wanglab/gogpt-training-data huggingface dataset:
Protein: Aminotransferase tdiD (EC 2.6.1.28) (Terrequinone biosynthesis protein D) (A7XRY8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Aminotransferase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent. The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD. The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules. The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain. TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1. Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5.
Interaction partners:
- monoamine oxidase
- Amine oxidase
- Probable methyltransferase tdiE
- Aromatic-amino-acid transaminase, hypothetical
- aromatic-amino-acid transaminase
- Aromatic-L-amino-acid decarboxylase, putative
- Indoleamine 2,3-dioxygenase
- Indoleamine 2,3-dioxygenase
- Tryptophan synthase
- tryptophan synthase
Sequence:
MGSIGANNAVADPTPLFSSRVQKWEPGAIRSLLPLEALPGMISLVAGKPSPETFPIAEIAISLKDTPAGTGRIVVDGDELNQALQYGLPRGNAQLIQWFESLQRSVHGLDENGGWSCCIGNGSQELIHRVIQVFTDPGDPVLLETPAYPGVAGFLRADGQELIPVYSDAQGLNPASLEQALSEWPGDSPRPKVLYTTPTGSNPTGQSCTESRKAEILRLAKRFNFIILEDDAYYYLNYGDDKQRARSYLALERDVNGESGRVVRFDSLSKIVSPGMRLGILTAQAAVVDKVVRITENINLQPSSTTQLLALSLLRHWGQAGFLKHCAEAAEVYRRRRDVFVSAAERHLQGRATWVVPTAGMFVWLELKLPPEMDSFELLKSQGMKNGVLAIPGVAFMPGNEQTCYIRVSFSLVPERDMDEACRRIAGLVDRCACHS
Protein: Dynamin-like GTPase OPA1, mitochondrial (EC 3.6.5.5) (A1Z9N0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
- Transmembrane GTPase Marf
- Serine/threonine-protein kinase Pink1, mitochondrial
- Mitochondrial fission 1 protein
- E3 ubiquitin-protein ligase parkin
- Presenilins-associated rhomboid-like protein, mitochondrial
- Transmembrane GTPase fzo
- Transport and Golgi organization protein 11
- ATP-dependent zinc metalloprotease YME1L
- Cytochrome c-1
- Cytochrome c-2
Sequence:
MLRIYQNTYRRTARKAVVYSTKVACCNHSTLCGITSHPRRAQDSGSSSSNGRHRGHEEFLLAGNPARGWQMPPPSRGYGMLVVRILRGALKLRYIVLGGAIGGGVSLSKKYEEWKDGLPNFKWLEDAMPQGERWSQFSRNLIEVGSLVKNAIEVDPKLKQLGEDKLSEWRNWFDSRLDDAIEAADYQGVQIVETKDDLKAKTTVAALGITSDESRKKYEKLQSQVETLQTEIMNVQIKYQKELEKMEKENRELRQQYLILKTNKKTTAKKIKKSLIDMYSEVLDELSGYDTGYTMADHLPRVVVVGDQSSGKTSVLESIAKARIFPRGSGEMMTRAPVKVTLAEGPYHVAQFRDSDREYDLTKESDLQDLRRDVEFRMKASVRGGKTVSNEVIAMTVKGPGLQRMVLVDLPGIISTMTVDMASDTKDSIHQMTKHYMSNPNAIILCIQDGSVDAERSNVTDLVMQCDPLGRRTIFVLTKVDLAEELADPDRIRKILSGKLFPMKALGYYAVVTGRGRKDDSIDAIRQYEEDFFKNSKLFHRRGVIMPHQVTSRNLSLAVSDRFWKMVRETIEQQADAFKATRFNLETEWKNNFPRLRESGRDELFDKAKGEILDEVVTLSQISAKKWDDALSTKLWEKLSNYVFESIYLPAAQSGSQNSFNTMVDIKLRQWAEQALPAKSVEAGWEALQQEFISLMERSKKAQDHDGIFDQLKSAVVDEAIRRHSWEDKAIDMLRVIQLNTLEDRFVHDKQEWDSAVKFLESSVNAKLVQTEETLAQMFGPGQMRRITHWQYLTQDQQKRRSVKNELDKILKNDTKHLPTLTHDELTTVRKNLQRDNVDVDTDYIRQTWFPVYRKHFLQQALQRAKDCRKAYYLYTQQGAECEISCSDVVLFWRIQQVIKITGNALRQQVINREARRLDKEIKAVLDEFSDDEEKKGYLLTGKRVLLAEELIKVRQIQEKLEEFINSLNQEK
Protein: Chromatin structure-remodeling complex subunit SFH1 (RSC complex subunit SFH1) (SNF5 homolog 1) (Q06168)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is essential for mitotic growth and required for cell cycle progression.
Subcellular location: Nucleus {ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.
Interaction partners:
- Nuclear protein STH1/NPS1
- Chromatin structure-remodeling complex subunit RSC2
- Chromatin structure-remodeling complex subunit RSC4
- Chromatin structure-remodeling complex protein RSC8
- Chromatin structure-remodeling complex protein RSC6
- Chromatin structure-remodeling complex subunit RSC9
- Chromatin structure-remodeling complex protein RSC3
- Chromatin structure-remodeling complex subunit RSC7
- Actin-related protein 7
- Actin-like protein ARP9
Sequence:
MSHQNQLIPQAYISNFHNRLTNEDDGIPIFTMAQQTRQHKRAKVVNYAEYDNDLFDEFNMNGSNFNNADTHYKDNAVSHENTPALTNGVTMDGSEYNVLENMNGADSIISNNKYDAGSNMVVESLSGLNSNNNASNGPSNKAQAQDIGNAVLPDLQDQHHNPFNILRYPKIRDTFINGKVVSPYRLNTDQETKANANSGEAIMIPITLDIEHMGHTIKDQFLWNYNDDSISPEEFASIYCKDLDMTSATLQTQIANIIKEQLKDLENIAATEIMSDLHVIINLTCNLQDRFFEDNFQWNLNDKSLTPERFATSIVQDLGLTREFIPLISQSLHETILKIKKDWVDGHLIQDHVPNDAAFGYLSGIRLDIDELGSNWCPRVEILTKEEIQKREIEKERNLRRLKRETDRLSRRGRRRLDDLETTMRM
Protein: Trifunctional enzyme subunit beta, mitochondrial (TP-beta) [Includes: 3-ketoacyl-CoA thiolase (EC 2.3.1.155) (EC 2.3.1.16) (Acetyl-CoA acyltransferase) (Beta-ketothiolase)] (Q99JY0)
Organism: Mus musculus (Mouse)
Function: Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA thiolase activity.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P55084}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P55084}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P55084}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P55084}. Note=Protein stability and association with membranes require HADHA. {ECO:0000250|UniProtKB:P55084}.
Interaction partners:
- Trifunctional enzyme subunit alpha, mitochondrial
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal bifunctional enzyme
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MTTILTSTFRNLSTTSKWALRSSIRPLSCSSQLHSAPAVQTKSKKTLAKPNMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSDIVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYPK
Protein: Secreted phosphoprotein 24 (Spp-24) (Secreted phosphoprotein 2) (Q62740)
Organism: Rattus norvegicus (Rat)
Function: Could coordinate an aspect of bone turnover.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Insulin-like growth factor-binding protein 1
- Alpha-2-HS-glycoprotein
- Beta-2-glycoprotein 1
- Apolipoprotein M
Sequence:
MELATMKTLVMLVLGMHYWCASGFPVYDYDPSSLQEALSASVAKVNSQSLSPYLFRATRSSLKRVNVLDEDTLVMNLEFTVQETTCLRESGDPSTCAFQRGYSVPTAACRSTVQMSKGQVKDVWAHCRWASTSESNSSEEMIFGDMARSHRRRNDYLLGFLYDEPKGEQFYDRSIEITRRGHPPAHRRFLNLQRRARVNSGFE
Protein: GTPase Era (Bex protein) (P42182)
Organism: Bacillus subtilis (strain 168)
Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (By similarity). Binds both GDP and GTP. Complements an E.coli era disruption mutant.
Subcellular location: Cytoplasm. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Endoribonuclease YbeY
- Cytidine deaminase
- Ribonuclease 3
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS9
- DNA repair protein RecO
- DEAD-box ATP-dependent RNA helicase CshA
- Small ribosomal subunit protein uS10
Sequence:
MTNESFKSGFVSIIGRPNVGKSTFLNRVIGQKIAIMSDKPQTTRNKVQGVLTTGTSQTIFIDTPGIHKPKHKLGDFMMKVAQNTLKEVDLILFMINAEEGYGKGDEFIIEKLQTMSTPVFLIVNKIDKIHPDQLLLLIDEYRKRYPFKEIVPISALEGNNIETLLAQIEAYLPEGPQFYPSDQVTDHPERFIISELIREKVLHLTREEIPHSIAVAIESIKGQDNGSVHVAATIVVERDSQKGIVIGKKGSLLKEVGKRARADIEALLGSRVYLELWVKVQKDWRNKMSQLRDFGFKEDEY
Protein: Ribonuclease L (G3V915)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- ATP-dependent RNA helicase DHX33
- ATP-binding cassette sub-family E member 1
- Interferon-induced, double-stranded RNA-activated protein kinase
- Endoplasmic reticulum chaperone BiP
- 2'-5'-oligoadenylate synthase 2
- 2'-5'-oligoadenylate synthase 1A
- WD repeat-containing protein 90
- Ankyrin repeat domain 45
- 2'-5'-oligoadenylate synthase-like protein 1
- 2'-5' oligoadenylate synthase
Sequence:
METTDHSTPQCGSASAGGQKTVGKDDYLLIEAVNKGDADRVQQLLEQGADANVCEESGGWTPLHNAVQSGRVDIVNLLLRYGADPHRRKKNGATPFIIAGICGDVSLLQIFLSRGANINERDMHGFTAFMEAAEYGNVEALKFLFAEGADVNLRRETTEDRRRLKQGGATALMSAAENGHPEVVRILLDEMKAEADARDNMGRNALIRSLLNRDCENVEIHVEEITSVLIQYGADINVRGEGEKTPLISAVERKHTGLVQMLLSQEGIKVNDRDSEGKTALQIAVELKLKEIVRLLLEKGADTKCGDLVWIAKRNYDHGLVKLLLSYEANHDTNPPAKDWLPHSARWGEDLKRLHSVSRPMIGKLKIFMNDAYKIASTSEGGIYLGIYDNREVAVKVFCENSSRGRKEVACLRDCGDHSNLLTFYGSEEHKGNLYVCVSLCESTLEKFLNVPREEPMEKGEDKFALSVLLSIFKGVQKLHMHGYSHQNLQPPNILIDSEKAVRLADFDESIQWMRESQTVQRDLEDLGRLVLYVVNKGEIPFETLKGQNDEELLTIAPNEETKDLVHCLFSPGENVKNCLMDLLGHPFFWTWENRYRTLRDVGNESDIKVRNNKSKLLKLLQPQTHAPSRSFDRWTSKIDKRVMSDMNGFYKSRKGYRDTVGDLLKFIRNIGEHINEEKNRQMKEILGDPSRYFQETFPDLVIYIYKKLKETEFRKHFPQPPPSLSVPEAAGPGGVQS
Protein: Peroxisomal membrane protein PEX16 (D3ZGV2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Peroxisome membrane {ECO:0000256|RuleBase:RU365003}.
Interaction partners:
Sequence:
MRKLGGNLDLPFKVASPIPTSCLSWCTLPLTCLCCSMTGSFGRSFEKLPVSLSQQKLLTWLSVLECVEVFMEMGAAKVWGEVGRWLVIALIQLAKAVLRMFLLIWFKTGIQTSPPIVPLDRETQAQPLDGDHNLGSPEPSYVGKRSNRVVRTLQNSPSLHSRHWGAPQQREIRQKQQQEELSTPPTPLGLQETIAESLYIARPLLHLLSLGLWGQRSWAPWLLSGVVDMTSLSLLSDRKNLTRRERLELRRRTILLLYYLLRSPFYDRFSEAKILFLLQLLADHIPGIGLVARPLMDYLPSWQKIYFYSWG
Protein: Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1) (Liver FBPase) (A0A060XAF0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- malate synthase
- Ribulose-phosphate 3-epimerase
- transketolase
- Transketolase N-terminal domain-containing protein
- Transketolase-like pyrimidine-binding domain-containing protein
- transketolase
- Transketolase
- transketolase
- Transketolase N-terminal domain-containing protein
- Transaldolase
Sequence:
MSERCAFDTNVVTLTRFVQEEGRKAKGTGELTTLLNSICTAVKAISTAVRKAGIANLYGIAGSTNVTGDQVKKLDVLSNDMVINMIKSSFTSCVLVSEENERALIVEPEKRGKYIVCFDPLDGSSNIDCLVSIGTIFAIYRKTTDDEPNEKDALQSGRHIVAAGYALYGSATMMVLSTGQGVNCFMLDPSIGEFILTDKDVKIKKRGKIYSLNEGYAQHFYPDITEYLKKKKYPEDGSAPYGGRYVGSMVADVHRTLVYGGIFLYPANVKSPKGKLRLLYECNPMSFIIEQAGGMATTGEMNVLDIKPENIHQRVPVVLGSPEDVQEYIAIYKKTRM
Protein: CD59B glycoprotein (MAC-inhibitory protein) (MAC-IP) (Membrane attack complex inhibition factor) (MACIF) (Protectin) (CD antigen CD59) (P58019)
Organism: Mus musculus (Mouse)
Function: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (By similarity).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Complement decay-accelerating factor, GPI-anchored
- Complement decay-accelerating factor transmembrane isoform
- Membrane cofactor protein
- Complement component C9
- CD59A glycoprotein
- Complement C5
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Vitronectin
- Complement factor H
- Complement component C8 beta chain
Sequence:
MRAQRGLILLLLLLAVFCSTAVSLKCYNCLDPVSSCKINTTCSPNLDSCLYAVAGRQVYQQCWKLSDCNSNYIMSRLDVAGIQSKCCQWDLCNKNLDGLEEPNNAETSSLRKTALLGTSVLVAILKFCF
Protein: 5'-3' exoribonuclease 1 (EC 3.1.13.-) (Q9XZU2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR006743}.
Interaction partners:
Sequence:
MGVPKFFRYISERYPCLSELAREHCIPEFDNLYLDMNGIVHNCSHPDDNNIHFHLEEEQIFQEIFNYVDKLFYLIKPQRLFFLSVDGVAPRAKMNQQRSRRFRTAREAEQQEAKAAQRGELREHERFDSNCITPGTEFMVRLQEGLRAFLKTKISTDPLWQRCTVILSGQEAPGEGEHKIMDYIRYMKTQPDYDPNTRHCLYGLDADLIILGLCTHELHFVVLREEVKFGRNVKRTSVEETRFFLLHLGLLREYLELEFDALRTDEHKLDIAQLIDDWVLMGFLVGNDFIPHLPCLHISSNALPLLYRTYIGIYPTLGGNINENGKLNLRRLQIFISALTEVELDHFKEHADDLKYMNNKSEAFDMDVGEITESQNLDSDLGALINKSMLLYDDDSEEDCSDENAVLLKEFQNYKRNFYRNKFKRDPNDELIEELCHHYVNALQWVLDYYYRGVQSWDWYYPFHYTPFISDLKNIEQVEIAFHMGTPFLPFQQLLAVLPAASAKLLPVAYHDLMLLPTSPLAEFYPLEFESDLNGKKHDWEAVVLIPFIDEGRLLAAMLPCEAQLSLEERERNRHGPMYVYKYSTVAQGPMPAYPPLRALPVLYCTEVAKWSHEIAVNLPYSVCIELPNAARTVFFPGFPTMQHLPFDFELRNDRVKVFEQVSRNQNIVLKPRKRQLEDTLTAVASQYLGKVIHVGWPHLVKAIVVRVATRDQRVDSEGITLNDSRRFDSECKALQEHFITRMGIQFANYDVLVYVRTFAGNSTEFRDKGALMVRDSWSSSVTGYPAQGVVADLTVWERMRKNFLNVEHYFPVGSTIFLITDPYYGSEGTVQDPRLAYTNGRIQVSIMVRPEPKVNAARQLQEERDRDYLSTFQVCNLLRISGRTLGRLSGTVWVVLGPRRQKMENVDQAQHWPAAQVSAAERGACRILLPHEQPVVLLQPGRGSDAQLLPALPRRYRLLWRLQRSRRVRIRTGRVPQCGWPSPRRGMANWVRQQPHMKVERISCGSKTVCRETIELLIAAVDELRSLPVKHVKLQVKPHLLIKPNVTLPDVYRSKRPVRLFDRVVIVRTIYMVPVGTKGTVIGIHPVTDPNPVRLECVHAVDTFCKVLFDSPVPNCNNIHGIAEDRVYKVPEIALVIIKTDEEGKKQNDCELPVRDPQPNQAQDEPVRATSSRYVTAAGSTSVPITMKTQISDEFVKTRSSPIARTDSYKPSSEPKPVPVPEQITNWRERVSTPTNKPQPAPNNWRINRSSSRQQGGSIFVAPPTKTPDAAASTASTAFTAASSATLTPLDQTLALMSVLGVGEDQSSPPLQEAVQQQRPPLLQQQRAPFPGQMPNLPKPPLFWQQEAQKQEALQQEAQQQEAQKKQQQAHAQMEPERINSQHFYRSGQTGAALNQPPLGAPSKRQWHEWVHPRMQHANAFHAGVNNGYQMRPKKNIAAQSTFNNNVHMHLQQPYYPNQQQQQQQQQPLQLTEINNAPPRYSTIQDFVPIQAYRPKKLNRVQPAGRQDVDATKNPSRSPVLQQPTNETIDTKASSSLPVQSAGEQVIGLMQTLEIKQPAASQSESDGVSTGSANAPTATTSSQAVNRRKHRVPRIGAKFDLEYILPDSPHPT
Protein: Jim, isoform F (M9PGG2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAINFSASFAACIAAGLKVPRQIMYCITQDTGQPYVLYKDSQDAERNPGAIGATPAQWGSEMYPNIQQQAQQHLTAQQQQQQQQQNAAQAAAQAAAVAAAAGQPQSPPGGGQEARDNGSGDGRQQQVSPSSSPYPSVQQQQRANGAGDEDPMNHQLANQQNPAPNQNQSSNDPQHSGSNAGESGNPHVQQNGGPQNDPGNSFRTPDYYDPRHAAPQGGMLAPPGFPPLHYLNKGVLPMEQSGGGGGAGGGEAYALPEMLPAQQNGQQNAGPANTNANEGGAGANGSGGVGGATGASVGVGSVGVTSGGRTGNGPGRPHKNKPHSDLRLFKCLTCGKDFKQKSTLLQHDRIHTDARPFPCSECGKRFRQQSHLTQHLRIHANEKPFTCPYCSRSFRQRAILNQHIRIHSGEKPFACPECGKHFRQKAILNQHVRTHQDVSPHLIFKNGPHPTLWPSDVPFPGEDNDTKGDIAGTGGGYHDEDSQGTPDGSGGMHYPSYFKDGKGQKILPEVLQHIGVRPANMPLYVRCPICDKEFKQKTTLLQHGCIHIESRPYPCPECGKRFRQQSHLTQHLRIHTNEKPFGCMYCPRFFRQRTILNQHLRIHTGEKPYKCGQCGKDFRQKAILDQHTRTHQGDRPFCCPMPNCRRRFATENEVTKHIDNHMNPNTTKVRRQQQQQHQQQQQQQQQQQQQQQQQNNNAVAQVANHLMNDAKSLAAQQFLNNNNPSAVDNKANILPVRSIASNAAAAAVVQQSVVKNELYFPQCYGPPFQHPFQAQQQQAQQPSVAHANGGPTPPVTVTVANSVASGVVVQQNASASVVAQXHPTTAATGAQQQQPSAPQQQHHPPPPPPTSTAHHIASAAAAVTAVTPSSAHASPVAAPQTVTLSITLPPPPASHTVHPGHPGHPGHPGVANGAAPPPPTLSHAIPIHPHIHSIFGSL
Protein: Mitochondrial dynamics protein MIEF1 (Mitochondrial dynamics protein of 51 kDa) (Mitochondrial elongation factor 1) (Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like) (SMCR7-like protein) (Q9NQG6)
Organism: Homo sapiens (Human)
Function: Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization. Binds ADP and can also bind GDP, although with lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity and the assembly of DNM1L into long, oligomeric tubules with a spiral pattern, as opposed to the ring-like DNM1L oligomers observed in the absence of bound ADP. Does not require ADP for its function in recruiting DNM1L.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:24515348}; Single-pass membrane protein {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:24515348}.
Interaction partners:
- Dynamin-1-like protein
- Density-regulated protein
- Mitochondrial fission factor
- Mitochondrial fission 1 protein
- Mitofusin-1
- Mitofusin-2
- WD repeat-containing protein 90
Sequence:
MAGAGERKGKKDDNGIGTAIDFVLSNARLVLGVGGAAMLGIATLAVKRMYDRAISAPTSPTRLSHSGKRSWEEPNWMGSPRLLNRDMKTGLSRSLQTLPTDSSTFDTDTFCPPRPKPVARKGQVDLKKSRLRMSLQEKLLTYYRNRAAIPAGEQARAKQAAVDICAELRSFLRAKLPDMPLRDMYLSGSLYDDLQVVTADHIQLIVPLVLEQNLWSCIPGEDTIMNVPGFFLVRRENPEYFPRGSSYWDRCVVGGYLSPKTVADTFEKVVAGSINWPAIGSLLDYVIRPAPPPEALTLEVQYERDKHLFIDFLPSVTLGDTVLVAKPHRLAQYDNLWRLSLRPAETARLRALDQADSGCRSLCLKILKAICKSTPALGHLTASQLTNVILHLAQEEADWSPDMLADRFLQALRGLISYLEAGVLPSALNPKVNLFAELTPEEIDELGYTLYCSLSEPEVLLQT
Protein: POU domain, class 2, transcription factor 1 (NF-A1) (Octamer-binding protein 1) (Oct-1) (Octamer-binding transcription factor 1) (OTF-1) (P14859)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR.
Subcellular location: Nucleus.
Interaction partners:
- POU domain class 2-associating factor 1
- Host cell factor 1
- POU domain, class 2, transcription factor 2
- POU domain, class 2, transcription factor 3
- Transcription factor SOX-2
- Breast cancer type 1 susceptibility protein
- Histone acetyltransferase p300
- Transcription factor Sp1
- Host cell factor 2
- X-ray repair cross-complementing protein 6
Sequence:
MNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTNLQPAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQPATPTRTIAATPIQTLPQSQSTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENLSSDSSLSSPSALNSPGIEGLSRRRKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQKEKRINPPSSGGTSSSPIKAIFPSPTSLVATTPSLVTSSAATTLTVSPVLPLTSAAVTNLSVTGTSDTTSNNTATVISTAPPASSAVTSPSLSPSPSASASTSEASSASETSTTQTTSTPLSSPLGTSQVMVTASGLQTAAAAALQGAAQLPANASLAAMAAAAGLNPSLMAPSQFAAGGALLSLNPGTLSGALSPALMSNSTLATIQALASGGSLPITSLDATGNLVFANAGGAPNIVTAPLFLNPQNLSLLTSNPVSLVSAAAASAGNSAPVASLHATSTSAESIQNSLFTVASASGAASTTTTASKAQ
Protein: DEAD-box ATP-dependent RNA helicase CshA (EC 3.6.4.13) (P96614)
Organism: Bacillus subtilis (strain 168)
Function: The most abundant DEAD-box RNA helicase. An ATP-dependent RNA helicase with RNA-dependent ATPase activity. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures. In vitro, unwinds dsRNA in both 5'- and 3'- directions. Plays a role in ribosomal 50S subunit assembly. Its deletion leads to changes in mRNA levels for over 200 transcripts.
Subcellular location: Cytoplasm, nucleoid. Cell membrane. Note=Shows transcription-dependent localization at subcellular sites surrounding the nucleoid (PubMed:16352840). Associated with free 50S ribosomal subunit, 70S ribosome and polysomes (PubMed:16861794). Cell membrane association shown in (PubMed:20572937). {ECO:0000269|PubMed:16352840, ECO:0000269|PubMed:16861794, ECO:0000269|PubMed:20572937}.
Interaction partners:
- Polyribonucleotide nucleotidyltransferase
- Ribonuclease Y
- Ribonuclease J1
- ATP-dependent 6-phosphofructokinase
- Ribonuclease J2
- ATP-dependent RNA helicase DbpA
- Ribonuclease P protein component
- GTPase Era
- Elongation factor G
- Peptidyl-prolyl cis-trans isomerase B
Sequence:
MTITFQDFNLSSDLMKAINRMGFEEATPIQAQTIPLGLSNKDVIGQAQTGTGKTAAFGIPLVEKINPESPNIQAIVIAPTRELAIQVSEELYKIGQDKRAKVLPIYGGQDIGRQIRALKKNPNIIVGTPGRLLDHINRRTIRLNNVNTVVMDEADEMLNMGFIDDIESILSNVPSEHQTLLFSATMPAPIKRIAERFMTEPEHVKVKAKEMTVSNIQQFYLEVQERKKFDTLTRLLDIQSPELAIVFGRTKRRVDELAEALNLRGYAAEGIHGDLTQAKRMVALRKFKEGAIEVLVATDVAARGLDISGVTHVYNFDVPQDPESYVHRIGRTGRAGKTGMAMTFITPREKSMLRAIEQTTKRKMDRMKEPTLDEALEGQQQVTVERLRTTISENNLNFYMTAAAELLEDHDAVTVVAAAIKMATKEPDDTPVRLTDEAPMVSKRYKNQRSSKRRDGQGGGYRGGKGKSNNRSSYDKKRSNDRRSSGDRRQKKSY
Protein: N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase (N-acetylglucosaminyltransferase) (EC 2.4.1.150) (I-branching enzyme) (IGNT) (Q8N0V5)
Organism: Homo sapiens (Human)
Function: Branching enzyme that converts linear into branched poly-N-acetyllactosaminoglycans. Introduces the blood group I antigen during embryonic development. It is closely associated with the development and maturation of erythroid cells.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- Galactoside alpha-
- Type 2 lactosamine alpha-2,3-sialyltransferase
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
- Beta-1,4-galactosyltransferase 1
- Galactoside alpha-
- Beta-1,4-galactosyltransferase 4
- Alpha-
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6
Sequence:
MMGSWKHCLFSASLISALIFVFVYNTELWENKRFLRAALSNASLLAEACHQIFEGKVFYPTENALKTTLDEATCYEYMVRSHYVTETLSEEEAGFPLAYTVTIHKDFGTFERLFRAIYMPQNVYCVHLDQKATDAFKGAVKQLLSCFPNAFLASKKESVVYGGISRLQADLNCLEDLVASEVPWKYVINTCGQDFPLKTNREIVQYLKGFKGKNITPGVLPPDHAVGRTKYVHQELLNHKNSYVIKTTKLKTPPPHDMVIYFGTAYVALTRDFANFVLQDQLALDLLSWSKDTYSPDEHFWVTLNRIPGVPGSMPNASWTGNLRAIKWSDMEDRHGGCHGHYVHGICIYGNGDLKWLVNSPSLFANKFELNTYPLTVECLELRHRERTLNQSETAIQPSWYF
Protein: Major mite allergen Der p 23 (Major house dust mite allergen Der p 23) (Major HDM allergen Der p 23) (Peritrophin-like protein Der p 23) (allergen Der p 23) (L7N6F8)
Organism: Dermatophagoides pteronyssinus (European house dust mite)
Function: Does not bind chitin in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:23460742}. Endoplasmic reticulum {ECO:0000269|PubMed:23460742}. Cytoplasmic vesicle {ECO:0000269|PubMed:23460742}. Note=Localizes to the peritrophic matrix ligning the midgut and on the surface of fecal pellets. {ECO:0000269|PubMed:23460742}.
Interaction partners:
Sequence:
MKFNIIIVFISLAILVHSSYAANDNDDDPTTTVHPTTTEQPDDKFECPSRFGYFADPKDPHKFYICSNWEAVHKDCPGNTRWNEDEETCT