lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular Localization:
Mitochondrion.
Sequence:
MNQCRLRSLARIRRSLTLGLRGTDQHVLARQALRTIQTTSQRRGVHDLDSFANGCSAAYIEGLYNKWKRNPSSVDESWNELFSSNDWSSPKRSPLQVSHSRKYRRPPVERIAVKARSGERTASGGASAAPAAPPSDWKNIDDHHVIQAIIRAYQSRGHLAADLDPLGIVGPKKRTSVDGTQRHAAREVLRQHFSYIFNDLNTVFKLPSSTMIGGDQEFLSLKEILDRLERIYCGHIGVEYMQITSLTKTNWLRDRFEKPGGLDLTKEEKKLILERLTRSTGFENFLAKKFSSEKRFGLEGCDIMIPAIKEVVDRATDHGVESILIGMAHRGRLNVLANICRKPISDILSQFHGLQATDSGSGDVKYHLGVFQERLNRQTNRMVRITVVANPSHLEHVNPVLLGKARAEMFQRGDTCGSTVMPIIIHGDASFSGQGVVYESMHLSDLPNYTTYGTIHIVSNNQVGFTTDPRFSRSSRYCTDVAKVVNAPILHVNADDPEACIQCARIAIDYRTRFKKDVVIDIVGYRRNGHNEADEPMFTQPLMYQRIKKLKPCLQLYADKLIKEGVVTDSEFKAMVSSYEKICEDAWAKSKTIKTIKYSSWIDSPWPGFFEGRDRLKLCPTGISTDTLKTIGNMFSTPPPPEHKFETHKGILRILAQRTQMVQDKVADWSLGEAFAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHHQSEDKVVYNSLDHLYPDQAPYSVSNSSLSECAVLGFEHGYSMASPNALVMWEGQFGDFCNTAQCIIDTFIASGETKWVRQSGVVMLLPHSMEGMGPEHSSGRIERFLQMSDDDPDVYPDTCDADFVARQLMNVNWIVTNLSTPANLFHCLRRQVKMGFRKPLINFSPKSLLRHPLARSPFKDFNECSCFQRIIPDKGPAGKQPDCVQKLVFCSGKVYYDLVKERDDHEQVETVALVRVEQVRRLPTRHLFLFMITMIGRILQLCPFPYDLISQQLELYPKAELLWAQEEHKNMGAWSYVQPRFDTALLKNENESRCVSYHGRPPSASPATGNKVQHYNEYKALITSIFGELTPENKKRIEDRIKKQQAKAKADAQSKPSTKPPAAPPKGGSSPPPGKGESGGKKRSDSSPSASIAPTGPAPRKPLISLPSRPPRGGKQRSGSAPAPNLVDEDSAARNREPDASAYDGASPSAWKRSGSAPAPSVVPRASASRSPSRKSPSPSHDGISPSTRQESLSKKKSGSAPAPTPTSRGPFRTAPSNTEFIKRRPAKDYGSRNETQSTPGESELDPTKPQP
The following text describes a protein:
Function:
Functions as a guanine nucleotide exchange factor (GEF) for Rab small GTPases. Activates specifically RAB5A protein (Probable). Functions cooperatively with RAB5A to regulate post-Golgi dense vesicle-mediated transport of storage proteins to the type II protein bodies (PBII) protein storage vacuoles in developing endosperm.
Subcellular Localization:
Cytoplasm. Golgi apparatus, trans-Golgi network. Prevacuolar compartment. Note=Expressed in trans-Golgi network and prevacuolar compartment when recruited by GPA3.
Sequence:
MDGGGGGDAFGSATAPLAWHDFLERMRQPSAADFVKSIKGFIVTFSNRAPDPEHDSAAVQEFLENMEGAFRAHTPWAGSSEEELESAGEGLEKYVMTKLFNRVFASVPEDVKSDEELFEKMSLLQQFIRPENLDIKPEYQSETSWLLAQKELQKINMYKAPRDKLACILNCCKVINNLLLNASIVSNENPPGADEFLPVLIYVTIKANPPQLHSNLLYIQRYRRQSRLVSEAQYFFTNILSAESFIWNIDGESLSMDERDFQKKMDLARERMLGLSASSENQDNQNNLDVREQKSQTLKASRDSDVNLSLKDNFQGPGLEMRRDSDASSNPVERVQSISDLEKKGAAELLKDDDLNKKIQEYPFLFARSGDLTVADVENLLNSYKQLVLKYVALSQGMGINLENPPVQSMQTVSDLVESEEPKNVKNAVNFSEGSSKTSDDIKNDTLYSEVDNTGTQQTAVDPSYQKAQQDEASDQPEHA
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MNGISEQRSSPKTVFEDLRLSIDPTTIRLALGEKPVKSIDPDGTIAYDETKTPDAKLTEQLERIWNEYPNGLLELTERKLERLPPDEDAVKPQGEGVDEEKKRDPFSMMTYEEMEKLRSEIFLQLNDARNELWFVLELAKTLSSSSSFTTQPPPPPAALHQKKGKAKPAPPAPTTLPSIPGEPPILPPGTFSTTPSDFPIKPPHAQIYELERLLQAKRIALNECQGLIDGAVGELRLMAHAGDRFWKDIRNLKEGEGGRGQWAVVPKPDFGRVGGEGEKAKDVVIPYAIDEAPSGTRARCLAGFDLDPTKKDGLTFGDRHHLRLRATLRDDSGAVISSTPVKVEDQSDVRAMMEAAQMEAFDEDLFNEIRFAAARIPKNETEPQRVSFPVADKILSFELYDTRSLPSSPTSSICDIIVSSTRLSLLNIHRQRKINLVAPSQNFASPIPSILLPIIDTLRFRQLCSLVSSTLNGFDRTLRDAGLDSRMEKRMLKDGQDEIKEMRAVLLGKRGAEVLTGEYSLGIDDSYIITINISAPYNTIVYLSSISFPLANPDELSQVVSDDLSVQLLRLASRHLHGKLADEHKKGLYFDSLEEVIRIGETGLLRLSIPASFHTIYGSVESDWISVQAYDSRQSDITVFAWLDTVTHAIESSLSSNGSTTQVR
The following text describes a protein:
Function:
Involved in the release of fatty acids from the oil body in germinating seedlings. Can hydrolyze triacylglycerols and diacylglycerols but not monoacylglycerols, phospholipids, galactolipids or cholesterol esters. SDP1 lipase activity is required to limit triacylglycerol accumulation in roots, leaves and stems, which are vegetative tissues. Functions synergistically with PDAT1 in regulating fatty acid flow from membrane lipid synthesis toward peroxisomal beta-oxidation through a transient triacylglycerol pool.
Miscellaneous:
MISCELLANEOUS: Transcript levels do not correlate positively with enzyme activity, suggesting a post-transcriptional regulation.
Subcellular Localization:
Lipid droplet. Membrane; Peripheral membrane protein. Peroxisome. Note=Associates with the oil body membrane. Migrates from peroxisomes to the oil body surface through peroxisomal tubulation.
Sequence:
MDISNEASVDPFSIGPSSIMGRTIAFRVLFCRSMSQLRRDLFRFLLHWFLRFKLTVSPFVSWFHPRNPQGILAVVTIIAFVLKRYTNVKIKAEMAYRRKFWRNMMRTALTYEEWAHAAKMLEKETPKMNESDLYDEELVKNKLQELRHRRQEGSLRDIMFCMRADLVRNLGNMCNSELHKGRLQVPRHIKEYIDEVSTQLRMVCNSDSEELSLEEKLSFMHETRHAFGRTALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELQSFFENSLHSLQFFDQLGGVFSIVKRVMTQGALHDIRQLQCMLRNLTSNLTFQEAYDMTGRILGITVCSPRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRSGEIVPYHPPFNLDPEVGTKSSSGRRWRDGSLEVDLPMMQLKELFNVNHFIVSQANPHIAPLLRLKDLVRAYGGRFAAKLAHLVEMEVKHRCNQVLELGFPLGGLAKLFAQEWEGDVTVVMPATLAQYSKIIQNPTHVELQKAANQGRRCTWEKLSAIKSNCGIELALDDSVAILNHMRRLKKSAERAATATSSSHHGLASTTRFNASRRIPSWNVLARENSTGSLDDLVTDNNLHASSGRNLSDSETESVELSSWTRTGGPLMRTASANKFIDFVQSLDIDIALVRGFSSSPNSPAVPPGGSFTPSPRSIAAHSDIESNSNSNNLGTSTSSITVTEGDLLQPERTSNGFVLNVVKRENLGMPSIGNQNTELPESVQLDIPEKEMDCSSVSEHEEDDNDNEEEHNGSSLVTVSSEDSGLQEPVSGSVIDA
The following text describes a protein:
Function:
Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MKLPLLRPLWPGLAPAAGSPDAAPEPAKPSLPAAWLLLHALFCATSMAVGFRFSRLIVYLLFLPTPPINPAAHLVSLVSPPVMLAGAGNATTATITTTTTTTTTVTTTTTVAAEIGAAHPHHHHGPVFVGRHPIRVRSWPHPDPNELLKAHRILAAVQNAQRSSKRRGAGPPRPVIAVTPTTTSALQVPSLTSLAHTLRLVDAQLMWIVVEPGHRTDAVAAVLSRSNLDFLHITGPGDSTASLRMHALREIRAKRMDGIVVFADENSILRTELFDEGQKVSTMGAVPVGILGEDDGASESFLQAPSCDAAGKLVGYHVSEETVLPVNRSDMLLSSRLEWTGFVVSARVLWEDAKERPQWVRDLAAIDDADARAASPLALVTDAGRVEPLAGCAQAALAWSLRSESLHDVKFPHEWKIDPPLLNTGSHQENAKPETPLKQTNLASTEDQH
The following text describes a protein:
Function:
Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
Subcellular Localization:
Nucleus.
Domain:
The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Sequence:
MAEQGAGEADAGGGEPPPAAVMTAAAEALAGQRSLPTPFLTKTYQLVEDPAVDDVISWNEDGSTFVVWRPAEFARDLLPKYFKHNNFSSFVRQLNTYGFRKIVPDRWEFANDCFRRGEKRLLCDIHRRKVVAAAAAAPPPPSPGMATAAAAVASGAVTVAAAPIPMALPVTRAGSPAHSSEEQVLSSNSGSGEEHRQASGSGSAPGGGGGGSASGGDMGEENERLRRENARLTRELGHMKKLCNNILLLMSKYAATQHVEGSAGISSIANCSGESSEAVPPPPPLPPAILDLMPSCPALATAAAAAGLAIDGEPDPSARLFGVSIGLKRTRDDAAAAADEDGGGEDQAEHGGADVKPEAADPHPAGGGGGSSTEASPESHPWPIYRPTPMYHAVRPTCNGPDRAGSDQDGSSSSQTMGPGEFDDLQKMMVVQQSNFVMHWGRSECGSGVRGFGW
The following text describes a protein:
Function:
ABC transporter involved in fatty acid import. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTTDTRGPAPGRSAVVLALRHYGRELLRLRRLALPALLLPAVGNIGIRYIAPLLIAKLAGQAADDGGLTLGRALPYVLGFGLTLLLAEAVWRVGQHCLNRVDALGMEHLYVSGMDELLAKDAAFFHDNFAGSLTKRVLSFGKRFEDFVDTVTYRIVGSLVPLVFGAVVLWSYEPMLVVGLFLMIGLTVVAATPLIRRRQRLVNDREAAIARVSGHVADSLMNMETVRAFAAERREAAEHRGRVADSRRLTLRSWDYGNLRVDTLIAPMSVLTNVLGLLVAIAFGGPGQGVEEVVVAFTYYSNATQIMFEFNQIYRRLESSTTEAAQFTELLLDPPTVVDADAPAPLAPRDSGIRFEAVTFAHAGAKPIFRGLDLDVPAGARIGLVGRSGGGKTTLTRLLLRMSDIERGRILIGGQDISLLRQSDLRSLIAYVPQEPAMLHRSLRDNIAFARPGATDEEIHAAAAAAHVTEFADQLPDGFGTLVGERGVKLSGGQRQRVALARAILRDAPVLLLDEATSALDSESELLVQDALWRLMDGRTALVVAHRLSTVAGMDRLVVLDRGRVVEQGPHEKLLAADGAYARLWRHQSGGFLGESTGPTVDGDGRDDGDGRDDGDGRVDGDGRDDGDRRDDGDRRGGGPPHVRPRRESSGPPSEEAARSAP
The following text describes a protein:
Function:
Involved in the regulation of phagocytosis. May repress rab21.
Sequence:
MIKANWTSTSAFNLELALDESRDWIERVINQKFPSDFQSSLRDGIFLCKLINQIQPNSVPKYNQSPSTDFAKRENIQLFIKSAKHSMGLRDTQLFESQDLFESIRIRNIAITLYWLGRAARASQTYKGPQLDLLKFQGMNCSACKKAITNNDYLTTMTQQFHTSCAVCCSCSCKLDPKKKFYQESNNFWCENCMLGATNLGGSNNSSGGKNKSNNNNNNKCSGCFGSLEKGYVPDENDKEKKYCTSCICDLCHDPLIGNFQVKDGKKVCDSCSCKSCGKSLEDGYYEEGISKYCEPCAKDRNKPKQVMDKDGHDHHHHNHNKPTTTTTTTNSNSPLAKKKSDSCKMCDKPVDNKTKKYGDDRDKYCTPHEKDGTCGKCNGELVGSAISVMDKNFHPQCFKCDSCNKNLNQNDQIKKSPTTGNPLCGPCSSNNNKSSKNCHDCKKPISGSSVEALDRPYHPNCLKCYSCSKNLKEDFTEVDNEPFCNPCASQLNQYTSGNQKQPKQGGSPFITSGWLDSDRCVVCVKPLNGEVAKIFDSFYHKGCFKCTDKSCNAPLLTGYFPHDKKPYCQKCSIKIQQSTTTDHCAKCSKPIIEGSILKVAGKVYHKSCYDNEKHTSSSSSSSSVNCFKCKSQITGTQFVRLDQKDYCMKCSPSASSSTTVTHGERLNYGMTVDPRSGKRVFNTSK
The following text describes a protein:
Function:
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MVFRIASSPYTHNQRQTSRIMLLVLLAAVPGIAAQLWFFGWGTLVQILLASVSALLAEALVLKLRKQSVAATLKDNSALLTGLLLAVSIPPLAPWWMVVLGTVFAVIIAKQLYGGLGQNPFNPAMIGYVVLLISFPVQMTSWLPPHEIAVNIPGFIDAIQVIFSGHTASGGDMNTLRLGIDGISQATPLDTFKTSVRAGHSVEQIMQYPIYSGILAGAGWQWVNLAWLAGGVWLLWQKAIRWHIPLSFLVTLALCAMLGWLFSPETLAAPQIHLLSGATMLGAFFILTDPVTASTTNRGRLIFGALAGLLVWLIRSFGGYPDGVAFAVLLANITVPLIDYYTRPRVYGHRKG
The following text describes a protein:
Function:
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Sequence:
MDFFGLDTDRLQSGEQHKSVLGSNDLKFCLEIVVEISNFIKTSLGPKSGDKLIVDENGNIIVTNDGYSIIKYLSKSSKFDDEDDEDDQDNNIINLESSHHNNNNKYNNNNNNNNNNKNFSKSSSINRKRFQTVVELLIDCCKTQERLYGDGTTSVLVLIGSFCSSALKLIFEKGIPPHIVSNAFQNSLNHALKLLNNNYYLNVNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSENNNEISLEKVTESSLLSKSISFYKEELSKLSIESVKLIYSFYKRVELKRIKVITIQGSTLEDCRLIKGCLIKRFFSHENMPKTIDNASIIVLSFPLEFPKPKTNFNISINSIDQLNQFIEIKSNYYQSIKDAIKLIKGLKCVVCQWGIDQEINQFLYQFGISAISWVGGDDLERISISSGANIINDLDSLLLLNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNISDQFIGYVGQIKELVMGNDSSSRYIEFSDCKNSSTVTILVRGGSKEMCDETAQCLRDSIHIVGGCLKDPRIVPSGGSTELYLFNQFKHFKSATTTTMMMMAIKSWSESLLTIPITLLENGGYDCQKHIIKLIQIHSDNDFRYYGVNINNNTSDRCNKEFDLYNCSISMDTNQNIIQDMKFKSWELLNLKKSILKLATETTCMLLSMDAFICL
The following text describes a protein:
Function:
Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
Sequence:
MKLRPYLTCETGLICFEDGSRTSTHTMSDWTPEGALPADLKEEIAAAATGTESLLAFLNVVERLKTTPRTGWLRYKMIDDPESIADHQYRMSIIAMLSLSPVNQNTCVKMALVHDMAEAIVGDITPFDDMTKAEKSRREHSSIIYMAALVEKYNPVAAKEIVDLWNQYENCSTDEARLVKDIDKFELMLQTYEYEKQHKFAEDLSQFYTLRGVIKTEEIGKLADELLRKRQLAMDKLGVKWD
The following text describes a protein:
Function:
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Subcellular Localization:
Cytoplasm.
Sequence:
MQHKLIAFIGGGNMAQAIILGLLKQGYPAEQIIVNDPNEEKRAFFANLDVATSENNVGSAIKAEVVLLAVKPQMMAEVCSPLSAVDFSDKLLISIAAGISTERLNALIPSVKSIVRVMPNTPALVGEGMAGLFAPKNTSENYRTFAQDLLGAVGRTVWVNDETQMHAVTAASGSSPAYFFLMLEAMQKALIKMNIDEKTARELVQQSMLGAAKMVTENPQIALSTLRENVTSKGGTTAAALAVFDAQHFNQTIEQAMQACLSRSQEMETLF
The following text describes a protein:
Function:
Extracellular metalloprotease that contributes to pathogenicity.
Sequence:
MRSSTTVLILLVSLACFASANYEGYQVWRIKPTTENQMRWLSYVEENMADEFDFWTGISRIPGHPVDIMVRPNGQGTLRMLLKQQKMDFEIMIDEVNKLVSNQMAEILARRKGEQSIGIRLDNFDYNVYHTYDEIQQWVADMASENSDIIEPFLLGKSYEGREINGFRIRGTGSQSANPPGVWFEGGIHAREWVSPSTVMGFTQKLIDQYRAGEDLVVRMFDNIDWYIVPSLNADGYSYTWTNDRLWRKTRSPNAGAACTGTDPNRNWPYQWGGVGTSPWPCSDIYHGSEALSEVEVANVVAFLRKKKTEGQDFMVFIDWHSYSQVIISPWSYLDSDPRTEDYDDQMAMATAMSDAILATSQKVYGYGAGAEILYPAAGSSKDWGYASFLENWGDTVGGLGAKYSYTVELRDTGEYGFLLPEDQIQDTYDEIHAAVRAIGTHVLNELGL
The following text describes a protein:
Function:
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Subcellular Localization:
Cytoplasm.
Sequence:
MNRVVVGLQWGDEGKGKVVTYLSRYHDIVARFSGGANAGHTVNYGDFKVIHHLLPSADFTKNRGIAIGSGVLLDPQVLTEELRELKEKFPDYSGEIFISESAHVVLPVHKEMDRIIDEVLKIGTTKRGIGPACADRVMRVNVRVAELGNEEKLRYFLEKNLSLKKIYGVDFDAEKMMGDLSTFYETIKDFVVSPVQLKRILEEKSVLFEGTQGVLLDLDVGTYPYVTSMNCSSSGVSAGMGFPVEVDEVLGVFKAYTTRVGEGPFPTELTGEEGEKLRKAGHEYGSTTGRPRRCGWLDLPLLRYAIEISGVDSLVMTKADVLNGFEKIKVCVRYSDGRDLVSLRDLEKKEPVYEVFDGWKSLEDKNFERFVDFIERETGRPVRYISTGEKLEDIVEV
The following text describes a protein:
Function:
Catalyzes the reversible ATP-dependent phosphorylation of mevalonate 5-phosphate to produce mevalonate diphosphate and ADP, a key step in the mevalonic acid mediated biosynthesis of isopentenyl diphosphate and other polyisoprenoid metabolites.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
SQPPSSSLSAPPTCTSPPPGPCAPSTHNSSPGQGPFGEILTSVGHLPLLSLRGGAQPRGVTCPLRSSLGRFPASKGQVNQLGQDRQRREATRCGEKVSAAPFGRLGADVCAILRLSGPLKEQYAQEHGLNFQRLLDASTYKEAYRRDMIRWGEEKRQADPGFFCRKIVEGVSQPVWLVSDTRRVSDIQWFQETYGAMTQTIRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGGFDWVIENHGDEQRLEEQLENLIEFIHSRL
The following text describes a protein:
Function:
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Sequence:
MSFDSLPALPLDPLPDAALPTAPRRRQTVSVNVGGVMVGSAHPIVVQSMTNTDTANAEATAIQVAQLARAGSEIVRVTVNTREAAAAVPELVQRLADIGVHVPIVGDFHYNGHLLLREYPETARLLAKYRINPGNVGAGQRHDENFATMIEVAKEFDKPVRIGVNWGSLDQQVLARLMDENAAAGHPKSPTDVTIDAMIVSALDSARFAEELGLGHDKILISVKVSSAPELWQVYRQLAPLCDYPLHLGLTEAGMGMKGIVASSVALAPLLTEGIGDTIRVSLTPEPGAPRKLEVEVAQQILQSLGLRQFLPQVTSCPGCGRTTSSFFQTLAQKIQDFIRESMPEWKAKYPGVEDMQVAVMGCVVNGPGESKHANIGISLPGTGEDPRAPVYQDGKLLTTLKGPRIAEEFQELLEKYVEERYGQGVAQG
The following text describes a protein:
Function:
Histone demethylase that demethylates 'Lys-9' (H3K9me) of histone H3 with a specific activity for H3K9me3 and H3K9me2. No activity on H3K4me3, H3K9me1, H3K27me2 and H3K36me3/2. Involved in the control of floral organ development by demethylating H3K9me3 and H3K9me2 in the promoter regions of DH1 and MADS47. The 'Lys-9' demethylation of these two genes is required for induction of their expression.
Subcellular Localization:
Nucleus. Note=Localizes mainly in heterochromatin foci.
Sequence:
MQQVEGRNCLPAEVRIGLETLKRRRLERMRLTAQNNAGDGPPVPARSGGDALRTPANCGVRLHANNGTALPSRTTQNKDPFAKRRVDKFDMSSLEWIDKIEECPVYYPTKEEFEDPIGYIQKIAPVASKYGICKIVSPVSASVPAGVVLMKEQPGFKFMTRVQPLRLAKWAEDDTVTFFMSERKYTFRDYEKMANKVFAKKYSSASCLPAKYVEEEFWREIAFGKMDFVEYACDVDGSAFSSSPHDQLGKSNWNLKNFSRLSNSVLRLLQTPIPGVTDPMLYIGMLFSMFAWHVEDHYLYSINYHHCGAFKTWYGIPGDAAPGFEKVASQFVYNKDILVGEGEDAAFDVLLGKTTMFPPNVLLDHNVPVYKAVQKPGEFVITFPRSYHAGFSHGFNCGEAVNFAISDWFPLGSVASRRYALLNRTPLLAHEELLCRSAVLLSHKLLNSDPKSLNKSEHPHSQRCLKSCFVQLMRFQRNTRGLLAKMGSQIHYKPKTYPNLSCSMCRRDCYITHVLCGCNFDPVCLHHEQELRSCPCKSNQVVYVREDIQELEALSRKFEKDICLDKEISGFDSYKQAEKNEPFFEITRNLRNTEVNLIEDAFSGATAADAAKSSPATSTLTSFAQHDVPVLAEAIVCANQADQLYSTTEQTISSPLVKGTDAVGANSSSMADANNGTGSCNASAVEYSGNSDSESEIFRVKRRSGVSVKPASDAKTSNLSDQQVLRRLKKVRPEIQQHNKRPEDYGHCSVPSGRMSMKNLNSSSSCGEEHWRMKRRQLETQQDESSYSAKQKSYSYPSTSYSFRGEFVEMSRDAAAEVRPKRLKIRLPSSSTNRVVEQGSSGQRFTRDDKSLGCWPAI
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase (By similarity). Required for mesoderm patterning during embryonic development (By similarity). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP. Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP (By similarity). In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL. Associates with UBE2D2 as an E2 enzyme. Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates. Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (By similarity). Mediates ubiquitination and degradation of sumoylated PML (By similarity). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm. Nucleus, PML body. Note=Upon TGF-beta treatment, translocates from nucleus to cytosol.
Domain:
The SUMO interaction motifs (SIMs) mediates the binding to polysumoylated substrate; The RING-type zinc finger mediates the E3 ubiquitin-protein ligase activity and binds directly to free ubiquitin (By similarity). Non-covalent ubiquitin-binding stabilizes the ubiquitin-conjugating enzyme E2 (donor ubiquitin) in the 'closed' conformation and stimulates ubiquitin transfer (By similarity).
Sequence:
MSQWTPEYNELYTLKVDMKSEIPSDAPKTQESLKGILLHPEPIGAAKSFPAGVEMINSKVGNEFSHLCDDSQKQEKDMNGNQQEQEKSLVVRKKRKSQQAGPSYVQNCVKENQGILGLRQHLGTPSDEDNDSSFSDCLSSPSSSLHFGDSDTVTSDEDKEVSVRHSQTILNAKSRSHSARSHKWPRTETESVSGLLMKRPCLHGSSLRRLPCRKRFVKNNSSQRTQKQKERILMQRKKREVLARRKYALLPSSSSSSENDLSSESSSSSSTEGEEDLFVSASENHQNNPAVPSGSIDEDVVVIEASSTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHASRPQEPRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTVVPTTSARMESQATSASINNSNPSTSEQASDTASAVTGSQPSTVSETSATLTSNSTTGTSIGDDSRRTTSSAVMETGPPAMPRLPSCCPQHSPCGGSSQNHHALGHPHTSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPPQVQAPCGANSSSGTSYHEQQALPVDLSNNGIRSHGSGSFHGASAFDPCCPVSSSRAAIFGHQAAAAAPSQPLSSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPTYASLTRPLHHQASACPHSHGNPPPQTQPPPQVDYVIPHPVHAFHSQISSHATSHPVAPPPPTHLASTAAPIPQHLPPTHQPISHHIPATAPPAQRLHPHEVMQRMEVRRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERSAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGTSFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES
The following text describes a protein:
Function:
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Sequence:
MTPVLSLDMEDPIRFIDENGSFEVVKVGHNLAIHGKKIFDELAKRNLKIILDLKFCDIPSTVERSIKSWDHPAIIGFTVHSCAGYESVERALSATDKHVFVVVKLTSMEGSLEDYMDRIEKLNKLGCDFVLPGPWAKALREKIKGKILVPGIRMEVKADDQKDVVTLEEMKGIANFAVLGREIYLSENPREKIKRIKEMRL
The following text describes a protein:
Function:
Binds to membranes via its F-BAR domain and mediates membrane tubulation. Plays a role in cellular transport processes by recruiting dynamins to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with cobl, and by recruiting cobl to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission (By similarity). Required for normal embryonic development, including normal development of laterality, normal body size and shape, as well as normal brain and heart development. Required for normal development of stereocilia and kinocilia in sensory hair cells of neuromasts in the posterior lateral line organ, and thus also for balance keeping and normal swimming behavior.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Synapse, synaptosome. Synapse. Cytoplasmic vesicle membrane; Peripheral membrane protein. Cell projection, ruffle membrane. Membrane; Peripheral membrane protein. Note=Detected in axons. In primary neuronal cultures, present at a high level in presynaptic nerve terminals and in the cell body. Detected at vesicular structures in neuron cell bodies and neurites (By similarity). Detected at the apical surface of cells at the basis of forming cilia, but not in the cilia themselves.
Domain:
The F-BAR domain mediates membrane-binding and membrane tubulation.
Sequence:
MSGAYDESAMSDETTDSFWEVGNYKRTVKRIEDGHRLCNDMMSCIQERAKIEKAYSQQLTDWSKRWRQLVERGPQYGTLERAWLAVMTEAEKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQMMGGFKETKEADEGFRKAQKPWAKKLKELETAKKTYHMACKEEKIASAREANSKGEASVTTDQQKKLQEKVDKCKNDVQKAKEKYEKSLDELNKCTPQYMENMEVVFDQCQQFEEKRLNFLREVLLDTKRHLNLTESQSYATVYRELERTIVSASAQEDLKWFSSVHGPGMHMNWPQFEEFNPDLSHAISKKEKVKRNHDGVTLTQVTHGAEHGTPQTGDRGSVSSYEKNQQYSAEWSDDEQPPTAAQSASETNGGNPFEEDSKGVRVRALYDYEGQEQDELTFKAGDELTKLEDEDEQGWCKGRLDSGQLGLYPANYVEPV
The following text describes a protein:
Function:
Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells.
Subcellular Localization:
Cytoplasm.
Sequence:
MADGTNRTNGTSSFDFPKFTYDKKDFVMDCQSWKVKPQNFKLSKFDNLLRTSWTQAMADGCFKYTLDSMETKLVPGKFGVVAQLNEKRFVERRKPQQITSVSQPYDPGKFNFTKVQDKEILFEVCPSDQNSSPPNYMIINVSPLEFGNCLLVPSVFDQTPQILTVDSLKLAFDIAFLSSHRGFHIGYNSLCAFASVNHLHFHVWYLDYPSPLETLPTKHVHKDMYEVTNFPTKIFVFYLSSAADVERIARQVHAVTSYFVSNEIAHNLSICRGLGQGSDADSSAVRVYLWPRKPVIGAKDETGFNIAVCEMGGHLPIRTRTFFESITEQDFIDQLKSVTLEEQEFHRLKEHITHLL
The following text describes a protein:
Function:
Component of the ribosome.
Sequence:
MGVTFKISKTGQLNPKSIDLSEKSKAIVESSAGDASGFLQSSLLHVSPDYEFSFVLSLYLNGYSIGKPSEAVKQTSFRDAPKTLDKNIATQLFKVLMKYRPEDKAAKKDRLLKKAQAEAEGKPSESKKPIVVKYGLNHMTYLSEQNKAQIVVIAHDVDPIELVVWFLHFAERWKCLTALSKANLVLERSFTRRLLLACV
The following text describes a protein:
Function:
Odorant receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTNSSVKGDFILVGFSDQPHLEKILFVAVLISYLFTLVGNTVIILIFDICFTTSIVSQLLWNLKGPDKTITFLGCVIQLYISLALGSTECVLLAVMAFDRYAAVCKPPHYTAVMNPQLCQALAGVAWLSGVGNTLIQGTVPSMIKLACVDIHDNEVQLFVASLVLLLLPLVLILLSYGHIAKVVIRIKSVQAWCKGLGTCGSHLIVVSLFCGTITAVYIQSNSSYVHAHGKFISLFYTVVTPTLNPLIYTLRNNDVKGALRLFNRDLGT
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MARLHISVLFAAALILLVSAKKSGDVTELQIGVKYKPESCTIQAHKGDKIKVHYRGSLTNGEVFDSSFERGDPIEFELGSGQVIKGWDQGLLGMCVGEKRKLKIPAKLGYGAQGSPPKIPGGATLIFDTELVAVNGKSSSDAGKSTVDESEL
The following text describes a protein:
Function:
Protein-lysine N-methyltransferase. Monomethylates PRMT5, modulating its transcriptional activity. May also act as a histone methyltransferase. Plays a critical role in cardiac development. Acts as a key epigenetic regulator of gene expression during cardiac development via its dual activities as a methyltransferase and negative regulator of HDAC1.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MNIDTLSDTIAQGFIAKVHELLANKSSCKSKELSLRWCLAGDLAFTKSQFHRALSYYSQAIQYFPHQTGDQQSTLQICLPSILSKRAEVLFLVGEYEASLNDIAEASSLQYNHVIRDKLLKLQKSCLRKQARHSQNKNGSSGSACLSGGRHPKMANGSSLLKINYDQNQGRFLQASSEIRAGDTLIAEEPYSAVLLPENAKTHCECCYKSLVAPVPCNHCSSVLYCSAACRNKAWSQYHHVECEIFPVLEIVDTFTHLSLRILLTTSAKDIIDVLNGLSRDVATTSCSLPGCTVSGSYPGDYGSVFSLVTNSDLQPIKALMSFAMNSAFLVEFLENGTSSACIHCSQIKSDKTKVQTELDSDDDSDCSEVYNACEEQRTQNGNFEQDRTICSRNTPYSRQAYTSLGITTEEFCGKDGLSSDVVGALLVHHLQQMPCNVHAITAIVSTSSSDEEDEEMGSSHDQVVAREQRRIASAIYPTASLLNHACDPDVLVSFVDGVLVARATHNIAPGSGITHCYGPHVNHMPREERQKLLYKQYFFTCQCSACTSDEEMENTRLCFSAFACPRCKCPMKTSPLEPSLARCQNKKCTLEKSIEEELSHSRQAELLFFKAVRTMERIGVQEALGLFQECLRTRTQILHPHHKDLAETHDALARCYAMIGDFKLASQHCLQSSEAVEKAFGSTSVEYAHELHKLSQLLFNDRQAKKALPMIDKAASLLATYYGRNHPDVQELVEMKACLTSNGSVHINY