wanglab/gogpt-training-data huggingface dataset:
Protein: Isoleucine N-monooxygenase 1 (EC 1.14.14.39) (Cytochrome P450 79D3) (Valine N-monooxygenase 1) (EC 1.14.14.38) (Q6J541)
Organism: Lotus japonicus (Lotus corniculatus var. japonicus)
Function: Involved in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin and of the nitirle glucosides rhodiocyanoside A and D. Can use L-isoleucine > L-valine as substrate, but not L-leucine, L-phenylalanine or L-tyrosine.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:D5JBW8}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGLMPDFLSLCHEFPWTFLLVVIFSFMIFKVTKTHLVNKSKKYKLPPGPKPWPIVGNLPEMLANRPATIWIHKLMKEMNTEIACIRLANTIVIPVTCPTIACEFLKKHDASFASRPKIMSTDIASDGFITTVLVPYGEQWKKMKRVLVNNLLSPQKHQWLLGKRNEEADNLMFYIYNKCCKDVNDGPGLVNIRIAAQHYGGNVFRKLIFNSRYFGKVMEDGGPGFEEVEHINATFTILKYVYAFSISDFVPFLRRLDLDGHRSKIMKAMRIMRKYHDPIIDDRIKQWNDGLKTVEEDLLDVLIKLKDANNKPLLTLKELKAQIIELAIEMVDNPSNAFEWALAEMINQPELLKRATEELDNVVGKERLVQESDIPKLQFVKACAREALRLHPMEYFNVPHLCMNDTMVGDYLFPKGTQVLLSRVALGRNPKFWTDPLKFNPERHLKEGIDVVLTEPDLRFISFTTGRRSCPGVALGTTMTVMLFARMLHGFSWSPPPDVSSIDLVPSKDDLFLAKPLLLVAKPRLAAELYRTNEI
Protein: Guanylyl cyclase, membrane (EC 4.6.1.2) (DdGCA) (GCA) (Guanylate cyclase) (Q553Y7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Synthesizes cyclic GMP (cGMP) from GTP, after activation by heterotrimeric or monomeric G proteins. Involved in chemotaxis.
Subcellular location: Membrane {ECO:0000305|PubMed:2564393}; Multi-pass membrane protein {ECO:0000305|PubMed:2564393}.
Interaction partners:
- Adenylate cyclase, germination specific
- F-box domain-containing protein
- Ankyrin repeat-containing protein
- Uncharacterized protein
- Protein SGT1 homolog
- Adenylyl cyclase-associated protein
- Patatin family protein
Sequence:
MMFGNLPDVRKPKEGYKKYLEYFDLRFPRIQEEKHFQSYYYYTYLKQIRISIIFLTSVLFIGTMTAYISPLDISYLPYYDSKNIYYFNYVQPNVTTTSSSTTTTSSTTNSIDSTVENNNFTEADGHLTNYYFPYLANKARDTFILRMITIGLLLFYFIFTFTAKFKRLWKLFTTITLFLVSCIVLIFESDIRTIPGRMVLLFIIIAISSGMTFLPSMLASGGLCLFFFFYFMFYSQIAGKQMVLLSLVLLISWIILMIISRFKEQLFRDKFRTLENLKIQTIRSEKIINQMLPTVVVQRLRLQSSKDQSLETTLENDKELSIKKDEESNLTGKKQSKVVVSPPPPPTAAAPQQQDNEISTPQNSRKIVDPQSPSSLMPGQYSVTDLIVDSYDPVTVLFCEIVNFNALVEKMSSTQVINLLNEVYNSFDRLTDVYGVTKVEHIGNVYMVVGGCPELCPDHAQRVAHMSLGMLSVIRRFGIVQVRIGMHTGPVVGGIIGKKKLSWHLFGDTINTSSRMASHSSIGRIQVSHPVQQLLRPYFLFEDRGKIQVKGKGLMRTFYLVKTKQLDKRYTSIFSSLHREKPYIPPVDISEVSFENQNNTIGKGDDIASGSATGPTHPNIPNSMLSAIPSRVSIEMNPLGGSGSIQKRERKGSIFANVMPPKVLNFLQTGSLTSPQQQPLPQQSNSEETISNSPRLSSTPQSTSTLQHSSSTGALGSLINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNLPVSLISPISQNTTPTGSLSLPVTEKKKQTVQFGSISRSSSISKGTVGRSPSPALFDGGIEMDDNGGGAGDDFNTMEPNLDLGKGIHGSNVISTNNSKLNKLEKDLTKHYTLDKFKLSFISRGNLVEKEYRNEYILKNWNRILASMLMIVALFGLSGLVDYFFLKLSSISSIVKVEPMPSSSSSSLSSSSSNSMTSSEEKFITLHTIRSEENLIYDIITGVRYGFVFFCLIVIYVVSKFKTFSIRKWIQEVVMVFFIVLAAVLIVLTSVPPLNKIPLDSVILSIEIMFITICYNFSGIKFWYSNIVCAFCIIFIEISKTWKQAYHSRDIYLSHNYYLITAVLINIITSYFEELFNRLNWVHGRLLDKDQRETESLVAEILPADIVKSMKSGRQLIVDEFKNVTIFLSDIVGFTEMAARMSPRQLVETLNQIYSTFDEIAQEFGVLKIATIGDAYFCVSGCPDKDQTDHAFRVANMAIKMLESIKSIRTVDNIPIRMRIGIHTGPVIAGVVGIKMIHYQLWGESVQITQQMESTSRADMIHVSEDTFNILKSKYLFEERPDGIIKKRKIKTYFLLRALTENDPQPEVKTRSVSVSKSNFGGSLQYNQITPTLNLPVSQLIIKDQNEIKNQNDHDNDDENGNENGNESSSSNINEEEEDDDNSNNNNNNEDDESSYEDDQEMNQYLNNSENNKNNNNNSNQINEEDGNWAKNYDGSSESS
Protein: UBA domain-containing protein Mud1 (EC 3.4.23.-) (DNA-damage-inducible protein DDI1 homolog) (UBA domain-containing protein 1) (Q10256)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Recognizes and binds polyubiquitin chains. Acts as a linker between the 19S proteasome and polyubiquitinated proteins via UBA domain interactions with ubiquitin for their subsequent degradation. Aspartic protease. Appears to act as negative regulator of constitutive exocytosis. May act at the level of secretory vesicle docking and fusion as a competitive inhibitor of SNARE assembly. Required for S-phase checkpoint control (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P40087}. Cell membrane {ECO:0000250|UniProtKB:P40087}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40087}; Cytoplasmic side {ECO:0000250|UniProtKB:P40087}.
Interaction partners:
- Polyubiquitin
- Cell division control protein 16
- UV excision repair protein rhp23
- 26S proteasome regulatory subunit rpn10
- Deubiquitination-protection protein dph1
- AN1-type zinc finger protein C1271.05c
- Mitochondrial intermediate peptidase
- Probable uroporphyrinogen-III C-methyltransferase
- 26S proteasome regulatory subunit rpn1
- Uncharacterized protein C9E9.15
Sequence:
MNNLTPENIRQTILATPFLLNRIRTEFPQLAAVLNDPNAFATTWQSINASQLLQIPSSTYSMGMPSFSEDDLFDVEVQRRIEEQIRQNAVTENMQSAIENHPEVFGQVYMLFVNVEINGHKVKAFVDSGAQATILSADCAEKCGLTRLLDTRFQGVAKGVGMAKILGCVHSAPLKIGDLYLPCRFTVIEGRDVDMLLGLDMLRRYQACIDLENNVLRIHGKEIPFLGESEIPKLLANVEPSANAHGLGIEPASKASASSPNPQSGTRLGTKESVAPNNEGSSNPPSLVNPPTDPGLNSKIAQLVSMGFDPLEAAQALDAANGDLDVAASFLL
Protein: Vicilin Jug r 6.0101 (Allergen Jug r 6) (Vicilin Jug r 6) (allergen Jug r 6.0101) (A0A2I4E5L6)
Organism: Juglans regia (English walnut)
Function: Seed storage protein.
Interaction partners:
Sequence:
MAFKPKIPIALLLLTSLLAICAGLALAMQDPELKQCKHQCRHQRQFDEQEKEHCQRSCDEYHIEKKARERAERRRSEEGSSREEGYEEEELGGEREEENPYVFEDEDFETRVRTDEGRIQVLEKFTKRSKLLRGIENFRVAILEANPQTFISPAHFDAELVVFVAKGRATITTVREEKRENFNVEQGDIMRIPAGTPVYLINRDENEKLYIVKILRPVSVPGHFEAFHGSGGEDPESFYRAFSWEVLEAALKTRRDQLEKLFGKQTQGVIIKASKEQIRSMSKHEETTPRIWPFGGDSTHPFNLFHKRPSQSNQFGRLFETDPKECKQLQDLDLMVSFANITKGSMAGPYYNSRATKISVVIEGEGYFEMACPHLSSSGSRGQREGSGSSRRRSRSGPSYQQIRGRLRPGMVFVAPAGHPVAVIASRNKNLQVLCFDVNAQGNIRFPLAGKNNIVNEFEKEAKELAFNFPAREVEKIFRNQDQEFFFPGPSRQPEEGGRAFE
Protein: Thioredoxin (Q6FND5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- peptide-methionine
- Glutathione reductase
- Thioredoxin reductase
- Thioredoxin reductase
- thioredoxin-dependent peroxiredoxin
- Tryptophan synthase
- thioredoxin-dependent peroxiredoxin
- Glutathione peroxidase
- Transcription factor
Sequence:
MVKQITSVSEFDSAIAVDKLVVVDFFATWCGPCKMIAPMIEKFAAEYSTADFYKLDVDELPEVAQKNEVSAMPTLVLFKNGKEVAKVVGANPAAIKQAIANNV
Protein: Candida glabrata strain CBS138 chromosome D complete sequence (Q6FWH2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Xylulose kinase
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- serine C-palmitoyltransferase
- Candida glabrata strain CBS138 chromosome G complete sequence
- 5-aminolevulinate synthase, mitochondrial
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- S-formylglutathione hydrolase
- Acetyl-coenzyme A synthetase 1
- Acetyl-coenzyme A synthetase 2
Sequence:
MRSLAYFKTGDIHFTDKIDTPKINNDHELMIDVAWCGICGTDLHEFLEGPIFMPKDGDTHYLSGLDLPLPMGHEMSGIVKEVGKGVTRFKPGDRVVIEATTSCGDTHRWPKSKVAKGELCPACEMGLPNCCTHGSFQGLGSVGGGFAEQVVVGEKHVVKIPDKLPLDVAALVEPLSVAWHAARLAEFKEGSNALVLGSGPIGLAMILALKGMKAGKIVVSEPAKLRRELAEKLNVVVFNPTHTRAQNAIEKLKELSPKDHGFDYTFDCSGVQDTFNAAVKAACIQGHIVNVAIWGPKPVAFHPMDMTYGEKKLTGTMGYVTRDFEEVVDAIDKGYISIEECKLLITGRVKLEDGMEKGFHELIEHKETNVKILLTPNNHGELQ
Protein: Mating pheromone alpha (Q59QG8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Alpha-factor pheromone receptor
- Ste3p
Sequence:
MKFSLTLLTATIATIVAAAPAQYTGQAIDSNQVVEIPESAVEAYFPIDDELTPVFGEIDNKPVILIVNGTTLTSGANNEKREAKSKGGFRLTNFGYFEPGKRDANADAGFRLTNFGYFEPGKRDANAEAGFRLTNFGYFEPGK
Protein: GRAM domain containing 1A (M0QZ12)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
Sequence:
MDDVLPLMPWETLLAQGSPQGSPDLPAGQRKQQPQGDRAQGLASESWKLLEVPIIHITPSSDGESPACTPTPRRRQQQRMPDPQSLSQDSTTPHSGRSTPSSSPSLRKRLQLLPPSRPPPEPEPGTMVEKGSDSSSEKGGVPGTPSTQSLGSRNFIRNSKKMQSWYSMLSPTYKQRNEDFRKLFSKLPEAERLIVDYSCALQREILLQGRLYLSENWICFYSNIFRWETTISIQLKEVTCLKKEKTAKLIPNAIQICTESEKHFFTSFGARDRCFLLIFRLWQNALLEKTLSPRELWHLVHQCYGSELGLTSEDEDYVSPLQLNGLGTPKEVGDVIALSDITSSGAADRSQEPSPVGSRRGHVTPNLSRASSDADHGAEEDKEEQVDSQPDASSSQTVTPVAEPPSTEPTQPDGPTTLGPLDLLPSEELLTDTSNSSSSTGEEADLAALLPDLSGRLLINSVFHVGAERLQQMLFSDSPFLQGFLQQCKFTDVTLSPWSGDSKCHQRRVLTYTIPISNPLGPKSASVVETQTLFRRGPQAGGCVVDSEVLTQGIPYQDYFYTAHRYCILGLARNKARLRVSSEIRYRKQPWSLVKSLIEKNSWSGIEDYFHHLERELAKAEKLSLEEGGKDARGLLSGLRRRKRPLSWRAHGDGPQHPDPDPCARAGIHTSGSLSSRFSEPSVDQGPGAGIPSALVLISIVLIILIALNVLLFYRLWSLERTAHTFESWHSLALAKGKFPQTATEWAEILALQKQFHSVEVHKWRQILRASVELLDEMKFSLEKLHQGITVSDPPFDTQPRPDDSFS
Protein: Ankyrin repeat domain 27 (V9GYL8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALYDEDLLKNPFYLALQKCRPDLCSKVAQIHGIVLVPCKGSLSSSIQSTCQFESYILIPVEEHFQTLNGKDVFIQGNRIKLGAGFACLLSVPILFEETFYNEKEESFSILCIAHPLEKRESSEPLAPSDPFSLKTIEDVREFLGRHSER
Protein: glutathione transferase (EC 2.5.1.18) (G8HHE8)
Organism: Meleagris gallopavo intermedia
Interaction partners:
Sequence:
MSGKPVLHYPNSRGRMESVRWLLAAAGVEFEEKFLEKKEDLQKLQSDGSLLFQQVPMVEIDGMKLVQTRAILNYIAGKYNLYGKDVKERALIDMYVEGMADLYELIMMNVVQPADKKEEHLANALDKATNRYFPVFEKILNHGHDFLVGNKLSRADVSLLETILVVEERKPDALAKFPLLQSFKARISNTPNIKKFLQPGSQRKPPLQEKDIPSLMAIFH
Protein: 2-methylcitrate synthase 2 (2-MCS) (MCS) (EC 2.3.3.5) (Citrate synthase 2) (CS) (EC 2.3.3.16) (Q8NSL1)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity.
Interaction partners:
- Probable 2-methylisocitrate lyase 2
- 2-methylcitrate dehydratase 2
- 2-methylcitrate dehydratase 1
- Phosphate acetyltransferase
- Uncharacterized protein involved in propionate catabolism
- 2-oxoglutarate dehydrogenase E1/E2 component
- methylmalonate-semialdehyde dehydrogenase
- NAD-dependent aldehyde dehydrogenases
- Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit
- Detergent sensitivity rescuer dtsR2
Sequence:
MSSATTTDVRKGLYGVIADYTAVSKVMPETNSLTYRGYAVEDLVENCSFEEVFYLLWHGELPTAQQLAEFNERGRSYRSLDAGLISLIHSLPKEAHPMDVMRTAVSYMGTKDSEYFTTDSEHIRKVGHTLLAQLPMVLAMDIRRRKGLDIIAPDSSKSVAENLLSMVFGTGPESPASNPADVRDFEKSLILYAEHSFNASTFTARVITSTKSDVYSAITGAIGALKGPLHGGANEFVMHTMLAIDDPNKAAAWINNALDNKNVVMGFGHRVYKRGDSRVPSMEKSFRELAARHDGEKWVAMYENMRDAMDARTGIKPNLDFPAGPAYHLLGFPVDFFTPLFVIARVAGWTAHIVEQYENNSLIRPLSEYNGEEQREVAPIEKR
Protein: Serine/threonine-protein acetyltransferase HopZ1a (EC 2.3.1.-) (Protein orf34) (Q6VE93)
Organism: Pseudomonas syringae pv. syringae
Function: Serine/threonine-protein acetyltransferase translocated into infected cells, which impairs host microtubule network and host immunity by mediating acetylation of target proteins. Blocks secretion in host cells by mediating acetylation of host tubulin, thereby impairing host microbubule network. Impairs host cell immunity by mediating acetylation of host TIFY/JAZ transcription repressors (Arabidopsis thaliana TIFY10B/JAZ2, TIFY11A/JAZ5, TIFY11B/JAZ6, TIFY5A/JAZ8, TIFY9/JAZ10 and TIFY3B/JAZ12), thereby activating host jasmonate signaling.
Subcellular location: Secreted {ECO:0000305|PubMed:20636323}. Host cell membrane {ECO:0000269|PubMed:24204266}. Host cytoplasm, host cytoskeleton {ECO:0000269|PubMed:22319451}. Host nucleus {ECO:0000305|PubMed:24204266}. Note=Secreted via type III secretion system (T3SS). {ECO:0000305|PubMed:20636323}.
Interaction partners:
Sequence:
MGNVCVGGSRMSHQVYSPDRADTPPRSERNTPDRRQRAAGDAERTQSMRLQQKINDLKPYVRHARGPIKAYGQAALDRASGKKTSVSFAELDATHLDAMVYIENQRNPGLNLKHFRDHKELIQALQSDGPSAFRAIFPQTCPETGQTLKHHVMADVRLHQGGAPTIIITEPAVIVGARYQQLQRHNLTLEDLSESGVPLSQVAIIETQAQKTSDDCVMYSLNYAIKAHKNAAQFDDIHHGLQHGTLSTESESRARTTLGALEASSSYSVMHEGAHAAFGADVLPVDFYKHGASLTQAKQLMKRPDGRMAGRVNSEGHSEAENLVQRNQAFRVKRRELLDDETPSNTQFSASIDGFRLQEIKRVLAEEQR
Protein: DNA replication checkpoint protein tel2 (Q9P3W5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the TORC1 and TORC2 complexes required for the regulation of the cellular respons to changes in available nutrients. Required for normal entry into S phase. Regulates activation of the DNA replication checkpoint. Required for efficient phosphorylation of mrc1, which is essential for the activation of cds1 kinase. Also plays an important role in genome stability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- TEL2-interacting protein 1
- RuvB-like helicase 2
- SAGA complex/NuA4 acetyltransferase complex subunit Tra1
- RuvB-like helicase 1
- Tel2-interacting protein 2
- ASTRA-associated protein 1
- Serine/threonine-protein kinase tel1
- Serine/threonine-protein kinase tor2
- Protein kinase rad3
- DNA repair protein rad16
Sequence:
MKSFASELSKPIQKPRLKEILKELQHIGVPSPCNLRLYHELISVIVPTFWNGKINSEIDFLLAKCFSTLLGLKLLCVRLDNFVQEANLQNIHLVTVYLELLEKAFECIDLDDNCKLIWESTVLSDHQKQSLWTEFIFFLGNFKITNSMSAAMLTFKVYDDSKRLKASSMADYIGVLSSKLACIISKPAVKTPEIYSKLFHYLLHSSNLKAFINPLIPLTQKFCVQLQKLFADLTVSDQMLFLNQLLLEHNTKYPTNFSYSTARDDRITGSLATLLRLNFSSTHFLRLIEFYWGVPTNLIIKRVEVVCSSISYKESDKKELEKTVDSLFNIWSNAQFLRSYTLLAQESLTIYLLLFIPKLEAKYLNNLSKSLMFSNAISCRLDSLDDDIRMHGMIMAEVISTYSGVSLSNPLAFDVPIMKTTKAKVLKSLSSLKDEFLPIEILNDESVIAETSIEKEETNVTHLEKPVISKNDDLIRGDDLEPYDFPDIDSEDTDDDPTVSRSKTHSPVYVQDLCKMLKDTESFEKQRVALENASKLIKRKSAFGTELRDHADELLQTLISLQNRFDLMNFDEMQMTAIVELLLTCLDICGPVICTNLFVSDYSMRQKILILSCISLAASKFNDDDNERLFPSQLLPGNLHDQFYSPTIEKISDELERKLVFPVMSECKDYAEGPKFLQTRYISKQSEIESKKPLPKANRLSLKVDKSLFLLLTSGYMLASRKTAFIEPLFLVYYLKTLGILFFETFTSKIEGANRMLREYVDVLNEVCRLRSDTPEVNEGLLFSFLAILEISSGRTLANEFGKHLLFFEAYTKFLFESPDQGEKVKSLSAAVLILFENKLSEFRTLALEKLLDDSAPLVPERFGLAGL
Protein: Dehydrogenase/reductase SDR family member 6 (EC 1.1.1.-) ((R)-beta-hydroxybutyrate dehydrogenase) (3-hydroxybutyrate dehydrogenase type 2) (EC 1.1.1.30) (4-oxo-L-proline reductase) (EC 1.1.1.104) (Oxidoreductase UCPA) (Short chain dehydrogenase/reductase family 15C member 1) (Q9BUT1)
Organism: Homo sapiens (Human)
Function: NAD(H)-dependent dehydrogenase/reductase with a preference for cyclic substrates (By similarity). Catalyzes stereoselective conversion of 4-oxo-L-proline to cis-4-hydroxy-L-proline, likely a detoxification mechanism for ketoprolines. Mediates the formation of 2,5-dihydroxybenzoate (2,5-DHBA), a siderophore that chelates free cytoplasmic iron and associates with LCN2, thereby regulating iron transport and homeostasis while protecting cells against free radical-induced oxidative stress. The iron-siderophore complex is imported into mitochondria, providing an iron source for mitochondrial metabolic processes in particular heme synthesis (By similarity). May act as a 3-hydroxybutyrate dehydrogenase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16380372}.
Interaction partners:
- D-beta-hydroxybutyrate dehydrogenase, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial
- 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic
- Acetoacetyl-CoA synthetase
- 3-ketoacyl-CoA thiolase, peroxisomal
Sequence:
MGRLDGKVIILTAAAQGIGQAAALAFAREGAKVIATDINESKLQELEKYPGIQTRVLDVTKKKQIDQFANEVERLDVLFNVAGFVHHGTVLDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSVKGVVNRCVYSTTKAAVIGLTKSVAADFIQQGIRCNCVCPGTVDTPSLQERIQARGNPEEARNDFLKRQKTGRFATAEEIAMLCVYLASDESAYVTGNPVIIDGGWSL
Protein: Uncharacterized protein LOC503753 (Zgc:113263) (F1QGF1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MEALWTNKIEDPLSLMSFTVPPLRLLSAAMWQVTERRQVKHYGMLEEFVSLVTETIPELLNQNQRAQLILGLRARHLLELCRGKHQGSLKEIQPHLKRLCRPRVNKEFADEDMEESETCFLDLVRTLISNPKEKEHYFQNIFPEEYGPKFDKNLHALMEDFLLKLDRMVSVPDLSETVSWLRTCPSLLDDCIDSVSVPKDMKSLLEHHTAKGNLQDSEGNNCTFSSQSLPPLVQVVISSDHTESGEPSDLNGQDNDDEQASKTSSDGWTIKKIKLKTETEEEDNDQNWPITEAKSTGTRDGYDDGCLGEEPNQTQSKINTRKSLKRKRDEIADTSREYTFINHLGAYTEESSYQSSDASKVPWTEEETFGLIDIWGKDSVQRSLKDCARNRHIFNLISKKMFERGFTRTAEQCHTRIKRLKMSFRQYHDSILKGERADWKFYDVLEKILCGKDSAEQEDSNNDVSVPEESSGQQAEDETDWEALSHAGLDGTKNISWTDLETQTLIRIWGEDKTQRELRGVLQNGHIFAMISKKMSTHGYIRTAEQCQSRVKRLKLCFKQAYESKNIEGKEPAEFKFYKQMERIMANEEPCSSQIKEEESADIEYQVYKYQEIETAMNCMDDRKKVAWSDAETLILLQLWGNEQVQQNLQRCPHNGHIYSDISEKLNTHGYLRTAEQCHTRIKRLKISYRQCRDSISSPEAERVEFKFYDLMEDIFQRNASSKASGENEDDSCITSESQGSSAEQTSSWSDSETVALIDIWADDEVQEALRESVHNNHVFADIAEKLNSQGFFKTPEQCRWKIKNLSKNFRQCYERKKCGRENVDCKYYDKLEQVLGDEAFSMDVFEEDDQDADYQPTAMVAVSESGRKMTWSDQETLALLEIWGDDRVQHSLMSCPKNRHIYRYISKRMIALGFNRTGVQCHSRIKRLKSQFYYDGREECKFYDQLEKILLKDRTSEDKEMSELESITDSDSDSLALSKPLTTDGPKLAWGDSETHTLISIWGSDGIQERLKGCVKRKPVFQQIALIMAEKGYSRTDEQCRSRIKRLKASYRQHLDNYRNEGEQVEWKFYKQLNKIFQKYPLDDTETTVQETKAVWRKNPSRSAKAHSSD
Protein: Exocyst complex component EXO70 (Exocyst complex protein of 70 kDa) (P19658)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in the assembly of the exocyst.
Subcellular location: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:15583031}. Bud {ECO:0000269|PubMed:15788396}. Bud neck {ECO:0000305}. Note=Its polarization in the cell depends on EXO84. {ECO:0000269|PubMed:15788396}.
Interaction partners:
- Exocyst complex component SEC6
- Exocyst complex component SEC5
- Exocyst complex component SEC15
- Exocyst complex component SEC8
- Exocyst complex component SEC3
- Exocyst complex component SEC10
- Exocyst complex component EXO84
- GTP-binding protein RHO3
- Cell division control protein 42
- Ras-related protein SEC4
Sequence:
MPAEIDIDEADVLVLSQELQKTSKLTFEINKSLKKIAATSNQSSQLFTPILARNNVLTTLQRNIESTLNSVASVKDLANEASKYEIILQKGINQVGLKQYTQVVHKLDDMLEDIQSGQANREENSEFHGILTHLEQLIKRSEAQLRVYFISILNSIKPFDPQINITKKMPFPYYEDQQLGALSWILDYFHGNSEGSIIQDILVGERSKLILKCMAFLEPFAKEISTAKNAPYEKGSSGMNSYTEALLGFIANEKSLVDDLYSQYTESKPHVLSQILSPLISAYAKLFGANLKIVRSNLENFGFFSFELVESINDVKKSLRGKELQNYNLLQDCTQEVRQVTQSLFRDAIDRIIKKANSISTIPSNNGVTEATVDTMSRLRKFSEYKNGCLGAMDNITRENWLPSNYKEKEYTLQNEALNWEDHNVLLSCFISDCIDTLAVNLERKAQIALMPNQEPDVANPNSSKNKHKQRIGFFILMNLTLVEQIVEKSELNLMLAGEGHSRLERLKKRYISYMVSDWRDLTANLMDSVFIDSSGKKSKDKEQIKEKFRKFNEGFEDLVSKTKQYKLSDPSLKVTLKSEIISLVMPMYERFYSRYKDSFKNPRKHIKYTPDELTTVLNQLVR
Protein: Uncharacterized protein (Q38EH5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGNQKAVAGRQDATLSSAAGTKHSAKLPPLLAPLTRVITLEMIWYLLCHIVCLFTLIFGAGDELFTSRKRWFALGLTKQPQRREYSAGGVYEMFATKATIENKPMLPPHRLNSDLVLSLLFVLTFNGFFLALSRSVSRLIAEGDERREFREGTFDIKSGTDDKVSKGKGVPFRLINCREIMYKVTLGATLVFCVLITTCVILQPPSEVQGAAPSLVLLSSVVPIYYGDRPNGARALERFYSAYQSVIITVLVGLVLDANFLAKA
Protein: Deoxyribonuclease gamma (DNase gamma) (EC 3.1.21.-) (DNase I homolog protein DHP2) (Deoxyribonuclease I-like 3) (DNase I-like 3) (Liver and spleen DNase) (LS-DNase) (LSD) (O55070)
Organism: Mus musculus (Mouse)
Function: Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends (By similarity). Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA. Acts in internucleosomal DNA fragmentation (INDF) during apoptosis and necrosis. The role in apoptosis includes myogenic and neuronal differentiation, and BCR-mediated clonal deletion of self-reactive B cells. Is active on chromatin in apoptotic cell-derived membrane-coated microparticles and thus suppresses anti-DNA autoimmunity. Together with DNASE1, plays a key role in degrading neutrophil extracellular traps (NETs). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation. Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q13609, ECO:0000269|PubMed:12050166}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13609}. Secreted {ECO:0000269|PubMed:12095301, ECO:0000269|PubMed:15796714, ECO:0000269|PubMed:27293190}. Note=Contradictory reports exist about the subcellular localization under normal physiological conditions. Shown to translocate to rough endoplasmic reticulum and to be transported through the entire secretory pathway for secretion. However, under conditions of cell death, may diffuse and/or be actively transported to the nucleus. {ECO:0000305|PubMed:15796714, ECO:0000305|PubMed:27293190}.
Interaction partners:
- Deoxyribonuclease-2-alpha
Sequence:
MSLHPASPRLASLLLFILALHDTLALRLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSRRSTTYNYVISSRLGRNTYKEQYAFVYKEKLVSVKTKYHYHDYQDGDTDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKEIDELVDVYTDVRSQWKTENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTVKKSTSCAYDRIVLCGQEIVNSVVPRSSGVFDFQKAYDLSEEEALDVSDHFPVEFKLQSSRAFTNNRKSVSLKKRKKGNRS
Protein: Cilia- and flagella-associated protein 299 (Q810M1)
Organism: Mus musculus (Mouse)
Function: May be involved in spermatogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30820741}. Nucleus {ECO:0000269|PubMed:30820741}. Note=Mainly cytoplasmic. {ECO:0000269|PubMed:30820741}.
Interaction partners:
- Cilia-and flagella-associated protein 96
- Uncharacterized protein C4orf36 homolog
- Cilia- and flagella-associated protein 184
Sequence:
MDQDEGLTAVDNIVTQFNTYEDFLDSQITTVDLYYLEDESLARQLVELGYRGTGEIVKREDFEARKAAINIARQAERTQKKTLTSAGKELHDDFLKALAMREEDNRAGKLSTVIFIRDRNPHGQEVSGYIDYAHRLKSEDFEVYFNGKRRLLPRTTDMSFYNWDSHIAVCNSSPNYQVIADNPEGLLFKYKRDRKILNVDPKAHPGDNSTRIPIQTDLYAHVVLFDHVSRRKT
Protein: Decoration protein gp12 (Gene product 12) (gp12) (Q38581)
Organism: Bacillus phage SPP1 (Bacteriophage SPP1)
Function: Decoration protein that binds to each capsid protein hexamer after capsid expansion and forms spikes at the surface of the capsid. Each of the 60 hexamers has three copies of the decoration protein gp12 in its center.
Subcellular location: Virion {ECO:0000269|PubMed:22514336}. Note=180 copies of the decoration protein are localized on the exterior of the capsid. {ECO:0000269|PubMed:22514336}.
Interaction partners:
Sequence:
MSKRIPRFLRNIQLPAGPQGPKGDPGPKGDTGAKGADGFGTEAQYNDIISRLEALEQSSGGGTT