lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. In vitro, the amidase active site also catalyzes hydrolysis of amide and ester derivatives of glutathione (e.g. glutathione ethyl ester and glutathione amide) but lacks activity toward acetylspermidine (N1 and N8) and acetylspermine (N1).
Miscellaneous:
MISCELLANEOUS: Gsp forms mixed disulfides with the thiols of a variety of E.coli proteins. These mixed disulfides represent a previously uncharacterized type of post-translational modification. The level of these proteins is increased by oxidative stress, which implies that Gsp might protect protein thiols against irreversible oxidation; MISCELLANEOUS: No metal ion is required for the amidase activity; MISCELLANEOUS: Gsp hydrolysis to GSH and spermidine proceeds with formation of a glutathionyl acyl-enzyme intermediate, utilizing a cysteine residue as the catalytic nucleophile. For Gsp synthesis, GSH is likely phosphorylated at one of two GSH-binding sites to form an acylphosphate intermediate that then translocates to the other site for subsequent nucleophilic addition of spermidine.
Domain:
The two activities reside in distinct domains (N-terminal amidase and C-terminal synthetase). The two domains expressed independently are folded and functional; liberation of the amidase domain from the synthetase domain highly activates the amidase activity.
Sequence:
MSKGTTSQDAPFGTLLGYAPGGVAIYSSDYSSLDPQEYEDDAVFRSYIDDEYMGHKWQCVEFARRFLFLNYGVVFTDVGMAWEIFSLRFLREVVNDNILPLQAFPNGSPRAPVAGALLIWDKGGEFKDTGHVAIITQLHGNKVRIAEQNVIHSPLPQGQQWTRELEMVVENGCYTLKDTFDDTTILGWMIQTEDTEYSLPQPEIAGELLKISGARLENKGQFDGKWLDEKDPLQNAYVQANGQVINQDPYHYYTITESAEQELIKATNELHLMYLHATDKVLKDDNLLALFDIPKILWPRLRLSWQRRRHHMITGRMDFCMDERGLKVYEYNADSASCHTEAGLILERWAEQGYKGNGFNPAEGLINELAGAWKHSRARPFVHIMQDKDIEENYHAQFMEQALHQAGFETRILRGLDELGWDAAGQLIDGEGRLVNCVWKTWAWETAFDQIREVSDREFAAVPIRTGHPQNEVRLIDVLLRPEVLVFEPLWTVIPGNKAILPILWSLFPHHRYLLDTDFTVNDELVKTGYAVKPIAGRCGSNIDLVSHHEEVLDKTSGKFAEQKNIYQQLWCLPKVDGKYIQVCTFTVGGNYGGTCLRGDESLVIKKESDIEPLIVVKK
The following text describes a protein:
Function:
tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
Sequence:
MGVRCKFWLLKKKRFCAIPPLPNTEFCGNHSTRSDDRWIQCSIDPSHSVLESNLENHLRRCPLLKHNNSLSLQPFYQKGINGGDEEDEDVSSESKRMAVQCITVPELIKLIEKIKSVHASICKDIQDSYNIPEVCRNWINRANDWKIPFQEKHVIQQASILGNLEKLGAIKSCSSVGEQLHSPAVVEFGAGRGYLTQMLADCYGVSKVFLIERKSYKLKADRSLRQKESLMLERLRIDIEDLNLNAIGSLQGVPYLAIGKHLCGPATDMTLRCCVGENGSTSYLRGLSIATCCHHLCQWKHYINKSFFLSQGMSKDEFHAVTWFTSWAVDSADHEESDTKMYRENEKVLEGDDDDDDLLRNMCARDRAVLGFMCKDIIDAGRLMWIREHGLEKSELVKYVPSNISPENRLLIASC
The following text describes a protein:
Function:
D-mannose/D-glucose-binding lectin which binds alpha-methyl-D-mannoside, D-mannose and D-glucose in that order. Also binds to serum fetuin and ovalbumin. Has hemagglutinating activity towards rabbit erythrocytes. Is not toxic towards larvae of the brine shrimp Artemia. Induces relaxation in rat endothelized aorta. Shows a transient edematogenic effect in rat.
Miscellaneous:
MISCELLANEOUS: Binds one manganese (or another transition metal) ion and one calcium ion. The metal ions are essential for the saccharide-binding and cell-agglutinating activities.
Sequence:
ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFVFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
The following text describes a protein:
Function:
Through its association with the EHMT1-EHMT2/G9A and PRC2/EED-EZH2 histone methyltransferase complexes may function in gene silencing, regulating repressive post-translational methylation of histone tails at promoters of target genes.
Subcellular Localization:
Nucleus.
Sequence:
CYQFRQSPQDGVKISGKILRFSCSECKGEAAFSPNDLLKHFQVAHQGCLPTYPCDMCNFTANDFPVLQQHRLGHRDTYVKCEICNDNVQYSLLQLTRHFSSYHSSNGHYRCEKCKFSTKDVGTFVQHIHRHSEVQYKCGKCQHVSYTKGEFQRHLLVHTGTFPFQCQFCDYGATRKDYVLKHMNAVHSDEIERKCKLKDKEDGAKTLADAKSGLKLLLKRNTAGVARDAQWRTAGFHALSGGGLLDEYGRLANPEKTLEETQQFLERTVASEKDCIQWAKARKSEQQYLSPSTPAVLKPKMESCLGSNSGFLKTGGSGSSVLMVKNKISIPPNCTTKFMGFKMVDGKRHLVLKVIPAAKLGSSPQTVAPSVEKDAKGRGPEKGMNGPICVEDVALQCSSLPVSSHSSLSQSTLPACSDSQSSINKGSSVVKELLQAENQESSSTSHTVVNDGHPISDDEQKPSSSASPTTCKVFHTTSQKAQIAHPSKAEMDQQSEHTSLVEFASNKTSPEMDKESLSSKETLLESIVVDNENNSDLNSSRQEVFSFHNYSKDRASSESSDTVKESGDQEASQLMTDVCVKDSFQSQCAKDLTGTSLTLADVLSPHSQDCKVDEEMGEIIADQLSSQGVMEKVPDSEIEVDECIATVEEDSAEPSDVLEEPEDSLFMPKITSVFSLQSEENGPQLDVNQLLEKVLETENKKASILSAQEKKELKVAAGESTVGNPCSATALGRILEEHSDAIISQQLEKERISSANQDPVKNSAATLRILQPINVTEGKKQVFLKPCQNGFALPIQVGSNQGFQLITGSSHPQINVSYLNTGKERPKKPPGLTFTLNNGRIGTTAQIVGDKKVSGGAGNGEESAVLCCGSSTGHYIVNNMPLKGSLILSNSVQSLSGERTSNLPTCFLVQRQLPMVTSTSCQSGVTVSHNIQGQPQRPVLAVPINSPEKPAVVQAGRQAFLLKCVTPVKQGTLLNSQIEAKVLNQNCTSNESGGNKVLLKIVRNASGSSFPSSTGELNGIQTLAMTNQPVYLTTGALQSSCISRSSNQSIVNVSTGYKTSGPSQDSSNEPLTVSQLLNCSSPAAVQGKSKEKESGVNSHGKIKRVCLPSPKQNHLAIRKKRQRGLLLEESSGPSPKAKKPLSKKWKETEKGPADAHELCATPVPKDVERTLRLSPFSATQRIKCPRRNQPVVVLNHPDADVPEVVNVMKTINKFKGHVLKVALSQRTIDALSELNCDPLNENPSLNIHATRSRRAKPVSPVKERYILKLRLKKTSRNKYKVVKSTSDSTEKPTFSCWFCGRIFDNQEEWIGHGQRHLMEATRDWNKLF
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 (By similarity).
Subcellular Localization:
Nucleus. Chromosome, centromere. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis.
Sequence:
MAPARRKAAAGARGRKLSAFLKDFDREVRSRVEQLRTNGERLVKEMENLYDVELLRLPAALREMNWLEFFAKGGSQKVVEEAVTADLGITEINKLTAELIQTPLKIVTKEKSKQGIEATEEAAEVPLLPPAKKAKHDSQLLLEQAAASTNPRNGKVRTSTKKAPVSRSRRAPSARVKRVSKRSSKSSFITPATGRNLDLCARGGASIVTPRFDSRVFKTPGLRTPAVNERVYTISANGSPLADGMMSSLPFLLGGGESIRLTASDLTKKNLLHLNPEGRGIMQKLSVRLCTSLYSAKT
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 and as sensor of hydrogen peroxide-mediated signaling events.
Sequence:
MDVKYEFTLPSSSGADFHSAEHLPLVVYFYPKDSTLGCTTEGLDFNARLEQFEALGYTVVGISRDGVKAHQNFCAKQGFRFELLSDKDETVCRLFDVIKLKKLYGKESLGIERSTFVLNKDGEIAHEWRKVKVAGHAQEVLETLSR
The following text describes a protein:
Function:
Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets.
Subcellular Localization:
Cell membrane. Secreted. Cytoplasm, cytosol. Note=Predominantly secreted. Also found associated with the plasma membrane.
Domain:
The IGFBP N-terminal domain mediates interaction with TSC2 substrate.
Sequence:
MQIPRAALLPLLLLLLAAPASAQLSRAGRSAPLAAGCPDRCEPARCPPQPEHCEGGRARDACGCCEVCGAPEGAACGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDANTYANLCQLRAASRRSERLHRPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELFRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKHRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDKIKKFLTESHDRQAKGKAITKKKYIGIRMMSLTSSKAKELKDRHRDFPDVISGAYIIEVIPDTPAEAGGLKENDVIISINGQSVVSANDVSDVIKRESTLNMVVRRGNEDIMITVIPEEIDP
The following text describes a protein:
Function:
Essential light chain for the class II conventional myosin MYO1. Also acts as light chain for the class V unconventional myosin MYO2 and for IQG1. Involved in the assembly of the contractile actomyosin ring at the bud neck during cytokinesis by recruiting IQG1 to the bud neck. Also required for chitin and MYO2-dependent secretory vesicle deposition to the center of the bud neck for septum formation. May stabilize MYO2 by binding to its IQ domains. Its major function is probably not to regulate MYO1 activity, but rather to coordinate actin ring formation and targeted membrane deposition during cytokinesis via its interactions with MYO1, IQG1 and MYO2.
Subcellular Localization:
Bud neck. Bud tip. Note=Concentrates to sites of polarized growth, namely to the incipient bud site in G1, to the bud tip during S and G2 phases of the cell cycle and to the bud neck during cytokinesis.
Sequence:
MSATRANKDIFTLFDKKGQGAIAKDSLGDYLRAIGYNPTNQLVQDIINADSSLRDASSLTLDQITGLIEVNEKELDATTKAKTEDFVKAFQVFDKESTGKVSVGDLRYMLTGLGEKLTDAEVDELLKGVEVDSNGEIDYKKFIEDVLRQ
The following text describes a protein:
Function:
A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones. Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C20 to yield 20R,22R-hydroxycholesterol that is further cleaved between C20 and C22 to yield the C21-steroid pregnenolone and 4-methylpentanal. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein. Note=Localizes to the matrix side of the mitochondrion inner membrane.
Sequence:
MLAKGLPLRSVLVKGCQPFLSTVWEGPGHPRVPTGDGASISTQIPRPFSEIPTPGNNGWLNLYNFWREMGSQKIHYHQVQNFQKYGPIYREKLGSVESVYIIDPEDVALLFKFEGPTPERFCIPPWVAYHQYHQRPVGVLLKKSGAWKKDRLALNQEVMAPEAIKNFIPLLDPVSQDFVKVLHRRIKQQGSGKFSGDISDDLFRFAFESITNVMFGERLGMLEERVDPEAQRFIDAVYQMFHTSVPMLTFPPDLFRLFKTKTWRDHVAAWDVIFNKAEIYTQNFYWELRQKRDVDNYPGILHRLLKSNKLLFEDVKANITEMLAGGVDTTSMTLQWHLYEMARSLEVQEVLREEVLAARRQAQGNVSTMLQLVPLLKASIKETLRLHPISVTLQRYLENDLVLRNYMIPAKTLVQVSTYAMGQDPTFFLNPSKFDPTRWLGKDKELIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFRVEMQQLRDVGTTFNLILMPDKPIFLTFRPFNQGPPQRRAESSNCRHGEGQMGNRWAAGPIPRARTTRA
The following text describes a protein:
Function:
Exhibits an intrinsic ATPase activity that is stimulated by both 70S ribosomes and 30S ribosomal subunits. Could be involved in protein-chain elongation and in release of deacyl-tRNA from ribosomes after peptide bond synthesis. Stimulates the synthesis of polyphenylalanine in vitro.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MTHLELVPVPPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIAWMPQGLGKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSATLEEAFINLLPQAQRQAHQAVVIPPYQPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGAASLEEAFIAYLQEAAGQSNEAEAPPVVHDTTHAPRQGFSLRRLFSYSRREALELRRDPVRSTLALMGTVILMLIMGYGISMDVENLRFAVLDRDQTVSSQAWTLNLSGSRYFIEQPPLTSYDELDRRMRAGDITVAIEIPPNFGRDIARGTPVELGVWIDGAMPSRAETVKGYVQAMHQSWLQDVASRQSTPASQSGLMNIETRYRYNPDVKSLPAIVPAVIPLLLMMIPSMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIALGMLNFFLLCGLSVFVFGVPHKGSFLTLTLAALLYIIIATGMGLLISTFMKSQIAAIFGTAIITLIPATQFSGMIDPVASLEGPGRWIGEVYPTSHFLTIARGTFSKALDLTDLWQLFIPLLIAIPLVMGLSILLLKKQEG
The following text describes a protein:
Function:
Tubulin is the major constituent of microtubules (Probable). The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Note=Expressed during all cell cycle phases with maximal expression at the S/G2 phases. In the nucleus, forms a ring-like structure surrounded by six equally-spaced gamma-tubulin-rich patches.
Sequence:
MPREIITLNVGQCGNQLGSEFFKKICSEHGILPDGSLSTNEFIDDRKDVFFYQADDQRYVPRSINIDLEPRVLDSIRTSEWSNFYNPENFIIPTNNGAGNSWANGYYTTEKMSEIEEIIDREVEHCDSLEGFFFCHSICGGTGSGLGSKIMEMISEKYPKNILTSFSVMVKENPDVVVSPYNSILTLRRLITECQSVVVFDNSALADITHTQFGVDEATVFDMNSIISSSMSAFTANLRFPSTLYNSLNSLMIHLCPSRFSHFLMTSYTPLRQVNQISSRTSAIDVMKRLIQPQNIMARTRLKEGKYISMCDFFQGDVSYDEINEALQRFTDRRLAEFVPWNKEAIKVVHTRVSPLVKRGNRMSGMLLANNTSIRYYFQDILKAFDQMFKKRVYLESYREQFHDNFQEFEESKEIVKCVIEEYAKAESIEYSDYSYPIHKYLKGIAKEKIAE
The following text describes a protein:
Function:
A acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MSSTKPLPMHGDGGSQFEIFTVVLIPAVGILLRNLFLPWITHGKRFPSNGRLYWIKFLVDFIFIVAPTLLVQTVLADSVGFVHLIMFSVIALLLVFMLVEQAMVVKDGATARHILNKIIEEHHAPTTFLTYFRSAIFILVAIAVLGVDFAIFPRRFAKTETVGHSLMDVGVAAFIAANGLVPPLKTSSRKEEGERKRASRRFSLIYSSTLLLVGLGIVRTIVLSILGYPYQVSEYGIHWNFFYTLAVVNLVTYLLPSQFTLITATIFAAVHQTALSNGVQAWVLDETAPRDSFLEANREGICSLAGYIAIYYYSRAMGRFIAKTALAGLRVRSWSAAVLHMLLLCGIFAAAQLAAEAALGPPSRRLVNLPYILAMISMECYLLAGCIGVQTISYIIWAARVPHFGSEENPFATSEPCLMTALNKHPLLFFLVSNVTTGVVNISIRALDLESWSLGPPVALCLLFAHMLAATAVPIFLCAKKKQ
The following text describes a protein:
Function:
Component of the FERRY complex (Five-subunit Endosomal Rab5 and RNA/ribosome intermediary). The FERRY complex directly interacts with mRNAs and RAB5A, and functions as a RAB5A effector involved in the localization and the distribution of specific mRNAs most likely by mediating their endosomal transport. The complex recruits mRNAs and ribosomes to early endosomes through direct mRNA-interaction. Plays a role in mast cell degranulation.
Subcellular Localization:
Cytoplasm. Early endosome.
Sequence:
MKKNRERFCNREREFVYKFKVGSQCLELRVPLKFPVQENASHLHGRLMLLHSLPCFIEKDLKEALTQFIEEESLSDYDRDAEASLAAVKSGEVDLHQLASTWAKAYAETTLEHARPEEPSWDEDFADVYHDLIHSPASETLLNLEHNYFVSISELIGERDVELKKLRERQGIEMEKVMQELGKSLTDQDVNSLAAQHFESQQDLENKWSNELKQSTAIQKQEYQEWVIKLHQDLKNPNNSSLSEEIKVQPSQFRESVEAIGRIYEEQRKLEESFTIHLGAQLKTMHNLRLLRADMLDFCKHKRNHRSGVKLHRLQTALSLYSTSLCGLVLLVDNRINSYSGIKRDFATVCQECTDFHFPRIEEQLEVVQQVVLYARTQRRSKLKESLDSGNQNGGNDDKTKNAERNYLNVLPGEFYITRHSNLSEIHVAFHLCVDDHVKSGNITARDPAIMGLRNILKVCCTHDITTISIPLLLVHDMSEEMTIPWCLRRAELVFKCVKGFMMEMASWDGGISRTVQFLVPQSISEEMFYQLSNMLPQIFRVSSTLTLTSKH
The following text describes a protein:
Function:
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Subcellular Localization:
Mitochondrion.
Sequence:
MSIAICGGGIAGLSTAFYLARLIPKCTIDLYEKGPRLGGWLQSVKIPCADSPTGTVLFEQGPRTLRPAGVAGLANLDLISKLGIEDKLLRISSNSPSAKNRYIYYPDRLNEIPSSILGSIKSIMQPALRPMPLAMMLEPFRKSKRDSTDESVGSFMRRRFGKNVTDRVMSAMINGIYAGDLNDLSMHSSMFGFLAKIEKKYGNITLGLIRALLAREILSPAEKALKAALLAEPKTAELSNSMKSTSMFAFKEGIETITLSIADELKKMPNVKIHLNKPAKTLVPHKTQSLVDVNGQAYEYVVFANSSRNLENLISCPKMETPTSSVYVVNVYYKDPNVLPIRGFGLLIPSCTPNNPNHVLGIVFDSEQNNPENGSKVTVMMGGSAYTKNTSLIPTNPEEAVNNALKALQHTLKISSKPTLTNATLQQNCIPQYRVGHQDNLNSLKSWIEKNMGGRILLTGSWYNGVSIGDCIMNGHSTARKLASLMNSSS
The following text describes a protein:
Function:
Plays a role in the reduction of telomerase activity during differentiation of embryonic stem cells by binding to the core promoter of TERT and controlling its down-regulation.
Subcellular Localization:
Nucleus speckle.
Sequence:
MWGQWQTAAAVAPTAALPPQPSVPPPLPDAPPPPPPSDATAGAGASSGASAPIVTTAAAVTTAPGFNPYSSGQATGAGNPYQQYTAAQYAAMTPEQQYALQHHWQQWQTYQEEYAKWHAQYGEQYKREMAAAAATTTAVQGVPAPVVATPAAAPVPVVAPPGPQAYPVAHNYYQGVSASPAQSTTPVAVAGAPPLPGKIMAQPQMYNQPPPPPQKGGYNQHPNDIQSMWSGPPPMQQPPPNRYGGGQMNQMNYNIAGQDNQGFPNLQQPPPSLQRPTPQQQQPHLNHMDHGQWGNNQHGVGNNNRPTWDTSGPPPDNTGQPNRWNGPPPANDVNNRWNGTSFNNNTNDGNRRWDGTSNQAPSGGDQQLNRWMSEPPPSLPNPNQQYQNQNSWMSGPPPSISDPPQDHQQQNNSSQNARSSRWQGINSDIDTPPMRTNNKPNSIQNSRNSWGDGGGDGNQSKNPFIKNPQSDFGNYGNSYNSQDQGSAGGGNFGGFGDDSGGKQSQDSFAGRGGGPGNNINNNFSNNRRQNNRRDNNRNQGFSDERGGGDSGPGGYNPNRGNYNQRNSFNQSNAPYKQSQQNRNQQQPPDLDEASFDLLFDQWEQQFEEWKLANANHPDRDEYRRYEEEFEKQRRRIAERREQMRRRRQLQMGGSAGGSTTDIRKEAAAGASTTAEQKPNKDPFEGQGRFADQGDQDHGSGPNFGNGNRQSGNAGHFGKENRPFESAGVPAFRGNQGPPPGMHNQYQTAQEAIQQILDEQPDESNQEIPTKPAASNENSSDVKKAKTTASPVAPPIAPVVPPEVKAPAAPVVPDPTVVPPTQPPPVSTNYGKRRQRAAPSQIPAKQVKEEEPIFTISLDDDDDDDEEKEVVQDAPNTPMGSIFKKNDGIPGLDLVDDGSNKNNSSSVFNVVLKDSSEKKAADETEKQPGDVSADKKGDESLSNALKDPNFINNLSQAVANVQEREQRDRHEQRDDQESGTDGRPLSFAEWQRKKNSGNENKSQDAGDSVSTNNGEKPDNNGPPGGFGPGNGPGGGPGSGPGQNDGSRFDVFGPNQVSGNNFIDLDNNGPPGFGPPGRNFGPNGPGPRGNFGPNFGHNFGPRGPGGPFIRPNGPLPGPGPNFGPHFRPNGPNFGPNFGPNFGPRPGSRNFGPRGPDGPFGPGRDDFGGPPFGGPRPHMGPNGPGHNMRGFNGGPISDNPFRRQGGPPGPGFGNDDLGAGPPRGPRNFGNRFGNPGGGGGGGGGGGNNNRKNWNDGPEQQQFHDRLNHNDAIYRPLKVFDYSNNPTAAKVIDYGHKSGDGNPIDGPSGSNPDDRIPEFKAMKTFEYGHSSYMGSNRLGMPGGMGGGGDHNQAMTGGRGMAAGPGRFGGPGGAGNKRKNKKKNKQQKNGELMTFNQNQQMQSNTVEERSITNPEQDEERAHNELRNQNQADEFQKNEERNDLEDISEGEDNLQSIVFDDDNEELPPPPSMKIWNQGNAQEQYNPFPVNPLRRQLGDYSDKLEAPSPAMSLFPSAANANDRTSDPMKASNLEMCVATSENRNTFSLDEVLLYPGRLNRPKRICIILRGPPGCGKSHVARLIKEKELEMGGANPRILSIDDYFLIENDYDEKCPKTGKKIPKKEILYEYDDTMEETYMQYLIKSFKKTLSDNLYDFVIVDCNNNSLRTLNEFYCHAKDSNFVPYIVDLHCDLETCLGRNSHQRSVNDIRVVLDNWCQTPTHYIKLDVSSLLENVVEMEDVEDMATDDNACADVGATVGESAALEDAAVEETDDSNSADASNYCGFLKSKWERDTTEDNLARLDGTKRLMQNRRTTSMADYLQLEDWKPPTTSDNGKKRVRWADIEEKRSQKKMRAIGFVVGQTDWNRMMDPNAGSRALNKTKFIERIKRR
The following text describes a protein:
Function:
Endonuclease involved in group I intron homing. Recognizes and cleaves a 19-24 bp palindromic DNA site.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MNTKYNKEFLLYLAGFVDGDGSIIAQIKPNQSYKFKHQLSLTFQVTQKTQRRWFLDKLVDEIGVGYVRDRGSVSDYILSEIKPLHNFLTQLQPFLKLKQKQANLVLKIIEQLPSAKESPDKFLEVCTWVDQIAALNDSKTRKTTSETVRAVLDSLSEKKKSSP
The following text describes a protein:
Function:
Involved in the TolC-like protein HgdD-dependent secretion of schizokinen, a dihydroxamate-type siderophore. Transports schizokinen from the cytoplasm to the periplasm.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MLPKLILLATLYISQFIPTTFFIQALPVFMRQQKMSLDVIGFLGLLILPSGLKFLWSPFIDRYRLGKLGHYRGWIICFQLLLISTMLVTAFIDIQDNLNAFLTCMFLASLFSSSQDIATDALAVNLLEPQERGLGNAIQSGGNIFGAIIGGGVMLILLDKIGWRYSLITLSIFMLINLVPILIYREKSQHQLENSTFFRSYFQPFISFLSRPKALPWLFVVLLYMMGDSVTSLMIRPLLVDRGLSLPDIGWILGIVSYSARIVSALIAGLVIVKLGRIKSLIIFGFIADLTTLLYIIPAIGVSSLLVLYTVCIIVNATQSMAYTALLSAMMDKCEKNTAATDYTMQVSVMFLGGIAATVLSGMLATTMGYSFIFIMSAAVSLLSVFLITQEYGVSS
The following text describes a protein:
Function:
Functions redundantly with BOI2 to promote the fusion of secretory vesicles with the plasma membrane at sites of polarized growth.
Miscellaneous:
MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
Subcellular Localization:
Bud. Bud neck. Note=Localizes to the periphery of buds during much of the budding cycle and to necks late in the cell cycle.
Domain:
The PH domain binds to phospholipids which is important for localization to the bud; The SH3 domain is important for localization to the neck.
Sequence:
MSLEGNTLGKGAKSFPLYIAVNQYSKRMEDELNMKPGDKIKVITDDGEYNDGWYYGRNLRTKEEGLYPAVFTKRIAIEKPENLHKSPTQESGNSGVKYGNLNDSASNIGKVSSHQQENRYTSLKSTMSDIDKALEELRSGSVEQEVSKSPTRVPEVSTPQLQDEQTLIQEKTRNEENTTHDSLFSSTADLNLSSESLKNISKSNISTKSLEPSSESVRQLDLKMAKSWSPEEVTDYFSLVGFDQSTCNKFKEHQVSGKILLELELEHLKELEINSFGIRFQIFKEIRNIKSAIDSSSNKLDADYSTFAFENQAAQLMPAATVNRDEIQQQISSKCNKLSSESSDRKSSSVTTELQRPSSVVVNPNFKLHDPAEQILDMTEVPNLFADKDIFESPGRAPKPPSYPSPVQPPQSPSFNNRYTNNNARFPPQTTYPPKNKNPTVYSNGLIPNSSTSSDNSTGKFKFPAMNGHDSNSRKTTLTSATIPSINTVNTDESLPAISNISSNATSHHPNRNSVVYNNHKRTESGSSFVDLFNRISMLSPVKSSFDEEETKQPSKASRAVFDSARRKSSYGHSRDASLSEMKKHRRNSSILSFFSSKSQSNPTSPTKQTFTIDPAKMTSHSRSQSNSYSHARSQSYSHSRKHSLVTSPLKTSLSPINSKSNIALAHSETPTSSNNKEAVSQPSEGKHKHKHKHKSKHKHKNSSSKDGSSEEKSKKKLFSSTKESFVGSKEFKRSPSELTQKSTKSILPRSNAKKQQTSAFTEGIRSITAKESMQTADCSGWMSKKGTGAMGTWKQRFFTLHGTRLSYFTNTNDEKERGLIDITAHRVLPASDDDRLISLYAASLGKGKYCFKLVPPQPGSKKGLTFTEPRVHYFAVENKSEMKAWLSAIIKATIDIDTSVPVISSYATPTIPLSKAQTLLEEARLQTQLRDAEEEEGRDQFGWDDTQNKRNSNYPIEQDQFETSDYLESSAFEYPGGRL
The following text describes a protein:
Function:
Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain. AHA motifs are transcriptional activator elements.
Sequence:
MDYSTVKQEEVEVVVLDGEEEAAAAAAPVPLPAAMGVGAAVAPFLVKTFEMVEDPATDAVVSWGGAARNSFVVWDPHAFAAGLLPLHFKHANFSSFLRQLNTYGFRKVSADRWEFANEDFLGGQRHLLANIRRRRRGAGTGSTTPRAVNCGGGGGEGEVERLRRDKEALARELARLRRQQQEARAQLLDMERRVRGTERRQEQCTEFLARALRSPDVLDNIARRHAAAVERKKRRMLAAAADDDGLTFEALALAAAADTSHSTGGAVTTDMIWYELLGEEQAEIDIEVDQLVASASAAADTASEAEPWEEMGEEEVQELVQQIDCLASPSS
The following text describes a protein:
Function:
May function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Regulates centriole biogenesis by suppressing the formation of aberrant centriolar protein complexes in the cytoplasm and thus preserving mitotic spindle integrity. Prevents the formation of the STIL-CPAP complex (which can induce the formation of aberrant centriolar protein complexes) by interfering with the interaction of STIL with CPAP. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.
Subcellular Localization:
Nucleus. Nucleus, nucleolus. Cytoplasm. Note=In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Cytoplasmic localization is crucial for its function in suppressing the formation of aberrant centriolar protein complexes.
Sequence:
MKIFVGNVDGADTTPEELAALFAPYGTVMSCAVMKQFAFVHMRENAGAVRAIEALHGHELRPGRALVVEMSRPRPLNTWKIFVGNVSAACTSQELRSLFERRGRVIECDVVKDYAFVHMEKEADAKAAIAQLNGKEVKGKRINVELSTKGQKKGPGLAIQSGDKTKKPGAGDTAFPGTGGFSATFDYQQAFGNSTGGFDGQARQPTPPFFGRDRSPLRRSPPRASYVAPLTAQPATYRAQPSVSLGAAYRAQPSASLGVGYRTQPMTAQAASYRAQPSVSLGAPYRGQLASPSSQSAAASSLGPYGGAQPSASALSSYGGQPAAASSLNSYGAQGSSLASYGNQPSSYGAQAASSYGVRAAASSYNTQGAANSLGSYGAQAASYGAQSAASSLAYGAQAASYNAQPSASYNAQSAPYAAQQAASYSSQPAAYVAQPATAAAYASQPAAYAAQATTPMAGSYGAQPVVQTQLNSYGAQASMGLSGSYGAQSAAAATGSYGAAAAYGAQPSATLAAPYRTQSSASLAASYAAQQHPQAAASYRGQPGNAYDGTGQPSAAYLSMSQGVVANANSTPPPYERTRLSPPRASYDDPYKKAVAMSKRYGSDRRLAELSDYRRLSESQLSFRRSPTKSSLDYRRLPDAHSDYARYSGSYNDYLRAAQMHSGYQRRM
The following text describes a protein:
Function:
The 83 kDa subunit binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit.
Subcellular Localization:
Secreted.
Sequence:
MLPRAWLRWACLLLLARCARPCPAGCDCFAQELFCSDAGLAAVPPDIPPLATDIVFVETSLSTLGSRAFSGSPNLTKVVFLNAPLQHLGPDAFGGLPRLQDLEVTGGAFANLSSAAFSNLTSLGKFTFNFNLLEALPEGLFGHMEALESLQLQGNRLQSLPRRLFQPLTRLQSLNLAQNLLAHLPEGLFDPLGSLQTLRLSDNALSGLPPGVFGGLHSLRELFLDGNSISELPPGVFSRLFRLEQLWLQRNAIGHLPLSVFSSLGNLTFLSLQGNALRVLPAGLFAPTPGLLVLSLSYNKLEAVSEGAFANLSSLSSLTLSHNAITHLPAGVFRGLEGLVKLYLGSNNLTALHPALFQNLSNLELLSLSRNLLTTLPTGIFDSNYNLFNLALHGNPWQCDCHLAYLFQWLYQYSDRLFNIQTYCAGPAYLKGQVLPALKEEQLVCPVTRDHLGFQAPGPEHGDPGSSWDLGVEERAVWSRCTYSNPEGTVVLACDEARCRWLNIQLSPRQGSGPPGMTYNASQGWDLKSSCGSVRVTVAIEARPGGH