lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Cyclin subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. As part of the CTDK-I complex, involved in RNA polymerase II transcriptional elongation and pre-mRNA 3'-end processing. Together with ctk3, required for ctk1/lsk1 CTD kinase activation (By similarity). Together with ctk1/lsk1, required for the regulation of cytokinesis by phosphorylating 'Ser-2' residues found in the heptad repeats of the CTD.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Nuclear localization is dependent on ctk1/lsk1.
Sequence:
MAENENHVLSIRMSHPYYSEKEISRILSTRDPKENNLRMQAFAWISTLSKTLKFPVRTSGLAMLLYSRFQLFFPVNEIPLLECATACLVVASKIEDTAKKFRDILLAHYLQKHPGSEVDAHSQVCYKLIEENKKRILGLERMTLELICFDFRVRHPHNYMVKFAKSLKFSSSTASIAWNVCTDAYKTYTMLKYPAHIVAVASISIACKLQQLPQPIIPRSFFAPPALTEAVIADILDLYMHYQPHTCIGNMYTTEKLLGLCVDFQRAQKNSGRPQKPPQIDPHSSSLADEYRESNKRLQESKESCARFILDCDRKYFNTEFEKRMLEERRNKGTV
The following text describes a protein:
Function:
Required for the biosynthesis of the quorum-sensing signaling molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)-quinolone (Pseudomonas quinolone signal or PQS), which are important for biofilm formation and virulence. The PqsC/PqsB complex catalyzes the condensation of 2-aminobenzoylacetate (2-ABA) and octanoyl-CoA to form HHQ. PqsB, together with PqsC, catalyzes the coupling of 2-ABA with the octanoate group, leading to decarboxylation and dehydration, and resulting in closure of the quinoline ring. PqsB is probably required for the proper folding of PqsC rather than for a direct enzymatic role in the process.
Subcellular Localization:
Cytoplasm.
Sequence:
MLIQAVGVNLPPSYVCLEGPLGGERPRAQGDEMLMQRLLPAVREALDEAAVKPEEIDLIVGLALSPDHLIENRDIMAPKIGHPLQKVLGANRAHVFDLTDSSLARALYVVDTLASDQGYRNVLVVRGESSQGLEVDSESGFALADGALALLCRPTGKAAFRRGALGGDPAQEWLPLSIPLNTDIRQVGDVKGHLNLPAQPGLPEAVRAGFTRLAGDFPQLNWVREEWFGQGRPDGRCLGPFELASQLRAAQRDRLDELLLISFDPFGMVVEGVTLELAGEAHA
The following text describes a protein:
Function:
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Subcellular Localization:
Cytoplasm.
Sequence:
MAKVRVYELAKEFGVESKVVMAKLQELGEFVRSASSTIEAPVVRKLTDAFQQGGGNGRSAGRPAAPKKAAPRPSAPSPAQAGPSQAAPAAGDRAAAPRPSAAPKAPAAQQPAAPSAPAPAPSQGPRPTPGPKPAPRPAPAAPEFTAPPAAPAAPSTPAPAPSGPKPGGARPGAPKPGGARPSGPGQDRGQQGGQGRPGGQRPGAPAQRPGGRPGGPRPGNNPFTSGGNAGMARPSAPRPQGGPRPGGPGGAPGGGPRPQGPGGQGGGPRPQAPGGNRPSPGSMPRPQGGGAGPRPGGGPRPNPGMMPQRPAAGPRPGPGGGGRGPGGAGRPGGGGGRPGGGGFAGRPGGGGGGRPGGGGGFAGRPGGGGGFGGGGGRPGFGGRPGGPGGRGGTQGAFGRPGGPARRGRKSKRQRRQEYEAMQAPSVGGVMLPRGNGETIRLSRGASLTDFAEKINANPASLVAVMMNLGEMVTATQSVSDETLHLLAGEMNYTVQIVSPEEEDRELLESFDLEFGEDEGSEEDLVVRPPVVTVMGHVDHGKTRLLDAIRKTNVIAGEAGGITQHIGAYQVATEVNDEERKITFIDTPGHEAFTAMRARGARSTDIAILVVAANDGVMPQTVEALNHAKAAEVPIVVAVNKIDVEGADPTKVRGQLTEYGLVAEEYGGDTMFVDISAKQGLHIDSLLEAVVLTADASLDLRANPVQDAQGISIESRLDRGRGAVATVLVQRGTLRVGDTMVVGDAYGRVRAMLDDNGNNVAEAGPSTPVQVLGLTNVPGAGDNFIVVEEDRTARQIAEKRAARERNAAFAKRTRRVSLEDLDKVLKAGEVQQLNLIIKGDASGSVEALESSLLQLDVGEEVDIRVLHRGVGAVTESDIDLAMGSDAIVIGFNVRAAGRAAQMAEREGVDVRYYSVIYQAIEEIEAALKGMLKPEYEEVELGTAEIREVFRSSKLGNIAGVLIRSGEVKRNTKARLLRDGKVIAENLNIEGLRRFKDDVTEIREGFEGGINLGNFNDIKVDDVIATYEMREKPRV
The following text describes a protein:
Function:
May be involved in oxidative stress response.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MASSSLCHRYFNKITVTPFFNTKKLHHYSPRRISLRVNRRSFSISATMSSSTKKVLIPVAHGTEPFEAVVMIDVLRRGGADVTVASVENQVGVDACHGIKMVADTLLSDITDSVFDLIMLPGGLPGGETLKNCKPLEKMVKKQDTDGRLNAAICCAPALAFGTWGLLEGKKATCYPVFMEKLAACATAVESRVEIDGKIVTSRGPGTTMEFSVTLVEQLLGKEKAVEVSGPLVMRPNPGDEYTITELNQVSWSFEGTPQILVPIADGSEEMEAVAIIDVLKRAKANVVVAALGNSLEVVASRKVKLVADVLLDEAEKNSYDLIVLPGGLGGAEAFASSEKLVNMLKKQAESNKPYGAICASPALVFEPHGLLKGKKATAFPAMCSKLTDQSHIEHRVLVDGNLITSRGPGTSLEFALAIVEKFYGREKGLQLSKATLV
The following text describes a protein:
Function:
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular Localization:
Nucleus.
Sequence:
MDAISDPTFKHARSRKQVTEESPSLLTVIIEIAPKLWTTFDEEGNEKGSIIKVLEALIVFLNAHLAFNSANKVAVIAAYSQGIKYLYPESTSALKASESENKTRSDLKIINSDMYRRFRNVDETLVEEIYKLFELEKKQIEQNSQRSTLAGAMSAGLTYVNRISKESVTTSLKSRLLVLTCGSGSSKDEIFQYIPIMNCIFSATKMKCPIDVVKIGGSKESTFLQQTTDATNGVYLHVESTEGLIQYLATAMFIDPSLRPIIVKPNHGSVDFRTSCYLTGRVVAVGFICSVCLCVLSIIPPGNKCPACDSQFDEHVIAKLKRKPVVPRLKAKKKVTKP
The following text describes a protein:
Function:
Collagen VI acts as a cell-binding protein.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MRAARALLPLLLQAFWTAAQDEPETPRAVAFQDCPVDLFFVLDTSESVALRLKPYGALVDKVKSFTKRFIDNLRDRYYRCDRNLVWNAGALHYSDEVEIIQGLTRMPGGRDALKSSVDAVKYFGKGTYTDCAIKKGLEQLLVGGSHLKENKYLIVVTDGHPLEGYKEPCGGLEDAVNEAKHLGVKVFSVAITPDHLEPRLSIIATDHTYRRNFTAADWGQSRDAEEAISQTIDTIVDMIKNNVEQVCCSFECQPARGPPGLRGDPGFEGERGKPGLPGEKGEAGDPGRPGDLGPVGYQGMKGEKGSRGEKGSRGPKGYKGEKGKRGIDGVDGVKGEMGYPGLPGCKGSPGFDGIQGPPGPKGDPGAFGLKGEKGEPGADGEAGRPGSSGPPGDEGQPGEPGPPGEKGEAGDEGNPGPDGAPGERGGPGERGPRGTPGTRGPRGDPGEAGPQGDQGREGPVGVPGDPGEAGPIGPKGYRGDEGPPGSEGARGAPGPAGPPGDPGLMGERGEDGPAGNGTEGFPGFPGYPGNRGPPGINGTKGYPGLKGDEGEAGDPGDDNNDIAPRGVKGAKGYRGPEGPQGPPGHQGPPGPDECEILDIIMKMCCECKCGPIDLLFVLDSSESIGLQNFEIAKDFVVKVIDRLSRDELVKFEPGQSYAGVVQYSHSQMQEHVSLRSPSIRNVQELKEAIKSLQWMAGGTFTGEALQYTRDQLLPPSPNNRIALVITDGRSDTQRDTTPLNVLCSPGIQVVSVGIKDVFDFVPGSDQLNVISCQGLAPSQGRPGLSLVKENYAELLEDAFLKNVTAQICIDKKCPDYTCPITFSSPADITILLDGSASVGSHNFDTTKRFAKRLAERFLTAGRTDPAHDVRVAVVQYSGTGQQRPERASLQFLQNYTALASAVDAMDFINDATDVNDALGYVTRFYREASSGAAKKRLLLFSDGNSQGATPAAIEKAVQEAQRAGIEIFVVVVGRQVNEPHIRVLVTGKTAEYDVAYGERHLFRVPSYQALLRGVFHQTVSRKVALG
The following text describes a protein:
Function:
Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MAKPHVVFIHLDLGIGGAESLVLNLAKATLPPNFADQHDDDDGSPNEPSGSISIYTTHCSPSHCYDEVRPPNGPLSPFVNVRGSWIPRKLSLGGTALCSALRILYLTSCAMSENPDASVFVLDVLPTGVPYLVEYNNVMAGVLFYCHFPDKLLTRDTVNELYRWVLDTTEEWAMSFSDLIVVNSKFTMGQVEQTFPSLFLPRNDSNILYPAIESSISKEKKRNNRAKGKTDSTMKDSKARGPIVSLNRFERKKNVPLLLHAYDLLLEQSIKGKSDIHLPPLIIAGGYDPLNVENVEHLAELRVVADEILAPSITFYPSISNDQRTQLLSSASVWCYTPHREHFGIVPLEAMDAGVPVVAIRSGGPMETIVDGVTGRLVEYAVKGFADAIASILADPNNSKTMGRRGRERVDQVFGMDTFRKQWWELLNEAQKRGSERHFSRTFSY
The following text describes a protein:
Function:
Component of the SPOTS complex that acts as a negative regulator of sphingolipid synthesis. Acts by inhibiting serine palmitoyltransferases (LCB1 and LCB2) activity. Along with ORM2, plays a role in the phosphorylation of LAC1 and YPK1, the distribution of actin patches between mother and daughter cells, and in endocytosis. Disruption or inhibition of sphingolipid synthesis leads to the activation and phosphorylation of YPK1 through the TORC2 and PKH1 pathways, which in turn phosphorylates ORM1 and LAG1 to activate sphingolipid synthesis.
Miscellaneous:
MISCELLANEOUS: Present with 2800 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MTELDYQGTAEAASTSYSRNQTDLKPFPSAGSASSSIKTTEPVKDHRRRRSSSIISHVEPETFEDENDQQLLPNMNATWVDQRGAWIIHVVIIILLKLFYNLFPGVTTEWSWTLTNMTYVIGSYVMFHLIKGTPFDFNGGAYDNLTMWEQIDDETLYTPSRKFLISVPIALFLVSTHYAHYDLKLFSWNCFLTTFGAVVPKLPVTHRLRISIPGITGRAQIS
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Sequence:
MSSGASSSSSPPPAEAGDGYWVAREEAAARLEAMAARALEDELSAEQLETNNQLQEDEVLALQAIYGDDMVILEDKAGLRSFRFIFVQYPVPNDTKVLLNFRPNGTMVGTDNNYGSQDVGELFCACSLKHLPPLVSTCLLPRSYPSTCAPYFTISARWLDEPSVYLCAMFDEIWTELPGQEVVYRWVDWLNVSSWSCISLNDNILLVPDADVADERAIARKLLVDATIPLMQNYSEKRSQEIFLKSLHECGTCLSENTGFNFTKLPCHHSFCMKCMESHCRIHVKEGTLTMLTCPDTTCRSPLPSSILKSLLGDDCYMRWESFALQKLLDTMPDLVYCPRCDAACLEVDNDAQCPECFFTFCSLCKERCHVGKECLTPAKKISILREQHQKYSLPEKQLLKEQKEIDELLNVCCNHMTCRNCGKSFCYRCNQRVSGYNYFWSGNCELFEHNNQGRRFRLDEDPDDDDPEELEPELPWLCPCPICGCWNEKFDTNNHISCMGCRGHYCALCQKRVLKSSEHYGPRGCQQHTYP
The following text describes a protein:
Function:
Cargo receptor for the autophagic turnover of the iron-binding ferritin complex, playing a central role in iron homeostasis. Acts as an adapter for delivery of ferritin to lysosomes and autophagic degradation of ferritin, a process named ferritinophagy. Targets the iron-binding ferritin complex to autolysosomes following starvation or iron depletion (By similarity). Ensures efficient erythropoiesis, possibly by regulating hemin-induced erythroid differentiation. In some studies, has been shown to enhance the androgen receptor AR transcriptional activity as well as acting as ligand-independent coactivator of the peroxisome proliferator-activated receptor (PPAR) gamma (By similarity). Another study shows only weak behavior as a coactivator for the androgen receptor and no alteration of the ligand responsiveness of the AR (By similarity). Binds to DNA replication origins, binding is not restricted to sites of active transcription and may likely be independent from the nuclear receptor transcriptional coactivator function (By similarity). May inhibit activation of DNA replication origins, possibly by obstructing DNA unwinding via interaction with the MCM2-7 complex.
Subcellular Localization:
Cytoplasmic vesicle, autophagosome. Autolysosome. Nucleus. Chromosome.
Sequence:
MNTSLEQSGCYSNRETLLRCSDARRELELAIGGVLRAEQQIKDNLREVKAQIHSCISRHLECLRSREVWLNEQVDLIYQLKEETLQQQAQQLYWLMGQFNCLIHQLEYTQNKDLANQVSVCLERLGSLALKPEDSTVLLFEADTSALRQTITTFGSLKTIQIPEHLMAHASSSSIGPFLEKRGYIQVPEQKSASSGTAVSLSEWLLVSKPAIGLQAPYVPSTNPQDWLIPKQTSENSQTSARACSFFSDAWGNLKGLENWLLNSHQQEIAGKPSSSKCNSHCSTSSFSPEAEKAEDVELLDQDELDLSDWLVTPQEPCELEKPVDGSWETSEKFKLLFQVFREPYNVSDWLVKPDSCTNCQGNQPRGVEIENLGNLKCLNDHLEAKKSVSVPGATISDGWLAQNHQDTWKVEEVCKANEPCTSFAECVCDDNCEKEAMYKWLLKKGGKDKNGMPMEPKSEPEKHRESLTLWLCPSRNELTEQAKAPKAMAPARIADSFHVIKNSSLSEWLMGPTCKGGPKDVPNTEERAGKEMLQSSMATSWCPFNTADWVLPGKKVGSLSQFPSGEDKWLLRKKAQEAFLNSPLQEERNFRPDCYGLPAVCDLFACMQLKVDKEKWLYRTPLQM
The following text describes a protein:
Function:
Involved in the maintenance of the Golgi structure.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane.
Sequence:
MELDEDEDDEDSRRPLLEELDIDLPNIIYKIRCVLVPFGMDRSRLRNDPDFWGPLLVVILYAVFSLYGHLSVVSWIITIWMVGSILLFVLGRVLGGDTGFAQTLGVVGYSVLPLILTAALVTLLPLPETLHVMLKDDRHMEKPGGPGGRVHWLDLISTWHAWIGCVGLGDCNGREQDGVGCESVMGKEEGREPSGSGAEEAVWRLPETTDVKQVMPQVQAQAQAATKLQQHLNGQQKQYEHDLAFLSKLCKLEQQHAQAMADLCRNYERTAPSINAFWSMGSWSRSSEVAAEGRAGRSGSDAGRNSGGGGGGGGEAGSPAHSSERSHVTPVPGAAVDRPAMKTFVQELQSHATVQLEAMREWEAGCLEPLTAALGDMRQTPTAMQLVNKRLGALQKLLTKLEVETGLYRSKMIELQEDELLAASAYLPTSAEHAIIMSSQTPYQTEEGVGTLPDSVEDDLAEPDATPVVSAADSKVAATATATATQPAQPRRLPDTLTIPGATSSTTAPPLVPLTPPQRRRIAKIQSPAVQASTRERHLLTKTYQKLLGDYQQVHDEVWFGCGPTPHESASGLLKLSRPAETIVAAHFPLAPKRDQRGTQGHASLNLLRFNHNVIPPTQRQRDREREREPQTSEERRQRHVKRRASQLPPTSSIRHCVQQLTTISSHSPTQSWRQISSLTRRLSRGLPKTLFSEAATYSSTARSDALVLPATSPVVMNGSATQPLPARQTLTPPSSPRAKPKRSSTDMTIFDQFLPLLARDLDDDIERRASGDESGRNSAKTVTDDVEKLGAQGNDQTSAQNHAQPPASENEHNEPVADQSVLASPTSPTSPTSPTSPSVPTSPTSPTARPQSPGSRGSRSPLPDDKPLDDVLRPRFSLSHKSSMTTLEETDDEDVFEEEDEEEAAEAPPSPTQRCATDSDASTLTASPLHRPSLGPMLSLSQHASSSELQTAMDTSGASSGSMGVSSSSASPSADGRHLPKSPLNPARSRFRSSSPLRASQSAPRSGSVSEQSSSTSLRSEQSYISSATSATSRRRKPSQAQTEGEDFLEVTTVRALNFLSRAKGPQRQGLRYIRTVLRHHQKWITSDALLRGMVRIYCNDDQDEAIGADRDSVRLSVVTFCTWWAREANLAQATLRRIERFLEQLPTMADLTKPEAPNLHLERSDISIDSEALAKLLFSLDLEYYKRVTVDDLWSAEQPNATISAWRTFLNNVCSFAAASIVHHQDARTRAMFFSRWIHTCQHLVLQGDINMAHRLMSCFHSPILVRLTATRHHFSSDTTTALNNLAQLFFDSDDELYLQHLERAACDETLLCIPTLEHLVADLRAQREAAQSSQNPHKDLEGLIDVQTAIDDFLMFQVRSTAAHRQPSRLRTKLIHILSHAPSEDALMAASNMCEPSIVHSLRTYRVQGRDAMKRACCGSSKPELFARWLADGRRPLLFDQLSRQGLNMPSMECSRVELELRVQDLVTQLWSSLWTNRKAVSEEDWELCQQLVPLFPSFAVMASSADAVRPHDVAQVLYEVHLYGSHRCMPHLFDLSPAPASLLACDHCQQPIQSLCATCQDCERHAHAECSLFISRNCSVLFKAKPILAGAGRLQQAASSAASSVERRSASSTVRHDSMDSDGSAMSMDSSTPPAPMPSPLTMRSHGSGPRRMVSTIGGHRMLAQMEGQRLRDA
The following text describes a protein:
Function:
Does not show antimicrobial, myotoxic, hemolytic and cell-promoting activities.
Subcellular Localization:
Secreted.
Sequence:
FEMQYCWSHSGVCRDKSERNNKPMAWTYCENRQKKCEF
The following text describes a protein:
Function:
Functions as a two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction through the multistep His-to-Asp phosphorelay. Functions as a positive regulator of the cytokinin signaling pathway. May play a regulatory role in salt and drought tolerance during plant development.
Subcellular Localization:
Cytoplasm, cytosol. Nucleus.
Domain:
Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer.
Sequence:
MNSPMFELSNLMGFMFSAGLLDNAFNRLQQLQESSSNPGMVSELVKKFCEDGEQTIRELANLLNEQVVDYHQVTISAYNIKGRSSSFGARRVANASIELCEFCKEKNKLGCLMTLESIKNEFYDLRDKLHTMVQLEKRVEAYFPRK
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNEILKPLHVATDILGINVYKVTPKGLIYSKLKILRVVLYQTVWFISTCSFIKNYQFLNVARASAITLVVFTRVFLWGLNMMAILYLMLFRNGKMILIRQKLSEIDNKLEALGLKERLSNLAQRHKKTLTVLILIEIFALNLSSEIVTHILLERNDFFASFVVLQYSRLFSTTFLTYFLIQTLIVQKRFELINELFQKGNKTILWHLVSCHLKLQRLVKILNSMFDLQILITVTFYFAQTVLDLYTGITVALFETNKGIFVFIALKNALQNIIELFYLTRRCSELCIQANLAKKLVLDFEIDIQDEEKRNFIVASGLKLSNNKLEITALRMFSINYSLLHSLCSAVFTYICVMLQFDNKIPKVSIKS
The following text describes a protein:
Function:
Main component of the myelin sheath that plays an important role in myelin membrane biogenesis and myelination (By similarity). Plays an essential function in apical endocytosis. Plays an important role by activating the Notch signaling pathway, which is essential for cell differentiation and results in correct patterning of the intestinal epithelium, particularly of the posterior gut absorptive cells.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Myelin membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein. Vesicle. Note=In polarized cells, localized predominantly in the apical membrane. Located in lipid raft (By similarity). Recycled between the plasma membrane and the Golgi complex (By similarity). PLLP is continuously recirculating in the cell (By similarity).
Sequence:
MADFPGKVSTQTSSQEPQRSFAISSSVDMGFIKSIPGILLIAEIVVGLLVWTLIASTPHYLIPALGWVLFVSITLWLLSIALLVILLLSLHQRLPSVPWPLVLLVFYSVAALLYLTAFLANAATVPGGYYQGHLGASAFFGIVETLLYTASSYFAYLGWRGEGQNAAGSTVPV
The following text describes a protein:
Function:
Promotes cell fusion during zygote formation.
Subcellular Localization:
Cell tip. Note=Localizes at the mating projection tip (shmoo).
Sequence:
MFKTSYNLYDLNYPKNDSLTPIRDYKNDYFHKNDDKLPEIVRKPTRKLSKHENKLNDKKFTNKRPASLDLHSIVESLSNKKIYSPINTEIFQNVVRLNLSPQIPNSPHEGCKFYKIVQEFYLSEVEYYNNLLTANNVYRKALNSDPRFKNKLVKLDSSDELLLFGNIDTIASISKILVTAIKDLLLAKQRGKMLDANEWQKIFTKNEVQQQLYSTFDISEAFEQHLLRIKSTYTSYFVSHQKQMELFTTLRMNKNHFFNKWYEYCLKESGCIKLEDILKSPMKRLTQWIDTLETLESCYEDILSPELGLKLSPTRRKYSLFSNKLETEVSEYKSNSMYNFSLTPSEIIQSYDEDQFTHLLKPPDKQNKNICNASRQESNLDNSRVPSLLSGSSSYYSDVSGLEIVTNTSTASAEMINLKMDEETEFFTLADHISKFKKVMKGLLELKKNLLKNDLSGIIDISLRRINAWKKVIECERPSGAFFAHDNLISTMCSSYIDKLHEQKNQVTILKLTELETDVMNPLERIIAHCTTVKSKLKDLQALKKDYMLFLQEKKANVRDIKRDLLGMHFQNLQNQMKRELPVFITLIHDTIECILLNYIKVFLKYLEIIAGGKKYLQKDLENMSLNDSIATGQIKNLDILQCYSKSRYMTKRMVRKDWPFPGDPSGSRVVRKLFEL
The following text describes a protein:
Function:
Involved in regulation of actin and microtubule organization. Involved in cell adhesion.
Sequence:
MAHTNLPEKFQVVIENGENILQRVYNTYKLFQNNKVKPSFFNDEKISKILKNLIAKYPELPENNDKSITGFDLLTSRAKQHLEELEDHYYTITDAYDWKEASFILMQEISSNTVSINFNNNIQLCSKFLDVLVLYGKINYLVSLIPDKKIITAVYAKLFLYTRSASEPTFSKMGRWINDIEQPFKKIQEEFRVLNDAVGHALSSFELTYAKRRVITQLRKDGALNLILKPEDIARPVQDSYRIELAYAGRIQQWILFGYLFAPGTLSTPQSIELLRFTLSECFYLSVFKDISISIHNEFNTLFKNYKSKTINLQKQKKIIKDAAQASTQEAPRKHAERRVYIRQELEAMWNLFRDKPCLLAPKINVLLAALSMAKEEIFWYFRHTDVIPPEKVKKFYNKQNEVREKRISSLLSLVDHLVQLVHTHKKMIQNYYLEYISGADILGLQKVITPQLLQNAGSIVTQAVNTIVNELKSLNANGQDYSFEGFRANWMRLGYLLQSNSCPLKESESKQITSRLNLIYTHSKNVDCLDQLLDEYGNMTQLWSYKEPLFHSFDAAIVDMTCDQPSHSMIYLKLLSQFPNHVANQFYPEEKELIGKECVELANSCLTKITNRIVSIMANTIASTFLSDEQQLADVNAAFPLLQKKKDWKPPKDFVPPIEPASESQFRNRANLEQLRSEEKNAFQLCTALNEFLDITIYDHIFVPREFLREKLGSALKQYMRQSIQPPAPTSSSSQIDINITRLSTYESQLRVFIGVLILVENHVDIDIGDLIRETILTEFYAKALGKSGRVDWFPEGEIEMNELTLHSITSYYVDLVSKKLNTPGVVFSPVKLGFISKAGTPFRAEEHADLTEMRALCDLVGPYGIKVIEREILRFILTTTTSMKEILSLNAANLEEFASNYYKPKAMELLKKFKTTDLDLIVTKSIAIGNALHLRSMIRESMKDVITDNFPYINNAVANAFDQYNRNTFMFPDFLGVDTLALDSGLNVGIADQYLKVILRKVSSEADKRIWELLPVMFSLTFYGNIWKETQYKATIDAHSNNVHVLSKTIIDLLIAFGAINSTTGNEAELFQSFKRFLEISSVNILRMFKGKQGEKFVPNEIQSVIIFLDKFTQQCPLLSKDSLEQYIPYSLIRNMYKDLYEHKNLQKQQSETSEQNF
The following text describes a protein:
Function:
Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficient activity with xanthine.
Subcellular Localization:
Cytoplasm.
Sequence:
MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSEMVLVGLLRGSFMFMADLCREVQVPHEVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILGLREPKSLAICTLLDKPSRREVDVPVEFVGFSIPDEFVVGYGIDYAQRYRHLPYVGKVVLLDE
The following text describes a protein:
Function:
Proton-coupled monocarboxylate symporter. Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L-lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate. Dimerization is functionally required and both subunits work cooperatively in transporting substrate.
Subcellular Localization:
Basolateral cell membrane; Multi-pass membrane protein. Cytoplasm.
Sequence:
MPPTPSAPPVHPPPDGGWGWIVVAAAFISIGFSYAFPKAVTVFFKEIQQIFHTTYSEIAWISSIMLAVMYAGGPVSSVLVNKYGSRPVVIAGGLLCCLGMVLASFSSSVVQLYLTMGFITGLGLAFNLQPALTIIGKYFYRKRPMANGLAMAGSPVFLSSLAPFNQYLFNTFGWKGSFLILGSLLLNACVAGSLMRPLGPNQTTSKSKSKTGKTEDDSSPKKIKTKKSAWEKVNKYLDFSLFKHRGFLIYLSGNVIMFLGFFAPIIFLAPYAKDQGIDEYSAAFLLSVMAFVDMFARPSVGLIANSKYIRPRIQYFFSFAIMFNGVCHLLCPLAQDYTSLVLYAVFFGLGFGSVSSVLFETLMDLVGAPRFSSAVGLVTIVECGPVLLGPPLAGKLVDLTGEYKYMYMSCGAIVVAASVWLLIGNAINYRLLAKERKEENARQKTRESEPLSKSKYSEDVNIKVSNAQSVTSERETNI
The following text describes a protein:
Function:
Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
Subcellular Localization:
Endoplasmic reticulum membrane.
Sequence:
MASAMVTSLRLRPNFSAATSPSSSSSAGNVKYRPAVILPGLGNNTGDYKKLEVTLGEYGVPAVVAAVSRLDWFRNAAGLVDPAYWRGTLRPRPVLDWYLNRIDDAVREANELAQGQGLCLIGHSAGGWLARVYMEEYGNSDISLLLTLGTPHLPPPRGLPGVIDQTRGLLYYVEENCAKAVYTPELKYVCIAGRYIRGARLVDNADADIDSDVTVGIDSGEGISELAIASNKKSGTFRARFVGQGYKQVCGRADVWGDGVVPEVSAHLEGALNVSFDGVYHSPVGSDDETRPWYGSPVIVKDWIHHLLE
The following text describes a protein:
Function:
Involved in the restart of stalled replication forks, which reloads the DnaB replicative helicase on sites other than the origin of replication. Functions in the PriA-PriB and PriA-PriC restart pathways, but probably not in the PriC-Rep pathway. Displaces ssDNA from a PriB-ssDNA complex. Also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaC protein and other prepriming proteins DnaB, PriA, PriB and PriC a prepriming protein complex on the specific site of the template DNA recognized by PriA. Binds single-stranded (ss)DNA in a cooperative manner; both the N- and C-terminal domains are required for cooperativity. Forms a spiral filament on ssDNA.
Miscellaneous:
MISCELLANEOUS: There are about 50 molecules per cell. At this concentration it should exist in a 3:1 monomer:trimer state.
Domain:
The N-terminus (NT, residues 1-88) dissociates PriB from ssDNA, but a smaller region (residues 1-69) does not. The NT is also involved in trimerization. The C-terminus (CT, residues 99-154) is involved in ssDNA binding and forms a 3-helix bundle with a long flexible tail (residues 155-179). Both domains are required for cooperative ssDNA-binding. The CT is also involved in trimerization.
Sequence:
MSSRVLTPDVVGIDALVHDHQTVLAKAEGGVVAVFANNAPAFYAVTPARLAELLALEEKLARPGSDVALDDQLYQEPQAAPVAVPMGKFAMYPDWQPDADFIRLAALWGVALREPVTTEELASFIAYWQAEGKVFHHVQWQQKLARSLQIGRASNGGLPKRDVNTVSEPDSQIPPGFRG
The following text describes a protein:
Function:
Inhibitor of bone morphogenetic protein (BMP) function, it may regulate BMP responsiveness of osteoblasts and chondrocytes.
Subcellular Localization:
Secreted.
Sequence:
MLWFSGVGALAERYCRRSPGITCCVLLLLNCSGVPMSLASSFLTGSVAKCENEGEVLQIPFITDNPCIMCVCLNKEVTCKREKCPVLSRDCALAIKQRGACCEQCKGCTYEGNTYNSSFKWQSPAEPCVLRQCQEGVVTESGVRCVVHCKNPLEHLGMCCPTCPGCVFEGVQYQEGEEFQPEGSKCTKCSCTGGRTQCVREVCPILSCPQHLSHIPPGQCCPKCLGQRKVFDLPFGSCLFRSDVYDNGSSFLYDNCTACTCRDSTVVCKRKCSHPGGCDQGQEGCCEECLLRVPPEDIKVCKFGNKIFRDGEMWSSINCTICACVKGRTECRNKQCIPISSCPQGKILNRKGCCPICTEKPGVCTVFGDPHYNTFDGRTFNFQGTCQYVLTKDCSSPASPFQVLVKNDARRTRSFSWTKSVELVLGESRVSLQQHLTVRWNGSRIALPCRAPHFHIDLDGYLLKVTTKAGLEISWDGDSFVEVMAAPHLKGKLCGLCGNYNGHKRDDLIGGDGNFKFDVDDFAESWRVESNEFCNRPQRKPVPELCQGTVKVKLRAHQECQKLKSWEFQTCHSTVDYATFYRSCVTDMCECPVHKNCYCESFLAYTRACQREGIKVHWEPQQNCAATQCKHGAVYDTCGPGCIKTCDNWNEIGPCNKPCVAGCHCPANLVLHKGRCIKPVLCPQR
The following text describes a protein:
Function:
Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MEQVDLPNANKIAAGANKASVRVVNGLGALMGSKAMAAVDFEKDSMAEMLARDQREKEHYRHHKHISEQPWTLNNWHLHVNWVNIVLVVVVPIIGLYLALSGRVPPRFEVLALAIVYYSLGGLGITAGYHRLWAHRSYSARWPLRVMYALFGASSVEGSIKWWGHSHRIHHRYTDTPRDPYDARRGLWYSHMGWMLLQPNPRYRARADIEDLMNDWVVRLQHRHYVLIMAFMAFLLPAIICHFIFRDFWGGLVYAGILRVFAIQQATFCINSLAHYLGDQPFDDRRTPRDNWITALVTLGEGYHNFHHEFPTDYRNAIRWYQYDPTKVFIYCASLVGLAYDLKKFSQNAIQQGLIQQKQKKLDNARSRLNWGTPLSQLPVWDRSEFVRASRENSGLVVISGIVHDVSGYITEHPGGETLIQAALGKDATRAFNGGVYMHSNAAHNILATMRVAVVKEGQDAATRFAARRGEALEKKTA
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:
MEEKKAESTNKNAKKVNLLDHNSIKHMLDESVSDVSHILTLRFLHILRSVKYDHPFVLCVDRYEPWVQGGREAEQHEADLRDGYHRVLNGVMQLILFTKEKNAILFTYPLEIKSGNMALAALVSLVFAIGAVLFFDNGSFTSTGLVVSSKLPRFSDEYTLTIDSADPKSISAGKSVQFTKSVTQWFTKEGVLVEGLFWKDVEALIKDYANEEPKKQK
The following text describes a protein:
Function:
Cell wall formation.
Subcellular Localization:
Cytoplasm.
Sequence:
MSRSGARVERVPLARYTTLGVGGESEMWFVETHEQLAEAMSAPYRILGGGSNLVVSDSGVPERVLRLSGPLAERDLTPDPELSTPDLIVTGWVGGGVPLPGLIRALQKLGWSGLEGTVGIPGQVGGSVWMNAGTRFGEMFDGLHTIEIVTPDGVRQVTPDDLKWGYRQSGIPRGHVVSRVRLKLRPSTPEAVLAKMEHADQARKGQPKNKTPGCAFKNPGGVSAGKLIDEAGLKGTQVGNARIAPEHGNFIVNLGGATAADVHALLALIRERVGVPLELEYELWPEQLGG