wanglab/gogpt-training-data huggingface dataset:
Protein: Galectin-8 (Gal-8) (LGALS-8) (Q9JL15)
Organism: Mus musculus (Mouse)
Function: Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy. Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture. Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52. Required to restrict infection of bacterial invasion such as S.typhimurium. Also required to restrict infection of Picornaviridae viruses. Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.
Subcellular location: Cytoplasmic vesicle {ECO:0000250|UniProtKB:O00214}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00214}.
Interaction partners:
- Calcium-binding and coiled-coil domain-containing protein 2
- CD166 antigen
- Tripartite motif-containing protein 16
- Tax1-binding protein 1 homolog
- Podoplanin
- E3 ubiquitin-protein ligase LRSAM1
Sequence:
MLSLNNLQNIIYNPIIPYVGTITEQLKPGSLIVIRGHVPKDSERFQVDFQLGNSLKPRADVAFHFNPRFKRSSCIVCNTLTQEKWGWEEITYDMPFRKEKSFEIVFMVLKNKFQVAVNGRHVLLYAHRISPEQIDTVGIYGKVNIHSIGFRFSSDLQSMETSALGLTQINRENIQKPGKLQLSLPFEARLNASMGPGRTVVIKGEVNTNARSFNVDLVAGKTRDIALHLNPRLNVKAFVRNSFLQDAWGEEERNITCFPFSSGMYFEMIIYCDVREFKVAINGVHSLEYKHRFKDLSSIDTLSVDGDIRLLDVRSW
Protein: Protein SCO1, mitochondrial (P23833)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the accumulation of subunits 1 and 2 of cytochrome c oxidase complex. Thought to play a role in either mitochondrial copper transport or insertion of copper into the active site of COX.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:1944230}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase assembly protein COX11
- Cytochrome c oxidase copper chaperone
- Copper chaperone ATX1
- Cytochrome c oxidase assembly factor 6
- Heme A synthase COX15
- Ribosome assembly protein RSM22
- Cytochrome oxidase assembly protein SHY1
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c oxidase subunit 3
Sequence:
MLKLSRSANLRLVQLPAARLSGNGAKLLTQRGFFTVTRLWQSNGKKPLSRVPVGGTPIKDNGKVREGSIEFSTGKAIALFLAVGGALSYFFNREKRRLETQKEAEANRGYGKPSLGGPFHLEDMYGNEFTEKNLLGKFSIIYFGFSNCPDICPDELDKLGLWLNTLSSKYGITLQPLFITCDPARDSPAVLKEYLSDFHPSILGLTGTFDEVKNACKKYRVYFSTPPNVKPGQDYLVDHSIFFYLMDPEGQFVDALGRNYDEKTGVDKIVEHVKSYVPAEQRAKQKEAWYSFLFK
Protein: MARCKS-related protein (MARCKS-like protein 1) (Macrophage myristoylated alanine-rich C kinase substrate) (Mac-MARCKS) (MacMARCKS) (P49006)
Organism: Homo sapiens (Human)
Function: Controls cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation. When unphosphorylated, induces cell migration (By similarity). When phosphorylated by MAPK8, induces actin bundles formation and stabilization, thereby reducing actin plasticity, hence restricting cell movement, including neuronal migration (By similarity). May be involved in coupling the protein kinase C and calmodulin signal transduction systems (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P28667}. Cell membrane {ECO:0000305|PubMed:22751924, ECO:0000305|PubMed:25255805}; Lipid-anchor {ECO:0000305|PubMed:25255805}. Note=Associates with the membrane via the insertion of the N-terminal N-myristoyl chain and the partial insertion of the effector domain. Association of the effector domain with membranes may be regulated by Ca(2+)/calmodulin. Colocalizes with F-actin at the leading edge of migrating cells (By similarity). In prostate cancers, shows strong expression at apical and/or basal regions of the cell and also has weak cytoplasmic expression (PubMed:22751924). {ECO:0000250|UniProtKB:P28667, ECO:0000269|PubMed:22751924}.
Interaction partners:
- Calmodulin-like protein 4
- Calmodulin-like protein 5
- Calmodulin-like protein 3
- Calmodulin-like protein 6
- Myristoylated alanine-rich C-kinase substrate
- Calmodulin-1
- Protein kinase C delta type
- Protein kinase C epsilon type
- RecQ-mediated genome instability protein 1
Sequence:
MGSQSSKAPRGDVTAEEAAGASPAKANGQENGHVKSNGDLSPKGEGESPPVNGTDEAAGATGDAIEPAPPSQGAEAKGEVPPKETPKKKKKFSFKKPFKLSGLSFKRNRKEGGGDSSASSPTEEEQEQGEIGACSDEGTAQEGKAAATPESQEPQAKGAEASAASEEEAGPQATEPSTPSGPESGPTPASAEQNE
Protein: Serine/threonine-protein kinase CTR1 (EC 2.7.11.1) (Protein CONSTITUTIVE TRIPLE RESPONSE1) (Q05609)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a negative regulator in the ethylene response pathway. Phosphorylates the cytosolic C-terminal domain of EIN2, preventing the signaling in the absence of ethylene. Interacts with C24:1-ceramide upon hypoxic conditions (e.g. submergences) to in turn regulate EIN2 endoplasmic reticulum (ER)-to-nucleus translocation and EIN3 stabilization.
Interaction partners:
- Ethylene receptor 1
- Ethylene response sensor 1
- Ethylene receptor 2
- Ethylene response sensor 2
- Protein EIN4
- Ethylene-insensitive protein 2
- Protein ETHYLENE INSENSITIVE 3
- Mitogen-activated protein kinase kinase 9
- EIN3-binding F-box protein 1
- ETHYLENE INSENSITIVE 3-like 1 protein
Sequence:
MEMPGRRSNYTLLSQFSDDQVSVSVTGAPPPHYDSLSSENRSNHNSGNTGKAKAERGGFDWDPSGGGGGDHRLNNQPNRVGNNMYASSLGLQRQSSGSSFGESSLSGDYYMPTLSAAANEIESVGFPQDDGFRLGFGGGGGDLRIQMAADSAGGSSSGKSWAQQTEESYQLQLALALRLSSEATCADDPNFLDPVPDESALRTSPSSAETVSHRFWVNGCLSYYDKVPDGFYMMNGLDPYIWTLCIDLHESGRIPSIESLRAVDSGVDSSLEAIIVDRRSDPAFKELHNRVHDISCSCITTKEVVDQLAKLICNRMGGPVIMGEDELVPMWKECIDGLKEIFKVVVPIGSLSVGLCRHRALLFKVLADIIDLPCRIAKGCKYCNRDDAASCLVRFGLDREYLVDLVGKPGHLWEPDSLLNGPSSISISSPLRFPRPKPVEPAVDFRLLAKQYFSDSQSLNLVFDPASDDMGFSMFHRQYDNPGGENDALAENGGGSLPPSANMPPQNMMRASNQIEAAPMNAPPISQPVPNRANRELGLDGDDMDIPWCDLNIKEKIGAGSFGTVHRAEWHGSDVAVKILMEQDFHAERVNEFLREVAIMKRLRHPNIVLFMGAVTQPPNLSIVTEYLSRGSLYRLLHKSGAREQLDERRRLSMAYDVAKGMNYLHNRNPPIVHRDLKSPNLLVDKKYTVKVCDFGLSRLKASTFLSSKSAAGTPEWMAPEVLRDEPSNEKSDVYSFGVILWELATLQQPWGNLNPAQVVAAVGFKCKRLEIPRNLNPQVAAIIEGCWTNEPWKRPSFATIMDLLRPLIKSAVPPPNRSDL
Protein: Protein takeout (Q9VBV3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Participates in a novel circadian output pathway that conveys temporal and food status information to feeding-relevant metabolisms and activities. Involved in male courtship behavior. In the brain-associated fat body, transcription is enhanced by the dsx and fru male-specific isoforms and repressed by the dsx female-specific isoform.
Subcellular location: Secreted {ECO:0000269|PubMed:10892651}.
Interaction partners:
Sequence:
MFAIAFAVVLCLLVSVDAKFPEDPKPCKYGDGECIMKLCNTLFSENSAEGDPGLNLMQLDPLKVDRMVISQGESSSPVGITLTFTDNLLYGIKDQRIVKVKGFGRDLTAKHEVKIVTKTFSLVGPYNIQGKVLILPISGTGQSNMTMVNVRAIVSFSGKPLVKNGETYLDVTDLKITMKPESSHYHFSNLFNGDKALGDNMNVFLNENSEAIYKETAKAIDRSFGKLYLGVVKGVFSKLPYAKFFADES
Protein: Multivesicular body subunit 12A (CIN85/CD2AP family-binding protein) (ESCRT-I complex subunit MVB12A) (Protein FAM125A) (Q96EY5)
Organism: Homo sapiens (Human)
Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in the ligand-mediated internalization and down-regulation of EGF receptor.
Subcellular location: Cytoplasm. Nucleus. Endosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Colocalizes with F-actin. Some fraction may be nuclear.
Interaction partners:
- Tumor susceptibility gene 101 protein
- Vacuolar protein sorting-associated protein 37B
- Vacuolar protein sorting-associated protein 28 homolog
- Vacuolar protein sorting-associated protein 37A
- Vacuolar protein sorting-associated protein 37C
- Vacuolar protein-sorting-associated protein 25
- Ubiquitin-associated protein 1
- Vacuolar protein sorting-associated protein 37D
- Vacuolar protein-sorting-associated protein 36
- Signal transducing adapter molecule 1
Sequence:
MDPVPGTDSAPLAGLAWSSASAPPPRGFSAISCTVEGAPASFGKSFAQKSGYFLCLSSLGSLENPQENVVADIQIVVDKSPLPLGFSPVCDPMDSKASVSKKKRMCVKLLPLGATDTAVFDVRLSGKTKTVPGYLRIGDMGGFAIWCKKAKAPRPVPKPRGLSRDMQGLSLDAASQPSKGGLLERTASRLGSRASTLRRNDSIYEASSLYGISAMDGVPFTLHPRFEGKSCSPLAFSAFGDLTIKSLADIEEEYNYGFVVEKTAAARLPPSVS
Protein: RNA-binding protein 44 (RNA-binding motif protein 44) (Q3V089)
Organism: Mus musculus (Mouse)
Function: Component of intercellular bridges during meiosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells. Not required for fertility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21364893}. Note=Detected in the intercellular bridges. Localization to intercellular bridges is identified in all stages of tubules but dynamically increases from stage I pachytene spermatocytes to stage XII secondary spermatocytes and disappears after the formation of step 1 round spermatids (stage I). In addition, it is localized in the cytoplasm in pachytene spermatocytes to secondary spermatocytes. The cytoplasmic signal increases dramatically in stages X-XII, decreases from step 1 to step 3 spermatids, and disappears in step 4 spermatids.
Interaction partners:
Sequence:
MQATAALETDSDKNYPKNGGHFQNDKLYNPKKENMFFSNGCNGVILAFPDGKEDSLATEERASDKENSIVDQRDLSELSFSENQDSNRGNIFSQSSEFEDSNDYAFLNETYSIHYSESKLKDENLLHLYSGLHPEVHKRVEMIFDTLDNNSIGLGRSAEASGADCGDVQKSDVDEDSQQEYHSAELECISAHLAKTVSRSSLDVSELKTSSYDFKCGGNFEDNHGKLESGPSPSLESLNGFAQECSLQVSTSQSSDMLQEYHEPKYEKCKEQEVDLTYHKAFDGILQRSSSPLNHQKVPETQVYTKEVKSQTTESKDFYGNRIFQNKALQRPENATMFPQDRALETHLKANDAHQPSGPCALDDSVISLCGSSQYKSLPEPGFFSPVIPRVAVTDYQAEVEGSCLHHVQGSATNKACSLMKEVCLTSVPDAAACIAAVQQTLHVSSRVNASSSIVSASSITETKMVRQSQAEEWQSDKRSVACNTAWSCGQQCRDAQRAAPGSDSGRPLSTGCLKPSGNSLNENSLELRKVFDTTDRQKHCNRAFQLCEEKAVPSRCCQKTTERAIKAEMHLLDVCYQMCHRHCHHIYKLVMESRAGLNRNLQTDSAKKELGAALLSVLEDLKLRYMNLKGKVHKGIPLEELPPLSVESKLLSAFSDFVSRLMKDEACSLSGANSELDNQSLPDVDVSPGLLKTLSQMSFIPDSSQPEQGKSPMSDVCKNGDTDIGFNCLKLNDKECKTVQEASEDWFDATERLIGADFSETQDSTAECEEWQPRNPLELKNSELHGKGQGFLIHVGGLCPSVSEADLRSHFQKYQVSEISIYDSTNYRYASLAFAKNSNAKMAVKEMNGVKINGKSVTVRLVKIPGEYTPPPLSTTGNSTSMNHLEKNTNKDATSASSICRLPRAKSRQLESEQDSEFPPLDQGVKKNCNQMKSGQLLPETPFQFIPPNTLNLRSFTKIMKRLAELHPDISRDHIIEALQEVRINHKGFLNGLSINTIVKMASSFLRNSALK
Protein: Ribosomal large subunit pseudouridine synthase E (EC 5.4.99.20) (rRNA pseudouridylate synthase E) (rRNA-uridine isomerase E) (P75966)
Organism: Escherichia coli (strain K12)
Function: Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA.
Interaction partners:
- Phosphatase NudJ
- Ribosomal large subunit pseudouridine synthase C synthase)
- Ribosomal large subunit pseudouridine synthase D synthase)
- Dual-specificity RNA pseudouridine synthase RluA
- tRNA-specific 2-thiouridylase MnmA
- tRNA pseudouridine synthase C
- Ribosomal large subunit pseudouridine synthase B
Sequence:
MRQFIISENTMQKTSFRNHQVKRFSSQRSTRRKPENQPTRVILFNKPYDVLPQFTDEAGRKTLKEFIPVQGVYAAGRLDRDSEGLLVLTNNGALQARLTQPGKRTGKIYYVQVEGIPTQDALEALRNGVTLNDGPTLPAGAELVDEPAWLWPRNPPIRERKSIPTSWLKITLYEGRNRQVRRMTAHVGFPTLRLIRYAMGDYSLDNLANGEWREVTD
Protein: Doublecortin domain-containing protein 1 (Doublecortin domain-containing 5 protein) (M0R2J8)
Organism: Homo sapiens (Human)
Function: Microtubule-binding protein which plays an important role in mediating dynein-dependent transport of RAB8A-positive vesicles to the midbody during cytokinesis.
Subcellular location: Midbody, Midbody ring {ECO:0000269|PubMed:22159412}. Midbody {ECO:0000269|PubMed:22159412}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22159412}. Note=Associated with microtubules, in particular, with stabilized microtubules of the mitotic spindle during metaphase and with midbody microtubules during cytokinesis. {ECO:0000269|PubMed:22159412}.
Interaction partners:
- DnaJ homolog subfamily C member 24
- Elongator complex protein 4
- Mitochondrial inner membrane protease subunit 1
- Metallophosphoesterase MPPED2
- Neuronal migration protein doublecortin
- Paired box protein Pax-6
Sequence:
MAKTGAEDHREALSQSSLSLLTEAMEVLQQSSPEGTLDGNTVNPIYKYILNDLPREFMSSQAKAVIKTTDDYLQSQFGPNRLVHSAAVSEGSGLQDCSTHQTASDHSHDEISDLDSYKSNSKNNSCSISASKRNRPVSAPVGQLRVAEFSSLKFQSARNWQKLSQRHKLQPRVIKVTAYKNGSRTVFARVTVPTITLLLEECTEKLNLNMAARRVFLADGKEALEPEDIPHEADVYVSTGEPFLNPFKKIKDHLLLIKKVTWTMNGLMLPTDIKRRKTKPVLSIRMKKLTERTSVRILFFKNGMGQDGHEITVGKETMKKVLDTCTIRMNLNLPARYFYDLYGRKIEDISKVPLLEKCLQNSITPLRGLLWVSKGEGFSPSGAKMYIQGVLLALYQRLKSAKKYYKQLNLVMNEQKEKITEKVILSMTAKEHHKEQEEVSRLIDELQTAIKSNIGHLCKLGPQLQAEQEQFSSYVYQHIKSLPANTLVPGGLQLKVFENGKNTGEISVGISKKDLGSDSPIQTDHMMERLLLKIHQRLQGSSINPPGLNYSSMRLFDENGQEIKNPLSLKNEQKIWVSYGRAYRSPLNLALGLTFDRVSAFARGDIMVAYKTFLDPNAVLLPGCGNWEVCEGFPINFNCTSQQIPDQFEKVDLENHFLQNKVDPNIVLHASVSIGKWSFSGSEASSRSQIAPSILWPVASVWLITKTGMILSRAITQGCLAIGHPIRVKAAEGTSLEGYKLILQKRHSGDDSQKWVFGTDGCIYSKAYPQFVLTYLEELNAQVDVTQTEYHIHHGAWTTAHQEHGRNLAEEVLQESASNLGLKQLPEPSDTHLMPEGSLEETGELTVALVRKLEEKHPKASAQRWAIKHEGTSKPGQWKHSRVENPLWNKLTYMWPVLPSGQLNEEFDWPIQGLLVPSSPPMKKPICKTTEPYAPVRLRVLQNGEKNKNRSVTILGPDISPGRKTQCTEILNLPSAARRLYNEKGKEIFALKDLQRDELVYVSCGELWINPDLSIAQQKKQIFLRNLESDIAKIQIFCSTHKIEALVLEVQSDIVSGSKLAVHKPVAIFGEEKQVTEPEEKQMQEDPLTTENASSEILDSHVRAHLRMKACHTLPRYAWQETSHDFDEDDSLPKKTEKGLFENVEPQKKHSCSPKHSKLHKHCHQQFEYRDGQIISHAAPQLVLGVQGPNLRSGMEVVLVEKKSDGSHQRWIHQEDSRTFHLVSNPDLVLAVSMTKTRNEVCGYPVIVQKYKPYNNGAANQKWHYMKNIKALVAFHSTALDKEITSANYAGVCTSSVIKEENIDQPGYCYLSPDGKRKTMLCLACGQSMRTEKGLKQLLPGVPFLCISGTKTQKPFLQGPFKVISVAEVDLSCDKAEKTLSYYQARLLSLRMKTCTQAASHSGMAATHQKAVKIIAYKNGDGYRNGKLIVAGTFPMLLTECTEQLGLARAASKVYTKDGTPIFTLRDLVLWALDESFLQRDSEKQKQDAAPVGKEQIIVEKNPRMKVKNRLFAKSVTSDSLDGIDKSLLTLILRNPIAIWVSCGEPFLPPNALQKAEKLEKQNWLKKDRILADLDTMRHKMRQLKGRRVAACQPATMVPTKSPVQPVVVEGGWTEQTQQEIKLMELIRHTEAHLSEIQEMESKINFPIATKRIAVKPSNLYKQPNTKRVWIYLNGGRPEDGTYAWGKTISELLQDCSSRLKMTHPARALYTPSGEPIQSWDDIERDMVICVSMGHGFKTPKELKQLMEIRANYARIRRQQGPQATDIVVSPSTKLLSLAHLHN
Protein: Phenylcoumaran benzylic ether reductase IRL1 (EC 1.23.1.-) (Isoflavone reductase-like 1) (GbIRL1) (IFR-like protein 1) (M1T9X3)
Organism: Ginkgo biloba (Ginkgo) (Maidenhair tree)
Function: Oxidoreductase involved in lignan biosynthesis. Catalyzes the NADPH-dependent reduction of phenylcoumaran benzylic ethers. Converts dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl alcohol (IDDDC), and dihydrodehydrodiconiferyl alcohol (DDDC) to tetrahydrodehydrodiconiferyl alcohol (TDDC). May regulate changes in lignin content and accumulation of flavonoids.
Interaction partners:
Sequence:
MGKSRILIIGATGYIGRQVAKASAALGHPTLILVRETTASNPEKAQLLESFKSSGITIVHGSLEDHASLVEAIKKVDVVISTVGGAQIADQLNIIKAIKEVGTIKRFLPTEFGNDVDKTSAVEPAKGLFALKVKIRRAIEAEGIPYTYVSSNCFAGYFLPNLGQPGLTAPPRDKIVIFGDGNAKAVFVKEEDIGTFTIKSVDDPRTLNKTLYLRLPANTFSFNELVALWEKKIGKTLEKVYVPEEQVLKTIAETPFPGNIIISIAHSIFVKGDQTNFEIGDNGVEGSELYPDVKYTTVDEYLNQFV
Protein: TM4SF1 protein (Q8NE91)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MCYGKCARCIGHSLVGLALLCIAANILLYFPNGETKYASENHLSRFVWFFSGIVGGGLLMLLPAFVFIGLEQDDCCGCCGHENCGKRCAMLSSVLAALIGIAGSGYCVIVAALGLAEGPLCLDSLGQWNYTFASTEGQYLLDTSTWSECTEPKHIVEWNVSLFSILLALGGIEFILCLIQVINGVLGGICGFCCSHQQQMTAKRTNPGQSHNLPLFHCNLYISLVFICKTLY
Protein: Leucine-rich repeat-containing protein 36 (ROR gamma-binding protein 70) (Q1X8D7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEQWELDEEGIRRLGALTLEQPELVESLSLQGSYAGKIHSIGDAFRNFKNLRSLDLSRNLITSLKGIQYLCSLQDLNLYYNNIPSLVEVSRLQPLPFLKELDLRLNPVVRKDTDYRLFAVYTLQTLEKLDDRTVREGERKAAKLHFSQLGNSENFLLEVEKSSREKTMKNCVTGESSASKVSANVDSRIEMDSNKGLFIPFPNREIKDSLSTSATQGNGTRDQKLDTFPLGTQTQEVARREMPSDNHQEDEFRHYSPRQSTVRSPEKMTREGYQVSFLDNKSSGSSPEKELIPKPDTFHLTHDASLSKCLDVGDSSQIHPYQLPSDVGLENYDSCYSQTLSLHGSLGKRPQRSKNYQEYSIKPSNDIKTTASHSCGDLLTSLSNPDSSTGRLLKLSSDLYATTHFNSDPAVLVNVEQQLSTSLDDLTPAHGSVPNNAVLGNRTTPLRTLLLSPGTSEHRKIFTKRSLSPSKRGFKWKDNILANLNLKHGFQDATGSEPLSSDLGSLHGLAGNHSPPISARTPHVATVLRQLLELVDKHWNGSGSLLLNKKFLGPARDLLLSLVVPAPSQPRCCSHPEDTMKAFCRRELELKEAAQLVPNDMESLKQKLVRVLEENLILSEKIQQLEEGAAISIVSGQQSHTYDDLLHKNQQLTMQVACLNQELAQLKKLEKTVAILHESQRSLVVTNEYLLQQLNKEPKGYSGKALLPPEKGHHLGRSSPFGKSTLSSSSPVAHETGQYLIQSVLDAAPEPGL
Protein: THUMP domain-containing protein 1 (Q9NXG2)
Organism: Homo sapiens (Human)
Function: Functions as a tRNA-binding adapter to mediate NAT10-dependent tRNA acetylation modifying cytidine to N4-acetylcytidine (ac4C).
Interaction partners:
- RNA cytidine acetyltransferase
- Pseudouridylate synthase TRUB1
Sequence:
MAAPAQQTTQPGGGKRKGKAQYVLAKRARRCDAGGPRQLEPGLQGILITCNMNERKCVEEAYSLLNEYGDDMYGPEKFTDKDQQPSGSEGEDDDAEAALKKEVGDIKASTEMRLRRFQSVESGANNVVFIRTLGIEPEKLVHHILQDMYKTKKKKTRVILRMLPISGTCKAFLEDMKKYAETFLEPWFKAPNKGTFQIVYKSRNNSHVNREEVIRELAGIVCTLNSENKVDLTNPQYTVVVEIIKAVCCLSVVKDYMLFRKYNLQEVVKSPKDPSQLNSKQGNGKEAKLESADKSDQNNTAEGKNNQQVPENTEELGQTKPTSNPQVVNEGGAKPELASQATEGSKSNENDFS
Protein: BTB/POZ domain and ankyrin repeat-containing protein NPR3 (OsNPR3) (Q75HA6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in defense response against the bacterial blight disease caused by Xanthomonas oryzae pv. oryzae (Xoo). Plants expressing an NPR3/NH3 transgene driven by its native promoter show enhanced resistance to the Xoo pathogen, and exhibit elevated sensitivity to benzothiadiazole (BTH) treatment and enhanced induction of defense-related genes upon treatment with BTH. Intriguingly, constitutive over-expression of NPR3/NH3 with a ubiquitin promoter does not confer disease resistance to Xoo.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5ICL9}.
Interaction partners:
- BTB/POZ domain and ankyrin repeat-containing protein NPR1
- BTB/POZ domain and ankyrin repeat-containing protein NPR2
- Os12g0138800 protein
- Transcription factor TGA2.1
- Transcription factor TGA2.2
- Os11g0142300 protein
- Transcription factor TGA2.3
- Transcription factor TGAL1
- Transcription factor TGAL6
- Transcription factor TGAL10
Sequence:
METSTISFSSSSPPSPPPPQPAPGDIDAVSLGRLSRNLENLLDPAFLNCADAEIVLASGGGDPGGGAVVGVHRCILAARSRFFYDHFSSAPAPAPATAGDKPQLDLDGLVPGGRHIGRDALVAVLSYLYTGRLRSAPPEAAACLDDGCSHDACRPAIDFVVESTYAASGFQISELVSLFQRRLSDFVNKALAEDILPILVVASTCHLPELLNQCIQRVANSNLDNRYLEKRLPDDLYAKLKEFRVPDEPHSGILDPEHEKRVRNIHKALDSDDVDLVGMLLKESPVTLDDAFAIHYAAAYCEPKVLAELLKLESANVNLKNSSGYTPLHMACMRREPDIIVSLIEKGASVLERTQDGRDALTICKRLTREKDRNEKSEKCKERSKAYLCIGVLQQEIKRRPQILEDQMSAEESIATPLLVDNFHMRLLNLENRVAFARIFFPSEAKLVMRIAQADSTQEFAGLTSANFSKLKEVDLNETPTMQNRRLRERLDALTKTVELGRRYFPHCSEVLDKFLNEESTDLILLESGTAEDQQTKRMRFSELREDVRKAFTKDKAAGAAISSSTSASSSPRYETKLRPGNKKGKLSR
Protein: NOD2a protein (Nucleotide-binding oligomerization domain-containing 2) (Nucleotide-binding oligomerization domain-containing protein 2) (F8W3K2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004187}. Cell membrane {ECO:0000256|ARBA:ARBA00004193}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Receptor-interacting serine-threonine kinase 2.
- ATG16 autophagy-related 16-like 1
- Mitochondrial antiviral-signaling protein
- Erbb2-interacting protein.
- Angio-associated, migratory cell protein.
- Autophagy protein 5
- NACHT, LRR and PYD domains-containing protein 1 homolog
- Ubiquitin-like protein ATG12
- Toll-like receptor 2.
- TNF receptor-associated factor 6
Sequence:
MNAQQLILKQRAELLAVLCGGGSDEPLESVLDLLLAQEVLVWEDYLRVRVAEKPLCANIRQLLDLVYDKGEDACSYFLAAIEQELAEEQKAGLCFGNGCVMVGKDRPATATSTLLADRPMLVRRLRDNIDGALNILLTTGCFSIKDCDSVQLPVYTPSQQVRRLLDQVKFKGETAAKTLLEYLEQPEPTSPISAEKENTPSADCLVYQKKLRSSVASQSLFLSTYGGTGRFSLDDIYTDGHLEVMNSSGETTTLGLEDVVGPMGTLNEDADTVLVSGEAGSGKSTLVQRLHLLWAREALLLNTFLLFPFSCRKLNAEHRELSLKELLFLHCCWPDRNQDEVFQFILDHPHLVLFTFDGLDEFKLGFTDEERHCCPTKQVPIPVLLFNLLQGTLMKGVMKVVTSRPHAVGPSLKRYLRKEVLLKGFSPGGIDCFVKKHYSDPAMATRVIESVQGNTALLGLCHIPVFCWIVIKCYQELLAGQDGIPQTITDVYLLVLQHFFQRKSSQPQSGLGKAWLAEHLDTVLKLGELALEGLQTSCYVFSGYELQRNRITEQDVGIGFLIYCSDISVNDCKRYEFLHITLQCFFAALYVILNRNNDRSAISRLFQPRNRQVSGLSQSCLGQCMDHSVEESHEAETANLQITAQFVSGLLSQRHNNLLLECCPAAVRERNVKQVVKSLSKRMQRHFKSIPRPVEGEKKSMHAMPSFVWLIKCIYELQDNSIAQDAMAKLDVEHLKLTYCNIGPVECTALAYVLKNLRKPVGLQLDNNSVGDVGVEQLLPCLPMCHSLYLRNNNISDEGIRKLLEKGIECENFQKIALFNNKLTDTCTQYFSCLLKSKQNFLALRLGNNNITSVGAEQLAEGLSYNQSLQFLGLWGNKVGDRGAEVLADALTNSKTLIWLSLVDNGVGSAGACALAKFIRQNKSLEELWLNKNSICKEGVDCLIEALKMNTSVKKVWLRGNNLSPQEEEQLSQQECRLTF
Protein: Urease accessory protein D (AtURED) (Q7Y0S0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the maturation and activation of urease via the functional incorporation of the urease nickel metallocenter.
Interaction partners:
- Urease accessory protein G
- Urease accessory protein F
- Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- Phosphoribosylformylglycinamidine cyclo-ligase, chloroplastic
- Phosphoribosylamine--glycine ligase, chloroplastic
- Urease
- Adenylosuccinate synthetase, chloroplastic
- phosphoribosylaminoimidazole carboxylase
Sequence:
MATGKVVVEKVGGRSTATSCFSKYPLKFLLPSKAAPAGTDVVWIYSITYGGGIVSGDSISCEFTIGDGCTAVITTQSSTKVYKAIGSKCSEQILEARIGSEALLVVIPDPVTCFSTARYYQKQIFRLLSDSNLVLVDWITSGRHANGEKWDFEFYKSINNVYLEDDHPLFLDTVLLEKRSIQSIAERMQDYQAIAMVILFGAKLKEIQKQVQENVKNMMSEQLQLSYSSRRHKSESSSRNRFMKPEFIASCSTFGPEGKGVVVRIASDSTESVYNFLRQQLAELEPVLGQAPYA
Protein: SnoI (Q00G34)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FSVGGEMRLCLPQFLNNVLNDFSLEQINRIFDELGIYCSQCTHDQLVEFKAAKILPSDVKASGLITRTDAERLCAALLHRSDRNSYVPIESLAKGALSFHVYHKCFGKCEGICTPDMYSYQKPTCIKCLECDGWFSPQKFVGHVHRKFENHTCHWGFDSRNWHDYLHVALDVENREKYQIILDQLKEVELKEMHKAQRELEHKKRKVRWV
Protein: Trans-2,3-dihydro-3-hydroxyanthranilate isomerase (EC 5.3.3.17) (Phenazine/pyocyanine biosynthesis protein PhzF) (O69754)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Isomerase that catalyzes the condensation of two molecules of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) into the phenazine ring system. The final product is not yet known.
Interaction partners:
- Phenazine biosynthesis protein PhzD1
- anthranilate synthase
- Phenazine biosynthesis protein PhzB2
- Phenazine biosynthesis protein PhzB1
- Phenazine biosynthesis protein PhzA1
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- Probable pyridoxamine 5'-phosphate oxidase
- Phenazine biosynthesis protein PhzA2
- 5-methylphenazine-1-carboxylate 1-monooxygenase
- Phenazine-1-carboxylate N-methyltransferase
Sequence:
MHRYVVIDAFASEPLQGNPVAVFFDCDDLSGERMQRMAREMNLSESTFVLRPQQDGDARIRIFTPVNELPFAGHPLLGTAIALGAETDKDRLFLETRMGTVPFALERQDGKVVACSMQQPIPTWEHFSRPAELLAALGLKGSTFPIEVYRNGPRHVFVGLESVAALSALHPDHRALCDFPDLAVNCFAGAGRHWRSRMFSPAYGVVEDAATGSAAGPLAIHLARHRQIPYGQQIEILQGVEIGRPSRMYARAEGAGERVSAVEVSGNGAAFAEGRAYL
Protein: mRNA export factor GLE1 (Nucleoporin GLE1) (Q5A2J1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
- Nucleoporin NSP1
- FG-nucleoporin
- RNA export factor
- Nucleoporin
- ATP-dependent RNA helicase DBP5
- mRNA export factor MEX67
- Uncharacterized protein
- Nuclear pore complex protein
- FG-nucleoporin
- Nuclear pore complex protein Nup85
Sequence:
MKFGLPDNFEVVVDVSSKPANQITLSLIKPSRPKNTFNDVFKKTCNDIDENTLDFIKFKQNEINERVDTLQSKMKSREAQADANITHLIQDFNSQLRIQNEQVEELIRKEKERIRLELERKRREEEERRRREEEERRRQEEEERRRKEEEERKRKEEAKRLEEEERKRKEEEEARKKREAELKRQQELKIQREKELLEQKKKERESRFTTDYNQIEKTLYKYKQDIQDIKNNVKLKLNEDPDLKKQVNQYKRKINPKFGQLSNSLSQFNKISTEVIGMIKAVETNALVFKWVLNFTAKAIIDQAETEVIVRPNSAVPLAKLAYAILQAIPDFEYYLNARFIKKCPYIIGYNCSIDSEEGRERMGWKRPDGSKWEEETKYDERMGGIVSVWAAMTTITNHGSQKSLYSFEASWQFLARTANLQTSMLVNTHFTILGNWWEAAGASFLGVYGNQSQKLMYIVVVQLTDVVASKKFPSAARLRIMGEEWVTRRQIQSLKAMEY