lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the decarboxylation of the cysteine moiety of 4-phosphopantothenoylcysteine to form 4'-phosphopantotheine and this reaction forms part of the biosynthesis of coenzyme A.
Sequence:
MEPNSGRLPGLEATGPQMEPRATSSAAAPLRRQFRVLVGVTGSVAALKLPLLVSKLLDIPDLEVAVVTTERAKHFYSPRDVPVTLYSDADEWEMWKRRSDPVLHIDLRRWADLMLVAPLDANTLGKVASGICDNLLTCVIRAWDRSKPLLFCPAMNTAMWEHPITEQQVGQLKDFGYIEIPCVAKKLVCGDQALPAAKEPHLVMRTCLLEVLGHEHAPLTSFRVRRLTCAEPCVLGTHDLYFIHHPVRRALPPSPS
The following text describes a protein:
Function:
Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.
Subcellular Localization:
Nucleus speckle. Nucleus, nucleolus.
Sequence:
TRAWESEVMGSGPGSATCQLCDLGQVDPASMPTWAAGSTARLQELRATRQSQGMRSVYVSGFPRGTDPSQLSQYFQTFGPVSGIVMDKDKGVFAIVELGDVGTREAVLSQPQHRLEGHRLRVRPREQKEFRALAPGSLGGRPLDSQQLVRALAEAPDVGAQMGKLVELWELSGPERQLRELVVALMQEVFTEFFPGCVVRPFWVWYGRTGSLGHLALPFPQQDLKVPDSPGLDSALASPVDAQVLASTSASPPASPQDSEPPVFPVAPRTPDSALASETPASPQSSPSGSPLGRGSAEAAQGKAGEEKATLELVGSVLRGCVPGVHRVRPVPSARRPVVKFCHRPSGLHGDVSLSNRLALYNSQYLRLCSQLDGRVRPLVYSLRCWAQGRGLTGSGPLLSNYALSLLALYFLQTRSPPVLPPLTQLNQMAGEGEQVEVDGWDCSFPQDASRLEPSTNVEAVSSLLSQFFSCVSAWDLRGSVLSLREGRALAVAGGLPRGAWGGLRLGPLNIQDPFDLSHNVAANVTGRVAGRLQSCCREAASYCRSLRFRRLCPRGRDWGLLPLLRPGPRDPPPPPAAPIPLPPGPAAQRRWAADWDEGARGGGRRRRGGTPQGGGSKRARRAGGERGPQEEQKPPGSGEQPDGGGDREEQSGGEEKMGLELRRHGREPALAAGGQPSPVGADAGRPPAREPGGGSGTEEGQETPSPSVATWRWALDHRAWQGRRRARRQLKKEAGASWLEAEAQVTRELRRQELGEPGPETDPLLTFTASASPSGLVLSPGHDPQGLFPDLHHFLQSFLPQALRHALKLGRVV
The following text describes a protein:
Function:
Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.
Sequence:
MGTVVSTLQRPTLYVSMDSSHAQFVRDTISGNKVVIFSKSYCPYCSMAKEQFRKINVKATVIELDQRDDGNEIQAVLGEMTGSRTVPRCFIDGKFVGGGTDVKRLYEQGILQKYFQ
The following text describes a protein:
Function:
Protein phosphatase that shows typical type 2C protein phosphatase (PP2C) activity. Catalyzes the dephosphorylation and concomitant reactivation of the E1 alpha subunit (PDA1) of the pyruvate dehydrogenase complex. Required for efficient mitophagy in stationary phase cells.
Miscellaneous:
MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion intermembrane space. Mitochondrion matrix.
Sequence:
MRLGNAYAYCKPSQNVGLKLDLLRGLPGYVGHATSRINRLENQDNYSIKMMRSWPNAYGSALNCSVFDGHGEKGAQLSQLLADKLCSSLDFPEPSWDKQDLKKLVQEYARRFPEGNYWKHKLSTFEKFYNKFIKNCNSKQELLLMKEGDSAILGQNGGRMIFDKMGNIIDKIALLTELDRLRLFYGFARFDLDQCCGLGTAAGSTASSIFLYPYDDPNAPIDEGKDDDSWIISHSGLLKLIVTQVGDSKIILCDQDGIAHALTTTHHINSSRERHRLSIDPSRLDPDAFGETRFLNNFANTRSFGDVAGKPYGISSEPDIFSFLVGNTLHLPRSERSKLPFNGDECFLALVTDGITNKLADQEVVDLITSTVNSWGLKKATPQFVAEETIKFIQAIATKHSDNATCVVVRLSNWGNWPNVDRTGPQRETKLMNAQSNETKLN
The following text describes a protein:
Function:
Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function; Serine protease component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. C1R catalyzes the first enzymatic step in the classical complement pathway: it is activated by the C1Q subcomplex of the C1 complex, which associates with IgG or IgM immunoglobulins complexed with antigens to form antigen-antibody complexes on the surface of pathogens. Immunoglobulin-binding promotes the autocatalytic cleavage and activation of C1R. Activated C1R then cleaves and activates C1S, the second protease of the classical complement pathway. It is unclear if C1R activates C1S within single, strained C1 complexes or between neighboring C1 complexes on surfaces.
Subcellular Localization:
Cell surface. Endoplasmic reticulum. Golgi apparatus. Secreted.
Sequence:
MSVFRTARTSFILWFLLYVLVCECLPLSDSDTVMHGELHSPQYPEPYPPNALEQWDLTVPEGFQIRLTFTHLDIEASDGCYYDSLTVLHNGKLLWKFCGNENSGDGNHPGHQPILSPGNSLTLIFQSDDSNPERHQNVGFFAHFQAIDVDECSAPETGNGPLCSQICLNTLGSYLCACHHGYELRSDKSTCVLTCGDGIFDEPEGHLSSPGYPNLSPYSLSCQYVISVKNGFTVSLNFSDIFHIESVDSENGPHCLHHWLQVTLPNKEPVKLCGKKSPGLIDTNSSSVTLEYHTDNEGMSKGWSLDYSTGRMKCPMPGSVTRGRVTPSMTEYFYRDHIYVRCDQGYKLMMNTQEIKTFSTVCQSNGQWHLPLPECHIIDCGDPEPLLNGGVTFLSGSQNQYLSLVQYHCNEPFYSLEGDQNVTFTCEADRQWRSNDLAVTKPTCLPVCGQPTQEIRDFLRIFGGKDAPQNTIPWQVLLTVGSGRGGGIIIADKWIMTAAHVLAHKGQQVSKDLVKMYVGGTEVGAMINSPLYAESVHVHPGYDSVDDLSYNNDIALIKLGNPLTFRAAVMPVCLPAKDSSYTTGKIGLVSGFGLVNDNGSRILTNRMKYVQLPLVDRKKCNDSFNLLKERKHKVPHLTNNMFCAGTPEGGKDACQGDSGSPFTLTENKQFWVAGIVSWGVDCGLAGAYGVYTKVVEYLDWINRTMQEN
The following text describes a protein:
Function:
Catalytic subunit of the glycosylphosphatidylinositol-mannosyltransferase I complex which catalyzes the transfer of the first mannose, via an alpha-1,4 bond from a dolichol-phosphate-mannose (Dol-P-Man) to the glucosaminyl acyl phosphatidylinositol (GlcN-(acyl)PI) intermediate to generate alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol and participates in the sixth step of the glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MRTWHVVALAAVVRAVLICWAEYQDSRMAVKYTDIDYVVFTDAARFVANGGSPYQRATYRYSPLLAYLVLPNIWLHPVFGKVLFSTADLLVAGLLSHLLRATGASPRLRAIATAAWLFNPYTATISTRGSCDVLSVLLLLGLLVMLLHGADVAAGALYGLAVHFRIYPVIYGPAIVLFLLRRAAVRQGLVRLRPGNASSSSSSSSSSTGGGGRGSLRQWAGAVRPAAAFCLAAAATFAVLGAAFYYLYGNAFLNEAFLHHLGRKDPRHNFSPYYYPIYLQGYAAAAPGSSSSSSAAGLAAGGDGATSMPPPPPRPGQDGAATAAAAAVELAARLLQPLWGLMERLLPLQEPWRLAAAPQAVALMALSAAYHADLPSAWLLQTWAFVTLNKVVTAQYFVWYLCLLPLALPALAAQTAVPAAALVGGGAVWVAAQLHWLGWAYQLEMKGRSVHVGLWAAGLVFQLANTAAVVLLARALKGAGAAAAAAPKAAAGSAGPQAAPLTAGHGDAAGVEDEGGEDEGGEGAGGEGGGRRQVLSFLEASLRVQGVLAPPPGGQRLGPGFVSPERKQQ
The following text describes a protein:
Function:
Transcription factor. Involved in responses to transient and long-term shade. Required for the light-mediated inhibition of hypocotyl elongation. Necessary for rapid light-induced expression of the photomorphogenesis- and circadian-related gene APRR9. Seems to play a role in multiple PHYB responses, such as flowering transition and petiole elongation.
Subcellular Localization:
Nucleus.
Sequence:
MEAKPLASSSSEPNMISPSSNIKPKLKDEDYMELVCENGQILAKIRRPKNNGSFQKQRRQSLLDLYETEYSEGFKKNIKILGDTQVVPVSQSKPQQDKETNEQMNNNKKKLKSSKIEFERNVSKSNKCVESSTLIDVSAKGPKNVEVTTAPPDEQSAAVGRSTELYFASSSKFSRGTSRDLSCCSLKRKYGDIEEEESTYLSNNSDDESDDAKTQVHARTRKPVTKRKRSTEVHKLYERKRRDEFNKKMRALQDLLPNCYKDDKASLLDEAIKYMRTLQLQVQMMSMGNGLIRPPTMLPMGHYSPMGLGMHMGAAATPTSIPQFLPMNVQATGFPGMNNAPPQMLSFLNHPSGLIPNTPIFSPLENCSQPFVVPSCVSQTQATSFTQFPKSASASNLEDAMQYRGSNGFSYYRSPN
The following text describes a protein:
Function:
Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins.
Subcellular Localization:
Virion membrane; Multi-pass membrane protein. Host Golgi apparatus membrane; Multi-pass membrane protein. Note=Largely embedded in the lipid bilayer.
Sequence:
MSNMTQLTEAQIIAIIKDWNFAWSLIFLLITIVLQYGYPSRSMTVYVFKMFVLWLLWPSSMALSIFSAVYPIDLASQIISGIVAAVSAMMWISYFVQSIRLFMRTGSWWSFNPETNCLLNVPFGGTTVVRPLVEDSTSVTAVVTNGHLKMAGMHFGACDYDRLPNEVTVAKPNVLIALKMVKRQSYGTNSGVAIYHRYKAGNYRSPPITADIELALLRA
The following text describes a protein:
Function:
Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function.
Sequence:
MDIDLSRRNKKPRLLLESERERLEEFIDSIHYSARYSDDQFEYRHVQLPKNMLKKIPADYFDSSKGTLKLLWEEEWRALGITQSLGWEHYEVHEPEPHILLFK
The following text describes a protein:
Function:
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Sequence:
MSRLLLALIKRSNFVTSQTKGCRLPSATFNRSLSILETAEAKSLPSKVRSFVEDCVKLCQPSQVHICNGSEQENRSLIQQMQQQGMIESLPKMENCWLTRTDPADVARVESRTFVVTTKRSDAIPNRMDGVAGQLGNWMSPDDLPKAIQERFPNCMKGRTMYVVPFSMGPVGSPLSKIGIELTDSPYVVASMRVMTRMGQQVLETLGEGDFVRCLHSVGSPLPMTRPLINSWPCNPDQTIIIQCPETSEILSFGSGYGGNSLLGKKCFALRIGSVIAKREGWLAEHMLILGITNPQGQKKYIAAAFPSACGKTNLAMLTPTLPGYKVECVGDDIAWMHFDKEGRLRAINPENGFFGVAPGTNYATNPNACYNFFLYAMLTIQKNTIFTNVAKTSDGGVFWEGLEKEVTGVDITSWLGDANWTKSSGKPAAHPNSRFCAPASQCPIIDPLWESPEGVPIDAILFGGRRPRGVPLVYEALNWKHGVFVGASVSSEATAAAEHKGRSIMHDPFAMRPFFGYNAGNYLGHWLSMEKPGRKLPKIFHVNWFRRSTDGSFLWPGFGENSRVLDWVLKRCDGADVAESSPIGLIPKQGSIDTNGLKEQVNWEELFSLPKNFWQDEVLDLEKYFSEQFGNDLPNAIAEELHKLKQRVNQM
The following text describes a protein:
Function:
Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein. Note=Localizes to the division septum.
Sequence:
MNATLRILAWLIAVALVALPVVAVLNGWVGAERWPLARLRVSGDFKRVPAEELRAVVLPYARSGFFAVKLQDAQDAIARLPWVESAQVRKRWPDVLEVHVVEHKPFARWGTDRMLSEQGRLFRTPPLLKDFKLPQLGGPDAKTQEVVALYNESRALFAPTGLDVERLEMDARGSWSLGLSNGVQIVIGRDDARARLQRFARVLPQLTDPQRPIARADLRYTNGFTVERRMENGESGMDKKPKPVPPAAPHALVLNSLRLRTPLLTIPHSPFAIPGFKT
The following text describes a protein:
Function:
Involved in dynein arm assembly, is important for expression and transporting outer dynein arm (ODA) proteins from the cytoplasm to the cilia. Acts as a crucial component in the formation and motility of spermatozoal flagella.
Subcellular Localization:
Cytoplasm. Cell projection, cilium. Dynein axonemal particle. Cell projection, cilium, flagellum.
Sequence:
MGWITEDLIRRNAEHNDCVIFSLEELSLHQQEIERLEHIDKWCRDLKILYLQNNLIGKIENVSKLKKLEYLNLALNNIEKIENLEGCEELAKLDLTVNFIGELSSIKNLQHNIHLKELFLMGNPCASFDHYREFVVATLPQLKWLDGKEIEPSERIKALQDYSVIEPQIREQEKDHCLKRAKLKEEAQRKHQEEDKNEDKRSNAGFDGRWYTDINATLSSLESKDHLQAPDTEEHNTKKLDNSEDDLEFWNKPCLFTPESRLETLRHMEKQRKKQEKLSEKKKKVKPPRTLITEDGKALNVNEPKIDFSLKDNEKQIILDLAVYRYMDTSLIDVDVQPTYVRVMIKGKPFQLVLPAEVKPDSSSAKRSQTTGHLVICMPKVGEVITGGQRAFKSMKTTSDRSREQTNTRSKHMEKLEVDPSKHSFPDVTNIVQEKKHTPRRRPEPKIIPSEEDPTFEDNPEVPPLI
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent rRNA methyltransferase which may methylate two specific adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 12S mitochondrial rRNA. Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA. In this complex TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand. Stimulates transcription independently of the methyltransferase activity.
Subcellular Localization:
Mitochondrion.
Sequence:
MWVPGAGIPSRLTLSAFTRAARFCVLNSGVARWKDVPAENCRGLYDFHTQLKPDVEFGKLSSRLYKSRSETKRYVTSPRVAETVVRVLRGKRKAGQLILECNPGPGVLTRALLESGARVIALESDKNFIPELKSLGNSVNGRLEVIYCDFFKLDPRNHGMVTPPVMTSDMLFQYLGVKAHPWKKGFPLKVVGILPAKTERNTLWKILHDLYSCSSVYKYGRAELNLFISEKECRKLTANPQTPALYQSLSVLGQTACGIKVLCTEPSSLFDTYAIKGELEKQRHRESLEQNLCFVQLTPHRNLFTGTLTPFNYDVFFHMLRQCFMKRNAKLIDHLPSLSPIDAVHILKQIKKKKDVRVVDMYPKDFLRLFETIECSKDDTCKWLYDEFMEDALS
The following text describes a protein:
Function:
Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
Sequence:
MPGAPNVLEDVHRSCAEVAALHREHVSINDAALAELAAELAAAADDVRGAVRGLPLPIRFHSLEQELTLLALFHLLDFGSGHLARPESRRQSGGRDWREALQYGLLGLHLGGTRLDSHKLKSFSMYDMNQVFGLDATVEVPVMPGVTMSKPGPLQPLCKSLLAALTDTGAQLAEAGHKTPGELLLAIGEELAKAGRTSASAFVEELVDTLPAFRDTVLYDGRTLVLQRRAQNLAADLACVYGGREGGGRFAFPDVDQLAGDSGPTTIAALRAKGVLQVADPDLAATLDSGAELPAGPHERALRAAAVVACDRLAAAANAAAGSSGGATVTESGAGQSLPAEADAEGKEAEAEAGTASEGAGEGAGAEPSGTGAATAASAAAQAGGDSGSRKSGAATATATAAAAAAAIRPVDVGAYLCYLTEPGRELADRAKPHVTLGVTGY
The following text describes a protein:
Function:
Multifunctional transcription factor that induces cell cycle arrest, DNA repair or apoptosis upon binding to its target DNA sequence. Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Negatively regulates cell division by controlling expression of a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2.
Subcellular Localization:
Cytoplasm. Nucleus. Nucleus, PML body. Endoplasmic reticulum. Mitochondrion matrix. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity). Competitive inhibition of TP53 interaction with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and subsequent translocation of TP53 to the nucleus (By similarity).
Domain:
The N-terminal and C-terminal disordered regions undergo liquid-liquid phase separation (LLPS) following homotetramerization and activation. Post-translational modifications, such as phosphorylation or lactylation affect the ability to undergo LLPS; The nuclear export signal acts as a transcriptional repression domain. The TADI and TADII motifs (residues 17 to 25 and 48 to 56) correspond both to 9aaTAD motifs which are transactivation domains present in a large number of yeast and animal transcription factors.
Sequence:
MEEPQSDLSIELPLSQETFSDLWKLLPPNNVLSTLPSSDSIEELFLSENVTGWLEDSGGALQGVAAAAASTAEDPVTETPAPVASAPATPWPLSSSVPSYKTYQGDYGFRLGFLHSGTAKSVTCTYSPSLNKLFCQLAKTCPVQLWVNSTPPPGTRVRAMAIYKKLQYMTEVVRRCPHHERSSEGDSLAPPQHLIRVEGNLHAEYLDDKQTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDPSGNLLGRNSFEVRICACPGRDRRTEEKNFQKKGEPCPELPPKSAKRALPTNTSSSPPPKKKTLDGEYFTLKIRGHERFKMFQELNEALELKDAQASKGSEDNGAHSSYLKSKKGQSASRLKKLMIKREGPDSD
The following text describes a protein:
Function:
Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
Subcellular Localization:
Cytoplasm.
Sequence:
MKVKAPGRINIIGEHTDYNDGYVLPFAVNRYVFLSIEGSERFIFHSENVNETVEMEKIEKLNKWTDYISGVIASFEKRGYRVSPVKISVSSNLPIGAGLSSSAALEVATAYAISEYFGFNVPKLELVKIAREAEVEFVGVRCGIMDQFTAVFGKKDHAIFLDTMTLEYEYVPLKLEGYEINLVDSNVKHELSSSEYNRRRQECEEVLKTLEKKSFREVTKEDLERLSGTLRKRAQHVLEENERVLKSVQALKEGDFETLGKLLFSSHESLRDLYEVSCEETDFIVDYLRGKEGILGARMVGGGFGGGVIVLSKKGAFGKIKEELVESYRKRFGIDLIFHEIESSDGVQKI
The following text describes a protein:
Function:
Essential transcription regulator during early development. Coactivates transcription of some euchromatin genes and repress transcription in of euchromatin genes translocated to heterochromatin.
Subcellular Localization:
Nucleus. Cytoplasm. Chromosome. Note=On polytene chromosomes, it mainly localizes to transcriptionally active euchromatin sites but also localizes to heterochromatic regions such as the chromocenter and the chromosome 4. Cytoplasmic in nursing cells and growing oocytes.
Domain:
The PHD fingers mediate the transcription repression in heterochromatin; The SAY domain is essential for fly viability and transcription activation.
Sequence:
MNDLRQQQMVAATSSSGSESGTAVESAAATSTAGSAGAAGRPQSNCSANSNAKSVAASSTSEEEQRVSSTSSPAQRDQQLNADRDREQEPEPQQQQQREEALQHQHNQPGHITSTTASPPPTLPPPTTPCDDAPSTTGASASASSASGEAPSAASAAGAAGGPMAATALEVESEERDGHKIILKLSKHANPNSNANESQPGGDERRVEPLRIQLPCGGAEGGLVAKQQDAFDADASSCSSSCAEDEVATTLGQQLRNTPHIVPKLTIRAANERRVGSVVPKLTIKLPENPAASGSNSNSGSCSAAVSGAQSAMPAKNDAHLSSLSPASASSSSASSSSSSSSSSSLAEMQTVPKLMIKTTLAGSSCISSSEELPQQQQQIPKLTIKTGGGGQEHVHTVIMTHDLNNAQSIPKLTIKTKSIEMIEDEQAAKLEQQLQPLPKLTIKNLCSPKHKVRAVLEEKPPTAASKLAIPKPTPNPTPAPMTNGGESNSSSQEFCGFSDPDADIAAPASDDVRRNSDDMVIDDSLSKEHDPKIFHNLPPMPASNGIASGGSKASKASKSAQSQHNVVDMVDLTSSPSPGSSPTHVPNNFTGRISPKGLLIDCLRMQTAIGCYVPEEADSRVRPAASPNSNILLSQLTAPAKSFTTTTPKSKSSKYPQLTERLMANGSGTGGGSVIAAESEAVVGPLPAANPAQSIIESIEILDTPDGSPRVAYMDEDSNPMLNKHLQTIHKLAMDHGVEQRMDTQDNNNENHLKRTNSEGNESPSSRLPPSKQRRLDNDENDQQTQNCHDPARKCSESLQALPPSHRSRKQKHERILNTDLEGSLFPPTQQQSISTPDQNGALSSEVEGEDAKAQDPLEPATPQPPPVATPAGTGKKRGRPKRIQNQSSPDGGGAVTPKPGTPQEEANSAVKSRRVQLLRKRLAIDMVSVGQEQADMKAKEKESSVGVPNARVEDGLAETLESPKTRDHRPLRATRRTTTSTNTNLQPTPKSTRKRQSKASVQQSQLPPPTMAQFGSSESESNNNNNSSISFALSAQIDLTMCSSSSSTSSGAAANQQVIGGSGSSSMLPPTTILSSSDPLPDVIFQPNDFSSIMATQQLRSSRPSSISCGSTGGSQPDCHDEDNYTSALDNSGDETALPMPPTRGRGRGRRSRGGRGRGSSSVDRAVSVGGTASTTPATQPRAPRMSRGASAVAKAIAMSRPRCVGGLKHQPDPERLKGLFSPSPQVFEEDTRMSADLSNSNQSMASLMEPPLTPQKQPDFLNNEESQSSMVSNVSMMDSNQGQSADAILGSALKRPKKKKMETCVAEDTDYSASSIAEYDWPPPKGCCPSKNRDTFMIQEQVALYLGITSFKRKYPDLPRRSVDMEERNWLQEKGLVSEKLCDLGITAVWASDILDIMYADFFDKYEEYKEYIRRKHLREIEAKQKALGLTVGAGRGLQARDRAMLSATKWNAYFNKSRKDERQSCMDLQTFTINQPQPRTAPTCTRLERSTSDLIRAVAEEANIPAPPNLLPPRDYDEAFRNSDYAYPLTVVPDQFSMAYRQFEPAELRAYPLDTALDKPPTDLMAQLLQAKSEAVGSDEIKTSAPAPKDLGQEQSAIKSVTVTAPVRRSRRSTRQQTDKVRTASSSSTSSAQSVSSASSGNGSSSDTESGDESDFSSTSSCSSSTGASSGAGSEDEDGNECSSSVRLSTCGVCLRSQHRNARDMPEAFIRCYTCRKRVHPSCVDMPPRMVGRVRNYNWQCAGCKCCIKCRSSQRPGKMLYCEQCDRGYHIYCLGLRTVPDGRWSCERCCFCMRCGATKPEGLPQVAALSQASGGPSANGDRSKAARNKRLKWVHEYRIDHVTKIREHAAMFCVPCARNKPAKRQSAAGAAGAAAVTPVLEATSAQTDDSPMPSPGLTTNGGRALSPTAALSPKAAVPVASLPPVLEATTVTTNIAGTIGRRQAGNAVNITTMQCSSSSSSNFSGNGVTEDAANVTATGTATAAAGAPAATPIGIAPPPVVA
The following text describes a protein:
Function:
Catalyzes the reduction of FAD with the concomitant oxidation of NADH. NAD is the physiological electron donor. Subsequently, the reduced flavins diffuse to the oxygenase component NphA2.
Sequence:
MTETAGELDPEVTPLHLRKALGRFASGVTIVTTAECEDEDSVHGMTANAFTSVSLDPPLVLVSISTRAKMDTKIRETGTYGISILAGDQEPVSLHFAGAAHEPDRVRFVWRRGVPLLEGALVHLACTVVASHPAGDHTLHVGRVEQLWYDDGHPLVFYTGSFRSLELLGRDEPWGF
The following text describes a protein:
Function:
May play a role in ethanolic fermentation during anoxia.
Sequence:
MDTKIGSIDDCKPTNGDVCSPTNGTVATIHNSVPSSAITINYCDATLGRHLARRLVQAGVTDVFSVPGDFNLTLLDHLMAEPDLNLIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSVLNAIAGAYSENLPLICIVGGPNSNDYGTNRILHHTIGLPDFSQELRCFQTVTCYQAVVNNLDDAHEQIDKAISTALKESKPVYISVSCNLAAIPHHTFSRDPVPFSLAPRLSNKMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKACDAFVELADASGYALAMMPSAKGFVPEHHPHFIGTYWGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGYSLLLKKEKAIVVQPDRITVANGPTFGCILMSDFFRELSKRVKRNETAYENYHRIFVPEGKPLKCESREPLRVNTMFQHIQKMLSSETAVIAETGDSWFNCQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQASPEKRVLAFIGDGSFQVTVQDISTMLRNGQKTIIFLINNGGYTIEVEIHDGPYNVIKNWNYTGLVDAIHNGEGNCWTAKVRYEEELVEAITTATTEKKDCLCFIEVILHKDDTSKELLEWGSRVSAANSRPPNPQ
The following text describes a protein:
Function:
Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
Subcellular Localization:
Nucleus.
Sequence:
MWEERLGAVDFAFDGDILQGDPPNMSGVIDLCDSDQESPVNSKTTKSTLQDDDSSSSSSSSSDDEIWNTNVPFSQGSTTSTSRIGKRSVAGRGGAAGGTKSLTINEEYDEDDVGEGSSRQKANHYRKFGSKRATTSGAGASVSAANTSKKKSIPTKPNGADVDCIEIDLSSSDDERGNASVPAKNTATQRDSQLGDYFSHSNFDNKVARKSQVQFDSSDDENNNNDDSMVYNHDGLNGKGALRNKEIAAKKTKVLIPYENKKKSCYDSDSQSSSLGSNLAAKKAKVRNPYEKKKKCCYDSDSSSSSLESHPRGVAFSGNSRRKKKGAPIATSTDVPVSQTKEKVHNPYKKSSSNNTSTTGSNNSTQQKKAYESDIDDHSSSTASLLEEKKSNAKQHTFSPLTEENQVMSLDTDSDIGELAKTTHKIAEKMSRQSASDDSSIEKPPAKKANAMKSVDFSFELRGAFDSDDDNFSGGGESDSDDLMEPRVAVDSDHDEEDAKPAAKPSAAQSFTLRDRVGTDFVEMESDDDDSSASSGIPLFTPRPFKKATKGSKSVSDAKAAANAAILTSEAGASNTAPDKKCPNTAASSSSASSKLLTPRLFSPPLNSPLRTFAVKRKVPTPAIPAMSKEMMNEIGGKLYPDLRHNFMVALVSHAKRLRMNAYERSGYDSALRSVVALSLHLQPLRSAEAARRIKGVGTNFYDLMKESSAGTKGKTPFAPKKNKYSTVTAAALVALLELEEGNKGVASAGGQSFPMEELITVINSRLDPAANSSLNSTTEKYLEADNMDPYWTQVKRLCTANAAADLDGPFVKERKRKTACKSGVVFELLDRGRLMAHKLRELAKAGPVEPGPLRQLPNETVDEEFGNVCMSMDCREGGGAGKSLHKMCDQLDIRGVPYVVRELKIADYIFFVGDKLAPILIERKTSEDVAGSLHDGRWERQQRTMRKAQFVLGDGPARRCQICYIIEGDANKRKVHGGNVGRRTYFQSVEDVENATEQLPLLGFSVMRSKGTLDTIGILAKIAQDVSWKANNGNIDVKFTYKQFLSRVKALPDEMGDPPTSREHQNPAPPVVVNASLTQPANPPPPGNGHNDTFTVQDNMDKSFSATSQDQDPDLHDIHHDENIAAAAELRKLSMQALKEQCKERGEKLGGKKDDLISRLLKPRKPELLIMRMRRGEYVPKVPSCNAALMVALLLHHVPGTQGLAKERLMVLAEETGVSKESMGGDGGNFYDGWSGVKQLQEGDPALVKREKGHRYSLTTQPPDSAGIAVAHALHIVAHREGLCQCGQDVS
The following text describes a protein:
Function:
Involved in synaptic functions in photoreceptor cells, the signal transduction in immune cells as a Src family kinase activator, endosome recycling, the uptake of bacteria and endocytosis, protein trafficking in sensory neurons and as lipid-binding chaperone with specificity for a diverse subset of myristoylated proteins. Specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated GNAT1 and is required for G-protein localization and trafficking in sensory neurons. Probably plays a role in trafficking proteins in photoreceptor cells. Plays important roles in mediating Src family kinase signals for the completion of cytokinesis via RAB11A.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole.
Sequence:
MSYSCIGTEAVCNSQDSSSSSAQRSGTSKSNNPSGGSGRSAESSDHQTQDTPTPKPLVAMRVKKGCNSTETGVPVTTEEELLRKPVITPEDVLGLQKITENYLCSPDENVYSIDFTRFKIRDMETGTVLFEITKPPAAERGQGDKKDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPINNFRMIERHYFREQLLKSFDFEFGFCIPSSKNTCEHIYEFPPLSEEIMREMILHPYDTQSDSFYFVDNKLVMHNKADYSYSGGP