lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'. Plays a role in hematopoiesis and malignant transformation.
Subcellular Localization:
Nucleus.
Sequence:
MSETPAQSSIKQERISYTPPESPVASHRSSTPLHVHTVPRALRMEEDSIHLPTHLRLQPIYWSRDDVAQWLKWAENEFSLRPIESNKFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHILKQRKSRMLFSPFFPPGDSIHTKPEVLLHQNHDEDNCVQRTPRTPAESVHHNPPTIELLHRPRSPITTNHRPSPDPEQQRPQRSPLDNMSRRLSPVEKAQGPRLQQENNHQETYPLSVSPVENNHCLPSSPWQESTRVIQLMPSPIMHPLILNPRHSHSVDFKQSRHSEDGMNREGKPINLSHREDLAYLNHIMVSMSPPEEHAMPIGRIADCRLLWDYVYQLLSDSRYENFIRWEDKESKIFRIVDPNGLARLWGNHKNRTNMTYEKMSRALRHYYKLNIIRKEPGQRLLFRFMKTPDEIMSGRTDRLEHLESQVLDEQTYQEDEPTIASPVGWPRGNLPTGTAGGVMEAGELGVAVKEETRE
The following text describes a protein:
Function:
RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly.
Sequence:
MLVQLPRLTNTLRDPFDVDQAYLQRKLILQNYNRPRNSASSLDESELARKIVHRWEEASFEVRQAYKQFIAAVVELIDGEMPSEEFHEVAVAVYRLFGMPVEEDSVDRNIAEKKLELQKILGHMVTDANLERVASLSQNLFGLVSTDHGSLHDLETHVNGSSNDLEFGADLIFQAPTRFLLDVSLEVGELPSEESFAPYSSFHEGWFEHNDSQHNPCASNGGNFNLSWLRDACDRIVKECASQLSRDELAMAICRVLDSDKPGEEIAGDLLDLVGDGAFETVQDILSHRKELVDAIHHGFLVLKSEKTASNAQSRMPSYGTQVTVQTESEKQIDKLRRKEEKRQRRGTEYGAENDLSAADFSSLLQASETKNLLDDLVGSGPGAQSLAVTALPQGTVRKHYKGYEEVIIPPTPTAQMKPGERLIEIKELDDFAQAAFRGYKSLNRIQSRIFQTVYHTNENILVCAPTGAGKTNIAMISILHEIGQHFKDGYLHKDEFKIVYVAPMKALAAEVTSTFSHRLSPLNMTVRELTGDMQLSKNELEETQMIVTTPEKWDVITRKSSDMSLSMLVKLLIIDEVHLLNDDRGPVIEALVARTLRQVESTQTMIRIVGLSATLPNYLEVAQFLRVNPEMGLFFFDSSYRPVPLAQQYIGISEQNFAARNELLNEICYKKVVDSLRQGHQAMVFVHSRKDTAKTAQKLVELGRKYDDLEVFKNDTHPQFNLIKREVVKSRNKDLVELFEYGIGVHHAGMLRADRGLTERLFSDGLLKVLVCTATLAWGVNLPAHTVVIKGTQLYDPKAGGWRDLGMLDVMQIFGRAGRPQFDKSGEGIIITSHEKLAYYLRLLTSQLPIESQFISSLKDNLNAEVALGTVTNVKEACAWLGYTYLFIRMRLNPLAYGIGWDELVADPSLSSKQRSLVTDAARALDKAKMMRFDEKSGNFYCTELGRIASHFYIQYSSVETYNEMLRRHMNDSEVIDMVAHSSEFENIAVREEEQNELETLVRTSCPLEVKGGPSNKHGKISILIQLYISRGSIDTFSLVSDAAYISASLARIMRALFEICLRRGWCEMSLFMLEYCKAVDRKIWPHLHPLRQFDKDISSDILRKLEERGADLDRLQEMQEKDIGALIRYANGGKLVKQCLGYFPWIQLSATVSPITRTVLKVDLRITPEFIWKDRFHGATERWWILVEDSENDHIYYSELFTLTKRMARGEPQKLSFTVPIFEPHPPQYYIRAVSDSWLHAEAFYTISFHNLALPEACTSHTELLDLKPLPVTSLGNSTYEALYKFSHFNPIQTQSFHVLYHTDNNVLLGAPTGSGKTISAELAMLHLFNTQPDMKVIYIAPLKAIVRERMNDWKKRLVSQLGKEMVEMTGDYTPDLMALLSADIIISTPEKWDGISRNWHSRSYVKKVGLMILDEIHLLGADRGPILEVIVSRMRYISSQTERAVRFVGLSTALANAGDLADWLGVGETGLFNFKPSVRPVPLEVHIQGYPGKFYCPRMNSMNKPAYAAICTHSPTKPVLIFVSSRRQTRLTALDLIQFAASDEQPRQFINILEEALQMVLSQITDQNLRHTLQFGIGLHHAGLNDKDRSLVEELFANNKIQVLVCTSTLAWGVNLPAHLVIIKGTEYYDGKAKRYVDFPITDILQMMGRAGRPQFDQHGKAVILVHEPKKSFYKKFLYEPFPVESSLKEQLHEHINAEIISGTICHKEDAVHYLTWTYLFRRLTVNPAYYGLENTGPEILSSYLSSLVQNTFEDLEDSGCIKMSDDSVEPMMLGSIASQYYLSYMTVSMFGSNIGPDTSLEVFLHILSAASEYDELPVRHNEENYNEALSKRVRYMVDRNRLDDPHVKANLLFQAHFSQLELPISDYVTDLKSVLDQSIRIIQAMIDICANSGWLLSSITCMHLLQMVMQGLWFDKDSNLWMLPSMSDDLASLLNKRGISKVQQLLDLPNATLQTQVGNFPASRLYQDLQRFPRVQVRLKLQRKGSDDAKAPALNIKLEKINSKRNASRAFAPRFPKVKDEAWWLVLGNTFTSELYALKRVSFSDRMVTHMELPSTSTGLQGMKLIVVSDCYIGFEQEHSIDHLTY
The following text describes a protein:
Function:
Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MCSDFRRAESGTELLARLEGRSSLKELEPNLFADEDSPVHGDIFEFHGPEGTGKTEMLYHLTARCILPKSEGGLQIEVLFIDTDYHFDMLRLVTVLEHRLSQSSEEAMKLCLARLFLAYCSSSMQLLLTLHSLEALLCSRPSLCLLIVDSLSSFYWIDRVSGGESVALQESTLQKCSQLLERLVTEYRLLLFATTQSLMQKGSDSADGPSSSKHPCDGDMGYRAYLCKAWQRVVKHRVIFSRDDEAKSSRFSLVSRHLKSNSLKKHSFMVRESGVEFC
The following text describes a protein:
Function:
Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues.
Subcellular Localization:
Secreted, cell wall. Secreted, extracellular space, apoplast.
Sequence:
MGSVRGSSGWVAAAVMLWLVAGVAARADSIKDFKQWSPQQTEMYPNRTGVKLILKDPKASYTGMASPLQYTYAANGAYIKMPPGDSAGVVSTFYMASSGPKHCEFDFEFLGNKPGMPYLLHTNIFVDGVGGREQQIRLWFDPRKEAHFYNFQWNKDLLVFYIDSMPVRMFKNLENEIPGFKYPKKCAMGVYLSVWDGSSWATDGGRVKLDWASAPFVTTYDRFKLAGCVAKNGDAASIEKCQTSFAAAPGDHVQKMGQTKTRQLREVKAKYLHYNYCDDRKRYPVAPRECAYNVL
The following text describes a protein:
Function:
Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfer of an acyl group on a lysophosphatidic acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors. Functions in phosphatidic acid biosynthesis. May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2. Involved in keratinocyte differentiation. Regulates lipid droplet fusion.
Subcellular Localization:
Cytoplasm. Lipid droplet.
Sequence:
MAAAVAISLSLAALPAAVAASSSSSGPAGTSSSIRIRRAAMAEEESAEESPGEGSGWLSSWLPAWCPTSLVHLKDAEEKILKCITSTYSKQYVFISNGNKIWTLMFSQNLSQKTPLVLLHGFGGGVGLWALNFEDLCENRTVYAFDLLGFGRSSRPQFDADAEVAENQFVESIEEWRRKMGLDRMILLGHNLGGFLAAAYSLKYPSRAKHLILVEPWGFPERPSSAEHERSIPIWIKALGAVLSPFNPLAGLRIAGPFGLSLVQRIRPDFKRKYSSMFDDDTVTEYIYHCNVQSPSGETAFKNMTVPYGWAKRPMLQRIAHMHKDIPITVIYGARSCIDGNSGTTIQSLRPNSYVKTIAILGAGHYVYADQPEDFNQKVKEICNSVD
The following text describes a protein:
Function:
Lignin degradation and detoxification of lignin-derived products.
Subcellular Localization:
Secreted, extracellular space, apoplast.
Sequence:
MKWRSLPAATVAIATGVVFFLSAIGAPAAMASVVEHTFVVRQVKMTHLCKETLATVVNGQFPGPAIEVTEGDSVTVHVVNQSPYNLTIHWHGVKQRLNCWADGVPMITQCPILPNQNFTYRFNVAGQEGTLWWHAHVSFLRASVHGALIIRPRRGASSYPFPKPYKEIPIIIGEWWEMDLLKADWDIKQHVIDAYFNASTINGKLGDLYSCSGAVEDGYLLDVEPGRTYLLRIINAALFSEYYLKIAGHKFTVVAADANYVSPYTTDVIAIAPGETMDALLVADADPGRYYMVALPNQSPLPDPQSPTLITRGIVQYSNKQRAADGGGRPSSDIPVSPEMPDQHDMITSFYFHGNLSGLHHPQHLDVPKHVDERLFITLGLGSICRGGQSSCKRSENNESMDVATMNSFTYQQPAVATPLLELHYYSIDNRVLSMLQELPDKPPRVFNYTDPALIPPGPKEAKLEPTSKATIARRFRQGAVVEVVFQGMAILSSESNPMHLHGHDVFVLAQGEGNYDATRDVPRYNLVNPAVKNTVFVPRLGWVAVRFIADNPGIWYMHCHFGFHLSMGMVALFIVEDGSTVDTSLPAPPADFPTCGHDHNVMSNEFYPI
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
MTSLTIQMARWLKKEAVWRYVGFVSTILGLLCYGLSSSFNSLFGEWSLLKIFLYSVFSLFICLWSLFPKVWQYSTSLRLKAHLAFLVLTITSVYSYFADKVVNRKPDAYSLISSAAFAIVSLSLSRQTECGFEVDFLYFFLGCLIVQLLKIKLALAIAGVGFSYNLGVQDEHSVVIDVNSLRTDNASIMPQLRTCIRALQQGNSNVTNMLLEHVKEYLQDNSNLAGIDHNFVIEALPSGYINELLETIKLMMGGDGLEKECCDVYCNWQRESLEECLINLFEVQEINVKQKWEEKQLEEYIIRRWIKALKLSAQIQFPNEQRLSDGVFSGFSSIADLCFTEVCRGATIQLLKCVDEVVSESSPKWPLSKMLDMLQTLRGLIPEFQSLFPESMVKEVMTVHHKLGETCRVIFMKMEDNIFCNPSVKII
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Sequence:
MSLRIATTTARAIPARAVATRSIMTLRRVAVPQASPKGYRQSSILQDTAKTAHSAFANLASAAPIKKGDKMPDVEIKIDGPEGKVNLGKEKGKNVVVLVPGAFSGVCSNQVPPYITSFSDFKAKGINNVYVVAVNDIFVVNAWKDKMIGEFSSKEGEGVKFAADDTAALASALGLTFDAQPVFGGPRLKRGVLVVNDGVVEYVGVEDSPGDITISAADKVIKQL
The following text describes a protein:
Function:
Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. Uses malonyl-CoA to add 2 carbons per cycle to the chain of long-chain fatty acids. Condensing enzyme required for the formation of isopentadecanoate (C15iso) and isoheptadecanoate (C17iso), both play critical roles in animal development and growth.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MMDQILGTNFTYEGAKEVARGLEGFSAKLAVGYIATIFGLKYYMKDRKAFDLSTPLNIWNGILSTFSLLGFLFTFPTLLSVIRKDGFSHTYSHVSELYTDSTSGYWIFLWVISKIPELLDTVFIVLRKRPLIFMHWYHHALTGYYALVCYHEDAVHMVWVVWMNYIIHAFMYGYYLLKSLKVPIPPSVAQAITTSQMVQFAVAIFAQVHVSYKHYVEGVEGLAYSFRGTAIGFFMLTTYFYLWIQFYKEHYLKNGGKKYNLAKDQAKTQTKKAN
The following text describes a protein:
Function:
Acts as a component of the histone chaperone complex chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto DNA during replication and repair. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer.
Subcellular Localization:
Nucleus.
Sequence:
MKVITCEISWHNKEPVYSLDFQHGNDKFNRLASAGVDTAVRLWKIERSPEGKAVVEFLASLARHTKAVNVVRFSPNGEILASGGDDAAILLWKLNETKECEPAPFQEQDEFELNKENWTVFKTLRGHLEDVYDICWTQDSNFMVSASVDNTAITWDVTKGQKLSIFNEHKSYVQGVTWDPLGQYIATLSCDRIMRVYKTETKRVAYNVSKMTSSPGPDGEAKSFRMYHDDSMKSFFRRLTFTPDGSLLLTPAGCVEAGETVINTTYVFGRKNLRRPIAHLPCPTKATLAVRCCPVYFELRPTMKDDSGESRPQGLITQPYRMVFAVASEDAVLFYDTQQLFPFGYVSNVHYHTLSDISWSSDGNFLAISSTDGYCSFVTFEEGELGVPLKEKPVALIPKTPATERKIKKAQSKKVSSPGSRQELTPSNKSMEHSAPSTPMNSRPTPASGSRECTPVSSNSLASTPNSEDKRNAKGGQPRRIMLNTLEAWSKPTTPSPRRISLISVKTNSPSSAPSSPALSTTPRPEANPSVPPSEDVGCKPPESKRLRTEDSPSCSSSDKPSGSDQTNK
The following text describes a protein:
Function:
Plays a fundamental role in microtubule organizing center structure and function. Component of the infraciliary lattice (ICL) and the ciliary basal bodies.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MGACSGKQKPVRKGKQQLSEIKRFAKQNIRQFYRFGKVLGSGSFGTVKVGYSVRDSKAFAIKTIHKYRMREQFYLVLRELDILTQLDHPNIIKVFEEYEDDMYYHFVMEYCSGGELLERIVEEGNIGESDSKEIMQQLFSAINYLHSMGIAHRDLKPENILFASKEKDAPIKVIDFGLSKKFRNINQKLQRMNSKVGTPIYVAPEIIAGDYSFQCDEWSLGCILHVLLCGNPPFSAKKLDMLEAKIKHSDVDFSLSVFEHISLEAKDLIKNLLVKQPKKRITCGKALEHQWFKNMKQSSHQQKLSNNQHQKIIRLLHTYANSSKLKKETLKILINQLTENQISQLKDVFVSYDKDCNGTISIQELLQIMSNLGFKESEEELVQMIKKFNNINPSNDDITQDTQITYTSFLSALVNCKSYLNKERLWNLFKYFDSDNKNFITIEDVRKAFEREGRQLSESKLVSLFSEILQNEKQKIIDFDQFCQMMQDNLYNSNNDSKNLEKELDCFEN
The following text describes a protein:
Function:
Catalyzes the hydrolysis of a wide range of substrates including cholesteryl esters, phospholipids, lysophospholipids, di- and tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFAs). Preferentially hydrolyzes FAHFAs with the ester bond further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed more quickly than saturated FAHFAs. Has an essential role in the complete digestion of dietary lipids and their intestinal absorption, along with the absorption of fat-soluble vitamins (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MGRLEVLFLGLTCCLAAACAAKLGAVYTEGGFVEGVNKKLSLLGGDSVDIFKGIPFATAKTLENPQRHPGWQGTLKATNFKKRCLQATITQDNTYGQEDCLYLNIWVPQGRKQVSHNLPVMVWIYGGAFLMGSGQGANFLKNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPGNFGLRDQHMAIAWVKRNIAAFGGDPDNITIFGESAGAASVSLQTLSPYNKGLIRRAISQSGMALSPWAIQKNPLFWAKTIAKKVGCPTEDTGKMAACLKITDPRALTLAYKLPVKKQEYPVVHYLAFIPVIDGDFIPDDPINLYNNTADIDYIAGINNMDGHLFATIDVPAVDKTKQTVTEEDFYRLVSGHTVAKGLKGAQATFDIYTESWAQDPSQENMKKTVVAFETDVLFLIPTEIALAQHKAHAKSAKTYSYLFSHPSRMPIYPKWMGADHADDLQYVFGKPFATPLGYRPQDRAVSKAMIAYWTNFARSGDPNMGNSPVPTHWYPYTLENGNYLDITKTITSASMKEHLREKFLKFWAVTFEVLPTVTGDQDTLTPPEDDSEVAPDPPSDDSQVVPVPPTDDSVEAQMPATIGF
The following text describes a protein:
Function:
Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine. Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine. Can convert (S)-tetrahydrocolumbamine to tetrahydropalmatine. Can convert (S)-norreticuline to (S)-norcodamine. Can convert (S)-reticuline to (S)-codamine. Substrate preference is (S)-scoulerine > (S)-tetrahydrocolumbamine > (S)-norreticuline > (S)-reticuline.
Sequence:
MATNGEIFNTYGHNRQTATVTKITASNESSNGVCYLSETANLGKLICIPMALRAAMELNVFQLISKFGTDAKVSASEIASKMPNAKNNPEAAMYLDRILRLLGASSILSVSTTKKSINRGGDDVVVHEKLYGLTNSSCCLVPRQEDGVSLVEELLFTSDKVVVDSFFKLKCVVEEKDSVPFEVAHGAKIFEYAATEPRMNQVFNDGMAVFSIVVFEAVFRFYDGFLDMKELLDVGGGIGTSVSKIVAKYPLIRGVNFDLPHVISVAPQYPGVEHVAGDMFEEVPKGQNMLLKWVLHDWGDERCVKLLKNCWNSLPVGGKVLIIEFVLPNELGNNAESFNALIPDLLLMALNPGGKERTISEYDDLGKAAGFIKTIPIPISNGLHVIEFHK
The following text describes a protein:
Function:
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Sequence:
MSSGNVPKIERLSCVPNDYPWGEVGNDSLAARLASKNGAVSFDLKPEQAYAELWMGTHPNNPAHLFSSPDTLLSTHLKKNPSLLGAANRFSPPFTGAKGSGAEGQEEGHVPFLFKVLTCKQALPLQIHPDKALAKKLHEENPKQFGDINHKPEIAVCLSDRFLGFASFRPYDKIASLLKSVQEISLLPSLLQKSIKSFISAPSAETLQPTWEGFIKLGDNEESVKKFSDRVLSQGLKAFDSVDIEDEDKNRLVRAVELGKKYNPGDAGLFSSLLFLNLIELKKDQGMYVGADGPHAWLEGEIVELMAISDNVLNVGFTSDDSKDDPSLVAKAVTCTPKAIKDLLLDASKYSKSQNGRTTVYSTPFEEFSIMKIAGDEILSPLDGAGVAVVLEGEWTVEDQEGTKRGGEGTDGEGGEGTIWFIGSATETKWTAKGGKGQIWIAFYDKTAKKDDVGKK
The following text describes a protein:
Function:
Acts as a target recruitment subunit in the E3 ubiquitin ligase complex zyg-11-cul-2-elc-1. Required for metaphase to anaphase transition and M phase exit at meiosis II. Regulates polarity establishment.
Sequence:
MDHNAALTTCSTSAIPRLARLATERIAELIENDALPEFDHKVIASCSNDIFEVLRQKKKLNHQTLQTMCSTSRFQINKIDLMGNKVELQDLELCSNQNLVSFRLGDIDYFPNTNKIQVADVLDTALNRTSRQQLRHLDLSGRHRITSNWPTYVARKLPRLESLAFANRSTANETLSQIGASLLNLRFLDISSTCVTDISCISSLRNLEVLIMYNLNILKGDVTETLSNLTKLRVLDISRKVNTDYLQETSQDAHLDLALGIYNRSVEAIESGTATPWAELRAIDMSGLSIVQFGTDRALAFVEKIIEAHPKLEQISLLATPLDSSLIEIPNRNLQVINTVSRRSIIFALSHYANLDRPAFITHALHSVYYQLQSGYDKFSQEELKECLRLVCISMQQGLNTLPVQIAGSACLYHLCKMKRIKRLSVKEVNNCIERSLDAAEQYRSMTQLQKNVWLTICNDYLLHLDEIDFYRTCKVALDTMLLNRDASVERMTIAIVSIVTPKMRPSEAKILTTETKYVYHLVKIMNDYLEAYTREHRVGHERDNENALYTLKFTLSALWNLTDECPATCKAFLDAGGVQIAFRILKAFDYHGNVQTKVLGILNNLAEVEELHLGQLCKNEYISVLISCLDGSFNEVDSKGRYREVERSYFAAGILANLLTNTDGWESENQRDEACEKLLELIEQYPTLPSAMVSYKSFIPFSRIVRESNSNGAIMWCLWGVHHVLQHREKNKAPTYEKGYIEMFMDSGLSPIVEDMSHGHSKHIHNLDIRVVHLAREIIDIVSCHSLSSSPVRLVRRV
The following text describes a protein:
Function:
Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress.
Subcellular Localization:
Secreted.
Sequence:
MPHTRLLLLLLMLCMARSSLHYKLYKAESIFSCLKEALEEAKSRNIENNSVLSKREYESEPREILSQEEMDEEDEKEKRTFPPAARYRYISQPQVKGRVYQNKAKSDSRTKFTLSLDVPTKLMNIMFDIAKAKKMNAKAAANAQLMAQIGRRK
The following text describes a protein:
Function:
Protein kinase that may play an important role in cellular stress response. May be involved in the regulation of processes such as cell survival, neuronal excitability and renal sodium excretion.
Sequence:
MAYYDPTPPSPSNEVNLGASVNPHAKPTDFDFLAVIGKGTFGKVLLAKLKADGKFYAVKVLQKKVILKKKEQKNIMAERNVLLKSLKHPFLVGLHYSFQTSEKLYFVLDYVNGGELFYHLQRERCFSEPRARFYTAEVASAIGYLHSLNIVYRDLKPENILLDYQGHVVLTDFGLCKEGIEPEGTTTTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLHEMLYSLPPFYSRDVSEMYDAILHKPLHLPPGKSESACLLLYGLLQKDQHRRTGAIADFLEIKNHVFFAPINWDDLYHKRITPPYNPNVRGPADLQHIDPEFTREMVPHSVGRTPEPTPSLATSSSNAFTGFSYISGEDGFL
The following text describes a protein:
Function:
Chaperone that functions as a gatekeeper on the periplasmic side of the SecYEG translocon. Facilitates the translocation of precursor proteins across SecYEG by interacting with the translocating substrate. Also plays a role in the release of newly synthesized secreted proteins at the periplasmic exit site of the Sec translocon.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. Note=Located at the lateral gate of SecY.
Sequence:
MLIEKMHNLTNSKISKFILGLIAVSFLVGGMSGYLFSSNDTYAAKVNGEVISQQDFLNRYNQEFEIRAQREGEAFVAQSDSPEFVTALRQNIVNLMIDQELLRQYVKELKLGVSDEMIKRAIVTDPNFQVKGKFDNAVYQRILQQNHLTSDGYASILRASLPLEQIQNGVANSEFIVPAQVKNSAEVFFQKRLARLATLSLADEMAKQSVSDDEIKTYYEANQKSFVQPEQVKVQYIDLSADNISRNLQVTDVEIAQYYQDNKAQFMTQHLAHIQFANEQDAKVAYEELQKGANFADVAKAKSLDKISGENGGDLGWVNENELPKAFEDAAAALQVGQYSQPINVDGNYHIVLVQERKAQSLENVKAQIADLVRKSLMESRYFSLEKQASDKAFEDSKSLNTAAQAAGVKVQESDYFSRQNVPAGLNFPNVIYTIFESDTTNVGMNSEPINVGDYHTIIVRVLDRKAEGVKSLEEAKIDIETFLKRQKAENALNGKAQQAVKKLSENPESKVDGINFSSEQTFTLSENKDPILTNGIFSIAKPESSKALYQVVHNSNGDVVVVALNKVEQGSLSEKELSQFAMQLLRSHQSELQVQLIQGLRERAKIEVNDSFINQDDEAQQ
The following text describes a protein:
Function:
Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with AURKB or AURKC, the N-terminus associated with BIRC5/survivin and CDCA8/borealin tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs AURKB/C toward substrates near microtubules. The flexibility of the SAH domain is proposed to allow AURKB/C to follow substrates on dynamic microtubules while ensuring CPC docking to static chromatin (By similarity). Activates AURKB and AURKC. Required for localization of CBX5 to mitotic centromeres. Controls the kinetochore localization of BUB1.
Subcellular Localization:
Nucleus. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle. Midbody. Chromosome, centromere, kinetochore. Note=Colocalized at synaptonemal complex central element from zygotene up to late pachytene when it begins to relocalize to heterochromatic chromocenters. Colocalizes with AURKB at a connecting strand traversing the centromere region and joining sister kinetochores, in metaphase II centromeres. This strand disappears at the metaphase II/anaphase II transition and relocalizes to the spindle midzone (By similarity). Colocalizes with AURKB at mitotic chromosomes. Localizes to inner kinetochore. Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Cocalizes to the equatorial cell cortex at anaphase.
Domain:
The IN box mediates interaction with AURKB and AURKC; The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. It can refold after extension suggesting an in vivo force-dependent function. The isolated SAH domain is monomeric.
Sequence:
MGTTAPGPIHLLELCDQKLMEFLCNMDNKDLVWLEEIQEEAERMFTREFSKEPELMPKTPSQKNRRKKRRISYVQDENRDPIRRRLSRRKSRSSQLSSRRLRSKDSVEKLATVVGENGSVLRRVTRAAAAAAAATMALAAPSSPTPESPTMLTKKPEDNHTQCQLVPVVEIGISERQNAEQHVTQLMSTEPLPRTLSPTPASATAPTSQGIPTSDEESTPKKSKARILESITVSSLMATPQDPKGQGVGTGRSASKLRIAQVSPGPRDSPAFPDSPWRERVLAPILPDNFSTPTGSRTDSQSVRHSPIAPSSPSPQVLAQKYSLVAKQESVVRRASRRLAKKTAEEPAASGRIICHSYLERLLNVEVPQKVGSEQKEPPEEAEPVAAAEPEVPENNGNNSWPHNDTEIANSTPNPKPAASSPETPSAGQQEAKTDQADGPREPPQSARRKRSYKQAVSELDEEQHLEDEELQPPRSKTPSSPCPASKVVRPLRTFLHTVQRNQMLMTPTSAPRSVMKSFIKRNTPLRMDPKCSFVEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGASKALNVTVDVQSPACTSYQMTPQGHRAPPKINPDNYGMDLNSDDSTDDEAHPRKPIPTWARGTPLSQAIIHQYYHPPNLLELFGTILPLDLEDIFKKSKPRYHKRTSSAVWNSPPLQGARVPSSLAYSLKKH
The following text describes a protein:
Function:
Promotes divisions in the guard cells (GCs) after the guard mother cells (GMC) symmetric division.
Sequence:
MALEEEEESQNAPFCVLDGLFCEEESEFHEQVDLCDESVEKFPFLNLGLSDHDMLWDDDELSTLISKQEPCLYDEILDDEFLVLCREKALDWIFKVKSHYGFNSLTALLAVNYFDRFITSRKFQTDKPWMSQLTALACLSLAAKVEEIRVPFLLDFQVEEARYVFEAKTIQRMELLVLSTLDWRMHPVTPISFFDHIIRRYSFKSHHQLEFLSRCESLLLSIIPDSRFLSFSPSVLATAIMVSVIRDLKMCDEAVYQSQLMTLLKVDSEKVNKCYELVLDHSPSKKRMMNWMQQPASPIGVFDASFSSDSSNESWVVSASASVSSSPSSEPLLKRRRVQEQQMRLSSINRMFFDVLSSSPR
The following text describes a protein:
Function:
May modulate the activity of casein kinase-1. Inhibits CSNK1D autophosphorylation (in vitro).
Sequence:
MGAGNFLTALEVPVAALAGAASDRRASCERVSPPPPLPHFRLPPLPRSRLPGPVSRPEPGAPLLGCWLQWGAPSPGPLCLLFRLCSCTCFAPLPAGADMDPNPRAALERQQLRLRERQKFFEDILQPETEFVFPLSHLHLESQRPPIGSISSMEVNVDTLEQVELIDLGDPDAADVFLPCEDPPPTPQSSGMDNHLEELSLPVPTSDRTTSRTSSSSSSDSSTNLHSPNPSDDGADTPLAQSDEEEERGDGGAEPGACS
The following text describes a protein:
Function:
Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase. Capable of transferring glucosyl residues to unbound acceptors such as free oligoglucans or oligoglucan derivatives.
Subcellular Localization:
Cytoplasm. Vacuole. Note=Localizes to glycogen granules (glycosomes) in the cytoplasm. Localizes to the vacuole during nitrogen starvation-induced glycophagy (autophagy of glycosomes).
Sequence:
MYKKLAIATLLYSADYLPGVFALGHQVNKLLEEAGKKGDIETCLIVTTSLFNGTLSELAKNILQSIYTKIVLVEPLNCQEESIQKNSENLALLERPELSFALIKARLWELTQFEQVLYLDSDTLPLNKEFLKLFDIMSKQTTSQVGAIADIGWPDMFNSGVMMLIPDADTASVLQNYIFENTSIDGSDQGILNQFFNQNCCTDELVKDSFSREWVQLSFTYNVTIPNLGYQSSPAMNYFKPSIKLIHFIGKHKPWSLWSQKNFIKNEYHDQWNEVYEEFKEEHQLNNEVSKPKISDSDKTETPETITPVDAPPSNEPTTNQEIDTISTVEENVDNQNAEPVPNSDHSPAPNPVPLDFTKWLTTFINKDHLTNQPVNESREYSKENDNNIINSSSNRDQESPPNSTQELNSSYSVVSTQADSDEHQNAEEEDSTTDNASNSGEESHLDDISTAASSNNNVSNQPDGKNFSNSKENNISVESSPSNPEQKRSTDNIQKPSVSTNDLPDDVEPHTSVDDNIQYLEKDKEGYEEFLPDVYESNAIDNEEEFFDDDARDATEGETKTSAVADKQEDMKLTAEETNQPQQEMPNFKFDWEDSDYLSKVERCFPDDIFEYAVE
The following text describes a protein:
Function:
Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Sequence:
MPREDRATWKSNYFLKIIQLLDDYPKCFIMQQICMFLHGKAVVLMGKNTMLRKVIRGHLENNPALEKLLSHVHFNMGFVFLEGVRNVASICLQIGYPAVASVPHSIINGYKRVLAVAVETDYSFPLAEKVKAFLADPSAFVAAAPVAVETADPVAAAPAKVEAKEESEELDKDMGFGLFD
The following text describes a protein:
Function:
Has a role in transport between endoplasmic reticulum and Golgi.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MLSGGYYQGSGDPQDPQQQQPQPQSGNPFMSPEVFKYAQMLTGGIQLPPQFQQLNTDKLTQQFQQSQSLIPPYFAITRASFLHKIKNLACPFIVKQWSRSVPEGQTCSPIDNPNAPELYTPLVFTFIFMLITSLIKGAEKGFSMDFLYICILKFICILFFEIVICKLCFSNFGIQGTYPILSLLSDFSSISFYLTIISLFSWNRALFYVSYLYCAAAAFLWTLRTLNSEQCMAQRQTQSTQIITYFLLILAAIQIILLYLLAPKCY
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 promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. 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 (By similarity).
Subcellular Localization:
Nucleus, nucleolus. Cytoplasm. Nucleus.
Sequence:
MASVALSEAEKVYIVHGVQEDLRVDGRGCEDYRCVEVETDVVSNTSGSARVKLGHTDILVGVKAEMGTPKLEKPNEGYLEFFVDCSANATPEFEGRGGDDLGTEIANTLYRIFNNKSSVDLRSLCISPREHCWVLYVDVLLLECGGNLFDAISIAVKAALFNTRIPRVRVLEDEEGAKDIELSDDPYDCIRLSVENVPCIVTLCKIGCRHVVDATLQEEACSLASLLVSVTSKGVVTCMRKVGKGSLDPESIFEMMESSKRVGKVLHVSLQSLLHKEESLGPKRPRVGFLG