lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
KAAEALLKVVKTQKKNEILAETCRINLVIAMNRIPSRKMKKVFIPLPHPVFTTSSEICVFTKDVESKDIEKSQEHYEDLFRNKVGFVPKFIPLTSMKKDYKSFEAKLALCGSYDLFLSDARITRLLPPLIGKHFFTKAKNPRDIDLTATDLKKEFFNRISHARWLITAHGDTTMIHAASSNLTAEQIADNLEHCISAVVSQLPRGWSNVRALRIKTNDSIAIPVY
The following text describes a protein:
Function:
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. SKI6 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Miscellaneous:
MISCELLANEOUS: Present with 5150 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MSRLEIYSPEGLRLDGRRWNELRRFESSINTHPHAADGSSYMEQGNNKIITLVKGPKEPRLKSQMDTSKALLNVSVNITKFSKFERSKSSHKNERRVLEIQTSLVRMFEKNVMLNIYPRTVIDIEIHVLEQDGGIMGSLINGITLALIDAGISMFDYISGISVGLYDTTPLLDTNSLEENAMSTVTLGVVGKSEKLSLLLVEDKIPLDRLENVLAIGIAGAHRVRDLMDEELRKHAQKRVSNASAR
The following text describes a protein:
Function:
Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGQATSRSGGEWKKSKKINLSDQGSVKYSLDRFVSEVVISKGYVENMKSSNLKILIGLICIIFAVAAHFYPRDFPQNRNFTIICTALYLASSGILLLISYLKDKNTILLTFPLPGSPEDPGLMISSNLPRFTDAYTLTVSSANPKSAFARRPVQLCKSVTKWFTEDGLLVEGLFWRDVEKLVDDYERALMKTDNA
The following text describes a protein:
Function:
Bifunctional enzyme that catalyzes two enzymatic reactions in biochemically unrelated pathways: acts as an aminodeoxychorismate (ADC) lyase (ADCL) in folate biosynthesis, converting 4-amino-4-deoxychorismate (ADC) to 4-aminobenzoate (PABA), and as a D-amino acid transaminase (DAAT) in peptidoglycan (PG) biosynthesis. DAAT activity is strictly restricted to D-alanine and D-glutamate. May function as a metabolic toggle that alternates between ADCL and DAAT activity, prioritizing the former over the latter in response to substrate accumulation. Bifunctionality of this enzyme provides a failsafe mechanism for a metabolic coupling between nucleic acid and cell wall biosynthesis that appears to ensure prioritization of PABA production over D-alanine/D-glutamate biosynthesis.
Sequence:
MVVTLDGEILQPGMPLLHADDLAAVRGDGVFETLLVRDGRACLVEAHLQRLTQSARLMDLPEPDLPRWRRAVEVATQRWVASTADEGALRLIYSRGREGGSAPTAYVMVSPVPARVIGARRDGVSAITLDRGLPADGGDAMPWLIASAKTLSYAVNMAVLRHAARQGAGDVIFVSTDGYVLEGPRSTVVIATDGDQGGGNPCLLTPPPWYPILRGTTQQALFEVARAKGYDCDYRALRVADLFDSQGIWLVSSMTLAARVHTLDGRRLPRTPIAEVFAELVDAAIVSDR
The following text describes a protein:
Function:
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Subcellular Localization:
Cytoplasm. Nucleus. Chromosome, telomere.
Domain:
This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Sequence:
MSEKPDLRQRCSDIYREIKEKKLTVVKQGAEAITIKTEFYPGEVCLLKCRPAKRWRHPILDQKLSRKRCLVEARLLAKCHYVGIKCPMLYFIDANRGQIYMEWIDGPCVRDYIREICECEIEKKLIPLMKRIGSEVAKMHKNDIVHGDLTTSNMMLESHNNPVPIFIDFGLGSVSESEEDKAVDIYVLERALSSTLPESESLFHHVLDSYAQSWKQSKATLRRFEEVRMRGRKRTMIG
The following text describes a protein:
Function:
Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B.
Subcellular Localization:
Nucleus.
Domain:
The UBP-type zinc finger binds 3 zinc ions that form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. It recognizes the C-terminal tail of free ubiquitin.
Sequence:
MGKKKVKDRSAGTDSSSETAGPSCTHIRKGTENSVLKKACLNEHWSSCQDCEQDKPEEKQILEDQTDGESPAVWMCLKCGHRGCGRSGNQHAIKHYETPRSEPHCLVLSLDVWSVWCYICDDEVQYSSTGQLAQLITNIRKQVLTAPDKRNASKKSWKEDISVMNSAEQTQDEEKGKKGKQKSSSKQEDSPKSHQSAAAGSSAVVSVRGLSNLGNTCFFNAVVQSLSQTQYLRELLKQIAEEKSSFSITPALSSELDPLQIQLERPGSLTLAMCQLMNEIQETKKGVVTPKELFTQVCKKAPRFKGFQQQDSQELLRYLLDGMRAEEAKRVNSGILEALKSSGKNFEAEQTKKIVKEYEKDGAPKNFVDRVFGGAMSSTVMCKECKTVSLVTEMFLDLSLPVADEAYRKKNQKKAVQHRHSVSDDGDQDTSSLANGNEDMPTGTGSKYQQKKAKKQAKKQAKNQRRQQKQGGKVTLDAITNQSSTDPADSSMQTQTVSVNGSADAQPADTNQEDLSLEKHNEDQDDEEPEQEQAASVNNRFTALSEDQTTEDIAEQVNEDEDEIEQNCAEEEELVEELNTMSLTTPSEGDVENGEDTLEDVKEYTVVNRDPELAFRALASRTAPVKQECSVESCLYQFTEVEHLTENNRLMCVTCTKQQPGYKDGCKKAVYRDALKQMLISDPPVVLTLHLKRFQQVAYSVCKVNRHVQFPQILDLAPFCSLNCTGVKEGETQVLYSLYGIVEHSGTMRSGHYTAYVKSRPSTHNCVQNGTAAASGDAEASKGSWFHISDSSVHPVPEAKVQSSQAYLLFYEKIS
The following text describes a protein:
Function:
rRNA N6-methyltransferase that specifically methylates the adenine in position 4220 of 28S rRNA. N6-methylation of adenine(4220) in 28S rRNA is required for translation.
Subcellular Localization:
Nucleus, nucleolus. Cytoplasm. Note=Accumulates in the nucleolus, where ribosome biogenesis takes place.
Domain:
The regulatory loop blocks the catalytic center by bridging the methyltransferase domain and the C-terminal CCHC-type zinc finger, resulting in an autoinhibitory conformation.
Sequence:
MAASRNGFEAVEAEGSAGCRGSSGMEVVLPLDPAVPAPLCPHGPTLLFVKVTQGKEETRRFYACSACRDRKDCNFFQWEDEKLSGARLAAREAHNRRCQPPLSRTQCVERYLKFIELPLTQRKFCQTCQQLLLPDDWGQHSEHQVLGNVSITQLRRPSQLLYPLENKKTNAQYLFADRSCQFLVDLLSALGFRRVLCVGTPRLHELIKLTASGDKKSNIKSLLLDIDFRYSQFYMEDSFCHYNMFNHHFFDGKTALEVCRAFLQEDKGEGIIMVTDPPFGGLVEPLAITFKKLIAMWKEGQSQDDSHKELPIFWIFPYFFESRICQFFPSFQMLDYQVDYDNHALYKHGKTGRKQSPVRIFTNIPPNKIILPTEEGYRFCSPCQRYVSLENQHCELCNSCTSKDGRKWNHCFLCKKCVKPSWIHCSICNHCAVPDHSCEGPKHGCFICGELDHKRSTCPNIATSKRANKAVRKQKQRKSNKMKMETTKGQSMNHTSATRRKKRRERAHQYLGS
The following text describes a protein:
Function:
Active efflux pump that plays an important role in chloramphenicol resistance. Overexpression causes pyrazinamide resistance.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTAPTGTSATTTRPWTPRIATQLSVLACAAFIYVTAEILPVGALSAIARNLRVSVVLVGTLLSWYALVAAVTTVPLVRWTAHWPRRRALVVSLVCLTVSQLVSALAPNFAVLAAGRVLCAVTHGLLWAVIAPIATRLVPPSHAGRATTSIYIGTSLALVVGSPLTAAMSLMWGWRLAAVCVTGAAAAVALAARLALPEMVLRADQLEHVGRRARHHRNPRLVKVSVLTMIAVTGHFVSYTYIVVIIRDVVGVRGPNLAWLLAAYGVAGLVSVPLVARPLDRWPKGAVIVGMTGLTAAFTLLTALAFGERHTAATALLGTGAIVLWGALATAVSPMLQSAAMRSGGDDPDGASGLYVTAFQIGIMAGALLGGLLYERSLAMMLTASAGLMGVALFGMTVSQHLFENPTLSPGDG
The following text describes a protein:
Function:
May act as Rab effector protein and play a role in vesicle trafficking (By similarity). Involved in apical-directed transport in polarized epithelial cells; the functions seems to implicate Rab8, BIN1 and possibly DNM1.
Subcellular Localization:
Endosome. Recycling endosome.
Domain:
The CAAX motif is a signal for prenylation and required for endosomal colocalization with Rab8 and Rab10; The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates binding to Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound forms).
Sequence:
MTSVWKRLQRVGKRAAKFQFVACYHELVLECTKKWQPDKLVVVWTRRNRRICSKAHSWQPGIQNPYRGTVVWMVPENVDISVTLYRDPHVDQYETKEWTFIIENESKGQRKVLATVDVNLAHHAGPVPAQVPLRLRLKPKSVKVVHAELSLTLSGVLLREGRATDDDMQSLASLMSVKPSDVGNLDDFAESDEEEANGPGAPEVRTRGPQSDLSRELKTLCEEEDEGHIRPQQAAARPSSAEDTSPAPVSAPAPPVRAFRGQGSEPAAITGGQVGPETPEPPPSPPETRSTGQPGQTMVPTPAPRLRKGSDAPSSPVPCSGDEVPNTSEDPPTGMGSSGETQAQISSQEGTEAHEARPEPDIEVRGSKDSLGGERSKVEEEERGDGPGASGTGNREKNTKKSDTTAGEAGESSELHQVDAEHKSKVQHRATEGPEAAGLTPKARLGDTPEAPPRSAQRRMGVRTQEEAPSDLNPPPAEPEEHLGDLRDARPAGQEKGSAEVRSKVPAIGRAGPEQGSSARAASAGPQVSCVQTVPSDGQGVKSRDQRAQEAEVGESRVLETEAEWVPWEVIGTSKTDAGIPESLDTEAGTAESEILEAQESEAARSEGLEPEAAGTAESEVLRTQNNEIVVLGMPRTGPEIREPEEFGETEVGGFTVPDTKTVIAETEILETQGVVDGEAAVLKTQAEISETQKTEAGEAEAGTLESQKVAAEGLGAPEVGAEMAEAEKLGVQETEVEIWRIPRIETETAGTETLGIHKIGPPQMQPRLVGDQETDVSVMETAEDAILGTREITAGCGVLLIEAKIPESKIDRSLETEEGDLGVLEVDTGIAEAKILGIPERAPGVQKALGAGTEVARVLEAEAASSEVPETDAEEAETLQAKERSESSVALRVVANLPESELLGTQKTEVGGTGISQREVREAETEIPKTQEISSEGSGVPDLEAKMEESGRKMEIWETPEVEKVNSELFGTQKGSEIPELETKTIKSEILDAQETEVRDLGLRRGEAEKAEAEMLETQKMEAKTARDEEIELVDPGVSSPEAEALRVQWAGTVVLESGEVKADILGVQKPGSWGALKYEALDVPVTKQRLSGAKEVVPEVPRAQEPETKVLGIVEAKSWTLGQQEAEMEGFESPENKSNIFEAQEADSGVLGTMKGKEAVESLEEAGLSKAQVASEAGAGVPRPSGASSLEEPEEDRRLPGSQAPPTLVSSSQSLLEWCQEVTNGYRGVCITNFTTSWRNGLAFCAILHRFYPDKIDYFSLDPLNIKQNNKQAFDGFAALGVSRLLEPADMVLLSVPDKLIVMTYLCQIRAFCTGQELQLVQLEGGGGSGTYRVGNAQPSLPDCLDAGDLAQRLREHGAEVPTEPKEAVNRGTGAIPKVASRDTDLSCSSKDGEAEVAQEAIPQEAPTDGPRARSSTTPVVPAEGLVNGVGASGGVRLRRSSVNGEAGPVPPPRAHGSFSHVRDADLLKKRRSRLRNSNSFSVDDQDSGAAVGAGPAGPGAVEGPNPASSPDANPLPAPVPQQPPGGPPPTEESSPSLGEEAGLQRFQDTSQYVCAELQALEQEQGQIDGRAAEVEKQLRSLMESGANRLQEEVLIQEWFTLVNKKNALIRRQDQLQLLIEEQDLERRFELLSRELRAMLAIEEWQKTVAQQHREQLLLEELVSLVNQRDELVRDLDQKERIALEEDERLERGLEQRRRKVSRQLSRRERCTLS
The following text describes a protein:
Function:
Promotes lateral root initiation and development, independently of auxin (IAA) and abscisis acid (ABA).
Subcellular Localization:
Nucleus.
Sequence:
MSRRLRRKVSRKGKEKVVAHSYTEFEEGVSTSERNGDVDWTCLPDDTVIQLFSCLNYRDRASLASSCKTWRCLSASSCLWNSLDLRAHKCDLAMASSLASRCRNLQKLRFRGAESADAIIFLQARNLREISGDYCRKITDATLSVIAARHELLECLQLGPDFCERITSDAIKQIAFCCPKLTKLRLSGIRDVQGDAINALGKHCLHLIDVGFLDCLKVDELALGNVASLRFLSVAGTSNLKWGVVSHVWHKLPNLVGLDVSRTDVGPAAISRLLNLSLSLKVLCALNCPVLEGDVNFIVPKIKGKSLLAHFTDIFEGIASLFVDITSKGKTVFLDWRNSKKTHKCMDEMMSWFEWILSHSLLRSAENNPQGLDDFWLKQGAPLLLILMQSSQEDVQERAATGLATFVVIDDEHASIDRGRAEAVMRDGGIRLLLDLAKSWREGLQSEAAKAIANLSVNVNVAKAVAEEGGIDILASLARSMNRLVAEEAAGGLWNLSVGEEHKGAIAEAGGVKALVDLIFKWSSGGDGVLERAAGALANLAADDKCSMEVALAGGVHALVMLARNCKFEGVQEQAARALANLAAHGDSNGNNAAVGQEVGALEALVQLTRSPHEGVRQEAAGALWNLSFDDRNREAIASAGGVEALVALAQTCSNASPGLQERAAGALWGLSVSEANSVAIGREGGVAPLIALARSDAEDVHETAAGALWNLAFNPGNALRIVEEGGVPALVHLCSSSVSKMARFMAALALAYMFDGRMDEYALVGTSSESTSKIVSLDGSRRMALKHIEAFILMFSDRQAFTAAAASSAPAALAEVTEGARIQEAGHLRCSGAEIGRFISMLKNPSVLKACAAFALLQFTIPGGRHALHHAKLMQNAGAARVLRATAAAATAPIEAKIFARIVLRNLEHHQAESSKGL
The following text describes a protein:
Function:
Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
Sequence:
MEVEMDMEMKQSKFKSICVFCGSSPGKKSSYREATIELGRELVSRNIDLVYGGGSIGLMGLISQAVFDGGRHVIGVIPKTLMPREITGETVGEVKAVADMHQRKAEMARQSDAFIALPGWYKTPKVLLFINLSMGTLRLGAFSWTTSVGGYGTLEELLEVITWAQLGIHDKPVGLLNVDGYYNSLLSFIDKAVEEGFICPNARHIIVSAPTAKELVKKMEEYEPQHERVASKLSWEMEQLGYPAKCEISR
The following text describes a protein:
Function:
Chitin-binding protein which slows larval growth when consumed by the lepidopteran species S.ricini and M.brassica, but not when consumed by the mulberry specialist B.mori. Lacks chitinase activity.
Miscellaneous:
MISCELLANEOUS: On the 2D-gel the determined MW of this protein is: 56 kDa.
Subcellular Localization:
Secreted.
Sequence:
MKFRTLLIIFSLVFLLEIVSASEPQCGRDAGGALCHGNLCCSHWGFCGTTAIYCDVDQGCQSQCWSSPPPPSPPPPPPSPPPPSPPPPSPPPPSPPPPSPPPPSPPPPSPPPPSPPPPGGPERPDHRCGRALGNPPCNPGRCCSIHNWCGSTAAYCRGSSCQYQCWNSLLSALISNGNNAISKIISKSVFDEMFKHMKDCPSKGFYSYDAFIIATTSFPHFGTTGDITTRKRELAAFFAQTSLATTGQRFDSQDLYVWGYCHINETTNGNDNDYCTSAHWPCPSGKKYNSRGAVQLTHNYNYGLAGEALGLDLINNPDLVATDPVISFKTAIWFWMAQHDNKLSCHDILINANSGYVIGNIIKNSGYQNGLITNTISTMRGIGYYKRYCDMLGVSYGDNLDSWYDQTHFSEVARM
The following text describes a protein:
Function:
Involved in the uptake of chitosugars.
Subcellular Localization:
Cell outer membrane; Multi-pass membrane protein.
Sequence:
MRTFSGKRSTLALAIAGITAMSGWIVVPQAQASGFFDDSTLTGGIYYWQRERDRKDVTDGDKYKTNLSHATWNANLDFQSGYAADMFGLDIAAFTAIEMAENGDSGHPNEIAFSKKNKGYDEDYSGDKSGISLYKAAAKFKYGPVWARAGYIQPTGQTLLAPHWSFMPGTYQGAEAGASFDYGDAGALSFSYMWTNEYKAPWHTEMDKFYQADKKTNVDYLHSIGAKYDFKNDLVLEAAFGQSEGYVDQYFAKASYKFDLGGNPFTTSYQFYGARDKVDDRSVNDIYDGTAWLQALTFGYKVAEVVDLRLEGTWVKADGQQGYFLQRMTPTYASSNGRLDIWWDNRSDFNANGEKAVFFGAMYDLKNWNLPGWAVGASYVYAWDAKPATWQSNPDAYYDKNRTIEESSYSLDAVYTLQEGRAKGTMFKLHFTEYDNHSNIPSWGGGYGNIFQDERDVKFIVIAPFTIF
The following text describes a protein:
Function:
Required for proper chromosome segregation during mitosis and error-free mitotic progression.
Subcellular Localization:
Chromosome. Nucleus, nucleolus.
Sequence:
MSSETQQQQINTNECEKQKEEIIKEIIVKEEPDIKEEKKEIKKPIRGANVSGRPWKEAYKKRSIKDNVAMAGISWEEKMEMKKRRQMMRALDEEIRTRQAEEEAKRKEARKQAIIRKKENIAKNTIVQQITNKKKLRHMSGKQFRQLRTFHFDEIE
The following text describes a protein:
Function:
Central scaffolding component of the centrioles ensuring their 9-fold symmetry (By similarity). Required for centrosome biogenesis and duplication. Required both for mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. Not required for centriole formation in embryonic stem cells but necessary to maintain centriole architecture. Required for the recruitment of STIL to the procentriole and for STIL-mediated centriole amplification (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Component of the centrosome. Associated only transiently with nascent procentrioles during centriole biogenesis (By similarity). Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles.
Domain:
The 35 nM long coiled-coil domain mediates homodimerization while the globular N-terminus links the dimers at an angle of 40 degrees to form the inner ring.
Sequence:
MSQVLFQQLVPLLVKCKDCEERRGSVRVSIELQSLSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAFPQKFIDLLQQCMQEHAKETPRFLLQLLSSATLLENSPVLLNVVETNPFKHLIHLSLKLLPGNDVEIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQDTLGTSATPHSTSNSTIRSGLSPNLNVVDRLNYPSCGIGYPVSSALTFQNAFPHVVAAKNTSHPISGPKVHFNLQLTKPSASIDGQPGAAVNRPCSNDKENGETLGLESKYLKRREASIPLRGLSQNLLSDSDHQKDGMLGAFQLSSKPTVLPSSSSAYFPGQLPSS
The following text describes a protein:
Function:
Inhibits autoprocessing of CASP1, CASP1-dependent IL1B secretion, PYCARD aggregation and PYCARD-mediated apoptosis but not apoptosis induced by FAS or BID. Displays anti-inflammatory activity. Required for immunity against C.albicans infection. Involved in the innate immune response by contributing to pro-inflammatory cytokine release in response to invasive bacterial infection. Contributes to T-cell-mediated inflammatory responses in the skin. Plays a role in protection against periodontitis through its involvement in induction of IL1A via ERK activation in oral epithelial cells infected with periodontal pathogens. Exhibits both ATPase and GTPase activities.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasm.
Sequence:
MAMAKARNPREALLWALSDLEENDFKKLKFYLRDMTLSEGQPPLARGELEGLIPVDLAELLISKYGEKEAVKVVLKGLKVMNLLELVDQLSHICLHDYREVYREHVRCLEEWQEAGVNGRYNQVLLVAKPSSESPESLACPIPEQELDSVTVEALFDSGEKPSLAPSLVVLQGSAGTGKTTLARKMVLDWATGTLYPGRFDYVFYVSCKEVVLLLESKLEQLLFWCCGDNQAPVTEILRQPERLLFILDGFDELQRPFEEKLKKRGLSPKESLLHLLIRRHTLPTCSLLITTWPLALRNLEPLLKQARHVHILGFSEEERARYFSSYFTDEKQADRAFDIVQKNDILYKACQVPGICWVVCSWLQGQMERGKVVLETPRNSTDIFMAYVSTFLPPDDDGGCSELSRHRVLRSLCSLAAEGIQHQRFLFEEAELRKHHLDGPRLAAFLSSNDYQLGLAIKKFYSFRHVSFQDFFHAMSYLVKEDQSRLGKESRREVQRLLEVKEQEGNDEMTLTMQFLLDILKKDSFSNLELKFCFRISPCLAQDLKHFKEQMESMKHNRTWDLEFSLYEAKIKNLVKGIQMNNVSFKIKHSNEKKSQSQNLFSVKSSLSHGPKEEQKCPSVHGQKEGKDNIAGKPKEASTGKGRGTEETDEEVRSPKNTYI
The following text describes a protein:
Function:
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Subcellular Localization:
Cytoplasm.
Sequence:
MCGIVGYIGTQTAVNILIEGLERLEYRGYDSAGIATVTEGKIESVRAKGKLFNLKEKLENHSNFSRLGIGHTRWATHGKPEEHNAHPHLDNQQRIAVVQNGIIENYQTLRDQLKEKGYQFYSETDTEVIPILIADILKDLPSDDPDEALLEAIGKAVHQLEGAFAIAVLDAHCPEQLIVARQQAPLILGFGQGEFFCASDVTALVHHTTTVLSLENGEIARLTPLGVEVYDFNLKRVRKLPRTLDWSATTVEKQGFRHFMLKEIYEQPAVVRTCLATYLNEQWRAADHPSHSPVFLGLDPQLTKNLQHIQVLACGTSWHAGLVGKYLLEQLAGIPTTVHYASEFRYAAPPLTPHTLTIGVTQSGETADTLAALEMEKQRRLTLEDDYKPLILGITNRPESTLATMVNEIINTHAGIEIGVAATKTFVAQVLAFYFLALDIAFQRHSLSLEAIEHIMVGLRQLPAQIETILEQQGSAIEALAHEFAETQDFIFLGRGINFPIALEGALKLKEISYIHAEGYPAGEMKHGPIALLDAKVPVVAIAMPGSVHDKVISNAQEAKARDARLIGVTPMDDSQARSVFDDLLLVPHVEEMLSPIVAVIPLQLLSYHIAARRGLDVDQPRNLAKSVTVE
The following text describes a protein:
Function:
Part of the dynein complex of respiratory cilia.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme. Dynein axonemal particle. Note=Located in the proximal region of respiratory cilia.
Sequence:
MEIVYVYLKKRSEFGKQCNFSDRQAELNIDILPNPELAALYVERNPVDTGIQCSASMSEHEANTERFEMESCGVNHVEGGWPKDVNPQELEQTIRFRKKVEKDENYINAVMQLGSIMEHCIKQNNAIDIYEEYFDDEEAVEVTEEAPSAKTINVFRDPQEIKRTATHLSWHPDGNRKLAVAYSCLKFQRAPMSMNYDSYIWDLENPNRPEIALKPLSPLVTLEYNPKDSHVLLGGCYNGQIACWDTRKGSLVAELSTIEFSHRDPVYGTIWLQSKTGTECFSASTDGQVMWWDIRKISEPIEVVIMDISRKEQLENALGAISLEFESTLPTKFMVGTEQGIVISCNRKAKTQAEKIVCTFYGHHGPIYALQRNPFYPKNFLTVGDWTARIWSEDSRESSIMWTKYHMAYLSDGAWSPVRPAVFFTTKMDGTLDIWDLVFKQCDPALSLKVCDDPLFCLRVQDNGCLIACGSELGTTTLLEVSSSLSTLQRNEKNIASSIFERETRREKILEARHREMRLKEKGKVEGKEDDQKEEEAALDLDELVGKAEEEFFEVIFSELKRKEAEALKKKPKPRKKSSVKVEAEEEVEENVGEEEEAGGIIGIDAVEDMSEEAGEEQEDVPT
The following text describes a protein:
Function:
Involved in lipid metabolism and utilization.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus envelope.
Sequence:
MASLSETLRSHWPIALFGVILFVAGGTELYWNEGRAVHNMMALDEAHADIYSVRFTEEEQEVGLEGRIVHLSGPILVGEPLTEPDYNIQLLAVKLRRRVQMYQWVEEAVEHNYGDSVGTTHSDSRTYYYTREWRDKIVDSRNFYNRHGHTNPSHFPIESHVQVADAVFIGRYELGAEVKEKFNNYQELTSDIRPEDSGVKLHLGIYYHTNDVFNPEVGDLRLLFSFAGMEGEVFSVVGKLSGNKLVPYITSRGVPVLLVYPGGLSVQEVFRLEARAQVLHTWWWRFVGWLLIFFGVTCNTKILRLLFVRVPLLVALAPDPQFPVTGNLLIAFSLALTIAAVAWILHRPVIGACLLLAGASPYVWFTRNLVDYHRLD
The following text describes a protein:
Function:
Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Sequence:
MVNYKEKLDEAIHLTQQKGFEQTRAEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYGRTFDVNSNCLIPRPETEEVMLHFLQQLEDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQSQIQFLTGDALKPLINEGIKLNGLISNPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPVVFEIGYNQGEALKSIILNKFPDKKIDIIKDINGHDRIVSFKW
The following text describes a protein:
Function:
May be involved in environmental stress response.
Sequence:
MGGESCNLDKDDAEILKPSSSSPSSPSPPTSPPSIFCKPQPPPQQQPSLVLLQHEAIGSNDAQVPESKVASCFLYKRKRNEEEEEEKEEEEEEEEEEKEENSLTVKLINRCSTCRKRVGLAGFRCRCGNLFCARHRYSDIHHCSFDYKTAGREEIAKANPVIRAAKIIRI
The following text describes a protein:
Function:
Negatively regulates telomere length by preventing telomere elongation or promoting degradation of the telomere ends. Recruited to telomeres by interaction with the C-terminus of RAP1, which binds directly to telomeric repeat DNA. This may create a negative feedback loop in which the addition of new telomere repeats creates binding sites for inhibitors of telomere length extension. May also influence the balance of transcriptional silencing at telomeres and the silent mating type locus HMR, which is mediated by SIR (Silent Information Regulator) proteins including SIR3 and SIR4. RIF1 competes with SIR proteins for binding to the C-terminus of RAP1. In the absence of RIF1, a limiting cellular pool of SIR proteins may preferentially associate with RAP1 at sub-telomeric loci, causing enhanced telomeric silencing and attenuated silencing of the HMR locus.
Subcellular Localization:
Nucleus. Chromosome, telomere. Note=Localizes to telomeres. Telomere association begins in G1/S, attains a peak during late G2/S phase of the cell cycle, and is lost during telophase. Localization to telomeres may be increased by telomere uncapping caused by expression of a mutant telomerase RNA subunit (TLC1).
Sequence:
MSKDFSDKKKHTIDRIDQHILRRSQHDNYSNGSSPWMKTNLPPPSPQAHMHIQSDLSPTPKRRKLASSSDCENKQFDLSAINKNLYPEDTGSRLMQSLPELSASNSDNVSPVTKSVAFSDRIESSPIYRIPGSSPKPSPSSKPGKSILRNRLPSVRTVSDLSYNKLQYTQHKLHNGNIFTSPYKETRVNPRALEYWVSGEIHGLVDNESVSEFKEIIEGGLGILRQESEDYVARRFEVYATFNNIIPILTTKNVNEVDQKFNILIVNIESIIEICIPHLQIAQDTLLSSSEKKNPFVIRLYVQIVRFFSAIMSNFKIVKWLTKRPDLVNKLKVIYRWTTGALRNENSNKIIITAQVSFLRDEKFGTFFLSNEEIKPIISTFTEIMEINSHNLIYEKLLLIRGFLSKYPKLMIETVTSWLPGEVLPRIIIGDEIYSMKILITSIVVLLELLKKCLDFVDEHERIYQCIMLSPVCETIPEKFLSKLPLNSYDSANLDKVTIGHLLTQQIKNYIVVKNDNKIAMDLWLSMTGLLYDSGKRVYDLTSESNKVWFDLNNLCFINNHPKTRLMSIKVWRIITYCICTKISQKNQEGNKSLLSLLRTPFQMTLPYVNDPSAREGIIYHLLGVVYTAFTSNKNLSTDMFELFWDHLITPIYEDYVFKYDSIHLQNVLFTVLHLLIGGKNADVALERKYKKHIHPMSVIASEGVKLKDISSLPPQIIKREYDKIMKVVFQAVEVAISNVNLAHDLILTSLKHLPEDRKDQTHLESFSSLILKVTQNNKDTPIFRDFFGAVTSSFVYTFLDLFLRKNDSSLVNFNIQISKVGISQGNMTLDLLKDVIRKARNETSEFLIIEKFLELDDKKTEVYAQNWVGSTLLPPNISFREFQSLANIVNKVPNENSIENFLDLCLKLSFPVNLFTLLHVSMWSNNNFIYFIQSYVSKNENKLNVDLITLLKTSLPGNPELFSGLLPFLRRNKFMDILEYCIHSNPNLLNSIPDLNSDLLLKLLPRSRASYFAANIKLFKCSEQLTLVRWLLKGQQLEQLNQNFSEIENVLQNASDSELEKSEIIRELLHLAMANPIEPLFSGLLNFCIKNNMADHLDEFCGNMTSEVLFKISPELLLKLLTYKEKPNGKLLAAVIEKIENGDDDYILELLEKIIIQKEIQILEKLKEPLLVFFLNPVSSNMQKHKKSTNMLRELVLLYLTKPLSRSAAKKFFSMLISILPPNPNYQTIDMVNLLIDLIKSHNRKFKDKRTYNATLKTIGKWIQESGVVHQGDSSKEIEAIPDTKSMYIPCEGSENKLSNLQRKVDSQDIQVPATQGMKEPPSSIQISSQISAKDSDSISLKNTAIMNSSQQESHANRSRSIDDETLEEVDNESIREIDQQMKSTQLDKNVANHSNICSTKSDEVDVTELHESIDTQSSEVNAYQPIEVLTSELKAVTNRSIKTNPDHNVVNSDNPLKRPSKETPTSENKRSKGHETMVDVLVSEEQAVSPSSDVICTNIKSIANEESSLALRNSIKVETNCNENSLNVTLDLDQQTITKEDGKGQVEHVQRQENQESMNKINSKSFTQDNIAQYKSVKKARPNNEGENNDYACNVEQASPVRNEVPGDGIQIPSGTILLNSSKQTEKSKVDDLRSDEDEHGTVAQEKHQVGAINSRNKNNDRMDSTPIQGTEEESREVVMTEEGINVRLEDSGTCELNKNLKGPLKGDKDANINDDFVPVEENVRDEGFLKSMEHAVSKETGLEEQPEVADISVLPEIRIPIFNSLKMQGSKSQIKEKLKKRLQRNELMPPDSPPRMTENTNINAQNGLDTVPKTIGGKEKHHEIQLGQAHTEADGEPLLGGDGNEDATSREATPSLKVHFFSKKSRRLVARLRGFTPGDLNGISVEERRNLRIELLDFMMRLEYYSNRDNDMN