wanglab/gogpt-training-data huggingface dataset:
Protein: Transcriptional regulatory protein EDS1 (Expression dependent on SLT2 protein 1) (P38073)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSHHVPNLYGTPIRDPHERKRNSASMGEVNQSVSSRNCERGSEKGTKQRKKASHACDQCRRKRIKCRFDKHTGVCQGCLEVGEKCQFIRVPLKRGPAKKRGSVVSIEKFSSDNDPLQYRPRTHSYPMNSGNNYLPSLARNSSFPSISSLFVPSITAQSQQFVKVPYDDIKRRSSLAILGSDSSISTEFGGNYRLDENLNVRQEGKDIVAKGMITPVEEMGACSSNVRRQGSQSLPIQEQRASPYINPFISGRSRLSSLSYTSEATTSEGNTQGKNQCMLTPNSVRSIEKERLNSLTAGFPNKKLGTDGRSDKWDKNSTWKPVYRSSNPSHPSTEKNVSLNQEASAKPLMLGTYRQFDATSFYKVLGIYYNFFHINFPVIPINKSKFTDMLDPEKPNVIDEIRQINNEIIQCFKTALEVLVFCKIKQRRSSKSTKSWSRDSLCDFQKGLYYIQNFNKCIADCFQSLITIKPVLKQNSSVIPSRIKFIYFSTIIVLNFILILAGEESSLLLGPSVGVFNEFQAHKLFLPFQNTSPMLLLNSNEESGDEILDYAVLFKRLYILLNILDTLQSFRLGQPKLINLNFGSAIETYFSDKTGHNQVVEKAPVALDNILRNLKLGEFITYFVLNRKSLQVNVPHHLLFTNQTDYGEFAVEKGEHDNIAGKFETLLKKKEILIRKLLNIEQKNDHILENCCNSDAEMKNIGELVCSMITLVSGILDSITNMNAENSVDLDSKPLPNAYFAQDSEEELMSPTQSITSNLASEENTRCTTKDLMGTVSIFMLPMVEECYNIISLIGPIPTTLISLYIRNGNMAKGINDRIMTLSTALNELVQITALFNTLEPFRKNAHDRAKRYYVSATSSTGCYESVMKSMYSGKCAASNASNVAPSEEENKKILKKFADIGWKLMDDSELGCCCCFFN
Protein: Cyanate transport protein CynX (P17583)
Organism: Escherichia coli (strain K12)
Function: This protein is part of an active transport system that transports exogenous cyanate into E.coli cells.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Cyanate hydratase
- Carbonic anhydrase 1
- DNA-binding and peroxide stress resistance protein YaaA
- HTH-type transcriptional regulator CynR
Sequence:
MLLVLVLIGLNMRPLLTSVGPLLPQLRQASGMSFSVAALLTALPVVTMGGLALAGSWLHQHVSERRSVAISLLLIAVGALMRELYPQSALLLSSALLGGVGIGIIQAVMPSVIKRRFQQRTPLVMGLWSAALMGGGGLGAAITPWLVQHSETWYQTLAWWALPAVVALFAWWWQSAREVASSHKTTTTPVRVVFTPRAWTLGVYFGLINGGYASLIAWLPAFYIEIGASAQYSGSLLALMTLGQAAGALLMPAMARHQDRRKLLMLALVLQLVGFCGFIWLPMQLPVLWAMVCGLGLGGAFPLCLLLALDHSVQPAIAGKLVAFMQGIGFIIAGLAPWFSGVLRSISGNYLMDWAFHALCVVGLMIITLRFAPVRFPQLWVKEA
Protein: Interleukin-31 receptor subunit alpha (IL-31 receptor subunit alpha) (IL-31R subunit alpha) (IL-31R-alpha) (IL-31RA) (Cytokine receptor-like 3) (GLM-R) (hGLM-R) (Gp130-like monocyte receptor) (Gp130-like receptor) (ZcytoR17) (Q8NI17)
Organism: Homo sapiens (Human)
Function: Associates with OSMR to form the interleukin-31 receptor which activates STAT3 and to a lower extent STAT1 and STAT5. May function in skin immunity. Mediates IL31-induced itch, probably in a manner dependent on cation channels TRPA1 and TRPV1 (By similarity). Positively regulates numbers and cycling status of immature subsets of myeloid progenitor cells in bone marrow in vivo and enhances myeloid progenitor cell survival in vitro (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:11877449, ECO:0000305|PubMed:14504285}; Single-pass type I membrane protein {ECO:0000305|PubMed:11877449, ECO:0000305|PubMed:14504285}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q8K5B1}. Cell projection, axon {ECO:0000250|UniProtKB:Q8K5B1}.
Interaction partners:
- Interleukin-31
- Oncostatin-M-specific receptor subunit beta
- Tyrosine-protein kinase JAK1
- Oncostatin-M
- Probable ATP-dependent RNA helicase DDX4
Sequence:
MMWTWALWMLPSLCKFSLAALPAKPENISCVYYYRKNLTCTWSPGKETSYTQYTVKRTYAFGEKHDNCTTNSSTSENRASCSFFLPRITIPDNYTIEVEAENGDGVIKSHMTYWRLENIAKTEPPKIFRVKPVLGIKRMIQIEWIKPELAPVSSDLKYTLRFRTVNSTSWMEVNFAKNRKDKNQTYNLTGLQPFTEYVIALRCAVKESKFWSDWSQEKMGMTEEEAPCGLELWRVLKPAEADGRRPVRLLWKKARGAPVLEKTLGYNIWYYPESNTNLTETMNTTNQQLELHLGGESFWVSMISYNSLGKSPVATLRIPAIQEKSFQCIEVMQACVAEDQLVVKWQSSALDVNTWMIEWFPDVDSEPTTLSWESVSQATNWTIQQDKLKPFWCYNISVYPMLHDKVGEPYSIQAYAKEGVPSEGPETKVENIGVKTVTITWKEIPKSERKGIICNYTIFYQAEGGKGFSKTVNSSILQYGLESLKRKTSYIVQVMASTSAGGTNGTSINFKTLSFSVFEIILITSLIGGGLLILIILTVAYGLKKPNKLTHLCWPTVPNPAESSIATWHGDDFKDKLNLKESDDSVNTEDRILKPCSTPSDKLVIDKLVVNFGNVLQEIFTDEARTGQENNLGGEKNGYVTCPFRPDCPLGKSFEELPVSPEIPPRKSQYLRSRMPEGTRPEAKEQLLFSGQSLVPDHLCEEGAPNPYLKNSVTAREFLVSEKLPEHTKGEV
Protein: Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.360) (Disrupter of telomere silencing protein 1) (Histone H3-K79 methyltransferase) (H3-K79-HMTase) (Lysine N-methyltransferase 4) (Q04089)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. Can bind to DNA (in vitro).
Subcellular location: Nucleus {ECO:0000269|PubMed:11029058}.
Interaction partners:
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Histone H3
- Histone H4
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Polyubiquitin
- Histone H2A.2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Histone H2A.1
- E3 ubiquitin-protein ligase BRE1
- Regulatory protein SIR3
Sequence:
MGGQESISNNNSDSFIMSSPNLDSQESSISPIDEKKGTDMQTKSLSSYSKGTLLSKQVQNLLEEANKYDPIYGSSLPRGFLRDRNTKGKDNGLVPLVEKVIPPIHKKTNNRNTRKKSSTTTKKDVKKPKAAKVKGKNGRTNHKHTPISKQEIDTAREKKPLKKGRANKKNDRDSPSSTFVDWNGPCLRLQYPLFDIEYLRSHEIYSGTPIQSISLRTNSPQPTSLTSDNDTSSVTTAKLQSILFSNYMEEYKVDFKRSTAIYNPMSEIGKLIEYSCLVFLPSPYAEQLKETILPDLNASFDNSDTKGFVNAINLYNKMIREIPRQRIIDHLETIDKIPRSFIHDFLHIVYTRSIHPQANKLKHYKAFSNYVYGELLPNFLSDVYQQCQLKKGDTFMDLGSGVGNCVVQAALECGCALSFGCEIMDDASDLTILQYEELKKRCKLYGMRLNNVEFSLKKSFVDNNRVAELIPQCDVILVNNFLFDEDLNKKVEKILQTAKVGCKIISLKSLRSLTYQINFYNVENIFNRLKVQRYDLKEDSVSWTHSGGEYYISTVMEDVDESLFSPAARGRRNRGTPVKYTR
Protein: Uncharacterized protein (Q38AP6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFPIPPATFVHQFPLFPATCCSDSTGFFKGLALPVSPLTIASTPTALTTRRDFVVLRQPWRQLVVALSLSFRTPGMLLSCLFDQPTWGGVAFLRAWRVRCCCFQDCTVSLRV
Protein: Down and out, isoform A (Down and out, isoform B) (FI18831p1) (Q9V3J9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASSTSSARGNNKAATTNTTAATAPVSTASSAAVSGSGATSAAATASAPPAVTLSELIGQQLKHLNADELLHKDELQLLLLITPVQRQKLSRNLEDGDLEASTSAAPLSRPENGEEDDDLIGAVGGLGISSPTTTKEPVLDFRPHVLKWFQHLRHQTGHFKSEEESRRLREAGNDSYRKERHPLKASDLFTEAIFLAPARNTLAAALAHANRSLVLFDCGLYAESYDDCLCALDLGYPEEYLPLIKLRQAACALKLRNFALCEEHLHELLHIELNQVFEARTHELWHQCEVLKVERFEMAVQTGDDLDINDSKAFEIAWLDNSSSLHTTRAVAKNALIFESEAVAMVPSGNCRVCDYCGITQFIPFPCIYCSNRLVVYCSRQCRFKHAAIHAVECFGHQIELFESFGEVFGMPRLLQLAFRMLITGLPELLGHCRKKPTLSKLWSAINGGLQERQDIAYSAVLRLERLKEERPTDTVIALALAAHILSIYLSKCTTFFDQLEKSLPTASRMSSAEWELLCAALLMRHIGQLRHRSLTACRSFVLPADPHVFSPLNEFQLWAAPMRLQEGHLHLLAGEVAVVSYSVYPDTLNLCRHSCSSTICAKFSGRTVTALALLDLPAGSGIYNCFAGGNFQQLPREERTKQLLESGIRCHCNACQLTHSDDQFHKFHRYRCDNPNCMEIFTPNALPHAPSLRWWLSEEYTQPEFNGADLIMCPHCGEYQKLEWFWAFTTSLIDCELIEERCKLYAAIERAENQLMDLHECKVALARLLLEQCLMVHREGATVLDDWEFNKLGSILRSVLPSVMAQYGGQSIEYVKYFSYFWDVMALSNYKCNDRELMQMLNALEFIADEFKDIFINYYEDYIAPKFAEESYGSVVDTQV
Protein: Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)] (P08566)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.
Subcellular location: Cytoplasm.
Interaction partners:
- Chorismate synthase ARO2
- Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited
- Phospho-2-dehydro-3-deoxyheptonate aldolase, phenylalanine-inhibited
- Chorismate mutase
- Probable prephenate dehydratase
- Multifunctional tryptophan biosynthesis protein
- Tryptophan synthase
- Prephenate dehydrogenase [NADP
- Anthranilate phosphoribosyltransferase
- Aromatic/aminoadipate aminotransferase 1
Sequence:
MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALILAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTSSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREGWYKECSNFSFFAPHCSAEAEFQALRRSFSKYIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTMKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFVPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKGPFKAIFDAVTKE
Protein: (Z)-gamma-bisabolene synthase 2 (EC 4.2.3.40) (Terpenoid synthase 13) (AtTPS13) (Q9T0K1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in sesquiterpene (C15) biosynthesis. The major product is (Z)-gamma-bisabolene with minor amounts of (E)-nerolidol and alpha-bisabolol.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Alpha-humulene/
- (Z)-gamma-bisabolene synthase 1 (Terpenoid synthase 12) (AtTPS12)
- Alpha-barbatene synthase
- Inactive squalene synthase 2
- Squalene synthase 1
- Uncharacterized protein At4g13230
- Probable alpha,alpha-trehalose-phosphate synthase 7
- Dehydrodolichyl diphosphate synthase 5
- Alkyl transferase
- Dehydrodolichyl diphosphate synthase 1
Sequence:
MESQTKFDYESLAFTKLSHSQWTDYFLSVPIDDSELDAITREIDIIKPEVRKLLSSKGDDETSKRKVLLIQSLLSLGLAFHFENEIKDILEDAFRRIDDITGDENDLSTISIMFRVFRTYGHNLPSSVFKRFTGDDGKFERSLTEDAKGILSLYEAAHLGTTTDYILDEALEFTSSHLKSLLVGGMCRPHILRLIRNTLYLPQRWNMEAVIAREYISFYEQEEDHDKMLLRLAKLNFKLLQLHYIKELKTFIKWWMELGLTSKWPSQFRERIVEAWLAGLMMYFEPQFSGGRVIAAKFNYLLTILDDACDHYFSIPELTRLVDCVERWNHDGIHTLEDISRIIFKLALDVFDDIGRGVRSKGCSYYLKEMLEELKILVRANLDLVKWARGNQLPSFEEHVEVGGIALTTYATLMYSFVGMGEAVGKEAYEWVRSRPRLIKSLAAKGRLMDDITDFESDMSNGFAANAINYYMKQFVVTKEEAILECQKMVVDINKIVNEELLKTTTVPRRVLKQALNFGRLLEVLYTKSDDIYNCSEGKLKEYIVTLLIDPIHL
Protein: Small heat shock protein 21 (Q5AHH4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Heat shock protein required for pathogenicity. Mediates thermotolerance and adaptation to oxidative stress and ethanol-induced stress. Required for invasive growth and filament formation under various filament inducing conditions. Plays a role in the capacity of damaging human-derived endothelial and oral epithelial cells during infection. Potentiates resistance to antifungal drugs, as well as resistance to killing by human neutrophils. Plays a major role in trehalose homeostasis in response to elevated temperatures. Regulates CEK1 activation by phosphorylation in response to elevated temperatures.
Interaction partners:
- Chaperone ATPase
- Heat shock protein 78
- Heat shock protein HSP70
- Heat shock protein 90 homolog
- Hsp12p
Sequence:
MSWFGFFDPDFDDFFGRPRKYATEVPPNFNPRKIAQGDNGKGQQVSRYGAGAGHPHRALARRDDFFDDFWKNFSSGKYFVGFDDNVKTTEESDKYVVSYDQENLSPDEVNVDFDKQENELIITVTQETEKDGTKKSSTFHSNLKFEKPVNFDDISAEIGEQGVQVTLPKVHADHEKIVNIPISKAAAKK
Protein: Polyubiquitin 4 [Cleaved into: Ubiquitin] (P0CH32)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase UPL4
- Protein NBR1 homolog
- E3 ubiquitin-protein ligase UPL3
- E3 ubiquitin-protein ligase PRT1
- Small ribosomal subunit protein eS19z
- Ubiquitin-conjugating enzyme E2 13
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL42z/eL42y
- 26S proteasome non-ATPase regulatory subunit 4 homolog
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGSF
Protein: Cadherin-4 (Retinal cadherin) (R-CAD) (R-cadherin) (P39038)
Organism: Mus musculus (Mouse)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May play an important role in retinal development.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Catenin delta-1
- Cadherin-2
- Catenin beta-1
- Junction plakoglobin
- Cadherin-20
- Catenin alpha-2
- Cadherin-7
- Cadherin-8
- Cadherin-6
Sequence:
MTTGSVLPLLLLGLSGALRAHREDLTVREACKAGFSEEGYTALISPNVLEGEKLLKVEFSSCVGTKGMQYETNSLDFKVGADGTVFATRELKIPSEQVAFTVTARERQSAEQWAAMVRLLVAQTSSAHSEHKKGQTVALDPSQPPNDTLLPWPQHQSSGGLRRQKRDWVIPPINVPENSRGPFPQQLVRIRSDKDNDIPIRYSITGVGADQPPMEVFNIDSMSGRMYVTRPMDREERASYHLRAHAVDMNGNKVENPIDLYIYVIDMNDNRPEFINQVYNGSVDEGSKPGTYVMTVTANDADDSTTANGMVRYRIVTQTPQSPSQNMFTINSETGDIVTVAAGLDREKVQQYTVIVQATDMEGNLNYGLSNTATAIITVTDVNDNPPEFTTSTFAGEVPENRIETVVANLTVMDRDQPHSPNWNAVYRIISGDPSGHFSVRTDPVTNEGMVTVVKAVDYELNRAFMLTVMVSNQAPLASGIQMSFQSTAGVTISVTDVNEAPYFPSNHKLIRLEEGVPAGTALTTFSAVDPDRFMQQAVRYSKLSDPANWLHINTSNGQITTAAILDRESLYTKNNVYEATFLAADNGIPPASGTGTLQIYLIDINDNAPQLLPKEAQICERPGLNAINITAADADMDPNIGPYVFELPFIPTTVRKNWTITRLNGDYAQLSLRILYLEAGVYDVPIIVTDSGNPPLSNTSVIKVKVCPCDENGDCTTVGAVAAAGLGTGAIVAILICIVILLIMVLLFVVWMKRREKERHTKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPEAMEHVLSKTPGVRRVDERPVGAEPQYPVRPVVPHPGDIGDFINEGLRAADNDPTAPPYDSLLVFDYEGSGSTAGSVSSLNSSSSGDQDYDYLNDWGPRFKKLADMYGGGEED
Protein: Solute carrier family 17 member 3 (A0A0G2JX26)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MATVVELSPTSEQCEFVLGLPVNKKTPPRKVPSLCSMRYSIAFIAHICNFTLIAQNSIISITMVAMVNNTDQPSHLNSSTEWFPDGLNGDQHEASKHLSIKAPVYNWSPQTQGIIFSSVQYGMMLMQGPGGYLAGKLGTKKVVGIALLGSSLLTLCIPLAANLGLAFLLATRAVQGLTQGAGYGGQFALWQKWAPPNERSRLCSIAMSGSIGVVCCLLWLILVYDDPVSHPWISSPEKEYILSSLDQQFNSEEQPLPIKAMLKSLPLWSMCLCSMTHQWLVNTLIIYTPTYISSVFKVNIRDNGLLSSLPFFVAWVIGILGGLLADFLLSKNFRLITVRKIITILGNTPPAALVVALPYVQSSYIATTTFLTLSCGLSPLCQSGVYINALDIAPRYASLLMGTSRGLAHSSAVMVPIVAGFFLNQDSEFGWRNFFFVLFAINLFGLIIYLVFAKADIQEWARERKLTRL
Protein: DNA-binding dual transcriptional regulator OmpR (Transcriptional regulatory protein OmpR) (P0AA16)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes. Plays a central role in both acid and osmotic stress responses. Binds to the promoter of both ompC and ompF; at low osmolarity it activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription. Involved in acid stress response; this requires EnvZ but not OmpR phosphorylation. Phosphorylated by EnvZ; this stimulates OmpR's DNA-binding ability. Is also dephosphorylated by EnvZ. A single OmpR protein can bind to DNA; OmpR dimers can form on the DNA in either direction, suggesting that interactions between the 2 DNA-binding domains are weak or absent.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:3533941}.
Interaction partners:
- Sensor histidine kinase EnvZ
- Sensor histidine kinase CpxA
- Phosphate regulon sensor protein PhoR
- Outer membrane porin C
- Outer membrane porin F
- Sensor protein PhoQ
- Aerobic respiration control sensor protein ArcB
- CsgBAC operon transcriptional regulatory protein
- Sensor histidine kinase CusS
- Sensor protein RstB
Sequence:
MQENYKILVVDDDMRLRALLERYLTEQGFQVRSVANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQSNPMPIIMVTAKGEEVDRIVGLEIGADDYIPKPFNPRELLARIRAVLRRQANELPGAPSQEEAVIAFGKFKLNLGTREMFREDEPMPLTSGEFAVLKALVSHPREPLSRDKLMNLARGREYSAMERSIDVQISRLRRMVEEDPAHPRYIQTVWGLGYVFVPDGSKA
Protein: TOPLESS-related 3 (F4K2T3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSLSRELVFLILQFLEEEKFKESVHRLEKESGFFFNTKYFDEKVLAGEWDDVETYLSGFTKVDDNRYSMKIFFEIRKQKYLEALDRQEKAKAVEILVQDLRVFSTFNEELYKEITQLLTLQNFRENEQLSKYGDTKTARGIMLGELKKLIEANPLFRDKLMFPTLRSSRLRTLINQSLNWQHQLCKNPRPNPDIKTLFTDHTCTLPNGPLAPSAVNQPVTTLTKPAAYPSLGPHVPFPPGPAAANAGALASWMAAASGASAVQAAVVTPALMPQPQNQMSILKRPRTPPATPGIVDYQNPDHELMKRLRPAPSVEEVTYPAPRQQAPWSLEDLPTKAALALHQGSTVTSMEFYPMQNTLLLVGSATGEITLWELAARERLVSRPFKIWDMSNCSHQFQALIAKETPISVTRVAWSPDGNFIGKLPVMHCWILIVCCLWSLVSVSYCAGVAFTKHLIQLYAFSGPNDLRQHTEIDAHVGAVNDLAFANPNRQLCVITCGDDKLIKVWDVSGRKHFTFEGHDAPVYSICPHYKENIQFIFSTAIDGKIKAWLYDNLGSRVDYDAPGKWCTRMLYSADGTRLFSCGTSKDGDSFLVEWNESEGSIKRTYKEFQKKLAGVVQFDTSKNHFLAVGEDGQIKFWDMNNINVLTSTDAEGGLPALPHLRFNKDGNLLAVTTADNGFKILANPAGFRSLRAMETPASETMRTPVDFKAVPGAPVASVNCKVERGSPVRHSQMLNGVDPSKSRIDDSTDKPKSWQLAEILDPSQCFQATLPDTAGSSTKVVQLLYTNSGAGILALGSNGIQRLWKWVPNEQNPSGKATATVVPQHWQPNSGLLMTNDVSGVNLENAAPCIALSKNDSYVMSAAGGKVSLFNMMTFKVMTTFMPPPPASTFLAFHPQDNNVIAIGMEDSTIHIYNVRVDEVKSKLKGHQKRITGLAFSTALNILVSSGADAQICFWSIDTWEKRKSVAIQMPAGKAANGDTRVQFHVDQLRILVVHETQLAVFDASKMECIRQWIPQDSLSAPISSAVYACNSQLIYTTFRDGNIGVFDADSLRLRCRISPSAYLPQGNQGLSPLVVAAHPQDPNQFAVGLNDGSVKMMEPTEGEGKWGMIPPSEAINSPSTTSNQTPEQLQR
Protein: tRNA (uracil-O(2)-)-methyltransferase (EC 2.1.1.211) (tRNA(Ser) (uridine(44)-2'-O)-methyltransferase) (tRNA Um(44) 2'-O-methyltransferase) (Q02648)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: tRNA (uracil-O(2)-)-methyltransferase, which catalyzes the formation of O(2)-methyluracil at position 44 (Um44) in tRNA(Ser).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA
- tRNA:m
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA pseudouridine synthase 4
- tRNA
- tRNA
- Multisite-specific tRNA:
Sequence:
MTGDGSAHISKNNQNQHKDRFKFIVNDKSILGPQWLSLYQTDGKVTFAKSHFEQAMMNVIREPNINSTVILRADILKEINHAAEAGSEPKFDESVLKKFEIDNGNESGEEDVKKINIEDLNIRSCETSESLKLSPVHEFVRRIIPRNFYKDAIINQTCLILNSKDPNFQETSLIVYTPHINSEKDCPFYIPRTQSVGILLHQSVLSVHYIPFPEDKTAFTDESERVVRTAYRLLQTANKHSKGVMQGYEKRVNHDQVVNKVNFQNTYIVLKKKYSKFLVENWAESTDPKKHVFEDIAIAAFLIELWIKVYGPDFRSKMQFRDLGCGNGALCYILLSESIKGLGIDARKRKSWSIYPPEVQSSLKEQVIIPSILLRPHPALKRQVPHLEHNGRFFPVKVTHEVIAPATVVYSSEDLLKSPQVNTAEFPPDTFIIGNHSDELTCWIPLLGHPYMVIPCCSHNFSGQRVRFNVRKRSPRSNEIKNQNNSKSTYSGLVDHVEYISSRVGWKVEKEMLRIPSTRNAAIIGVENATLKHFPTQAVYDMIWEDGGAEGWIQNTMSLLKRNPRNH
Protein: Shikimate kinase 2, chloroplastic (AtSK2) (EC 2.7.1.71) (Q8GY88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
- 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic
- Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic
- 3-phosphoshikimate 1-carboxyvinyltransferase
- 3-dehydroquinate synthase, chloroplastic
- Chorismate mutase 1, chloroplastic
- Chorismate mutase 2
- Chorismate mutase 3, chloroplastic
- Shikimate kinase 1, chloroplastic
- Arogenate dehydrogenase 1, chloroplastic
- Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic
Sequence:
MEAATVQRFQYSSWNDLRNFEGKPRGSLRYNTQRIKEDKRFRVVALTLDKRRDHRLRSVSDKNSSALLETGSLLHSPFDEEQQILKKKAEEVKPYLNGRSMYLVGMMGSGKTTVGKIMARSLGYTFFDCDTLIEQAMKGTSVAEIFEHFGESVFREKETEALKKLSLMYHQVVVSTGGGAVIRPINWKYMHKGISIWLDVPLEALAHRIAAVGTGSRPLLHDDESGDTYTAALNRLSTIWDARGEAYTKASARVSLENITLKLGYRSVSDLTPAEIAIEAFEQVQSYLEKEDGMARPDGL
Protein: Cuticular protein 66D (RE57183p) (Q9VSN3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQLLLVTATLAICGVVVSGQQGVDPAYLRQYYQQLQQQQQQQQAQPHDGTPIFEQNSEQTQQYVNSGQQIRIKDTVAEQIRAQQQQGYVAPSVRDYQQYQPQQAAYRPPAQAAPQPPRRIQQSSYQAPSTSILGKGQHKLSLQQQNEEEEYDDQNSSYQFGFDVKDDEFTNYQNRKEIRDGSVIKGSYSVVDSDGFIRTVKYTADPKEGFKAEVIREPTDIVVKIPTPPPPTQLLRAGGHKAQQEYSSGPSKQQYQHQQQQQQPQYHQYQ
Protein: Vinculin (O46037)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P85972}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P12003}. Cell membrane {ECO:0000250|UniProtKB:P12003}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12003}; Cytoplasmic side {ECO:0000250|UniProtKB:P12003}. Cell junction {ECO:0000250|UniProtKB:P12003}. Note=Cytoplasmic face of adhesion plaques. {ECO:0000250|UniProtKB:P12003}.
Interaction partners:
- Rhea, isoform B
- Paxillin, isoform F
- Integrin linked kinase, isoform A
- DE-cadherin
- Zyx102 protein
- Focal adhesion kinase, isoform D
- Breast cancer anti-estrogen resistance protein 1
- LIM domain-containing protein
- Canoe, isoform E
- Alpha-actinin, sarcomeric
Sequence:
MPVFHTKTIESILDPVAQQVSRLVILHEEAEDGNAMPDLSRPVQVVSAAVANLVKVGRDTINSSDDKILRQDMPSALHRVEGASQLLEEASDMLRSDPYSGPARKKLIEGSRGILQGTSSLLLCFDESEVRKIIQECKRVLDYLAVAEVINTMEQLVQFLKDLSPCLSKVHREVGAREKELTHQVHSEILVRCLEQVKTLAPILICSMKVYIHIVEQQGRGAEEAAENRNYLAARMSDELQEIIRVLQLTTYDEDTSELDNLTVLKKLSNAISNKMEQANEWLSNPYALRGGVGEKALRQVIDNATEISERCLPQDSYPIRKLADEVTAMANTLCELRQEGKGQSPQAESLVRGIRDRMGELKSLVHQAVLGVDKAGVQQTAHTIQGRLEQAVKWLQHPEINDGGLGERAINLIVEEGRKVAEGCPGHQKAEIQQLCDEVERLKRQAAGSGPAAKQAAKQLTQKLYELKAAIQNALVNRIVQDFMDVSTPLKQFTEAVLQPEGTPGREQNFNQKSNNLQAFSDRASKTSRMVAAGGACGNKKIAEILLSSAAQVDSLTPQLISAGRIRMNYPGSKAADEHLQNLKQQYADTVLRMRTLCDQATDPADFIKTSEEHMQVYAKLCEDAIHARQPQKMVDNTSNIARLINRVLLVAKQEADNSEDPVFTERLNAAANRLERSLPAMVGDAKLVATNIADPAAAAAWKNSFQRLLGDVREVRDAIAPPQPPPLPTSLPPPIPELSALHLSNQNAERAPPRPPLPREGLAPVRPPPPETDDEDEGVFRTMPHANQPILIAARGLHQEVRQWSSKDNEIIAAAKRMAILMARLSELVLSDSRGSKRELIATAKKIAEASEDVTRLAKELARQCTDRRIRTNLLQVCERIPTIGTQLKILSTVKATMLGAQGSDEDREATEMLVGNAQNLMQSVKETVRAAEGASIKIRSDQTSNRLQWVRRQPWYQY