lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Miscellaneous:
MISCELLANEOUS: In A.calidoustus, the austinoid gene cluster lies on a contiguous DNA region, while clusters from E.nidulans and P.brasilianum are split in their respective genomes. Genetic rearrangements provoked variability among the clusters and E.nidulans produces the least number of austionoid derivatives with the end products austinol and dehydroaustinol, while P.brasilianum can produce until acetoxydehydroaustin, and A.calidoustus produces the highest number of identified derivatives.
Sequence:
MNTTRHRLLATASRFVETLESLDVDAMLAIRSSTCLHHMCCPSFRNYSITNDQTREAFPQWKATITKYKFGVLDDSQILVDEQARKVMIHAETAAETTVGDYNNEYVFILRMAEDCNTVDEIWEFYDTIRLQDLRHRLEASHVPIGVDAPAPFTTTASPAAL
The following text describes a protein:
Function:
Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Plays a role in the circadian rhythm regulation. May act as RORA co-regulator, modulating the expression of core clock genes such as BMAL1 and NFIL3, induced, or NR1D1, repressed.
Subcellular Localization:
Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Note=Expression shifts from the cytoplasm to the plasma membrane upon stimulation with NGF.
Sequence:
MAQKPDGGAGLRGFQAEASVEDSALLVQTLMEAIQISEAPPTSQATAAASGPNASPQSSQPPTANEKADTEVSAAAARPKTGFKAQNTTTKGPNDYSQARNAKEMPKNQPKVAFKSQNATSKGPHAASDFSHAASTGKSAAKKSEMAFKGQNTTTKAGPSATYNFTQSPSANEMTNNQPKTAKAWNDTTKIPGADAQTQNVNQAKMADVGTSAGISETDGAAAQTSADGSQAQNVESRTIIRGKRTRKINNLNVEENSNGDQRRASLASGNWRSAPVPVTTQNPPGAPPNVLWQTPLAWQNPSGWQNQTARQTPPARQSPPARQTPSAWQNPVAWQNPVIWPNPVIWQNPVIWPNPIVWPGPIVWPNPMAWQSTPGWQSPPSWQAPPSWQSPQDWQGPPDWQLPPDWSMPPDWSFPSDWPFPPDWIPADWPIPPDWQNLRPSPNLRSSPNSRASQNQGPPQPRDVALLQERANKLVKYLMLKDYTKVPIKRSEMLRDIIREYTDVYPEIIERACFVLEKKFGIQLKEIDKEEHLYILISTPESLAGILGTTKDTPKLGLLLVILGIIFMNGNRATEAVLWEALRKMGLRPGVRHPLLGDLRKLLTYEFVKQKYLDYRRVPNSNPPEYEFLWGLRSYHETSKMKVLRFIAEVQKRDPRDWTAQFMEAADEALDALDAAAAEAEARAEARNRMGIGDEAVSGPWSWDDIEFELLTWDEEGDFGDPWSRIPFTFWARYHQNARSRFPQAFTGPIIGPSGTATANFAANFGAIGFFWVE
The following text describes a protein:
Function:
Acts as a ribosome collision sensor, splitting the ribosome into its 2 subunits. Detects stalled/collided 70S ribosomes which it binds and splits by an ATP-hydrolysis driven conformational change. Acts upstream of the ribosome quality control system (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes and their subsequent degradation. Probably generates substrates for RQC; Endonuclease that is involved in the suppression of homologous recombination and thus may have a key role in the control of bacterial genetic diversity.
Sequence:
MIRTETLRTLEFDKILSAVSGYAHSGATRDETALIRPLDDREAIVRRFGQVDEIRRLRQLGIDLSLRSFEDIAPLLAAVRPDGAVLDPTELVVLFPILRTMTAIAKQFAYRTDIPLLRELAGTLTGFPDLLDELEVSIDSEGEILDSASPLLSDLRQKKRHLTERIRRRLAEIVRETGVTTFLQDDFITQRGGRWVIPVRMDSKGMVPGVVHDVSNSGETAFMEPLEIIGLANELENLVAEEKAEMIRIVRTICRMIRQEADGLDEQFRILVRLDVLNGIALFADSLGAETPEITDARFIRVREGRHPLLALMARERGVGRVVPLDLGLGGAERPDSHVANQVMVITGPNAGGKTISLKTTGLLHLMALAGIPVPAASTSSFPLISDLLVDIGDEQSIEQSLSTFSAHVSNIAGILERADRRTVVLLDELGTGTEPVQGAAISCAVLADLQDKGALVIATTHLTDIVGFVHKRDGMVNASMEFDRQTLTPLYRLTVGEPGQSHALEIARRYGLPDRVVAVATGMLSRMETEFHELLAELKDQRRRHEEALAEAERLRRDAEEKARIARERLAEAETRRREATEKALQEAKEIVRAARRDVNAIIEEARREKSREARKKIDEAEAAVEAKLQEFHPEETLSLDAVREGDTVFVKAIGHDGTVTAVDRRTGRLRVRAGAMELEVAATDVSPRRGKATEAKIRTGSGRRPAPDAETPREINLIGLRVDDALARLEPFLNHASLEGYGELRIVHGKGTGALMRAVREYLDGHPLVREFRPGEPFEGGEGATVVTLR
The following text describes a protein:
Function:
As part of a ribonucleoprotein complex composed at least of HNRNPK, HNRNPL and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation. Could also recruit the nucleosome remodeling and histone deacetylase/NuRD complex to telomeric regions of chromosomes to regulate chromatin remodeling as part of telomere maintenance.
Subcellular Localization:
Chromosome, telomere. Nucleus.
Sequence:
MPRRKQEQPKRLPSHVSRQEEAEGELSEGEHWYGNSSETPSEASYGEVQENYKLSLEDRIQEQSTSPDTSLGSATPSSHTLELVALDGEVLRDSLPCQDHLSPGVSSLCDDDSPGSNKPLSSNLRRLLEAGSLKLDATATANGRVESPVNVGSNLSFSPPSHHAQQLSVLARKLAEKQEQNDQYTPSNRFIWNQGKWLPNSTTTCGLSPDSAILKLKAAANAVLQDKSLTRTEETLRFESFSSPFSSQSASSTLAALSKKVSERSLTPGQEHPPPASSFLSLASMTSSAALLKEVAARAAGSLLAEKSSLVPEDPLPPPPSEKKQEKVTPPPPPPPPPPPPPPAQSLELLLLPVPKGRVSKPSNSASEEESGKPFQCPICGLVIKRKSYWKRHMVIHTGLKSHQCPLCPFRCARKDNLKSHMKVHQHQDRGETFQCQLCPFTSSRHFSLKLHMRCHQHFLRTEAKVKEEIPDPDVKGSPHLSDSACLGQQREGGGTELVGTMMTSNTPERTSQGGAGISPLLVKEEPKEDNGLPTSFTLNAADRPANHTKLKDPSEYVANSASALFSQDISVKMASDFLMKLSAANQKEPMNLNFKVKEEPKEEEALSATLPRSSYVFSPESEVPAPGISEDTLKPQDGKGNVLRRDMSVKAASELLMKLSAESYKETQMVKIKEEPMEVDIQDSHVSISPSRNVGYSTLIGREKTEPLQKMPEGRVPPERNLFSQDISVKMASELLFQLSEKVSKENSHTKENTIRTTTSPFFSEDTFRQSPFTSNSKDVLPGESVLHGRISAPETEKIVLEAGNGLPSWKFNDQLFPCDVCGKVFGRQQTLSRHLSLHTEERKYKCHLCPYAAKCRANLNQHLTVHSVKLVSTDTEDIVSAVTSEGSDGKKHPYYYSCHVCGFETELNVQFVSHMSLHVDKEQWMFSICCTACDFVTMEEAEIKAHIGTKHTGEDRKTPSESNSPSSSSLSALSDSANSKDDSDSSQKNKSGNNLLVISVVPGSQPSLTSEEKPEKGFECVFCNFVCKTKNMFERHLQIHLITRMFECDVCHKFMKTPEQLLEHKKCHTVPTGGLNLCSRMTK
The following text describes a protein:
Function:
May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth.
Subcellular Localization:
Cytoplasm. Membrane.
Sequence:
PASPDGGTPAPHGGGPLTGSASPGLVQRCVVVQRDQHGFGFTVSGDRVVLVQSVRPGEPTITDTLPSPRPLAAGAYVALTLLGSSPASGGFSGLQRDPGPPPAPRSPPAESPPPPPPGPPPERITGPRPLQVSVPARPPAPPRPLLPPPAGSPVPARRRPPPPRSRFPQDSEVQKHAAQILLNMLRQEERELQRYCEEYSHRPDRLLEEQIEGARRRVCQLQLKIRQETGGVRVRGGCHSLDSQDGDSGPECGPERLPSGSEVSPARGPPELGHPRPLGPGRRGAGGGRGPDAGPRGSDRGPKPLIIGPEEDYDPGYFNDECDALFQDLEKLKARPAHLGIFLRYIFTQADPNPLLFYLCAEVFQQTGPKDSRNLGKTIWSVFLEKAAPLRVYVPDALLDDFDLRLRNNEDVRVAMSEAQAAALPDIQEQIQDYRRKRTMGLGSLYGENDLPDLDGDPLRERELAEKQLVALGDLVSRYEEDKSTAMEFALNTYATHAGLRGKEARSCGPADKTPSAPDKDKWLPFFPKTKKSANSKKERDALEDRKRNPILKYIGKPKGSSQSTFHVPLSPVEVKPGNVRTMIQHFENSQNYGAPAAAGPPGQRLSTGSFPEELLPGDSCRSEVKLGRSESLKGREELKRSRKAENVPRSRSDVDMDAAAEAARLHQSTSSSASSLSTRSLENPTPPYTPKMGRRSIESPSLSFPGEPLLPHLREDDLGRLSDLEPELEAQNWQHTVGRDVVAGLSQREIERQEVINELFVTEASHLRTLRVLDIVFYQPMRRDNLLAPQELNCLFPNLPDIIDIHNSWCEAMKKLRESGPVVKEVGDLMLTRFDGEGREELQEAAAQFCSQQSIALEIIRVKQRKESRFQLFMQEAESLPQCRRLQLRDLIVAEMQRLTKYPLLLDSILKHTDDDVPEREKLGRARDQCREILRFVNEALKQAENRHRLEGYQRRLDATSLERASNPLAAEFKSLDLTSRTMIHEGPLAWRISKDKTVDVLVVLLEDLLVLLQRQQDEKLLLKVHSKSAPGSSDSSKQSFVPVLKLNAVLVRSVATDKRAFFIICTSELGPPQIYELVAQTSLERNTWMELLEATVQRATRNPGPHSAAADPPKPGSPREPAPGPVHPPPRPGLWGGIHSGQSRGPSADPHPRPLPPAPPQTARLPPLPRRCGVLPSPHGGQTGARGGFPAGARLTAPLPHPALLPPSPPAPPVESLRHLILLTLLAGPGTEPTSDGAEDPPTPPRRGHAASPRGGPADRRGGEEEKGAGGPGRGSLTSLGQLPPRTRNSGIWESPELDGELDGGDGPAGAAGPPDPSPGGYKVVRRGEAGGGRGPGSPARTRGAGDGNCFYISVPPGRRDLNAGALGPGTPEVGTPRRADGWHLELGPPAGRVTGAVQRGIDPIFHTIQQLTLKLHRLKELEMAHHELLRSLGAESSGGTTPVGGPDPEPAGWADRTPGPPARDPGPDPPPGTGRRPQPSPEDGERSPAGPRRERSEDAGGPPGP
The following text describes a protein:
Function:
Cleavage of the 16 C-terminal residues from the D1 precursor of photosystem II (PSII). This proteolytic processing is necessary to allow the light-driven assembly of the oxygen-evolving cluster (a tetranuclear manganese), which is responsible for photosynthetic water oxidation.
Subcellular Localization:
Cellular thylakoid lumen.
Sequence:
MGKRTRRFWALAFSLLMGALIYLGNTPSALAFTEEQKLLLQSWRLVNQSYLDETFNHQNWWLLREKYVKRPLRNREETYTAIEEMLATLDEPFTRLLRPEQYGNLQVTTTGELSGVGLQININPETNQLEIMAPLAGSPAEEAGLQPHDQILAIDGVDTQTLSLDEAAARMRGPKNTKVSLEILSAGTEVPQEFTLTRQLISLSPVAAQLDDSRPGQSVGYIRLSQFSANAYKEVAHALHQLEEQGADGYILDLRNNPGGLLQAGIDIARLWLPESTIVYTVNRQGTQESFTANGEAATDRPLVVLVNQGTASASEILAGALQDNQRATLVGEKTFGKGLIQSLFELSDGAGIAVTVAKYETPQHHDIHKLGIMPDEVVEQPLISFAEITSPADVQYQAALDLLTGGVAIAHKSSSIPAMATAHKPN
The following text describes a protein:
Function:
Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38.
Sequence:
MATSTSTEAKSASWWNYFFLYDGSKVKEEGDPTRAGICYFYPSQTLLDQQELLCGQIAGVVRCVSDISDSPPTLVRLRKLKFAIKVDGDYLWVLGCAVELPDVSCKRFLDQLVGFFNFYNGPVSLAYENCSQEELSTEWDTFIEQILKNTSDLHKIFNSLWNLDQTKVEPLLLLKAARILQTCQRSPHILAGCILYKGLIVSTQLPPSLTAKVLLHRTAPQEQRLPTGEDAPQEHGAALPPNVQIIPVFVTKEEAISLHEFPVEQMTRSLASPAGLQDGSAQHHPKGGSTSALKENATGHVESMAWTTPDPTSPDEACPDGRKENGCLSGHDLESIRPAGLHNSARGEVLGLSSSLGKELVFLQEELDLSEIHIPEAQEVEMASGHFAFLHVPVPDGRAPYCKASLSASSSLEPTPPEDTAISSLRPPSAPEMLTQHGAQEQLEDHPGHSSQAPIPRADPLPRRTRRPLLLPRLDPGQRGNKLPTGEQGLDEDVDGVCESHAAPGLECSSGSANCQGAGPSADGISSRLTPAESCMGLVRMNLYTHCVKGLVLSLLAEEPLLGDSAAIEEVYHSSLASLNGLEVHLKETLPRDEAASTSSTYNFTHYDRIQSLLMANLPQVATPQDRRFLQAVSLMHSEFAQLPALYEMTVRNASTAVYACCNPIQETYFQQLAPAARSSGFPNPQDGAFSLSGKAKQKLLKHGVNLL
The following text describes a protein:
Function:
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDQLALLFMLLLGALLSVPIGARLGLPAPVLMTLLGIVLALLDFVPNVDIPPELILPGLLPPLLYAAVRRTSWRQFAANKRPIFLLAVALVFVTMVCVASVAHAIVPGLPIAAAFALGALVAPPDPVAATAVAGQLGLPRRLVSILEGEGLFNDVTAIVLYHVAIAAAVGGSFSPWRAGFDLVLSAVVAVAIGLVLGWGSNKLMSVLGDPTLQIGLTLLVPFVSYVAADELHGSGVLAVLTTAMFLAEYASDADDVMTRLGGHTVWDVVDTLVTGVAFGLIGLELHNAVRTASGRWTELLGWAAAILVVVVLVRLLWLLPATWLTQRLHARRDQDEDIPTSWRETVVMWWAGMRGVASVALALAIPLETDDGAAFPHREEIVFIAFGVIMGTLLLQGLTLPWLVGRLGVRADTEREQEFERDLALRAAKAAKQRLKEIESVEELPEELSEQMLRRAFDIGIRISPDLGDEERREAQEQRARRIKRVRRIQGEMLSAARHEVLAARSEPGADPEIVDRVLRHLDVRSLR
The following text describes a protein:
Function:
Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MDPSNHDEYPDRVAETFVDRTLLITGGTGFVGKVFVEKLLRSCPGIKKIYLFIRTKKDKEPNERIREMFNGPLFDLLKKQQGDEILKKVEAISADMEAPDLALAASDRKKLAEEVEMIYHCAATIRFDESLRKAVFLNTRGTKLMLDLAKECKKLIVFAHLSTAYCHLHERVLYEKAYPPPTSPHHVIKACEWLDEKALDTITDKILGDIPNTYAFTKALGESLVNDEMENLPTIILRPSVIIPIWKEPLPGWTDNINGPIGLLIGAGKGVIRTMYCKGESYADYIPVDIVANCLICSTFIYLQSNKRIFNLTSSAEYKVSFDEIIEIGRNVVSNKIPLNGVLWYPGGSMKRSRWHHNVDFFLFQLVPAVFLDALLIVLGYKPVLMRVQKRVSKGYEVFEYYANNQWDFNNDDSMKARQMLNPKERAIYKLDGDGIDYHDYFTDCVRAARLYILKEGDETIPSARRHMRLMRFVDVTCKTLLLFAFLYMLYKYLV
The following text describes a protein:
Function:
Involved in the final steps of cholesterol and steroid degradation. Opens the last steroid ring of cholesterol by catalyzing the hydrolysis of (3E)-2-(2-carboxylatoethyl)-3-methyl-6-oxocyclohex-1-ene-1-carboxyl-CoA (COCHEA-CoA) to 6-methyl-3,7-dioxodecanedioyl-CoA (MeDODA-CoA).
Sequence:
MPDKRTALDDAVAQLRSGMTIGIAGWGSRRKPMAFVRAILRSDVTDLTVVTYGGPDLGLLCSAGKVKRVYYGFVSLDSPPFYDPWFAHARTSGAIEAREMDEGMLRCGLQAAAQRLPFLPIRAGLGSSVPQFWAGELQTVTSPYPAPGGGYETLIAMPALRLDAAFAHLNLGDSHGNAAYTGIDPYFDDLFLMAAERRFLSVERIVATEELVKSVPPQALLVNRMMVDAIVEAPGGAHFTTAAPDYGRDEQFQRHYAEAASTQVGWQQFVHTYLSGTEADYQAAVHNFGASR
The following text describes a protein:
Function:
May participate in leucine metabolism. May transport leucine or a compound related to leucine metabolism.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKNDNQTLKRTMTSRHIMMMALGGAIGAGLFKGSSSAIDVAGPSVIIAYLLGGIILLFIMQGLAEMAVRNRNARTFRDLVQQVLGNYAAYFLDWIYWKMWVLNIAAEAVVAAIFIQYWLPGCPIWVLALGISLIVTIVNLLSVKIFAETEYWLAMIKITVIIIFIILGLLLLFVSFGDHTASGFSNLTDHGGFFPHGGTGLITAMLVVIYSYGGTEIIGVTLAETKNPEKVVPKAVRSTLTRIVAFYLLPFFIIVSLIPWNQVNSVPESPFVMVFKMVGIPGADHIMNAVILLAIISSMNSGLYGSSRILYTQASDGRLPKVFSKLSSKNVPMFAILMCTSSLYIGVLISLFAGSQTFNYLMGSLGYTVLFIWLIIGFAHLKSRKQQTETPAYYVKWFPYTTWFAIVALLAILIGVIMTTSIVITGITAAIYLLITVAYLVKGRKHQ
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.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein. Note=Localizes to the division septum where it forms a ring structure.
Sequence:
MSRLLLIVLLACSIASAIGVVYMRHMHRKLFVQLSKLEHSRDELNIEFGRLQLEQATWAESNRVDQVSRERIGMKFPETSDIVVIRP
The following text describes a protein:
Function:
Functions as a 2-dehydro-3-deoxy-D-pentonate aldolase.
Subcellular Localization:
Cytoplasm.
Sequence:
MKKFSGIIPPVSSTFHRDGTLDKKAMREVADFLINKGVDGLFYLGTGGEFSQMNTAQRMALAEEAVTIVDGRVPVLIGVGSPSTDEAVKLAQHAQAYGADGIVAINPYYWKVAPRNLDDYYQQIARSVTLPVILYNFPDLTGQDLTPETVTRLALQNENIVGIKDTIDSVGHLRTMINTVKSVRPSFSVFCGYDDHLLNTMLLGGDGAITASANFAPELSVGIYRAWREGDLATAATLNKKLLQLPAIYALETPFVSLIKYSMQCVGLPVETYCLPPILEASEEAKDKVHVLLTAQGILPV
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER).
Subcellular Localization:
Cytoplasm.
Sequence:
MLLSNEEFLKKLTDLLQTHQSKGTGSVYLSQKCNPVDEGEGSSASVLIRAKSGAAEKISTVVELDYFTDFFQSYAEVCKGQIVGLKKRDRKKTKKNKKKTTSSGHT
The following text describes a protein:
Function:
Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSPIRLSENSVLSSNNESNEAIFRSAPMTLVQFYVTIELARDMVGVLGKLGNVQFRDLNSKLTPFQRTFITELRSIDGLVSQLDFLHSIMIKQNTIKSDLYVNLHADMKPLPTSSEIDNIKTRLSEFYERIKHLDQSYNNLDRKRLKFIENRCVLNSLNEFHRSNLVGGGYDDEHTEDADYDDNAALLNEQRNHSLEIGYEAHNLDDISFNSLAGTIARDKVPILRNILWRVLRGNLYFHDIALDDEFPATESSMDLVHKNVFIIFIHGDFLRTRVRKIIQSLDGILFDNATGGSVARNETLTEINGKIEDLNNVVQTTKDQLVTELMIFQELYPDYCYIVQREKLIYETLNKFDEDSTRRCLVGEGWIPTNDFDKIRLALRNLIRQKTRRDGSDRDSNESVNISESIATETSLFAIDDSDHELTGFEIEDEDEVGSLIAVVNELATNRTPPTFHKTNKFTAAFQSIIDAYGIATYQEVNPGLATIITFPFMFSIMFGDLGHGFIVFLMAIYLILNEVRFGAMRNRDEIFDMAFTGRYIILLMGVFSMYTGLIYNDIFSKSMAIFSSGWKYVIPENYDATKGATLVAEKIAGKVYPFGLDWAWHGTENNLLFTNSYKMKLSVLMGYTHMNYSLMFSLVNYLFFKSRVDIIGNFIPGFLFMQSIFGYLALTIVYKWSVDWFGSNRQPPGLLNMLINMFLSPGTIEEPLYAGQKYIQVFLVLVAAVCVPWLLIYKPLVLKKQNDRAIQLGYSDLRSQRQHSLQLHEEEQALAMHDQGLNRDPPDDSFELLRGSDEEEQEFRFPNDVEPMFPSAGGHGGDDEDGFNFGDIVIHQVIHTIEFCLNCVSHTASYLRLWALSLAHAQLSTVLWSMTIQNAFGKTGTVGVIMTVVLFAMWFSLTVCILVFMEGTSAMLHSLRLHWVEAMSKFFQGEGYAYEPFTFKSIDI
The following text describes a protein:
Function:
Nuclear export factor for BMP-specific SMAD1/5/8 that plays a critical role in terminating BMP signaling and regulating mesenchymal stem cell differentiation by blocking osteoblast differentiation to promote myogenic differention. Directly recognizes dephosphorylated SMAD1/5/8 and mediates their nuclear export in a Ran-dependent manner.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MQCKLFVFDKTSQSWVERGRGLLRLNDMASTDDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKSIRITAMDTEDQGVKVFLISASSKDTGQLYAALHHRILALRSRVEQEQEAKMPAPEPGAAPSNEEDDSDDDDVLAPSGATAAGAGDE
The following text describes a protein:
Function:
Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA.
Sequence:
MRQFIISENTMQKTSFRNHQVKRFSSQRSTRRKPENQPTRVILFNKPYDVLPQFTDEAGRKTLKEFIPVQGVYAAGRLDRDSEGLLVLTNNGALQARLTQPGKRTGKIYYVQVEGIPTQDALEALRNGVTLNDGPTLPAGAELVDEPAWLWPRNPPIRERKSIPTSWLKITLYEGRNRQVRRMTAHVGFPTLRLIRYAMGDYSLDNLANGEWREVTD
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAPKKGVSKNLAAGRPPMATRPKKKGVVKNLAAGRPPTVTKPKSLARKTTKSIINKLHLLEKRKVQAMKKNDNTQVAAIEAEIEALGGIEKYQEASLQGQRHDRGGDSSNVLMEWVGPYLSSEEYKEGRLRMLEVGALSTKNACAQSNHFDITRIDLNSQEPGILEQDFMERPLPKDESEKFDIISLSLVLNFVPDHKDRGEMLVRTTQFLTSPKRFSGTTAAFFPSLFLVLPAPCVTNSRYLDQERLAAIMESIGYEMVESKTTQRLVYYLWRRTSDQVGNDRPFRKEELRSGSSRNNFAITLV
The following text describes a protein:
Function:
Metalloprotease.
Subcellular Localization:
Secreted.
Sequence:
MYRSILLFSLLALVLAKVAEPEKDDQVAVKIPTKRSVSEPPKDDDVAVKIPMRKKRGIAIHPWQWESHLWPNGEVPYDIASHYTATERATILSAMDAFKDVTCIRFRPRRSTDRNYLQINKHYQLERCFSYIGRQTSRWLFGTPAGNVETRMKLDPTCLLYNGRGTVMHELMHILGFYHEHQRDDRDRRIGGSAFHYNFKIYQRAKSYYMGGYDANSIMHYNFQNVPWQKRDYFSPSDIRNINTLYKCNNRVISRIAAPSTTQSTTTTTTVSDTQTNRPPRFELYEKKAIESNSLFRRRRS
The following text describes a protein:
Function:
Negetively regulates apoptosis via its interaction with cep-1.
Subcellular Localization:
Nucleus.
Sequence:
MVTTSSGGGIGYPANNGVTQVSLIHSSDSVRTVSTAPIYRPTSSMASTMAHKSSTAPFISANQRMSKPPVRVVAQPPPPHPQALSQQYHQQNPMMMYSAPNTRPHVIPTMQVQPTMAAQIKRNNPVNAQFQNPSEMIADYGVKPQSVEMVQRVRAVRRQVADEETELRRLRELEHETAQLQNKNYGRERELNVQGSMLKEAQLELRNASMRAQSLNKHLEEMYRRRQTAAAAALVEQRKMQQHQILLARAANQVSTQEVIRPRASVEPFQVNNTQQQQPSPQMMKSEEFSEKRDLNGQTGSYDAIDGSGDHQKIPTEPSYLAPCKENQQKYSELSKMASTDPHSNHSSPSTSSQKAPTLITFSPPSFEQKINSSTMTRDSPFVERPTSFGDSLDESRLRSGKTDLVSLRSDSLKATKRRSWAASEGTSMSEAEMIHRLLDEQRRGRSHFIPQLPTSQEEPSAITSETYAEEVVNSESKQVATSSDSTNNLELPTEQMVLGSDTTTEEDASSCSTRSDDGQNLEMEVAIERRTVKGILRRPNEKMNKGRIEFDPLALLLDAALEGELDLVRSSASKLTDVSQANDEGITALHNAICAGHYEIVRFLIENDADVNAQDSDGWTPLHCAASCNNLPMVRQLVEGGGCVLASTLSDMETPVEKCEEDEDGYDGCLKYLSAAHNSTGSINTGKVYAAYGYEAAFEDELSFDAGDELTVIEKDKVDKNWWTCEKNNGEKGQVPRTYLALYPSLKYRKKLNFVMFDLPLESNNNVE
The following text describes a protein:
Function:
Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II). Required to activate the protein kinase activity of CDK9: acts by mediating formation of liquid-liquid phase separation (LLPS) that enhances binding of P-TEFb to the CTD of RNA Pol II.
Subcellular Localization:
Nucleus.
Sequence:
MTGGAGHCGPERESEAGDRKKKAKDEGEALENTPSRRCGVEADKELSYRQQAANLIQDMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNRNIISPTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVLLETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPSRLKRIRNWRANQAAKKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNISVQDSHTSDNLSMLATGMPSTSYSLSSHQEWPQHQESARTEQIYSQKQETSLSGSQYNINFQQGPSISLHSGLHHRPDKISDHSSIKQEYTHKAGSSKHHGPISATPGVIPQKMSLDKYREKRKLETLDLDVRDHYIAAQVEQQHKHVQSQSASSSSVTSPIKMKIPITNTEKPEKYMADKKEKSGSLKLRIPIPPTDKSASKEELKMKIKVSSSERHSSSDEGSGKSKHSSPHISRDHKEKHKDHPSNRHHPSSHKHSHSHSGSSSGGSKHSADGIPPTVLRSPVGLSSDGISSSSSSSRKKLHVNDASHNHHSKMSKSSKSSGSSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVETNGPDVNHEYSTNSQHMDYKDTFDMLDSLLSAQGMNM
The following text describes a protein:
Function:
Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions and may be involved in various processes including cellular proliferation, migration, adhesion and attachment. May play a role in ER stress response (By similarity).
Subcellular Localization:
Endoplasmic reticulum. Sarcoplasmic reticulum. Secreted. Secreted, extracellular space. Secreted, extracellular space, extracellular matrix.
Sequence:
MAGTMHLLTAVSLILMLSSANAESTVYNLLTSPDCLPDLLHGGLAEQGVTELYILTTFRIQPGTGNTIFSLYNPRDNSKYFEFSVFGKANKAILRYLRRDGRMSAVTFNKLNLADGEKHRLLFHLKGLEVGHPGGFPHSQGALPVPGVELHLDCRLVETLRDLPAVFNGLNNHQAVELKTMQGKAQEGLEELKLAYGDSVENVASLQDCHTQSDSVQALGLNTKQLTTQMLELTKVINELKDVLIQQVKETSFLRNTISECQACGLSGAEVVKPKCAPGVCFRDDMCIETAEGVECGPCPDGYTGDGYSCDDVDECQFNPCFPGVRCVNMAPGFRCEACPLGFTGKPLEGVGVAYAQTHKQVCDDIDECKGPDNGGCTANSICVNSVGSYQCGRCKTGFTGDQIRGCKPEKSCGNRLQNPCDPNAQCTEERDGTITCQCGIGWAGNGYLCGKDTDIDGYPDERLRCRDPTCRKDNCVTVPNSGQEDADGDGKGDACDPDADGDGILNEQDNCWLTPNINQQNSDKDSHGDACDNCVRVDNPDQRDTDSDGLGDACDDDMDGDGLKNFLDNCQRVKNRDQLDRDGDGVGDACDSCPDIPNPNQSDIDNDLVGDSCDTNQDSDGDGHQDSKDNCPMVINSSQLDTDKDGIGDECDDDDDNDGIPDSLPPGPDNCRLVPNPEQIDDNNDGVGDICESDFDQDKVIDRIDNCPENAEITLTDFRAYQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFSGVDFEGTFHVNTVTDDDYAGFIFGYQDSSSFYVVMWKQTEQTYWQATPFRAVAEPGIQLKAVKSKTGPGEHLRNSLWHTGDTNDQVRLLWKDPRNVGWKDKVSYRWYLQHRPQVGYIRVRFYEGTELVADSGVTIDTTMRGGRLGVFCFSQENIIWSNLKYRCNDTIPEDFQEFSTQHGMDPL
The following text describes a protein:
Function:
Involved in ribosomal function.
Sequence:
MSTTVEKIKAIEDEMARTQKNKATSFHLGQLKAKLAKLRRELLQGASAGGGGGGVGFDVSRTGVASVGFVGFPSVGKSTLLSKLTGTESEAAEYEFTTLVTVPGVIRYKGAKIQMLDLPGIIDGAKDGRGRGRQVIAVARTCNLLFIVLDVNKPLHHKQIIEKELEGVGIRLNKSPPDIIVKKKEKGGISITNTVPLTHLDHDGIRAVMSEYRINSAEIAFRCDATVDDLIDVLEAPSRRYMPAIYVLNKIDSLSVEELELLYRIPNAVPISSGREWNLDELLEVMWDRLNLVRVYTKPKGTMPDFNDPVVLRSDRCTVRDFCNQIHKSLVEEFRNALVYGSSVKHQPQYVGLAHTLEDEDVVTILKK
The following text describes a protein:
Function:
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II.
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MKSASQLSCLLLKKRFVPKMKDILETEDQVSHKDIVEYIKSGVKDEKILKEVPNAEQSIVDAQVLSGTFTYTWPPVTSEGCLKDTIMFVYIKVQIEGETAIVARTYGVDVSKEIKHTYNQLLRLEQTLASKYKSGIKVDTKVIEVAGLSQQVEIIKGEEILKEGSVIMIRVWSGQLMICDTCYIGSKGLINLTKFVGSNSSSVFFSFKDEEEPAEVLSKFRDKKQQEDEDELKEYEQQRKETMKEEHRPKVETLKKEKIKAICYNNQKEMPSKNALYINSDVKKYAILLPINGQLVPFHVAYIKNITTREGFFRINFNVPRETEEGTVYVKELSFHVRDSDRISRIENDWKEMKKKWNEEEKIRNIRGMKEEKLVLRKESVPILRSVCINPVLKGKRTEGVLEAHMNGFRFVSSGGNVELMYDNIQHAFFQNGDTETVILLHFHMDPPVIIQNRPISDIQFYNEIMDISLNIDRGDRYYSEAEEAREEEREKRIRAKYNHLYAEFLTKVKEKDIPVSFEVPFRELKFGGTIKRNTATLVPTVKCLINISDAPYKVIELDTIEVVVFERLSRSLTLKNFDMVVIFKDHHKPVLQISSVSKTDLDHIKKWLNKCEIKSYETVQSLNWINIMEAVNSDPVAFAEKGWSFLDADNTKSDSEESEEVFEPDEELEKELDAEDDLSTDLSSEEESSSSSEEEDDDGESWSDLEREAIKDDLVKDREEHEMIGRAQMMKQRQRVQQRRPSQQRSTTIQNFFKKTSTTPTTSSSSNSRLQPIKINKAFVPTKKPSNLGGIKRQFSSSYAGTKKP