lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Multifunctional enzyme required for phylloquinone (vitamin K1) biosynthesis.
Miscellaneous:
MISCELLANEOUS: Consists of a fusion of four bacterial genes, menF, menD, menC and menH belonging to the same operon. In higher plants, the C-terminal chorismate binding domain is absent from the isochorismate synthase (MenF) module, leading to a non-functional module. The isochorismate synthase activity has been taken over by ISC1 and ICS2. In green and red algae lineages, this module has maintained its structural integrity and is functional.
Subcellular Localization:
Plastid, chloroplast membrane; Single-pass membrane protein.
Sequence:
MRSSFLVSNPPFLPSLIPRYSSRKSIRRSRERFSFPESLRVSLLHGIRRNIEVAQGVQFDGPIMDRDVNLDDDLVVQVCVTRTLPPALTLELGLESLKEAIDELKTNPPKSSSGVLRFQVAVPPRAKALFWFCSQPTTSDVFPVFFLSKDTVEPSYKSLYVKEPHGVFGIGNAFAFVHSSSVDSNGHSMIKTFLSDESAMVTAYGFPDIEFNKYSTVNSKDGSSYFFVPQIELDEHEEVSILAVTLAWNESLSYTVEQTISSYEKSIFQVSSHFCPNVEDHWFKHLKSSLAKLSVEEIHPLEMEHMGFFTFSGRDQADVKELKSIQSSCQFHCKLSPDVVFSNNMLNRETEVSNFLRDEANINAVWASAIIEECTRLGLTYFCVAPGSRSSHLAIAAANHPLTTCLACFDERSLAFHAIGYAKGSLKPAVIITSSGTAVSNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFNLPPPTDLIPVRMVLTTVDSALHWATGSACGPVHLNCPFRDPLDGSPTNWSSNCLNGLDMWMSNAEPFTKYFQVQSHKSDGVTTGQITEILQVIKEAKKGLLLIGAIHTEDEIWASLLLAKELMWPVVADVLSGVRLRKLFKPFVEKLTHVFVDHLDHALFSDSVRNLIEFDVVIQVGSRITSKRVSQMLEKCFPFAYILVDKHPCRHDPSHLVTHRVQSNIVQFANCVLKSRFPWRRSKLHGHLQALDGAIAREMSFQISAESSLTEPYVAHMLSKALTSKSALFIGNSMPIRDVDMYGCSSENSSHVVDMMLSAELPCQWIQVTGNRGASGIDGLLSSATGFAVGCKKRVVCVVGDISFLHDTNGLAILKQRIARKPMTILVINNRGGGIFRLLPIAKKTEPSVLNQYFYTAHDISIENLCLAHGVRYVHVGTKSELEDALFVPSVEEMDCIVEVESSINANAIVHSTLERFARQAAENSLGIVSASSFLHPMIKNVLLCQVSGIQYSQYRVKLCDRPTICSDEFSQFHREGFILSLTLEDGSIGYGEVAPLNSNVENLMDVEGQLQLVLHLMNEAKFSYMLPLLNGSISSWIWSELGITASSIFPSVRCGLEMALLNAMAVRHDSSLLGILHYQKEENGSAQPHSVQICALLDSEGTPLEVAYVARKLVQEGFSAIKLKVGRRVSSVQDALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPVQNKDDLIRFHEETGLPVALDETLDDFEECPLRMLTKYTHPGIVAVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYILFASYLEMENVKASTEQKQGTPPSVAHGLGTYRWLSEDVMMNTLGIFRSPYSGFVEGFIADASRNLKDVKINNDVIVRTSKGIPVRRYELRVDVDGFSHFIRVHDVGENAEGSVALFLHGFLGTGEEWIPIMTGISGSARCISVDIPGHGRSRVQSHASETQTSPTFSMEMIAEALYKLIEQITPGKVTIVGYSMGARIALYMALRFSNKIEGAVVVSGSPGLKDPVARKIRSATDDSKARMMVDNGLYIFIENWYNGGLWKSLRNHPHFSKIAASRLLHGDVPSVAKLLSDLSSGRQPSLWEELEDCDTNISLVFGEKDVKYKQIATRMYREMSKSKKSVNNIIEIVEIPEAGHAVHLESPLRVILALRKFLTRVHNSSTETELSQKLLLALKEM
The following text describes a protein:
Function:
May function as 2-oxoglutarate-dependent dioxygenase.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
MVWAPLGPPRTDCLTLLHTPSKDSPKMSLEWLVAWSWSLDGLRDCIATGIQSVRDCDTTAVITVACLLVLFVWYCYHVGREQPRPYVSVNSLMQAADANGLQNGYVYCQSPECVRCTHNEGLNQKLYHNLQEYAKRYSWSGMGRIHKGIREQGRYLNSRPSIQKPEVFFLPDLPTTPYFSRDAQKHDVEVLERNFQTILCEFETLYKAFSNCSLPQGWKMNSTPSGEWFTFYLVNQGVCVPRNCRKCPRTYRLLGSLRTCIGNNVFGNACISVLSPGTVITEHYGPTNIRIRCHLGLKTPNGCELVVGGEPQCWAEGRCLLFDDSFLHAAFHEGSAEDGPRVVFMVDLWHPNVAAAERQALDFIFAPGR
The following text describes a protein:
Function:
Component of the intraflagellar transport (IFT) complex B: together with IFT74, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds tubulin via its CH (calponin-homology)-like region. Required for ciliogenesis. Required for proper regulation of SHH signaling (By similarity). Plays an important role during spermatogenesis by modulating the assembly and elongation of the sperm flagella (By similarity).
Subcellular Localization:
Cell projection, cilium. Cytoplasm. Cytoplasm, cytoskeleton, cilium basal body.
Domain:
The CH (calponin-homology)-like region shows high similarity to a CH (calponin-homology) domain and mediates binding to the globular domain of tubulin.
Sequence:
MSDQIKFIVDSLNKEPFKKNYNLITFDSLGPMQLLQVLNDVLAEIDPKQDVDIREETPEQTAKRMLSLLGILKYKPPGNATDMSTFRQGLVIGSKPVIYPVLHWLLQRSSELKKRAYLARFLIKLEVPSEFLQDETVADTNKQYEELMEAFKALHKECEQLKTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLMKRLEEEIKFNSYMVTEKFPKELESKKKELHFLQKVVSEPAMGHSDLLELESKVNEVNAEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVSVKTNQTREFDGTEVLKGDEFKRYVSKLRSKSTVFKKKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGISGYSYTQEELERVSALKSEVDEMKGRTLDDMSEMVKKLNSLVSEKKSALAPVIKELRQLRQKCQLTQECDEKRTQYDSCAAGLESNRSKLEQEVRGLREECLQEESKYHYTNCMIKNLEVQLRRATDEMKAYVSSDQQEKRKAIREQYTKNITEQENLGKKLREKQKAVRESHGPNMKQAKMWRDLEQLMECKKQCFLKQQSPASIGQVIQEGGEDRLVL
The following text describes a protein:
Function:
May be involved in the efflux of glucose towards the cytosol.
Subcellular Localization:
Plastid, chloroplast inner membrane; Multi-pass membrane protein.
Sequence:
MQSSTYAVKGNAAFAFQRRTFSSDRSTTSTGIRFAGYKSLATTGPLYCSGSEAMGATLARADNGIQSVMSFSSVKARSVRAQASSDGDEEEAIPLRSEGKSSGTVLPFVGVACLGAILFGYHLGVVNGALEYLAKDLGIAENTVLQGWIVSSLLAGATVGSFTGGALADKFGRTRTFQLDAIPLAIGAFLCATAQSVQTMIVGRLLAGIGIGISSAIVPLYISEISPTEIRGALGSVNQLFICIGILAALIAGLPLAANPLWWRTMFGVAVIPSVLLAIGMAFSPESPRWLVQQGKVSEAEKAIKTLYGKERVVELVRDLSASGQGSSEPEAGWFDLFSSRYWKVVSVGAALFLFQQLAGINAVVYYSTSVFRSAGIQSDVAASALVGASNVFGTAVASSLMDKMGRKSLLLTSFGGMALSMLLLSLSFTWKALAAYSGTLAVVGTVLYVLSFSLGAGPVPALLLPEIFASRIRAKAVALSLGMHWISNFVIGLYFLSVVTKFGISSVYLGFAGVCVLAVLYIAGNVVETKGRSLEEIELALTSGA
The following text describes a protein:
Function:
Alpha-1,3-xylosyltransferase, which elongates the O-linked xylose-glucose disaccharide attached to EGF-like repeats in the extracellular domain of target proteins by catalyzing the addition of the second xylose. Known targets include Notch proteins and coagulation factors, such as F9.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MACRITGMRALHGILLLAAALAVFAFYYLGSGKENFSSTTRRIKENRAAQSTSTELDLIDAASSELKLSEKGKILESRGPLDYHLLMMFTKVHRNPGLRDKFQVALSSLIKYGKFESNEVLCLHFVSDEPSKEIGKSLLKDLLQGASFKYKVIFHDVGMLTEKLFPIVEAMQKHFSSGSGTYYSDSIFFLSVALHQIMPKEIYRIIQLDLDLKFKTNVRELFEEFDNFMHMSIIGIAQEMQPVYRHTFWQYRKENPSTKVGEPPPDGMPGFNSGVMLLNLEAMRQSRLYNELLEPNAVQQLAEKYHFKGHLGDQDFFSMIGMEHPELFYVLDCGWNRQLCTWWKDHGYMDVFDDYYRCEGNIKILHGNCNTPIPEE
The following text describes a protein:
Function:
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Subcellular Localization:
Cytoplasm.
Sequence:
MFTALFVLYGKKRLPVRESTSKKLRKIIHVDMDCFYVAIEMRDNPKLREKPVAVGGAAHSRGVICTANYIARGYGVQSAISSSYAKKLCPSLIILPVNMEKYRAIGHQIRGLFQEYTHLVEPLSLDEAYLDVSDCKIHQGSATRIAQEIREQIVKRHSLTASAGVASNKLLAKVASAWNKPNGIKVILPSKADDFVKTLPIEKIHGVGKITAQKMKAMNIHTCSDLQALSREALSKSFGSFGVTLYELCRGIDPRSVEPNRIRKSVSVEHTFSQDIATLSECEIELANLFNDLKQRLLKHTDRCIRKQFVKIKFNDFKITKAETITQTISLDLFKHLLYQIFERQQKPVRLLGVGVSFSEDPLLELQRTFEW
The following text describes a protein:
Function:
Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MNLKPYTLGRVATALLFLWITTATALASEADYDALFREANDLMGAGDLPAAMEVLKKVPAPRAGEEGDAFVRSRMQIAKLHFAAKEMDEALAAAREVLSLYPDNSEAKNFTASVEREKKPGYVTFLQDCLKFLPVLLKGAVMTLLLVLCTMFISPIGGLLIALGRISTFRPLSALCWFVIWLFRGTPLLLQLFFIYYGLPSLGITLKPITAAVIGLGLNYSAYLGEIIRGAIQSIDHGQTEAAKALGMTYGQTMRRVVIPQTYKRLMPPIGNEFIALIKDTALVSTIAMVELMRAADQMFNTYFNVTALVLAAVIYLIFTTFFTFLFEKIEHRAGIYERR
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. Overexpression of bL31m suppresses mutations in the COX2 leader peptide-encoding and initiation codon regions.
Subcellular Localization:
Mitochondrion. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1.
Domain:
Contains two functional domains. The central domain is sufficient for general mitochondrial translation but not suppression of COX2 mutants. The C-terminus sequence is sufficient for dosage suppression of COX2 mutants.
Sequence:
MLKSIFAKRFASTGSYPGSTRITLPRRPAKKIQLGKSRPAIYHQFNVKMELSDGSVVIRRSQYPKGEIRLIQDQRNNPLWNPSRDDLVVVDANSGGSLDRFNKRYSSLFSVDSTTPNSSSETVELSEENKKKTQIKKEEKEDVSEKAFGMDDYLSLLDDSEQQIKSGKLASKKRDKK
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for maturation of extramitochondrial Fe/S proteins.
Subcellular Localization:
Cytoplasm, perinuclear region.
Sequence:
MLGSATIDQAGEREARENDPAALNDSRLENQIYTFANTLEKFEKQLKQAQNGQTVEEAENMHGGAVWWMMAVAVALIGRDNARLYTRVTDRERDDYEVQMFIHCTLDIVEDKLSKANELYLGLLTSNHKHKSYGFVTNTGVKFILVLSLANTTLKDTDMRAHFKRLHLLYTNCLSNPFYELGKPLKSRALDEACNELFRSTPADMSGGFSGVVRLSNVNDYIAPSQACVIPLKPTLEQPAATEDEQLVSTHSKKPKTDKPVVKVSISLADCLACAGCVTSAETVLIEEQSVQRAIEGLRAAKLGVVTVSASSLASICTARGWTMEEGARRVTEFFRAKGARVVLDASVVQSLALRECWQEMRERIEQREKGGAHRPLLVSACPGFACYAEKSHGALLMPLMSRTRSSQGVAGVLVKEYLPRLIAASSNGPSLSPADIYHVAVMPCFDRKLEASRPENTAADGSRHVDCVLGTAELNGALSAFLEGREEEESMEVDESPELARVEEALPEEITGFMRGALLGLDGNLSGGYVEYGIDRWSAAKGGAVRVEETKAASNLDVIRVFSTRPGEEEERPFVAARVYGFRNIQNMVRKLKTGKKELEYDLVEVMACPSGCANGGGQIRAATTQERNRVTEGVERLYSNLPRQPTTVPSIDEFRASIEDEKMRMDLKDVGATVNANLAW
The following text describes a protein:
Function:
Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MMDIYVCLKRASWMVDNKRMRTASNFQWLLSTFILLYLMNQVNSQKKGAPRDLKCVTNNLQVWDCYWKAPSGTGRGTDYEVCIENRSHSCYQLEKTNIKIPALSHGDYEITINSLHDFGSSTSKFTLNEQNVSLIPDTPEILNLSADFSTSTLYLKWNDRGSVFPHHSNVIWEIKILRKESMELVKLVTHNTTLNGKDTLHHWSWASDMPLECAIHFVEIRCYIDSLHFSGRKEWSDWSPVKNISWMPDSQTKVFPQDKVILVGSDITFCCISQEKVLSALIGHTNCPLIHLDGENVAIKIHNISVSASSGTNVVFTTEDNIFGTVIFAGYPPDTPQQLNCETHDLKEILCSWNPGRATALVGPRATSYTLLESFSGKYVRFKRAEAPTNGSYQLFFQMLPNQEIYNFTLNAHNPLGRSESTILVNITEKVYPHTPTSFKVKDINSTAVKLSWHLPGNFAKINFLCQIEIKKSNTVQEQRNVTIKGVENSSYLVALDKLNPYTVYTFRIRCSTETFWKWSKWSNKKQHLTTEAIPSKGPDTWREWSSDGKNLIIYWKPLPINEANGKILSYNVSCSSDEETQSLSEIPDPQHKAEIQLDKNDYIISVVAKNSVGSSPPSKIASMEIPNDDLKIEQVVGMGKGILLTWHYDPNMTCDYVIKWCNSSRSEPCLMDWRKVPSNSTETVIESDQFRPGVRYNFFLYGCRNQGYQLLRSMIGYIEELAPTVAPNFTVEDTSADSILVKWEDIPVEELRGFLRGYLFYFGKGERDTSKMRVLESGRSDIKVKNITDISQKTLRIADLQGKTSYHLVLRAYTDGGVGPEKSMYVVTKENSVGLIIAILIPVAVAVIVGVVTSILCYRKREWIKETFYPDIPNPENCKALQFQKSVCEGSSGLKTLEMNPCTPNNVEVLETRSAFPKIEDTEIISPVAERPEDRSDAEPENHVVVSYCPPIIEEEIPNPAADEAGGTAQVIYIDVQSMYQPQAKPEEEQENDPVGGAGYKPQMHLPVNSTVEDIAAEEDLEKTAGYRPQANVNTWNLVSPDSPRSIDSNSEIVSFGSPCSINSRQFLIPPKDEDSPKSNGGGWSFTNFFQNKPND
The following text describes a protein:
Function:
Sodium-independent anion exchanger mediating bicarbonate, chloride, sulfate and oxalate transport. Exhibits sodium-independent sulfate anion transporter activity that may cooperate with SLC26A2 to mediate DIDS-sensitive sulfate uptake into high endothelial venules endothelial cells (HEVEC). In the kidney, mediates chloride-bicarbonate exchange, facilitating V-ATPase-mediated acid secretion. May function as a chloride channel, playing an important role in moderating chloride homeostasis and neuronal activity in the cerebellum.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein.
Sequence:
MTERAWRYILGMVQKRLPILEWLPHYSLKWLQLDSIAGLTVGLTVVPQALAYAEVAGLPVQYGLYSSFMGCFVYFFLGTSRDVTLGPTAIMSLLVSFYALHQPTYAVLLTFLSGCIQLAMGILHLDFLLEFISYPVIKGFTSAASITIGFGQIKNLLGLHDIPQQFFFQVYYTFLKVGQTRLGDTILGLVCIVLLLLLKAMRDQVPPLHQQMPRCVRLSHIIVWSITTARNALVILFAGLIAYSFQVMGSQPFLLTGKTAEGLPPFQLPPFSEATSNGTVSFIQMVQDMGAGLAVVPLMALLESITIAKTFASQNSYHIDSNQELLAIGLTNLLGSFVSSYPVTGSFGRTAVNAQTGVCTPAGGLVTGVLVMLSLAYLTPLFYYIPKAALAAVIITAVAPLFDAKILWTVWRVKRLDLVPMCVTFLFCFWEVQYGILAGILVSGMLLLYHVARPQIQQISKGPVLVLRPISGLHFPAVETLWKTVYNQALSASPPRCTILDCTHICNVDYTVMTGLGELLEEFQNHGASLVFAKLQAPVLFDLLSADLKGFQHFSTLEEAEKYLSEE
The following text describes a protein:
Function:
Probable component of a centromeric complex involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation.
Subcellular Localization:
Nucleus. Chromosome, centromere. Note=Localizes exclusively in the centromeres.
Sequence:
MEQKYEEDIQKLQQEIEMLEAEQEETLRSIFVQHGDRLQQGVKSACEERGGGGAQQHAVSKLITEVRELEKDLRRQTEINGITLNECFVKTLHKSERKLVQQLRLAGHCGLLLFQVEFAVTEIQEDNVLHRRVTELNIVVDGVEFKDFSAFVSRVEDTKDLLLFFRTLRTFSERCEDRRQTFQHFQEKYPDVVNLPEGCRSEIMIIRSPQLPGISMTLFWKIHVSKEGVVKPLLDLLLKMPDQALELDTKKVMEKGSDYFQSLLQLLGVEASIEGLIRAVCS
The following text describes a protein:
Function:
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Subcellular Localization:
Cytoplasm.
Sequence:
MRYTILTKGDSKSNALKHKMMNYMKDFRMIEDSENPEIVISVGGDGTLLQAFHQYSHMLSKVAFVGVHTGHLGFYADWLPHEVEKLIIEINNSEFQVIEYPLLEIIMRYNDNGYETRYLALNEATMKTENGSTLVVDVNLRGKHFERFRGDGLCVSTPSGSTAYNKALGGALIHPSLEAMQITEIASINNRVFRTVGSPLVLPKHHTCLISPVNHDTIRMTIDHVSIKHKNVNSIQYRVANEKVRFARFRPFPFWKRVHDSFISSDEER
The following text describes a protein:
Function:
Probable transcription factor that influences tracheary elements and xylem development by negatively regulating secondary cell wall fiber synthesis and programmed cell death.
Miscellaneous:
MISCELLANEOUS: Plants over-expressing NAC104 show severe dwarfism and suppression of tracheary element differentiation.
Subcellular Localization:
Nucleus.
Domain:
The NAC domain includes a DNA binding domain and a dimerization domain.
Sequence:
MNLPPGFRFFPTDEELVVHFLHRKASLLPCHPDVIPDLDLYHYDPWDLPGKALGEGRQWYFYSRKTQERVTSNGYWGSMGMDEPIYTSSTHKKVGIKKYLTFYLGDSQTNWIMQEYSLPDSSSSSSRSSKRSSRASSSSHKPDYSKWVICRVYEQNCSEEEDDDGTELSCLDEVFLSLDDLDEVSLP
The following text describes a protein:
Function:
Substrate adapter of E3 ligase complexes mediating ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, and which is involved in various processes, such as ribosome recycling and reticulophagy (also called ER-phagy).
Sequence:
MSDDLPIDIHSSKLLDWLVSRRHCNKDWQKSVVAIREKIKHAILDMPESPKIVELLQGAYINYFHCCQIIEILRDTEKDTKNFLGFYSSQRMKDWQEIEGMYKKDNVYLAEAAQILQRLAQYEIPALRKQISKMDQSVTDAIRKHSEYGKQAEDGRKQFEKEISRMQLKGVHLRKELLELAADLPAFYEKITAEIRKISAARDYFQAFRDYMSLGAAPKDAAPILPIIGLIGERGLDVTTYEWKYNQKPDKVEKPNFEMLLTAAEDSDEIDFGGGDEIDFGIAAEDDAVIDFSAVVDLVADDTGAVGEAIASGQDALHLLENSEAQKAVKHELIELLAFLSMRLDDETRETTADVLIRGAEKRPDGVAAVTEKRLKTWITEVEGILKELENPQKVHLFKIRGSPQYVEQVVEELEKKRDMEHRYKRLQTLMTENQETARQSVTKSNVELKTIVESTRVLQKQIEAEISKKYNGRRVNLMGGINQALGGN
The following text describes a protein:
Function:
Transcription factor that is part of a SLN1-YPD1-SKN7 two-component regulatory system, which controls gene expression in response to changes in the osmolarity of the extracellular environment. Under low osmotic conditions, phosphorylated and activated by the phosphorelay intermediate protein YPD1. Also activated in response to oxidative stress, independent on the two-component regulatory system. Regulates heat shock genes in response to oxidative stress and genes involved in cell wall integrity in response to osmotic changes.
Subcellular Localization:
Nucleus.
Domain:
Homotrimerization occurs through formation of a three-stranded coiled-coil structure generated by intermolecular interactions between HR-A/B regions allowing DNA-binding activity.
Sequence:
MSSLQQPIPPNSTLATTASSNQSGSNDFVKKLFLMLQEDSYKEVVRWTVKGDSFVVINTNEFTKDILPKHFKHSNFASFVRQLNKYDFHKVKISNEAKASYPYGEDAWEFKHPEFRINDAEALENIKRKGPTAKKSASNVTIKTEANNNGTQPTCNHNYSQLVSATNHLKEQVESLKNDKHSLYQEISVLERKYKTVVENIVAINTFNERYYRSMNVLINSIVQNGMKLPPLDFPPPVQLGPDSGIGSNLGPISSDTALPSISHHLSSPLPHHQQLLNRTIRPISSPIDGIPLVKLQQQSLGQNLQAPIGTPSAVPFSEEASSSIQAATPAPLAQPVAQPINQPPPPPPPPATQQQPLPPPPPPATATSQIPSAPPPPTQQQVGTSSSSVPTISPKSQGIVVSNSASPTTSAQISTTSVPNPKFHVLLVEDDNVCIQLCRKFLVKYGCSVTVVTDGLNAISTVEHTKYDLVLMDIVMPNLDGATATSVIRSFDTKTPIIAMTGNIEDNDLVTYLQNGMSDILAKPFTKDDLYAILSKHLLDPKENKQDNEPTVKKQKLS
The following text describes a protein:
Function:
Component of the DASH complex that connects microtubules with kinetochores and couples microtubule depolymerisation to chromosome movement; it is involved in retrieving kinetochores to the spindle poles before their re-orientation on the spindle in early mitosis and allows microtubule depolymerization to pull chromosomes apart and resist detachment during anaphase. Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and microtubules. Kinetochores also serve as an input point for the spindle assembly checkpoint, which delays anaphase until all chromosomes have bioriented on the mitotic spindle.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore.
Sequence:
MQSLEQCVNSLEAIVHQLDGSVSRLARNGEASNELCEGILKIKRVFELVPEYDVESARLALFEEVDPMVKTLGDKIEKALIRKRRELENLRQTSELNSLRLSGDLYFSETGIDNQDMDVSTDAIAIASATDAELDELRALKARRAELQELLDGR
The following text describes a protein:
Function:
Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
Sequence:
MVKALLVGSKVLVPSIDESRYLYSNGFYGKPIGISKPKGPKDIVRPLELSLIESVYLTKKGLINVVDKNGDLLEYKKLYEYSAMKINKFEILYKVYEDLREKGFIVRSGVKYGADFAVYTLGPGLEHAPYVVIAVDIDEEITPHELLSFGRVSHSTKKRLVLALVDRKSEGIRYIMFKWVKM
The following text describes a protein:
Function:
Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP (By similarity).
Miscellaneous:
MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion.
Sequence:
MNIGGGKFLLGRISNNPTSGIVGLANVGKSTFFQAITNSKLGNPANYPFATIDAECAKVNIPSVPLSNLLRIYQSAKCVPGTLTIYDIAGLTRGASQGHGLGNKFLNDIRHVEGIFQVVRGFLKEDITHIEGNVDPVRDLSVVQDELILKDLEFLENIRERLSKKMRMVSKNSKEHQEMKIETELLDALEEHLFNGKKIRHFKDHWNLDEVKILNKHNFLTSKPTLILLNVSPQDYVRNENKFVRNIIEWINEFSPGDKFLLFSAEFESQLMECKGIASEYFDKIKEDTNVSDQQLVSAIPQIILEMRKLLNLISFFTCGPQEVHQWNIREGTTAQEAAGVIHSDLRETFISADVIKYDDLKKMEPPLNESLLKSKGLIKRAGKQYIMQDNDIALFKAAGGKIKK
The following text describes a protein:
Function:
Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Domain:
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding; The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
Sequence:
MRLKIGFILRSLLVVGSFLGLVVLWSSLSSRPDDQSPLSRMREDRDVNNPLPNRGGNGLAPGDDRFKPVVPWPHVEGVEVDLESIRRKNKAKNEQERHAGGDSQRDVMQRQYLTFKPQTFTYRDPVLRPGVLGNFEPKEPEPHGVVGGPGEKAKPLVLGPEYKQAVQASIKEFGFNMVASDMISLDRSVNDLRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWYAPLVAPISKDRTICTVPIIDVISGNTYEIIPQGGGDEDGYARGAWDWSMLWKRVPLTSREKRLRKTKTEPYRSPAMAGGLFAIEKDFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLLFVPCSRVGHIYRLEGWQGNPPPLYVGSSPTLKNYVRVVEVWWDEYKDYFYASRPESKALPYGDISELKKFREDHNCKSFKWFMEEIAYDITAHYPLPPRNVEWGEIRGLETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGPDGSKVMITHCNLNEFKEWQYFKSLHRFTHITSGKCLDRSEVLHQVFISTCDSSKMTQKWEMNNIHSV
The following text describes a protein:
Function:
Catalyzes the decarboxylation of L-aspartate to produce beta-alanine.
Sequence:
MTRGEARRPPQEFDRVLSSMCTTPHPAAREAAQAFLATNPGDPETYPAVAERERDAVALLGEIVGLSSPHGYIAAGGTEANLQAVRAARNRADADAVNVVAPASAHFSFQKAADVLGVELRLAPTDGDHRADVAAVADLVDGDTAVVVGVAGTTEYGRVDPIPALADIAAGVDANLHVDAAWGGFVLPFTDHDWSFADAPVNTMAIDPHKMGQAPVPAGGFLARDPETLDALAIETPYLESDTQPTLGGTRSGAGVAGALASLRALWPDGYREQYERTQGNAEYLAAELAARGYDVVDPELPLVAADMPDAEFQALREEGWRISRTASDALRVVCMPHVTREMLAAFLDDVDALA
The following text describes a protein:
Function:
Specific and potent inhibitor of carboxypeptidase Y.
Miscellaneous:
MISCELLANEOUS: Present with 1030 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MNQAIDFAQASIDSYKKHGILEDVIHDTSFQPSGILAVEYSSSAPVAMGNTLPTEKARSKPQFQFTFNKQMQKSVPQANAYVPQDDDLFTLVMTDPDAPSKTDHKWSEFCHLVECDLKLLNEATHETSGATEFFASEFNTKGSNTLIEYMGPAPPKGSGPHRYVFLLYKQPKGVDSSKFSKIKDRPNWGYGTPATGVGKWAKENNLQLVASNFFYAETK
The following text describes a protein:
Function:
Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase (By similarity). May play a role as a transcriptional coregulator in various cellular pathways (By similarity). Catalyzes conjugation of SUMO2 to KAT5 in response to DNA damage, facilitating repair of DNA double-strand breaks (DSBs) via homologous recombination (HR) (By similarity). Mediates sumoylation of PARP1 in response to PARP1 trapping to chromatin (By similarity). Negatively regulates induction of interferon phi 1 (ifnphi1) mediated by mavs and ticam1/trif. Also inhibits ifnphi1-mediated activation of the interferon-stimulated genes (ISGs) pkz and cd40, and to a lesser extent rsad2 and isg15. May inhibit ticam1/trif-mediated activation of NF-kappa-B.
Subcellular Localization:
Nucleus.
Domain:
The LXXLL motif is a coregulator signature that is essential for transcriptional corepression.
Sequence:
MAAELVEAMNMVKSFRVSDLQTLLASMGRSKSGLKQDLVGRALRLVQTEYSPELLKNVRQLYETRFPKASAWLAARRPETVAVNYPALNSSPRGTGQGTDYLNGIPKPAPPPAAEVKLVPLPFYHNLETLLPPTELVAQNSEKLQESQCVFDLTPNQVDQIRNSSELRPGMKSVQVVLRICYTDSIGVQEDQYPPNIAVKVNQSYCHVPGYYPSNKPGVEPRRPCRPVNITPWLHLSTVTNRVTITWGNFGKRYSVAVYLVRVFTSGELFNQLKHCSVENPDRCRERIQDKLRFDPESEIATTGLRVSLICPLVKMRLGVPCRVLTCAHLQCFDAVFFLQMNEKKPTWTCPVCDKPAPFELLTIDGLLSEILKETPEDVEEIEYLTDGSWRPIRDDKEKERERENSRTPDYPVVDICVPEANGHSPAHSGTNQTGKSGSGGASAGTGSTSGGSGGGTVVDLTLDDSSEEEGGGGAEDSEETDDSQDSPAPKRGRYDYDKDLVTAY
The following text describes a protein:
Function:
Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Subcellular Localization:
Nucleus, nucleolus. Nucleus, nucleoplasm.
Sequence:
MVRSRSNSVKKDLKRKVDEPVDVQDEFDVEGLIDEGDSDDEDEAEQEVAQENVTKDKKNTSKTENEEDADDESDSDAELEALIGEEEDLSGSELEDELAYFSDAGDDEVDPSILKHLDDGVRLRSLSRSSDQTDELKDVVEIVPGADGKPRMIKKEIHAVYDSDDSDQEESNTIGNVPLSAYDQMPHIGYDINGKRIMRPATGSALDNLLETIDLPEGWTGLLDKSTGKGLNISKEELELIKRIQKNETTDDASNPYEDLVEWFSSKTEIMPLSAAPEPKRRFIPSKHEAKRVMKMVQAIRQGKLLTKPKEDPDARPNYDVWADNLTDVQDHVMTLRAPKMPPPTHDESYNPPAEYLPTEEEIAEWNALAPSERERNYVPKKYTALRHVPGYSESVRERFERSLDLYLAPRVRKNKLNIDPDSLIPDLPSPKDLMPFPIRCATTYKGHKGKVRAISVDPSGEFLATGGDDGTLRVWEVLTGRELYRCRLVASIDAQDDSVECVQWNPAVPGMLAASAGEHIFLIVPPTLFDFDIENTGREKIEQGWGFAEGGREQQDIDTKGLDDDADSDSDDETGHVKKKSPPAKWITPTAKQQASGIGAIITATKTIKRLAWHRKGDYLVTVAPSAQHRAVAIHQISKHSSQSPFNKSKGIVQDAMFHPFRPHLYVATQRYVRIYDLAKQVMAKKLMPGARWVSSLDIHPRGDNVILSSFDKRLLWHDLDLSDKPYKTLRYHEKAVRHAAFHKGGLPLFCSASDDGNINIFHGTVYDDMMTNPLLVPLKVLKGHDVKSGLGILRVEWHPREAWLFSAAADGTAKLWTT