lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.
Subcellular Localization:
Nucleus.
Sequence:
MTTTIDENNNNNNNDDKENINTRTQTGDQEPTEDEQEERPSQPSTDNHQPKKIETTTTNNETEPSASTSKSDPTLIKLIGNNVPSIPLEVLKRNPHSKDPSPSAPKWIWAPIDHPARKDGLKLNHWVRTDDQEVYRFAKYDTTSNVFSYTTEEYYHLLRDDDWTKAETDYLFNLLNTYDLRFPVVHDRYEFVGSHERTLDDLKARYYSICQKLIPHRPSTSSTSTHLDDPNKKQLIQSYHFDKQREVERKKHVKSLLNRTPAQLQQEEFIYIETRRLEQNLLKRIRNRDEVMKIIGGFQHHILNEMKFWPIVEPSPTTLQLSRLAISNSINNNLNSANNPSGFAHPPESTSRSAHLNQLDKRNARREDTTMDDLPINASSGGLVGDNQEMNGERPKGIDPQEQIEHDTKHCIYRLDSNSLTGSTTGSGGHHRTVCLRSARIPLPKTAAAQTRISTVWSELNIPNLLSYLPKPLIMPTRKNVESYERLIQATNQLIDLKRLIDRVDNDLKVHRKKKDSLLATLSTSSTHPTSPAKIELDNPPARPPQPNPPIESNPEDPSLLGPDPPEDYHTGSRLGNRAFIIIKSG
The following text describes a protein:
Function:
Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Subcellular Localization:
Cytoplasm.
Sequence:
MHVFYTPDIQKNYELPEEEAQHCTRVLRLGIGDEITLTDGKGHFYKAEITVATNKRCLVAIKETIFQEPLWPCHLHIAMAPTKNMDRNEWLAEKATEIGFDELTFLNCRFSERKVIKTERIEKILISAIKQSLKARLPKLNEMTDFDKFIAQEFQGQKFIAHCYEGEKPQLKNVLKAGEDALVLIGPEGDFSEEEVKKAIECGFTPISLGKSRLRTETAALVACHTMNLLNQ
The following text describes a protein:
Function:
GTPase that plays important roles in innate immunity against S.typhimurium pathogens by mediating formation of an inflammasome in neutrophils. Neutrophils are recruited to the infection site, and then mediate bacterial clearance through the Gbp4 inflammasome-dependent biosynthesis of prostaglandin D2.
Subcellular Localization:
Inflammasome.
Sequence:
MDKPVCLIDTGSDGKLCVQQAALQVLQQIQQPVVVVAVVGLYRTGKSFLMNRLAGKRTGFALSSNIKPKTEGIWMWCMPHPTKAGTTLVLLDTEGLEDVEKGDSKRDTYIFSLAVLLSSTLVYNSRGVIDNKAMEELQYVTELIEHIKVTPDEDADDCTAFAKFFPHFIWCLRDFTLELKLDGKDLTEDEYLEFALKLRPGTSKKVMMYNLPRECIRKFFPCRTCFTFPSPTTPEKRSILESLSPAELDPEFLEVTKRFCKFVFDRSEVKQLKGGHTVTGRVLGNLTKMYVDTISSGAVFCLENAVIAMAQIENEAATQEGLEVYQRGMEKLKSSFPLELEQVSSEHQRLSSMATQAFMARSFKDTDGKHLKALEGEMGKLFDAYRSQNKQVGLETHCDLLLYMRCKDPLILHVYFFPVNDARSKEKVEQNERSSLPISHPRPDRPFQVKTPHVLEVPGASVYPEEGISFRTDVEPNFFKVRKLQVDDVQMNLVRQKDKMSVWTTTIWKEEFVHLQQVRDERKLNSEIEKNDFFNAHRVAFIERVTNVKSIADKLHGQRIIHKELYSEITQTNVTRQQIMRKICDSVDSSGRIAKCKFIDILQEEERCLLEDLKQSES
The following text describes a protein:
Function:
Voltage-dependent high-conductance channel with a slight cation-selectivity; selective for amino acids but excludes triosephosphates or uncharged sugars (By similarity). Non-essential amino acid-selective channel protein and translocation pore for NADPH:protochlorophyllide oxidoreductase A (PORA) and possibly PORB.
Subcellular Localization:
Plastid, chloroplast outer membrane; Multi-pass membrane protein.
Sequence:
MEKSGGRIVMDEIRSFEKAHLFDLGHPLLNRIADSFVKAAGVGALQAVSREAYFTVVDGAGFDSNNVGPPSEITGNKKHRFPNLRGESSKSLDALVKNTGKESLQWGLAAGLYSGITYGMTEVRGGAHDWRNSAVAGALTGAAMAMTTSERTSHEQVVQSALTGAAISTAANLLSSVF
The following text describes a protein:
Function:
Transcription activator that recognizes the motif 5'-TAACGG-3' in the promoter of endosperm-induced genes. Promotes vegetative-to-embryonic transition and the formation of somatic embryos from root explants in a WUS-independent manner but via the expression of embryonic genes (e.g. LEC1, LEC2, FUS3 and WUS). May play an important role during embryogenesis and seed maturation. Together with MYB115, activates the transcription of S-ACP-DES2/AAD2 and S-ACP-DES3/AAD3 thus promoting the biosynthesis of omega-7 monounsaturated fatty acid in seed endosperm. Negatively regulates maturation genes in the endosperm.
Subcellular Localization:
Nucleus.
Sequence:
MEFESVFKMHYPYLAAVIYDDSSTLKDFHPSLTDDFSCVHNVHHKPSMPHTYEIPSKETIRGITPSPCTEAFEACFHGTSNDHVFFGMAYTTPPTIEPNVSHVSHDNTMWENDQNQGFIFGTESTLNQAMADSNQFNMPKPLLSANEDTIMNRRQNNQVMIKTEQIKKKNKRFQMRRICKPTKKASIIKGQWTPEEDKLLVQLVDLHGTKKWSQIAKMLQGRVGKQCRERWHNHLRPDIKKDGWTEEEDIILIKAHKEIGNRWAEIARKLPGRTENTIKNHWNATKRRQHSRRTKGKDEISLSLGSNTLQNYIRSVTYNDDPFMTANANANIGPRNMRGKGKNVMVAVSEYDEGECKYIVDGVNNLGLEDGRIKMPSLAAMSASGSASTSGSASGSGSGVTMEIDEPMTDSWMVMHGCDEVMMNEIALLEMIAHGRL
The following text describes a protein:
Function:
Has a ligand-stimulated tyrosine-protein kinase activity. Binds 3 insulin-like peptide ligands. Regulates cell number and cell size during development by regulating cell growth and survival, affecting body size and organ size, including ovaries and imaginal disks. Plays a role in life-span determination. May be involved in regulation of other neuroendocrine signaling pathways. Involved in the development of the embryonic nervous system. Functions upstream of dock/dreadlocks for photoreceptor (R cell) axon guidance and targeting in the visual system. Involved in the acs mediated recovery of gut enterocytes following the cytoplasmic purge response to intestinal bacterial infection.
Subcellular Localization:
Membrane; Single-pass type I membrane protein. Cell projection, axon. Cell projection, growth cone membrane; Single-pass type I membrane protein. Note=Enriched in the axons and growth cones of R cells.
Sequence:
MFNMPRGVTKSKSKRGKIKMENDMAAAATTTACTLGHICVLCRQEMLLDTCCCRQAVEAVDSPASSEEAYSSSNSSSCQASSEISAEEVWFLSHDDIVLCRRPKFDEVETTGKKRDVKCSGHQCSNECDDGSTKNNRQQRENFNIFSNCHNILRTLQSLLLLMFNCGIFNKRRRRQHQQQHHHHYQHHHQQHHQQHHQRQQANVSYTKFLLLLQTLAAATTRLSLSPKNYKQQQQLQHNQQLPRATPQQKQQEKDRHKCFHYKHNYSYSPGISLLLFILLANTLAIQAVVLPAHQQHLLHNDIADGLDKTALSVSGTQSRWTRSESNPTMRLSQNVKPCKSMDIRNMVSHFNQLENCTVIEGFLLIDLINDASPLNRSFPKLTEVTDYIIIYRVTGLHSLSKIFPNLSVIRGNKLFDGYALVVYSNFDLMDLGLHKLRSITRGGVRIEKNHKLCYDRTIDWLEILAENETQLVVLTENGKEKECRLSKCPGEIRIEEGHDTTAIEGELNASCQLHNNRRLCWNSKLCQTKCPEKCRNNCIDEHTCCSQDCLGGCVIDKNGNESCISCRNVSFNNICMDSCPKGYYQFDSRCVTANECITLTKFETNSVYSGIPYNGQCITHCPTGYQKSENKRMCEPCPGGKCDKECSSGLIDSLERAREFHGCTIITGTEPLTISIKRESGAHVMDELKYGLAAVHKIQSSLMVHLTYGLKSLKFFQSLTEISGDPPMDADKYALYVLDNRDLDELWGPNQTVFIRKGGVFFHFNPKLCVSTINQLLPMLASKPKFFEKSDVGADSNGNRGSCGTAVLNVTLQSVGANSAMLNVTTKVEIGEPQKPSNATIVFKDPRAFIGFVFYHMIDPYGNSTKSSDDPCDDRWKVSSPEKSGVMVLSNLIPYTNYSYYVRTMAISSELTNAESDVKNFRTNPGRPSKVTEVVATAISDSKINVTWSYLDKPYGVLTRYFIKAKLINRPTRNNNRDYCTEPLVKAMENDLPATTPTKKISDPLAGDCKCVEGSKKTSSQEYDDRKVQAGMEFENALQNFIFVPNIRKSKNGSSDKSDGAEGAALDSNAIPNGGATNPSRRRRDVALEPELDDVEGSVLLRHVRSITDDTDAFFEKDDENTYKDEEDLSSNKQFYEVFAKELPPNQTHFVFEKLRHFTRYAIFVVACREEIPSEKLRDTSFKKSLCSDYDTVFQTTKRKKFADIVMDLKVDLEHANNTESPVRVRWTPPVDPNGEIVTYEVAYKLQKPDQVEEKKCIPAADFNQTAGYLIKLNEGLYSFRVRANSIAGYGDFTEVEHIKVEPPPSYAKVFFWLLGIGLAFLIVSLFGYVCYLHKRKVPSNDLHMNTEVNPFYASMQYIPDDWEVLRENIIQLAPLGQGSFGMVYEGILKSFPPNGVDRECAIKTVNENATDRERTNFLSEASVMKEFDTYHVVRLLGVCSRGQPALVVMELMKKGDLKSYLRAHRPEERDEAMMTYLNRIGVTGNVQPPTYGRIYQMAIEIADGMAYLAAKKFVHRDLAARNCMVADDLTVKIGDFGMTRDIYETDYYRKGTKGLLPVRWMPPESLRDGVYSSASDVFSFGVVLWEMATLAAQPYQGLSNEQVLRYVIDGGVMERPENCPDFLHKLMQRCWHHRSSARPSFLDIIAYLEPQCPNSQFKEVSFYHSEAGLQHREKERKERNQLDAFAAVPLDQDLQDREQQEDATTPLRMGDYQQNSSLDQPPESPIAMVDDQGSHLPFSLPSGFIASSTPDGQTVMATAFQNIPAAQGDISATYVVPDADALDGDRGYEIYDPSPKCAELPTSRSGSTGGGKLSGEQHLLPRKGRQPTIMSSSMPDDVIGGSSLQPSTASAGSSNASSHTGRPSLKKTVADSVRNKANFINRHLFNHKRTGSNASHKSNASNAPSTSSNTNLTSHPVAMGNLGTIESGGSGSAGSYTGTPRFYTPSATPGGGSGMAISDNPNYRLLDESIASEQATILTTSSPNPNYEMMHPPTSLVSTNPNYMPMNETPVQMAGVTISHNPNYQPMQAPLNARQSQSSSDEDNEQEEDDEDEDDDVDDEHVEHIKMERMPLSRPRQRALPSKTQPPRSRSVSQTRKSPTNPNSGIGATGAGNRSNLLKENWLRPASTPRPPPPNGFIGREA
The following text describes a protein:
Function:
May be involved in extracellular digestion.
Subcellular Localization:
Secreted.
Sequence:
MNKLLTLGMLSLLMIGASQYFDASEVSIQQRFELYTTKYQKFYGPSEKIYRAKIFEERIKLFEAHNADKTQTFTMGENQFTDLTQEEFKAIYLRRRSPQKLVNEKYVPTNEANLTSANWAGLTSVKDQGYCGAAWAFAAIGAVESVLRINSVTNLDLSEQQLIDCDLENQGCEDGNLNNSLNWAQNNGVTTSASYPYTGQTDGCKKPTGQFKFKGYQKVEPDQMQAAIIKSPIAATVDATTWLFYKSGVFNKCTFEELNHDALIIGFKDDGTWIVKNSWGQWWGEDGIIRLAPGNSCGIQEQSYIAYV
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular Localization:
Cytoplasm. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MRRTQVDCEDRGRAGYLVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSAVSGGSTAALITETIIETEKPKVAPAPSRPSGPSKALKLGAKGKEVDNFVDKLKSEGETVMSSAVGKRVSEAARVLAPPINTESVHMKIEEKITLTCGRDGGLQTMELHGMIMLRISDEKFGRIRLHVENEDKKGVQLQTHPNVDKKLFTADSLIGLKNPEKSFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEESLELNDVVITIPLPSGVGAPVIGEIDGEYRHDSRRNTLEWCLPVIDAKNKSGSLEFSIAGQPNDFFPVQVTFVSKKNYCNIQVTKVTQVEGNSPVRFSTETTFLVEKYEIL
The following text describes a protein:
Function:
May be a cell-type-specific regulator of pigment cell differentiation.
Subcellular Localization:
Nucleus.
Sequence:
MDSSRELSGEEPRSPSPRHETSKMRLSPDRPSHHPARPPASLASQPLRPAHYQDDDDSYRTHTPPPSQPRTKGFSIESILSPTDKHRKSPRSPPMSPSSPSMSSNGYSEGPIYGSTRHPLSATVPGLGRAALDELAAHRAAALHIPSAALPFSHLAHNPAFYAWMHGASFLHYHGMPAFNSHPPIAQPLTNSSRLAMAKDISPRPTQSHSSFGEEGGEKDSRGRESPDSEHRRNNGHEEDDDDDDDQSPQKKKKKTRTVFSRSQVFQLESTFEVKRYLSSSERAGLAANLHLTETQVKIWFQNRRNKWKRQMAAELESANLAHAAQIRAQANLAQVSAVHVHAYAQRMVRVPILYHENHPTTGSSLHSPNILPFPMPYPGSYHQISSSTSSTSSARSPTSTSIVT
The following text describes a protein:
Function:
Together with cefD2, catalyzes the reversible isomerization between isopenicillin N and penicillin N. This two-component IPN epimerase system may function by two sequential steps, an activation of isopenicillin N by the acyl-CoA synthase component cefD1, followed by epimerization by the acyl-CoA racemase component cefD2.
Sequence:
MAPGGLLTLAGAAAASTAAAAYLDAKLHLTKDLNQLARAERGAQNFARAVEQRKASGFFLFEAAAARLGDAPCIWSRGHPEYSWTQTYQRACQYGHYFRDLGVVAGQHVGVYLYNSPELMFIWMGLLSIGAAPALINYNLGSDALVHCVRLSRSRFLIYDDASDCSSRIHEVGERLRDINVEAIMLSGSGTTGLPKAAPITVARNYPSASLLPKTFGQKPGPNGDRTYYCIPLYHGTGGIAAMNDLMSGISIALAPKFSLSRFWDDCIESGSTIFVYVGELIRYLLSAPASPKDRQHRVRLVWGNGLSPELWTKFQDRFGVSDIGEFYASTEGVLTLLKHYRGGGFGLGAVGHHGWLLRRKFHNDYVPVRIDPETGDIWRSPKTGFAERLPYERGGEILARLPSRSAWAGYWHAEEATQKKLVENVFEKGDLYFRTGDALRRDADGHWYFLDRLGDTYRWKGENVSTTEVGQVLGSHADIAEANVYGVQVPNHDGRAGCAAIALKNAATPDTLDWSRLTSLLRSELPSYAVPVFIRVRETVGGMSTDNHKHNKVPLRDEGVDPRSMGSKVPGSEKDRFFWLPAGASKYVPFTERDWDLLSGQSAARPRL
The following text describes a protein:
Function:
Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. Mediates the traffic of PKD1:PKD2 complex from the endoplasmic reticulum through the Golgi to the cilium.
Miscellaneous:
MISCELLANEOUS: [Isoform 5]: May be due to an intron retention.
Subcellular Localization:
Cytoplasm. Early endosome. Recycling endosome. Cytoplasmic vesicle.
Sequence:
MAQPGPAPQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQWREEVASLQAIMKETVRDYEHQFHLRLEQERAQWAQYRESAEREIADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEEDEQQRVNKRKDNKKTDTEEEVKIPVVCALTQEESSTPLSNEEEHLDSTHGSVHSLDADLMLPSGDPFSKSDNDMFKDGLRRAQSTDSLGTSSSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTVSLGSLQMPSGFMLTKDQERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSETEWNLLQKEVHNAGNKLGRRCDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKEKQELEDFLKQSAEDSSHQISALVLRAQASEVLLEELQQSFSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQLAEDFILPDTVEVLRELVLKYRENIVHVRTAADHMEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEMKVNLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDINQLPET
The following text describes a protein:
Function:
Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Subcellular Localization:
Nucleus.
Sequence:
MDLVDQLMTEGMEGPSSPGPPSSPGANLPSSFAGRTPGTTSAHGGPSSDQYREPAAMDVPPDEEVRMRRIMEQETVPKVQDATGEKVRDLFEEFLETYVDGSNPEEYSDDEDGTAYDGRPYVRQIKGLRSFNKSSIFVDYRHMSETEDGILAQAISDQYYRFMPFLLRGLTNVIRKIEPVLLQQSVGFSEDGSSTFGGSKSSSASDQPRHFQICFHNLPVVCRIRELKTDKIGCLISLGGTVTRTSEVRPELYLGAFQCQECHTEVDGVEQVFKYTEPSICPNPMCGNKKMWKLLMDNSVFLDWQKVRVQENAHEIPAGSMPRTIDVILRGENVERARAGDQMIFTGAPVVIPDVTQLGLPGVKPRAVRDGGRETSAVESGAVTGLRELGARDLTYRISFLACYAAPANILDASANDNYAENAADEQEEYIRSLKSAEVEQLRDMVHGQDIFRRLVRSIAPAVYGHETVKKGILLQLMGGVHKKTADGIRLRGDINICLVGDPSTAKSQFLKYVTSFLPRSVYASGKASTAAGLTAAVVKDEDSGEFTIEAGALMLADNGICAIDEFDKMDLADQVAIHEAMEQQTISIAKAGINATLNARTSILAAANPAKGRYDRRLGLRANVQMSAPIMSRFDLFFVILDECNEATDTALASHVVDLHMHTDEAIDPPFSTEQLQRFIKYARTFKPMLTPEARAVLVQQYQQLRADDATGAGNSYRITVRQLESMIRLSEAIARANCSTIISPAFVHEAAKLLRDTIILVEREDVLLDEEEDTVDAAEDAVDEAMEATQLANHTPRDQITHQQYTHMVNMIVSKLSENYTDDADASRIGMSLDALLEFVLEQYEEDMVDEEDVENHTRLTKKVIKKMKKNNLLMTVRGNLDDLEAPGDGTELYVIHPNAAAAELEETRQTGGVMPDDE
The following text describes a protein:
Function:
Required for vacuolar protein sorting; may be required for the consumption of transport vesicles containing vacuolar protein precursors. Required for vacuolar fusion.
Domain:
The CUE domain (Coupling of ubiquitin conjugation to ER degradation) is monoubiquitin-binding and is required for intramolecular ubiquitination.
Sequence:
MDYPSFHEDPTKDESTVAEQRKGQSNEEKPLIDLNDSLDEQRNAYNEHCKNHDQQPSQQVRNMEDEANQYEQTDSSSDQEVMNEKQSLDKENRNDNIPHENNPGQQEINEPIFDFHMFLEQLRSSSAEPVAKYLKSFLSEFTKRRWTVNYQVKLIRDFLKFINEKIEQYEPWASGSQAEIDNAKEGMEKLVLNRLYTSLFSPEIAKSGIPLSSEHSDDVEEDRVLSEKMELFQWITEENLDIKKQKSSSKFFKLAADELRRINDYHAPRDKIICLLNCCKVIFSYLRNVVKEESADMFVPILIFVVLQARPAHLVSNIQYIQRFRSPEKLTGEVMYYLSTLMGAMSFIETLDCSSLTITEEEFNAQIEKSIKKMEERKLSEKSESKTAVNENATYKDPVLSRGLSSSIDVSTGVALVNLPEELENMKYLQIDTPESKEYPRSTRPRGSSHSGSFTTDSGKRSRRNSNKYVGSSDRPPYRVSRAYSSSATHSPIVHEEQPVDDGLQQNDDLREATTASLETAEAERLQAREKAEAITALRAMFPAFDSEVIEVVLNAQQGRLSSSIDSLLEMS
The following text describes a protein:
Function:
Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MVADRRDWTTVSFEEGREALKEWREEHARRSEEVVELWEHVLSRSPSSLADELCTVYEQVCIAALDCSRTDLAHECINALHKRFPGSSRVLRLQAMFYEARGQWKTADDIYEKLITADETNPAYRKRRVAMLLGQGKRLEGIKALVEHLESFITDSEAWLQLSELYLAESDYARAAHAMEEVLLTAPTNSIYLRRLADIRYTQGGQENVEVARAYYEQALKFSPVDLRALYGIVLSCNTLVATARVTPDKKREYMTAAAAALARIQERYESVEPEAANPEEHSNIMEAVRGMEIH
The following text describes a protein:
Function:
Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MIGVVLVLASLLSVGGQLCQKQATRPLTAGGRRRHLMLWLGLALICMGAAMVLWLLVLQTLPVGIAYPMLSLNFVWVTLAAWKIWHEQVPPRHWLGVALIISGIIILGSAA
The following text describes a protein:
Function:
This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA. Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA. Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA.
Sequence:
FANRSEIAVRIIRTLKKIGIKSVAVYSEADTNSMYVQHADEAYYIGDSPATESYLSIKNIISAIRESGASAVHPGYGFLSENPNFANILKREGVVLIGPSAGTIKKMGDKIEAKKIAIEAGVSTVPGYMGTINDVKQAVDIAKEIGFPVIVKAAAGGGGRGMRVVNNPTEMANAFESAKLEAANSFSDDRLFIEKLIQTPRHIEIQLIADQYGNSVCLGERECSIQRHHQKVIEEAPSSFITEDIRQEMYRQVISLSQKVGYYSAGTVEFIVDSNKNFYFLEMNTRLQVEHPVTELITGIDIVEEMIKIAAGEKLSFMQDDVKLKGWAFESRICAENPSRGFLPSSGRIIAYSEPAKSPNIRIDTGIGLGGEVSMFYDSMIAKLCTYGETREQAIEVMRSALSSYIINGIAHNISFLEAVMLHPRFVSGDISTAFIQEEYPDGFSGASLTSEVTTVFLATAIFIYISEQRRASLISGNINNQANKIGTRWVVTIDDKLFPVLITPVENGYNIRHESDRIYIRSNWNLGNELFTAIINGKKTNVKIENIRTGYLLSHAGISVKAFVRSPRISELEALMVSKVVVEESSELQAPLSGQIAAIKVKEGQEVTAGQEIMILTAMKMENLILAERDGKIAKIFVNEKDNVVRGQVLLEFA
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MLPLEKAFASPRSSPAPPDLPTPGSAAGVQQEEPETIPERTPADLEFSRLRFREFVYQEAAGPHQTLARLHELCRQWLMPEARSKEQMLELLVLEQFLGILPDKVRPWVVAQYPESCKKAASLVEGLADVLEEPGMLLGSPAGSSSILSDGVYERHMDPLLLPGELASPSQALGAGEIPAPSETPWLSPDPLFLEQRRVREAKTEEDGPANTEQKLKSFPEDPQHLGEWGHLDPAEENLKSYRKLLLWGYQLSQPDAASRLDTEELRLVERDPQGSSLPEGGRRQESAGCACEEAAPAGVLPELPTEAPPGDALADPPSGTTEEEEEQPGKAPDPQDPQDAESDSATGSQRQSVIQQPAPDRGTAKLGTKRPHPEDGDGQSLEGVSSSGDSAGLEAGQGPGADEPGLSRGKPYACGECGEAFAWLSHLMEHHSSHGGRKRYACQGCWKTFHFSLALAEHQKTHEKEKSYALGGARGPQPSTREAQAGARAGGPPESVEGEAPPAPPEAQR
The following text describes a protein:
Function:
Catalyzes the interconversion of ribulose-5-P and ribose-5-P. It probably also has activity on D-allose 6-phosphate.
Sequence:
MKKIAFGCDHVGFILKHEIVAHLVERGVEVIDKGTWSSERTDYPHYASQVALAVAGGEVDGGILICGTGVGISIAANKFAGIRAVVCSEPYSAQLSRQHNDTNVLAFGSRVVGLELAKMIVDAWLGAQYEGGRHQQRVEAITAIEQRRN
The following text describes a protein:
Function:
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MPPTAQPLEFDDTANAVLPVLYSSTDEEVGIWRELLASKKTNTNQGSTVIVLGDNRSGKSSLLSRLDKSDRTVKPKSLLGYRVLHVQNDARDASYAYQLGTAGANLNPSELLQIPVWSLDGNAACASLLKHALPATPAEAIFILTASIDNPNLIHSLKRWANVCTEQAQKHFTKEDLKAGRSQQEKMWQEYVDPVQSQMSTSVVGSFADEHNLLPLDQGTLTENCGVTFMVVITKSDLVLGKEFTDAQFAKISIQLRKFCLSLGATLVFTSAKETKNIQLLQKYIVHRSFGTAFTSAAQVIERESIFVPAGWDGEKKIDIIRESIPDVDSALEPTRDKLRPVAKEQLIEAEEDQAFLKKLMDILATSTTTAAPKPRTMQEEPTDKDSPLANFFSNLLNKDKPSKVSSPSTVSQPMDAAATQAQLDRLLKSAQSPKPQPRDSDA
The following text describes a protein:
Function:
Involved in brassinosteroid (BR) signaling.
Subcellular Localization:
Cytoplasm. Membrane; Peripheral membrane protein.
Sequence:
MEPPLYPGRFGSSPGSGVGFAGSSDASVMGTNDDATVSKASCTKMGYVKDDFVKYFIKRFTKRAPVINRGYYARWAAVRKLLHQFLTAAPSENPNVPVKKQVLSLGAGFDTTYFQLQAEGTAPAVYYEVDFLEVTSRKMAAIAHHLELCNILPKYAQVQKDKGEVRSSNYNLVAADLRNVSSLEEALKGAGFDPSVPTLILAECVLIYLEAKDSEALIRWAGDKIKTGVFVIYEQIRPDDAFGQQMIRNLEMRGCPLLGIEATPTPEAKKQRFLNAGWQRAEALDMDAIYTHHLAKADVQRIEKLEIFDEFEEWHIMQEHYCIALGVSDYHQTGMFDRFGFWPTPASPRTQRRSPGTPRTPVGD
The following text describes a protein:
Function:
Lectin involved in innate immunity. Agglutinates all types of human erythrocytes, Gram-positive and Gram-negative bacteria. Has a stronger agglutinating activity towards Gram-negative bacteria than towards Gram-positive bacteria. Specifically recognizes acetyl group-containing substances on agglutinated cells. The hemagglutinating activity was inhibited by EDTA, acetyl group-containing mono- and disaccharides, N-acetyl derivatives of amino acids, other acetyl group-containing substances, propionamide and benzamide. Enhances the antimicrobial activity of big defensin against Gram-positive bacteria but not against Gram-negative bacteria.
Subcellular Localization:
Secreted.
Sequence:
MGCLREQYLFNVFEAIISTLESKLQRIENLDKAVEHLMRRVEGLDNRVNNNIDKTESVIAKLSLLDSKLFNFDSKKPDGSNDGNVGRRLVALDQKVSDIDNKLNVLKSQLDNNLLQGEDINAEASEKKPVSMNVVEITKALNTEVINHVTKELGQLREATGSVDRKLQFHITLVSENLGKVLTMMTDIHHAIVDDITSHYNRTTTPAPEPKNNKIDALVQQIRPIISVSEKMDEVWDVVVGTKSSVDDLVPKSDELLTQTQRQERAIGEIHNDLRTKTNKIIANLDKVEKRLKKQEDDVATLAQRPVPAELLLDPTIDRLVEYDPSRYVDEYSTDTTLPATFTTLPPPTTATQASTLNQSSTTPVSSSTQATTEKRAEKRKSGLIFPSVKNKPSPANTTFATEVLANVKDVKGYSCVDLLNAGMRDSGVYYLQIRGTTYWFLKVYCEQEIADGGWTVIQRRDDFGDPRENFNRDWNDYKNGFGDPAKEFWLGNENIYMLTNNEEYILRVELEDFEGNKRFAQYSHFKIFSEGEYYKLEIDGYEGNAGDSLNDPWYGSNNSPFSTYNRDNDRSSLNCASMLKGGWWWKSCGRGLNGLYLNDPQDLTARQGIVWFRWRGWDYTLKKAMMMIKPKGPVTTT
The following text describes a protein:
Function:
Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Acts as an enzyme that recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue (By similarity). The HMCES DNA-protein cross-link is then either reversed or degraded. HMCES is able to catalyze the reversal of its thiazolidine cross-link and cycle between a cross-link and a non-cross-linked state depending on DNA context: mediates self-reversal of the thiazolidine cross-link in double stranded DNA, allowing APEX1 to initiate downstream repair of abasic sites. The HMCES DNA-protein cross-link can also be degraded by the SPRTN metalloprotease following unfolding by the BRIP1/FANCJ helicase (By similarity). Promotes error-free repair of abasic sites by protecting abasic sites from translesion synthesis (TLS) polymerases and endonucleases that are error-prone and would generate mutations and double-strand breaks (By similarity). Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity). The HMCES DNA-protein cross-link is then either reversed or degraded. According to a model, the HMCES DNA-protein cross-link (By similarity).
Subcellular Localization:
Chromosome. Note=Recruited to chromatin following DNA damage. Localizes to replication forks.
Domain:
The N-terminal catalytic Cys-2 residue forms a thiazolidine linkage to a ring-opened DNA abasic site. Glu-127 catalyzes reversal of the thiazolidine linkage; self-reversal is favoured by duplex DNA formation (By similarity). Glu-127 is also involved in sensing abasic sites in single-stranded DNA (ssDNA). His-202 stabilizes the abasic sites by forming a hydrogen bond with the O4' hydroxyl group (By similarity).
Sequence:
MCGRTACSLGAARLRRACAYRDRQGRRQQPEWLREGRYRPSYNKGPQSSGPVLLSRKHVQQDADSSERVLMDMRWGLVPSWFKEDDPSKMQFKTSNCRSDTMLSKSSYKGPLLKGKRCVVLADGFYEWQQRGGGKQPYFIYFPQNKKHPAEEEEDSDEEWRGWRLLTMAGIFDCWEPPKGGEPLYTYTIITVDASEDVSFIHHRMPAILDGDEAIEKWLDFAEVPTREAMKLIRPAENIAFHPVSTFVNSVRNDTPECLVPIELGVPKEVKATASSKAMLGWLKSSQEGSPQKKEDTLPRWKSQFIHSPSPKKSSAGILRQWLGQEGGPPAKKQKA