wanglab/gogpt-training-data huggingface dataset:
Protein: N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase (EC 3.5.1.89) (P23797)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26928762}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1
- GPI mannosyltransferase 3
- GPI mannosyltransferase 1
- Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit
- GPI-anchored wall transfer protein 1
- GPI-anchor transamidase
Sequence:
MKMLRRTKVNFSKLLYKITKLAIVLTILYIYFTPKIVSRNNASLQHIFPHKYGDYEINLVIAHPDDEVMFFSPIISQLNSYFPRTVPFNIICLSKGNAEGLGETRVRELNESAALLLHNERAVSVQVMDFQDGMDEIWDIDSITSSLSQKIDIKNHNLNQIIVTFDSYGVSNHINHKSCYAAVKKLVDDYAQPKTKRNEQPPHVTALYLRSYKNNIVLKYNSFIWEILKILYDLISPFRRIIQALPPNTAAEKDKLSLMNTHAQYVLAFATMLNAHESQVVWFRYGWWIFSRFVFVNEFDVYTY
Protein: Protein DOUBLE-STRAND BREAK FORMATION (AtDFO) (Protein DSB FORMATION) (Q8RX33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for meiotic double-strand break (DSB) formation, the initial event for meiotic recombination.
Interaction partners:
- Protein PUTATIVE RECOMBINATION INITIATION DEFECT 1
- Putative recombination initiation defects 3
- Protein MULTIPOLAR SPINDLE 1
- Pachytene checkpoint protein 2 homolog
- Transcription coactivator
- Type 2 DNA topoisomerase 6 subunit B-like
- Meiotic recombination protein SPO11-2
- Meiotic recombination protein SPO11-1
- WD repeat-containing protein VIP3
- Double-strand break repair protein MRE11
Sequence:
MRHNIKFKSKGTLKIRNTAQISLWKKCSDSMIADQTYLFINRVQDRRFDEESLRILELSLVAMNVKSFLEVRSRLRDFMRSESVVIFGELTGESMVAKLSVLEFFARAFALLGDMESCLAMRYEALNLRQLKSPSCLWLGVSHSEWTKFAVQSMENGFPSIAGKASENALLSLKKDSLIEPKSEDNSDILDAAEKVRRLRDSAASLTSSHSGIFIYIVSSLKFAVCNRLLTTF
Protein: ESAT-6-like protein EsxB (10 kDa culture filtrate antigen CFP-10) (CFP-10) (Secreted antigenic protein MTSA-10) (P9WNK5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A secreted protein. Acts as a strong host (human) T-cell antigen. Involved in translocation of bacteria from the host (human) phagolysosome to the host cytoplasm. Might serve as a chaperone to prevent uncontrolled membrane lysis by its partner EsxA; native protein binds poorly to artificial liposomes in the absence or presence of EsxA. EsxA and EsxA-EsxB are cytotoxic to pneumocytes. EsxB (and EsxA-EsxB but not EsxA alone) activates human neutrophils; EsxB transiently induces host (human) intracellular Ca(2+) mobility in a dose-dependent manner, monocytes and lymphocytes do not respond. Neutrophils respond to EsxB by chemotaxis and primed neutrophils treated with EsxB produce reactive oxygen species (ROS); Ca(2+) release and the ROS burst via are induced by an unidentified G-protein coupled receptor. May help regulate assembly and function of the type VII secretion system (T7SS).
Subcellular location: Secreted {ECO:0000269|PubMed:14557536, ECO:0000269|PubMed:15378760, ECO:0000269|PubMed:16048998, ECO:0000269|PubMed:9846755}. Secreted, cell wall {ECO:0000269|PubMed:19906174}. Host cell surface {ECO:0000269|PubMed:15973432, ECO:0000269|PubMed:19265145}. Host endoplasmic reticulum {ECO:0000269|PubMed:25356553}. Note=Probably secreted via the ESX-1 / type VII secretion system (T7SS) (PubMed:19876390). Binds to CD14+ and CD19+ host (human) cells (PubMed:19265145). Localized on the cell surface of host (human) cell monocytes and macrophages (often in patches), but not fibroblasts (PubMed:15973432). Exogenous EsxA and EsxA-EsxB complex can enter host (human and mouse) endoplasmic reticulum (PubMed:25356553). {ECO:0000269|PubMed:15973432, ECO:0000269|PubMed:19265145, ECO:0000269|PubMed:19876390, ECO:0000269|PubMed:25356553}.
Interaction partners:
- 6 kDa early secretory antigenic target
- ESX-1 secretion system protein EccCb1
- ESAT-6-like protein EsxH
- PPE family immunomodulator PPE68
- ESX-1 secretion-associated protein EspC
- ESX-1 secretion-associated protein EspA
- ESX-1 secretion-associated protein EspI
- ESX-1 secretion system protein EccCa1
- ESAT-6-like protein EsxG
- ESAT-6-like protein EsxP
Sequence:
MAEMKTDAATLAQEAGNFERISGDLKTQIDQVESTAGSLQGQWRGAAGTAAQAAVVRFQEAANKQKQELDEISTNIRQAGVQYSRADEEQQQALSSQMGF
Protein: Eyes absent homolog (EC 3.1.3.48) (Q9W6E8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEMQDLASPHSRVSGSSESPNGPNIDNSHINNNSMTPNGTEGDNITMLTTADWLLSSSSQSAAVKTEPMSSSEIATSVADGSLDSFSGSAIGTSGFSPRQTHQFSPQIYPSNRAYPHILPTPSAQNMAAYGQTQYTTGMQQAAAYGTYPQPVQPYGISAYGIKTEGGLTQAQSPGQSGFLSYSSSFSTPQTGQAPYSYQMQGGSFTTTSGLYAGSNSLTNSTGFNSTQQDYPSYPTFGQSQYAQYYNSSPYTSPYMTSNNTSPTTPSTTATYTLQEPPSGITSQALTEQPTGEYSTIHSPSTPIKDSDSDRLRRATDVKARGRGRRNNNPSPPPDSDLERVFIWDLDETIIVFHSLLTGSYANRFGRDPPTSVSLGLRMEEMIFNLADTHFFFNDLEECDQVHIDDVSSDDNGQDLSTYNFSTDGFHAAATSANLCLATGVRGGVDWMRKLAFRYRRVKEIYTTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALTLIHSRSNCVNILVTTTQLIPALAKVLLYGLGVVFPIENIYSATKIGKESCFERVIQRFGRKVVYVVVGDGVEEEQGSKKHNMPFWRISSHSDLMALHHALDLEYL
Protein: Autotransporter heptosyltransferase TibC (EC 2.4.99.-) (Q9S4K6)
Organism: Escherichia coli O78:H11 (strain H10407 / ETEC)
Function: Glycosylates the TibA adhesin.
Interaction partners:
Sequence:
MSTLKNTFFITPPDTPTQAGPENIFYDFNDGARVLLPEGKWHVRLLDADSENILFCCDVDKGWVTSSKKYFVRFRIQVFRQGEETPLLDETLKLKDRPVLISFPTGTLGDLLGWFPYAERFQSLHKCRLECTMSQDIIDLLAPQYPQIQFSTPDKPRTVAPYATYRVGLYFGGDTNNQPVDFRKVGFHRSAGYILGVDPREAPVRLDLSAPRVIQEPYVCIATQSTCQAKYWNNGTGWSEVIAHLKSLGYRVMCIDRDAHYGQGFVWNHIPWGAEDFTGKLPLQERVNLLRHASFFIGLPSGLSWLAWATRIPVVLISGFSLPNSEFYTPWRVFNSHGCYGCWDDTSLNFDHHDFLWCPRHKNTDRQFECTRLITGAQVNGVINKLHRSLTEQGVEATLKKGVSNE
Protein: FcRI (Q2V8M5)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
- LOW QUALITY PROTEIN: carcinoembryonic antigen-related cell adhesion molecule 5.
Sequence:
MHFFHIFIVFITLLACVRMDDIDPTPPPVKAKATVSLGKPRLFSGEDVQMTCSVPDDPSSNWTYEWFHDGELLSATEVYSLNKAQVLQSGNYTCKGLKTIKAWPYIVPSIPSDPLKIHVDGGWVLLQTPFEPLIIEENMTLTCRVRDDPLLSNVIFYKDGVEFNKQKGTDVVFTKLTLEDAAIYSCRATWIKNMEYQSSQSLPSYVTVLDILETPTMTIVGGRGRVRSGNKVEFRCITKVNAREQDLNIEYFYLKNGNRLGPASARDTYAISEVNINHTGNYTCKVRIRALNVERWSNQVNLKVLPPLNL
Protein: Green-sensitive opsin (Green cone photoreceptor pigment) (P28683)
Organism: Gallus gallus (Chicken)
Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein.
- G protein-coupled receptor kinase
- G protein subunit alpha transducin 2
- G protein subunit beta 1
- S-antigen visual arrestin.
- Rhodopsin
- Peripherin-2
- Retinoid isomerohydrolase
- Rhotekin.
- Cone-rod homeobox
Sequence:
MNGTEGINFYVPMSNKTGVVRSPFEYPQYYLAEPWKYRLVCCYIFFLISTGLPINLLTLLVTFKHKKLRQPLNYILVNLAVADLFMACFGFTVTFYTAWNGYFVFGPVGCAVEGFFATLGGQVALWSLVVLAIERYIVVCKPMGNFRFSATHAMMGIAFTWVMAFSCAAPPLFGWSRYMPEGMQCSCGPDYYTHNPDYHNESYVLYMFVIHFIIPVVVIFFSYGRLICKVREAAAQQQESATTQKAEKEVTRMVILMVLGFMLAWTPYAVVAFWIFTNKGADFTATLMAVPAFFSKSSSLYNPIIYVLMNKQFRNCMITTICCGKNPFGDEDVSSTVSQSKTEVSSVSSSQVSPA
Protein: Inner centromere protein A (XL-INCENP) (xINC) (xIncenp) (Mitotic phosphoprotein 130) (O13024)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with aurkb/aurora-B, the N-terminus associated with cdca8/borealin and/or cdca9/dasra-A tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs aurkb/aurora-B toward substrates near microtubules. Activates aurkb.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NQS7}. Chromosome {ECO:0000269|PubMed:12464631}. Chromosome, centromere {ECO:0000269|PubMed:10996078}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10996078}. Midbody {ECO:0000250|UniProtKB:Q9NQS7}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9NQS7}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis (PubMed:10996078). Colocalizes to the equatorial cell cortex at anaphase (PubMed:10996078). Colocalizes with AURKB at mitotic chromosomes (PubMed:10996078). {ECO:0000269|PubMed:10996078}.
Interaction partners:
Sequence:
MNDAECLSHLLQVCARKTEEFVRTLDSKHMVWLLEIEEEARKMFSSDFNAEPELMPKTPSQKRRRKKRTSILPDENRDPSGRRISRRQSNASWSSSVRRLSVRNQNKANDDSIQEEPAQLKRMTRARAQASIKSTPVLETALPESPSQICQKNAQVKISEQERRSAEQKLIESDFELKTVPEITKDNVSETVNSAVPAVPVTPENKSRAAGKLKIAASSTPEQKAEMVDLTCESPRPANEQQLNLSNQSATPTGSKSDRRSVRRSLVVRKSSSRRASLASQFSLASKRESMTREAVRKSIRQSISQKKAAMEISSTSSQRSYQSSIEMVDDEITIKIRPETVPSETVSEEAPAAESPRRSLRSRAFKKIAISNLPDSEEPPRKVTRQMVAGNAEPTPETTEDAQNIRRKSYKRAVDELSDDERPSEEERSPPRKKTPSPPCPPSKIVRPPPHMKSFLHTVQKNQLLMMTPGSIGKNIIMKSFIKRNTPLKTDPKTEEKERQRLDALRKKEEAELQRKQKIEEGKKRKQEELKVRREERLRKVLQARERVEQLEEEKKKKIEQKFAQIDEKSEKVREDRMAEEKAKKKMTAKKQEEVECRRKQEEEARRLKVKQMEEEERRHQELLQKKREEEELERQKKIAEAKRLAEQERERQLLAEKERLRAEREKERIEKEKALQLQRELERAAQEKEQQRREAEERKKREQQERLEQERLRKEQEAKRLQEEEQRKAKEQAAVAASAPVMNVTVDMQNSPACESYEMTPKSCKVPSVKVNEDNYGMDLNSDDSTDDESQPRKPIPAWASGNLLTQAIRQQYYKPIDVDRMYGTIDSPKLEELFNKSKPRYFKRTSSAVWHSPPLSSNRHHLAVGYGLKY
Protein: Cytochrome P450 (EC 1.14.14.-) (Q91W87)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368047}. Microsome membrane {ECO:0000256|RuleBase:RU368047}.
Interaction partners:
Sequence:
MRLPTGAELWPIAIFTVIFLILVNLMHWRQRWTAHYPPGPMPWPVLGNLLHMDFQNMPAGFQKLRGRYGDLFSLQLASESVVVLNGLTALREALVKHSEDTADRPPLHFNDLLGFGPRSQGIVLARYGPAWRQQRRFSVSTMHHFGLGKKSLEQWVTEEARCLCAAFADHTGHPFSPNTLLDKAVCNVIASLLYACRFEYDDPRFIRLLGLLKETLKEEAGFLPMFLNVFPMLLRIPGLVGKVFPGKRAFVTMLDELLAEHKTTWDPTQPPRDLTDAFLAEVEKAKGNPESSFNDENLRTVVGDLFSAGMVTTSTTLSWALMLMILYPDVQRRVQQEIDEVIGQVQCPEMADQARMPYTNAVIHEVQRFADILPLGVPHKTSRDIELQGFLIPKGTTLITNLSSALKDETVWEKPLCFHPEHFLDAQGHFVKPEAFMPFSAGRRSCLGEPLARMELFLFFTCLLQRFSISVPDGQPQPSDHGVFRALTTPCPYQLCALPR
Protein: Potassium channel TASK2 (Potassium channel, subfamily K, member 5) (TASK2 potassium channel) (Q9JK62)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Intermediate conductance calcium-activated potassium channel protein 4
- Potassium voltage-gated channel subfamily KQT member 1
- Potassium voltage-gated channel subfamily E member 3
- Inward rectifier potassium channel 13
- Potassium channel subfamily K member 9 channel 3)
- Potassium channel subfamily K member 3 channel) channel 1)
- Potassium channel subfamily K member 18
Sequence:
MVDRGPLLTSAIIFYLAIGAAIFEVLEEPHWKEAKKNYYTQKLHLLKEFPCLSQEGLDKILQVVSDAADQGVAITGNQTFNNWNWPNAMIFAATVITTIGYGNVAPKTPAGRLFCVFYGLFGVPLCLTWISALGKFFGGRAKRLGQFLTRRGVSLRKAQITCTAIFIVWGVLVHLVIPPFVFMVTEEWNYIEGLYYSFITISTIGFGDFVAGVNPSANYHALYRYFVELWIYLGLAWLSLFVNWKVSMFVEVHKAIKKRRRRRKESFESSPHSRKALQMAGSTASKDVNIFSFLSKKEETYNDLIKQIGKKAMKTSGGGERVPGPGHGLGPQGDRLPTIPASLAPLVVYSKNRVPSLEEVSQTLKNKGHVSRPLGEEAGAQAPKDSYQTSEVFINQLDRISEEGEPWEALDYHPLIFQNANITFENEETGLSDEETSKSSVEDNLTSKEQPEQGPMAEAPLSSTGEFPSSDESTFTSTESELSVPYEQLMNEYNKADNPRGT
Protein: Aminopeptidase (EC 3.4.11.-) (B0BCZ1)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MNFAEREGSKRYCIQTKHVAILCAVVVGVGLIVGLAVGLTRSCDSSGDGGPGTAPAPSHLPSSTASPSGPPAQDQDICPASEDESGQWKNFRLPDFVNPVHYDLHVKPLLEEDTYTGTVSISINLSAPTRYLWLHLRETRITRLPELKRPSGDQVQVRRCFEYKKQEYVVVEAEEELTPSSGDGLYLLTMEFAGWLNGSLVGFYRTTYTENGQVKSIVATDHEPTDARKSFPCFDEPNKKATYTISITHPKEYGALSNMPVAKEESVDDKWTRTTFEKSVPMSTYLVCFAVHQFDSVKRISNSGKPLTIYVQPEQKHTAEYAANITKSVFDYFEEYFAMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDPKESASSNQQRVATVVAHELVHQWFGNIVTMDWWEDLWLNEGFASFFEFLGVNHAETDWQMRDQMLLEDVLPVQEDDSLMSSHPIIVTVTTPDEITSVFDGISYSKGSSILRMLEDWIKPENFQKGCQMYLEKYQFKNAKTSDFWAALEEASRLPVKEVMDTWTRQMGFPVLNVNGVKNITQKRFLLDPRANPSQPPSDLGYTWNIPVKWTEDNITSSVLFNRSEKEGITLNSSNPSGNAFLKINPDHIGFYRVNYEVATWDSIATALSLNHKTFSSADRASLIDDAFALARAQLLDYKVALNLTKYLKREENFLPWQRVISAVTYIISMFEDDKELYPMIEEYFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVLETVKNNIEWLKQHRNTIREWFFNLLESG
Protein: Ubiquitin carboxyl-terminal hydrolase 27 (EC 3.4.19.12) (Deubiquitinating enzyme 27) (Ubiquitin thioesterase 27) (Ubiquitin-specific-processing protease 27) (X-linked ubiquitin carboxyl-terminal hydrolase 27) (Q8CEG8)
Organism: Mus musculus (Mouse)
Function: Deubiquitinase involved in innate antiviral immunity by mediating deubiquitination of CGAS and RIGI. Negatively regulates RIGI by mediating 'Lys-63'-linked deubiquitination of RIGI, inhibiting type I interferon signaling (By similarity). Also regulates 'Lys-63'-linked ubiquitination level of MDA5/IFIH1 (By similarity). Acts as a positive regulator of the cGAS-STING pathway by catalyzing 'Lys-48'-linked deubiquitination of CGAS, thereby promoting its stabilization. Can reduce the levels of BCL2L11/BIM ubiquitination and stabilize BCL2L11 in response to the RAF-MAPK-degradation signal. By acting on BCL2L11 levels, may counteract the anti-apoptotic effects of MAPK activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:27013495}. Nucleus {ECO:0000269|PubMed:27013495}.
Interaction partners:
- Transcription and mRNA export factor ENY2
- Ataxin-7-like protein 3
- SAGA-associated factor 29
- Transformation/transcription domain-associated protein
- Transcriptional adapter 3
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 12
- SPT3, SAGA and STAGA complex component
- Ataxin-7
Sequence:
MCKDYVYDIDIEQIAKEEQGEALKLQASTSTEVSQQQCSVPGLGEKYPTWETTKPELELLGHNPRRRRIASSFTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHLAGYRQQDAHEFLIAALDVLHRHCKGDDVGKVASNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCTSFWPMSPGRESSLNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHFKRFEHSAKQRRKITTYISFPLELDMTPFMASSKETRVNGQLQLPTNSANNENKYSLFAVVNHQGTLESGHYTSFIRHHRDQWFKCDDAVITKASIKDVLDSEGYLLFYHKQVLEPEPEKVKEMTPQAY
Protein: Large ribosomal subunit protein bL12cz (50S ribosomal protein L12-1, chloroplastic) (CL12-A) (P36210)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein bL9c
- Large ribosomal subunit protein uL4c
- Large ribosomal subunit protein bL28c
- 50S ribosomal protein L33
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Large ribosomal subunit protein uL15c
- Large ribosomal subunit protein bL31c
- Large ribosomal subunit protein bL17c
- Large ribosomal subunit protein bL27c
Sequence:
MASTTLSIATTIRSSSYPTLASINHFPSRTTTIEFPSRFGGGSSSTLTHRATHLRPIAAVEAPEKIEKIGSEISSLTLEEARILVDYLQDKFGVSPLSLAPAAAAVAAPADGGAAAVVEEQTEFDVVINEVPSSSRIAVIKAVRALTSLALKEAKELIEGLPKKFKEGITKDEAEEAKKTLEEAGAKVSIA
Protein: HMG box-containing protein 4 (High mobility group protein 2-like 1) (xHMG2L1) (Q6WKW9)
Organism: Xenopus laevis (African clawed frog)
Function: Negatively regulates Wnt/beta-catenin signaling during development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
Sequence:
MSYRDLRECIDLERGTEDVGLAAGRSQREKKRSYKDLLREEEEIAEQVRKSSKKRSKELDLFSGNELHKKKKKHSSDDYHADHSTDSAKKKKKTSLPSPSSSDTAMDLLKAITSPQADTSTTHPSKKPEKILATPISFSSPSQPPHKDYHKKSGEVSGDDSSHRSKKSKPLTLREPDGLRMKLIMSPNEKSEEEAVSPQGGPGHSDSASSKKNSKKLGREEIESRSSHKKHKKQSYTPRSGGTPDSASSTGGELDAGELVIDDSLRDMKKKKKSKKSKKKKDKHKDEKHKKHSKSKREHEVEQSQTQIASPGLPSPPPPPATTPPTSPPSIPLQPQALVTHTEEQSDKKKKKEDPEKPKKKNMSAYQVFSKEYRVSIIAEHPGIDFGELSKKLAEVWKQLPEKDKLVWKQKAQYLQHKQNKAEATTVKRKSSSSESAPKSKGSSSGLVSPNKKSPTSSVASFSTSPAKVPDTEPIDVAAHLQLLGESLSLIGHRLQETEGMVAVSGSLSVLLDSILCALGPLVCLTSHVPQLNACPKQILSNTLDNIAYVMPGL
Protein: Stevor (Q8I215)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKMYYLKMLLFNYLINTLVLPHYENYLYNPYNVSLNPNNTQRTTIKSRLLAQTQIHNPHYHNDPELKEIIDKMNEEAIKKYQKTHDPYEQLKDVVEKNGTKYTGGNDAKPMSTLEKELLETYEEMFGNESDMLKSGMSPNVDEKSSTCECTDLNGVKLAKTKGRDKYLKHLKHRCIGGICSCTVGSAILTMIGLAATKATIIKFLTVPPLSYNASTSPVTIYNMFVGITAWGPDAVGSIPTYSIVALQPWGIAALVLLILAVALIILYIWLYKRRKNSWKHECKKHLCK
Protein: Ribonuclease ageritin (EC 4.6.1.23) (Ribotoxin) (C0HLG3)
Organism: Cyclocybe aegerita (Black poplar mushroom) (Agrocybe aegerita)
Function: Fungal ribonuclease involved in fungal defense. Highly specific and highly toxic fungal endonuclease that cleaves a single phosphodiester bond in the 28S RNA of eukaryotic ribosomes at a universally conserved GAGA tetraloop of the sarcin-ricin loop (SRL). The damage of the SRL inhibits the binding of translation elongation factors and halts protein biosynthesis, ultimately resulting in the death of the target cells. Shows antitumor activity. Exerts cytotoxicity and induces apoptosis towards rat glial cells and human glioma cells, and also displays some activity towards human neurolastoma cell lines. Shows a strong entomotoxicity against Aedes aegypti larvae, yet no nematotoxicity against nematodes.
Subcellular location: Vacuole lumen {ECO:0000269|PubMed:32998313}. Note=Possibly sequestered into the vacuole to avoid its toxic activity on ribosomes. {ECO:0000305|PubMed:32998313}.
Interaction partners:
Sequence:
MSESSTFTTAVVPEGEGVAPMAETVQYYNSYSDASIASCAFVDSGKDKIDKTKLVTYTSRLAASPAYQKVVGVGLKTAAGSIVPYVRLDMDNTGKGIHFNATKLSDSSAKLAAVLKTTVSMTEAQRTQLYMEYIKGIENRSAQFIWDWWRTGKAPA
Protein: NADPH--hemoprotein reductase (EC 1.6.2.4) (Q384R3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Anamorsin homolog
- Homocysteine S-methyltransferase, putative
- Cytochrome b5, putative
- Cytochrome b5, putative
Sequence:
MIFLVISTAIIAVLAWFVAGVFIRGGGGRGKTAAPQVVGVAQYPSQPSSRVDVRVLFGSQTGTAEMFAKTVTREGLRLGVPMKLADVENYRPSDLAGEKYVIIICATYGEGEPTDTMVGFHEWLVDDSRAVGEELSGVKYTVFALGDRQYKFFCREGITVDRRMSELGAQRFYPLGYGDCGNSIEEEFDNWCHNLWPVLGRALSLVLKSNSTEPVAPECRMKLWGPPEEAPLPFPKLASVLEPTQRLPSWAPVKVNKELLSNATGRSTRLIEFDTSETVISYQAGDHLGVLPSNPSEMVNTYLRVLGVSEQESSQVISLQNRATGKNVFPCRVSIRTALTWYIDLAGPPKKSTLRAFAHHCTDPVEKDTLLKLLSTEPESVEAYGKLVLELRTVLGFLQRFKSMSPPLSFFLEMMPRIAPRYFSISSDSLTHPTSVAITVAVVEGGLCTNLLQQAAVGQNIPVFVRKSNFHLPLRAKDRPIIMIGPGTGVAPFIGFLHRRSAWLEKGNKVGDALLFFGCRRREEDHIYADFMEKCLSNGALSVRDVAYSREQADKVYVQHRLAARGKEVWEIISRGGNVYVCGDAKNMARDVERQLLDIAQKYGAMKEDEATALLEKLATDERYLKDVWTA
Protein: Serine/threonine-protein kinase STE11 (EC 2.7.11.25) (P23561)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it phosphorylates the STE7 protein kinase which itself, phosphorylates the FUS3 and or KSS1 kinases.
Interaction partners:
- High osmolarity signaling protein SHO1
- Protein STE50
- MAP kinase kinase PBS2
- Protein STE5
- Serine/threonine-protein kinase STE7
- Serine/threonine-protein kinase STE20
- Guanine nucleotide-binding protein subunit beta
- Mitogen-activated protein kinase FUS3
- Protein STE12
- Cell division control protein 24
Sequence:
MEQTQTAEGTDLLIGDEKTNDLPFVQLFLEEIGCTQYLDSFIQCNLVTEEEIKYLDKDILIALGVNKIGDRLKILRKSKSFQRDKRIEQVNRLKNLMEKVSSLSTATLSMNSELIPEKHCVIFILNDGSAKKVNVNGCFNADSIKKRLIRRLPHELLATNSNGEVTKMVQDYDVFVLDYTKNVLHLLYDVELVTICHANDRVEKNRLIFVSKDQTPSDKAISTSKKLYLRTLSALSQVGPSSSNLLAQNKGISHNNAEGKLRIDNTEKDRIRQIFNQRPPSEFISTNLAGYFPHTDMKRLQKTMRESFRHSARLSIAQRRPLSAESNNIGDILLKHSNAVDMALLQGLDQTRLSSKLDTTKIPKLAHKRPEDNDAISNQLELLSVESGEEEDHDFFGEDSDIVSLPTKIATPKNWLKGACIGSGSFGSVYLGMNAHTGELMAVKQVEIKNNNIGVPTDNNKQANSDENNEQEEQQEKIEDVGAVSHPKTNQNIHRKMVDALQHEMNLLKELHHENIVTYYGASQEGGNLNIFLEYVPGGSVSSMLNNYGPFEESLITNFTRQILIGVAYLHKKNIIHRDIKGANILIDIKGCVKITDFGISKKLSPLNKKQNKRASLQGSVFWMSPEVVKQTATTAKADIWSTGCVVIEMFTGKHPFPDFSQMQAIFKIGTNTTPEIPSWATSEGKNFLRKAFELDYQYRPSALELLQHPWLDAHII
Protein: Seripauperin-8 (P0CE92)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MVKLTSIAAGVAAIAATASATTTLAQSDERVNLVELGVYVSDIRAHLAQYYMFQAAHPTETYPVEVAEAVFNYGDFTTMLTGIAPDQVTRMITGVPWYSSRLKPAISSALSKDGIYTIAN
Protein: RE40017p (Q8IGR6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYDLDMETSFNSLWETCILRQSTGANDIDESELNQEYLKEGSVFVHNTDVDGKPLLVFRVKMHSKSKNLDELIRIVVYWVERTQREQHLTQLTIFFDMSGTSLASMDLEFVKRIVETFKQFYPNSLNYILVYELGWVLNAAFKVIKAVLPPKAVEILKMISKKDINQYINKDNCLAIWGGEDNYEFSFVPEAKKVISKPVAANAGDDDQFADKKVTFVDSAPMVLKETNINKMHTPSEGMLHINPKDFVNFNSKNAEATMTIKSIATSAVTYKIQTTSPEKFRVRPRCGIIQPNQEATINIWLKSEHKLSDDSKDKFLVMAMVAPGGECGGADVTELWRSKSPTSADVEQHRLVCRFDENKSKAQLDCASKSSKASVDCSKKSGAGVDPATAMERQLAFTQNLQYVTLALLFLLFAGFGFLMYQQLGQHAATCPKATAYSCAKRK
Protein: Mitogen-activated protein kinase kinase kinase 13 (EC 2.7.11.25) (Leucine zipper-bearing kinase) (Mixed lineage kinase) (MLK) (O43283)
Organism: Homo sapiens (Human)
Function: Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibitors of NF-kappa-B.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9353328}. Membrane {ECO:0000269|PubMed:9353328}; Peripheral membrane protein {ECO:0000269|PubMed:9353328}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 7
- C-Jun-amino-terminal kinase-interacting protein 1
- C-Jun-amino-terminal kinase-interacting protein 2
Sequence:
MANFQEHLSCSSSPHLPFSESKTFNGLQDELTAMGNHPSPKLLEDQQEKGMVRTELIESVHSPVTTTVLTSVSEDSRDQFENSVLQLREHDESETAVSQGNSNTVDGESTSGTEDIKIQFSRSGSGSGGFLEGLFGCLRPVWNIIGKAYSTDYKLQQQDTWEVPFEEISELQWLGSGAQGAVFLGKFRAEEVAIKKVREQNETDIKHLRKLKHPNIIAFKGVCTQAPCYCIIMEYCAHGQLYEVLRAGRKITPRLLVDWSTGIASGMNYLHLHKIIHRDLKSPNVLVTHTDAVKISDFGTSKELSDKSTKMSFAGTVAWMAPEVIRNEPVSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLHLPVPSTCPDGFKILMKQTWQSKPRNRPSFRQTLMHLDIASADVLATPQETYFKSQAEWREEVKKHFEKIKSEGTCIHRLDEELIRRRREELRHALDIREHYERKLERANNLYMELSAIMLQLEMREKELIKREQAVEKKYPGTYKRHPVRPIIHPNAMEKLMKRKGVPHKSGMQTKRPDLLRSEGIPTTEVAPTASPLSGSPKMSTSSSKSRYRSKPRHRRGNSRGSHSDFAAILKNQPAQENSPHPTYLHQAQSQYPSLHHHNSLQQQYQQPPPAMSQSHHPRLNMHGQDIATCANNLRYFGPAAALRSPLSNHAQRQLPGSSPDLISTAMAADCWRSSEPDKGQAGPWGCCQADAYDPCLQCRPEQYGSLDIPSAEPVGRSPDLSKSPAHNPLLENAQSSEKTEENEFSGCRSESSLGTSHLGTPPALPRKTRPLQKSGDDSSEEEEGEVDSEVEFPRRQRPHRCISSCQSYSTFSSENFSVSDGEEGNTSDHSNSPDELADKLEDRLAEKLDDLLSQTPEIPIDISSHSDGLSDKECAVRRVKTQMSLGKLCVEERGYENPMQFEESDCDSSDGECSDATVRTNKHYSSATW
Protein: SD26770p (Q86PC5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSSSAITGSDQVIGSVSSTTIGDKSSNISSCDSGHDGLFHSVSMSAPWSHPRDTLTDSLYCDIPSSADESDAVSILNTHLKITEPFDCQTAPVYAKDIPKKGNLDSVVNLLINNNTKDLRFAFLTTSRLFSPPHQLLSKIIAKIDNEEENVLRLLNEWLDTCPGDFSHELLLQELENKRNVKGLAAFLDGIPQALAQKDENGRSQLNNLLTKQSSASSLGRQSSIKSLKRFAANVYKTDNVLNNCSSAFELAHQLYAIEYAYLSQIRLEEFVEILEKDELKTCISQTKAGTLGSNCISQVTIDSYVQWFNQLSYLTATEILKLGKKSQRAQMIDFWVETALECFNTGNFNSLMAILTALNLTAIARLKKTWAKVQTTKFEGLEHQMDPSSNFLNYRSTMKAAVWRSEREMANEIERAIIPFFSLFLKDLHAINESHETKLANGYINFEKCLHLGTQLRNFGKWQRLDCPYEQLPSVVSYLLKAEVLSEDLLMKASYESEPPETGEEKDHYKTLKAARKSNT