wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear factor of activated T cells 3 (H3BR83)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XLDDRRPITLCVCVRARVCDLEPDDCASIYIFNVDPPPSTLTTPLCLPHHGLPSHSSVLSPSFQLQSHKNYEGTCEIPESKYSPLGGPKPFECPSIQITSISPNCHQELDAHEDDLQINDPEREFLERPSRDHLYLPLEPSYRESSLSPSPASSISSRSWFSDASSCESLSHIYDDVDSELNEAAARFTLGSPLTSPGGSPGGCPGEETWHQQYGLGHSLSPRQSPCHSPRSSVTDENWLSPRPASGPSSRPTSPCGKRRHSSAEVCYAGSLSPHHSPVPSPGHSPRGSVTEDTWLNASVHGGSGLGPAVFPFQYCVETDIPLKTRKTSEDQAAILPGKLELCSDDQGSLSPARETSIDDGLGSQYPLKKDSCGDQFLSVPSPFTWSKPKPGHTPIFRTSSLPPLDWPLPAHFGQCELKIEVQPKTHHRAHYETEGSRGAVKASTGGHPVVKLLGYNEKPINLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIIASTKVLEIPLLPENNMSASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGKVLSLQIASIPVECSQRSAQELPHIEKYSINSCSVNGGHEMVVTGSNFLPESKIIFLEKGQDGRPQWEVEGKIIREKCQGAHIVLEVPPYHNPAVTAAVQVHFYLCNGKRKKSQSQRFTYTPVLMKQEHREEIDLSSVPSLPVPHPAQTQRPSSDSGCSHDSVLSGQRSLICSIPQTYASMVTSSHLPQLQCRDESVSKEQHMIPSPIVHQPFQVTPTPPVGSSYQPMQTNVVYNGPTCLPINAASSQEFDSVLFQQDATLSGLVNLGCQPLSSIPFHSSNSGSTGHLLAHTPHSVHTLPHLQSMGYHCSNTGQRSLSSPVADQITGQPSSQLQPITYGPSHSGSATTASPAASHPLASSPLSGPPSPQLQPMPYQSPSSGTASSPSPATRMHSGQHSTQAQSTGQGGLSAPSSLICHSLCDPASFPPDGATVSIKPEPEDREPNFATIGLQDITLDDDQFISDLEHQPSGSAEKWPNHSVLSCPAPFWRI
Protein: Aminomethyltransferase, mitochondrial (A0A1B0GUU7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQYRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFTNEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALLALQGTVTSGCPSPSLKKNVAMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK
Protein: Cyclic beta (1,2) glucan succinyl transferase (Q6Q7W5)
Organism: Brucella abortus
Interaction partners:
Sequence:
MVPQGRDTRIDVFRALALLTIFINHVPGTIYEHFTHKNLGFSDSAEAFVLISGMAVALAYGSKFVSGNRLVLSLKMWRRASVLYITHIMTTMATIAIFAAAAIFLKRSELLTQINIAPLIKKPVEGLFGLVTLGHQLGYNNILSMYAVMLILTPILLFLARISLPLMLGVSGVVWFLSGLYHVAPVNYPTEGVWFINPLSWQFLFAIGIAGVMHVRGGGQLPKHPLLIGLAVGYLVLALAWVRIPLWSINISMGLPMVITGFDKTFLSAPRLLHVLAMAYLIAVVPTLNSIARTAPEHPLAVLGKHSLPVFVAGTLLAMVAQVMKLVNPGGLPYDTLLIATGIVMQFALAYYLEWLPTIGWGKKGAVQAKPAPAAEPVVIQVSANPEPAMQRY
Protein: C2 domain-containing protein (G5EDP5)
Organism: Caenorhabditis elegans
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 47
- C2 domain-containing protein
- Phospholipid scramblase
- Synaptosomal-associated protein
- Phorbol ester/diacylglycerol-binding protein unc-13
Sequence:
MWGDTEKPDPLLLGTHIGDGRHHPHHPHHHAHHAHFGLAGKPFYHVDRFTVTATSSSTTTTTTNSLSSNHHLPLHLHHHHHHNGMTTGTSSMGQIDGTGSTGSRAKNQQPIVMWKGETSRKKRFEPFCSPMVPHVPIRERLARRGTSADMSDDASAYTCYAPRRRRMSLLQSLRQQNRALADSGFDMHRQRTDSDSTNRDTCSPTQKISPPVTPTKKTTMASQIKNKIFGKKKDASASGNVYNNGEYSQSCDLINGRSRKSPSTTNDSGRGSQGHLEEKMEAMVIEEHLENDCGCEEEEEIDAPILSSKRSGINRHRTSSCPDITSLGLNHPTTSAASSGGKKCPIAVDTDTEEDNFERVKRPCSPISAADCLVERRLNRKFIEQRRQQVAMCHIDETCDVVSRISTTSRRTAQTEDLADFDDNASSIILDHFLSTTELNFDDSDSADFSLNGACEDEFDEPAPSSSNTATSVQTDLTLLNVEQEISEYLEHCRDASVNITEEGMNFIAKHFFEYQSFMNIPHKAVHLHKVPASQAGTDPSMGWAPKNMLKAGKHQPAPGARANRVHRDPRPNGTKYGRAGKHEHREWGDRHGELRDEKVACHKDAWTKFLANDDQGARTAFECDFEDRVLATEEETLQEKLCRTSPEAMNLNALYAAANKAVSCGGDVCELLTILTYAPTVQFVTTTVKKAKALPYNNAPFARIMLFEGRRLMEQKQTTVNPSLVHKSSVDGSKPSSSSASTSSNDNPSDVSFSESFLFHVPPTKLDRSHIVIELYDHDDEGGLQKIGHCVIGRLVDGTGNAHWIQMVRQHGLPVCMWHKIGHN
Protein: Antiviral helicase SKI2 (EC 3.6.4.13) (Superkiller protein 2) (P35207)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA helicase component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for cell growth only in the presence of M1 replicon.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10744028, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Antiviral protein SKI8
- Superkiller protein 3
- Superkiller protein 7
- 5'-3' exoribonuclease 1
- 5'-3' exoribonuclease 2
- Exosome complex component RRP45
- Exosome complex component CSL4
- Small ribosomal subunit protein RACK1
- Exosome complex component SKI6
- Small ribosomal subunit protein uS3
Sequence:
MSEGFSSSSIQELYQSLKEITNNADVELFEDRITKLDFESTDEPKHANDIIKDRFLRPSNALPWSLLDMVQDVPHTSSPEDCSGKLDYKELLKVPDPINRTSYQFKRTGLEGKISGYKEEVDLKEVANANASNSLSITRSINHNQNSVRGSTAQLPFTPGGIPMKSVKTDSEQNGSSTMANATKLLHKDGQGLFDIPEGMNRGIKPMDSPAENEDQNGQFKELKQLNEIDNELDIRIEANEAKLKEEEKSAKSISEEIMEEATEETTADNADDAEIDELLPIGIDFGRTKPVSKSVPVKKEWAHVVDLNHKIENFDELIPNPARSWPFELDTFQKEAVYHLEQGDSVFVAAHTSAGKTVVAEYAIAMAHRNMTKTIYTSPIKALSNQKFRDFKETFDDVNIGLITGDVQINPDANCLIMTTEILRSMLYRGADLIRDVEFVIFDEVHYVNDQDRGVVWEEVIIMLPQHVKFILLSATVPNTYEFANWIGRTKQKNIYVISTPKRPVPLEINIWAKKELIPVINQNSEFLEANFRKHKEILNGESAKGAPSKTDNGRGGSTARGGRGGSNTRDGRGGRGNSTRGGANRGGSRGAGAIGSNKRKFFTQDGPSKKTWPEIVNYLRKRELLPMVVFVFSKKRCEEYADWLEGINFCNNKEKSQIHMFIEKSITRLKKEDRDLPQILKTRSLLERGIAVHHGGLLPIVKELIEILFSKGFIKVLFATETFAMGLNLPTRTVIFSSIRKHDGNGLRELTPGEFTQMAGRAGRRGLDSTGTVIVMAYNSPLSIATFKEVTMGVPTRLQSQFRLTYNMILNLLRIEALRVEEMIKYSFSENAKETLQPEHEKQIKVLQEELQTIEYKSCEICDNDIEKFLELMLAYKEATVNLMQEMVKSPSILHILKEGRLVAFRDPNDCLKLGFVFKVSLKDAVCVIMTFTKPYKLPNGEPNHLIYFPKADGYRRRNFPKFQKTDFYMEEVPVTAIEVITKRKFAAPLGKVIKKDVAALNEFNAETNNILDGKTLKEAINIEKQGLKIHQILLDRTNIRDEIFKLKSIKCPNLSQHIVPKFKAHVIKKKIEELYHLMSDQNLSLLPDYEKRLAVLKDTEFIDQNHNVLLKGRVACEINSGYELVLTELILDNFLGSFEPEEIVALLSVFVYEGKTREEEPPIVTPRLAKGKQRIEEIYKKMLCVFNTHQIPLTQDEAEFLDRKRFAMMNVVYEWARGLSFKEIMEMSPEAEGTVVRVITWLDEICREVKTASIIIGNSTLHMKMSRAQELIKRDIVFAASLYL
Protein: T-complex protein 1 subunit zeta 1 (TCP-1-zeta 1) (CCT-zeta 1) (Chaperonin CCT6A) (Q9M888)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit epsilon
- TCP-1/cpn60 chaperonin family protein
- T-complex protein 1 subunit theta
- ATP binding protein
- Nucleic acid-binding/zinc ion-binding protein
Sequence:
MSVRVLNPNAEVLNKSAALHMTINAAKGLQDVLKSNLGPKGTIKMLVGGSGDIKLTKDGNTLLKEMQIQNPTAIMIARTAVAQDDISGDGTTSTVIFIGELMKQSERCIDEGMHPRVLVDGFEIAKRATLQFLDTFKTPVVMGDEPDKEILKMVARTTLRTKLYEGLADQLTDIVVNSVLCIRKPQEPIDLFMVEIMHMRHKFDVDTRLVEGLVLDHGSRHPDMKRRAENCHILTCNVSLEYEKSEINAGFFYSNAEQREAMVTAERRSVDERVQKIIELKNKVCAGNDNSFVILNQKGIDPPSLDLLAREGIIALRRAKRRNMERLVLACGGEAVNSVDDLTPDCLGWAGLVYEHVLGEEKYTFVEQVKNPHSCTILIKGPNDHTIAQIKDAVRDGLRSVKNTLEDECVVLGAGAFEVAARQHLINEVKKTVQGRAQLGVEAFANALLVVPKTLAENAGLDTQDVIISLTSEHDKGNIVGLDLQDGEPVDPQLAGIFDNYSVKRQLINSGPVIASQLLLVDEVIRAGRNMRKPT
Protein: U6 snRNA-associated Sm-like protein LSm6p (Q38FH8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MASVNMEDWIQKPAVCVTVFGESHEGLLQGIDNNFNTVLKQSVGNKENELTFVRGESVVYVGFSDIAESTVPEGNAGCGSVASTTS
Protein: Distal membrane-arm assembly complex protein 1 (Transmembrane protein 261) (Q96GE9)
Organism: Homo sapiens (Human)
Function: Required for the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Involved in the assembly of the distal region of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27626371}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Distal membrane-arm assembly complex protein 2
Sequence:
MGSRLSQPFESYITAPPGTAAAPAKPAPPATPGAPTSPAEHRLLKTCWSCRVLSGLGLMGAGGYVYWVARKPMKMGYPPSPWTITQMVIGLSENQGIATWGIVVMADPKGKAYRVV
Protein: Jonah 99Fii (EC 3.4.21.-) (RE68767p) (Q9VA67)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Jonah 25Biii
- Venom allergen-1
- Jonah 25Bii, isoform A
- trypsin
- Jonah 44E, isoform A
- Zinc carboxypeptidase A 1
- Jonah 99Fi
- Trypsin theta
- Uncharacterized protein, isoform A
- Trypsin alpha
Sequence:
MKLFVFLALAVAAATAIPTPEQKLVPTPVKDVKIQGRITNGYPAYEGKVPYIVGLLFSGNGNWWCGGSIIGNTWVLTAAHCTNGASGVTINYGASLRNQPQYTHWVGSGNFVQHHHYNSGNLHNDISLIRTPHVDFWHLVNKVELPSYNDRYQDYAGWWAVASGWGGTYDGSPLPDWLQAVDVQIMSQSDCSRSWSLHDNMICINTNGGKSTCGGDSGGPLVTHEGNRLVGVTSFVSSAGCQSGAPAVFSRVTGYLDWIRDNTGISY
Protein: Nicotinamide nucleotide adenylyltransferase 3 (D6RGH7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLSCA
Protein: Zinc finger protein Worniu (Q9U7P8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDKLKYSRCPLKKRPIMVEESSPEDHLSHDEGPVDLSVASAAVPMEPHWMAKSEPEPQPVPTELRRRFDAAMNQTKEQLARRIWEETREIARAFPDVFTREEIAKSLARLGYGEFELPPEEEVMEPEPEPEQHLPLRYTRDASPTIIKAEPSDEEQFPLRNYNNNLLKSIAEYEDCMKMQNIKEEIPPIPSPQLFYPPPTPLAEPEDLSVTQRRVLSENMNLQNVARALLSMQHMAPQHAPPPIDMEEDQENQDINQLKIKSSNDLYYQCQQCNKCYATYAGLVKHQQTHAYESTEYKIIRSQPGGSGAIVDQTEFCTVQASALIQAANVASAQSMQKPVGVPRYHCQDCGKSYSTYSGLSKHQQFHCPSAEGNQVKKVFSCKNCDKTYVSLGALKMHIRTHTLPCKCPICGKAFSRPWLLQGHIRTHTGEKPFSCQHCNRAFADRSNLRAHMQTHSDVKKYSCPTCTKSFSRMSLLAKHLQSGCQTEQSGGPSGSGGGFDQQQLQQHLQVYEEGHNPHQLYYAGSVGSSNGEEEEGGEYQMQPPAIY
Protein: Uroporphyrinogen-III synthase (UROIIIS) (UROS) (EC 4.2.1.75) (Hydroxymethylbilane hydrolyase [cyclizing]) (Uroporphyrinogen-III cosynthase) (P51163)
Organism: Mus musculus (Mouse)
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme) (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24145442}.
Interaction partners:
- Porphobilinogen deaminase
- Uroporphyrinogen decarboxylase
- Delta-aminolevulinic acid dehydratase
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Protoporphyrinogen oxidase
- Ferrochelatase, mitochondrial
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- 5-aminolevulinate synthase, non-specific, mitochondrial
- Mitochondrial glycine transporter
Sequence:
MKVLLLKDAKEDDSGLDPYIQELRLCGLEATLIPVLSFEFMSLPSLSEKLSHPEGFGGLIFTSPRAVEAVKLCLEKDNKTEAWEKSLKDRWNAKSVYVVGSATASLVNKIGLDAEGAGSGNAEKLAEYICSKPSSELPLLFPCGTIKGDTLPKMLKDKGIPMESMHVYQTVPHPGIQGSLKSYYEDQGIPASITFFSPSGLKYSLEYIQALSGSSFDQIKFIAIGPSTTRAMAAKGLPVSCTAESPTPQALAAGIRNVLKPNHCC
Protein: Krueppel-like factor 5 (Basic transcription element-binding protein 2) (BTE-binding protein 2) (Intestinal-enriched krueppel-like factor) (Transcription factor BTEB2) (Q9Z0Z7)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds to GC box promoter elements. Activates the transcription of these genes.
Subcellular location: Nucleus.
Interaction partners:
- CCAAT/enhancer-binding protein beta
- CCAAT/enhancer-binding protein delta
- CCAAT/enhancer-binding protein alpha
- Peroxisome proliferator-activated receptor gamma
- Steroid hormone receptor ERR2
- F-box/WD repeat-containing protein 7
- Estrogen receptor beta
- POU domain, class 5, transcription factor 1
- Homeobox protein NANOG
- Nuclear factor NF-kappa-B p105 subunit
Sequence:
MPTRVLTMSARLGPLPQPPAAQDEPVFAQLKPVLGAANPARDAALFSGDDLKHAHHHPPAPPPAAGPRLPSEELVQTRCEMEKYLTPQLPPVPIISEHKKYRRDSASVVDQFFTDTEGIPYSINMNVFLPDITHLRTGLYKSQRPCVTQIKTEPVTIFSHQSESTAPPPPPAPTQALPEFTSIFSSHQTTAPPQEVNNIFIKQELPIPDLHLSVPSQQGHLYQLLNTPDLDMPSSTNQTAVMDTLNVSMAGLNPHPSAVPQTSMKQFQGMPPCTYTMPSQFLPQQATYFPPSPPSSEPGSPDRQAEMLQNLTPPPSYAATIASKLAIHNPNLPATLPVNSPTLPPVRYNRRSNPDLEKRRIHFCDYNGCTKVYTKSSHLKAHLRTHTGEKPYKCTWEGCDWRFARSDELTRHYRKHTGAKPFQCMVCQRSFSRSDHLALHMKRHQN
Protein: Protein IQ-DOMAIN 19 (AtIQD19) (Protein FURCA 3) (A0A1P8B590)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). Acts as a positive regulator of trichome branch initiation. May associate with nucleic acids and regulate gene expression at the transcriptional or post-transcriptional level (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}. Cell membrane {ECO:0000269|PubMed:28115582}.
Interaction partners:
Sequence:
MVLGCPKREAVKEFGVQCLKQENVCPIITSRNQTHTHTHITISSSLTLHNGGLSLQKIIMGKTSKWFRSLLTGKKERTKEHIIQSECVFTSSIPGTPKEKRRWSFRRSSATGPPPPACAITLKDSPPPPPPPPPPPPLQQPFVVEIVDNEDEQIKNVSAEEIEEFAAIKIQACYRSHLARKALRALKGLVKLQALVRGHLVRKQATATLRCMQALITLQAKAREQRIRMIGGDSTNPRTSIHKTRINNFYHENEENIKIVEMDIQSKMYSPAPSALTEMSPRAYSSHFEDCNSFNTAQSSPQCFSRFKEYYNGDTLSSYDYPLFPNYMANTQSSKAKARSQSAPKQRPPEIYEKQMSGRRRSSMEAPRNNGVPRAVRMQRSSSQLGSNTAKESQQHHHHQYYPWMAIKLDRSNISLMESECGSTSTVMTNTNYGRHVDVQGNNNMY
Protein: Cytosolic sulfotransferase 17 (AtSOT17) (EC 2.8.2.38) (Desulfoglucosinolate sulfotransferase C) (AtST5c) (Q9FZ80)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of desulfo-glucosinolates (dsGSs), the final step in the biosynthesis of the glucosinolate core structure. Substrate preference is desulfo-benzyl glucosinolate > desulfo-6-methylthiohexyl glucosinolate. Increased specific activity with increasing chain length of desulfo-glucosinolate derived from methionine. Preferred substrate is desulfo-8-methylthiooctyl glucosinolate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16367753}.
Interaction partners:
- S-alkyl-thiohydroximate lyase SUR1
- Cytosolic sulfotransferase 18
- Cytosolic sulfotransferase 16
- Cytochrome P450 83A1
- UDP-glycosyltransferase 74B1
- Methylthioalkylmalate synthase 1, chloroplastic
- Methionine aminotransferase BCAT4
- Dihomomethionine N-hydroxylase
- Methylthioalkylmalate synthase 3, chloroplastic
- Probable inactive 2-oxoglutarate-dependent dioxygenase AOP2
Sequence:
MESKTINDVVVSESNHELASSSPSEFEKNQKHYQEIIATLPHKDGWRPKDPFVEYGGHWWLQPLLEGLLHAQKFFKARPNDFFVCSYPKTGTTWLKALTFAIANRSKFDVSTNPLLKRNPHEFVPYIEIDFPFFPSVDVLKDEGNTLFSTHIPYDLLPESVVKSGCKIVYIWRDPKDTFVSMWTFAHKERSQQGPVVSIEEAFDKYCQGLSAYGPYLDHVLGYWKAYQANPDQILFLKYETMRADPLPYVKRLAEFMGYGFTKEEEEGNVVEKVVKLCSFETLKNLEANKGEKDREDRPAVYANSAYFRKGKVGDWQNYLTPEMVARIDGLMEEKFKGTGFLSSKS
Protein: RNA-splicing ligase RtcB homolog (EC 6.5.1.8) (3'-phosphate/5'-hydroxy nucleic acid ligase) (Q54Y09)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs.
Interaction partners:
- Protein archease-like
- RNA transcription, translation and transport factor protein
- Probable ATP-dependent RNA helicase ddx1
- Probable RNA 3'-terminal phosphate cyclase
- Probable RNA 3'-terminal phosphate cyclase-like protein
- 2'-phosphotransferase
- Eukaryotic translation initiation factor 2 subunit 1
- Uncharacterized protein
Sequence:
MTDSVVRGFEDELSFIEKIDSVRYRVKKGFVPNMNVDGMIYVNDSIKDYLYEELEQYSKRGVSGFLPAVKQIANVASLPGIVGHSLGMPDIHSGYGFSIGNVAAFDTEDPLSIVSPGGVGFDINCGVRLLRTNLTEKDIEPIKEQLCQSLFDHVPVGVGSKGVIPMNIKTLNQALEMGVDWSLGEGYAWVEDKEHCEEYGRMLNADPTKVSERAKKRGLPQLGTLGAGNHYLEVQVVDEIYDKAAANKMGIDRQGQICIMIHSGSRGLGHQVATDSLTLMEKAMARDHIHLNDKQLACSRINSTEGQDYLSGMAAAANFAWVNRQSMTFLTRQAFAKAFNSTPDDLDMHVIYDVSHNIAKFEEHNVNGRPKKLLVHRKGATRAFAPHHPLIPVDYQFTGQPVLIGGTMGTCSYVLTGTELGMNETFGSTCHGAGRSCSRNKSRNNLSYTDVLDSLQAKGISIRVASPKLVMEEAPESYKDVVQVIETCHKAGISKKSVKLRPIAVIKG
Protein: Mitochondrial tRNA-specific 2-thiouridylase 1 (EC 2.8.1.14) (A0A2R8Y4R7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKNWDSLDEHGVCTADKDCEDAYRVCQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGADAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPALYRDLLRTSRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAVRALATG
Protein: Bifunctional nitrilase/nitrile hydratase NIT4A (LaNIT4A) (EC 3.5.5.4) (EC 4.2.1.65) (3-cyanoalanine hydratase) (Cyanoalanine nitrilase A) (Q5QGZ8)
Organism: Lupinus angustifolius (Narrow-leaved blue lupine)
Function: Involved in the cyanide detoxification pathway. Has nitrilase and nitrile-hydratase activity in the ratio 4.0:1, producing both asparagine and aspartic acid from beta-cyano-L-alanine (Ala(CN)). Can also use 3-phenylpropionitrile as substrate, but not indole-3-acetonitrile.
Interaction partners:
Sequence:
MALVTTPTVNDGPLFAEVNMSSDFNAPTVRATVVQASTIFYDTPATLDKAERLLAEAASYGAQIVVFPEAFIGGYPRGSNFGVSIGNRTAKGKEDFRKYHSAAIDVPGPEVDRLAALAGKYKVYLVMGVIERDGYTLYCTVLFFGAQGRYLGKHRKLMPTALERIIWGFGDGSTIPVFETPIGKIGAAICWENKMPLLRTAMYAKGVEIYCAPTADSREVWQASMTHIALEGGCFVLSANQFCRRRDYPPPPEYVFEGTEENLTPDSVVCAGGSVIISPSGAVLAGPSYEGEALISADLDLGEIARAKFDFDVVGHYSRPEVLSLVVKDHPTNPVTFTSASTKIEDKTK
Protein: Dihydropyrimidine dehydrogenase [NADP(+)] (DHPDHase) (DPD) (EC 1.3.1.2) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase) (Q12882)
Organism: Homo sapiens (Human)
Function: Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil.
Subcellular location: Cytoplasm.
Interaction partners:
- Uridine 5'-monophosphate synthase
- Dihydropyrimidinase
- Thymidine phosphorylase
- Uridine phosphorylase 2
- Uridine phosphorylase 1
- Thymidylate synthase
- Beta-ureidopropionase
- Uracil phosphoribosyltransferase homolog
- Cytochrome P450 2A6
- Purine nucleoside phosphorylase
Sequence:
MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCFNCEKLENNFDDIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQFATEVFKAMSIPQIRNPSLPPPEKMSEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNEMTLSTLKEKGYKAAFIGIGLPEPNKDAIFQGLTQDQGFYTSKDFLPLVAKGSKAGMCACHSPLPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWNEDEDQMVHLKADVVISAFGSVLSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQYGASVSAKPELPLFYTPIDLVDISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQSPATVSHQKGKPVPRIAELMDKKLPSFGPYLEQRKKIIAENKIRLKEQNVAFSPLKRNCFIPKRPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKMVSRTTPYEPKRGVPLSVNPVC
Protein: Lipid A acyltransferase PagP (EC 2.3.1.251) (Lipid A acylation protein) (Q7WFT9)
Organism: Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Function: Transfers a fatty acid residue from the sn-1 position of a phospholipid to the N-linked hydroxyfatty acid chain on the proximal unit of lipid A or its precursors. Required for resistance to cationic antimicrobial peptides (CAMPs). Modifications of lipid A with an acyl chain to evade host immune defenses by resisting antibody-mediated complement lysis during respiratory infection.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000305}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00837, ECO:0000305}.
Interaction partners:
Sequence:
MTQYFRALAFFLLLVPATAMACDGWPSWARGACQRVDQIWNEGGNDLYLTGYSWHNRAMYSSDKIRSFNELAWGGGLGKSIYDEDGDWQGLYAMAFLDSHSDIEPIAGYGFQKIGRIGADTRLGIGYTVFLTSRSDIMSRVPFPGILPLVSAGYRDATLYATYIPGGKGNGNVLFMFGRWEF
Protein: Neuralized E3 ubiquitin protein ligase 1 (A0A8I5ZN22)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGNNFSSVSSLQRGNPSRASRGHPQNLKDSIGSSFPVPSHRCHHKQKHCPPALSGGGLPATPLLFHPHTKGSQILMDLSHKAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFYRINESAAMLFFSGVRTADPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLRCEADEARLSVSLCDLNVPGADGEDGAPPAGCPIPQNSLNSQHSRALPAQLDGDLRFHALRAGAHVRILDEQTVARLEHGRDERALVFTSRPVRVAETIFIKVTRSGGARPGALSFGVTTCDPGTLRPADLPFSPEALVDRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHNGAPAGMQLCVDASQPLWMLFSLHGAITQVRILGSTIMAERGGPSLPCSPASTPTSPSALGSRLSDPLLSTCGSGPLGGSAGGTAPNSPVSLPESPVTPGLGQWSDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTYRSS
Protein: Tropomyosin alpha-4 chain (TM30p1) (Tropomyosin-4) (P67936)
Organism: Homo sapiens (Human)
Function: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments (By similarity). Binds calcium.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P09495}. Note=Associates with F-actin stress fibers. {ECO:0000250|UniProtKB:P09495}.
Interaction partners:
- Tropomyosin beta chain
- Tropomyosin alpha-1 chain
- Troponin T, cardiac muscle
- Actin, alpha cardiac muscle 1
- Tropomyosin alpha-3 chain
- Troponin I, cardiac muscle
- Myosin-9
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin I, fast skeletal muscle
- ALK tyrosine kinase receptor
Sequence:
MAGLNSLEAVKRKIQALQQQADEAEDRAQGLQRELDGERERREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELNCI
Protein: WD repeat domain phosphoinositide-interacting protein 3 (WIPI-3) (WD repeat-containing protein 45-like) (WDR45-like protein) (WD repeat-containing protein 45B) (WIPI49-like protein) (Q5MNZ6)
Organism: Homo sapiens (Human)
Function: Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation. Binds phosphatidylinositol 3-phosphate (PtdIns3P), and other phosphoinositides including PtdIns(3,5)P2, forming on membranes of the endoplasmic reticulum upon activation of the upstream ULK1 and PI3 kinases and is recruited at phagophore assembly sites where it regulates the elongation of nascent phagophores downstream of WIPI2. In the cellular response to starvation, may also function together with the TSC1-TSC2 complex and RB1CC1 in the inhibition of the mTORC1 signaling pathway.
Subcellular location: Preautophagosomal structure {ECO:0000269|PubMed:28561066}. Lysosome {ECO:0000269|PubMed:28561066}.
Interaction partners:
- Autophagy-related protein 2 homolog A
- OTU domain-containing protein 7B
- Autophagy-related protein 2 homolog B
Sequence:
MNLLPCNPHGNGLLYAGFNQDHGCFACGMENGFRVYNTDPLKEKEKQEFLEGGVGHVEMLFRCNYLALVGGGKKPKYPPNKVMIWDDLKKKTVIEIEFSTEVKAVKLRRDRIVVVLDSMIKVFTFTHNPHQLHVFETCYNPKGLCVLCPNSNNSLLAFPGTHTGHVQLVDLASTEKPPVDIPAHEGVLSCIALNLQGTRIATASEKGTLIRIFDTSSGHLIQELRRGSQAANIYCINFNQDASLICVSSDHGTVHIFAAEDPKRNKQSSLASASFLPKYFSSKWSFSKFQVPSGSPCICAFGTEPNAVIAICADGSYYKFLFNPKGECIRDVYAQFLEMTDDKL
Protein: Probable isocitrate dehydrogenase [NADP], mitochondrial (IDH) (EC 1.1.1.42) (IDP) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) (O14254)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Aconitate hydratase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Probable citrate synthase, mitochondrial
- Isocitrate dehydrogenase subunit 2, mitochondrial
- Probable NAD-specific glutamate dehydrogenase
- Glutamate synthase
- NADP-specific glutamate dehydrogenase
- Malate dehydrogenase, mitochondrial
- Aspartate aminotransferase, mitochondrial
Sequence:
MLEVRAAVKAPFKLAAAGRGFMNMRMASSKSFQKITVKNPVVEMDGDEMTRVIWKIIREKLVLPYMDIKLDYYDLGIEARDKTNDQITVDAAKAILKNDVGIKCATITPDEARVKEYNLKKMWKSPNGTIRNILNGTVFREPILIKNIPKYIPGWTNPICIGRHAFGDQYKSTDLVASGPGKLELSFTPKGNPSAKETYNVYEFNGSGVAMSMYNTDDSIRGFAHSSFQMALQKKMPLYLSTKNTILKKYDGRFKDTFQEVYESDYKQKFEELGLWYQHRLIDDMVAQAIKSNGGFVWACKNYDGDVMSDVVAQAYGSLGLMTSVLIHPNGRTFESEAAHGTVQRHYMQYLKGKKTSTNSIASIFAWTRGLAHRGRLDGNERLVKFANALEHACVRCVEKGIMTKDLYLLSKSPNGYVDTFEFLDAVKSELDSELVNIA