lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Endomembrane system; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MSFETAGYQLAPVLPELVLAVGAMALLMLGAYRGQETTKTVTTLAILLLIVVGVLEYMLPAGKQVTFGGSFIVDDFARFMKILALIGSAVTLVLSTEFLSDPSRRIFEYAILVLLSTLGMMVLISAGDLISLYLGLELMSLALYVVASSNRDNAKSTEAGLKYFVLGALSSGMLLYGSSLVYGFTGTVSFTGIAATATTANVGLVFGLVFLLAGLCFKVSAVPFHMWTPDVYEGAPTPVTAFFASAPKVAALAVFTRVTLTAFPGIVSQWQQILVFVAIASMALGSFAAIGQSNIKRLMAYSSIGHMGFALVGLASGTVEGAQGVLMYIVIYVAMTLGSFSIILAMKRNGQAVEQISDFAGLSRTNPLLAFMFAMLLFSLAGIPPLAGFFAKWYVFVAAIKANLFTLAVIGVLSSVVGAYYYLAIVKTMYFDEPAGQVDPVRVEVKTVLAVAGLFNILFALFAGPVVSVASAAAKSLF
The following text describes a protein:
Function:
ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. Catalyzes an ATP-dependent conformational change of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA (By similarity).
Subcellular Localization:
Nucleus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MSIDNQASTALKNSGQEVKNNTNQTSELSKEEKLRKRREQLELWRQKKQQQQQEQEEVQNKAKKTEDSTNNTSTEEVKKSRQQRIEEWKRARLQKQQATKEKTTTITIKKKVHSQTTRPTLKRNLDFGDDEDDRKNSHRPVFKKPSLEYDEISEHQNDKESEDELDVFLASIRESELKSDNTKAEKAIESIPEGDVENEKENDDYGGDGDEEDESDEESRLQDLISTKLTKLQNKGKELQSIDHSQENYQEFRKVFYREAYELSALSDEQVELIRQDLDNIKVKGTDVPRPILKWSHLALPTNLSSVIHDKLKFEKPSAIQSQALPTILSGRDVIGIAKTGSGKTLSYVLPMLRHIQDQQFSKDNQGPIGLILSPTRELALQIEKEILNFTKRNNNLRVCCCYGGSSIENQINELKKGVEIIVGTPGRVIDLLAANSGRVLNLKRCTFVVLDEADRMFDLGFEPQVNKILTQIRPDRQTVLFSATFPRKMETLAKQILTDPVVIIVGGISVVAPEIKQEVVLFETSAEEQDKYKQQRVEKLHDILTNYQIEHPDSKILVFTEKQNDADELVANLLSNKYPAIAIHGGKDQMDRKYAIKEFASMDSGINILIATSIAARGLDVRNLGLVINFDPPNHMEDYVHRVGRTGRAGAKGNAITFVSSSQPKEVFNLVKALKLSHSDIDPKLEEIANKFVTKVKAGKEKISSGFGGKGLDNLQEVRDNKLKLEKQRFGDQQPQRQQEETETKKSNDEPVPDIALPEFNIIEGNTPETSGPDKCKFYCRIVINDLPQKVRWNIVQRESLSKIIDESRTSITTRGQYYPPGSKPLSNDQERNGSLAKLYLLVEGLTLQSVTEAITLIKKKMLESLDILNQRENLQPTGRYVV
The following text describes a protein:
Function:
Involved in pectic arabinan modification in mucilage secretory cells. Also acts as a beta-D-xylosidase during the remodeling of xylans in vascular development.
Miscellaneous:
MISCELLANEOUS: Might be processed at the C-terminus.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MSCYNKALLIGNKVVVILVFLLCLVHSSESLRPLFACDPANGLTRTLRFCRANVPIHVRVQDLLGRLTLQEKIRNLVNNAAAVPRLGIGGYEWWSEALHGISDVGPGAKFGGAFPGATSFPQVITTAASFNQSLWEEIGRVVSDEARAMYNGGVAGLTYWSPNVNILRDPRWGRGQETPGEDPIVAAKYAASYVRGLQGTAAGNRLKVAACCKHYTAYDLDNWNGVDRFHFNAKVTQQDLEDTYNVPFKSCVYEGKVASVMCSYNQVNGKPTCADENLLKNTIRGQWRLNGYIVSDCDSVDVFFNQQHYTSTPEEAAARSIKAGLDLDCGPFLAIFTEGAVKKGLLTENDINLALANTLTVQMRLGMFDGNLGPYANLGPRDVCTPAHKHLALEAAHQGIVLLKNSARSLPLSPRRHRTVAVIGPNSDVTETMIGNYAGKACAYTSPLQGISRYARTLHQAGCAGVACKGNQGFGAAEAAAREADATVLVMGLDQSIEAETRDRTGLLLPGYQQDLVTRVAQASRGPVILVLMSGGPIDVTFAKNDPRVAAIIWAGYPGQAGGAAIANIIFGAANPGGKLPMTWYPQDYVAKVPMTVMAMRASGNYPGRTYRFYKGPVVFPFGFGLSYTTFTHSLAKSPLAQLSVSLSNLNSANTILNSSSHSIKVSHTNCNSFPKMPLHVEVSNTGEFDGTHTVFVFAEPPINGIKGLGVNKQLIAFEKVHVMAGAKQTVQVDVDACKHLGVVDEYGKRRIPMGEHKLHIGDLKHTILVQPQL
The following text describes a protein:
Function:
Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSNYKNCRWFMPVNILLTFVIGSMLGWLLLIIARPPQHLKGLIIGTCAAGNLGNMLLIILPAVCKEKASPFGDPDVCYEYSIAYASLSLAIGAVYLWLYVYNLVRVFAGPPIDSGNKDVASTDETVTVQEDLTRTLLPSSLSSTNINGKSKVMLNVMKQQLRNFSRHINLKAVDAAIPIVTLIVGGNLLRGLKGSGISLPIVFGIVSVKYVFLPVCGILMVKGAIYLGFVDIADPLYVFILLLQFAVPPAMNTGTIMQLFGVGESECSVIMLWTYGLASVSLSLWSTIFMWLVS
The following text describes a protein:
Function:
Actin-based motor molecule with ATPase activity that localizes to the mitochondrion outer membrane. Motor protein that moves towards the plus-end of actin filaments. Required for mitochondrial inheritance during mitosis. May be involved in mitochondrial transport or positioning.
Sequence:
MLQQVNGHGSGSAAHSGESLREDLKELLGGEVPPQQLNDLTKVNPVTLETVLRCLQARYMADTFYTNAGCTLVAMNPFKPVPQLYSPELMREYHAASQPQTLKPHIFTVGEQTYRNVKSLIEPVNQSVVVSGESGAGKTWTSRCLMKFYAVVAASPMSWESHKVAERIEQRILNSNPVMEAFGNACTLRNSNSSRFGKFIQLQLNGAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQIYKGAHAEERVRWRLPEGAAFSWLPHPERTLEGLWLGFLYRGLFRGDQGGHASFGHRCPHPEQHLSGSVGTSALLLGLPEDHLLETLQIRTIRAGRGQQVFQKPCSQAECNTRRDCLAKLVYARLFDWLVSVINSSICAAPDSWTTFIGLLDVYGFESFPNNSLEQLCINYANEKLQQHFVAHYLRAQQEEYAMEGLAWSFVSYQDNQPCLDLIEGSPVSICSLINEECRLNRPSSAAQLQTRIESALTGHPRLGRDRLSPEPSFIVLHYAGPVRYRTAGLVEKNKDPVPPELTSLLQQSQDPLLKVLFPADPEDKSPEEPSGQNRAPVLTVVSKFKASLEQLLQVLHGTTPHYIRCIKPNSQAQAQIFHREEVLSQLEACGLVETIHISAAGFPIRVSHRNFMERYQLLRRLRPAITPSPHGPCPDGGRSECPPCTEPATLQGLLQEILHTLPAPLHCGRTKVFMTDSTLELLERGRAQVLEQCARHIQRGWRRHRCRTQARRRRAAVLIQAAVRSWLTRKHIQQLHAAATVIKRAWREWRIRMAFLASEELDGVEEKHSPHAPCSPGSSPLPPAQTRLQGAITRLWPLGLALANAAVGVHGFQRKLVVFACLQLPVGSPRSCAVQTAQEQAGVLSIRALPQGSIRFHCRKSPLRYADTCPGPSPDSVTGFNQILLERHRPGHV
The following text describes a protein:
Function:
Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor.
Subcellular Localization:
Periplasm.
Sequence:
MKPLLTALLLVLLGAPAAFAADLGYPLDAPAPDGRRPGGTLAESRPAPPLAAEENKDLKRERNYPEQPPTIPHSIVGYRIDKDSNKCLSCHSRANSARTQAVMISITHYMDRDGQPLAAVSPRRYFCVQCHVPQQDVKPLVDNRFENIDQILEKEAANAARKP
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MWSLRVLVLTAACGLFSSVNAWKNTNLIRTYDLTKSYVKETITIKLENDLQEAANVYTLMKDLVDDERVVSAVALEKTQGGSVSLDIVPSLTTEDGLDIRFPSPVLPGESKTIHVSLTLDGAQKPVPAKIKQDDQQYLVYRASKTFVSPYDTEKQRLKFKFPTNNVPSFTEFTDASGNKQPARAGNTLTYETLETVERDTPKELVSVRYEYTAPLPRARQLDIEVDIHQFRKEISVVEKTTLENHAAELRGHFNRAKWAMSRFYNPLTAALGSFRIYLPKDVRDVSFKDEDGNVTTSHMRADRQHTVLDLIPRFPVFGGWNYYFRLAWNMALDSFAADKNGRTVVTLPSMWSLEDALFSNVSWTLTLPEGAKDIKVNVPTELSLKNVTTVYHFLDIQGRQSFVYEASDVSDEFSQKVIEISYVYDTLAHRLRLAVIVGIIGVLFTAAYMIWAP
The following text describes a protein:
Function:
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor. No activity with brassinosteroids.
Subcellular Localization:
Cytoplasm.
Sequence:
MDEKDILRNLREEEEEEEENQSEETKILISSLPWEIDYLGNKLFKYQGYWYYEDVLQSIPNIHSSFQPQETDIVVASFYKSGTTWLKALTFALVQRSKHSLEDHHHPLLSHNPHEIVPYLELDLYLNSSKPDLTKFLSSSSSSSSPRLFSTHMSLDALKLPLKKSPCKVVYVCRNVKDVLVSLWCFLNANKGVEWGDFSQNEKIIRAENYSFKAIFESFCNGVTLHGPFWDHAQSYWRGSLEDPKHFLFMRYEELKAEPRTQVKRLAEFLDCPFTKEEEDSGTVDKILELCSLSNLSSLEINKTGSLGGVDYKTYFRKGQVGDWKSYMTSEMVNKIDMIVEEKLKGSGLKF
The following text describes a protein:
Function:
Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
Sequence:
MKYGRMNPRFLVTEACVPIAQNCSFPCAVSLEIDDPKEKQGRSISEEIVSQQDDGVFATKDRETCSQVSSKVVKGLKQKTAEVSREGGSIVNSASIGVDSAHGRVGYAVVGLYSLGQTCFFNSVIQNLLAIDSLRVYFCKVEKDVGPVSGALRKIFLQTNIGTGLREPIVPRSLFECLCIKAPQFRENQQDDSHELLRCLLDLLSHEEMQPRKHSKFSQAPIPGPTFVNDLFGGRISSTITCTKCQHSSTCYEAYLDLSLTVPAKRDQLVVLLVDGCLALFVEPEILSNDNGWHCENCSRVMREQRVVDSENLKVTTDATKRCSERVRFTYRLVGVVEHRGVMEGGHYIAYVRGTKDNGDCVWYCTNDIRIREVSLEKVLCSKACILFDERTRRSSDYHVH
The following text describes a protein:
Function:
Binds and cleaves RNA, particularly in stem-loops. Associates with pre-ribosomal particles in chloroplasts, and participates in chloroplast ribosomal RNA metabolism, probably during the final steps of 23S rRNA maturation. May enhance transcription by the plastid-encoded polymerase and translation in plastid via the stabilization of ribosome assembly intermediates. Required for chloroplast integrity. Involved in the regulation of the circadian system. Involved in the regulation of heteroglycans and monosaccharide mobilization. Required for full expression of genes transcribed by the plastid-encoded RNA polymerase (PEP). Essential for embryo development.
Subcellular Localization:
Plastid, chloroplast, plastoglobule. Plastid, chloroplast. Cytoplasm. Note=Present in stromules. In the cytoplasm, accumulates around chloroplasts.
Sequence:
MAKMMMLQQHQPSFSLLTSSLSDFNGAKLHLQVQYKRKVHQPKGALYVSASSEKKILIMGGTRFIGLFLSRILVKEGHQVTLFTRGKSPIAKQLPGESDQDFADFSSKILHLKGDRKDYDFVKSSLSAEGFDVVYDINGREAEEVEPILEALPKLEQYIYCSSAGVYLKSDILPHCEEDAVDPKSRHKGKLETESLLQSKGVNWTSIRPVYIYGPLNYNPVEEWFFHRLKAGRPIPVPNSGIQISQLGHVKDLATAFLNVLGNEKASREIFNISGEKYVTFDGLAKACAKAGGFPEPEIVHYNPKEFDFGKKKAFPFRDQHFFASVEKAKHVLGWKPEFDLVEGLTDSYNLDFGRGTFRKEADFTTDDMILSKKLVLQ
The following text describes a protein:
Function:
Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation (By similarity). Hydroxylates the guanylate binding protein 128up. May be involved in regulation of behavior and circadian rhythms.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MSEVERALDVLLQEAEELCIGSSVVELDRIPTALEFCREFYSKNQPVVIRKALNWPAIGKWTPKYLIEALGDRSVDVAITPNGYADGLATQNGQEYFVLPLETKMKLSEVVRRLDDPTGAVHYIQKQNSNLSVDLPELAADLRVSDLDFAQQSFNKPPDAVNFWLGDERAVTSMHKDPYENVYCVISGHKDFVLIPPHQLSCVPRGIYPTGVYKTSDSGQFYIEPLRDEEGSDQFTEWVSVDPLSPDLAKYPEYARAKPLKVRVHAGDILYLPNYWFHHVSQSHKCIAVNFWYDLDYDSRYCYYRMLEQMTSARSG
The following text describes a protein:
Function:
Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MITTVSSPEKCFPTFCSLSQLNLLCFFTLGLAFCNKFNGGVVFKGDISKVSDELAVGLTTGFLGIFTSGWNQKILDRSERIRNGGAKPQLFLACLVGPFCVWIRFFSARFNGRGLGKNVANDEFGLLGCLSTVSTFVAELHAKYESKHPWRDCAYAATTFSISFILGTLIVPVWVKGL
The following text describes a protein:
Function:
Orphan nuclear receptor.
Sequence:
MAQPIPTDPMHFPTTHGYPAIYPYGQQYPPDMSNFAANPQFTPELFQMYFQLYTNQQFTHPAPPHPATEIESSSHTQASPTMNQSSEEGRDSGNETISPPLPPQPHLYQNNSSQTTPAVSPHYPAPLPPQVQHQTPVQVITPEQHLQQINQTIPNNQTPVQLAPQNSAYAINNLLSPQNSPNAEEDEQENRQTRRNTFPTSENRKRPIPSGPPIVPPNFTSNYTPMMMQNFAAFMDPSYFKRESCQICGDSASGYHYGVLSCEGCKGFFRRSVHRKSTYVCQKGAACSFSLENCTINRGIRTRCQACRYARCLAVGMNKESVRITKDEPKKTEYTKWSEAQSNELKELTEVFKSTMPSSMRFNSFNDVFEAIKKLIEDVKGLKTIFKSDSGNIPNVIRLFSKGFLTIRAAFTFDTIPFYSAINPNFNSDVEQLRSGIRNTVFNDNLLALVTAIHIIKSAESGENSSVLPIYCKELRSQFSITHPQESGIYERIIAKLGPCSN
The following text describes a protein:
Function:
The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin.
Sequence:
MVARMTSENLPRKGGGRDRNRRDSGHHSGRLFASYPQTKTYFPHFDLSQSSAQLRTHGSKVISAIGEAVKNIDNMGGALSKLSELHAYILRVDPVNFKVGCRPGGRGGLGRELGRVLGRARDSPCNSPDSSSLLPQLLSHCILVSLASRFPADFTAEAHAAWDKFLSIVSSILTEKYR
The following text describes a protein:
Function:
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Subcellular Localization:
Cytoplasm.
Sequence:
MGKNTFEENLENLDKIIESLESGELSLDDAIKEYENAMKLIKSSSKILNEAEGKLLKVIEKNGEIDIEEI
The following text describes a protein:
Function:
Potential disease resistance protein.
Domain:
The LRR repeats probably act as specificity determinant of pathogen recognition.
Sequence:
MANSYLSSCANVMVERINTSQELVELCKGKSSSALLKRLKVALVTANPVLADADQRAEHVREVKHWLTGIKDAFFQAEDILDELQTEALRRRVVAEAGGLGGLFQNLMAGREAIQKKIEPKMEKVVRLLEHHVKHIEVIGLKEYSETREPQWRQASRSRPDDLPQGRLVGRVEDKLALVNLLLSDDEISIGKPAVISVVGMPGVGKTTLTEIVFNDYRVTEHFEVKMWISAGINFNVFTVTKAVLQDITSSAVNTEDLPSLQIQLKKTLSGKRFLLVLDDFWSESDSEWESFQVAFTDAEEGSKIVLTTRSEIVSTVAKAEKIYQMKLMTNEECWELISRFAFGNISVGSINQELEGIGKRIAEQCKGLPLAARAIASHLRSKPNPDDWYAVSKNFSSYTNSILPVLKLSYDSLPPQLKRCFALCSIFPKGHVFDREELVLLWMAIDLLYQPRSSRRLEDIGNDYLGDLVAQSFFQRLDITMTSFVMHDLMNDLAKAVSGDFCFRLEDDNIPEIPSTTRHFSFSRSQCDASVAFRSICGAEFLRTILPFNSPTSLESLQLTEKVLNPLLNALSGLRILSLSHYQITNLPKSLKGLKLLRYLDLSSTKIKELPEFVCTLCNLQTLLLSNCRDLTSLPKSIAELINLRLLDLVGTPLVEMPPGIKKLRSLQKLSNFVIGRLSGAGLHELKELSHLRGTLRISELQNVAFASEAKDAGLKRKPFLDGLILKWTVKGSGFVPGSFNALACDQKEVLRMLEPHPHLKTFCIESYQGGAFPKWLGDSSFFGITSVTLSSCNLCISLPPVGQLPSLKYLSIEKFNILQKVGLDFFFGENNSRGVPFQSLQILKFYGMPRWDEWICPELEDGIFPCLQKLIIQRCPSLRKKFPEGLPSSTEVTISDCPLRAVSGGENSFRRSLTNIPESPASIPSMSRRELSSPTGNPKSDASTSAQPGFASSSQSNDDNEVTSTSSLSSLPKDRQTEDFDQYETQLGSLPQQFEEPAVISARYSGYISDIPSTLSPYMSRTSLVPDPKNEGSILPGSSSYQYHQYGIKSSVPSPRSSEAIKPSQYDDDETDMEYLKVTDISHLMELPQNLQSLHIDSCDGLTSLPENLTESYPNLHELLIIACHSLESFPGSHPPTTLKTLYIRDCKKLNFTESLQPTRSYSQLEYLFIGSSCSNLVNFPLSLFPKLRSLSIRDCESFKTFSIHAGLGDDRIALESLEIRDCPNLETFPQGGLPTPKLSSMLLSNCKKLQALPEKLFGLTSLLSLFIIKCPEIETIPGGGFPSNLRTLCISLCDKLTPRIEWGLRDLENLRNLEIDGGNEDIESFPEEGLLPKSVFSLRISRFENLKTLNRKGFHDTKAIETMEISGCDKLQISIDEDLPPLSCLRISSCSLLTETFAEVETEFFKVLNIPYVEIDGEIFS
The following text describes a protein:
Function:
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MLKIKLEKTTFENAKAECSLVFIINKDFSHAWVKNKELLETFKYEGEGVFLDQENKILYAGVKEDDVHLLRESACLAVRTLKKLAFKSVKVGVYTCGAHSKDNALLENLKALFLGLKLGLYEYDTFKSNKKESVLKEAIVALELHKPCEKTCANSLEKSAKEALKYAEIMTESLNIVKDLVNTPPMIGTPVYMAEVAQKVAKENHLEIHVHDEKFLEEKKMNAFLAVNKASLSVNPPRLIHLVYKPKKAKKKIALVGKGLTYDCGGLSLKPADYMVTMKADKGGGSAVIGLLNALAKLGVEAEVHGIIGATENMIGPAAYKPDDILISKEGKSIEVRNTDAEGRLVLADCLSYAQDLNPDVIVDFATLTGACVVGLGEFTSAIMGHNEELKNLFETSGLESGELLAKLPFNRHLKKLIESKIADVCNISSSRYGGAITAGLFLNEFIRDEFKDKWLHIDIAGPAYVEKEWDVNSFGASGAGVRACTAFVEELLKKA
The following text describes a protein:
Function:
GTPase-activating protein (GAP) for CDC42 and/or RHO1. Negative regulator of the pheromone-response pathway through the STE20 protein kinase; acts at a step between the G-protein and the MAP kinase module. Dominant suppressor of bud emergence defect caused by deletion of IPL2/BEM2. Involved in the control of polarized cell growth and proper bud site selection.
Miscellaneous:
MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
Sequence:
MASTAPNEQFPSCVRCKEFITTGHAYELGCDRWHTHCFACYKCEKPLSCESDFLVLGTGALICFDCSDSCKNCGKKIDDLAIILSSSNEAYCSDCFKCCKCGENIADLRYAKTKRGLFCLSCHEKLLAKRKYYEEKKRRLKKNLPSLPTPVIDNGHTDEVSASAVLPEKTFSRPASLVNEIPSGSEPSKDIETNSSDIVPHFITGYNDSDDNSGSSKFGSNVSIDVIGPEENSTEHVNDDVKEEAEAPSANMSLNVATDPTLSCKEPPSHSRNLLNKTPLRNSSGQYLAKSPSSYRQGIIVNDSLEESDQIDPPNNSSRNASELLTSVLHSPVSVNMKNPKGSNTDIFNTGEISQMDPSLSRKVLNNIVEETNALQRPVVEVVKEDRSVPDLAGVQQEQAEKYSYSNNSGKGRKISRSLSRRSKDLMINLKSRATGKQDSNVKLSPASKVTSRRSQDLMRDNDSHTGLDTPNSNSTSLDILVNNQKSLNYKRFTDNGTLRVTSGKETALEEQKNHSFKSPSPIDHLLQSPATPSNVSMYRTPPLDSSLTFDRRNGSSYSNQNYSIPSWQKTPKTQLENSDNFEEQKETLYENSESRNDPSLDKEIVTAEHYLKQLKINLKELESQREELMKEITEMKSMKEALRRHIESYNSEKNKLYLDSNELSNNPPMINEISLGESPPVKHVATASSVARSSVKPKFWKFFSSAKPQTEQSIQGVSTNNTNSIVKSAPVLLSAPSSGSNSGRLEISPPVLQNPNEFSDVRLVPIENDANMGQSKDGEEYLDGSNLYGSSLVARCNYENNEIPMILSVCIDFIESDEENMRSEGIYRKSGSQLVIEEIEKQFSAWKVQQNTETPNILTEQDLNVVTGVLKRYLRKLPNPIFTFQIYEPLMRLVKSKKMMENLPFVGGKLSLEAKNSDTYMSSKSALKNILEDLPREHYRVLRVLSEHIEKVTRYSHWNRMTLYNLALVFAPGLIRDFSGEKDIIDMKERNYIVAFIFGNYKDILT
The following text describes a protein:
Function:
Forms a fork protection complex (FPC) with TOF1 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:
MSYVMDETEEGINIDNTQHDLELDRDSSTQQPAQTHEDDGDLLGLDKPIKLKTRAKIAKVDNQRIFNHNGIPLLVKTHSKLLRTLKKNDKNFYSEPRSSISKSQKFEHEYENLSSVLQFYQLWCHGLFPKATFKDCIHLIRALGARSPQLRLYRRELIAAELHKLKVAKGIIADENQDAPSIPEEENTTDPSNEEWNSMHMSALVPGSSNKNGLFVDSNSNEDFETTNEVNAAASLADKDALSTDDKAEQTNAITSDTHNNDVDSDDPFSDDDDINIDAHTENLHPASGTQHQDRPKETTEENEDLELELMREYGA
The following text describes a protein:
Function:
Adrenomedullin/ADM and proadrenomedullin N-20 terminal peptide/PAMP are peptide hormones that act as potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis; [Adrenomedullin]: ADM function is mediated by the CALCRL-RAMP2 and CALCRL-RAMP3 receptor complexes with ADM showing the highest potency for the CALCRL-RAMP2 complex.
Subcellular Localization:
Secreted.
Sequence:
MKLVPVALLYLGSLAFLGADTARLDVASEFRKKWNKWAVSRGKRELRVSSSYPTGLAEVKAGPAQTLIRTQDVKGASRNPQTSGPDAARIRVKRYRQSMNNFQGPRSFGCRFGTCTVQKLAHQIYQFTDNDKDGVAPRSKISPQGYGRRRRRSLPEPGLRRTLLFPEPRPGGAPAPRAHQVLANLLKM
The following text describes a protein:
Function:
May be required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX1.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MATLGHTFPFYAGPKPTFPMDTTLASIIMIFLTALATFIVILPGIRGKTRLFWLLRVVTSLFIGAAILAVNFSSEWSVGQVSTNTSYKAFSSEWISADIGLQVGLGGVNITLTGTPVQQLNETINYNEEFTWRLGENYAEEYAKALEKGLPDPVLYLAEKFTPRSPCGLYRQYRLAGHYTSAMLWVAFLCWLLANVMLSMPVLVYGGYMLLATGIFQLLALLFFSMATSLTSPCPLHLGASVLHTHHGPAFWITLTTGLLCVLLGLAMAVAHRMQPHRLKAFFNQSVDEDPMLEWSPEEGGLLSPRYRSMADSPKSQDIPLSEASSTKAYCKEAHPKDPDCAL
The following text describes a protein:
Function:
Together with MOM1 and PIAL1, regulates transcriptional gene silencing (TGS) independently of changes in DNA methylation. E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates. Involved in stress responses and sulfur metabolism.
Subcellular Localization:
Nucleus.
Sequence:
MSTAAAARPVAGTGLREKTAASLVNSFRLASVTQRLRYHIQDGAKVDPKEFQICCISFAKGIDFAIANNDIPKKVEEFPWLLKQLCRHGTDVYTKTALMVLMISVKHACHLGWFSDSESQELIALADEIRTCFGSSGSTSPGIKSPGSTFSQIMERFYPFVKLGHVLVSFEVKAGYTMLAHDFYISKNMPHSLQEKIRLFVAQTDNIDTSACISNPPEVSFLLNGKGVEKRVNIAMDTGPQLPTNVTAQLKYGTNLLQVMGNFKGNYIIIIAFTGLVVPPEKPVLKDYLQSGVIEASPDSDIIEGPSRVSLSCPISRKRIKLPVKGQLCKHLQCFDFSNYVHINMRNPTWRCPHCNQPVCYPDIRLDQNMAKILKDVEHNAADVIIDAGGTWKVTKNTGETPEPVREIIHDLEDPMSLLNSGPVVFDLTGDDDAELEVFGDNKVEDRKPCMSDAQGQSNNNNTNKHPSNDDYSSIFDISDVIALDPEILSALGNTAPQPHQASNTGTGQQYSNLSQIPMSIDPMPVPVPFSQTPSPRDRPATTSTVFTIPNPSPQYSQVHASPVTPTGTYLGRTTSPRWNQTYQSQAPPMTTPYTSRKVSVPVTSQSPANVSSFVQSQHVPRVLSQPNNYGVRGLTSSHASTSRQHPSGPTVQSVSRLSDLVDVDLTVPDTSNWRPRMRGSLVPGSHSTALDHMIIRPSQQSQTSTRLNSSQPVQTPSVQTSQAQSPFTTAAYRTETVLGNRNHPVPAPPGIVRPTGPTS
The following text describes a protein:
Function:
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins (By similarity).
Subcellular Localization:
Cytoplasm.
Domain:
The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity (By similarity).
Sequence:
MEQVRNYYQILGVPRNATAEEIKKSFRKLARQYHPDVNPNDKTAEEKFKDINEAYDVLSDETKRRELDSRLFGRFRRPPTSRFSPNSNGGRSPNGTSVNGQVRTPTGRTGTRQPAQSWQDFSETRRTKVVSPARPVPRDVEANLTLPLEKAYRGGKERIRLEDGRSLEVEMPGGMGDGQRIRLKQQGINGGDLYLKINLSPHPLFTLQGTDIACQVPVTPSEAILGGAIEVMTIDGLVKMTVPAGLKNGQKLRLAKKGFPNNQGDRGDQLVEIRVEIPPEPSPEELELYRRIREKETFNPRQKFFDF
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MFRSPISYCDGVCFLSSTPSCQNARLYSTVSSTGSGSFSPVKWLLSIGVVSTSVYFGAAYAATKNETIHKLWINNQVPGGEAALDLTRSFESRIRKINLSDIHQSVSDTTDMIKTNAEHAFDYTGRTIHQATEMTNATIETVSGYVDTVSNATSDTIKVATNVINETTDTIQSVVHDAEAVYSSVVSAVTGVTARQSESKADSSSSAKPSAVTAPAISNAEPQPAAKKPVAEKKVTETPAIVKIQTDDHPASPKTLKKQDLPSEKTIAAPVSAPTPVPAVMEKQTPVDDKTSKTVLETKIEKKPVVTKVKSKPEVKETPVEKVAVPQSPPLIETIDAEAGVKAIQNRLPVFESFMVTLDDLSKTVNHLLNEAEPLSGDATHLRKARKDLDALTKFVTHLEADEVAMVHTALSQQAVIFQRTIDAVRENSNNALSQKALELESELTSKLLDQEKNLTSAYEHNLAEQLIKQAEEFRAALDIDLQRQAAELEKFWSHEVKERVDQEREGRLSRLDHLALKVKYLERISLDAGEGFDRSHRIHQLQTALRAIRLAIDNPHTTNFSQELKALQALCEGDEFVSQIVSSLPKDAARQYTSYQELTNYLHNITTPLRRSQLVSDDTGALSYALSLFLSYFILPKHGRVAGTDLESILARTEHHLFNNRMDEATREINQLSGWPKRLSRDWLAKARTHLEIQQAIKLIEVHLNLQSMGVV
The following text describes a protein:
Function:
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
Sequence:
MVESVPMTREGYNKIKAEINRMENEEMPMIVQKIAEAREEGDLKENAEYHAQRENQGMLMAKINELRDKIARASIIDVSSLPKDEVVFGCTVTVEDVAYGDEEQFTLVGAGDEDYDSGKILVTSPFGQGLVGKKVGETAEVDVPAGKLKFKILKIEFNL