wanglab/gogpt-training-data huggingface dataset:
Protein: RAD50 DNA repair-like protein (Q384J8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Endo/exonuclease Mre11
- Protein artemis
- non-specific serine/threonine protein kinase
- BRCT domain-containing protein
- Recombination initiation protein NBS1, putative
- BRCT domain-containing protein
- Flap endonuclease 1
- KU70 protein
- DNA polymerase
- Replication protein A subunit
Sequence:
MTSIEQIEISGVRSFDPNPNNRQRIVFKKPLTVILGKNGAGKTTIIEALLNACTGQMPPGGGTEKSSFVYDPKVVGENDVKAQIRLLFTGRGGKVMQVIRSFQATRTRNKTTFATLDNIVAFQDSATGKIISSTYRANDVDRAIPDMLGVSPAVLEHVIFCHQEDGNWPLSPPKEVKKIFDDIFAATRYVLALDRLRENNKELRRQQKEHEASLMSLSEHREQARQISADITVKEETVAGIKAKTDALAPQLQELQAIATALDNVEHRAEGLSREAAVIEGRIGEKRESLSRLNVSPPGYSLGELLQRRQNFGEKLRELESTVSTKKELMERAVAELRRCEESVVSLRSGIEFREKQEQQHKRECEELKVIMSDLSMKFVIDGEINEHCLTKITEYVNEELHNEEQKRSGELNSIDAGIRAVEDRRSTTLRAMDTEGKEKEMKEEQLRHLMKRCGDAKEALGKLAPYVTPTRLKNVQDTITELEKRVEAMELLQKGDARYRQRQDILQSVEAQNKVVAQLRQELSRHKQRSGREAEMNLLRTQIAEKEEIINNRLQEELIAGLNDLGCNTGGSQTLTTVTMQIDKLRRKMADTLYSVEAEANDLDRQLIALKQNRSQLEGKIVSENIELQRKRVQCISKLGNDDALTNFEALLVEARDRYHKLNEKLSGSKALAACHAHFVEQAKVEDKCPLCGRAFGSENELNDFLASFKVGQQTSGKDSIKEGDVEKALQRVRGLEQLESDVMDVRRLADNAPQLEESLKSTIKQIRDKEILLEDVHNKRDKVKDEMQRAQKLVQAAMEVNAMTSEKQALLQQLNRREAACAEASTSSANIGGAGEPCCAGELASLSYEELSDKYESANAELHRLNVLLSEMQRGEEGGSAQALVKELTMKRSELCELKMKLTRQAEVEATIAQYAEQEEGYVSRIAEIDDQREKLVAQLESYNKELEALHAKRKELELASQQGYIGQLKRTLGLLSAVLPRLRDYITSRVGEELSRDRESLCVNEKRRDTQAEEVKLLRLSIDDTLRIINEEQRLRVEVDKYIEYLEKKGSIEEDEKRLSDVRCTLSELKVNAVPAAEAVLGKDVVERESVGRIRELIRGKISALECLRAQQDGVAEAMRQDIESLKGQLTRDKYKDIEKRYRTTFLKVQTTEIAVSDVEKYYRALEKAVQTYHQEKIAQINQILADLWRHTYKGSDIDTIELRSEDDVTSTTARRSYSYRVVMKRGNSEMDMRGRCSAGQKVLASVLIRLALSEAFCCDCGILALDEPTTNLDEDNARSLAESLRMLIDSHRAVKHFQLIVITHDEHFVRALGGQALDTFYYIHKDREGAFSVIEERTFDQLFAS
Protein: Exosome complex exonuclease RRP41A (Q38AL8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNasePH-like protein exosome-associated protein 1 Rrp42 homologue
- Exosome complex exonuclease RRP40
- Ribosomal RNA processing protein 4
- Exosome component CSL4
- Ribosomal RNA processing protein 45
- Ribosomal RNA-processing protein 43
- Ribosomal RNA processing protein 6
- ATP-dependent DEAD/H RNA helicase, putative
- Ribosomal RNA-processing protein 44
- Mitochondrial exoribonuclease DSS-1
Sequence:
MPVIKEYINPAGLRLDGRRPNEPRRLALEFGKISGCDGCCTVVSGLSHVCATVYGPREVSNRLEGKYNEVTITCDVVVAAFAGERRREQQRYSRLSEDISASVLDVARSVVLLSQYPNSQIHICIEVLKQDGSDKAACINAACLALIDASIAMKDVVYTQTVGLIEGFDVVDLTTEEIHSQCPSICITVQGHDPTNIVWMESNSRLAPEVITRLVKVAQKASTDVFETALRGPLEEHAATVLRLQANLGNIE
Protein: COUP transcription factor 1 (COUP-TF1) (COUP transcription factor I) (COUP-TF I) (Nuclear receptor subfamily 2 group F member 1) (V-erbA-related protein 3) (EAR-3) (Q60632)
Organism: Mus musculus (Mouse)
Function: Coup (chicken ovalbumin upstream promoter) transcription factor binds to the ovalbumin promoter and, in conjunction with another protein (S300-II) stimulates initiation of transcription. Binds to both direct repeats and palindromes of the 5'-AGGTCA-3' motif. Represses transcriptional activity of LHCG (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- B-cell lymphoma/leukemia 11B
- Nuclear receptor corepressor 1
- Nuclear receptor corepressor 2
Sequence:
MAMVVSSWRDPQDDVAGGNPGGPNPAAQAARGGGGGAGEQQQAGSGAPHTPQTPGQPGAPATPGTQGDKGQGPPGSGQSQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPNPGQYALTNGDPLNGHCYLSGYISLLLRAEPYPTSRYGSQCMQPNNIMGIENICELAARLLFSAVEWARNIPFFPDLQITDQVSLLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDAAHIESLQEKSQCALEEYVRSQYPNQPSRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMSIQCS
Protein: Protein arginine N-methyltransferase 1 (EC 2.1.1.319) (Q9U2X0)
Organism: Caenorhabditis elegans
Function: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in target proteins. Catalyzes the formation of monomethylarginine and asymmetric dimethylarginine on histones H2A and H4, a specific tag for epigenetic transcriptional activation. Catalyzes asymmetric arginine dimethylation of mitochondrial proteins necessary for mitochondrial oxidative phosphorylation activity and thus aerobic respiration and ATP synthesis, and the mitochondrial stress response. Methylates arginine residues in P-granule components pgl-1 and pgl-3 to promote P-granule degradation by autophagy in somatic cells to ensure exclusive localization of the P-granules in germ cells. Modulates the interaction of P-granule proteins epg-2 and sepa-1. Methylates arginine residues in daf-16, which blocks ftt-2 binding to daf-16, prevents akt-mediated phosphorylation and allows for daf-16 to translocate to the nucleus. In turn, association with daf-16 therefore allows for the transcriptional activation of daf-16 and regulation of longevity-related genes. Maintains lifespan by modulating daf-16 activity downstream of the daf-2 signaling pathway. Plays a role in heat and oxidative stress resistance. Role in stress resistance and also fat storage may be in association with the daf-2 signaling pathway. Required for normal feeding behavior.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24140420}. Nucleus {ECO:0000250|UniProtKB:Q99873}. Note=Diffuse cytoplasmic localization during embryogenesis. {ECO:0000269|PubMed:24140420}.
Interaction partners:
- Forkhead box protein O
- Protein arginine N-methyltransferase 5
- Histone H4
- Small ribosomal subunit protein uS5
- Ribosome biogenesis protein NSA2 homolog
- RNA helicase
- Runt-related transcription factor rnt-1
- Core-binding factor subunit beta homolog bro-1 homolog)
- rRNA 2'-O-methyltransferase fibrillarin
- Putative H/ACA ribonucleoprotein complex subunit 2-like protein
Sequence:
MSTENGKSADAPVAAPAAKELTSKDYYFDSYAHFGIHEEMLKDEVRTTTYRNSIYHNSHLFKDKVVMDVGSGTGILSMFAAKAGAKKVFAMEFSNMALTSRKIIADNNLDHIVEVIQAKVEDVHELPGGIEKVDIIISEWMGYCLFYESMLNTVLVARDRWLAPNGMLFPDKARLYVCAIEDRQYKEDKIHWWDSVYGFNMSAIKNVAIKEPLVDIVDNAQVNTNNCLLKDVDLYTVKIEDLTFKSDFKLRCTRSDYIQAFVTFFTVEFSKCHKKTGFSTGPDVQYTHWKQTVFYLKDALTVKKGEEITGSFEMAPNKNNERDLDINISFDFKGEVCDLNEQNTYTMH
Protein: chitinase (EC 3.2.1.14) (C8VAA5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
- N-acetylglucosaminylphosphatidylinositol deacetylase
- PIG-P domain-containing protein
- CDP-diacylglycerol-inositol 3-phosphatidyltransferase PIS
Sequence:
MILKHAALALAALQCVAGLRFAMYIDEWHVNGLPGSDQTQGITHAIMGFAKSTDFTGDAPAAFQPFEPVSTFRNRFSPDTKVMIAIGGWGDSAGFSAGAKDEASRERYAKNVAAMLESTGFDGVDIDWEYPGGNGEDYKKVPNDQKVDEIETFPLLLQALRTAVGDKKIISIATPGKREDMIAYTTEQGPKIWPSVDMINIMSYDLMNRRNNETKHHTGIADSHDTIKAYLEIGAPPEKINLGFAYYAKWFTTQSDVDCGTYPIGCPTVAMEAADGSDNGKSGAMTFEPQNMAAQPSDLKVSTDMTCGLAKGTRCPAGTCCSIYGNCGTGDDFCLAACDSNFGECKGVPIQDSWRRARAEGQTDEEGGGQYYMDTQNHLFWTWDTPTLMTRKFTEIVDVEKLGGVMAWSLGEDTYNFEHLKAMQEGVAQRAGGTATPARTRCSGGSQSACSKRHGAVGVSLSRQQRPAKPHAGNSRSFLIVYKSTSVQFSAAVGFNSMKCFIVLTFVPLVLALTIPNTNKNHDASSVEFIQQHQQRLFGTKTTVAEYKRPSLKINHGTIIPANKERTQATATTSNPSYIHALRIEQAPYHLIARYSNALFALGLLLLVPLTLGIIELAGRLFRCVSVDECPERGREKQGTESHQEIEEWAFRQRERDNKKRPATVAVEMIDTMKIGS
Protein: Vacuolar ATPase assembly protein VMA22 (P38784)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for V-ATPase activity.
Interaction partners:
- Vacuolar ATPase assembly integral membrane protein VPH2
- V-type proton ATPase subunit a, vacuolar isoform
- V-type proton ATPase subunit d
- V-type proton ATPase subunit F
- V0 assembly protein 1
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit c''
- V-type proton ATPase subunit c
- V-type proton ATPase subunit e
- V-type proton ATPase subunit a, Golgi isoform
Sequence:
MSETRMAQNMDTTDEQYLRLIELLSNYDSTLEQLQKGFQDGYIQLSRSNYYNKDSLRGNYGEDYWDETYIGQLMATVEEKNSKVVVEIVKRKAQDKQEKKEEEDNKLTQRKKGTKPEKQKTQSHKLKQDYDPILMFGGVLSVPSSLRQSQTSFKGCIPLIAQLINYKNEILTLVETLSEQE
Protein: Pep3/Vps18/deep orange beta-propeller domain-containing protein (G5EAW8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}.
Interaction partners:
- Vacuolar assembly protein, putative
- Probable vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting protein
- Golgi complex component
- AvaB protein
- Vacuolar sorting protein
- TGF beta receptor associated protein 1, putative
- Vesicle transport v-SNARE protein vti1
- CCZ1/INTU/HSP4 first Longin domain-containing protein
- Ypt/Rab-type GTPase avaA
Sequence:
MALDTSSGYAAHSSLIEPDPLPMFDVRHVQLQFPLAADFVAAQVADNVLILALSTGRILRIDLNNPEHIDDVDLPKKSSETGVIRRMFLDPSASHLIITTTLGENYYLHTQSRHPKPLSRLKGLLIESVAWSPSLPTASTREILLGTTDGQVWETYIEPSTEFYRREERYASSIYRTSDGSPVTGIWAETVPTKAEQRRILVATHGKLSCFLGRTGRSGKEGAGPIYADLLSRETPVIHEIGQPSSSAPSNLVVSPSSSDAHHLDGHRDKEFAWLSSEGVYHGQLPYSLDMLHKPFESSSMLPRSIFPATESARGGKKLIQNPLTAMTLSEWHILVLVEGRVLAVNRMNDEIVFDQEVLEPGQAALGLVTDAMKGTYWLFTSQDIFEICVQDEDRDVWKIFLRKQKFEEALRYARTSSQKDAVSTASGDFLASKGRYIEAAGVWGKSSKAFEDVCLTLIKRGQHDALRKYLLSQLSVYKKSSSMQRTMVASWLIEVFMTKLNSLDDNITTKAELAEGSSTEEIEHELQAVRNEFQEFVTKYKSDLDQKTAYDIISSHGREKELLFFATVVNDHNYVLSYWIQRENWSEALNVLQRQSDPEVFYKHSSVLMTHAATGLVNILMRQTNLEPEKLIPALLNYNSTVSVPLSQNQAVRYLNFIIVNHPRPTAAVHNTLISIHASSRSSSEAGLLTYLQSQPSSPPPYDADFALRLCIQHQRFQSCIHIYSAMGQYLQAVELALQHDDIELAAIIADRPEGNNKLRKKLWLLVAEKKIRQSDTGIKDAIEFLRRCELLRIEDLIPFFPDFVVIDDFKDEICSALEDYSRHIDALRQEMDSSAQTARQIRSEIAALDTRYAIVEPGEKCWTCSLPVLSRQFFVFPCQHAFHSDCLGREVLEGAGGKKKYIRDLQSQLNEGALTSSQREEVVKELDGLIAEACILCGDHAIKQIDKPFITATDNVDEWCL
Protein: Uncharacterized fimbrial-like protein YcbV (P75860)
Organism: Escherichia coli (strain K12)
Function: Part of the elfADCG-ycbUVF fimbrial operon, which promotes adhesion of bacteria to different abiotic surfaces.
Interaction partners:
- Toxin-antitoxin biofilm protein TabA
- Uncharacterized fimbrial chaperone YcbF
- Uncharacterized fimbrial-like protein ElfG
- Uncharacterized fimbrial-like protein YcbU
- Probable outer membrane usher protein ElfC
- Uncharacterized fimbrial-like protein SfmF
- Probable fimbrial chaperone protein ElfD
Sequence:
MLKRIIWILFLLGLTWGCELFAHDGTVNISGSFRRNTCVLAQDSKQINVQLGDVSLTRFSHGNYGPEKSFIINLQDCGTDVSTVDVTFSGTPDGVQSEMLSIESGTDAASGLAIAILDDAKILIPLNQASKDYSLHSGKVPLTFYAQLRPVNSDVQSGKVNASATFVLHYD
Protein: Euchromatic histone lysine methyltransferase 1 (A0A1B0GU48)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESSKAKEVTIAKADTTSTVTPVPGQEKGSALEGRADTTTGSAAGPPLSEDDKLQGAASHVPEGFDPTGPAGLGRPTPGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDRPSPVERIVSRDIARGYE
Protein: Tumor necrosis factor alpha-induced protein 8-like protein 1 (TIPE1) (TNF alpha-induced protein 8-like protein 1) (TNFAIP8-like protein 1) (Oxidative stress-regulated gene-beta) (Oxy-beta) (Q8WVP5)
Organism: Homo sapiens (Human)
Function: Acts as a negative regulator of mTOR activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8K288}.
Interaction partners:
- F-box/WD repeat-containing protein 5
Sequence:
MDTFSTKSLALQAQKKLLSKMASKAVVAVLVDDTSSEVLDELYRATREFTRSRKEAQKMLKNLVKVALKLGLLLRGDQLGGEELALLRRFRHRARCLAMTAVSFHQVDFTFDRRVLAAGLLECRDLLHQAVGPHLTAKSHGRINHVFGHLADCDFLAALYGPAEPYRSHLRRICEGLGRMLDEGSL
Protein: PTB-containing, cubilin and LRP1-interacting protein (P-CLI1) (Phosphotyrosine interaction domain-containing protein 1) (Protein NYGGF4) (Q7Z2X4)
Organism: Homo sapiens (Human)
Function: Increases proliferation of preadipocytes without affecting adipocytic differentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16815647}.
Interaction partners:
Sequence:
MFSLPLSLPLCEDTAFLPSKCCSSHKTIKQARTLIMIFLASGTHFQTMLKSKLNVLTLKKEPLPAVIFHEPEAIELCTTTPLMKTRTHSGCKVTYLGKVSTTGMQFLSGCTEKPVIELWKKHTLAREDVFPANALLEIRPFQVWLHHLDHKGEATVHMDTFQVARIAYCTADHNVSPNIFAWVYREINDDLSYQMDCHAVECESKLEAKKLAHAMMEAFRKTFHSMKSDGRIHSNSSSEEVSQELESDDG
Protein: Uncharacterized protein, isoform B (A0A0B4KHV9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLDMTVIYDQEAALSYYDCYEICTKEDLRQNPKNEPRTLCKRCAVELKWAYDFHKKMAIANQQLREIFVATEANTEQEDDVEDEENEADMNEEFLMEEIEEKQETPIDSLEDIVPRNRHTGKSNCKFCHKEFRNHSRMAKHQMIHLANRPNFRCSQCDRVYLTKQALKVHVDSKHRQSGVHCDTCGKVFAIAKALEIHKRYHNRDFPYSCDLCDRRFAQRSHLTVHQQVKHSGSRFICEFPGCQKSFTSSSSLRNHECTHTAMPFECAHCHQSYPARNKLRMHLERKHNMVVQMEDLEEMRKFHIVRSKLVMAKIYSDQKESHHAKNDSAAISK
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FJQ4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- P-type Na
Sequence:
MAVWEQLEVSKAHVAYACVGVFSSIFSLVSLFVKEKLYIGESTVAGIFGLIVGPVCLDWFNPLEWGNSDVITLEITRIVLCLQIFAVAVELPRKYMKKHWLSVTMLLVPVMTAGWLIIGLFVWIIIPHINFPAALLVSACITATDPILAQSVVSGKFAKKVPGHLRNLLSAESGCNDGMAFPFIYLSLNLVLHPGRGGLIVKDWICITILYECLFGCILGVVIGYVGRISIRFAEEKNIIDRESFLAFYVVLAFICAGFGSLLGVDDLLVSFAAGAAFAWDGWFSQKTEESNVSTVIDVLLNYAYFIYFGAIIPWDQFNNGDIGLNVWRLIVLAIIVIFLRRIPAVMILKPVIPDIKSWREALFVGHFGPIGVGAIFAAILARGELEHEFLEEPTPLNVVPPEVETEHWQLIAILWPTICFFIITSIIVHGSSVAVITLGRHLNTVTLTKTFTTHTTNGNGKSSWMQRLPSLDKSGRSFSLHRVDTSATNETIHHETEPDELKQNDTMEDYSGVTTSGKPVRAAGGMRRRVTRKKKKSRGRKHAERLMRKTEKLNPMFGGYDDELNDLGREKLQLEKEAEAGTFALGRKNWPNADNDDDADGSPHTVIGTSISGSDQYDEEKVDSRHSLESTQSEKERKLAELKEQEETPHVAYAEGNKIIFENKQGEIIDEAKLNSPSDEEAQQSFRSPSSLKKTRSNDSTSRSMTSMNSLKRIITPPSVKKVHSLIDRSHPKYIAYKIDNQLIIEDDEGEVLRRYKINTHDKEESKTSPKVQTRNERSSSIVSRALSAVGLRNGSKTTLASDEVTGVAEGERQFVLTPVPTHMYDQNENQINEEDEEGTSYSGSENDNEEENSQSDDSYEYDSNQLSGEESNERSEDEESEDYDEDSDNYSETQIERDRRLNALGHISLPAEADDEEPAPYIPQLDQNNSRNKMKSTFARFKK
Protein: Beta-catenin-interacting protein 1 (Inhibitor of beta-catenin and Tcf-4) (Q9NSA3)
Organism: Homo sapiens (Human)
Function: Prevents the interaction between CTNNB1 and TCF family members, and acts as negative regulator of the Wnt signaling pathway.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Catenin beta-1
- Adenomatous polyposis coli protein
- Axin-1
- Glycogen synthase kinase-3 beta
- Casein kinase I isoform alpha
- Calcyclin-binding protein
- Glycogen synthase kinase-3 alpha
- E3 ubiquitin-protein ligase SIAH1
Sequence:
MNREGAPGKSPEEMYIQQKVRVLLMLRKMGSNLTASEEEFLRTYAGVVNSQLSQLPPHSIDQGAEDVVMAFSRSETEDRRQ
Protein: ATP-dependent DNA helicase (EC 5.6.2.4) (Q19046)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU364117}.
Interaction partners:
- Crossover junction endonuclease MUS81
- Regulator of telomere elongation helicase 1 homolog
- Exosome complex component 10 homolog
- DNA topoisomerase 3
- DNA repair protein RAD51 homolog
- Protein hsr-9
- DNA replication ATP-dependent helicase/nuclease DNA2
- Ku domain-containing protein
- Double-strand break repair protein mre-11
- Serine/threonine-protein kinase ATR
Sequence:
MTEIQFSEMSSGKRSLETITIDDSDEETDKEPAAKKPSNYTAWAEIFNKKKTESSAVSAIEKAKKDSEKERQRQKLREAIMERKRREALMNEPKKQKIEPVSTVKLEKSVNQKISANSEDFDVSGPSNSRETQESPLDPNDFVANPLAIGTGERLIRGQDIIERRDKVFLELFCHKKYRSRLQMQAINCILKRKCDVYVSLPTGAGKSLCYQLPAVVHGGITVVISPLIALMKDQISSLKRKGIPCETLNSTLTTVERSRIMGELAKEKPTIRMLYLTAEGVATDGTKKLLNGLANRDVLRYIVVDEAHCVTQWGHDFRPDYLTLGSLRDVCPGVPWVALTATANAKAQDDIAFQLKLRNPESFKSGTYRDNLFYDVAMRDHLATAPENHMASFITKCLTVDAKTSSSNLTKHEKAERSQNKKTFTGSAIVYCRSRNECGQVAKMLEIAGIPAMAYHAGLGKKDRNEVQEKWMNNEIPVVAATVAFGMGIDKPDVRAVIHWSPSQNLAGYYQEAGRAGRDGKRSYCRIYYSKQDKNALNFLVSGELAKLREKAKKNNAEGEKAEMQIKSIQTGLAKMLEYCESARCRHVSIASFFDDTECRPCKTNCDYCRDPTKTIRNVEAFINSEASTGRSMFRKSASSGESGFDSVYGGGKRGGETEDELLSAASTSKDAMDRMEQEEAKRVRSVISQEFAKRRQAAPPPRATARRVEPATDVNVIKPEQNVIKNVTLETRENWVRFLHRALDSNWIVSGPPAGVTTKQCAEQLEYGLYSISKNETTYKNKCGHKLAEIKKLTLKNAPFAYTNTEVEQNGFVKASNLS
Protein: 40S ribosomal protein S24 (B7ZD34)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- 40S ribosomal protein S12
- Large ribosomal subunit protein eL20
- Ribosomal protein L15
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein P1
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein uL5
Sequence:
MNDTVTVRTRKFMTNRLLQRKQMIVDVLHPGKATVPKTEIREKLAKMYKTTPDVVFVFGFKTQFGGGKTTGFGMIYDSLDYAKKNEPKYRLQRHGLYEKKKTSRKQRKERKNRMKKVRGIKKASVGASGKKK
Protein: Thymidine phosphorylase (EC 2.4.2.4) (TdRPase) (P07650)
Organism: Escherichia coli (strain K12)
Function: The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.
Interaction partners:
- Phosphopentomutase
- Deoxyribose-phosphate aldolase
- Purine nucleoside phosphorylase DeoD-type
- Uridine phosphorylase
- Cytidine deaminase
- Thymidine kinase
- Uracil phosphoribosyltransferase
- Pyrimidine/purine nucleoside phosphorylase
- Cytosine deaminase
- Pyrimidine 5'-nucleotidase YjjG
Sequence:
MFLAQEIIRKKRDGHALSDEEIRFFINGIRDNTISEGQIAALAMTIFFHDMTMPERVSLTMAMRDSGTVLDWKSLHLNGPIVDKHSTGGVGDVTSLMLGPMVAACGGYIPMISGRGLGHTGGTLDKLESIPGFDIFPDDNRFREIIKDVGVAIIGQTSSLAPADKRFYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGAFMPTYELSEALAEAIVGVANGAGVRTTALLTDMNQVLASSAGNAVEVREAVQFLTGEYRNPRLFDVTMALCVEMLISGKLAKDDAEARAKLQAVLDNGKAAEVFGRMVAAQKGPTDFVENYAKYLPTAMLTKAVYADTEGFVSEMDTRALGMAVVAMGGGRRQASDTIDYSVGFTDMARLGDQVDGQRPLAVIHAKDENNWQEAAKAVKAAIKLADKAPESTPTVYRRISE
Protein: Large ribosomal subunit protein uL6 (60S ribosomal protein L9) (Q54XI5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein eS24
Sequence:
MKVINSSRKVQIPENVTVDVKGRSVKVTGPRGTLSKSFDHASVDINLVGKKELTVDLWFGNRKQIACIKTITSIIENMITGVTKGYEYKMRFVYAHFPINVAVTDGGRVVEIRNFFGEKIVRRIELLDGITCYRNEKAKDEIVLTGNSLELLSQSCATIQLRSAIKYKDVRKFLDGIYVSERNVLESN
Protein: Toll-like receptor 11 (Toll-like receptor 12) (Q6R5P0)
Organism: Mus musculus (Mouse)
Function: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Profilin-4
- Profilin
- Profilin-3
- Profilin-2
- Profilin-1
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 12
- Toll/interleukin-1 receptor domain-containing adapter protein
- Toll-like receptor 3
- Toll-like receptor 5
Sequence:
MPRMERHQFCSVLLILILLTLVSLTLTGWAWTIPDCIIADSLLFPNLSYYIPFCTSAPGLHLLASCSNVKNLNQTLKRVPRNTEVLCLQGMVPTLPAKAFIRFHSLQLLRLQLRTTSVTSRTFQGLDQLQYLFFDHHAPCCLSLFLSPNCFESLRSLSSLSFQGYCLTYSQSIYLPTSLRHLTLRNSCLTKFQDLQRLFPDLLLSTSSTPNIKPGAPFLETLDLSYNLQLKQAGVRDLYGLTLHSLILDGTPLKALDLTDSGLLHLHFLSLVGTGIEKVPASLTGYSELRALDLGKNQIQNILENGEIPGYKALEFLSLHDNHLQTLPTRFLHTLPQLQKLNLSMNKLGPILELPEGLFSTNLKVLDLSYNQLCDVPHGALSLLSQLQELWLSGNNISSLSNESLQGLRQLRTLDLSWNQIKVLKPGWLSHLPALTTLNLLGTYLEYILGIQLQGPKMLRHLQLGSYPILDIYPPWPPTLLSLEIQAESCIQFMIHSGQPFLFLENLTLETSILLLKPDNITIHFPSLRRLTLRGYSFIFSTSQLQRFFPQQLPLLEHFFIWCENSYAVDLYLFGMPRLRVLELGYLNFFYESSTMKLEMLLKEVPQLQVLALSHLNLRNLSVSSFKSLQDLKLLLFNSERALEMNSNLQEFIPQMPQYVYFSDVTFTCQCEASWLESWATRAPNTFVYGLEKSICIANASDYSKTLLFSFLATNCPHGTEFWGFLTSFILLLLLIILPLISCPKWSWLHHLWTLFHTCWWKLCGHRLRGQFNYDVFISYCEEDQAWVLEELVPVLEKAPPEGEGLRLCLPARDFGIGNDRMESMIASMGKSRATLCVLTGQALASPWCNLELRLATYHLVARPGTTHLLLLFLEPLDRQRLHSYHRLSRWLQKEDYFDLSQGKVEWNSFCEQLKRRLSKAGQERD
Protein: Leucine-rich repeat-containing protein 25 (Monocyte and plasmacytoid-activated protein) (Q8N386)
Organism: Homo sapiens (Human)
Function: Plays a role in the inhibition of RLR-mediated type I interferon signaling pathway by targeting RIGI for autophagic degradation. Interacts specifically with ISG15-associated RIGI to promote interaction between RIGI and the autophagic cargo receptor p62/SQSTM1 to mediate RIGI degradation via selective autophagy. Also plays a role in the inhibition of NF-kappa-B signaling pathway and inflammatory response by promoting the degradation of p65/RELA.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:29044191}.
Interaction partners:
- Antiviral innate immune response receptor RIG-I
- NFAT activation molecule 1
Sequence:
MGGTLAWTLLLPLLLRESDSLEPSCTVSSADVDWNAEFSATCLNFSGLSLSLPHNQSLRASNVILLDLSGNGLRELPVTFFAHLQKLEVLNVLRNPLSRVDGALAARCDLDLQADCNCALESWHDIRRDNCSGQKPLLCWDTTSSQHNLSAFLEVSCAPGLASATIGAVVVSGCLLLGLAIAGPVLAWRLWRCRVARSRELNKPWAAQDGPKPGLGLQPRYGSRSAPKPQVAVPSCPSTPDYENMFVGQPAAEHQWDEQGAHPSEDNDFYINYKDIDLASQPVYCNLQSLGQAPMDEEEYVIPGH
Protein: Exosome complex component Rrp41 (EC 3.1.13.-) (O26779)
Organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Function: Catalytic component of the exosome, which is a complex involved in RNA degradation. Has 3'->5' exoribonuclease activity. Can also synthesize heteromeric RNA-tails.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00591}.
Interaction partners:
- Exosome complex component Rrp42
- Exosome complex component Csl4
- Exosome complex component Rrp4
- DNA primase DnaG
- Ribosome maturation protein SDO1 homolog
- RNA 3'-terminal phosphate cyclase
- Conserved protein
- Small ribosomal subunit protein uS4
- Pre-mRNA splicing protein PRP31
- Small ribosomal subunit protein uS11
Sequence:
MITIITQDQLKTSPSVREDGRAFDELRPLKIEAGILERADGSSYLEFGGNKILVAVYGPREAQIRKLQRPDRAVIRCRYNMAPFSVEERKRPGPDRRSVEISKITAEALRPALILEKFPRSVIDVFIEVLEAEGGTRCAGITAASVALADAGIPMRDMVVACAAGKVGDQVVLDLSEEEDKEGQADVPVAILPRTREITLLQSDGNLTPEEFERALDLAVEGCLRIHEVQKEALRKRYGE