lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the reversible hydration of carbon dioxide to form bicarbonate.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSACVPARADSARTKHVHPPHSPPPHGPRRFRVAGADVSAAIAVFLIALPLSLGIALATGAPLQAGLVAAAVGGIVAGRIGGCPLQVSGPAAGLTVVTADLIQHYGWRTTCAITVFAGIAQLGLGCLRVARSALAVSPAIVHGMLAGIGVTIAVAQLHIVLGGTPQSSVPDNLVALPAQLANLHPADLAVSVLTLTLLLLWPRIPGRAGQALGKLPAALIAVAGATAVAALTGLRLPKVDLPSWSSHALASLPDGPVLGLVAAVLTTTLVCSVQSLLGAVAVDKLVAARPSLTGRVKRSDLDRELLGQGAANIVSGSLGGLPIAGVAVRSSANVAAGAVSRNSTMLHGVLVVIAALLMVPALELIPLASLAALVMAVGLKMVSLNHIRTVTRHREVLVYAVTTCGVVFLGVLEGVALGIAVAVGVALHRLTRTRITHDETEGVHHVHVRGQLTFLAVPRLSRVLHQVPHGADAVVELDGSFMDHAAYETLQDWQKTHTAQGGSVDITGRRPGTRISEPAEEDGCRCRPWTPWRNHQCERPPTAPPRGTAGRSATDGSPAGNLGTSTGPNTPGTRDATGARGATGGSSAPDGPTGHELARGISAFHRNTGPLMRRELARLAREGQQPSQLFLTCADSRVVTSMITSSGPGDLFVVRNVGNFVPLPGEESGDDSVAAAIEYAVDVLKVRSITVCGHSGCGAMQALLAAEPGGARTPLQRWLRHGLPSLERALPDVDVDVDLNEQEQKRGAGRARPRLAGRGAADTAERLCLANVVQQLEHLRAHDSVARALGAGDLELHGMYFHVGEAQSYLLSEDAEGSVFELVRETNLTA
The following text describes a protein:
Function:
Contributes to the wild-type cellular response to nitrogen stress through signaling pathways that regulate the expression of genes involved in amino acid biosynthesis. Required for wild-type filamentous growth, cell growth, and cell-cell adhesion (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Cell tip.
Sequence:
MGMGFNPIKALFTGIGTVCVGVGALLSILCIINQTQHNIAFQNIYFIQLNTTSIFSVANQTAVVNNTSNLLNELTGTLVDTLETYIDQGATDLIEQVEQEMKDVSELPDWYSIGLWNYCQGNSSDYTNPTYCSTPSPSYYFNPLTMLETSINNATGSQINITLPSEVDLGLKVLKGACYAMRAMYILGFIFFALTIVSIVISCLPFFGPLFLNVFSFFATIFTFIAAVIAVATYRIAISELEKNIEILNIPIVLGKKIYAYSFLSAAAGLAACILYFIGNLTSGYSPL
The following text describes a protein:
Function:
Formins play an important role in the nucleation of actin and the formation of linear actin filaments.
Domain:
The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).
Sequence:
MEENTNNIDNGHMGDNNNENNNNSNNNNNNNSNSSSSFVKGRIDSLNKSTNGLIKIGRSVENSNNSITSGGSSSNSGEISSNNNNNNNNNGILKNSTSGSKDNTPLSESSINLRSIKTSGENKLNSSSSSNSNNNNIGVINKGVSTNLKSIMNALSSKSSENLSNFNNNNSLSSSPLKENQLVKSFDKNITPSKNNSPRAHLNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTTPTLNSPRNKNSIYNTNSNNNSNTTNSTPNSAITPNIIVENKIKEKIQLWGMLKSNCKKYKDMELNQIETSFGRGSADYNFDDEKVVSSNHFKIILHKTVLPYGISNGSLNNSPKPLSTIIPSSNTITTATTNNNNDNAESLTTYSESSEISTDSTGVCSSSSSTSSTLSSKSSSSSSFNKFMEFLLIYIEDNDSTNGTWVNGNKLNRGERVQLDDKSKITLSTPDFSSLSFTFESNISSLSDEEKGKLLKAIVILKDSLDDSTNSFGSSTTTTISGGGSGSSSVNSSGGGSGTTPINVTPNSSNVSVTKKVINRTPSFKMSNLSTKPEGFVSILKNEPTLKNIQLLLSTIKTSDDQWKENFIQTDCILMIVDLLSSNYKKLRYNEIDQAIDIECLSILSTIFTCSKSNQNALKQLSKSNELNFNDIFMLFLLNQQNSNHSVKTKSQFLQFLNSITSNEICHKMIISSIEKIHSIKKDKLKFKWLVESMVFESDFQYKLQSLTLINSLLSNCKNQTTLTKIKSDLQSLGIGKINDLLVLDSSIKEMSIQLTKFNNNFNSSSSSSSISSNSINNSQNNNNNNNNNNNTNNNNNNNSNNNNINNNNNNLNTRKNNFNCKTLNLKDPISLVLLLQNELKSNFSTSVPTSPTSKNPLITSNNNNTSIGNNSNNIITSILTDLYKIANNNNNNNNNTNNKPKMDSNSALTLLSDFSKIISSSISNEQEYQKSIPVLEEKIKILIPSFNNTCNNTTNNNSSAKNIEVDSSVNKSPNTEEDSTKKTINNSPAEDAQIVSASVPPPPPPPPGGNNNNESDVPSSSGGPPPPPPPPPPPGKSSGGGPPPPPPPPPKGGKGGPPPPPPIGGIGSKVVKVKEEQPSVPMKQLFWSKVPVAKTKKTIWENKSDKFELDKIQIEQLFCQKKPANGKGSPKDGIEKEKEEKLELLDPRRSYAVSILISKYKLTPIWVIDCLTSMDDKKLSKDMVRVLLHIVATNEEEEQFKKYEGDKSQLSDVDQFIIETLKVPKIRQRLECIEYKIQFESTLQELVLNAKCVQQVSTSIMSSTSFHGLLHFILRIGNYMNAGSSRGNAEGFKLGFLLTVGNTKSLDNKTSLLNYIIQFISEKYPQFLITKSTIPHLEQASRILWSEMLSQFEQLKSGMSMVQKELELQIKQIGSDNFTHKFKKFTSSKAEHLDSLQIFIKQVEETYQSTIAYFCEENIQPEEFFQIIFNFINLVLKVHKENEDIRIAALPKSKKYQEQQNKPTQNNDHSTKSKLSNLPSSSSINDESSSSASLSSLSTNVNANTENDNLELSKLGFLSKLRKKRSKSEQEPVVEPIQITPKVGSAASAEPSPSIKSRDKKESFKSPIFRSPKFKVSSISPKLKATLNSISKTLRKQQVESPSPNMSPFTSTAISEKASIYDKNINNIQPSSSSSSSSSSSSSSSTITGKKSHNTESEIKKEFISNSSMDKDKEKIKEKEKGTISKGKALLFGHSRSKSTTTSPSSSSSKKQIPSLSECLQESNKTHSRSSSYSPNSKVNSQLMSNPFIMMEQKQPKDSLPIAKDSKEIHNMGTTTTTTPIKVEKIVSVNEKPTIVTMQTKPIPLVPTTTTSTTTTTQTTPPPVTINEKEKETQSKEVITKDFRDIKLKQTGIIEEDRKIQQERQRQFKTFNGKLNSTNKFRTSSSAVFSRNKSLQNINSTKNPSSVGFGDLDLFQKENITINSIKQKLLLKQTQIRSTRTDSSRIKKGKNVSQIVKQVENESPLPNPNKTLSAIRRHNSNLSRKSSKSSNNSSTSSLESLVQTNVINGLNNLKSVSSSSSSSSSMVVNKNGIDDNQQKQQKQQQQQQQQQQQQQQLPQPQQQQQQQQQQQQQQQQQQQQQQQQPQQQSTTTTTISTHHPQLKQVQPQSPSSLSQQPTQQILKPAQPSSPLQSHYKPQQKPQTTYIPKPKPYIANPFPSSTTSTNSSPSNASDLTEVIKSTQSPFEREQTFTKPTLQPVKYPSSASSNSSSVSGSSQSTPLSAASLQPVGNRNLRKQHVTPPSSSISNSTATTKSKKEGNIRFVDQASPSSSSLEQSSNASNAGYTSPPRENSFSNLFKKHKKSHSKSKSTDNTLNGEIESVDENEKSRKKPKTVTKIIDFSKKLFSHKKSKSVDQSSKSNNTNNNNNNNNNNNNNNNNNNSNIDYNNSLNDVGSSSSFSSSSSSPTSNPFPIIQPPNQSPPTKNISSGNISNNTSYSSLGSMNGNNLVASPSSSITSCKPSPGAVSSTSSTLKTPDFFDHKKVQTPEQLGIKSTDIPKVIIIPPNFYQQPV
The following text describes a protein:
Function:
Nonenzymatic cofactor regulating the function and conformation of the RNA polymerase and part of the transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. Acts as a chaperone for newly synthesized free N protein, so-called N(0). Plays a role in virion assembly by acting as a bridge between N and L.
Subcellular Localization:
Virion. Host cytoplasm.
Domain:
The N-terminus is disordered and is involved in binding N(0). The region of interaction with the L polymerase is necessary for transcription. The hinge region is highly variable. The central domain is involved in oligomerization (By similarity). The C-terminus is basic and essential for binding the N-RNA template.
Sequence:
MDNLTKVREYLKSYSRLDQAVGEIDEIEAQRAEKSNYELFQEDGVEEHTKPSYFQAADDSDTESEPEIEDNQGLYAQDPEAEQVEGFIQGPLDDYADEEVDVVFTSDWKPPELESDEHGKTLRLTSPEGLSGEQKSQWLSTIKAVVQSAKYWNLAECTFEASGEGVIMKERQITPDVYKVTPVMNTHPSQSEAVSDVWSLSKTSMTFQPKKASLQPLTISLDELFSSRGEFISVGGDGRMSHKEAILLGLRYKKLYNQARVKYSL
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC).
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane.
Sequence:
MAPLSTAVGSNTATAGFTSVNSHRNTFNDPEIIEIDDDDDDDEPMGDDEEGNEEEEGINDGDEYEDESVENGDEEDEPEEESAEDMNGTESPLELVPAPNGRGGSDVFTPGLFTSAGARQALHPLRRTADRVTRQIEAFAERLDRFKQKGRTDDFGNYQAAYQLVKSYQVLAQDAIQDITKQNTLKRAKMGWSTSRTNGTASHDPKIEEELQRLQLEANTWQLLLNLISIDDPPSKASCKKAQETVFQKLHRYSSDREVWESFLSADHYALECVIIMKWLERTATTTPQDIDSLISELESQAERGQGHWTHGWLYTKETIKGQKRLRAWPQPLEPKDPGITASLLTSDVSEPLITQLDPDAVTRQKQHLQKQDQFYERATWMTCWKMLRQGENWTKIRDWAEERLENWKAVSLCGSSVDPESGGERTPVDDGMTRMMNFRSQESWRAACSALARNPHIEDFERAVYALLCGETEAAFKVCQSWDDYLYVHFNSVVLSRYQGFCKQFRRKLSHSPTAPVNFVPEPVGYSDFNKFVQYTKGNERIGVEARNPYRTIQAAILGKGYDTFFYSLAKAVSQVAKTGSEDSFVPDLSPTHVDDSLLIAAEDDDALRIATHLYIIASSIGYVRSDTQFFETASVNVIGYIANLEDAGIYEAIPLYASLLPAPQTHSVLGRVLIEILDPRERKQQVRLIEKYDINIEAVLEDQWNWISSTVSAVEHTRTVKRYPKVVRRDDGTRELVPVKTDFIGTEISRSDERLIRSLEWLRYVDGQWGRICHLGAFLYRKFYLSGKLAAARELSRRMKLSDISRESFGFDVAEFGYGIPNGSDRATPEPSSPTKSRLLGSAHKLNRPIPNGVPSDEQTNILVMQSQTMRDLEELTLAFDGLERFGLCWKKIDKCVSIYVLNRNGLLTDVAFRSKRRRDSGAVKDLRDELQDTLDEISMHVDAVLDEWLTAPADEAEEAELEEIRVTYIPELFLDYHNALYFSAHVLTSEILVQCMNLAMQVSENEYLTRSFVSSRRMAELVDALALSSKAMVQTRVKPGKRLLGGESLGIWTVEVPEDEEQEFLRQAK
The following text describes a protein:
Function:
Glycosyltransferase that transfers a rhamnosyl group from UDP-rhamnose to soyasaponin III in the biosynthetic pathway for soyasaponins.
Sequence:
MDSVALNGKSNDKPLHVAMLPWLAMGHIYPYFEVAKILAQKGHFVTFINSPKNIDRMPKTPKHLEPFIKLVKLPLPKIEHLPEGAESTMDIPSKKNCFLKKAYEGLQYAVSKLLKTSNPDWVLYDFAAAWVIPIAKSYNIPCAHYNITPAFNKVFFDPPKDKMKDYSLASICGPPTWLPFTTTIHIRPYEFLRAYEGTKDEETGERASFDLNKAYSSCDLFLLRTSRELEGDWLDYLAGNYKVPVVPVGLLPPSMQIRDVEEEDNNPDWVRIKDWLDTQESSSVVYIGFGSELKLSQEDLTELAHGIELSNLPFFWALKNLKEGVLELPEGFEERTKERGIVWKTWAPQLKILAHGAIGGCMSHCGSGSVIEKVHFGHVLVTLPYLLDQCLFSRVLEEKQVAVEVPRSEKDGSFTRVDVAKTLRFAIVDEEGSALRENAKEMGKVFSSEELHNKYIQDFIDALQKYRIPSAS
The following text describes a protein:
Function:
Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome formation. Required for the Cvt vesicles completion (By similarity).
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. Note=During pexophagy, accumulates in the vacuolar membrane region, where the peroxisomes contact the vacuole.
Sequence:
MTARGKNVRIQSLATEDEIFVYDRRFVSEPENVELPELPSPEPFTPDTPPDTLTNQNDLQAWRNLYMARRSWALGLVERCGAMDKSIHEHNERTDIIHRAAGVALENLKTHVGNLENRFQEAQTWANDLLKEQRAALDGWQRALTTLESIPAPKVFPFLGRPSTPKEHRDRPTGTLRDFVDANEVQKAGAEAAAESSRFARQIDDVAEAVRGITADTQRLIDDQLPSGADAADGLQEMITFAKKISSDYEHVIALPNNQKTLANISRLALTHTQDLLPSMLDISAEIHAGLEEAVRRHNTAMKVALDHMRTISAIELRLADVQSQIINLNVQSDAFDVVFSVYHMPMVYGSILVESVRRREFNEKMKADSLTLAEEMAVFRDEEQRRRKKWLKSMGDFISLTETTTPGVEINLQGLDYEWPEVSRNDIESYIEHLKSRPAMASLADGLTQQYKDLDAPTRHQRRRAKAFKQGSIFDLSRSSLLLRSDDMLRSLREEKSKLEEKLKGSESRIRKLEDLLHRQSQLSRPVSGNFNLEFPSSPASPYPDELSRRSSVSSRRMSANQSSEDKTLAQRIVTLEAELNAERETVQRLQKEAHAERLSNTDKIQEAQSTKRDLIDNLEARQREFDEERRYLEGELKKYRLRTEELEEELDRITDSRDHAKQDADERINQLETELQNLHIHTEEELHRANDLLEQMQAQKMTEESLQQRINELEKQQSEIKATEQENLQTLQAAFMNLSPGGAVPAEIPSIIKAIEVLSEGLSIHVKNAEEKMAEAVAENKALEERMNQLETEVQDAKQSAEQRESELAQVRGELAQEKEKLAAVQSELHDERSKLNALQSQHADGDTGTDALRQRVVEDERKLGILSQRLAEVEAQARESEKEVCAWKNKLKAISESEREATTRIEIRGSRAKELSQQLFEQVEKMEHMLEQLGFTVIRQDGEIVVQRASKVNASSGIGDSLAQSGVVSVKPDPSLLDWMQAETAQEETDRYMAFLESLYQFDVDVFGDAVVKRVKDIELLARKWQKEARGYRDKYHRMQSEAHDKIAYRSFKEGDLALFLPTRNQAIRSWAAFNVGAPHYFLREQDAHKLQTRDWLLARITKIEERVVDLSKSMNGAHPDRRSIGGTSDAASIDDENPFELSDGLRWYLLDANEEKPGAPATPGLGKSTVAPAHVDARGSIRLKRTSNGGNVAKTLTKSLDSRRNSSSSKKGPPFAISQRANESTAELARPAEANTPLSPSAQEAASTPEEVRRDQLQGP
The following text describes a protein:
Function:
Transcription factor, which binds preferentially the consensus sequence 5'-TAAGT[AG]-3' and can behave as a transcriptional repressor. Plays an important role in normal prostate development, regulating proliferation of glandular epithelium and in the formation of ducts in prostate. Acts as a tumor suppressor controlling prostate carcinogenesis, as shown by the ability to inhibit proliferation and invasion activities of PC-3 prostate cancer cells.
Subcellular Localization:
Nucleus.
Sequence:
MLRVPEPRPGEAKAEGAAPPTPSKPLTSFLIQDILRDGAQRQGGRTSSQRQRDPEPEPEPEPEGGRSRAGAQNDQLSTGPRAAPEEAETLAETEPERHLGSYLLDSENTSGALPRLPQTPKQPQKRSRAAFSHTQVIELERKFSHQKYLSAPERAHLAKNLKLTETQVKIWFQNRRYKTKRKQLSSELGDLEKHSSLPALKEEAFSRASLVSVYNSYPYYPYLYCVGSWSPAFW
The following text describes a protein:
Function:
Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Subcellular Localization:
Cytoplasm.
Sequence:
MPKFTPEELAVNAVPVIRQATSGDAEPDWRPLFRHECTFNPVIFQDVMLNLIKNPNINSSWLFRADILYDTEKNIQNGLETPLSELGDVPDIPSFDGFGLHRRLIRRLIPRSTMRDKPMDQTCLIYQSKGSDSEGGLQRHLVIYLPHVSTEAEMPYYHPTVRGIAFHHEWSPTETRGSVSVSYLYFEGGERPEKLTRIASHLLQAVYKHGQGRADGYQKRVHHDLLVPQDRVQNTYTALKQKYARALIESWVESTDPTKHVFEDLCIAAFLIELWTDIYGRNFFPGFVDIGCGNGLLVHILNLEGFKGWGFDARSRKSWATYSTRLETPTGVQESLQQLVLLPPPVSRAGISEISSEGFREELVHDGRFPKGTFIISNHADELTPWTPILAAISDCPFIMIPCCSHDLTGARFRAPAPKDKKKANSAYSSLVSWVTQITADCGWVAEQEMLRIPSTRNTAIVGRKRQGDVSAIDIGVIVDRYGGTAGYLETVVKLVKSTNLDEKH
The following text describes a protein:
Function:
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Subcellular Localization:
Cytoplasm.
Domain:
The C-terminal coiled-coil domain is crucial for aminoacylation activity; ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Sequence:
MKENIPSVYSFNEVEEKWYKYWLEKDYFHAEVDRSKKNYSIVLPPPNITGSLHMGHALNATIQDILIRWRRMQGFNALWIPGTDHAGIATQMVVERELLKEGKTRWDLGREKFLERVWQWKENYGNTIVEQLKKLGVSCDWKRFRFTMDEVYSRAVIKAFVELYKKGYIYKGERIINWCPRCKTALSDLEVRYVEENSFLWYIKYPLYQEDGYIVIATARPETMLGDTAVAVNPEDERYKALIGKKVVLPLVGRIIPIIADETVDPSFGTGALKVTPAHDIDDFEIGKKHNLEFISVIDENGIMSENAGKYKGLSVLECRKKIEEDLEKEGYLLKKEPYLHDLATCDRCGTPIEPLISEQWFMRMENLAKPAIEVVEKGEVKFIPDRWKKVYFDWMYNIKDWCLSRQLWWGHRIPAWYCENCGHVNVEEQKPEKCERCGSENLRQDEDVLDTWFSSALWPLGTLGWPEDTEDLNYFYPTSVLSTARDIINLWVARMIMMGLEFRKEVPFYYVYVHPTVLTREGKRMSKSKGTGVDPLELINKYGADVTRFGLAIQCTEMQDLRFHEENFENTKNFTNKIWNAARFVISNLDFNIDYNEVDLTKHSLSLSDKWILSRLQKTVYEVTDHLENFRFSEYVKTIYTFFWSEFCDWYIELSKPRLSNTEDPESRLIAQVILWKVLKESMQLLHPVMPFITEEIWQKLPSTHESIMISKWPEVNELFIDEEAEKDMEFIMESIRSIRAIRSEFNILPNEVINVEFLTPNKYKEILLQGYSGYFYTLAKAKLSTILEKRNLKHVAHKIVEDVNFYVNLEGLIDISKEREKVKKELEELYLLIDKVEKRLSNKDFIEKAPPEVVEKEKEKLESLKKKVEFLQERYRILK
The following text describes a protein:
Function:
Kinesin-like motor protein involved in anaphase B spindle elongation.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Cytoplasm, cytoskeleton.
Sequence:
MIQIFLRVKKAQPSSDASNKYGFLTVLNDYEILLESPEDSHAYRVSKSKTLEKASFTKVFPPSCTQLDVFSTICAPLIADSLVNMNDTLLFTLGVSGAGKTYTLFGPSDRPGVAFLALDALFYAIKGREASPQTVEFLRSQLEKCKIVEASKFLRGEAPLDIKVPNTEYYASHFPKIEEKNYQYAIYLSFAEIYNDRIFDLLEKASFFGHRHALSLKKSSTSDKKSIAGIQKVFVSNTTEAYKLIQKVLQLRKSTSTKSNSVSSRSHLIMSIELFKVCTKSNKFESCQIDLVDLAGSERTRSAETSGLLLREGASINRSLLTLGQCLEALRRKHEGKQHIIPFRQSKLTELLFHSGHLSGLAGINMLVNIDPFGSFDENAQVMRYSANAREILPPPLNENSGSQSPSHSLLQKSKNTSSTKALTSHLEQLQQENQQLRMLLADADSEMMNLEYEIRQQMTREMEERVSEVERTFLTKLLEESAQGIEYTDQKLEKMGGWMKKLQDENSEKTETIAQLEQIIEELHEELRSLEEESIKESSATQQNENQHKRSSRKLLYEDKQAIQEAHTINTKRKLWPQSTLIQAPNSDDEENVPSPSPKKKVVSPIKPLSPSRRPPLTSLYSGTTDIDINEL
The following text describes a protein:
Function:
Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
RPYKQGQALTEETGMKCLLPLMVNFITLSSAFLPDRKDKNEENNQLAQAYLNQFYSLEIEGSHLVQSKNRSLLDGKLQEMQAFFGLTVTGKLDSDTLEIMKVPRCGVPDVGQYGYTLPGWRKYNLTYRIMNYTPDMTHADVDEAIQKALQVWSKVTPLMFTRISKGVADIMIAFRTRVHGWCPRHFDGPLGVLGHAFPPGLGLGGDTHFDEDETWTTGDGEGFNLFLVAAHEFGHSLGLSHSSDQTALMFPNYVSLDPNKYPLSQDDINGIQSIYGSPSKVPTKPNGNPVPCACEPNLTFDAVTTFRREIMFLKGRHLWRVYSDITGAEFEFIDSFWPSLPADLQAAYESPRDEVLVFKDENFWVIRGNSVLPGYPKSIHTLGFPRRVKKIDAAVCDHDTKKTFFFVGIWCWRYDEMAQAMDRGFPQRIMKRFPGIRLRVDAVFQRNGFFYFFRGSRQFEYDMKAKNITQVMKTNTWFLCNEPLNSSSNVSVEGKAHSIGTVIFHHKSASLLSFSIVHVLTKAYS
The following text describes a protein:
Function:
Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Sequence:
MQIQVGSQNPTKIQAVKEMFPNIDVIGVQAESGVSAQPFSDEETKLGAITRAKYCAMNNPYTIGVGLEGGVMYIDNELYLCNWGALVTPENDIITASGARIKIPNDVEEGLLKNIELGELMDTYAEKKDVSKKEGAIGIFTNQLITRKEMFRHVVTLLKGQWMLLNSNNH
The following text describes a protein:
Function:
Inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator. May play a role in cell differentiation.
Subcellular Localization:
Secreted.
Sequence:
MDSLVAANNKFCFDFFQEISKDDAHKNIFVCPLSLSAAFGMVRLGARGDSAQQIDEVLHFNELPKDERKEPSEPSSKSKASDSSLEGQKQTTASQGQQGESTNEHRLLGCHFGKLLSRIDRDKAHYTLSMANRLYGEQEFPICPEYSDDITEFYHTTIESVDFQKDTEKSREEINFWVESQSQGKIKELFDKEAIDNSTVLVLVNAVYFKAKWEKEFDSENTVDAPFCLSENEKKTVKMMNQKGQFRIGFIEELQAQILEMKYTTGKLSMLVLLPSSSEDNVKSLQELEKKINHEKLLAWSNPENMSEKPVAISFPQFIMEDSYDLNSVLQDMGIRDVFDGTKADLTGISKSPSLHLSKVVHKTFVEVDEMGTQAAAASGAVVAEKALPSRVEFNANRPFLFFIRHNGTQSLLFCGRVYSP
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MEIITKRCIQQSQLFQPQLSKLAQQLNRNRTQSNITISKQVKITNQSISRIKLESIKSDSNNDTSYQNDEKSKQKVIAASRSGQFTRKVNLNNQVYIKKVYQGNYFFDKIKEILKSGLKDNTSLKKMSRDALNQIHMIMTYQEIIPEVSLLYYGKSQKQIKIVFDLDETLVHSEEVQKDKVYDFQNNEFGLFVRPYCCHVLKELSQLADLFVYTSANQKYAKTIINLIDPENTFFKGHFYRNNCVSLQSKMQIKHLGILSNNYSKIVIIDNSPIFYMGQPYNGIPIAPFIDDPQDNELPKLLSFLIEKILQSDDVRVTIRRFFQYDMFRQFSDGVSAFNILYN
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that plays a key role in endosome organization by retaining vesicles in the perinuclear cloud. Acts as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the ubiquitin conjugating enzyme UBE2J1. Ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport. Also acts as a regulator of type I interferon production in response to viral infection by mediating the formation of 'Lys-11'-linked polyubiquitin chains on TMEM173/STING, leading to stabilize TMEM173/STING. Also required to limit type I interferon response by promoting autophagic degradation of IRF3.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
KQEMGLVYFVFCFIGRSIDLLCFMLDLNFWVVNSLMRLLWAVFSFIYHLPALITNALLGCWNLILLGLLSAAEAVVGLAQGSLNALGGCLRALCGVLESFKMVGHLSSHVLLRARDLLHRGLLSGQSVLRQLCDGCGIALSLVLYFVNTVVNMLLIGTQNCFALAAATWEVVSGPFQKALELALTLFSYLSSSLVGTAILLWTPCQVALEFLCSLSHIFISVFLLNLYGLVLTLGIVSATTLYLNPDLSRRGADRTLHYISTVPALYRLQRVLQRLYLLALARAQAVVEADVWQRGTWPGSRAGHRRGATQAATPAGGSVGAGAGEHALGPPEHAGGQGDEPPENSTQSASATPSSSMDRPLQRCPSAEGYRGPPPDSLLTMLKEHEERKKCVICQDCVKTVLLLPCRHLCLCRDCANILLRQPIYQHNCPLCRQMILQTMDVYL
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MASQYAAELCMLLVEDNFGELFGRIFSTLHRYERLTLPRLLGLTRLSENRLRAALVAMIQHHLVHFYTAVEEGGVTYYSANMQAAYYLIRSGKILEFVEDRLGKYAATVMSTIMYLGHAQVSHLDTLPELRSDASKTNGVNEGEHDRPEGENETNGTNGEHVSDQPALLHPTLKALAGHGYIVRVREAHFQSIADNILNIERQIRSGDSVQSMKGKKLEEFVVEKTADMLKERLDGDLTRGLIVNGVPRGVKRSQTNGVSDDNETEKARFDYDDGEDEDEENEWLDDEVPMESSLTVRVNYEKLDVALRNRRFLELAERGAPPESAQIYDYLLRRIEYQTSKCRDASEIPREGEEGEQYSVPIPLSALARDIDPYLDLAGSLGPTNTPANNRLGKRTFDDTVDDNDDDHGATGNRTYEIDQHLSLLAQPPLNLTSKRLNGGIINWTVEFRHLARKLRHLELERIVEARYGDVALRVLRVLQAKGKLDEKRLQEISLLPFKDLRQVLASMQTGGFVDLQEVPRDAQRQPSRTIYLWYYDPDRARDSMLQDTYKAMSRCLQRLKFERGRLKDFLEKTERSDVKGNEELYLSEGELDRLREWRAKEALLIGEVARLDDMIAVMRDY
The following text describes a protein:
Function:
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Sequence:
MRFEEEIGSLQMLCDQFQNKINTLEKQMNEEKKDYVQKLHRLHEKNGEAIDKMKQLDHTMQAVSTKVVHLGDQLESVDQPRSRAHDAHQLMQHFDEFLSDQPLNSMIFTDPDKLLESADLVHKLYSISQELNKDKFANVQARIGQRYKVVEDLLIEEFVRSQRDEKKMAEVAKILSEFKGYSGCVDRYVDFLCQSIHPRGDGGEILADCLQLCRTQQPRISAIFPSPHTVMQKLVLNIFTGRMKETITARLRECKDTDDQEHYLRDLAYLYSSTLKMCKELEKLHISPDSAFLSTLTDSIFQRYIATYCSEELKYLNDQCSNLLQRFYESKKHVKKQIGGGLHELKRDVAARLMNVETYGGETFVAEDVAISILQETKNAFGRANQLCDKEELPRHVENIVDVLLKYLYGEHLDYAVETGLAGISLAESKTEPPAYFFSVVAKCTSVILLMIKQFEDPIFPIIKETIVEPSVAKKWQQSLRSLESKMSLGLERQLNSIVGYVKFLFSEQKKTDFRPDSQQIDIRVSPQCQLASRFLANQVAAMELGCDGENLEALQSDLATRLFKFMLTHIQQFTYNSTGAVLLLCDVGELRTLVSKWRVQNALTQWESLQALTNLLAVLPDQVNETAHSSLLENVDRQLIHDFVRLRTDFRSIKNFQI
The following text describes a protein:
Function:
Can bidirectionally induce pre- and post-synaptic differentiation of neurons by mediating interaction with IL1RAP and IL1RAPL1 trans-synaptically. Involved in pre-synaptic differentiation through interaction with SLITRK2.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MVHIARPLLLLLAFFLHADAETPPRFTRTPVDQTGVSGGVASFICQATGDPRPKIVWNKKGKKVSNQRFEVIEFDDGSGSVLRIQPLRTPRDEAIYECVASNNVGEISVSTRLTVLREDQIPRGFPTIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDTSNNNGRIKQLRSESIGGTPIRGALQIEQSEESDQGKYECVATNSAGTRYSAPANLYVRELREVRRVPPRFSIPPTNHEIMPGGSVNITCVAVGSPMPYVKWMLGAEDLTPEDDMPIGRNVLELNDVRQSANYTCVAMSTLGVIEAIAQITVKALPKPPGTPVVTESTATSITLTWDSGNPEPVSYYIIQHKPKNSEEPYKEIDGVATTRYSVAGLSPYSDYEFRVVAVNNIGRGPPSEPVLTQTSEQAPSSAPRDVQARMLSSTTILVQWKEPEEPNGQIQGYRVYYTMDPTQHVNNWMKHNVADSQITTIGNLVPQKTYSVKVLAFTSIGDGPLSSDIQVITQTGVPGQPLNFKAEPESETSILLSWTPPRSDTIASYELVYKDGEHGEEQRITIEPGTSYRLQGLRPNSLYYFRLAARSPQGLGASTAEISARTMQSKPSAPPQDISCTSPSSTSILVSWQPPPVDKQNGIITEYSIKYTAVDGEDDKPHEILGIPSDTTKYLLEQLEKWTEYRITVTAHTDVGPGPESLSVLIRTDEDVPSGPPRKVEVEAVNSTSVKVSWRSPVPNKQHGQIRGYQVHYVRMENGEPRGQPMLKDVMLADAQWEFDDTTEHDMIISGLQPETSYSLTVTAYTTKGDGARSKPKLVSTTGAVPGRPRLVINHTQMNTALIQWHPPVDTFGPLQGYRLKFGRKDVEPLTTLEFSEKEDHFTATDIHKGASYIFRLSARNKVGFGEEMVKEISVPEEVPTGFPQNLQSEGTTSTSTQLSWQPPVLAERNGIITKYTLLYRDINIPLLPVEQLIVPADTTLTLSGLKPDTTYDVKVRAHTSKGPGPYSPSVQFRTLPVNQVFAKNFHVKAVMKTSVLLSWEIPENYNSAMPFKILYDDGKMVEEVDGRATQKLIVNLKPEKSYSFVLTNRGNSAGGLQHRVTAKTAPDVLRTKPAFIGKTNLDGMITVQLPEVPANENIKGYYIIIVPLKKSRGKFIKPWESPDEMELDELLKEISRKRRSLRHGREVELKPYIAAHFDVLPTEFTLGDDKHYGGFTNKQLQSGQEYVFFVLAVMEHAESKMYATSPYSDPVVSMDLDPQPITDEEEGLIWVVGPVLAVVFIICIVIAILLYKRKRAESDSRKSSIPNSKEVPSHHPTDPVELRRLNFQTPGMASHPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYVNANYIDGYRKQNAYIATQGSLPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETHGLVQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGNTEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFDHYAT
The following text describes a protein:
Function:
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Sequence:
MNNVEKAIEALKKGEIILVYDSDEREGETDMVVASQFITPEHIRIMRKDAGGLICTALHPDICNKLGIPFMVDILEFASQKFKVLRELYPNDIPYDEKSSFSITINHRKTFTGITDNDRAFTIKKLAELVKEGRFNDFGKEFRSPGHVTLLRAAEGLVKNRQGHTEMTVALAELANLVPITTICEMMGDDGNAMSKNETKRYAEKHNLIYLSGEEIINYYLDKYLKD
The following text describes a protein:
Function:
Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis.
Subcellular Localization:
Cytoplasm, cytosol. Synapse. Note=Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1.
Domain:
The Ubiquitin-like domain is required for the interaction with RNF31; The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin. Binds preferentially linear polyubiquitin chains and 'Lys-63'-linked polyubiquitin chains over 'Lys-48'-linked polyubiquitin chains. Also binds monoubiquitin.
Sequence:
MAPPAGGAAAAASDLGSAAVLLAVHAAVRPLGAGPDAEAQLRRLQLSADPERPGRFRLELLGAGPGAVNLEWPLESVSYTIRGPTQHELQPPPGGPGTLSLHFLNPQEAQRWAVLVRGATVEGQNGSKSNSPPALGPEACPVSLPSPPEASTLKGPPPEADLPRSPGNLTEREELAGSLARAIAGGDEKGAAQVAAVLAQHRVALSVQLQEACFPPGPIRLQVTLEDAASAASAASSAHVALQVHPHCTVAALQEQVFSELGFPPAVQRWVIGRCLCVPERSLASYGVRQDGDPAFLYLLSAPREAPATGPSPQHPQKMDGELGRLFPPSLGLPPGPQPAASSLPSPLQPSWSCPSCTFINAPDRPGCEMCSTQRPCTWDPLAAAST