lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Single-stranded structure-specific DNA endonuclease involved in DNA excision repair. Makes the 3'incision in DNA nucleotide excision repair (NER). Binds and bends DNA repair bubble substrate and breaks base stacking at the single-strand/double-strand DNA junction of the DNA bubble. Plays a role in base excision repair (BER) by promoting the binding of DNA glycosylase NTHL1 to its substrate and increasing NTHL1 catalytic activity that removes oxidized pyrimidines from DNA. Involved in transcription-coupled nucleotide excision repair (TCR) which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes. Functions during the initial step of TCR in cooperation with ERCC6/CSB to recognized stalled RNA polymerase II. Also, stimulates ERCC6/CSB binding to the DNA repair bubble and ERCC6/CSB ATPase activity. Required for DNA replication fork maintenance and preservation of genomic stability. Involved in homologous recombination repair (HRR) induced by DNA replication stress by recruiting RAD51, BRCA2, and PALB2 to the damaged DNA site. During HRR, binds to the replication fork with high specificity and stabilizes it. Also, acts upstream of HRR, to promote the release of BRCA1 from DNA.
Subcellular Localization:
Nucleus. Chromosome. Note=Colocalizes with RAD51 to nuclear foci in S phase. Localizes to DNA double-strand breaks (DBS) during replication stress. Colocalizes with BRCA2 to nuclear foci following DNA replication stress.
Domain:
Both nuclear localization signals 1 and 2 act as a monopartite signal which binds to the high affinity site on KPNA2/importin-alpha; Both the spacer region (also known as the recognition (R) domain) and C-terminal domain are required for stable binding to the DNA repair bubble. However, both domains are dispensable for incision of DNA bubble structures.
Sequence:
MGVQGLWKLLECSGHRVSPEALEGKVLAVDISIWLNQALKGVRDSHGNVIENAHLLTLFHRLCKLLFFRIRPIFVFDGDAPLLKKQTLAKRRQRKDSASIDSRKTTEKLLKTFLKRQALKTAFRSSRHEAPPSLTQVQRQDDIYVLPPLPEEEKHSSEEEDEKQWQARMDQKQALQEEFFHNPQAIDIESEDFSSLPPEVKHEILTDMKEFTKRRRTLFEAMPEESNDFSQYQLKGLLKKNYLNQHIENVQKEMNQQHSGQIQRQYQDEGGFLKEVESRRVVSEDTSHYILIKGIQGKKVMDVDSESLPSSSNVHSVSSNLKSSPHEKVKPEREPEAAPPSPRTLLAIQAAMLGSSSEDEPESREGRQSKERNSGATADAGSISPRTCAAIQKALDDDNDEKVSGSSDDLAEKMLLGSGLEQEEHADETAERGGGVPFDTAPLTPSVTEVKECVTSGSSANGQTDSAHSFTTASHRCDTPKETVSLARAVKEASQISSECEVEGRPAALSPAFIGTPSSHVSGVLSEREPTLAPPTTRTHSDQGIDIHPEDPELQNGLYPLETKCNSSRLSSDDETEGGQNPAPKACSTVHVPAEAMSNLENALPSNAEERGDFQETIQLREVPEAAARELISAPKPMGPMEMESEESESDGSFIEVQSVVSNSELQTESSEASTHLSEKDAEEPRETLEEGTSRDTECLLQDSSDIEAMEGHREADIDAEDMPNEWQDINLEELDALESNLLAEQNSLKAQKQQQDRIAASVTGQMFLESQELLRLFGVPYIQAPMEAEAQCAMLDLTDQTSGTITDDSDIWLFGARHVYKNFFNKNKFVEYYQYVDFYSQLGLDRNKLINLAYLLGSDYTEGIPTVGCVTAMEILNEFPGRGLDPLLKFSEWWHEAQNNKKVAENPYDTKVKKKLRKLQLTPGFPNPAVADAYLRPVVDDSRGSFLWGKPDVDKISTFCQRYFGWNRMKTDESLYPVLKHLNAHQTQLRIDSFFRLAQQEKQDAKLIKSHRLNRAVTCILRKEREEKAPELTKVTEALDDAKGKTQKRELPYKKETSVPKRRRPSGNGGFLGDPYCSESPQESSCEDGEGSSVMSARQRSAAESSKISCSDVPDLVRDPPHGRQGCVSTSSSSEDDEDKAKTVLVTARPVFGKKKLKLKSMKRRKKKT
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
METPTPLPPVPASPTCNPAPRTIQIEFPQHSSSLLESLNRHRLEGKFCDVSLLVQGRELRAHKAVLAAASPYFHDKLLLGDAPRLTLPSVIEADAFEGLLQLIYSGRLRLPLDALPAHLLVASGLQMWQVVDQCSEILRELETSGGGISARGGNSYHALLSTTSSTGGWCIRSSPFQTPVQSSASTESPASTESPVGGEGSELGEVLQIQVEEEEEEEEDDDDEDQGSATLSQTPQPQRVSGVFPRPHGPHPLPMTATPRKLPEGESAPLELPAPPALPPKIFYIKQEPFEPKEEISGSGTQPGGAKEETKVFSGGDTEGNGELGFLLPSGPGPTSGGGGPSWKPVDLHGNEILSGGGGPGGAGQAVHGPVKLGGTPPADGKRFGCLCGKRFAVKPKRDRHIMLTFSLRPFGCGICNKRFKLKHHLTEHMKTHAGALHACPHCGRRFRVHACFLRHRDLCKGQGWATAHWTYK
The following text describes a protein:
Function:
Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSYPQAPSKFVNPDEIIPLSPPTKPPFAQYAASPLPATPHTPYSPPSPSRLSETIPLRPYLSLLPRILLTFFSPCLLPMILTIAHLIQNRSSTASLATSLKSSVLSACSGLAKAAASIKTLPRYLAMQTNQEAIRATQASILAIGTMLMDAITIIEAVVNFIVDTYRSLLLCTIELAVRGTLEILISAVQTISDAVTDTLNSVRSNIQDDIGDANDIIQTAVSAINRVTTLVNLNISVPEFSIPALSFLQNVTIPTTFEDGLITLNSSLPTLTDLKKKMDEIIDTPFEALISEINSTRLEMAASFNSSILSVPSLSSLSANSANDLSNDLCSDLDTSLIDDTAKALHKLSSIAIGLMFLLLFLIWAALAVWEWRKWKLMKDTVDAVNEEWDRDGKSDAWRMVAIVEHPVLERYSGTFLGKIAKMPRTRTNLRWFLSYLAHPTCLALLFISLFGFLSIQFQLVALNALKAHAQSSANSTVTASTNSLVTKLNAAALNSSQEYADSYNEAIAGYQDRINNELFGSWVNTTAVTLNSTLVEFYDEVEKALNASFGGTILYNPINTFMYCILGSKITNLEKGLTWISEHAFVDLPTFPSDILLLSNDSMNEIATPIAAAAVGSGDGGDDDDGVVGTLISHFESALKVERTFYGIMLGVWLALFLIGLAVVIWNSGGREKFMALRGVPSSSSPPGYGPPESKHPRWKAWLTNNHPIYDSYAEKQFRGTTPTNCLESYTHADVPNVNNGNDDHEKSFFKMRDSHAAGPFGSHATSAVRSTIASLAAPGQSFLKLSGRKLTDTTTPYDDKVPLAPVQTSEKYSRDHANSPFPRPSSESSESSAAQPFWVDKFYGAFEGVKSFFPTRSQRLGAALARKASQRTEGSFGASQVPTARTPGHDWIGGHQCLPEKKAEPEWSMVDPRMLGRALEDDKGRYPRVLPPSEMAAANYNPHPVYPRPMSRASTLGEGMVIPSTTSHPDPFQDMPPLPPKHKRASMDYVEEYESSHSRSSREDSRHGGVTSPASSSVSYFAAEPQLVSASKVQVGVAQKGGQATRALAEIVKELQEKRERKDPFGDDYERGL
The following text describes a protein:
Function:
Acts as a nuclear transcription factor that positively regulates the expression of heat shock genes. Binds to heat shock promoter elements (HSE).
Subcellular Localization:
Nucleus.
Domain:
The N-terminus is necessary for nuclear localization. The C-terminus is necessary for transcriptional activity (By similarity).
Sequence:
MKRRQKRKHLEIEESKEAGISKSQEDISHPESTGVPKAQSPGVGEVSSASEYFSCVSSPQKLIHRSKGTWKLLQDSSKPRSPLDQVPEGEATTAPSQQASSSCPSYKTCVSSLCMNKEERGMKIYYMQVQMKKGVAISWDTKETSESLEKQPRMEEATLPEGVWVGTPPSDVSTRNLLSDSEPIGEEKEHEEKPESDSPPGSPAVEERPRAKTPDWLVTMENGFRCMACCRVFATMESLQEHVQYGIREGFSCHVFHLTMAQLIGSMESESTQEEEEDHTEETEKPKEEKAEEQQPTEEDVGMKKPWSQCPGCVFDSPKDRRRRKDHCDNSGS
The following text describes a protein:
Function:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Subcellular Localization:
Nucleus.
Sequence:
MVVGPVVGSSSSGSSVSSAITSASPAANNNNNLPSYREQAEIHHQIMQLKQQQQLQQQVLLQRYQAQQQQLAHQHEQQMQEFLEQKKKAEEEARLERERHEKERLLALKNKEKREQSAVASSEVKQRLQEFVLNKKQREAAAAAAAAGNGTANAPSSSSAPYRAWTGAVPTLPASHGCSNNKGSTSQLSSGLGSGIVHPHPYRHPLLSGNFDDDFPLRKTASEPNLLKMRYKHRGTVERRNCSPLVARRRGGVPHHHLSAGSGPRMSQLTSNRRYSTNTHLVIEYFNDYPSLPPFHSIPGWTTFSEISPSQYHLMASHGQGSISDLTLYSSPSLPNISLGRPAIASHHAAEPPGLAMVSEVVDMRAAFSVRMGLPATGAGHHPLYQQPQPQHHPHAHPLHQHHHLLMPSGPPFFPPPPLDSGGGDYGSSGGSPESPGYIQKQMQLLEQAGHHTQILMSGLYNGAPITDAQVAQARLNKSGMRPLGRTQSAPLPLGHPLLQGAPHGVVPTVPLTQQQFDQYVRERHIYEQQHQHNLLKQQIRQTVLTRAGSRSQVENVEEETEAAVAREMSRDRERGAPLPEVIDLTEHKLEEEAEADRHSSRDGLSPLQLRVSSTRSSLQASPGSAFVPRGHHVARPLSRAFSSPLVSLDPPGAGPAGAGESGAAVVPMTLAAAGWGPSAGGAKTGSTSTALAYDGLMLRHQCMCGSNSAHPEHGGRLQSIWARLQETGAVHRCLRLRSRKATAEELQSVHSDVYTMLFGTEPMHRPKVDVNRFAELPMKNFVMLPCGGIGVDSDTTWNDIHTPSAARMAAGCVIDLAFKAAMGEIRNGFAIVRPPGHHAEAQQAMGFCFFNSVAIAAKQLRLRHKLERILIVDWDVHHGNGTQQIFYEDPHILYISIHRHDDGHFFPGTGNPLECGSEDGIGFNVNIAWSGGLNPPLGDAEYLAAFRALVMPIAQDFDPEIVLVSAGFDAATGHPSPLGGYQVSAACFGYMTRQLMELAGGKLVMALEGGYDLPAICDASHECVRALLGDEPVPIREEELARRPCQNAIDSLHKVISIQQPHWPIIKRYAFSVSLSAYEVEGVGRSRGEDSETLSAMAGLSVCRTDSSKSIAELSQEPMDQDESK
The following text describes a protein:
Function:
Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Miscellaneous:
MISCELLANEOUS: Overexpression reduces the sporulation efficiency possibly by modulating the function of KinA.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKIGKTLWRYALLYRKLLITAVLLLTVAVGAELTGPFIGKKMIDDHILGIEKTWYEAAEKDKNAVQFHGVSYVREDRLQEPVSKAKEAHIYQVGMAFYFVDQAVSFDGNRTVSDGKLTITNGDKSRAYAAEKLTKQELFQFYQPEIKGMVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQKMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNRMLNLNSLMSHNLVNVIRNLAFVCLIWHFGGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIVNQFSKLELARVSAGRVFELLEEKNTEEAGEPAKERALGRVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVERGNHEELMALEGQYYQMYELQKGQKHSIA
The following text describes a protein:
Function:
May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein.
Sequence:
MSTEEKVEMEAVPLKTDTDEAKTETTETVIDKKEAPKKTWFFKSDKKKVVTEEDVEEGKEKTKKKCFWRCQKEKKETGDEEEQKQEMTIGIDMQMRDEKQINNHVNIQFDDVFAEPETFHSVDCIWRINHRIFESTRTFFYKVFGILSIPIVFIFAILFAFASAVNNFLVMPLAALFTIPLTWIAKTWTFLVSNIFDPVANSIGLCFSKINVRKYGINNAPTDLIQA
The following text describes a protein:
Function:
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer. Produces a large proportion of the chitin that is not deacetylated to chitosan.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cell septum. Cell tip.
Domain:
The N-terminal myosin motor-like domain (MMD) does not seem to have motor activity but is indispensable for polarized cell wall synthesis via binding to actin that ensures the proper localization to the hyphal tips and septation sites near actin structures.
Sequence:
MAQQPPPSRFLGVTDLSSLAVTEDTVLVTLQERYISHKPYTSLSPAALVFLSPYSHLPIDDEESLLHYVEEYYQCNNEEGGSRNEQGWWKKKMEQPHVFQLALSAYYNMRRTGQDQVIIASGPTGSGKSELKRLAIEAITQVSLANPGKKGSKIGLQVSSAEFILKCFGNAHTLSNDEASRFGTYTELQFNERGRLEGLKTIVYYFERSRVSQAPINGERNFHAFYYLVSGAPEEERNFLKLGDVSDYRYLNCRVRRVGVDDRHRYSQLRQAFKLMGISSRLIAQIFQLLASILHIGNLRFSPSDGIQEGASVINVETLDIVAEFLGVHSESLAEIFSLKTVLVRKEVCTTFLGPEQAEQVRDELARTLYSLLFSWINEHINTKLCKDSFGSFIALVDLPGIQRNSGSMGSFNSVDQFCLNFAAEKMHNWVLHRVHETTRQEAETERLLISRVPYFDNSECLGMLSNPRGGLISVIDDLSQKKRSESNLLESLGKRFHNHPSMSISPQGNRSSASFTINHYDGPVTYSTSNFLERNANETSTDIIQLLRGDTTSRSQVSTTEGHGSSNPFIKGLFGMKNIAMQTHPRSDSTIVAAQQSVRPVRAPSTRRKKMMSLVPVSEEGGEETSDFQVGGGNDESYSSKELHCIAGQHWAAVDSLLKSFDQTQTWYIFALRPNDSQLPSQFDLRSMKQQVRSFGLVEMAQQLQTSWEVRLSHKEACERYNEELLYRGIPEGTGDVERLRDLKRLMSLNDADMGIGLQRVFLSHDLFRFLEDRLRAKEPGEQHAYEDLGHRKLQTDPFSPHRYQPTSFDSQDHVYKDPSIRPVDSSANLPLMEHAQPIVNSSLEIEDRESSAAPYVSYGGRSITDIEGYASSRDLLASSIHKSEKDPLDTEPQAGETTEVYRESIARRRWVWLCSILTWWIPGFLLSKIAGMKRQDIRQAWREKLAINMIIWFICGCAIFVIAILGPVICPTQHVYSTNELASHSYTLDPNNAFVAIRGEVFDLSQFAPTHLTAVSVVPTKSIMQYGGLDASELLPVQVSALCGGVSGSISQYVTLDSTNTTDVYSQYHDFRAFTNDSRPDWYAEMMIMMRHRFRVGFMGYTKKDLKKMAAQGKAVAIYDNLVYDMSNYIRQNGGGLKAPDGVNLTAQDQADRQFMSDQVVSLFKYNSGKDITTLLDNLGSTIGTDVVDRQKTCLRNLFILGKLDTRDSAQCQFSTYILLALSCVMVAVIGFKFLSALHFGSVRAPESHDKFVICQVPCYTEGEESLRRTIDSLCKLRYDDKRKLILVICDGNIKGFGNDKPTPAIVLDILGVDVNSDPEPLSFQSLGEGAKQHNMGKVYAGLYECAGHVVPYLVVAKVGKPNERQKPGNRGKRDSQMLVMHFLNKVHFSAPMNPLELEMYHQIKNVIGVNPSFYEYLFMVDADTTVDEMSLNRLVSAMRHDKKIIGVCGETSIANAKQSIVTMSQVYEYFISHHLSKAFESLFGSITCLPGCFSMYRLRSPDTNKPLFISHGIIQDYSENRVDTLHLKNLLHLGEDRYLTTLVLKHFQDYKTKFVRHAYAKTVAPDSIKVLLSQRRRWINSTVHNLAELVFLDQLCGFCCFSMRFVVFIDLLSTIIAPVTVAYIVYLIYLIVHDGSSIPTLSIIMLAAIYGLQAMIFIFRMRWDMIAWMIFYICAIPVFSFLLPLYSFWKMDDFSWGSTRLVVGDKGKKIVIHDEGKFDPSSIPLRSWEEYENELWDQESVHSGSYMPPKAEYSYDYPRTRSTYSHGGYAYGQPIHPMQTRSTSPVSSRYQMSQFRQSPYQSPYQGPYGGSTADFRSSRMDMAHRPSLDDTSSFHQPYQPAPRPQSSYAFNLPDPSSDSFTAPAVDYLGAQAITDSQLERSIRKICANAELDKLTKKGVRKELEREYGVELTERREAINRLVEKVLTE
The following text describes a protein:
Function:
Catalyzes the hydrolysis of phosphorylated glyceryl acetates in which the presence of a phosphate group is required for the enzymatic hydrolysis. Hydrolyzes a dibutyl glycerol derivative suggesting it acts on phosphoglycerol substrates with a butyrate leaving group. Also active with aromatic acetates and propionates. No activity with various sugar phosphates, with various nitrophenylphosphate or nitrophenylphosphonate derivatives, or with phosphorylated or non-phosphorylated sugar lactones tested. Does not hydrolyze non-phosphorylated carboxyesters with long chain leaving groups. No general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities detected when tested with the following non-specific substrates: p-nitrophenyl acetate, L-alanine nitroanilide, p-nitrophenyl sulfate, bis(p-nitrophenyl) phosphate, paraoxon, and p-nitrophenyl phosphate.
Sequence:
MSFDPTGYTLAHEHLHIDLSGFKNNVDCRLDQYAFICQEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGIDGTELKAGIIAEIGTSEGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQLALLQAHGVDLSRVTVGHCDLKDNLDNILKMIDLGAYVQFDTIGKNSYYPDEKRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDYLLTTFIPQLRQSGFSQADVDVMLRENPSQFFQ
The following text describes a protein:
Function:
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MHVTHLSLADFRSYARVEVPLDPGVTAFVGPNGQGKTNLVEAVGYLATLGSHRVSSDAPLVRMGAERAVIRAQVRQGERQQLIELELNPGRANRARVNRSSQVKPRDVLGIVRTVLFAPEDLALVKGDPGERRRFLDELITARSPRMAGVRSDYDRVLKQRNTLLKSAALARRHGGRTMDLSTLDVWDQHLARAGAELLAQRLDLIASVQPLADKAYEQLAPGGGPVALEYKPSAPGEAHTREDLYEQLMAALAEARKQEIERGVTLVGPHRDDLLLKLGSLPAKGYASHGESWSYALALRLASFDLLRAEGNEPVLVLDDVFAELDARRRERLAELVAPGEQVLVTAAVDDDVPHVLAGARFTVAEGTVERV
The following text describes a protein:
Function:
Acts as a signaling pathway regulator involved in innate immune system response. In response to interleukin 2/IL2 and interferon IFN-gamma/IFNG, interacts with signal transducer and activator of transcription/STAT which activate the transcription of downstream genes involved in a multitude of signals for development and homeostasis. Enhances the recruitment of CBP/p300 coactivators to STAT1 and STAT5, resulting in increased STAT1- and STAT5-dependent transcription. In response to interferon IFN-alpha, associates in a complex with signaling pathway regulator IFI35 to regulate immune response; the complex formation prevents proteasome-mediated degradation of IFI35. In complex with IFI35, inhibits virus-triggered type I IFN-beta production when ubiquitinated by ubiquitin-protein ligase TRIM21. In complex with IFI35, negatively regulates nuclear factor NF-kappa-B signaling by inhibiting the nuclear translocation, activation and transcription of NF-kappa-B subunit p65/RELA, resulting in the inhibition of endothelial cell proliferation, migration and re-endothelialization of injured arteries. Negatively regulates virus-triggered type I interferon/IFN production by inducing proteosome-dependent degradation of IRF7, a transcriptional regulator of type I IFN, thereby interfering with cellular antiviral responses (By similarity). Beside its role as an intracellular signaling pathway regulator, also functions extracellularly as damage-associated molecular patterns (DAMPs) to promote inflammation, when actively released by macrophage to the extracellular space during cell injury or pathogen invasion. Macrophage-secreted NMI activates NF-kappa-B signaling in adjacent macrophages through Toll-like receptor 4/TLR4 binding and activation, thereby inducing NF-kappa-B translocation from the cytoplasm into the nucleus which promotes the release of pro-inflammatory cytokines.
Subcellular Localization:
Cytoplasm. Nucleus. Secreted. Note=Cytoplasmic NMI localizes in punctate granular structures. Nuclear localization increased following IFN-alpha treatment. Extracelullar following secretion by macrophage.
Domain:
The coiled-coil domain is necessary for interaction with TRIM21 and for TRIM21-mediated ubiquitination of NMI; The NID domains are necessary for the interaction with IFI35. The NID domain 1 is necessary and IRF7 (By similarity).
Sequence:
MEADKDDTQQILKEHSPDEFIKDEQNKGLIDEITKKNIQLKKEIQKLETELQEATKEFQIKEDIPETKMKFLSVETPENDSQLSNISCSFQVSSKVPYEIQKGQALITFEKEEVAQNVVSMSKHHVQIKDVNLEVTAKPVPLNSGVRFQVYVEVSKMKINVTEIPDTLREDQMRDKLELSFSKSRNGGGEVDRVDYDRQSGSAVITFVEIGVADKILKKKEYPLYINQTCHRVTVSPYTEIHLKKYQIFSGTSKRTVLLTGMEGIQMDEEIVEDLINIHFQRAKNGGGEVDVVKCSLGQPHIAYFEE
The following text describes a protein:
Function:
Dimethylates the guanine residues at position 26 and 27 of one or more tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Sequence:
MEIVQEGIAKIIVPEIPKTVSSDMPVFYNPRMRVNRDLAVLGLEYLCKKLGRPVKVADPLSASGIRAIRFLLETSCVEKAYANDISSKAIEIMKENFKLNNIPEDRYEIHGMEANFFLRKEWGFGFDYVDLDPFGTPVPFIESVALSMKRGGILSLTATDTAPLSGTYPKTCMRRYMARPLRNEFKHEVGIRILIKKVIELAAQYDIAMIPIFAYSHLHYFKLFFVKERGVEKVDKLIEQFGYIQYCFNCMNREVVTDLYKFKEKCPHCGSKFHIGGPLWIGKLWDEEFTNFLYEEAQKREEIEKETKRILKLIKEESQLQTVGFYVLSKLAEKVKLPAQPPIRIAVKFFNGVRTHFVGDGFRTNLSFEEVMKKMEELKEKQKEFLEKKKQG
The following text describes a protein:
Function:
May be involved in splicing since overexpression antagonizes the suppression of splicing defects by SPP382 mutants.
Miscellaneous:
MISCELLANEOUS: Present with 1440 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAKRHSHYQGSRRRHARGSNSKKAGRGNAKGIQGRKIKKKPTPTNSWHNSSIPLGEGDLDDVGADFNPGRAFISPKTIEDYYFGRDAKSRSMKMGGLRPGNRYDSSTDLQAGRAAFRKRPMQFVKAKEVYDPSHNMIQKLRAKNETKNSEEIVEREADVFEEPGKMTSDVEYINNEDSENEDDDSQNSPSTDHSLSSNESKVEDGDLFFVDEEAQQSPDLTKIKRVCIEEIARPREVAIEFDPILTIGKVELSVSEGNESKEISVDVPNKGNKTYHPFAGYISNVLHGMHTSDSDNDELDYEIETENNSEPLYESSASSEVDQGFNYVGQRHNSRADNNLLPSPSPQLTEDIKCLSINGTKTFEGNNDNLPSPASEELEFGFKEEDFVINTNDIVVSNIRMGGVDNSYYLRCYRLLGDYDFHWIDQDLLTDFVVDELGLPEDRLPAYLNFIKNSLIPKIEPAEPTYSDIPISDSSDEGDSYEGDSYEDDEDMASSVVHSDIEEGLDDLIAYTLKHDTERFKTFETKSLETKGKGKKKKLLIDDALALDTETLETLQSKFSKRIETKAKKRKAKEDFIDQENRNSNDMLKKYPYGLHIQNIKDEFESFLSRNNDRLTFPPLDPHGNKTVMKIAKHYNMKSSKIGKANHTSVVVEKIKKTKWSSPNYSLIDQLMRQRPVFMRIDIRRPREEQAAFERTKTIRGKFHVKEGEIVGQNAPEIGNENIGRRMLEKLGWKSGEGLGIQGNKGISEPIFAKIKKNRSGLRHSES
The following text describes a protein:
Function:
Plays an important role in several reproductive functions. Induces Muellerian duct regression during male fetal sexual differentiation and plays a role in Leydig cell differentiation and function (By similarity). In female acts as a negative regulator of the primordial to primary follicle transition and decreases FSH sensitivity of growing follicles. AMH signals by binding to a specific type-II receptor, AMHR2, that heterodimerizes with type-I receptors (ACVR1 and BMPR1A), and recruiting SMAD proteins that are translocated to the nucleus to regulate target gene expression (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MQGPSLSQLVLVLMGALLEAGTPREEVSSTPALPREPRTGTEGLIFHWDWNWPPPGAWPPGGPQDPLCLVTLNGTPGNGSSPFLWVVGTLSSYEQAFLEAVRHARWGPQDLANFGLCPPSLRQAALPLLQQLQAWLGEPRGQRLVVLHLEEVSWEPTPLLKFQEPLPGEASPLELALLVLYPGPGPEVTVTGAGLPGAQSLCPTRDSGFLALAVDRPERAWRGSGLALTLRRRGNGASLSTAQLQALLFGADSRCFTRMTPALLLLPPQGPVPMPAHGRVDSMPFPQPRLSPEPEEPLPSTDPFLETLTRLVRALRGPPARIPPPSLALDPGALAGFPQGQVNLSDPAALERLLNSEEPLLLLLPPPTAVTAGVPAPLQGPVTEMWASSLARRVATEFQSAAAELRGFPGLPPTATLLLARLLALCPGDRGDPGGPLRAVLLLKALQGLRTEWRWRERSGPARAQRSAGTAVSNGPCALRELSVDLRAERSVLIPETYQANNCQGTCGWPQSDRNPRYGNHVVLLLKMQARGAALARPPCCVPTAYAGKLLISLSEERISAHHVPNMVATECGCR
The following text describes a protein:
Function:
Functions as a recycling factor of the spliceosome, a machinery that forms on each precursor-messenger RNA (pre-mRNA) and catalyzes the removal of introns. Chaperones the re-annealing of U4 and U6 snRNAs (small nuclear RNAs) released from previous rounds of splicing, an initial step in reforming the U4/U6-U5 tri-snRNP (small nuclear ribonucleoprotein) that can reassemble into another spliceosome complex; this step involves binding U6 and facilitating the unwinding of the U6 internal stem loop, followed by base-pairing of U6 to U4.
Subcellular Localization:
Nucleus.
Sequence:
MMDINSLLSPQDANSQSGRSAPASGSSSGNTPPAPSPAPKPLRKGRAAATNRPVMASSPLATHVYAPPSRAPEPSPPSSLGSAVNMGGKSGSGTPPTVDLQNSRQPSTPGMDTLADLASMQHHQPPRPRAANLRTPSYESQLSPSTIHPNVNQISHNTPTPRSSFDIAMSDGPRESARRDYAGSSLLPDARRMATELFARIQVNPQSYEAHVNFIRLLHDGFVNHVYPPNNPDIHGDPREYDLLKDMRTAREEMDKLFAMGEDLWAEWIQDESMLATSVNERIAVMELCQRSIEEEYGSTKLWIIYGEWVLYLYNSAHGDSSQSRWSEEDRLVGREVFTWQSVLDTWQRGAEATRWRIHDSHLVWDRLLELQVRDLSRNPSQDKIARVRELFDIRLQTPHATWDLTFQAFSNFISTYYNANYENIMAETAGKYATPVKDQYAAREDLEIRLRNAAESGDRAQEWAIFGEYIEWELNRNRRRRNTNFELINAIYQRAVLRFQTDANIWEDYIMFLIDESMHGNAHPTTISALDRATRHCPGSGTLWSQYLLSSEREGQPFTKIADIKHKATSTGLLDVGGMEEVLKVHTAWCSYLRRRAFLSEATDEDLDVAEVGIRSAIESVQELGEKKYGRSYEGDPLFRLERIYIRYLSESGSWDSARETFKGLMGRRGNSYEFWLTYYHWELVSWSKFVQGEATVDAARRTPNPSFATAVLKQAIKRTDLDWPEKIMQVYVAHCEDYEDSEELQLAILETRKAMRAINARRQREAQEAAAQQAAAAATETQEASQSEKRKREDESTANGLPTKRARADRASVEAEPVALRRDRENSTVVVKNLPQGTTEHKVRQFFRDCGAINGVKMMPGEDGKSEVAMIEFNTRDDAAAAQTRDQKTFDGNTIQVHFGSETTLFVTNFPPTADENYIRDLFSKYGEIIDIRFPSLKYNTHRRFCYLQFKTSVAAHSALALDGSAVGNGLHLVVKISDPSRKQDRNGPIYEGREIHVSNVNWSASEDDLKELFSRFGTVELVRLPRKVDGGSKGFGYVVFSSKEEATAALAMHEQEFRGRPLHVKVSAPQGAKRIAATVVTRVGKSQSPAPEANGAPPATDLEEPTGERRDRTLGLMNVPDTVNDARIRALAEPYGKLVKVVLRPDHQGAIVEYADVNHAGKAALELEGQEITPGRKLHIGTVGEMLKQSAEKKAPVQAPKPKDKPKSSFLTPTAPIKRPPQPGGRSGKRGHLGVKRGTAQPTSTTTTMTTTTTNASGEGSKNQKSNDDFRAMIQRSQEDSNSESAS
The following text describes a protein:
Function:
Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPDKVVDLGGIWKALSPQTLKDIEARIKEEEKRKKERQEAGEEEEDEEVEELQPNKKLEAGSALPDKYGEVPIELVGRPIEEIDDYYKTKWTFVVIAKDRTIFRFSTTNGCFLLSPFNPLRRLALFTLTHSLFSTLVMLTILVNCVFMALNDPPKITEFIFNGIYTIEMLVKLSARGYALQHFTYLRDPWNWLDFAVVVLAYVTMFMDLGNLSVLRTFRVLRALKTISVVPGLKTIVNALIQSVINLRDVIILTSFGLCVFALVGLQLYMGQLRQKCVMEFPENGMNLAEFCYKFRDASQNALPNEYLHCADDLKMFNGNDEEIEQPRWVVNWVSWKDYFNYSTPRYKDIKGQITPEKKGYCFPPPNDDPLFNETETVHDIMFEWIDDSDCNVSVVNATNNAAVWHAWYYNKDHWLMARGLDGLCRNKSEDDPFCNPGFRCLRIGGNPDFGYTSFDNIGWALLTAFRLINQDYWENLYQQVLGTAGHANMLFFLLVIFLGSFYLVNLILAVVAMSYEEASQQTEDEEEEAMGAAGESGSGSSSESDSESESSSANVAARRKRSGSRSSRSSSRSGSKCGSTCKVHPSCSIVSWTALNGAFPSNSNFLSMQDIEMQPDGEVEAVQEKHTMEETEKEKSEKEIAVRKAGFVRDDEEYDSSDWETDDEEPPTPLQIAFNVLCGWKCPPCWNVIARISFLFICDPVMELFITLCIIFNTVFMAMDYHDISQNKPFEKTLEVGNYVFSGIFAGEFFFKLIGMGPKDYFAVGWNMFDSFIVILSCIEILMEQLMGGGLAGFSVLRSFRLLRVFKLAKSWPTLNKLLSIIGNSMGALGNLTFVLGIVIYIFAVLGMQVFGECYRTWTPLLDRPRWNFEDFLRSFMIVFRVLCGEWIESMWDCMRCDIVKFENCPGHENPEEKGVRYTCVPFFLLTVLIGNLIILNLFLALLLSSFSGLEESGDEGSGEPNNIVIGVNKIIFFFKYIIYCFLPCFVPKPKKNWPPFDQEEEEDAEDEGGDDDEEWKIEKTYVDGEVPTMDGEAVVLQNGYVGKRPSLAESGTPWSSQNGIPVAMCGFNSEMDIIDVTKAPRKKKESESNEKESENQYIPDGECIKDNKEMEESKDENKDGNRSSSTSNGLSKASTTPAKSSSEPSLCQKENGVVPMMDKIGNGLGSIPDKLSDGVLSNGKLSEGMLDPAYTPTKLSDGVLNMDEKPDGDLPDDPGSPGSKEKQSDYASSGVIVEYPPDCWPEKWAMPCCDECIKSPIGIKFAALRVKAYWIIEHNYFETFIIIMIVLSSGALAFEDKYINTEEKIIVKTVLGYADYAFTVIFTIEMVLKMLGYGFKTYFTNAWCWLDFIIVMASLVTAIPNLMGMGDSVPESLKTVRVIRALRPLRAISRAEGMKVVVNALIGAIPSVTNVLMVCLVFWLIFAIMGVQLFKGKFFKCMDEVNNPGEFKMKTCIIFNETFCNDPIAEVIPATCYDLNKNEKPACVLMEGPTDYCETQAICQECNNLYKTPTKIAELCEDFQEMCNITCPASYNVGYKVTEDVEDFLCYDENGGLKGPEMYFNKSVCLARNKTWENYKINFDNVGIAYLSLLQIATFKGWIQIIEHAVDGTDVDLQPVRDFGSMWYLYFVIFIIFGAFFTLNLFIGVIIDNFNAQKKKPGDGDGSSADLFMTEDQKKYMEQMKKLGSKSPSKGIPRPDNNFQGFFYDVAMTQAFEVVIMAFIMFNMLTMMMEHEGSSQKFKDILEKINLVFIAVFTGEMVWKMIAFGPKYFSQGWNIFDFVVVVMSIITQGLEDVMAALPVPPTLLRVIRVARVGRILRLVKGAKGIRTLIFSLLVSLPALVNIGLLLFLIMFIYAIFGMMNFAHCKRMQGLNEVINFETFFNSIILLFQVCTSAGWDGILNGLQDQLIPTINGTTPTKEQIDAGILDDIDKCWSLSRYTYLGIFFFVSYLIMNFLIVVNMYIAVILDNFSAATEEAAGGGVTEDDIDMYYSLWERYDPHASKYISLSKISQFVHQLDDPLRIAKPNKITLAYLDIPICTGDRLYCKDILKRLTERAMGTFDNDKEAVDEEEEEAVTTDHPEDYQRIGSTLTRRREEVAAMVIQRAIRKYVLKHDFDKEQAPQIIF