wanglab/gogpt-training-data huggingface dataset:
Protein: DNA replication licensing factor mcm10 (Cdc23 protein) (Minichromosome maintenance protein 10) (O42709)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for DNA synthesis. Required for entry into or completion of S phase. Involved in DNA replication and seems to participate in the activation of the pre-replication complex (pre-RC) and in transcription elongation. May play a role as key coordinator in assembling the replication fork. Proposed to function at replication origins following the binding of the mcm2-7 complex prior to the recruitment of sna41. Probably is required to stimulate phosphorylation of the mcm2-7 complex by the dfp1-hsk1 kinase complex. May recruit the DNA polymerase alpha:primase complex to replication origins and is required to maintain it on chromatin independently of sna41. May have primase activity. Binds to single-stranded DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:10783164}. Note=Associates with chromatin.
Interaction partners:
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm6
- Cell division cycle protein cdt1
- DNA replication licensing factor mcm2
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm5
- DNA replication licensing factor mcm7
- DNA replication regulator sld2
- Origin recognition complex subunit 2
Sequence:
MHDPFIAEENDLDLEEKRLQRQLNEIQEKKRLRSAQKEASSENAEVIQVPRSPPQQVRVLTVSSPSKLKSPKRLILGIDKGKTGKDVSLGKGPRGPLPKPFHERLAEARNQERKRSDKLKTMKKNRKQSFQRKRNILEDGKSEEEKFPMKCDEIDPYSRQAIVIRYISDEVAKENIGGNQVYLIHQLLKLVRAPKFEAPEVDNYVVMGIVASNSGTRETVNGNKYCMLTLTDLKWQLECFLFGKAFERYWKIQSGTVIALLNPEVLKPKNPDIGRFSLKLDSEYDVLLEIGRSKHLGYCSSRRKSGELCKHWLDKRAGDVCEYHVDLAVQRSMSTRTEFASSMATMHEPRARREKRFRGQGFQGYFAGEKYSAIPNAVAGLYDAEDAVQTERERKERYKKQRAQAEREREILVRLSKRCCASSSSSSNSNNLSTGMSMRTLGHQYLNLQGSGVKNLHDKGNPTALSKDSEIDSSTKKPSVLASFNASIMNPKSSLPSFSNSAILGTNDAASGTPVPQDTTSTKVSPAVVFTSSPRIFSPQSLRKIGFDPTHSADASTTHSTATGLSRSGSLKNIKFRYEFTESDDEDDLEIVP
Protein: Solute carrier family 26 member 9 (Anion transporter/exchanger protein 9) (Q7LBE3)
Organism: Homo sapiens (Human)
Function: DIDS- and thiosulfate- sensitive anion exchanger mediating chloride, sulfate and oxalate transport. Mediates chloride/bicarbonate exchange or chloride-independent bicarbonate extrusion thus assuring bicarbonate secretion. May prefer chloride anions and mediate uncoupled chloride anion transport in an alternate-access mechanism where a saturable binding site is alternately exposed to either one or the other side of the membrane (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17673510, ECO:0000269|PubMed:26801567}; Multi-pass membrane protein {ECO:0000269|PubMed:32818062}. Endomembrane system {ECO:0000269|PubMed:26801567}; Multi-pass membrane protein {ECO:0000269|PubMed:32818062}. Note=Localization to the cell membrane is inhibited by WNK kinases (WNK1, WNK2, WNK3 or WNK4) in a kinase-independent mechanism. {ECO:0000269|PubMed:17673510}.
Interaction partners:
- Cystic fibrosis transmembrane conductance regulator
Sequence:
MSQPRPRYVVDRAAYSLTLFDDEFEKKDRTYPVGEKLRNAFRCSSAKIKAVVFGLLPVLSWLPKYKIKDYIIPDLLGGLSGGSIQVPQGMAFALLANLPAVNGLYSSFFPLLTYFFLGGVHQMVPGTFAVISILVGNICLQLAPESKFQVFNNATNESYVDTAAMEAERLHVSATLACLTAIIQMGLGFMQFGFVAIYLSESFIRGFMTAAGLQILISVLKYIFGLTIPSYTGPGSIVFTFIDICKNLPHTNIASLIFALISGAFLVLVKELNARYMHKIRFPIPTEMIVVVVATAISGGCKMPKKYHMQIVGEIQRGFPTPVSPVVSQWKDMIGTAFSLAIVSYVINLAMGRTLANKHGYDVDSNQEMIALGCSNFFGSFFKIHVICCALSVTLAVDGAGGKSQVASLCVSLVVMITMLVLGIYLYPLPKSVLGALIAVNLKNSLKQLTDPYYLWRKSKLDCCIWVVSFLSSFFLSLPYGVAVGVAFSVLVVVFQTQFRNGYALAQVMDTDIYVNPKTYNRAQDIQGIKIITYCSPLYFANSEIFRQKVIAKTGMDPQKVLLAKQKYLKKQEKRRMRPTQQRRSLFMKTKTVSLQELQQDFENAPPTDPNNNQTPANGTSVSYITFSPDSSSPAQSEPPASAEAPGEPSDMLASVPPFVTFHTLILDMSGVSFVDLMGIKALAKLSSTYGKIGVKVFLVNIHAQVYNDISHGGVFEDGSLECKHVFPSIHDAVLFAQANARDVTPGHNFQGAPGDAELSLYDSEEDIRSYWDLEQEMFGSMFHAETLTAL
Protein: DNA-directed RNA polymerase subunit beta (RNAP subunit beta) (EC 2.7.7.6) (RNA polymerase subunit beta) (Transcriptase subunit beta) (P60281)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit often mutates to generate rifampicin (Rif) resistance. Interaction with RbpA partially restores Rif-inhibited transcription; once the subunit is Rif-resistant however RbpA no longer stimulates transcription.
Interaction partners:
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta'
- RNA polymerase-binding transcription factor CarD
- DNA-directed RNA polymerase subunit omega
- RNA polymerase sigma factor SigA
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein uL11
- RNA polymerase-binding protein RbpA
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL6
Sequence:
MLEGCILAVSSQSKSNAITNNSVPGAPNRVSFAKLREPLEVPGLLDVQTDSFEWLVGSDRWRQAAIDRGEENPVGGLEEVLAELSPIEDFSGSMSLSFSDPRFDEVKASVDECKDKDMTYAAPLFVTAEFINNNTGEIKSQTVFMGDFPMMTEKGTFIINGTERVVVSQLVRSPGVYFDETIDKSTEKTLHSVKVIPGRGAWLEFDVDKRDTVGVRIDRKRRQPVTVLLKALGWTNEQIVERFGFSEIMMGTLEKDTTSGTDEALLDIYRKLRPGEPPTKESAQTLLENLFFKEKRYDLARVGRYKVNKKLGLNAGKPITSSTLTEEDVVATIEYLVRLHEGQTSMTVPGGVEVPVEVDDIDHFGNRRLRTVGELIQNQIRVGLSRMERVVRERMTTQDVEAITPQTLINIRPVVAAIKEFFGTSQLSQFMDQNNPLSGLTHKRRLSALGPGGLSRERAGLEVRDVHPSHYGRMCPIETPEGPNIGLIGSLSVYARVNPFGFIETPYRKVENGVVTDQIDYLTADEEDRHVVAQANSPTDENGRFTEDRVMVRKKGGEVEFVSADQVDYMDVSPRQMVSVATAMIPFLEHDDANRALMGANMQRQAVPLVRSEAPLVGTGMELRAAIDAGDVVVADKTGVIEEVSADYITVMADDGTRQSYRLRKFARSNHGTCANQRPIVDAGQRVEAGQVIADGPCTQNGEMALGKNLLVAIMPWEGHNYEDAIILSNRLVEEDVLTSIHIEEHEIDARDTKLGAEEITRDIPNVSDEVLADLDERGIVRIGAEVRDGDILVGKVTPKGETELTPEERLLRAIFGEKAREVRDTSLKVPHGESGKVIGIRVFSREDDDELPAGVNELVRVYVAQKRKISDGDKLAGRHGNKGVIGKILPVEDMPFLPDGTPVDIILNTHGVPRRMNIGQILETHLGWVAKAGWNIDVAAGVPDWASKLPEELYSAPADSTVATPVFDGAQEGELAGLLGSTLPNRDGEVMVDADGKSTLFDGRSGEPFPYPVTVGYMYILKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMECWAMQAYGAAYTLQELLTIKSDDTVGRVKVYEAIVKGENIPEPGIPESFKVLLKELQSLCLNVEVLSSDGAAIEMRDGDDEDLERAAANLGINLSRNESASVEDLA
Protein: PslE (Q9I1N4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PslD
- PslF
- PslG
- PslJ
- PslH
- PslI
- PslA
- dTDP-Rha:alpha-D-Gal-diphosphoundecaprenol alpha-1,3-rhamnosyltransferase
- Alginate biosynthesis protein AlgA
- PslL
Sequence:
MIEIRSLRDLLRLLFIYQREFKLAALSAVVIIVLGAFLLPAKYESNARLLVKPGRDSTLPIEISNRQALVMPSTQRDPIVDEERLLTGRPIVRQVAERYLEVLANRPPPEGLWKRTKFYVKKAIGAVFDGIRVTLETFGVIEETTAVERLAKDLEKKFEVTHAAGSTVMEISFTWSEPEVAQEVVKAWIEIYMEERTQALGRKSLYAFYEAQTADSAAQIKSYKAQILKHLNEIGASSIEDRLQDLSERINVLRGERFNSIRLIASSDSALESTRQQLKGLPREIVTVRQIALNPAQQDLRRLLNQKRLERADMMRTYTDDAPPVKALDASIRALEKEVQDEGATVQSSEDRAPNTLTTHLERVLLDETSNNAALRTQLAEQEKQLAELEAQRREALDIEPTLARLQRELNATERNYALYVDSLEKSRIDRELDKSQISNISVIEEATYNPGRIFPKTLLMLFLAVPFGLAVGLLVVYLCYLLDQRIHDGGLVEEKFGLPLWTTLPELSNSTAESSNAFTASIYRLYGLLPYARIEEKGLTLGLTSARHGEGVTFIIEQLRRLLEENGVRVRIGGEPAQPGEVVLLDAPALLDSREAFIALRRADLIALVVEAQKSTVPVVEHALTILTTAFGKVDGIIINRRRFEVPSKVLQTIARYRSAF
Protein: ADAM metallopeptidase with thrombospondin type 1 motif 14 (E9PX39)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MAWLRALLHCLLPWYCALCAAAGSQTPDLRLSGKLHDYVVTVPCSTDFQGRFLSHVVSAPAAPSPRSHLRVARSPLSLERETPRPGGPRQHFLYFNVTVFGKLLHLRLQPNRRLVAPGAPVEWQEDFRELFRQPLQQECVYTGGVTGMPGAAVAISNCDGLAGLIRTDNSDYFIEPLERGQQEKEAGGRTHVVYRREAVQREWKEPHGDLHNEAFGLGDLPNVLDLVGDRLGDAERKRRHAKPGSYSIEVLLAVDDSVVRFHGREHTQNYVLTLMNIVDEIYHDESLGAHVNIALVRLIMVGYRQSLSLIERGNPARSLEQVCRWAHSQQRQDPSHTEHHDHVIFLTRQNFGPSGMQGYAPVTGMCHPLRSCALNHEDGFSSAFVVAHETGHVLGMEHDGQGNGCDDETSLGSVMAPLVQAAFHRFHWSRCSKLELSRYLPSYDCLLDDPFERTWPQPPELPGIDYSMDEQCRFDFGTGYHTCLAFRTFEPCKQLWCSHPDNPYFCKTKKGPPLDGTECAPGKWCFKGHCIWKSPEQTYGQDGGWSSWTNFGSCSRSCGGGVRSRSRSCDNPPPAYGGRPCSGSMFEYQICNSEDCPGPYEDFRAQQCAKRNSYYTHQDAKHSWLPYEPDSDAQKCELICQSADTGDVVFMNQVVHDGTRCSYRDPYSVCARGECVPFGCDKEVGSMKTDDKCGVCGGDNSHCRTVKGTLGKGSKQAAALKQVQIPAGARHIQIELLEKAPHRIAVKNQVTGSFIFNPKGKEASSRTFTALGLEWEHEAEDTKDSLRTNGPLPEAIAILVLPPAEGKPRGSLAYKYVIHEDLLPLIGSNNVLLEETDTYEWALKSWSPCSKACGGGIQFTKYGCRRRRDHHMVHRHLCDHKKRPKPIRRRCNQHSCPQPTWVTEEWGACSRSCGKLGLQTRGVQCLLPLSNGTHKAMPAKACLGNRPEAKKPCLRVPCPAQWRTGAWSQCSATCGEGIQQRQVVCRNTSSALGPCEGVKPDMVQICSLPACGGDLQNSTVKAEVQDPVTKTGYREPQSRPLTPEDRISTMEPCVRDRSVFCRMEVLDRYCTIPGYHRLCCESCIKKTSGPNASLALPPTFSTPGSLLPAPKATLEDVKSTRGPTSLEDHRQSQPTQLPDVADRISPVTQYPVTPQMLSPKAFPGNSPATPRRPPQDWTQTAMPTSEGQGQSREEPGHGGTSLPATSPVT
Protein: Inactive tyrosine-protein kinase 7a (Zgc:112211) (Q502I0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGLWTRRRGRKLASAENVLLALTLIGEVIMAQAASFYFTKAPKSQDALHGRSAMLRCEVNDPQGVSYAWIQNGEPVTNSERRFLDGGNLKFTAIDRTLDSGNFQCIASKNSTGEEERTAETSFNIKWLESGAVSLKSPESVAEIQSSSQVILRCNIDGHPRPTNRWFKDGTQITEKNYKINNKERSLTLPNASPDDNGLYFCCAKNAAGQVCSSDNFTLNIIGLCVSLDSK
Protein: Multidrug and toxin extrusion protein 1 (MATE-1) (Solute carrier family 47 member 1) (A7KAU2)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Multidrug efflux pump that functions as a H(+)/organic cation antiporter. Plays a physiological role in the excretion of cationic compounds including endogenous metabolites, drugs, toxins through the kidney and liver, into urine and bile respectively. Mediates the efflux of endogenous compounds such as creatinine, vitamin B1/thiamine, agmatine and estrone-3-sulfate. May also contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17442726}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q96FL8}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane; at the brush border membranes of the proximal tubules (kidney) and at the bile caniculi (liver). {ECO:0000250|UniProtKB:Q96FL8}.
Interaction partners:
- Solute carrier family 22 member 2
- Solute carrier family 22 member 1
- 3-hydroxyacyl-CoA dehydrogenase type-2
- Solute carrier family 22 member 6
Sequence:
MEAPVELGPGGRQASPERRHWLRCLVLSDFREELRALLVLACPAFLAQLMVFLISFVSSVFCGHLSKLELNAVTLAIAVINVMGVSVGFGLSSACDTLISQTYGSRNLKHVGVILQRGSLILLLCCLPCWALFLNTQHILLLFRQDPAVSRLTQTYVTIFIPALPATFLYTLQVKYLLNQGIVLPQVVTGVAANLVNALANYLFVYQLHLGVMGSALANTVAQFTLALLLFLYILRSKVYQATWGGWSLECLQDWASFFRLAIPSMLMLCMEWWAYEIGSFLSGILGMVELGAQSVTYELAVIVYMIPMGLSVAVNVRVGNALGAGNIEQAKKSSAVALLVTELIAVVFCVMLLSCKDLVGYIFTSDRDIIALVAQVTPIYAVSHLFESLAGTSGGILRGSGNQKFGAIVNAIGYYVVGLPIGIALMFAAKLGVIGLWLGIVVCAVSQAVCFLGFIARLNWTKACQQARVHANLTVNTASNGNSAVLPDQPHPVGPDSHGGIVLRDADRKEGAELNEQVHPELPLPVRPEDSAHLSGKQLALRRGLLLLGVILVLLAGILVKVYVRTQ
Protein: Protein sll1483 (P74615)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Rqc2 homolog RqcH
- Sll0157 protein
- NAD
- Ssr2194 protein
- Sll1236 protein
- Sll0846 protein
Sequence:
MKTAARIVAFTALTGFALGMPTVAMAEMETTEKSAVVSQAATDSAMTIVEVAAGNETFSTLVAAVKAADLVEALSAEGPFTVFAPTNDAFAALPAGTVESLLLPENKDKLVKILTYHVVPGKITAAQVQSGEVASLAGEALTFKVKDGKVKVNKATVISADVDASNGVIHVIDQVILPPM
Protein: E3 ubiquitin-protein ligase SNT2 (EC 2.3.2.27) (Histone E3 ligase SNT2) (RING-type E3 ubiquitin transferase SNT2) (SANT domain-containing protein 2) (P53127)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcriptional regulator that, together with ECM5, recruits histone deacetylase RPD3 to a small number of promoters of stress-response genes in response to oxidative stress. Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. Note=Localizes to promoters of stress-response genes in response to oxidative stress. {ECO:0000269|PubMed:23878396}.
Interaction partners:
- Protein ECM5
- Histone deacetylase RPD3
- Chromatin modification-related protein EAF6
- Factor arrest protein 11
Sequence:
MPKEEDFQLPRRREAAKNVNYNEMEIDTKLVQQIQIAEKSGAKTKGSNSQTPRNCKRTSNPASRNEKFKYQKFLHDKNTCWNFIPTLPPSFRKNSRFSNILDLDDAMIDLKKMSLFNTESVLLSANDTIYMISEPAGEPYYVGRVVNFVSKPEFSNTIHEAIKTTSVFPAKFFQVRMNWFYRPRDIQEHVNTFNPRLVYASLHQDICPISSYRGKCSIFHKDEVFDVLPNEKECIIRPNIFYFDELFDRYTLKYYKVYSTDKILNKWNSKSPFLYVLNRRFRYIYTEPKYPLENVLKKYVFHELEVNELSPADYQWDKRCQFCKEWCIQKESLSCDECGVCAHLYCMDPPLDRKPNKDVVWTCFSCLQKQQGTKDSHVRFLEEQALELDFIRSVRQKIEEISSKAIKENVGYNTENCWFQYLGIYSISHIGDALNDSMFFPYPFKPSRVGVKYQWNGCNHNVPWRRNSYISANSEEERGSTKTSELAWVLDASKITTRKLSEYIEQCKSEICPILNVRGETCNFIDVVLKNLLFTNYDTAEAFKKCKRELSRKFLKEPSFTAVEIRKFEEAVEKFGSELRPVCEYVGTQPMSMIVRFYYNWKKTERGLTVRGKLSKLSKNKRKKEIANHENDVETKYIDDSSFDTEKLSLAESSFQCMFCKTDYSPMWYRVTGGSDDEKIKIRMQTGVNEKTEISEKSPAHSKKNEKLGALCIRCARMWRRYAIKWVPPLETLRKITGTCQNSFYSAIEGIIEENNTNKFTLSPFQAHNKLLEWELVQDSELIIRQRMKVYKNPNSFVKMKRYSMTFHTQLYKMAVRSYRKNEFHPETMQRDLELFIEDNKEVRKAIPEQKPERAKNTKDEFPVNIIRQSPGTIKTSDTSRNRKCNDVFIEKASNNNIPKITNASNDLIEISIKTGGSSSGSVSVDKGFKFVKFDNKTFQRLRNSLKLVNNKLPKYNEPSTKKIKMINDIALSNPLNEPNGASYNYTVISHSKETSVALEKYHDGNKPSKMLEKDMILKHTKNKPKNPDTAWANNSARTFCSVCKEKFNDNDNYEVVCGNCGLTVHYFCYAIKLPKDMKKNTNLKTFKWLCDPCSNDLNPIISTTYQCSMCPTKDYDYDRYRSQSFKICPDALKCTSLGTWVHLVCSLFNEDIKYGNGQSMQPALNTTAVLIKHSRFTCGVCRINGGGLVKCNKCQYRYHITCAQNSSNFKLMFEKKNMSVDTTLPCIKDVKLNDTYTLRPILICDRHDISLEGNELYPLSYKPQHTLSYIEQYCRYYKCESDHSLVELRYFEQLRLRHGEMPGNSHDSAIKPKIYVLPFERTCPHCGTNKSLYWYEDIICHSCNLRSGAQELDFDSASANISNDNGLPVEITQQLMEGIEPAMFDIDISEAGTDKNTHPSSQ
Protein: Chromatin modification-related protein EAF7 (Q5A6Q7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Chromatin modification-related protein EAF3
- Enhancer of polycomb-like protein 1
- SWR1-complex protein 4
- Histone acetyltransferase
- Chromatin modification-related protein EAF6
- Protein AF-9 homolog
- Chromatin modification-related protein EAF1
- Chromatin modification-related protein YNG2
- RuvB-like helicase 1
- Vps72/YL1 C-terminal domain-containing protein
Sequence:
MATLDENNPSKQTHRHWSIENEIKLFSLLCDYKPAGKNKQHNIKIIINNINESLDSKEEPFSEYDVWNKLRSLYDLEKIDQIEELSTENTSTEETTNQVSSGSANITKDTKNAKTTLDAKEPIQDKKEMDKEKSESSSLSTPEPPQRRTRSARDTTKSKRNLRDTPKEKSQYNDEEITSGGAEKSKVEVSSTSDHTDDQSPTPGSTKKGLDEQTNDDMSDIEDVDKDKGDETIAKIKKENTSEQEEDKNKKQTEEEAEEEEEEGDHVSGDERESKNKDTSEDEDGEDNEDQDEDDVEVIEDSHTDKENESSSEESSPEPMTKRTRQRTRSTHEKTEHTSPNIKKRTRQSVKFDDKPAEPSDTGSRKRRAPPGSVSPPHPPKTRRRTRSVTHEIEEEDASTQSADDAEPEIIKVETRHTTRRSSRISMEPSSSTPNVRVRRSSRKR
Protein: CG2899 (Q2XY02)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
PASAPDTGSTNANDPISGSLSVDSNLVIIQDMIDLSANHLEGLRTQCAISSTLTQQEIRCLESKLVRYFSELLLAKMRLNERIPANGLVPHTTGNELRQWLRVVGLSQGTLTACLARLTTLEQSLRLSDEEIRQLLADSPSQREEEELRRLTRAMQNLRKCMESLESGTAASNNDPEQWHWDSWDRPTHIHRGSVGNIGLGNNSTASPRTHHRQHGVKGKNSALANSTNFKSGRQSPSATEELNSTQGSQLTLTLTPSPPNSPFTPSSGLSSSLNGTPQRSRGTPPPARKHQTLLSQSHVQVDGEQLARNRLPTDPSPDSHSSTSSDIFVDPNTNASSGGSSSNVLMVPCSPGVGHVGMGHAIKHRFTKALGFMATCTLCQKQVFHRWMKCTDCKYICHKSCAPHVPPSCGLPREYVDEFRHIKEQGGYASLPHVHGAAKGSPLVKKSTLGKPLHQQHGDSSSPSSSCTSSTPSSPALFQQRERELDQAGSSSSANLLPTPSLGKHQPSQFNFPNVTVTSSGGSGGVSLISNEPVPEQFPTAPATANGGLDSLVSSSNGHMSSLIGSQTSNASTAATLTGSLVNSTTTTSTCSFFPRKLSTAGVDKRTPFTSEYTDTHKSNDSDKTVSLSGSASTDSDRTPVRVDSTEDGDSGQWRQNSISLKEWDIPYGDLLLLERIGQGRFGTVHRALWHGDVAVKLLNEDYLQDEHMLETFRSEVANFKNTRHENLVLFMGACMNPPYLAIVTSLCKGNTLYTYIHQRREKFAMNRTLLIAQQIAQGMGYLHAREIIHKDLRTKNIFIENGKVIITDFGLFSSTKLLYCDMGLGVPHNWLCYLAPELIRALQPEKPRGECLEFTPYSDVYSFGTVWYELICGEFTFKDQPAESIIWQVGRGMKQSLANLQSGRDVKDLLMLCWTYEKEHRPQFARLLSLLEHLPKKRLARSPSHPVNLSR
Protein: C-methyltransferase NovU (EC 2.1.1.-) (Novobiocin biosynthesis protein U) (Q9L9E7)
Organism: Streptomyces niveus (Streptomyces spheroides)
Function: C-methyltransferase that acts together with NovW to catalyze the formation of dTDP-4-keto-6-deoxy-5-C-methyl-L-lyxo-hexose from dTDP-4-keto-6-deoxy-D-glucose in the novobiocin biosynthesis pathway, an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Interaction partners:
Sequence:
MQDIVRPIDECRVCGHDDWLDVVSFGSTPLAGNLLGDEDDAGGETLFPLDVVVCRRCWLMTLRHVIEPDVLFGHYRYVASDAGSIIQHMRKLVDLCVERIGLTDGDLVVEFGSNTGAHLELFRQAGPRVVGVDPARNLAGVANDRGVETIPAGFTAEVGEEIATRHGLARLVYGRQCFAHIPDIHEVLNGVSALLAPDGLFFVEVPYLVELLKNNQFDTIFHEHFSYFSLGSLCTLFESHGLRVVDVHTADVHGGSIVVFAAPAAADHEVRPAVAEMLAEERSQGIAEERTYREFADRTERVRAQIRELVRGVVADGKTVAGYGAPTKGSALLAACGLGHQEIRFCSDTTVLKQGKILPGSRIPIWSPEQAAGHVPDYYLLLAWNYAPEIIDNEKEFLENGGRFIVPIPEPRVISAESTL
Protein: MYB-like transcription factor EOBII (MYB-like protein NON1) (PhNON1) (Protein EMISSION OF BENZENOIDS II) (PhEOBII) (E0CJS3)
Organism: Petunia hybrida (Petunia)
Function: MYB-type transcription factor controlling the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) by regulating the expression of ODO1 and EOBI, key regulators of the shikimate pathway, and of several biosynthetic floral scent-related genes including IGS, PAL2 and CFAT. This scent, mostly produced in the evening and night by the petals, attracts the pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta). Binds to and activates the ODO1 and EOBI promoters via MYB binding sites (MBS) 5'-AAACCTAAT-3' and 5'-CTAACT-3'. Regulates the promoters of IGS1, CFAT and PAL2. Controls flowers petal opening by modulating a global transcriptomic switch.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:20543029}.
Interaction partners:
Sequence:
MDKKPCNSQDAEVRKGPWTMEEDLILINYIANHGEGVWNSLAKSAGLKRTGKSCRLRWLNYLRPDVRRGNITPEEQLLIMELHAKWGNRWSKIAKHLPGRTDNEIKNYWRTRIQKHIKQAETMNGQAASSEQNDHQEACTSQMSNGPNDNTIDQTYSPTSYSGNVDTFQAGPNFLTEANDNMWSMEDIWSMQLLNGD
Protein: Large ribosomal subunit protein P1w (60S acidic ribosomal protein P1-1) (Q8LCW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
- Large ribosomal subunit protein uL10x
- Large ribosomal subunit protein uL10y
- Large ribosomal subunit protein uL24z
- Large ribosomal subunit protein eL32z
- Large ribosomal subunit protein eL8y
- Large ribosomal subunit protein uL6x
- Large ribosomal subunit protein eL30x
- Large ribosomal subunit protein eL29z
- Large ribosomal subunit protein P3z
- Large ribosomal subunit protein uL10z
Sequence:
MSTVGELACSYAVMILEDEGIAITADKIATLVKAAGVSIESYWPMLFAKMAEKRNVTDLIMNVGAGGGGGAPVAAAAPAAGGGAAAAPAAEEKKKDEPAEESDGDLGFGLFD
Protein: MAGE-like protein 2 (Necdin-like protein 1) (Protein nM15) (Q9UJ55)
Organism: Homo sapiens (Human)
Function: Probably enhances ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases, possibly through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Acts as a regulator of retrograde transport via its interaction with VPS35. Recruited to retromer-containing endosomes and promotes the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASHC1 together with TRIM27, leading to promote endosomal F-actin assembly. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Significantly promotes the cytoplasmic accumulation of CLOCK (By similarity).
Subcellular location: Early endosome {ECO:0000269|PubMed:23452853}. Cytoplasm {ECO:0000250|UniProtKB:Q9QZ04}. Nucleus {ECO:0000250|UniProtKB:Q9QZ04}. Note=Recruited to retromer-containing endosomes via interaction with VPS35. Colocalizes with CLOCK and BMAL1 in the cytoplasm, and with PER2 in the cytoplasm and nucleus (By similarity). {ECO:0000250|UniProtKB:Q9QZ04, ECO:0000269|PubMed:23452853}.
Interaction partners:
- Zinc finger protein RFP
- Ubiquitin carboxyl-terminal hydrolase 7
- Nuclear pore-associated protein 1
- E3 ubiquitin-protein ligase makorin-3
- Small nuclear ribonucleoprotein-associated protein N
- Phospholipid-transporting ATPase VA
- Oxytocin-neurophysin 1
- Chondrosarcoma-associated gene 1 protein
- Ubiquitin-protein ligase E3A
Sequence:
MSQLSKNLGDSSPPAEAPKPPVYSRPTVLMRAPPASSRAPPVPWDPPPIDLQASLAAWQAPQPAWEAPQGQLPAPVVPMTQPPALGGPIVPAPPLGGPMGKPPTPGVLMVHPPPPGAPMAQPPTPGVLMVHPSAPGAPMAHPPPPGTPMSHPPPPGTPMAHPPPPGTPMAHPPPPGTPMVHPPPPGTPMAHPPPPGTPMAHPPPPGTPMAHPPPPGTPMAHPPPPGTPMAQPPAPGVLMAQPLTPGVLMVQPAAPGAPMVQPPPAAMMTQPQPSGAPMAKPPGPGVLMIHPPGARAPMTQPPASGAPMAQPAAPPAQPMAPPAQPMASWAPQAQPLILQIQSQVIRAPPQVPQGPQAPPAQLATPPGWQATSPGWQATQQGWQATPLTWQTTQVTWQAPAVTWQVPPPMRQGPPPIRPGPPPIRPGPPPVRQAPPLIRQAPPVIRQAPPVIRQAPPVIRQAPAVIRQAPPVIRQAPPVIRQAPPVIRQAPPLIRQAPPPIRPAPQVLATQPPLWQALPPPPPLRQAPQARLPAPQVQAAPQVPTAPPATQVPAAPPAGPQVPQPVLPAPLSAPLSAPQAVHCPSIIWQAPKGQPPVPHEIPTSMEFQEVQQTQALAWQAQKAPTHIWQPLPAQEAQRQAPPLVQLEQPFQGAPPSQKAVQIQLPPQQAQASGPQAEVPTLPLQPSWQAPPAVLQAQPGPPVAAANFPLGSAKSLMTPSGECRASSIDRRGSSKERRTSSKERRAPSKDRMIFAATFCAPKAVSAARAHLPAAWKNLPATPETFAPSSSVFPATSQFQPASLNAFKGPSAASETPKSLPYALQDPFACVEALPAVPWVPQPNMNASKASQAVPTFLMATAAAPQATATTQEASKTSVEPPRRSGKATRKKKHLEAQEDSRGHTLAFHDWQGPRPWENLNLSDWEVQSPIQVSGDWEHPNTPRGLSGWEGPSTSRILSGWEGPSASWALSAWEGPSTSRALGLSESPGSSLPVVVSEVASVSPGSSATQDNSKVEAQPLSPLDERANALVQFLLVKDQAKVPVQRSEMVKVILREYKDECLDIINRANNKLECAFGYQLKEIDTKNHAYIIINKLGYHTGNLVASYLDRPKFGLLMVVLSLIFMKGNCVREDLIFNFLFKLGLDVRETNGLFGNTKKLITEVFVRQKYLEYRRIPYTEPAEYEFLWGPRAFLETSKMLVLRFLAKLHKKDPQSWPFHYLEALAECEWEDTDEDEPDTGDSAHGPTSRPPPR
Protein: TRUD domain-containing protein (Q385G9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- tRNA/rRNA methyltransferase SpoU type domain-containing protein
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
- 50S ribosomal protein L17, putative
- 50S ribosomal protein L13, putative
- GTP-binding protein, putative
- Large ribosomal subunit protein bL21m
- Pseudouridylate synthase RPUSD4, mitochondrial
- KOW domain-containing protein
- Ribosomal protein L11, putative
- Large ribosomal subunit protein mL43
Sequence:
MKVSSRGPIVRWALSRPTSGLVSSPSEWRCGRDLSDEEKHSGLLLRIRDICQPLAKNDQLPVAVVKAQPSDLQVNEVDAVGDVAALSKVVKGKWRKISRQKTLLIEDDARTPFSDPSKSFSPRVQSYGEYVRLTGKLPRDLPVLRFVLYRDSYSLNSVENRLGYVLSLQPDCVFLRDQPGGSFGCITQHGVCLGVTKEILSHASRHYNLHPLIFEPREYFSTDKLHSLLQGARGHHHRVLLRCVEGSQDTIKALLKKTAERGFINYFWLDRFSVGTNRFFDMAVLAARGDYLKSIGALLHCVAESNGVHYDHFLKYLNADPSTVPGIAQTWATTAKHMRSPNWIVQLLRGLHKYHADAECGKSSYLAELWSALPMREALRRSAAEFVWNAMASQRLLSKGLNVVEGDVVRMGPADSVSGCDSSSLPNNCGNYHLVTKDDEEKGTFKITDVVLPVPYGSVAANNCLFPHLSPLDKKLYVEFATKHGMSFLFDEQMPSPLSNPLQFYRHLITKPVNMQVSVIRDPNSLTSIKSDLAVMQERKLVQIGDIDYSTRVREPCVYNVSERFTEKMEEILKTHRGPNSVVLSCYLPEDSSPFVMLREVFDLRHASFHDLYGLL
Protein: 5-aminolevulinate synthase (EC 2.3.1.37) (5-aminolevulinic acid synthase) (Delta-ALA synthase) (Delta-aminolevulinate synthase) (Q7T2F0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU910713}; Peripheral membrane protein {ECO:0000256|RuleBase:RU910713}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000256|RuleBase:RU910713}.
Interaction partners:
Sequence:
MDAIIRCPFLSRVPQTFLQQARKSLVAYAVKCPVMMDLASRPLLRPLCSSSASFQKVEDSSSAGHEASDAPAVPAGHPAPPAGHASASKCPFLAAEMSQKNSGVVRQASMALQEDVSEVRTVQKDVSASALTPLKDGMNGGNLMKKLMKQRPAHVSHLLQDNMPKNVSSFRYDEFFEKKIEEKKSDHTYRVFKTVNRRATEFPMADDYTESLSFKRNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSGAGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLAKMMPGCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAKHLRELLEKSDPSTPKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKMDIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPMLLSGARQSVQILKSEEGRTLRRKHQRNVTLLRQMLMDSGLPVIHCPSHIIPVRVADAEKNTEVCDIMMSRYNIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTWTEVGLPLKPHSSAECNFCRQPLHFEIMSEREKSYFSGLSQPISACG