lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of centriolar satellites contributing to primary cilium formation (By similarity). In complex with CFAP263, acts as a regulator of ciliary beating that connects radial spoke 3 (RS3) to the inner dynein arm (IDA) and the nexin-dynein regulatory complex (N-DRC). The complex is positioned parallel to N-DRC and forms a connection between the arch at the base of RS3, the IDA tail and N-DRC (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Cell projection, cilium. Note=Colocalized with HAP1 at centriolar satellites. Centriolar satellite localization requires PCM1 (By similarity). Localizes at cilium but not at the ciliary tips (By similarity).
Sequence:
MTDDDSETSASETQAQEESDLPVFQLCGLVEELSYGNSALKTETEMFEKYYNKLELKDQRPPRLSEIKITGAEIAQLRSRRKSKSRMGMERVMGLSVDQKLELVQKELEDTKDEIRHMRANAERDLQHHEAIIEEAEIRWTEVQKEVHDFEKDILKTISKKKGSILATQKVMKYIEDMNRRRDNMKDKLRLKNVSLKVQRKKLLLQLRQKEEVGEALHDVDFQQLKIENAQFLETIEARNQELIQMKLASGNTLQILNAYKRSSLLKTSRVVILQSKLHHAMQMSLNLTKEFLLRKELLEKIEKETLQAEEDRAKALALNKQLRKQLSEFRAPQVMIYIWEKIRNGDLEKTIRMWERKVEIAEMSLKGYRKAWNKMKTTNEQLQAISGPGK
The following text describes a protein:
Function:
May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus.
Subcellular Localization:
Cytoplasm, cell cortex.
Sequence:
MPGSRSSNNDNEHNRSPRESGEDSEDESEILEESPCGRWLKRREEVEQRDVPGIDCAHLAMDTEEGVEVVWNEVQFSERKNFKLQEEKIQLVFENLTQLEHPNIVKFHRYWTDTHNDKPRVIFITEYMSSGSLKQFLKRTKKNVKKLPLQAWKRWCTQILSALSYLHSCSPAVIHGNLTCDTIFIQHNGLVKIGSVAPDAIHHHVKTCRDNIKNMHFIAPEYGLSPTTTAIDVYSFGMCALEMAALEIQGNGDSGTLVTDEHIRRTVESLEDTQQKDFIIKCLSHDPAKRPSARELLFHSLLFEVHTLKLLAAHCLVNTSSSYDDVLQRIYKPDILYAEICRPNNVYKYHLGDIVATEKLDKFIEDVKYGIYPLTAFSAQKPPPTRPRALSPETAESVKSATPEPLDIETRRVVNMICSVKPRDVNCELFMTILLRMDDKMNRQLTCPISQDDSAVMLSHELVHLGFIHEMDREKIATMIDDTLRNHQLKLNDVTETVESTGALNPTSGSVAAIGSMPKPPLPAGASPVGGGGASSSIAGKSNHLHHHVPVHSASLERGWKVADTESMPSTMPAIVETSGVSVNSMIDGGNFAGHLDDAEEARENDEELEALERMVELRRFSREEAQATLLSNEQHDKIVPAKTCTPSNVLHHARPGAAETTDRNNTNRTSSTGAGAVNNVEPVASSKPIKP
The following text describes a protein:
Function:
Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVRHKNRYIIIEVTESPGDTRKPTNALKLNQNLLYRSIINMVQKLHGDFGVAACTAGFVLRYCNEKTRVAIIRCRHGPHKLVASSLPILKSIGTIDVHLNILYTGATMKHCFNFIQRYQQKKFDEFCVGLKTDEEKEELRREIMQLEPLLKMP
The following text describes a protein:
Function:
Proton-coupled metal ion symporter operating with a proton to metal ion stoichiometry of 1:1. Selectively transports various divalent metal cations, in decreasing affinity: Cd(2+) > Fe(2+) > Co(2+), Mn(2+) >> Zn(2+), Ni(2+), VO(2+) (By similarity). Essential for maintenance of iron homeostasis by modulating intestinal absorption of dietary Fe(2+) and TF-associated endosomal Fe(2+) transport in erythroid precursors and other cells. Enables Fe(2+) and Mn(2+) ion entry into mitochondria, and is thus expected to promote mitochondrial heme synthesis, iron-sulfur cluster biogenesis and antioxidant defense (By similarity). Can mediate uncoupled fluxes of either protons or metal ions.
Miscellaneous:
MISCELLANEOUS: Nifedipine induces duodenal iron accumulation and mobilizes iron from the liver of iron-overloaded mice.
Subcellular Localization:
[Isoform 1]: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein; [Isoform 2]: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein; Apical cell membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein. Extracellular vesicle membrane; Multi-pass membrane protein.
Sequence:
MVLDPKEKMPDDGASGDHGDSASLGAINPAYSNSSLPHSTGDSEEPFTTYFDEKIPIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWVLLLATIVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRIILWLMVELAIIGSDMQEVIGSAIAINLLSAGRVPLWGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYITVKPSQSQVLRGMFVPSCPGCRTPQVEQAVGIVGAVIMPHNMYLHSALVKSRQVNRANKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFEKTNKQVVEVCKNNSSPHADLFPSDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVILTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSEFSNGIGWRIAGGILVLIVCSINMYFVVVYVQELGHVALYVVAAVVSVAYLTFVFYLGWQCLIALGLSFLDCGRSYRLGLTAQPELYLLNTVDADSVVSR
The following text describes a protein:
Function:
Lipoamide dehydrogenase is an essential component of the alpha-ketoacid dehydrogenase complexes, namely the pyruvate dehydrogenase (PDH) complex, the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, and likely also the 2-oxoglutarate dehydrogenase (ODH) complex. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes. Is also able to catalyze the transhydrogenation of NADH and thio-NAD(+) in the absence of D,L-lipoamide, and the NADH-dependent reduction of quinones in vitro; Together with AhpC, AhpD and DlaT, Lpd constitutes an NADH-dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system; Appears to be essential for Mtb pathogenesis.
Miscellaneous:
MISCELLANEOUS: The active site is a redox-active disulfide bond.
Subcellular Localization:
Cytoplasm.
Sequence:
MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIFTKDAKAFGISGEVTFDYGIAYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTLLVDLNDGGTESVTFDNAIIATGSSTRLVPGTSLSANVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIADGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQLAHVAEAQGVVAAETIAGAETLTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVGHMINF
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated proteins and mediates their ubiquitination and subsequent degradation.
Subcellular Localization:
Cytoplasm, cytosol.
Domain:
The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
Sequence:
MNASTSSPSQQLQQAINSTIDKECAVCYSEMILPTTIPSCGHKFCFICLKGVSVSNNGDCPICRGPIDSQIFKKPLQAVDLKMDIPGTPSAAAPDPVVKQEVDDEDVKPDVKKLQEELKKQQAAAAAQKMFWLYRGRHQGWWRFDPRIEKEIEEAFTHQMPMTEVTICGNPYIVDFSQMCQYPKNQSNYSRNVKRVNSTDFDSLNVKGMSGVFVATTSPPAAAN
The following text describes a protein:
Function:
Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
Subcellular Localization:
Nucleus.
Sequence:
MEKKKKDTVKRKRKQKPSARELHRPRSSDANATFALLLASLSNTPHSVIFINKCLFKLRRFLLLSQTSMTPLLALLPTLLRSTRPELACRASDIIGAASLVSFDANEEFAFDSETVEGLISLFQSRIRKVLLSACNVVLDFSTTTFAQRQVLKFSALNKLMFVFLHIFNGLECARLWSECDESLHSLKIGIKEDELSLAFLSATVVLINACEVESIPQSLSEAFLRILKQIRVRVSDQEVIKGARKCNEEGRLYKSNIAASQPTGSLSFEVVQRGLFGASDTTSEDFISNYWEVSPFLLSRATRDPDMHDIFGAFVQSLNWNGRVPSLLSSILQHLVACFPIASDEQNILNFLNEVKDRLGCPIIYQQDIRAVKTERQSRKEMHYFRDFHSGCSKEPLYFTFDDVLKCGQAYKEGYTVALRGLEFCYQSIAAIADTLALMFGQPSVGANLYLTPPNSQGLVCHFDDHCVFVCQIFGSKQWTIFSPPSQLLPHLYDNLLGSDINCTKAGRREFFLREGDLLYIPRGFPHEAYTSSAVSDGSPGFSFHLTLSIEVEPPFEWGGVSHFALHCWSENQKRLLLHVAIGIISNFDPSFRKACLTAVVSLPPVVYNGLFQGQRNTFFYLIDKIRTESRFMEVLSSIEVAIQKNEDPFQQIRWLWVLCMEKETSSEYNTNKSFMIEDLLSLCAQHKDKFEAAFLNVKSRFCSEVVFEVVTSNRMLLQKCRNTRKQYINRMFLLHDKL
The following text describes a protein:
Function:
Cytochromes P450 are a group of heme-thiolate monooxygenases.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Sequence:
MLASGLLLVALLASLTVMVLMSVWQQRKSRGKLPLGPTPLPFIGNYLQLNTEQICDSIMKISERYGPVFTIHLGPRRVVVLCGHDAIKEALVDQAEEFSGRGEQATFKWVFKRCGEGRTKPLRRFSIATLRDFGVGKRGIKEKAGFLIKVQDTPSVEAGEGKRPGIDPTFFLSCTTSNVISSIFTATSTGQLYEMFSSVMKHLPGPQQQAFKELQGLEDFIAKKVEHNQCTLDPNSPWDFIDSFLICMQGEEKNPNTEFYLKNLVMTTLNLFYAGTETVSTTLHYGFLLLMKHPEVEAKVHEEIDRVIGKNQQPKFEDRAKTLYTEAVIHEIQRFGDLLPMGVARRVKKDTKFRDFFLSKGIEVFPMLGSVLRDLRFFSNPRDFNPQHFNPQHFLGEKGQFKKRDAFVPFSIRRRNCFREGLARMELFLYLTTIMQNFRFKSRQSPKDIVVSPKHVGFVTVPRNYTKSYLPC
The following text describes a protein:
Function:
Required for host-cell death and may support an EsxA-independent virulence function. Secreted processed form of EspB binds to phosphatidic acid and phosphatidylserine. Inhibits IFN-gamma-induced autophagy in murine macrophages.
Miscellaneous:
MISCELLANEOUS: BTP15, an inhibitor of ESX-1 secretion, decreases secretion of this protein without being bacteriocidal. BTP15 inhibits autophosphorylation of MprB with subsequent up-regulation of espA and decreased secretion of EspB and EsxA.
Subcellular Localization:
Secreted. Note=Secreted via the ESX-1 / type VII secretion system (T7SS). Secretion requires both EspK and EccCb1, but not EspA, EspC and EspD.
Domain:
The N-terminal region contains a fused PE/PPE homology domain. The C-terminal region is disordered.
Sequence:
MTQSQTVTVDQQEILNRANEVEAPMADPPTDVPITPCELTAAKNAAQQLVLSADNMREYLAAGAKERQRLATSLRNAAKAYGEVDEEAATALDNDGEGTVQAESAGAVGGDSSAELTDTPRVATAGEPNFMDLKEAARKLETGDQGASLAHFADGWNTFNLTLQGDVKRFRGFDNWEGDAATACEASLDQQRQWILHMAKLSAAMAKQAQYVAQLHVWARREHPTYEDIVGLERLYAENPSARDQILPVYAEYQQRSEKVLTEYNNKAALEPVNPPKPPPAIKIDPPPPPQEQGLIPGFLMPPSDGSGVTPGTGMPAAPMVPPTGSPGGGLPADTAAQLTSAGREAAALSGDVAVKAASLGGGGGGGVPSAPLGSAIGGAESVRPAGAGDIAGLGQGRAGGGAALGGGGMGMPMGAAHQGQGGAKSKGSQQEDEALYTEDRAWTEAVIGNRRRQDSKESK
The following text describes a protein:
Function:
Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments. Plays a role in lamellipodial protrusion formations and cell migration.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane. Cell projection, lamellipodium. Note=Found on macropinosomes. Colocalized with heterodimeric capping protein (CP) and F-actin in lamellipodia but not with F-actin in stress fibers.
Domain:
The C-terminus is necessary for localization to the cell membrane.
Sequence:
MTEESSDVPRELIESIKDVIGRKIKISVKKKVKLEVKGDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVVCSKSAQMIVETEKCSISMKMASPEDVSEVLAHIGTCLRKIFPGLSPVRIMKKVSMEPSERLASLQALWDSQTVAEQGPCGGFSQMYACVCDWLGFSYREEVQWDVDTIYLTQDTRELNLQDFSHLDHRDLIPIIAALEYNQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRTDFAQKLASALAHNPNSGLHTINLAGNPLEDRGVSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSANPLTASTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDLSNTECSLDMVCGALLRGCLQYLAVLNLSRTVFSHRKGKEVPPSFKQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNLKGVSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIVWLSKNRSIQHLALGKNFNNMKSKNLTPVLDNLVQMIQDEESPLQSLSLADSKLKTEVTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMPIPMYDASQALKTNPEKTEDALQKIENYLLRNHETRKYLQEQAYRLQQGIVTSTTQQMIDRICVKVQDHLNSLRNCGGDAIQEDLKSAERLMRDAKNSKTLLPNLYHVGGASWAGASGLLSSPIQETLESMAGEVTRVVDEQLKALLESMVDAAENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSHCHHKLADHFSRRGKTLPQQESLEIELAEEKPVKRSIITVEELTEIERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEMEFDLDKALEEVPIHIEDPPFPSLRQEKRSSGFISELPSEEGKKLEHFTKLRPKRNKKQQPTQAAVCAANIVSQDGEQNGLMGRVDEGVDEFFTKKVTKMDSKKWSTRGSESHELNEGGDEKKKRDSRKSSGFLNLIKSRSKSERPPTILMTEEPSSPKGAVRSPPVDCPRKDTKAAEHNGNSERIEEIKTPDSFEESQGEEIGKVERSDSKSSPQAGRRYGVQVMGSGLLAEMKAKQEKRAACAQKKLGNDAVSQDSSSPALSGVERSDGGGAVPKLHPGLPENRFGLGTPEKNTKAEPKAEAGSRSRSSSSTPTSPKPLLQSPKPSLAARPVIPQKPRTASRPDDIPDSPSSPKVALLPPVLKKVPSDKERDGQSSPQPSPRTFSQEVSRRSWGQQAQEYQEQKQRSSSKDGHQGSKSNDSGEEAEKEFIFV
The following text describes a protein:
Function:
Assembly factor required for Rieske Fe-S protein UQCRFS1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MAASLRAEVLKCFRCLHRTRTKVFTNDQVAMDAARLKINSEFRKYQRISSQEAIAELIKLGHQAEEILRTSVVQVTPTAENTFRLHITKDTFMHNNTPYRG
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. This sigma factor is involved in the transition to post-exponential phase in the beginning of sporulation. It is also required for transcription of several stationary phase genes. Association with the RNAP core increases rapidly in early exponential phase, and reamins constant expression level after.
Sequence:
MNLQNNKGKFNKEQFCQLEDEQVIEKVHVGDSDALDYLITKYRNFVRAKARSYFLIGADREDIVQEGMIGLYKSIRDFKEDKLTSFKAFAELCITRQIITAIKTATRQKHIPLNSYASLDKPIFDEESDRTLLDVISGAKTLNPEEMIINQEEFDDIEMKMGELLSDLERKVLVLYLDGRSYQEISDELNRHVKSIDNALQRVKRKLEKYLEIREISL
The following text describes a protein:
Function:
Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May be involved in neurite formation. Inhibits protein phosphatase 1-alpha activity. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction.
Subcellular Localization:
Cytoplasm, cytoskeleton. Synapse, synaptosome.
Domain:
Interacts with p70-S6K via its PDZ domain; The PP1 binding region is natively unstructured, upon PP1 binding, it acquires structure, blocks a substrate-binding site, and restricts PP1 phosphatase specificity to a subset of substrates.
Sequence:
MLKAESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKPDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPNENAAIIAKTRGKGRPSSPQKRMKPKEFVEKTDGSVVKLESSVSERISRFDTMHDGPSYAKFTETRKMFERSGHESGQNNRHSPKKEKAGEAEPQDEWGGSKSNRGSSDSLDSLSPRTEAVSPTVSQLSAVFENSESPGAITPGKAENSNYSVTGHYPLNLPSVTVTNLDTFGRLKDSNSRPSSNKQATDTEEPEKSEAVPVPEVAQKGTSLASLPSEERQLSTEAEDVTAQPDTPDSTDKDSPGEPSAESQAMPKSNTLSRPKEPLEDAEANVVGSEAEQPQRRDLTGGGDLTSPDASASSCGKEVPEDSNSFEGSHVYMHSDYNVYRVRSRYNSDWGETGTEQDEGDDSDENNYYQPDMEYSEIVGLPQEEEIPANRKIKFSCAPIKVFNTYSNEDYDRRNDDVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVGADAGLEKLGIFVKTVTEGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGNVRFVIGREKPGQVSEVAQLISQTLEQERRQRELLERHYAQYDADDDETGEYATDEEEDEVGPILPGGDMAIEVFELPENEDMFSPSDLDTSKLSHKFKELQIKHAVTEAEIQKLKTKLQAAENEKVRWELEKNQLQQNIEENKERMVKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIRRQEVERKKLEEVEKAHLVEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRPSPGEVSKGDTMENVEVKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPTRTRLYDSVSSTDGEDSLERKNFTFNDDFSPSSTSSADLSGLGAEPKTPGLSQSLALSSDESLDMIDDEILDDGQSPKHTQSQSRAVHEWSVQQVSHWLVGLSLDQYVSEFSAQNISGEQLLQLDGNKLKALGMTSSQDRALVKKKLKEMKMSLEKARKAQEKMEKQREKLRRKEQEQMQRKSKKSEKMTSTTEQP
The following text describes a protein:
Function:
Core regulatory subunit of the histone H2A phosphatase complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.
Miscellaneous:
MISCELLANEOUS: Present with 7010 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSLPGTPTTSPTPMDEDTEQAVSVNTEPKRVKVYILENNEWKDTGTGFCIGEVDEGKFAYLVVSDEDSPTETLLKSKLEGNIEYQRQEETLIVWKDLGGKDIALSFEESMGCDTLCEFIVHVQRNIESNISLVTVKSSDNGLGSVHDIITGPVTLPSNDQQQNSQTLLEALKILNENTSFDFLKNETIEFILQSNYIDTLISHFHKAEEEKIPKDLFLLSNIIKTLILYNKRDILESMVEDDRIMGIVGILEYDTEYPTSKANHRKYLGSKGPNFKEVIPLENEDLKIIMKKCFRLQFLKDVVLVRFLDDHNFNLISEIVMDLETCIIDFLQVGTFLDRLIELYDTKTLPESSSEKEKFVQKRKDGIRLLQQCVQMSINLDAVDRSKFYKTLVRKGLFKVLDYAFHMETDSNVRILATDTIITIIEHDILLIHNVQNEDSFKRQHKSAPDDKSSHRKYPQDYSSSTDSKLLLILSTILLSDRSPGLREQVVQALNTLLHPEGCVGNGEGSYDLMGRSNYEAKNTSEDFPSFSYGLNSDSINLNNYHYSSDEMNNLEPESESEFQVMEYFANFYNKIAPILFGPLIKKDITTEMAEIDGQIEKVTKDDLLLIHLVKLVSFVCTEHDRVLSRRFILENGILDSVSKLIGGNHMMQLRLTAVRCIKNLMCLDDKYYHRYMISKNLYAPVFKLFQENIDKNNLANSCIQDFFRIIITECRAYQSDGHNRKEKTNGSYDGNGNDVKTNVNNNRTNFTILNKYLVQTYGDVLRKATDIPFIQDMLETGEENQPDHSSFENSIEGGNDISVNMSTDGFASNHLEDIDIKNVKRLHSEIEHFENDPHYSGDQLAFKKSVDQMNAST
The following text describes a protein:
Function:
Catalytic subunit of the glycosylphosphatidylinositol-mannosyltransferase I complex which catalyzes the transfer of the first mannose, via an alpha-1,4 bond from a dolichol-phosphate-mannose (Dol-P-Man) to the glucosaminyl acyl phosphatidylinositol (GlcN-(acyl)PI) intermediate to generate alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol and participates in the sixth step of the glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAWRKFVSLDYKVHLLVSLVVRLALVAYGVYHDQVSSVPYTDIDYKVFTDAARHVLDHKSPFERHTYRYSPLVAYLMIPNITLHSSFGKILFCIIDLIDATLIRIIVKTTLHEYFKYVGEPQNCITGRSRKKTKTKKNDQTDTTANLSLVVWLYNPLTLAIATRGNCDSIAVFFVLATLYLLQCRKQYFAAGLIHGLSIHFRLYPIVYSLTFYMYLSKFSFYSLEDRRKSHLREITGASDGRVATRKPERKTIFKRKYLLYLVPNFDQIRLVQGCILSLFSLIGIFYFLYGYKFVYETYLYHFTRKDTRHNFSLYFYLQYLTAWIKNIGIWQKVLVVLPQLVLLLVFSFRYGLNRFSLNFSVLAQTIVMVTYNSVLTSQYFVWIMAVLPLCLWQIRMSVNNAIFLVVVWFAAQGAWLLPAYFLEFHGQNTFLFIWIQSVSFFCANIAILGRLIMFFAPVKKEV
The following text describes a protein:
Function:
Molecular adapter that stimulates membrane curvature formation and subsequent endoplasmic reticulum exit site (ERES) establishment by recruiting PI3K complex I, leading to COPII vesicle-mediated transport. Promotes endoplasmic reticulum (ER) exit of cGAMP-activated STING1 oligomers.
Sequence:
MPKVISRSIVCSDTRDKEEYEGEKPLNVYYCLCGQMVLILDCPLEKLPLRKRDNARVIDGSKHAHKVTAEPGETVFLKWPDGIERQYRQKCKKCGLRLYYRHEEKGGTVTFVVSGAVVKEGKGVRKADIYQQVAAEAKPKKVMMTKRTKDMGKFSSVTVSTVDEEEEEIEAREVADSYASNARVIEKQLERKGMVKRKLQEMATEHERKKAKGTLIDK
The following text describes a protein:
Function:
Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.
Miscellaneous:
MISCELLANEOUS: Present with 2970 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSMQQVQHCVAEVLRLDPQEKPDWSSGYLKKLTNATSILYNTSLNKVMLKQDEEVARCHICAYIASQKMNEKHMPDLCYYIDSIPLEPKKAKHLMNLFRQSLSNSSPMKQFAWTPSPKKNKRSPVKNGGRFTSSDPKELRNQLFGTPTKVRKSQNNDSFVIPELPPMQTNESPSITRRKLAFEEDEDEDEEEPGNDGLSLKSHSNKSITGTRNVDSDEYENHESDPTSEEEPLGVQESRSGRTKQNKAVGKPQSELKTAKALRKRGRIPNSLLVKKYCKMTTEEIIRLCNDFELPREVAYKIVDEYNINASRLVCPWQLVCGLVLNCTFIVFNERRRKDPRIDHFIVSKMCSLMLTSKVDDVIECVKLVKELIIGEKWFRDLQIRYDDFDGIRYDEIIFRKLGSMLQTTNILVTDDQYNIWKKRIEMDLALTEPL
The following text describes a protein:
Function:
DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. May have low 3'exonuclease activity and may be able to remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSTLEPEKRRQHEDKSNEIIDSPIFLNKISALPESENVHCLLLKQLIGSPQLKQTWQFNFCVDLNFLLENMHASVFPTVDVRITHGYDSKSDSLARLTAQMNHCPVNVKLYSVYVPMWGTHHSKIMVNFFKDDSCQIVIHTANLVEPDWIGMSQAIFKTPLLYPKANDSLSTSSVPEYGNPSKIRKHEGSLDIKDDRNCDIIDVDSAFENFKHKSDTRSSDDLGVIGRQFQQDFLAYLKNYRHTYELIEKLKMYDFSAIRAIFIGSVPGKFEGEEESSWGLGKLKKILKMLEKDSKKDEKTKFEESDICISQCSSMGSFGPKQEYIAELTDGFGCQRGNWKFLFPTVKEVQQSMLGWQSGSSIHFNILGKTAASQVETLKKGKNLCKWVAMKAGRQRVAPHIKTYMRFSNDGELLRWVLVTSANLSKPAWGTLEGHKAKSRSTRGLRIRSYEAGVLLYPKLFEESQRAPCIMTPTYKTNTPNLDEKRREFYGKRVIGVRMCWDFPPVEYEDKDEIWSPVINRTDKDWLGYVWPPNW
The following text describes a protein:
Function:
Probable transcriptional regulator.
Subcellular Localization:
Nucleus.
Sequence:
MEESNNFLLSPDSIWSQLLENSYALNEINCFQSFGTIDNNNNNYSNNNKNGNEELSQPTEIQQQLQNYQELQQQKYQERQQQYQTQYQQPYIEPIFEIVVTQQDQQELIPQQQQQEQDQQEDQDQEQEQELQQQQQQLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQKQQKQQKQQQQEQPSIIKEQDQEQKKIIQEQLCEKSIQTLENHFFNTNTPKLDHQILSNYSEFFKINQPITDIPTTLNTNLQSDNNNNNNNNNNNNNNNNNNNNNNNNNNNLLNEKQIESTSKIKRINLGYDITKITFNKIEKGKRNQTESSKNFRERKKEYIKDIELKLKELTIENDKLKKENDTLKKIGIEIMRSEPESINMIMECKKIIKKLEKALIDNDERSLIYLLYLYHSETSKRYSLTEIEVDKIINPYSQLKLKLAGYIQNPTTEILDIFGGNNNNNNNNNNNNNNNNNNNDNDDDNEEEEISWFKKYKKEANLTIEQSNKLDLLRDYHCLKFELLLKERRELDRDIKKLYNGIALSGFDLTPRSLANWDIDKQIETTNKLNLLKIKIISSLNLNLDTFSSISSILSPKQEALLLVRAHLFGSNKKNPHIEILNNVWTGLISKSSSPSFFEIAKLLKEMSDSANAKIMEDYLYKK
The following text describes a protein:
Function:
Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA.
Subcellular Localization:
Nucleus.
Sequence:
MKFLELPDLEAINSSLNFDADDCRVRGKCEIYTTKSTVADKKLYKTLETRYQEDMMALSTSKSPEFVNSWTQPSPFGNLDQSSTRRTFMFILATLNASHPDHDFSSLQPNDFYKERFLSHVIESINTTLSNLGRRFSANGMWEVIDRHIVLSDCDIYSYTPDSDSDPYGDGALIWSQSYFFFNRNMKRILYISLHGFRMPIDGHGPGDEEAFSTPGLVESDSEDGYNDEWIANMDD
The following text describes a protein:
Function:
Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status.
Sequence:
MAFLVRGSINSVRSWSRSYASMSKKGLVLGVYSSEGKDEVKFTPYAQKYNESTAGKLLEQINICGPVKAGQTRIFWELGKFPAVAVAGLGDASKWDELDEIDGAKENVRIAAAAGVRALSANKIAEIAVEDMEHPQQAAEGATLANYKFQAFKSKEKQTPLPAVSFAEDASGKADWDRGVIIAEAQNFARVLMETPANHMTPTIFADTVKQRLGAANVEVVVHDEAWAKEKKMGSFLSVTNGSNEPARFLELTYRGSQDEQCVALVGKGITFDSGGISLKPSANMDQMRADMGGAANVVSTILALAQLKAPVHVKGFVPLCENMPSGTATKPGDVVYAMNGKSICVDNTDAEGRLILADALCYASTFNPKFILDIATLTGAIKVALGDCVSGVFSSNNKLWETIHEAGSQTGDRVWRMPLFKHYSDQMCDHNGYDLNNLGKGKGGGSCTAAAFLREFVPKGTPWLHVDIAGVMGDCSDQSYTGSKGMSGRPMRTLVEFVTKAGSA
The following text describes a protein:
Function:
Involved in homologous recombination where it functions at an early stage of recombination in a pre-recombinogenic complex with rlp1 and sws1. Also has a role at a later stage of recombination in association with the rhp55-rhp57 complex.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MNQVTQFSGNSANLMLYWILKSYYSRFDRIMWIDTLGTFNPAALPLPCLEKTMLVRSFDAQGLKDAVDELESNLKSSEDQAYALCIDSFSNPIGLLMAQGNISFAHAFMMTLGRKCRILTRKFRLAVYLSTSLVYIKQLHLSKPALGNSWPFCLDHSYILEDQQHNKCLVHCNQSRKDLLGCSQLFLLLKGSFTHEYLTIDFYNGTPVSVSSKLHVSPSLYHSSTLNSPS