lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MNNDKMEAALNICNTLPGHVFDDTIKMLSRIDQSITNNILINKEGSIKINYDKEENKYYLGNMFNKEKDSYRSPYTNIYFPEHYINSYVPPEHLRTLEILYNKIFDRYRKAYYMNGLSSVYLWPNPIEDGFVACFLIKKKEIFDKETNIKWEATHLIQVNITNLNVHYQISCTINFEIKKNDNLLLSGNINKALENSKKVTDLYLIKDQYFHMENMGYLIECMENSLRKSIEYIYILKIQDMLNSIKYYNFTNHLTYNNTNKNISNISNSLIFSRENIQKELQTKIKQVRKK
The following text describes a protein:
Function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH also oxidizes malate to the non-canonical enol form of oxaloacetate, enol-oxaloacetate. Enol-oxaloacetate, which is a potent inhibitor of the succinate dehydrogenase activity, is further isomerized into keto-oxaloacetate.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MALSMLLVRNSAAISRLGMLSAPLRSAALSSRLAAPMTTTAQEEMAKFWDKNAQKKRPMSPHLTIYKPQLTAMLSITHRGTGAAMAGFVYAFSVGMLVVNPLLGWDFPTIFNFIKSLEIHPWLILGGKWCMAWPISYHAMNGIRHLNWDAGYGFDMKVLYRSGWFVFFGSFLLADLMLYFL
The following text describes a protein:
Function:
Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity.
Subcellular Localization:
Cell membrane. Cytoplasm, perinuclear region. Nucleus.
Sequence:
MGNKCPACLCGADRASEVKCGGSKKKRKTKKSESVLPTDLHSSGAQKNLTGETGNRSQRPDCLSLPTQQNNTKETKFPDFSLHGVQKSSPPSSSTTPIQSSKDHPYDPANVEMLFRMYKDDVEDLILADGVERLCFDLEVDPTEFIVLVLAWKLKASTMCRFTRDEFISGCQEMKCDSIHSIRSSFPRILKDAEINFKELYRFTFQFALDADEGQRSLPCDIAVAMWNVVFSTNQPLILPSWIQFLQERNVRGISRDTWHMFLYLVDAISEDIDNYNDNEAWPSLFDDFVQYKKDAMTKIEEKKVVVVMTDSAAGDSSSQRMEIPGSILTSGENTPEMAGNSPTSHVANKNETKSPETPSVETQTCGNSPGEILSHLHSENEVSSEQT
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MNAEREEVSLLACHETVAEKVVKTEDQETGGPSLLESPKRSRKTSHPVQIGKIGERLSWVAAKRAEHELNNGLLSQCPDFLKTIQVPYSGWRSPQRSRTPFPSPLGTPSGKCHGPEKEAASGDLQGDSLQSSPSTDCGKQAGDDNRKGDAPHEEGLTVEMQRQRFRWFCYQDAEEPRQICAQLRELCIQWLQPDLNPKEQMVDLIVLEQFLAILPEEIQSWVGDAGPETCAQAVDLVEEFLLRQQETERWKQEVLGEFEEVAMSFSREDDAGEGQLSREIKRETVTLLDDEWETEEEGSSFDPSLERFEPRDPGENVEDQGRPGWEQRVHIDQRRSKSMVYENGGSDGTDLQQRMMYAVKRRHICNICGKAFTQKSNLNRHQRTHMGEKRFHCFKCGKSFNWETSFIRHQQFHTGEKPYPCLDCGKRFSRTANLIIHRRIHTGEKPHQCLDCGQSFSQISNLVRHRRVHTGEKPYKCTECEKSFTQKSNLIKHQGIHSSDRPNTSSDYAGKLNQRPSHNRFERIPLGESRCICFKCGKTFSRRGNLLRHQTIHTKDKPHKCTECGKRFNQRTNLNAHQRIHTGEKPYRCPDCSKSFRWRAHLIIHKRLHTGEKPHRCVDCGQSFSQRSNLVRHQRTHTGEKPYQCSDCEKSFGQKSNLIKHQRIHAGENAFCQSLNGVSHDQILLEEDPYKCFRCGKVFSRRGNLLRHQSIHTREKPHKCPDCGKRFNQRTNLISHQRIHTGEKPFQCPECGKSFRQSPHLIKHMKVHTEEKALYGSLDYVGNVHPELNHERTNVGGKPYECLKCGKIFNWQSNFIRHQKIHAGEESHECSECGEKFNRQKSLIAHQRIHMTEKPYTCTECGQNFAWEAHLVIHQRIHTGEKPHMCPECGQSFSQRSNLIRHQRIHTGEKPYKCSECGQSFSQRTHLVVHERIHTGEKPHRCQDCGQGFSQRAHLIVHQRIHTGEKPHRCMDCGQGFCQRSNLLRHRRTHSCEKNN
The following text describes a protein:
Function:
Acts as a guanine nucleotide exchange factor (GEF) for RhoA GTPases.
Sequence:
MAEKEPGKKVAVYRSVSFKRLESWSANKTRSATDDPTEGAVEKAQPSATRSVGVSRKVSKISAANVSTADFKKNSPHSISPSIRQLSEKFNTATERTPAPAPVSKGVSKGTAPNRTDTPCVEMTNWPSVTKIRKLFGDGHRKPHRSTSDADDLKTRSPSENVENWTAKVNSDPRPPPPVPPPRSSSVPLSLRAQSLSFGWQHKQEARQQSDSLHSLHSSSKPQAAPSAAPACDKVSSSEEEDSYRRGSRGSFPLTHNSSGAGRNKNGSWVRPPGRSSGSEEDGPPAVAHNKDNVRRKSLRKKKKNVGGSSNNGESDDSYDEPLMEPFERRQFPCDLEQWVCKDEVLRPRSSLTAGVSRVSKVNISSFMPSPCGSQSSSRYSSTETLKEEDQPSTGSSLMSKSFHGNFTMYRSPSFSQGDCVPRPQVRVRPKLPFGIVRVPSEGLSENRSPHAFVNEKAKHRMSVSNPDIASETRTLLNFLKMDLSDLRYRKRGKGGGDRNEAVCSQQASYQNTSPSYRVGSRAQFPPQGRLSLKDLTATLRRAKSFTYSEKPVGRRQSATGTMKQSPSEQMLDTLGDRYTAVPDSPLRDQYIQEARQVFRDISQMGAQQEYYCGVDYKKVESDENIFREKSVDELSGHESSLTDEGIVTEPETGPCGISSSKDILGKSVKVRKQSSSGLYKTEYDAVAVGGESNYNKSVSQGPLEAPSTPSAIRRRRKFSSAGNNGSDSSNGSNGESSGEAYRSLSDPMPHRRCSISEDAKNFSVDSNLLGSLNSKNGMPESSATDLSEYTGSAASDLSVCSDGLKDYSTVIQSIVREPGAMDKLNDEKGNGKTVKKKSFSDPSRRGESDTPGFKGPSEPINEMDQSIIPSSSEPILSEQRDELGELQELYRPDAKLRSQSEHMLPSRLEADALEEAPCFPFDPKLAEVLSPRMARRSSKKRNNRATHQEGRAHQQPDDAEHLHRLQPSPKLRPASKHVRHASEPATFVPIVAPETHLSQSHPVHITVPEPSRPPQKPYPVVQAPSLEDVTKQYMLTLNTVDTPVPVTPETSRSTPATPTTGEAKLLRKANDDLSSAAQKSKPQVDMRKHVMMTLLDTEQSYVESLRTLIQGYMKPLKQPENSFICDPSLVDEMFYQIPEILEHHEQFLEQVLLCVQDWHDKQKVGSLLIESFSKDILVNIYSAYIDNFLNAKDAVRIAKEAKPAFLKFLEQCTRENKEKQALSDLMIKPVQRIPRYELLVKDLLKHTPEDHPDHPFLLDAQKNIKRLAERINKGRRSAEEAEKETRVLQEVEAHIEGVENLLNPQRKFLRQEMVVEVKTVGGKKDRSLFLFSDLLICTTLKRKSGSLRRSSMSLYTAASVIDTSSKYKFLWKLPLEDVEMVKGTSQATNRENIQKTIGRLDEDLSTLGQISKLSETLSFPHQGLDDVIRDLMAAVHRELAEKQSLSFSMTFLPTKVELTTASAENTFVFEFTGPEARSNFEQAFEDAKKKLAMNKDYWDPEFLKAIPIMKTRSGMQFSCASPSHSCPENTYEVWVCNSDGYVGQVCLLNIKDEPTVEACIAVCSARIICISAVPGLKARCVWDRGESLLSPPPPEPAPVPSEQNLHISISGSSLELVGPPRGRGRELVPFDSDDTDDESSPSPSSTLQSQASRSTISSSFGNDEMVGSKEMTTETTSSEEEQEFPSVASSYGPPRLSSDSPMDGRAMRRSSRGSFTRASLEDLLSIDPEAYQSSVWLGTEDGCIHVYQSSDNIRNRKNSMKMQHSASILCILYLDNKVFVSLANGEIIVYQREAGSFWDPQNSQTLSLGTPGSPVTKMVPVTGRLWCGCQNRILILNTNTLAQEHTFQIGQDSSRCVTSMVSYGQGVWIALQGSAQVRLYHAVTCESLMEVDVAPAVHKMLAGSDAIIRQHKAACLRITALLACKDLLWIGTSAGVVLTLTIPPVSSGTSPLRAPPVPMGSAHGHTGHVRFLTSIELPEGFDVAFPLPGDQGNPATSGEGGSGLQRQDSARRRASTLLQSKSNLLVISGGDGYEDFMLNNSSETVGRDDSTNHLLLWRL
The following text describes a protein:
Function:
Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the NADPH-specific conversion of aklaviketone to yield aklavinone. It can also convert maggiemycin and 7-oxodaunomycinone to epsilon-rhodomycinone and daunomycinone, respectively.
Sequence:
MENTQRSVIVTGGGSGIGRAVARAFAARGDRVLVVGRTAGPLAETVDGHKEAHTLAVDITDPAAPQAVVREVRERLGGVVDVLVNNAATAVFGHLGELDRTAVEAQVATNLVAPVLLTQALLDPLETASGLVVNIGSAGALGRRAWPGNAVYGAAKAGLDLLTRSWAVELGPRGIRVIGVAPGVIETGAGVRAGMSQEAYDGFLEAMGQRVPLGRVGRPEDVAWWVVRLADPEAAYASGAVLAVDGGLSVT
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6/CTU1 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
Subcellular Localization:
Cytoplasm.
Sequence:
MCSIGDDNFEELDNLKYMPAKEKPSPFSKCNKCKEEIPIVVLRSKDKYCRKCFLAGATHKFKATLGKHKLIRPNDRVLVIHKCGHPSTALLHFIRSGLDLETHKKLRFEPVVLFIEEFTHLTVTDRSEILKAIEKEVACFNFQVYLTSLAKLITTNSVETELHANFDRLEMDEDDKNVITKFVDQQLNETNKNDFLNITRQKLIVKIAKHLNCKFIFTPEISNDVASQLLTDISLGRGSTVSLNAGFCDSRDETVKILRPLRLFDLKELAFYNHLNSLEPVTYRKRDENPYKSVQQLMKKFVNELQVNYPATVTTILKTGDKLSLGTKPTNKCDFCNAPLEEEGPELTSAESTQFSHWVSTQTPAERRLAPERAFNNPTCDNYCFGCRKFRK
The following text describes a protein:
Function:
Acts as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates (in vitro).
Domain:
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Sequence:
MGNVISGGSRPENHRDRTSPPYPNPNAQYQGNYPSPYQDCARYPYGEMASPVQYVEHQEAVTIRNDINLKKETLRLEPDEQNPGKFLLSFTFDASVPGSITVMFFAKEGKDCNLIATKEDLFPSTQVSFAKGLEQRFKQACGTGIDFSDMSEADLVEANETDVYHVAVKAEVVSEDDHPESGTPNRQITHVVLEKDHKGEYKARVVKQILWVNGNRYVLQEIYGIGNTVDDNGEDANERGKECVICLSEPRDTTVLPCRHMCMCSGCAKLLRFQTNLCPICRQPVDRLLEITVNNNDRN
The following text describes a protein:
Function:
Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Subcellular Localization:
Membrane.
Sequence:
MLNDTFRIISNATLDDDPCSVSFIDQPFVKIPVMIIYCLVFVVCLSGNFLTLIVMTSHPMMRTPTNFFLSNLAIADLLVAIFCILQNMIHIVGFDHGNWPLGPVMCKLYLGLTNIMPCTSAGILVLVSLEKYIAVLHPLSGLKLLTPEHRWVATMIVWVISILVNFPYFLYAQNYTYLGVSACFRGSMPIWNSFSFIVWYLIPLTALVFIYSRISHLLWTSDSNRQSSRQSHESNGSLERGNGYANTAQPGSSWQMKNGRIVVYKQESLLNVPKREKKVKEPKRPKDTEGRRKVVRLLVAVVVSFALLTFPHHARLLYTSFQTGTICNSNWTMIFQPLSYIFLFISSAINPILYACLSKRFRNALSDVIHCRKGVFSRISRSRNRTLVSDVPPEDSRCPSPAPIRMHRIR
The following text describes a protein:
Function:
Recruited co-dependently with zhp-2 to the synaptonemal complex between homologous chromosome pairs to regulate the formation and number of crossover events between homologs during meiotic recombination. Together with zhp-2, promotes the accumulation of pro-crossover proteins, including zhp-3 and zhp-4, at a designated crossover site along the recombination intermediate. Limits the number of crossover sites along a recombination intermediate by restricting the association of these pro-crossover proteins with other recombination sites during late prophase. Also, together with zhp-2, plays a role in chromosome remodeling following crossover formation to promote two successive rounds of chromosome segregation during meiosis.
Subcellular Localization:
Chromosome. Note=In association with zhp-2, localizes to chromosomes from pachytene to early diakinesis in the germ line. Co-localizes with syp-1, a component of the synaptonemal complex from early prophase to mid-pachytene. From mid-pachytene to diplotene, co-localizes with syp-1 on one side of each crossover site. Remains co-localized with syp-1 along the short arm of homologous chromosomes through to late diakinesis. At late pachytene, localization at chromosomes is not dependent on syp-1.
Sequence:
MEFIVCNGCGCSPSKRQFFITACSHVFCETCRTTPTADFCHLCKIPTKTLKMDASLPKNVKKMFGDVGVMSTDIHKRLARVIGFQKIQKSIQLKMENKKSVMRKEQTKKVEKKTEEMHCQLSKLTSFEENNRKKLEDIERENEKLRNLISALELKVASSRDIDDDEFFMQGTPTSSNPSVAGSDVDNDELLDYDLLGLRNRSDSSSSNCSSQSNRGGSLF
The following text describes a protein:
Function:
Pore-forming subunit of Ca(2+) homeostasis modulator channels. Mediates ATP release from astrocytes and ATP-induced Ca(2+) influx in microglia thus regulating neuronal ATP and Ca(2+) homeostasis, synaptic transmission and neuroinflammatory response. May form intercellular gap junctions. The gating mechanism remains unknown.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MAALIAENFRFLSLFFKSKDVMIFNGLVALGTVGSQELFSVVAFHCPCSPARNYLYGLTAIGVPALALFLIGVILNNHTWNLVAECQYRRAKNCSAAPTFLLLSSILGRAAVAPVTWSVISLLRGEAYVCALSEFVDPSSLTAGDEGFPPDHATEILARFPCGEGPANLSGFREEVSRRLKYESQLFGWLLIGVVAILVFLTKCFKHYCSPLSYRQEAYWAQYRTNEDQLFQRTAEVHSRVLAANNVRRFFGFVALNKDDEELVTKFPVEGTQPRPQWNAITGVYLYRENQGLPLYSRLHKWAQGLTGNGTAPDNVEMALLTV
The following text describes a protein:
Function:
Kinesin-like protein required for chloroplast movements and anchor to the plasma membrane. Mediates chloroplast movement via chloroplast actin (cp-actin) filaments. Required for the chloroplast avoidance response under high intensity blue light. Mediates redundantly with CHUP1 the nuclear avoidance response under high intensity blue light. May act as a mitotic kinesin. Probably involved in division plane determination.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome. Cell membrane. Cytoplasm, cytoskeleton, phragmoplast. Note=Localizes to the spindle apparatus and condensed chromosomes in mitotic cells. Localizes in the forming cell plate and the cortical division zone (CDZ) during cytokinesis.
Sequence:
MADQRSKTNRWNWEVSGFEPRKSSSNASFAESTGHRTTGPLLRRNSISTPSLPPKQAIASKVNGLKEKVKLAKEDYLELRQEATDLQEYSNAKLDRVTRYLGVLAEKSRKLDQFVLETEARISPLINEKKRLFNDLLTAKGNIKVFCRARPLFEDEGPSVIEFPGDCTICVNTSDDTLSNPKKDFEFDRVYGPHVGQAALFSDVQPFVQSALDGSNVSILSYGQTNAGKTYTMEGSNHDRGLYARCFEELFDLANSDSTSTSRFSFSLSVFEIYNEQIRDLLSETQSNLPNINMDLHESVIELGQEKVDNPLEFLGVLKSAFLNRGNYKSKFNVTHLIVSIHIYYSNTITGENIYSKLSLVDLAGSEGLIMENDSGDHVTDLLHVMNSISALGDVLSSLTSGKDSIPYDNSILTRVLADSLGGSSKTLMIVNICPSVQTLSETISCLNYAARARNTVPSLGNRDTIKKWRDVASDARKELLEKERENQNLKQEVVGLKKALKDANDQCVLLYSEVQRAWKVSFTLQSDLKSENIMLVDKHRLEKEQNSQLRNQIAQFLQLDQEQKLQMQQQDSAIQNLQAKITDLESQVSEAVRSDTTRTGDALQSQDIFSPIPKAVEGTTDSSSVTKKLEEELKKRDALIERLHEENEKLFDRLTERSMAVSTQVLSPSLRASPNIQPANVNRGEGYSAEAVALPSTPNKNNGAITLVKSGTDLVKTTPAGEYLTAALNDFDPEEYEGLAAIADGANKLLMLVLAAVIKAGASREHEILAEIRDSVFSFIRKMEPRRVMDTMLVSRVRILYIRSLLARSPELQTIRVSPVECFLEKPNTGRSKSTSRGSSPGRSPVRYLDTQIHGFKVNIKAERRNKLASVVSRMRGLEQDAGRQQVTGVKLREMQDEAKSFAIGNKALAALFVHTPAGELQRQIRLWLAENFEFLSVTSDDVSGGNGGQLELLSTAIMDGWMAGLGAAVPPHTDALGQLLSEYAKRVYTSQMQHMKDIAGTLAAEEAEDAGQVSKLRSALESVDHKRRKILQQMKSDAALLNLEEGSSPIPNPSTAAEDSRLASLISLDGILKQVKEITRQASVHVLSKSKKKALLESLDELTERMPSLLDIDHPCAQREIATAHQLVETIPEQEDTNILEQSHDRRPSLESISSGETDVSQWNVLQFNTGSSAPFIIKCGGNNNSELVIKADARVQEPKGGEIVRVVPRPSVLVNMSLEEMKQMFVQLPEALSLLALARTADGTRARYSRLYKTLAMKVPSLKDLVSELE
The following text describes a protein:
Function:
Forms a fork protection complex (FPC) with CSM3 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MAQTTLDDWAKDPVDPEIRAHVHSLITALGGIGDDGTYSLGDDALLCLKDLRKWLKFGDGQLNRRDVARCMAEANLVKGDLLEILAKISPKAIEDKWRHKIAVAALELLVPLTWPFEIDPIEATVNHHRHGPYIQLAQIGYKRAILQFDRDRTLQTAVKIALPSMAVPLRERTPRDEGIIRIALYFIRNIAMLSPPTSAPMDIDEAEVSRSATIDTFHEQDIFQVLLSVASSIGEDFVAQDVIVLEILFFLLKGIDAEKLFMEDKKLGTKNADELKNLMQKEKAMLAGYARNAPTRHNRFGTMIWVKRDDEKVTTISGQDVLGKAQASMQKMDQTKKWNKPRRPGKKVDGEQEREEFDLPVALTVSARKHIKAFVEEFLDSSFNPLFLHLRKAIERETERVEIRHSRQFFYLASWFLRAECARRRTMKERAADPKDPAVLTAEDESYGLVAEVMNQETFILLNRFMQKSQDEKAWQDLNAGMKCFTQILLTVHEMSESALEDDQEIAENIQNRIFYEESTHDRVVMILRSYNGQGFGYLDAVTELSHVFLRMLERYAKQNVDLQVKSKRRARKIKKKVAETHGANGDEEGQVSDTEDIQQAQRTVSERKFDFQRFAAKFVNQSSVDTFVAFARYFSDLDTEQLKRIHRFFHRVAFKMELGVLLCRVDILQLFTKMMKGPGGLDPESPAYKEWDEFVRHFFRQVVKKVQERPELVVEMLFSKIPATLFFLDHGYDREITKSTPRAPAELEVKPGMEVPEQIGVAVGVLINQAKSDALHWVRDILISAAEERKAWEGAEEARKALAAAERPAGEEVAENTEEESPKPPSILVKPDSEERRLAMFKDNKLRLLMTLVGFSRLGEAHDPDATWIIPSAFTSTDLEFAIDLLRKYEFDPPTYEDGKGPEDLIRNKASAARRSTRRVDFDDDDEEAENAVEEDHGEYRAGKATERKPDGERKKLKRRQRVGTPVELDDEEKDRRAEARRKKELEKFAKQKSTEFVHDSDEEDDDDKDMEFFRREEALRTEIMKAFGKSLTAGSTETATSKKRKAEDSTSRTKRRKTPPKRKAQPFADSDDSDEDVQDAATPSSRAPSLSARDMIHDESEVEDEATDTPLSSQHANGVHESDEDTTTGATASITVKSQDVVMADDDDEEDEATPVARRPMARKRGAFIVDSDSE
The following text describes a protein:
Function:
Part of the binding-protein-dependent transport system AlsBAC for D-allose.
Subcellular Localization:
Periplasm.
Sequence:
MNKYLKYFSGTLVGLMLSTSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNLKKAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLMVDAEKSGKVIPLDKAPEFKLVDSILVTQ
The following text describes a protein:
Function:
Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MEALSRREENEIHEAAKKEALRSCDDYVKDFADCATGRTFSLPFMCKTRLNAMQGCMRDYMTQERMDAMKLDFIAHRSEKGREAVEALRKSREEKLRKMAGIKDEPARI
The following text describes a protein:
Function:
One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins.
Sequence:
MDHVALLKQFIGMCQSNPAILHSPEFGFFRDYLVSLGATLPPKPETPAPEGKCPMGGDKKEEKREEKPAEPEIPKPAEIPFPEIDNEGVIEPEEAVALPMGDSNKAPSDEDVEKASEERGKAQEALGNGDFDAALTHFTAAIEANPGSAMLHAKRASVLLKLKRPIAAIADCDKAISINPDSAQGYKFRGRANRLLGKWVEAKTDLATACKLDYDDDANEWLKEVEPNRSSTVSFLAE
The following text describes a protein:
Function:
Variant histones H2A are synthesized throughout the cell cycle and are very different from classical S-phase regulated H2A. May replace conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MPPQGASKLRLQKKHLLFTLLSLISCKAKDFSFRSFNAHTSLLARDKSWVKSLERLSHSAMAQKIEQLGVDLEARYKAQVSFQYESCGFKVLENAAADVSLSSKIDGKDRIEDGNRSMVQRIEDGNRSMVQRFRSQLTHLKRRGISNCGRCCLHLVTNGVGKDFVINNGACSCSTVVLEDGISLTEVGGLLQEWDGREEPAGQHALEDSLASEDLGSMLESIKVERAKYSLMCFQFPIGRIHRQLKQRTQANGRVGATTAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIHGDEELDTLTKGTIAGGGIIPHIHKSLVNKSSKE
The following text describes a protein:
Function:
Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the K5-type polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor.
Subcellular Localization:
Virion. Note=Tail appendage. Depolymerase 1 is connected to the phage tail via an N-terminal anchor domain, while depolymerase 2 is attached to depolymerase 1.
Sequence:
MIKNDFNQPKGSTIGVLKDGRTIQEAFDSLGYLGVAVLSPANYGAKGDGKADDTIPLRQCVQDACALGGRVVGTVGAEYKISGTIAGTVGDGKYVELDFTGSKFVPTTDDAVMTITGVATSPVAEVTVEVVSVNLGNGSTNTIAMKVTAPGGHSFTKKGEIGKAWSPVLCLNNDLSTQYAGEPFVVGLVESSTVFYTTSVFTELYMGTSLKVIRVPTTQVVVKGLDVESEWTTGWKASTLTLSGLLRPFVYKPKCKNINGPFVNLTGCYGATVFLPEGDNLRNAPSEGAYGYFVNDSASFGSTIYGINCTNARHAYTTSSPRSEPTDDKWWLKGRTLFSEITNGLGTGCHNAFDTHSPSYGIKFTNCRAVGDFRGVDTGGAGFQIRGDRSSLVDCTAINSKIGAAFTAVNISGNSELYISGFTYEGPAGHLALSLSGKAGQVNRVTISDSRWKTLEQYATAITNVEVSASNVEAVVDSATTASAAWRIGEGATLRTRGGAARFSAGSGHSVISLAASGAKVDVGDLEVTGSSFMQYLLATLSQYAGDVYIEADLDGAIPGNPVGGGGTDLKAAVVYTAGNKFRRPLAYRALTIGNANGNTLGLNYSGHDVITWEITATVAGANVNGITPGAFIGQQLNIGSSPASTQQLIINNGTNIAMGHAVTLEAGRGVTLYWNGANWRSGSV
The following text describes a protein:
Function:
Regulates global gene expression after oxidative stress. Interacts and stabilizes mRNAs and may regulate their transition between different cytoplasmic components after oxidative stress.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MNPQPDISGYFPSAYPMNNANRSPGSSRPGYNTAVGLTGVSRMTQRQMEAIGQPSAALFAAAAADDRFASYDNAAFRHNRLQPAAAFATDSFNGNNQAWAYNAGANTVNGALGDNRVRNGGRRALPTEWMSEQNGLGSHALNTPSTQYSSTFGQSVGLLNGDGNFAGDRHGYPGSMYDPRHDSKTLGSDLIPTAIVIKNIPFNVRKEMLTQIMTDLGLPQPYAFNYHFDNGIFRGLAFANFQSPLDTQTVIEQLNGYEVQGRKLRVEYKKMLPEHERERIEREKREKRGQLEEQHQPIALHSQSSMHSLNAAHTSRSRNSPLRKSSRRDLLPPNSNQDDVTGDVDLNNPETLKFYTELTLFRNDPNREIIIFPASITPQQRRTVHILAHNMGLEHRSVGEGPTRQLHVIKDTATATLASMAPPMHISPGVSADAHRRGLSRAATIDFAESRANAPGQFATLGRQGRHGPTLELPDSPDGGINALRGVKSFADLRSYTPSPSLSASGFPQSSLHSSSIAQYGEYSASLGGPNSVMTTPTTPGAASNKDTSLLISDLGSLSLSEPFNANRLRPRETPGAIGSQRSPLNGNSTRSVPERQPHGPSSGDWGESIGFAGRGRTNGHMQRDSDSSDNGTRGAATSASSRFQ
The following text describes a protein:
Function:
RNA-binding protein involved in the correct localization of transcripts in the cell. RNA localization is a widespread mechanism for achieving localized protein synthesis. Involved in structural and functional organization of telomeric chromatin and regulates silencing at the HMR locus (By similarity).
Subcellular Localization:
Cytoplasm. Cytoplasm, P-body. Nucleus. Chromosome, telomere.
Sequence:
MTMTDSSSPAPEGPAAPAEAAAPAKVDAQAPLVTLRLLLSLKEAARILGRGGNTIDNIRKANGVKIGISTKEKSCSDRLLEVTGSIDAVANSLADVVKVLTADDTNEEDAEPEPEQHIFKHLNFILPPPSPDEAEDPMKVKQIGNLRLIVTNSQVSSIIGTAGSKIKKLIDTHSSKLVVSKTFLPDSQDRILEIQGFPNSIANCIKDISQTLIKDDVLDTKEKRYYPHSKHSKDIHVTATVAIPAEYVGALLGHGGNRIANLRKYTRTKITVAQEPNQNNEREFTITGNDQKSVKLAQNMIMKNLGTEKERRLEKQ
The following text describes a protein:
Function:
Catalyzes the NADH-dependent reduction of a broad spectrum of quinone substrates, generating the corresponding hydroquinones. Highly prefers NADH to NADPH as a reducing substrate. Also displays a small NADH oxidase activity. Does not exhibit nitronate monooxygenase activity; is inactive against propionate 3-nitronate, 3-nitropropionate, nitroethane, 1-nitropropane, 2-nitropropane, and the anionic forms ethylnitronate, propyl-1-nitronate, and propyl-2-nitronate. Has no azoreductase activity since it is not able to reduce the azo dye methyl red with NADH. May be required to maintain an appropriate [NAD(+)]/[NADH] ratio for the catabolism of fatty acids in P.aeruginosa PAO1.
Miscellaneous:
MISCELLANEOUS: The two-electron reduction of quinones by this enzyme occurs through a Ping-Pong-Bi-Bi steady-state kinetic mechanism.
Sequence:
MGVFRTRFTETFGVEHPIMQGGMQWVGRAEMAAAVANAGGLATLSALTQPSPEALAAEIARCRELTDRPFGVNLTLLPTQKPVPYAEYRAAIIEAGIRVVETAGNDPGEHIAEFRRHGVKVIHKCTAVRHALKAERLGVDAVSIDGFECAGHPGEDDIPGLVLLPAAANRLRVPIIASGGFADGRGLVAALALGADAINMGTRFLATRECPIHPAVKAAIRAADERSTDLIMRSLRNTARVARNAISQEVLAIEARGGAGYADIAALVSGQRGRQVYQQGDTDLGIWSAGMVQGLIDDEPACAELLRDIVEQARQLVRQRLEGMLAGV
The following text describes a protein:
Function:
DNA repair protein involved in DNA non-homologous end joining (NHEJ); it is required for double-strand break (DSB) repair and V(D)J recombination and is also involved in telomere maintenance. Plays a key role in NHEJ by promoting the ligation of various mismatched and non-cohesive ends. In some studies, has been shown to associate with xrcc4 to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired. Alternatively, it has also been shown that rather than forming filaments, a single nhej1 dimer interacts through both head domains with xrcc4 to promote the close alignment of DNA ends. The xrcc4-nhej1/xlf subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other. The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors.
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes to site of double-strand breaks.
Domain:
The coiled-coil region mediates homodimerization; The Leu-lock (Leu-114) site inserts into a hydrophobic pocket in xrcc4; The XLM motif (also called the KBM motif or KBMX motif) and the interior region of the C-terminal tail preceding the XLM motif are essential for DNA end joining. The sequence of the C-terminal tail is not critical for its role in end joining but it must be sufficiently long to interact with xrcc4 and to stabilize the interaction of xrcc4 with lig4. A single XLM motif and C-terminal tail is sufficient to promote end joining.
Sequence:
MEAVLSALPWVPVNISGSDLLAKAWFGDSQYRVLLTDLSTVWEEEMSTDDIQSRAQDLNKRLRAPAQAFFSHLCSVARPCFSGLDEDQISAAQAALEQHGESLTVKLKSELAGLPFYWEFRCTTTPVAVVCRQLVRPLLAMTLVLQRQAEDLAALLARKDAEIQDYQENGAVLSRARLQTEPFEVHQYKENFITQILPQMNVTLDSLGFDSELQALYMAVNSGKTGRKRKHSPDSSPAAQENHITDHQHISESTDVGPSLASQEHNNAKESGRSQVANSQQTLPLSSTAGSEDRSTSRAKKKKAVGLFR
The following text describes a protein:
Function:
Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation.
Miscellaneous:
MISCELLANEOUS: Present with 8350 molecules/cell in log phase SD medium.
Subcellular Localization:
Golgi apparatus, cis-Golgi network. Endoplasmic reticulum. Preautophagosomal structure.
Sequence:
MSQRIIQPSASDQQFPGKSDGYEYTVGPKQAITSEASTTYIPSRIYSESLLFKRQEASLSAMAFLFQEMISQLHRTCKTAGDFETKLSDYGHNIGIRLLELLNFRASVSPSSLPRASAFLSQNESSSKLSNASNSPGMLANSSTATSASANERLQEKQTESLSNYITKMRRRDLKILDILQFIHGTLWSYLFNHVSDDLVKSSERDNEYMIVDNFPTLTQFIPGENVSCEYFVCGIIKGFLFNAGFPCGVTAHRMPQGGHSQRTVYLIQFDRQVLDREGLRFG