lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the cylindrical core that assembles on the inner surface of the capsid during capsid formation and plays a role in viral DNA ejection into the host cell. The inner core is composed of stacked rings of gp14, gp15 and gp16 proteins. Following binding to the host cell surface, the internal core is diassembled and gp16 is ejected along with gp14 and gp15 into the infected cell. Gp16 probably inserts in the host inner membrane and remains associated with gp15. The gp15-gp16 complex binds to both the viral DNA and the host inner membrane, probably escorting the leading end of the genome through the periplasm and controlling the extend of DNA translocated into the host cell. Functions as an exolysin that catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycans allowing the local digestion of the bacterial peptidoglycan wall.
Subcellular Localization:
Virion. Host cell inner membrane; Single-pass membrane protein. Note=The gp15-gp16 complex spans the periplasm and the cytoplasmic membrane.
Domain:
The N-terminus contains the transglycosylase activity (Potential). The C-terminus is essential for the viral DNA translocation into the host cytoplasm.
Sequence:
MDKYDKNVPSDYDGLFQKAADANGVSYDLLRKVAWTESRFVPTAKSKTGPLGMMQFTKATAKALGLRVTDGPDDDRLNPELAINAAAKQLAGLVGKFDGDELKAALAYNQGEGRLGNPQLEAYSKGDFASISEEGRNYMRNLLDVAKSPMAGQLETFGGITPKGKGIPAEVGLAGIGHKQKVTQELPESTSFDVKGIEQEATAKPFAKDFWETHGETLDEYNSRSTFFGFKNAAEAELSNSVAGMAFRAGRLDNGFDVFKDTITPTRWNSHIWTPEELEKIRTEVKNPAYINVVTGGSPENLDDLIKLANENFENDSRAAEAGLGAKLSAGIIGAGVDPLSYVPMVGVTGKGFKLINKALVVGAESAALNVASEGLRTSVAGGDADYAGAALGGFVFGAGMSAISDAVAAGLKRSKPEAEFDNEFIGPMMRLEARETARNANSADLSRMNTENMKFEGEHNGVPYEDLPTERGAVVLHDGSVLSASNPINPKTLKEFSEVDPEKAARGIKLAGFTEIGLKTLGSDDADIRRVAIDLVRSPTGMQSGASGKFGATASDIHERLHGTDQRTYNDLYKAMSDAMKDPEFSTGGAKMSREETRYTIYRRAALAIERPELQKALTPSERIVMDIIKRHFDTKRELMENPAIFGNTKAVSIFPESRHKGTYVPHVYDRHAKALMIQRYGAEGLQEGIARSWMNSYVSRPEVKARVDEMLKELHGVKEVTPEMVEKYAMDKAYGISHSDQFTNSSIIEENIEGLVGIENNSFLEARNLFDSDLSITMPDGQQFSVNDLRDFDMFRIMPAYDRRVNGDIAIMGSTGKTTKELKDEILALKAKAEGDGKKTGEVHALMDTVKILTGRARRNQDTVWETSLRAINDLGFFAKNAYMGAQNITEIAGMIVTGNVRALGHGIPILRDTLYKSKPVSAKELKELHASLFGKEVDQLIRPKRADIVQRLREATDTGPAVANIVGTLKYSTQELAARSPWTKLLNGTTNYLLDAARQGMLGDVISATLTGKTTRWEKEGFLRGASVTPEQMAGIKSLIKEHMVRGEDGKFTVKDKQAFSMDPRAMDLWRLADKVADEAMLRPHKVSLQDSHAFGALGKMVMQFKSFTIKSLNSKFLRTFYDGYKNNRAIDAALSIITSMGLAGGFYAMAAHVKAYALPKEKRKEYLERALDPTMIAHAALSRSSQLGAPLAMVDLVGGVLGFESSKMARSTILPKDTVKERDPNKPYTSREVMGAMGSNLLEQMPSAGFVANVGATLMNAAGVVNSPNKATEQDFMTGLMNSTKELVPNDPLTQQLVLKIYEANGVNLRERRK
The following text describes a protein:
Function:
Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process.
Subcellular Localization:
Nucleus.
Sequence:
MSATNTNTTGATQEEQLPTQPEDLANFMDQIFSQMESKFTDMAQQVLKRIDEMSSKINELESSIDTLMQQAEQDK
The following text describes a protein:
Function:
Involved in anterograde intraflagellar transport (IFT) (Probable). Involved in flagellar assembly.
Subcellular Localization:
Cell projection, cilium, flagellum. Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton, flagellum basal body. Note=Localizes to the cytoplasmic and membrane-bound portions of each of the eight axonemes, localizing particularly at the flagellar pores and at the distal flagellar tips. Localizes at a lower level to the cytoplasmic axonemes and to the basal bodies.
Sequence:
MSSDNIKVIVRCRPLNARETRENALNIIRMDEASAQVIVDPPEQEKSATQAKKVPRTFTFDAVYDQTSCNYGIFQASFKPLIDAVLEGFNSTIFAYGQTGAGKTWTMGGNKEEPGAIPNSFKHLFDAINSSSSNQNFLVIGSYLELYNEEIRDLIKNNTKLPLKEDKTRGIYVDGLSMHRVTTAAELSALMDKGFANRHVAATQMNDTSSRSHSIFMVRIECSEVIENKEVIRVGKLNLVDLAGSERQSKTGATGETLVEGAKINLSLSALGLVISKLVEGATHIPYRDSKLTRLLQDSLGGNSKTLMCANISPASTNYDETMSTLRYADRAKQIKNKPRINEDPKDAQIRQLRDHIARLEAQLAEAQANGAKPMDVLRIGKSLMKAINGDELNLDGTFQGTAGAKLSEARDGDSEGESTEEEIVFVEDEASRKAADELEAKRRALAEAKQKRESELEQKEALNKEAIVTLTDLKSQLSAIKNSVFVVKQLEIKDKVLGKAQQKLTTRQEKHNALQQALQNKQTEHQTKTAEILSAVEKLERLKADISKTEAEINEVNQEIDDITEQHALSIEEERRELKEVDKRSALLDAIIQTFIPQCEVAKAEALAEYDEETMKWAISPEKVDREHQMLLKRVRHMQILYPSGSTKPVFFGKGKDTRALVNFSQLSGNILELEPELPERMTVGEEMDGYQSYGMNEDEMHDTQLQMFYSQIDTYE
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MTVSTLKYQQQLRGMERLSQMAGRRAWCSEDSALGQEEEDMSRPSKTVTFKDVAVDLTQEEWQQMKPAQRDLYRDVMLETYSNLVTVGCHVTKPDVIFKLEQEDEPWVLEEEMFWRRSPEAARGGMKSFLSKDMAKDLKFEDVVIYFSLEEWECLHHSHRNLYRAVMLDNYSNLLSLSLANMKPRVVSLLEQGKEPWMVMRNGTKVWCADWESKTETKNFLPKDSSKIKTSQQKMAKNCTRSSLEDSRARGNREVTCELESQQVHEERHLRQAVVPSVERPGSIQCTAHREAHPGGKPCRCEKCQKMLVRKAPPSEREQSHSKEKGSEYTQSGKVFNCTSDMAVHQRPQESRKGSESKKNAIPCGSDTPKPPGAQGSERPHKCKECGKAFQTPSQLSHHQKLHVGEKPFKCKECGKAFPSNAQLSLHQRVHTDEKCFECKECGKAFMRPSHLVRHQRIHTGEKPHKCKECGKAFRYDTQLSLHLLTHAGARRFECKDCDKVYSCASQLALHQMTHTGEKPHKCKECGKGFISDSHLLRHQSVHTGEKPYKCKECGKGFRRGSELARHQRAHSGDKPYKCKECGKSFTCTTELLRHQKVHTGDRPHKCKECGKAFIRRSELTHHERSHSGEKPYECKECGKTFGRGSELSRHQKIHTGEKPYKCKQCGKAFIRGSHLTQHQRTHTGQRSE
The following text describes a protein:
Function:
Transcriptional repressor required to restrict transcription of ECB-dependent genes to the G1/M phase by repressing their transcription during S late phase. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. Binds the IMEI regulatory region in vitro, its relevance in vivo is however unclear.
Subcellular Localization:
Nucleus.
Sequence:
MESRNTVLPSLPNIITGTSNSPFQLHTLPNTNFPSDDQGDIRLPPLAASAHIVRPVVNIYKSPCDEERPKRKSPQAVDFLSQRVTTSMTPLSKPKKLSSHSPFTPTVRVCSKEQPPQSMHSYKKVNILTPLSAAKAVLTPTTRKEKKRSFAFITHSQETFPKKEPKIDNARLARRKRRRTSSYELGILQTAFDECPTPNKAKRIELSEQCNMSEKSVQIWFQNKRQAAKKHKNSGNTSHCKVHSNDSMSMISYSDAALEITSTPTSTKEAITAELLKTSPANTSSIFEDHHITPCKPGGQLKFHRKSVLVKRTLSNTGHSEIIKSPKGKENRLKFNAYERKPLGEVDLNSFKN
The following text describes a protein:
Function:
Encapsidates the RNA.
Subcellular Localization:
Virion.
Sequence:
MSTARVKASEIEKLLSGGDADVVIESDETEGFNFKNFVVANEGIRMTFNNGYTILRNRAGIYKTIKSGKFTFQNKPIIIPSANVSPSQDDWTFRRLEGFIRARMLVELLETKNEKEKQKMYEKICGLPLVSAYGLKPSDKFDATTARIMLTLGGPFTLLASLDSFAAAALPLAYFQNVKKEALGISRFSTYEQLCKVARVMAAKEFKFTDRYKKIFDETVKILTKCTPGTSGAASLVKFNEQIQILEGAFGKIVEDIGQSSKPKNPSKNDRY
The following text describes a protein:
Function:
Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs; Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MRPPRGGGSFRGRGGRDGGGRGGGGRFNRGGGRFGGGGGGWRDEGPPDQVVEVATFVHASEGDAVTKLCQEKIPHFNAPIYLQNKTQIGKVDEIFGPINESLFSIKMMEGIVATSYTEGDKFYINPLKLMPLAKFLPQPKGQSTGGRGRGRGASRGRGGFSTRGAPRGRGGFSSFRGAPRGRGGFSRGRGRGGY
The following text describes a protein:
Function:
Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a 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. Increases AURKB activity. Inhibits apoptosis induced by TGFB1. Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Membrane; Single-pass type I membrane protein. Mitochondrion.
Sequence:
MSTPIRLSKPVLLYIFFTYSSLHCLSAAENSDVKSSGQAVTGSEECWLQEKYEVIEKCRPCKQFELTSNSVPVCSVTGYVERVSCKSSGEVYRSCHNMRAEENTFWMFEGVWFGVFVAGYAAVFLRQRILDSAATARVHKQIASSV
The following text describes a protein:
Function:
Involved in microhomology-mediated end-joining (MMEJ) DNA repair by promoting recruitment of polymerase theta (POLQ) to DNA damage sites during mitosis. MMEJ is an alternative non-homologous end-joining (NHEJ) machinery that takes place during mitosis to repair double-strand breaks in DNA that originate in S-phase. Accumulates in M-phase; following phosphorylation by PLK1, interacts with POLQ, enabling its recruitment to double-strand breaks for subsequent repair. Also involved in the DNA damage response (DDR) signaling in response to genotoxic stresses such as ionizing radiation (IR) during the S phase. Recruited to sites of DNA damage through interaction with the 9-1-1 cell-cycle checkpoint response complex and TOPBP1 in a ATR-dependent manner. Required for the progression of the G1 to S phase transition. Plays a role in the stimulation of CHEK1 phosphorylation.
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to sites of DNA damage in a H2AX-independent manner.
Domain:
The RAD1-binding motif mediates interaction with RAD1.
Sequence:
MPPRKKRRQAAQKPQLLFHQQPLEAPKHRCRFPQLPVVTHTRQVPSKPVDHNTITSWVSPQFDTTAESWFPGKRKHHHRDHARRSSRKSTSSRFPCLTFETPQSSASSATPGILASRDGPSQPEKDISGRPLVPMLSPQSCRELSAHTFPDFPCVFIPPDIQTPESPGQGEPIPSELRENSLPSCSLHTSTPKSPEPGPVLVTDTPEEKYGIKVTWRRRRHLFAYLRERGKLSRSQFLVKD
The following text describes a protein:
Function:
Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.
Sequence:
MDPTHQPFRLYAEVIVNANINKILDYGIPAELENLVTVGSVVKVPLQRKLTNDKYKIAIVLKIKSSSDFVHVIQPILDISYEGITLPQDLIDLIFWISQYYFCPLGSAVSLFLPTVYAQTHSTKHQNNVFLGQNAERTQEILKTLDNPQQIAVLRKLLKTTKPLTPPELMRKTEVSAKTLDALVKQKFIRIVDSADLEIQDEQLHYFLPDPPTLNQEQLDAVNTISQSLVAEQFQTCLLFGVTGSGKTEVYLQVIRKARALGKSVILLVPEVALTIQTLSFFKMHFGSEVGVLHYKLSDSERTQTWYKASRGLINIIIGPRSAIFCPIQNLGLIIVDEEHDSAYKQSDLPPFYQARDVAVMRGKMTNATVILGSATPSLESYTNALSKKYTLSVLSKRASTSTPTKVFLIDMNLEMEKTRKKPFFSQTVIRSIEQRLEVGEQTIIFFNRRGFHTNVSCSSCKYTLKCPHCDMILTFHKTERILLCHLCNTRLSKPITSCPQCLGTMTLQYRGAGTEKIETLLREFFPTARTIRLDSDTTRFRGSHDALVKQFATGKADILIGTQMIAKGMHFPAVTLSVVLSGDSGLYIPDFRAAEQVFQLITQVTGRSGRSHLPGEVLIQTFLPQNSTISHALAQDFPAFYKEEILGRKVCNYPPFTRLIRCIFLGKCSDYTLKETQRVHTLIKQNLDSQASLMEISPCGHFKVKDLFHYQFLIKTRNILVANKQIQEALAAAKLSSKVRCIVDVDPVTTFF
The following text describes a protein:
Function:
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Localization:
Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles.
Sequence:
MNPGSPAEPHPTPVAMSPPPSSDGFIASSSRAGSPNCPPTPLEKPSAANVAKVDALMKQIASRTAAMDAATKEKEMKIVTAAQEYLKALMAKRGEEVMNAKAIHKEEQQVGAEKINEHKKSGDVWSAVGLLVDLQKPNQYSRSTEQMRTVLSALNATPAKK
The following text describes a protein:
Function:
Acts as an acyl-protein thioesterase that hydrolyzes fatty acids from acylated residues in proteins. Regulates the mitochondrial S-depalmitoylation of the nucleophilic active site residue of peroxiredoxin-5/PRDX5, a key antioxidant protein, therefore modulating mitochondrial antioxidant ability. Also catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, an active metabolite of the immunosuppressant drug mycophenolate.
Subcellular Localization:
Mitochondrion.
Sequence:
MSAPLCFFRVRCCLRMFCLSPKLSNTRLQVHQRFMMTDDRESLEHLHRTHASSIAFRQTPGKDPGVVFLPGYMSNMTGGKAVALEAYCRRRGHAFVRFDYQGLGESIGEMRKGEKLFDIWKSDALAVLDELTVGPQILVGSSMGGAIMLLLALERPERIHSLLGVATAVQFDRPLSYTEQKRGHVHEARGSAPGDSTHTTPHNFVDKHYTRCLSQNPMPVKQPIRLIHGMKDDTVPFRTSVDLAERLESKNVEVILRKEGGHRMSEPEDIRLLLDCLEELLKIR
The following text describes a protein:
Function:
Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes.
Subcellular Localization:
Nucleus.
Sequence:
MAMQTMREGLPSAPQISWWNAFGSQPLTPESLAGDSDSLAGVKVRSAGGIEQGVNKQSNSASHFSFSLGDVKSPRVVPKPHGSAFSMQPPYLELGFSQPQMYTKYPCVEQQYYGVLSPYGSHSSVMLPLNMETEDGTIYVNSKQYHGIIRRRQSRAKAAAVLDQNKPSSKFRKPYMYHSRHLHALRRPRGSGGRFLNTKSQNNAKKADGTKPTQPQQSNSQDSDVLHPENVTMNLSNRLGSEVTSMNYFLSSSVHPLGGMVMPSKWITAAAMDNGCCSFKT
The following text describes a protein:
Function:
GDP-GTP exchange factor (GEF) for the small GTPase BUD1/RSR1. Regulates the activity of BUD1 together with BUD2 which is a GTPase-activating protein (GAP) of BUD1. Required to produce both the axial and bipolar patterns of bud site selection. Determines the orientation of division axis. Overexpression can suppress mutations in PRP20 which is the GEF for GSP1. May be a cytoplasmic GEF for GSP1. Might also act on the Ras-like protein CDC42. Appears to bind to Ras proteins but not to activate them.
Miscellaneous:
MISCELLANEOUS: Present with 2110 molecules/cell in log phase SD medium.
Subcellular Localization:
Bud neck. Cytoplasm, cell cortex. Note=In haploid cells, forms double rings that encircle the mother-bud neck and split upon cytokinesis, each progeny cell inheriting BUD5 at the axial division remnant. In diploid cells, localizes to the poles of the cell.
Sequence:
MSPKNKYVYICVEYIYIYFAKIHKQSTLSSDTTKMFVLIDNVLAYLLEQDDLFVTARFAIQGQIVSRRVNKIHISNITDVLLQQFISHTLPYNDNIVPKKILDSMRTAVRQLLEATACVSRECPLVKRSQDIKRARKRLLSDWYRLGADANMDAVLLVVNSAWRFLAVWRPFVNSIQHATQELYQNIAHYLLHGNVNIQRVTALIQLVMGQDDLLFSMDDVLQEVFRIQLYLNKMLPHNSHKWQKPSPFDSANLLLNFRDWTTDNALLQELLLSYPTINKNKHKNHSVPRLIQIWVESYWQDSETTLKDILNFWYSHLAEYYEYQELFADIVQLFINKKRTRQLKIHYIGLTDKEIEENKPPLDYENLFLQYEIDKTNANDELCGATDLSDLLFQWKQGELLEVEAFALNVSPWSLAKTLTLLESSLYLDIETIEFTRHFKHNDTTIDSVFTLSNQLSSYVLETTLQQTHTISYWLQVALSCLYLRNLNSLASIITSLQNHSIERLSLPIDVKSDHLFQRLKVVVHPNNNYNVYRRTIKHIFHSQLPCVPFTSLLIRDITFIRDGNDTFTKDGNNVNMQKFNQITKIVAFAQYLQQKQYEDIHCSNTTARSLLGAMIKVHTLYNDNKDRAYQVSIAKVPRLT
The following text describes a protein:
Function:
Might be involved in RNA metabolism; it is missing helicase motif III and may not have helicase activity.
Subcellular Localization:
Nucleus.
Sequence:
MASGLAEESELSPGESELAVNPFDGLPFSSCYYELLEQRRALPIWAARFLFLEHLESSPTGVVLVSGDPGSGKSTQIPQWCAEFALARGFQTGQVTVTQPYPLAAMSLASRVADEMDLTLGHEIGYSIPQEDCTGPNTMLRFCWDRLFLQEVASTRGPGAWSVLILDEAQERSVASDLLQGLLRDTRLRNLPGDPRVVVVTDPALEPKFQAFWGNSPIVRVPREPGGDPTLAYKDTVPTDLVEAACQAVLELCQQEEAPGDVLVYLPSEEEISLCCESLSGEMGTLAVPGPPPRVLPLHPGCAQAIQTVYEDTDVSVRKIVVTHWLADFSFSLPSIQHVIDSGLELRSVYNPRIRAESQVLRPISKCQAEARLLRAKGFPPGSCLRLYSKSTLELEAPPLPHPKVCEENLSSLVLLLMRKQIAEPGECHFLDRPAPEALMRALEDLDYLAALNDDGELSDLGVILSEFPLPPELAKALLASCEFNCVDEMLTLAAMLTAAPGFTRPPLSAGEAALRRALEHADGDHSSLIQVYEAFVQSGADEAWCQARGLNWESLCQARKLRAELVELMQRIELPLSQPAFGSEQNRRDLQKALLSGYFLKVARDTDGTGNYLLLTHKHVAQLSPYCSYRNRRTPAQPPTWVLYHSFSISKDNCLCIVSEIQPEMLVELAPPYFLSNLPPSESRDLLNQLREGTAEPPAAATETSSPQEYGDGCVLQ
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 (By similarity). 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 (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MLRPLWPLFLTALFLNIYRAASVLIDEAGKNDFEISLLGKVNDLVYDTKNEYLYAVSQKGLLAKLNASNGDVIWRQSIAPETSQLNYNPVTNFIITVDKDYLYIWNSKNGILDRKIELADGKGKLFEVNKGFVYLNPHTRKFIELDLQASFSISIERDLQLDAISFLTYAEKNYVLFKRDGQFVLQALDHNYAVYGPETVLNVPENAQLLVTEKDVIIYSSNGVIYGIHVSMADISQLLIDEYKTFEWSSIPGKRHGYSITVDSQSTPVTYLFVIIDSEFVLIDEYIHEDTEALGYIHMEDNQTFSRVFAVANQIKFAPATVITIPNQLSRPVFRLFTFAEGEISAIVILDDGTFFSFSNTELVWKREEALAYAINPSILPTTLLTSYQKSIQDEENSSVSFLNRWYRHFNQLIDFLKHPHGFTSSSVLDDAFTTKIIIPTSTGSIFCLSSDPKQVHRILWRYDFNINPESVESWLLDISDEDPKFAFVHQWNDAFSFYILNASDGSVISQKSRDFKADEFYYVDNISKNLPNQIFAVKDYKVLPLTGDNSIFEKISQEANSIFVYTSETKVEGFSISADLTMDVQWSYNLAEGEIVIASIRRNPHEIVASFGRVLQNREVMYKYLNPNLFALFSKCKNDLVVYVMDSVTGSIVYQNKHQGIILFDKVYGVFSENWLVYSYQSDVPNLSTKIISVELFEGSHSNEKIDSNEIYSRHNDYRPYAFTKAYIFDREITTLGVTNTPQGITSRDVLLGLSSNQVAMIPQALLSPMRPVLRPNEKANDASFIPYEPIIPLNDDMVLSYNKRVYGVSQITSGITNFESTTLVLSTGLDVFFTRTAPSMPYDMLSSHFDKKQLMLTTFGILLAVLLTKPLVKKKQLNTKWYN
The following text describes a protein:
Function:
Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation; Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
Sequence:
MAFSLAHAGVLNLQALAFSPASCTTSQNAVRSSTGVAPAFMKQRAPFMFNSRRRCASIVAAADGNSSYRDLETVSAGSTEEISEEVLGGEIFRPMQDLQESGILDLVDQRGNDTSLARQRYSPDTETAINDSINVAYTLSYAFHSMAAFFDRDNIALQNVAKYFYDRSKYELDDALKLTDYQNRRGGRVQLLPLQAPFSEFDDPEKGDALNTFELALGLEKIQNEKYLALQAAIAEVGDPQADDYVKSTYLHPQIEKLKRTAEQVRQLRRVGKGYGVWHFDQELEGGEEIPEPVA
The following text describes a protein:
Function:
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase.
Subcellular Localization:
Cytoplasm.
Sequence:
MRRIEEKCKLIAQLDTKTVYSFMESVISIEKYVRAAKEYGYTHLAMMDIDNLYGAFDFLEITKKYGIHPLLGLEMTVFVDDQEVNLRFLALSSVGYQQLMKLSTAKMQGEKTWSVLSQYLEDIAVIVPYFDRVESLELGCDYYIGVYPETLASEFHHPILPLYRVNAFESRDREVLQVLTAIKENLPLREVPLRSRQDVFISASSLEKLFQECFPQALDNLEKLISGISYDLDTSLKLPRFNPARPAVEELRERAELGLVQKGLTSKEYQDRLDQELSVIHDMGFDDYFLVVWDLLRFGRSNGYYMGMGRGSAVGSLVSYALDITGIDPVEKNLIFERFLNRERYTMPDIDIDIPDIYRPDFIRYVGNKYGSKHAAQIVTFSTFGAKQALRDVLKRFGVPEYELSAITKKISFRDNLKSAYEGNLQFRQQINSKLEYQKAFEIACKIEGYPRQTSVHAAGVVISDQDLTNYIPLKYGDEIPLTQYDAHGVEASGLLKMDFLGLRNLTFVQKMQELLAEIEGIHLKIEEIDLEDKETLALFASGNTKGIFQFEQPGAIRLLKRVQPVCFEDVVATTSLNRPGASDYINNFVARKHGQEEVTVLDPVLEDILAPTYGIMLYQEQVMQVAQRFAGFSLGKADILRRAMGKKDASAMHEMRASFIQGSLEAGHTVEKAEQVFDVMEKFAGYGFNRSHAYAYSALAFQLAYFKTHYPAIFYQVMLNSSNSDYLIDALEAGFEVASLSINTIPYHDKIANKAIYLGLKSIKGVSNDLALWIIENRPYSNIEDFIAKLPENYLKLPLLEPLVKVGLFDSFEKNRQKVFNNLANLFEFVKELGSLFGDAIYSWQESEDWTEQEKFYMEQELLGIGVSKHPLQAIASKAIYPITPIGNLSENSYAIILVEVQKIKVIRTKKGENMAFLQADDSKKKLDVTLFSDLYRQVGQEIKEGAFYYVKGKIQSRDGRLQMIAQEIREAVAERFWIQVKNHESDQEISRILEQFKGPIPVIIRYEEEQKTIVSPHHFVAKSNELEEKLNEIVMKTIYR
The following text describes a protein:
Function:
Arabinose kinase. Involved in the salvage pathway which converts free L-arabinose to UDP-L-arabinose. May play a role in arabinose transport.
Miscellaneous:
MISCELLANEOUS: Sup1, a suppressor of the ara1-1 arabinose-sensitive phenotype, contains a second point mutation resulting in a premature stop codon and a complete loss of kinase activity. Therefore, the putative arabinose transport function is independent from the kinase activity.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MSERAKLQKKKKVTEDLLDSLLLLPPWRNFAISQSHQSIIESSSQRLPEKMRIDENEGVSASSKHLVFAYYVTGHGFGHATRVVEVVRHLIAAGHDVHVVTGAPDFVFTSEIQSPRLKIRKVLLDCGAVQADALTVDRLASLEKYVETAVVPRAEILETEVEWLHSIKADFVVSDVVPVACRAAADAGIRSVCVTNFSWDFIYAEYVMAAGYHHRSIVWQIAEDYSHCEFLIRLPGYCPMPAFRDVIDVPLVVRRLHKSRKEVRKELGIAEDVNVVILNFGGQPSGWNLKETSLPTGWLCLVCGASETLELPPNFIKLAKDAYTPDIIAASDCMLGKIGYGTVSEALSYKVPFVFVRRDYFNEEPFLRNMLEFYQCGVEMIRRDLLMGQWTPYLERAVSLKPCYEGGINGGEIAAHILQETAIGRHCASDKLSGARRLRDAIILGYQLQRVPGRDIAIPEWYSRAENELGQSAGSSPTVQANENNSLVESCIDDFDILQGDVQGLSDTCTFLKSLAMLDAIHDSEKSTEKKTVRERKAAGGLFNWEEEIFVARAPGRLDVMGGIADYSGSLVLQMPIREACHVAVQRNLPGKHRLWKHAQARQQAKGQVPTPVLQIVSYGSEISNRAPTFDMDLSDFMDGDEPISYEKARKFFAQDPAQKWAAYVAGTILVLMIELGVRFEDSISLLVSSAVPEGKGVSSSAAVEVASMSAIAAAHGLSIDPRDLAILCQKVENHIVGAPCGVMDQMTSSCGEANKLLAMICQPAEVVGLVEIPNHVRFWGIDSGIRHSVGGADYRSVRVGAYMGRKMIKSMASSILSPSASSANGGNPEELEDEGIDLLEAEASLDYLCNLSPHRYEARYADKLPDIMLGQTFIEEYADHDDPVTVIDQKRSYSVKAPARHPIYENFRVKTFKALLTSATSDEQLTALGGLLYQCHYSYSACGLGSDGTNRLVQLVQGMQHNKSNSEDGTLYGAKITGGGSGGTVCVVGRNSLRSSQQILEIQQRYKAATGYLPLIFEGSSPGAGKFGYLRIRRRISL
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquitination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein (By similarity). Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos (By similarity). Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner (By similarity). Does not affect PARP1 activation. Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest (By similarity). Promotes cell survival after gamma-irradiation. Facilitates DNA repair (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Nucleus. Note=Translocates to the nucleus after DNA damage, such as laser-induced DNA breaks, and concentrates at DNA breaks. This translocation requires PARP1 activation and PAR-binding (By similarity).
Domain:
The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
Sequence:
MAGCGEIDHSLNMLPTNKKASETCSNTAPSLTVPECAICLQTCVHPVSLPCKHVFCYLCVKGASWLGKRCALCRQEIPEDFLDKPTLLSPEELKAASRGNGEYVWYYEGRNGWWQYDERTSRELEDAFSKGKKNTEMLIAGFLYVADLENMVQYRRNEHGRRRKIKRDIIDIPKKGVAGLRLDCDSNTVNLARESSADGADSGSAHTGASVQLPVPSSTRPLTSVDGQLTSPVTPSPDAGASLEDSFAHLQLSGDSIAERSHRGEGEEDHESPSSGRVPDTSTEETESDASSDIEDAPVVVAQHSLTQQRLLVSSANQTVAERSDRPVAGGGTMSVNVRSRRPDGQCTVTEV
The following text describes a protein:
Function:
Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Domain:
The PAL motif is required for normal active site conformation.
Sequence:
MESSVLEWLGVEIIGVMSPVSICMFLVVLLVYSLSSPSTTATTIATAANLVYAENPSDTAAQKLEGAVLNAVVFIVFIALATFLLVLLYYYNCTAFLLHYTRFSTFFVLAAMGGSILLSLLERFSVPLDAVTSFLLLFNFAVVGVLSVFAGGGLPILLRQCYTVCLGIIVAAWFTKLPEWTTWTVLVALALYDLVAVLAPGGPLKLLVELESSRNEELPALVYEARPTVNTRNHAAAVGFIVAGVSDSETSRIELQVVSRVNSNNNNNLSSNNDNGENGINDEWERSPLVGGMRFGEVVVDEGMSPLVEMSGVGENEEEGEGVRRKIGERGIKFGLGDFVFYSVLVGRAAMYDLMTVYACYLAIISGLGCTLILLSMCRKALPALPISIALGVLFYFLTRLLMEPFIVGTATNLMMF
The following text describes a protein:
Function:
Scaffold protein in the commander complex that is essential for endosomal recycling of transmembrane cargos; the commander complex is composed of the CCC subcomplex and the retriever subcomplex. May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. Down-regulates activation of NF-kappa-B. Inhibits TNF-induced NFKB1 activation.
Sequence:
MTERQPLQSSALPTELSKAPGTGYMYMHMLIDIQWKLGMAVSSDSCRSLKYPYVSVTLKVADQSGQIVNKSFEMTVPQFQVCNSNIGFSVSCRTMLLSRLEQTGRKRGMPSPPSPPSTPPLLPRAHVHLCVAAVQSGEREEVIVDLLGLPSLGREARQEAGSFCPV