lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Plays a role in the recruitment of the exosome to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Nucleus.
Sequence:
MPPLHRAQFFLILAKSATALFTLRLRCRGIHPDDHAVRSENERLRLFEEKLNRYNKINKAPVKPSTTINYQAATRFIEHSLPDLTSEQKTKMRDISKGTGITQNNHKKRKHRSQPENKSASVRAAEFLSKAAKEIVYPDNGGLKGPFAVLQCDSDEEGMQVE
The following text describes a protein:
Function:
Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.
Sequence:
LPKLTGIKPSCLRPNGHEFSVDVTCEGCSNVVSRVLNKPGGVEFDIDLPKKKVCINSEHSVDILLETLEKTGKAVSYLGPK
The following text describes a protein:
Function:
Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
Subcellular Localization:
Membrane. Microsome membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MEGYIFRNWAETFFCKPELYFEPQDTAELTQIVERARTEGKRVKVCGSRHSPSDIACTTGYMINMKHINKVLSVDVDKHQIRVEAGVLLEKLNTDILPRYGLALSLLGAISEQTIAGAISTGTHGTGYDHGIMATTIVSLELLTGSGEVLPCSDSENPDVFNAALCGLGALGIILTVTIQCEPAFRLHEIQTSTTLDDVLDNLDSNVESCEHFRFMWYPHTDMVMVSKVNRTEKRITERTSSWFWDKFVGYYALEFSFWVSEFVPSLVPWINRLYFLIFASLPKERVDIGHKVFNFDCLFKQHVTEWAIPRNKTGEVLRELRHHVDTGRFYAHLPTEVRFTKADDIMLSPASGRETCYINIIHFRPYGRTTWNKKYWAVYEDIVIRAGGRPHWAKEHPMRNKDLSELYPRWSKFCGLRKKLDPFGMFLNTYLERILSD
The following text describes a protein:
Function:
Functions as a component of both the DNA-binding general transcription initiation factor complex TFIID and the transcription coactivator SAGA complex. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription. At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module). SAGA preferentially acetylates histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and deubiquitinates histone H2B. SAGA interacts with DNA via upstream activating sequences (UASs).
Subcellular Localization:
Nucleus.
Domain:
The histone-fold domain (HFD) is required for interaction with taf9; The C-terminal HEAT domain is required for bulk transcriptional elongation.
Sequence:
MSLTVWNIESIKDVAEMLGIGNLADEPAAAIAMDLEYRIHQVVQEATKFMVHSKRTVLTSADISSALRTLNVEPLYGFNNSRPLEFHEAAVGAGQNSLYYLDDEEVDFEKIINAPLPKVPRNISYSAHWLAIEGVQPAIPQNPTPSDHTVGEWASKGTSGVMPGASTAAKEARNGVTSMDNVEIKPLVRHVLSKELQLYFERITSALLDETNVELRDAALSSLRDDPGLHQLLPYFIMFLSDSVTRNLGNLVVLTTLMHMAWALLDNPNLFVEPYVQQLMPSILTCLVAKRLGSDPNNHEHYALRDLAAFLLGIVCDRFGNVYYTLKPRVTRTALKAFLDNTKPYSTHYGAIKGLKTMGKEAIRVLVVPNIKVYEVLVRKTLEKGNEEEIYEANKCMDALYDALLLLRDDQLPNQRTLPPNASGLLEKNVGSLMAEKIMKENDTSLLLGLLE
The following text describes a protein:
Function:
Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the eighth mannose residue in an alpha-1,6 linkage onto Man(7)GlcNAc(2)-PP-dolichol to produce Man(8)GlcNAc(2)-PP-dolichol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MWPNPGSPREATNRRAPGQRPAGRGWGRGEAKGARPSRAPPGRQLYSGQGAPRRERGPGGHIRCGQRPLVPARLPPRCFRPSWGLRFEGRRGGRRGGALRARGGDPEAAGATAWVRGAGRSGPARRLSALSGSGAGAAGTGGASRLASSAASGPACSCRPRGASCGRPHRVGAGGRAWSWRTWGSRSNNLLRVCFLFLSTLPPLTAAWGTENRPMGAAADERGRRVRRESHGWEEAVGRGPAAPAAGAAGGCRRHPPHHLPLRQSGGELQPAGHARPALLPAGHGQVRAVLGLGVIFGLWTLQKEVRRQFGATVATMFCWVTATQFHLMFYCTRTLPNVLALPVVLPALAAWLQLRWARFIRLSAFAILVFRAELSVFLGLALLLLLGTRRLTVAKALRCALPAGALCLGLTVAVDSCFWRYLVWPEGKVLWYNTVLNKSSNWGTSPLLWYFYSALPRGLGCSLFFVPLGAVDRRALALLLLSLGFVALYSLLPHKELRFVIYTFPVLNIVAARGCACLLNNYRKSWLYKAGSVLVIGHLAVNAAYSATALYVSHFNYPGGVAMHKLHQLVAPGTDVALHIDVAAAQTGVSRFLEVNGAWRYDKREDVRPGSGHMLAYTHLLMEAAPAHLALYRDTHRVLASVPGTTGVSLNLSRLPPLDVNLQTRLVLLERRRGPS
The following text describes a protein:
Function:
Involved in autophagy. Thought to act as an adapter protein that brings PGL granules to autophagic structures containing lgg-1. Association with other adapters such as sepa-1 is required for the accumulation and degradation of germ cell specific P-granules by autophagy in somatic cells. This ensures exclusive localization of the P-granules in germ cells. May also play a role in the removal of sepa-1 from somatic cells.
Subcellular Localization:
Cytoplasm. Note=Co-localizes with sepa-1 in cytoplasmic aggregates.
Domain:
The LIR motifs (LC3-interacting region) are required for its interaction with lgg-1 and lgg-2.
Sequence:
MSANRTVTVFSSSAEDQEPIELAEDSLQNLDKMLAEEKEEHQLLKDEVVLLRKENVEAKTYSTLLEIMLDEAEEKASSAQETTSEENNLKILNRDLVAENLELKEMKEELRKIWLSDSKKFQEALTRISDENTKLQKDCHELESIRQCAQFALDNCNEELEKTQTENEEHESRIETLEREVCEKDIAMKDIVERKDEISLQLELQTKEFTSALNDLMYGREDTLKQIHQMKENWKVKQNEFEVEITKLKSQNDYFDSERLQLTDRIRALLNELSDVRLELGSTRLAMKEKAEVTEAVTSFNKDLRDKLEDEIARLGECLQFRKDEHEQDEAVIAHLEEQLKLGSDKAAAFSSEHSDTIELLRESETELMELRMENYDLKEDFKILKEEKEDVNRTCECLREQLSTTIQERDIEKGQMQSEMDAKMVAVHQQYAKQIDNMKYNHMLAINQELIKGQMALESGKKKHANEILTVRNELEQSNAAHQSLRDQCSLLLSSEDDLRTAHLALESKMTLVSEECIALRVSRANAQKEIGNLTEHHKLEVALLEDAKSGIQQRLHYATIEIEQLKKINEVTQAQFKKETDEKNAEINEFQAAMVSMKQQYNVLGNHCRVLTSQGISDRTTIDKLQETIREHTELAIETKRIHDAEIVQLNDAHKKLVDNLGVEELDEEPKASTESEEKAEWEMVDEE
The following text describes a protein:
Function:
Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.
Miscellaneous:
MISCELLANEOUS: This enzyme is monofunctional, and its activity is unaffected by the end-product aromatic amino acids.
Subcellular Localization:
Cytoplasm.
Sequence:
MMIRGIRGATTVERDTEEEILQKTKQLLEKIIEENHTKPEDVVQMLLSATPDLHAVFPAKAVRELSGWQYVPVTCMQEMDVTGGLKKCIRVMMTVQTDVPQDQIRHVYLEKVVVLRPDLSLTKNTEL
The following text describes a protein:
Function:
Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity.
Subcellular Localization:
Nucleus.
Sequence:
MDQYIRRLRQELVSMKEVGEGLQEQMNSMMGALQELKLLQVQSALEQLEIAGDQNTFCGIVQDHCCQNVKENHKFRLRSNQQAGNEMAGGTSLDNILASEQGYSPAGSLCTHSMPGTKQGHQVKSLQGSKIDVVCSSSILSSVDTGSTNEQAFITESVHRQHPMEVTNTLPDPEFCTHEHLADESQDWTSSLMSQSRNRQPLVLGDNVFADLVGNWLDLPELEKKGGESGSNLSISKSQEIYKKLSLTANFFKKVLRSVRPDREKLLKEKPGWLHAEDQVVDISKRTKKGSKQKGVFYFPSQPDMKIFNRRVEKHCKKEAKCSKSTQDIRTEQKHQEYPSTGFDMNTAVWV
The following text describes a protein:
Function:
Required for pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MGKIHQASEHKFLDERGTSSATLAPNGLNRARIMEKAVVDRITESYFWKEQCFGVNEADIVDRVVDHVTYIGGVVGQSQKPTPFLCLAFKLLQLGPDDSILAEYLKFGGEKFKYLRALAIFYVRLTRTSADVFRTLEPFLEDRRKLRRKGRAGTSLTYMDEFADDLLTKDRVCATSLFKLTRRDVLEDLDELEPRVSPLGDLEDLLEEEEEEEKRREAEENGNERERAGSRDRSSDDEGRITDDDDERGGRRSRDRDEVMADRDGSPGPSAG
The following text describes a protein:
Function:
May play an important role in hippocampus-dependent long-lasting memory.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MRQTLPLLLLTVLRPSWADPPQEKVPLFRVTQQGPWGSSGSNATDSPCEGLPAADATALTLANRNLERLPGCLPRTLRSLDASHNLLRALSTSELGHLEQLQVLTLRHNRIAALRWGPGGPAGLHTLDLSYNQLAALPPCTGPALSSLRALALAGNPLRALQPRAFACFPALQLLNLSCTALGRGAQGGIAEAAFAGEDGAPLVTLEVLDLSGTFLERVESGWIRDLPKLTSLYLRKMPRLTTLEGDIFKMTPNLQQLDCQDSPALASVATHIFQDTPHLQVLLFQNCNLSSFPPWTLDSSQVLSINLFGNPLTCSCDLSWLLTDAKRTVLSRAADTMCAPAAGSSGPFSASLSLSQLPGVCQSDQSTTLGASHPPCFNRSTYAQGTTVAPSAAPATRPAGDQQSVSKAPNVGSRTIAAWPHSDAREGTAPSTTNSVAGHSNSSVFPRAASTTRTQHRGEHAPELVLEPDISAASTPLASKLLGPFPTSWDRSISSPQPGQRTHATPQAPNPSLSEGEIPVLLLDDYSEEEEGRKEEVGTPHQDVPCDYHPCKHLQTPCAELQRRWRCRCPGLSGEDTIPDPPRLQGVTETTDTSALVHWCAPNSVVHGYQIRYSAEGWAGNQSVVGVIYATARQHPLYGLSPGTTYRVCVLAANRAGLSQPRSSGWRSPCAAFTTKPSFALLLSGLCAASGLLLASTVVLSACLCRRGQTLGLQRCDTHLVAYKNPAFDDYPLGLQTVS
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
MALVAVAGSSRSTNTALEEKVAGVAALIDKWRPDDGQCSLFLDGSRREAGRFLCAAVELHGAMLLVASDVDQERGDECLVRAQGVLEAAMRRLQLELELLLSTVRSNAVDGAISGHDVVGDAGVVGHITMVADAMMAAGYGMECVSTFNSHRRAEFAAAVRRLLGFAPSQHAHFHKLTWEDVDGKVQSWHTAAGFAFNFAFSRERVLCHRVFAADAALADKVFAGIASDHAADLLAVAEAAVMRARRAPERLFHVLDVHATLAEILPAIACILGDKSEAAARATAALRNAGNAARGILMSLEQAIQKTTSSKAAVTGSAVHPLTRYVMNYLVLLADYEDTLARIYQQGESTLTSGSGSASRVSPSSSADSIGRLVSVLQRKLEAMAVGYRPSALRSLFMANNTHYVSKKVRGSSKLEGIVGEDWIEEQMAETRRHVDAFVHSAWRDVLVAGGEGADAAVKEAVATQRSWVVADDEMGDAVRAAAAAVVVPAYRALYRRHGTAAWMTPGDVNAMISRQFGGLRNEAAGARPVSAGSATSRRHRLRLTSFSDKLAHVQ
The following text describes a protein:
Function:
Probable receptor. Interaction with a ligand in the extracellular domain triggers the protein kinase activity of the cytoplasmic domain.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MPRPLAALLSTACILSFFIALFPRAASSRDILPLGSSLVVESYESSTLQSSDGTFSSGFYEVYTHAFTFSVWYSKTEAAAANNKTIVWSANPDRPVHARRSALTLQKDGNMVLTDYDGAAVWRADGNNFTGVQRARLLDTGNLVIEDSGGNTVWQSFDSPTDTFLPTQLITAATRLVPTTQSRSPGNYIFRFSDLSVLSLIYHVPQVSDIYWPDPDQNLYQDGRNQYNSTRLGMLTDSGVLASSDFADGQALVASDVGPGVKRRLTLDPDGNLRLYSMNDSDGSWSVSMVAMTQPCNIHGLCGPNGICHYSPTPTCSCPPGYATRNPGNWTEGCMAIVNTTCDRYDKRSMRFVRLPNTDFWGSDQQHLLSVSLRTCRDICISDCTCKGFQYQEGTGSCYPKAYLFSGRTYPTSDVRTIYLKLPTGVSVSNALIPRSDVFDSVPRRLDCDRMNKSIREPFPDVHKTGGGESKWFYFYGFIAAFFVVEVSFISFAWFFVLKRELRPSELWASEKGYKAMTSNFRRYSYRELVKATRKFKVELGRGESGTVYKGVLEDDRHVAVKKLENVRQGKEVFQAELSVIGRINHMNLVRIWGFCSEGSHRLLVSEYVENGSLANILFSEGGNILLDWEGRFNIALGVAKGLAYLHHECLEWVIHCDVKPENILLDQAFEPKITDFGLVKLLNRGGSTQNVSHVRGTLGYIAPEWVSSLPITAKVDVYSYGVVLLELLTGTRVSELVGGTDEVHSMLRKLVRMLSAKLEGEEQSWIDGYLDSKLNRPVNYVQARTLIKLAVSCLEEDRSKRPTMEHAVQTLLSADD
The following text describes a protein:
Function:
Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1; Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Sequence:
MAAAAIRKPVIPKDDSDDDKELQVELKGLVDRITGDESKLVNVSLDMLKYLIRTSTSSMTSVPKPLKYLAPFYGALRNKCDSMKDPLLKKNLSDVVSVLSMGAIDGSVKRDFDCLKYCLQGTMENIGDWGHEYIRQLEIEIVKQWVMCENNYKTLSPLVKQIMRFNCSHHDEIQGCDLLMEINQMYMLFDYVTRENYKPICLYLASCAKYVDDLESKKILKLISQFYYLFQEHCRCLVVAIQIKDSALIEKLFNTCTDKITLYQMAFICARHLYPIEFNLDDDDVRSILENSHLSHYFLSFARELDIMEPKSPEEVYKTWLEPVTLRQSVLGEKLDSARQNLASSFVNGFVNAGFGTDKLLTTDDGNKWIYRNKDVGMLSATAALGLLYLWDVDGGLTPIDKYLYTSDDNIKAGALLALGIVNCRIRNDCDPALALLGDYVGSGSEELQVGAVLGIGLAYAGSGRSDVLNLLLPVIQSSKLVKTLGVASLACGLISLGRNNNELSDIILTKMIESNGLDVLKSPFMLLAGLGVALAYFGTKDAIEVPTIVADVFEEPFRTIFQTMLQMCAYAGSGDVLIIQELLRLVEEKVEVPETTETKGSKDKKKNEWDYHMGKAIAVLAVAAISKGEELGTEMIQRIFGQISRYGEPSVRKAVPLAIALTSVSDPQPTIINVLTKYSHDIDDDVACNAIFGLGYVGAGTNNARLAVTLRQLALYHAKNPFQLFMVRIAQGLVHMGKGTMTLNPLHTDRQLLDPVAMAGILIPLVCLLKPHSLILGRCHYLLYSLAAAMQPRWLLTLDDNLNSVSVTVRVGQAVDTVGKAGDPKTIAGIHTHTTPVLLCANERAEFANGEYESTAPALDGICVLKKLD
The following text describes a protein:
Function:
Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MGFSLGFIYLFSYNLLQFCGHTWIFANMTARFLSFGKDAQFGTFYFVAVMMGACQLLSLLELFHIADGFDECRLFPRFMQVIERNVLLFLLISLEEFQSKPIVCVQFYLWNILGLLRYPHRLFCLIGTPYFKMLWVHQTLTIPVYLMSAVTEGISIFLMLPYLSESEGTDSVQPKVPAPMYMYSPYIVMSWILLLVLGSSLTVLLLLKERKENLESWNKKLN
The following text describes a protein:
Function:
Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents (By similarity). During homologous recombination (HR) repair of DNA double-strand breaks (DSBs) regulates the extent of repair synthesis. Possibly recruits the DNA polymerase zeta complex or another translesion polymerase to early DSB repair intermediates to initiate repair synthesis, while also blocking the access of more processive polymerases preventing them from acting during the initial stages of HR repair.
Subcellular Localization:
Nucleus.
Sequence:
MTRDEDNGFSEWGGYFEAKKSKLEEQFAAASDPFRKSDLFQGISIFVNGRTDPSADELKRIMMVHGGTFHHYERSHTTYIIASVLPDVKVRNMNLSKFISAKWVVDCLEKKKIVDYKPYLLYTNQKTSQPMLIFGKPKDNGANESKSDVEPPKDKAEVEVDSTKDETQMELGGILKNLQQAVATSPEKEASASESKITNLSTTSNNSTTARTAADPNFLSEFYKNSRLHHIATLGAGFKQYVCRLRQKHGTQGFPKRETLKSLANSHHNCLERYVMHIDMDCFFVSVGLRTRPELRGLPIAVTHSKGGNAATDVPVHPQADRKAELELFAQRFEHHFHDGDKAEKVRSGFDKKMSLSEIASCSYEAREKGIRNGMFVGQALKLCPELKTIPYDFEGYKEVAFTLYDTVAQYTLNIEAVSCDEMFVELTDLAHELNVDVMAFVSHLRQEVYSKTGCPCSAGVAGNKLLARMATKEAKPNGQFLLDSSNDILAYMAPMSLDLLPGVGSSISHKLKQAGLNNCGDVQNTTLEKMEKVLGKKLGQNLFQNCRGIDDRPLAYEQIRKTVSAEMNFGIRFTNSVECEQFLCQLSEEVTKRLVEIRRKARSINLKIMVRAAEAPVETSKYMGHGVCDIINKSSLIKYATDDVNVITTVVLDLMKDADIPPDELRGLGIHLTRLEDANEVRKENNIKEMFGKMSEMRKDKPIPQGAVGDKSIGDDKVNKPLVFENKPKPREPRNVLSMLTAAAVSRKSVTEDRSQRGTSKPITRPLSLVPKLDEDVLAQLPEDIRLEVIANREEHLCIAEYDGYRSPQYPTLRSPPLLNPYVTTNVSPLKATDLKPSTSRAAVARLQKRKERKEQEHYIRSDQIVADYIDDLPDFVNPHILKLISHPVEMPELLMGDNYKDLLNDWVSREEVPKPNDVDLILKQVSRMIKNDQLDHVCDVMKYWCRIINMKRSSSCCWHVAYKHIEESIQNQMLTIEGYSLLFIEYIRCIKCS
The following text describes a protein:
Function:
Exhibits glutathione-dependent thiol transferase activity (By similarity). Has dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid (By similarity). Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) (By similarity). Protects against environmental stress and oxidative stress.
Subcellular Localization:
Cytoplasm.
Sequence:
MVLTGVTSKAIRKGDAEPPLSKGSFRVYNMRFCPWAERAMLYVAAKGIEAEVVNLNVTDKLEWYWTKHYQGKAPAVEHNGKVVIESGFIPEYLDDAFPETRILPTDPYEKVQQKLLADRLTAVAHAVPLLFAVMRDRTLKDEKQRKVFEVLKQAENLLANDFYAGSQPGYPDYLSFPFFEKIWWSASLDGVVDLPTIEFPGEEEYPKLTKWFQKMISSDVVQSVTQSLEHGAAFMNAYATHQELNYDLGL
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. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAGVALKREGPQFISEAAVRGNAAVLDYCRTSVSALSGATAGILGLTSLYGFIFYFLASFLLSLLLVLKSGRKWNKYFKSRKPLFTGGLVGGLFTYVLFWTFLYGMVHVY
The following text describes a protein:
Function:
ATP-dependent kinase that could be involved in endoplasmic reticulum membrane assembly.
Miscellaneous:
MISCELLANEOUS: Present with 161 molecules/cell in log phase SD medium.
Sequence:
MVDTHKLADDVLQLLDNRIEDNYRVCVILVGSPGSGKSTIAEELCQIINEKYHTFLSEHPNVIEVNDRLKPMVNLVDSLKTLQPNKVAEMIENQGLFKDHVEDVNFQPVKYSALTSNNEECTAVVARGGTANAIRIAAVDNPVNVNKLAQDSINIAQIVPMDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSLCKVSSHHKFYSTSSVFEKLSKTFSQTIPDIFVPGFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAKRHLQSGLVTTIAEGREKFRSNDLLNGRDIDNHLIKVDNIVHIRND
The following text describes a protein:
Function:
Component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation (By similarity). Controls the production of several secondary metabolites, including monodictyphenone, emodin and emodin derivatives, as well as two anti-osteoporosis polyketides, F9775A and F9775B.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MASTHAAGSPAPSSSINSPILHPVNASVSNASLGEGSIRFSPAPPSTFSNQGDGVRSKRNKRDSRKKREAKGLDQESAPPKKKSVAVLNTAIPSSDLGILRPIAVGEPRHSDLFPPQPRQLNFAVRKMSGVIGQSWDFYEVVDKLTNKNGFRYSYAIADTDFPHIKYRQTDVPPYHARFSFEDSPAAILFSKDALAVTTNEPWHTARANVCAREGTYYYEARIISGIMSSSEATTSNGSNALPSRGHVRLGFARREADLDVNVGVDCYGYGIRDVNGEVVNRMRCEYFFPKGESIREGDVIGMLITLPPLSLHRKIVEGTYDPACDNFKPGPASATNIIRDRIPFHYKNDFCWQQSNVFPTKQLRDYAFNLKETPAFGPPSPLNAEDPSLRTLPGSSITIYKNGIKMGTPFKELYAFLPPASRLANGTNNLGLGERENADDGMIGYYPAVSCYGGGAVECRFQGPWWFSPPSATENGEPVKGIGERFDEQIVEDVLADIVDEVEAMLVWGSVDGNVVNNAEMDAPGVGAVGGTDVLKGGVGAAYDPATTLSTAPAESNGSGTASIKLADEDACHTGFEDTMSLGVANTPITDVPVPPEPEDTPMTGG
The following text describes a protein:
Function:
Mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries. Anchors LPL on the surface of endothelial cells in the lumen of blood capillaries. Thereby, plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis. Binds chylomicrons and phospholipid particles that contain APOA5. Binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL.
Subcellular Localization:
Apical cell membrane; Lipid-anchor, GPI-anchor. Basolateral cell membrane; Lipid-anchor, GPI-anchor. Cell membrane; Lipid-anchor, GPI-anchor.
Domain:
The N-terminal acidic region is intrinsically disordered (By similarity). This region contributes to LPL binding. It stabilizes LPL and protects LPL against loss of activity (By similarity).
Sequence:
MKALRAVLLILLLSGQPGSGWAQEDGDADPEPENYNYDDDDDEEEEEETNMIPGSRDRAPLQCYFCQVLHSGESCNQTQSCSSSKPFCITLVSHSGTDKGYLTTYSMWCTDTCQPIIKTVGGTQMTQTCCQSTLCNIPPWQNPQVQNPLGGRADSPLESGTRHPQGGKFSHPQVVKAAHPQSDGANLPKSGKANQPQGSGAGYPSGWTKFGNIALLLSFFTCLWASGA
The following text describes a protein:
Function:
Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. It is therefore an amino acid-dependent activator within the amino acid-sensing branch of the TORC1 pathway, indirectly regulating different cellular processes including cell growth and autophagy.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytosol. Lysosome. Nucleus.
Sequence:
MAEEQEFAQLCKLPTQPSHSHCVSNTYRSAQHSQALLRGLLALRDSGILFDVVLVVEGRHIEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIHGVSYNAMCQILHFIYTSELELSLSNVQETLVAACQLQIPEIIHFCCDFLTPWVDEDNILDVYRLAELFDLSRLTEQLDAYILKNFVAFSRTDKYRQLPLEKVYALLSSNRLEVSCETEVYEGALLYHYSLEQVQADRLPLHEPPKLLETVRFPLMEAEVLQRLHDKLDPSPLRDTVADALMYHRNESLQPSLQGPRTELRSDFQCVVGFGGIHSTPSTVLSDQAKYLNPLLGEWKHFTASLAPRMSNQGIAVLNNFVYLIGGDNNVQGFRAESRCWRYDPRHNRWFQIQSLQQEHADLCVCVVGKYIYAVAGRDYHNDLSAVERYDPATNSWAYVAPLKREVYAHAGATLQGKMYITCGRRGEDYLKETHCYDPGSDTWRPLADGPVRRAWHGMATLLDKLYVVGGSNNDAGYRRDVHQVACYSCTTGQWSSVCPLPAGHGEPGIAVLDNRIYVLGGRSHNRGSRTGYVHIYDVEKDCWEEGPQLDNSISGLAACVLTLPRSLLLEPPRGTPDRSQADPDFASEVMSVSDWEEFDNSSED
The following text describes a protein:
Function:
Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance.
Subcellular Localization:
Mitochondrion.
Sequence:
MHEILSFAFGGKSNFVSTHFWNAQEKYLDQGNDAQIDREVAFFERKTNNIGGDVVFHPRTLIYDDRDAFGTTIKNSKLLQPDIVENNNNIDIFGYAKNDNRKTGEGPEDVNTWSGKTVCVEAPPLPLHPYQAWLDQETDPAQANNGITNKADIDLNACTSWSDFHRLYYDPRSLQPLKLPTGFADCSTNSFITGQDAFQQKNADSDEHYVWDTAIRPLLEDCDMIQGFQLSLDVCSAWSGYASSYIRGIQDELEDERIPLWIFGIREQRTVMQETKQHFMNEALFMASTADAYSKYVPICVDTTAQSIWHTSAFASVALETFTLPTRLTREKRVQMSDIERVVSLTRSSKLFGMDAIVLGTKKASIIQRWDVSWGSGTALPNTLAPVYQCFRGTNMEEVNSLLAPKSMPSGPSLQLDKPAFPADVNTLPEELKKVHGVAVSTSGGPIGYDSDTEETFNSNSNSFLEKDHRGAIASVV
The following text describes a protein:
Function:
Catalyzes the decarboxylation of mevalonate 5-diphosphate (MVAPP) to isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to IPP, a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
Sequence:
MLKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDDQLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFKKIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNELLELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDGEDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRSAETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRHSNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFDAGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKVLSRE
The following text describes a protein:
Function:
Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MKLHHRMLRHFIAASVIVLTSSFLIFELVASDRAMSAYLRYIVQKADSSFLYDKYQNQSIAAHVMRALAAEQSEVSPEQRRAICEAFESANNTHGLNLTAHKYPGLRGTLQTASTDCDTIVEAAALLPAFDQAVEGNRHQDDYGSGLGMAEEKFHYYLDLNDRYVYFYEPVNVEYFAMNNWSFLQSGSIGIDRKDIEKVFTGRTVLSSIYQDQRTKQNVMSLLTPVYVAGQLKGIVLLDINKNNLRNIFYTHDRPLLWRFLNVTLTDTDSGRDIIINQSEDNLFQYVSYVHDLPGGIRVSLSIDILYFITSSWKSVLFWILTALILLNMVRMHFRLYQNVSRENISDAMTGLYNRKILTPELEQRLQKLVQSGSSVMFIAIDMDKLKQINDTLGHQEGDLAITLLAQAIKQSIRKSDYAIRLGGDEFCIILVDSTPQIAAQLPERIEKRLQHIAPQKEIGFSSGIYAMKENDTLHDAYKASDERLYVNKQNKNSRS
The following text describes a protein:
Function:
An odorant receptor which affects chemotaxis to the volatile odorant diacetyl. Specifies AWA neuronal cell fate via the odr-7 pathway.
Subcellular Localization:
Cell projection, cilium membrane; Multi-pass membrane protein.
Sequence:
MLTVSNWKTFIELIQFGGGAIGVFLNFSLILLTYFRSPPHLGAYKYLMYYISGFEILYAILNAIVQGHLFSHGPAFIFFRNLKHSYFGRAKGFYLLVAYCGSFGLSIALFGVHFIYRYGAVDNVFRKKFLGGKKLLMLFLLPIFYCVWWCLVVIICYRSSSKSDDFMRIPFLENYDTRVEEISYVMIWFHIANDEGILEPRWPTFIGIANLWFMVTSSFVCVIFFGIKCYRKITKALKHSKMSSYYARSIQKQLFQALVLQTLVPVVLMYGPVGILYMFPMLNIEVGFISTFVTATVEVYPAVDPLPTMFIVDNFRKTILCKNKRKIEDLVKSGDQSQNSLSKSFRWLPEPKQEGGSSRIAESGQSCFLLLATCISVIPTVTS