEPCGPSKDGETGLE
The following text describes a protein:
Function:
Nonselective cation channel probably playing a role in the regulation of membrane trafficking events. Acts as a Ca(2+)-permeable cation channel with inwardly rectifying activity. Mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal acidification and is involved in the regulation of membrane trafficking and fusion in the endosomal pathway. Also permeable to Mg(2+), Na(+) and K(+) (By similarity). Does not seem to act as mechanosensory transduction channel in inner ear sensory hair cells. Proposed to play a critical role at the cochlear stereocilia ankle-link region during hair-bundle growth (By similarity). Involved in the regulation of autophagy. Through association with GABARAPL2 may be involved in autophagosome formation possibly providing Ca(2+) for the fusion process (By similarity). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Possible heteromeric ion channel assemblies with TRPV5 show pharmacological similarity with TRPML3.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle, autophagosome membrane. Note=Recycles between the plasma membrane and intracellular compartments by a dynamin-dependent endocytic pathway. Under normal conditions, only a very minor proportion is present at the cell membrane. In the cochlea located at the base of stereocilia near the position of the ankle links (By similarity).
Domain:
The most N-terminal extracellular/lumenal domain (referred to as I-II linker or polycystin-mucolipin domain) contributes to a structure with a four-fold rotational symmetry in a tetrameric assembly; the structure contains a central highly electronegative pore with a 14 A diameter. The pore is critical for Ca(2+) and pH regulation. The protruding structure formed by the I-II linkers may contain all the interaction sites with lipids and proteins in the endolysosomal lumen.
Sequence:
MADPEVVVSSCSSHEEENRCNFNQQTSPSEELLLEDQMRRKLKFFFMNPCEKFWARGRKPWKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTIAFKHLFLKGYMDRMDDTYAVYTQSDVYDQLIFAVNQYLQLYNVSVGNHAYENKGTKQSAMAICQHFYKRGNIYPGNDTFDIDPEIETECFFVEPDEPFHIGTPAENKLNLTLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIRECKDWHVSGSIQKNTHYMMIFDAFVILTCLVSLILCIRSVIRGLQLQQEFVNFFLLHYKKEVSVSDQMEFVNGWYIMIIISDILTIIGSILKMEIQAKSLTSYDVCSILLGTSTMLVWLGVIRYLGFFAKYNLLILTLQAALPNVIRFCCCAAMIYLGYCFCGWIVLGPYHDKFRSLNMVSECLFSLINGDDMFATFAKMQQKSYLVWLFSRIYLYSFISLFIYMILSLFIALITDTYETIKQYQQDGFPETELRTFISECKDLPNSGKYRLEDDPPVSLFCCCKK
The following text describes a protein:
Function:
Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Subcellular Localization:
Cytoplasm.
Sequence:
MIVVLRLGHRPERDKRVTTHVALTARAFGADGIIIVSEEVDLKVKESVEDVVERWGGPFFVKFEKSWRKVMKEFDGVKVHLTMYGIHIDDIIDELREKLREGRDFMVIVGAEKVPREVYELADYNVAIGNQPHSEVAALAVFLDRLLEGKGLRKEFKGAKLKIIPQARGKMVVEVQKDAKQAEASGEGASRKNGQLPS