wanglab/gogpt-training-data huggingface dataset:
Protein: Protein smoothened (dSMO) (SMOH) (Smooth) (P91682)
Organism: Drosophila melanogaster (Fruit fly)
Function: Segment polarity protein required for correct patterning of every segment. G protein-coupled receptor that associates with the patched protein (ptc) to transduce the hedgehog (hh) signal through the activation of an inhibitory G-protein. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a hh-signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15616566}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium {ECO:0000269|PubMed:24768000}.
Interaction partners:
- Protein patched
- Kinesin-like protein costa
- Protein hedgehog
- Suppressor of fused homolog
- cAMP-dependent protein kinase catalytic subunit 1
- G protein-coupled receptor kinase 2
- cAMP-dependent protein kinase catalytic subunit 2
- Transcriptional activator cubitus interruptus
- Serine/threonine-protein kinase fused
- Kurtz arrestin
Sequence:
MQYLNFPRMPNIMMFLEVAILCLWVVADASASSAKFGSTTPASAQQSDVELEPINGTLNYRLYAKKGRDDKPWFDGLDSRHIQCVRRARCYPTSNATNTCFGSKLPYELSSLDLTDFHTEKELNDKLNDYYALKHVPKCWAAIQPFLCAVFKPKCEKINGEDMVYLPSYEMCRITMEPCRILYNTTFFPKFLRCNETLFPTKCTNGARGMKFNGTGQCLSPLVPTDTSASYYPGIEGCGVRCKDPLYTDDEHRQIHKLIGWAGSICLLSNLFVVSTFFIDWKNANKYPAVIVFYINLCFLIACVGWLLQFTSGSREDIVCRKDGTLRHSEPTAGENLSCIVIFVLVYYFLTAGMVWFVFLTYAWHWRAMGHVQDRIDKKGSYFHLVAWSLPLVLTITTMAFSEVDGNSIVGICFVGYINHSMRAGLLLGPLCGVILIGGYFITRGMVMLFGLKHFANDIKSTSASNKIHLIIMRMGVCALLTLVFILVAIACHVTEFRHADEWAQSFRQFIICKISSVFEEKSSCRIENRPSVGVLQLHLLCLFSSGIVMSTWCWTPSSIETWKRYIRKKCGKEVVEEVKMPKHKVIAQTWAKRKDFEDKGRLSITLYNTHTDPVGLNFDVNDLNSSETNDISSTWAAYLPQCVKRRMALTGAATGNSSSHGPRKNSLDSEISVSVRHVSVESRRNSVDSQVSVKIAEMKTKVASRSRGKHGGSSSNRRTQRRRDYIAAATGKSSRRRESSTSVESQVIALKKTTYPNASHKVGVFAHHSSKKQHNYTSSMKRRTANAGLDPSILNEFLQKNGDFIFPFLQNQDMSSSSEEDNSRASQKIQDLNVVVKQQEISEDDHDGIKIEELPNSKQVALENFLKNIKKSNESNSNRHSRNSARSQSKKSQKRHLKNPAADLDFRKDCVKYRSNDSLSCSSEELDVALDVGSLLNSSFSGISMGKPHSRNSKTSCDVGIQANPFELVPSYGEDELQQAMRLLNAASRQRTEAANEDFGGTELQGLLGHSHRHQREPTFMSESDKLKMLLLPSK
Protein: Zinc finger protein, putative (Q387V2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDPSRALQEGSEVSALNSTDNFQFPAQALTECTECNGDVAASSFARLSTDGEGGRASEKEGDSPDQMDNDNSEGGEFDIFEGVAPGVSKCSTPQTEGTYADRQPPQLSNALERETSQEINRIENKVDAVRIDSSTVNTSDDFISTVFDDVDRSPSPFIVLDHVEDGGCLTYQGTVDSAMLPLKEERARILQRLGMLRATEQSRRQQLCRKYEGEVNMRMVSLAVTAAEQIDAPYGNSTYLTSSSVVSTNLDTQHNEAEEREQEQDQDQVLPQDSRRGETTVTRGVMAGCSTTVSKEVTGSVREGASLVCDQVDNVESDEDEPHFTERLTMLDCMTQECYKGLVQEGEFFSGEAESMVSENSADTDSSGDGVHSRADNMTVCDSVDCNKLHTAPSEGFYIPVPMDRTGQVEYVFNGDDAQRRLKFRREEYELQRALGRVEGKIDALTACRLSKGIHYWQSDDSTDSCPRCGKVFSFTVRRHHCRRCGVLLCNDCCSQVGRDMYVQVRTSAVTSSDVGPSHGSSSSQRTTGNATDDAWLFGTCEPTGSGDTREKRPGSTPNSLQPNQTISDTWQYQGSSSNNNSLPNCICLPNNGRRDYRGRGGLKVRYVPWVRICNACYLVCLRARLGGNYKPILEDNRRRFHVLKEEEQSLLCINSTWEMRWAQLNVLKHVVIERTVHMAHDQVQQAVGVLSDWLQEWRLCLKP
Protein: Copper transport protein CTR3 (Copper transporter 3) (Q06686)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for high affinity copper (probably reduced Cu I) transport into the cell.
Subcellular location: Cytoplasmic vesicle membrane; Multi-pass membrane protein.
Interaction partners:
- Copper transport protein CTR2
- Metal-binding activator 1
- Cytochrome c oxidase copper chaperone
- Iron transport multicopper oxidase FET3
- Superoxide dismutase
- Low-affinity Fe
- Copper-transporting ATPase
- Ferric/cupric reductase transmembrane component 1
- Regulation of enolase protein 1
- Putative cystathionine beta-lyase
Sequence:
MNMGGSSSTAAKKATCKISMLWNWYTIDTCFIARSWRNDTKGKFAGSCIGCFALVVVAQWLTRFSRQFDVELLKRQKIKHLASYSPEEYVVKCGEEDAKSDIEELQGFYNEPSWKTTLISLQKSFIYSFYVWGPRRLNEPEDDLLKKVLSCCTLITPVDLYPTFLDHMIRVTIFVLQWGLSYIIMLLFMYYNGYIIISCLIGAIVGRFIFCYEPLGSLGANGSAQGTVSYDKESDDRKCCL
Protein: Protein SENSITIVE TO PROTON RHIZOTOXICITY 1 (Zinc finger protein STOP1) (Q9C8N5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor. Together with STOP2, plays a critical role in tolerance to major stress factors in acid soils such as proton H(+) and aluminum ion Al(3+). Required for the expression of genes in response to acidic stress (e.g. ALMT1 and MATE), and Al-activated citrate exudation.
Subcellular location: Nucleus {ECO:0000269|PubMed:19321711}.
Interaction partners:
- Aluminum-activated malate transporter 1
- Protein DETOXIFICATION 42
- Protein ALUMINUM SENSITIVE 3
- Probable manganese-transporting ATPase PDR2
- Multicopper oxidase LPR2
- Protein RAE1
- CBL-interacting serine/threonine-protein kinase 23
- Calmodulin-binding transcription activator 2
- Polygalacturonase inhibitor 1
- Probable WRKY transcription factor 46
Sequence:
METEDDLCNTNWGSSSSKSREPGSSDCGNSTFAGFTSQQKWEDASILDYEMGVEPGLQESIQANVDFLQGVRAQAWDPRTMLSNLSFMEQKIHQLQDLVHLLVGRGGQLQGRQDELAAQQQQLITTDLTSIIIQLISTAGSLLPSVKHNMSTAPGPFTGQPGSAVFPYVREANNVASQSQNNNNCGAREFDLPKPVLVDEREGHVVEEHEMKDEDDVEEGENLPPGSYEILQLEKEEILAPHTHFCTICGKGFKRDANLRMHMRGHGDEYKTAAALAKPNKESVPGSEPMLIKRYSCPFLGCKRNKEHKKFQPLKTILCVKNHYKRTHCDKSFTCSRCHTKKFSVIADLKTHEKHCGKNKWLCSCGTTFSRKDKLFGHIALFQGHTPAIPLEETKPSASTSTQRGSSEGGNNNQGMVGFNLGSASNANQETTQPGMTDGRICFEESFSPMNFDTCNFGGFHEFPRLMFDDSESSFQMLIANACGFSPRNVGESVSDTSL
Protein: Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit (Anaerobic formate dehydrogenase cytochrome b556 subunit) (Formate dehydrogenase-N subunit gamma) (FDH-N subunit gamma) (P0AEK7)
Organism: Escherichia coli (strain K12)
Function: Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:11884747}; Multi-pass membrane protein {ECO:0000269|PubMed:11884747}.
Interaction partners:
- Formate dehydrogenase, nitrate-inducible, major subunit
- Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit
- Formate dehydrogenase-O iron-sulfur subunit
- Formate dehydrogenase-O major subunit
- Formate dehydrogenase, cytochrome b556
- Formate dehydrogenase H
- Protein FdhE
- Anaerobic dimethyl sulfoxide reductase chain B
- Protein NrfC
- Selenocysteine-specific elongation factor
Sequence:
MSKSKMIVRTKFIDRACHWTVVICFFLVALSGISFFFPTLQWLTQTFGTPQMGRILHPFFGIAIFVALMFMFVRFVHHNIPDKKDIPWLLNIVEVLKGNEHKVADVGKYNAGQKMMFWSIMSMIFVLLVTGVIIWRPYFAQYFPMQVVRYSLLIHAAAGIILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYREIEKAEAKKESEEGI
Protein: Disks large-associated protein 2 (DAP-2) (PSD-95/SAP90-binding protein 2) (SAP90/PSD-95-associated protein 2) (SAPAP2) (P97837)
Organism: Rattus norvegicus (Rat)
Function: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9115257}; Peripheral membrane protein {ECO:0000269|PubMed:9115257}. Postsynaptic density {ECO:0000269|PubMed:9115257}. Synapse {ECO:0000269|PubMed:9115257}. Note=Postsynaptic density of neuronal cells.
Interaction partners:
- SH3 and multiple ankyrin repeat domains protein 3
- SH3 and multiple ankyrin repeat domains protein 2
- Disks large homolog 4
- SH3 and multiple ankyrin repeat domains protein 1
- Disks large homolog 2
- Disks large homolog 3
- Ras/Rap GTPase-activating protein SynGAP
- Disks large-associated protein 3
- Neuroligin-3
- SH3 and multiple ankyrin repeat domains protein 2-like.
Sequence:
MGTAQVLPGILQKHCCILPDRNTESQCTLCGEPEEEEGGDLAQPGLSFPGPAEEDIDQQYSWSPTQHFSEERYSPAPRNMKGLTGSRNQPQLCVGHTCGLSPTDECEHPHDHVRHGPDVRQPYLLSPAESCPMDHHRCSPRSSVHSECMMMPVMLGDHVSSSTFPRMHYSSHYDTRDDCATSHASTKVNRIPANLLDQFEKQLPLHRDGFHTLQYHRASAATEQRNESPGRIRHLVHSVQKLFTKSHSLEGSSKSNINGTKSEGRMDDHHQSHLSKHSKRSKSKERKPESKHKSGMSSWWSSDDNLDSDSTYRTPSVAHRHHMDHIPHCYPEALQSPFGDLSLKTSKSNSDVKCSACEGLALTPDTRYMKRSSWSTLTVSQAKEAYRKSSLNLDKPLVHPEIKPSLQPCHYLQVPQDDWGAYPTGGKEEEIPCRRMRSGSYIKAMGDEESGESDSSPKTSPTVALRPEPLLKSIIQRPLGDHQTQSYLQAATEVPVGHSLDPSVNYNSPKFRSRNQSYMRAVSTLSQASCVSQMSEAEVNGQFESVCESVFSEVESQAMDALDLPGCFRTRSHSYLRAIQAGYSQDDECIPVMTPSNMTSTIRSTAAVSYTNYKKTPPPVPPRTTSKPLISVTAQSSTESTQDAYQDSRAQRMSPWPQDSRGGLYNSMDSLDSNKAMNLALESAAAQRHAADTQSSSTRSIDKAVLVSKAEELLKSRCSSIGVQDSEFPDHQPYPRSDVETATDSDTESRGLREYHSVGVQVEDEKRHGRFKRSNSVTAAVQADLELEGFPGHVSMEDKGLQFGSSFQRHSEPSTPTQYGALRTVRTQGLFSYREDYRTQVDTSTLPPPDPWLEPSLDTVETGRMSPCRRDGSWFLKLLHTETKKMEGWCKEMEREAEENDLSEEILGKIRSAVGSAQLLMSQKFQQFYWLCQQNMDPSAMPRPTSQDLAGYWDMLQLSVEDVSMKFDELHQLKLNDWKIMESPERKEERKIPPPIPKKPPKGKFPITREKSLDLPDRQRQEARRRLMAAKRAASFRQNSATERADSIEIYIPEAQTRL
Protein: Cyclic AMP-dependent transcription factor ATF-6 beta (cAMP-dependent transcription factor ATF-6 beta) (Activating transcription factor 6 beta) (ATF6-beta) (Protein G13) (cAMP response element-binding protein-related protein) (Creb-rp) (cAMP-responsive element-binding protein-like 1) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 beta] (Q99941)
Organism: Homo sapiens (Human)
Function: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 beta), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11256944}; Single-pass type II membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription factor ATF-6 beta]: Nucleus {ECO:0000269|PubMed:11256944}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. {ECO:0000269|PubMed:11256944}.
Interaction partners:
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- Cyclic AMP-responsive element-binding protein 1
- DNA damage-inducible transcript 3 protein
- Wolframin
- Cyclic AMP-responsive element-binding protein 3-like protein 2
- Cyclic AMP-responsive element-binding protein 3-like protein 3
- Cyclic AMP-responsive element-binding protein 3-like protein 1
- Cyclic AMP-responsive element-binding protein 3-like protein 4
- Cyclic AMP-responsive element-binding protein 3
Sequence:
MAELMLLSEIADPTRFFTDNLLSPEDWGLQNSTLYSGLDEVAEEQTQLFRCPEQDVPFDGSSLDVGMDVSPSEPPWELLPIFPDLQVKSEPSSPCSSSSLSSESSRLSTEPSSEALGVGEVLHVKTESLAPPLCLLGDDPTSSFETVQINVIPTSDDSSDVQTKIEPVSPCSSVNSEASLLSADSSSQAFIGEEVLEVKTESLSPSGCLLWDVPAPSLGAVQISMGPSLDGSSGKALPTRKPPLQPKPVVLTTVPMPSRAVPPSTTVLLQSLVQPPPVSPVVLIQGAIRVQPEGPAPSLPRPERKSIVPAPMPGNSCPPEVDAKLLKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSELKLGSGNRKVVCIMVFLLFIAFNFGPVSISEPPSAPISPRMNKGEPQPRRHLLGFSEQEPVQGVEPLQGSSQGPKEPQPSPTDQPSFSNLTAFPGGAKELLLRDLDQLFLSSDCRHFNRTESLRLADELSGWVQRHQRGRRKIPQRAQERQKSQPRKKSPPVKAVPIQPPGPPERDSVGQLQLYRHPDRSQPAFLDAIDRREDTFYVVSFRRDHLLLPAISHNKTSRPKMSLVMPAMAPNETLSGRGAPGDYEEMMQIECEVMDTRVIHIKTSTVPPSLRKQPSPTPGNATGGPLPVSAASQAHQASHQPLYLNHP
Protein: E3 ubiquitin-protein ligase AIRP1 (EC 2.3.2.27) (Protein ABA INSENSITIVE RING PROTEIN 1) (AtAIRP1) (RING-type E3 ubiquitin transferase AIRP1) (Q93ZF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses E3 ubiquitin-protein ligase activity in vitro when associated with the E2 enzyme UBC8 in vitro. Plays combinatory roles with AIRP2 in the positive regulation of the abscisic acid-mediated drought stress response.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:20884812}.
Interaction partners:
- E3 ubiquitin-protein ligase AIRP2
- E3 ubiquitin-protein ligase SDIR1
- Probable pterin-4-alpha-carbinolamine dehydratase, chloroplastic
- E3 ubiquitin-protein ligase RHA2B
- E3 ubiquitin-protein ligase RHA2A
- RING/U-box superfamily protein
- E3 ubiquitin-protein ligase RZF1
- Probable E3 ubiquitin-protein ligase XERICO
- E3 ubiquitin protein ligase DRIP1
- E3 ubiquitin protein ligase DRIP2
Sequence:
MGCCCCLPSIPESSRTIDEHLPLSRATPSSLSNAYSSPLSPPIPLAITNINLQTSPPKLPRTQGNSSEASPGLTQVVPEKKTWHVDDLTDFELKKQYREAIDECPICLEEYEIDNPKLLTKCGHDFHLACILAWMERSEACPVCDKELVLTES
Protein: Glycerophosphodiester phosphodiesterase (EC 3.1.4.46) (Q8IM31)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase
- Malate:quinone oxidoreductase
- Vacuolar transporter chaperone, putative
Sequence:
MIYFLLFICIVSLLKTIEMSSPSASIVGHRGCGSSTAGGISRYPENSLFSFKKALDENVDGVELDVWLTKDNQVIVLHGTEDGLLGHTLLCNKDCENKNIEELNLDEIQKYHFKEPWILNHGKTFNENNYELNNNQKKYSSLTEQEKLEKENEYENFDKAYINLEEHEDIEKLINEKFLNNFYNLNNKNNYEEPINDTEYIEKEKKLFEEYNLDTNINTEEDYINSIKCSHCKDIYKKYMMPKTHYHLKKKQLLFKFISMFYHVPLLENLLNLYKNKLTYDIELKGNKEDLGLYILNILQNYKDYKFKFSSFNWLLQYNDIQEKIHKQENNNSFNYEAYPFYNVDRIDLLKVLRNNKLNIPVALLFSDDEIMPDINTILYTMKYYNAQWAHFSFRLKKNSIVVHSNPSNITIPIEDFIKIFHNNNKKIMIYWGTEDNDKADDIFSYLKLDADSLCPNDIVLAKYVLQGIKENDTI
Protein: ATPase synthesis protein 25, mitochondrial (Q09726)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: mRNA stabilization factor specific for the 0.95 kb oli1 mRNA. Also involved in oli1 ring formation (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Matrix side {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein bL27m
- Cardiolipin synthase
- Nuclear control of ATPase protein 2
- Rsm22-cox11 tandem protein 1
- Rsm22-cox11 tandem protein 2
- Probable mitochondrial-processing peptidase subunit alpha
- Mitochondrial intermediate peptidase
- Amino-acid acetyltransferase, mitochondrial
- Large ribosomal subunit protein bL19m
- Intermediate cleaving peptidase 55
Sequence:
MPTYRFNYLRFNKLCVSFFRSKFDKRPFASQKFPENLVPDNSSNDANSQPEEVSSKKPWYVDEKHNLFPKKAHFDAVALPPIPKGAPNFLADVLNLLKKKYYATDLSFVNSPADSFWCDSDLILLASCNCGSEVVSATNGLLRLLKQKNVGPVNVDGLTSASRRKILERRMRKRSNLSNRQLNTSENNWTCLSIENFGISIHVITKNFREYYKLDNIEHVKDETLYSDLEHGKQSRVSLTSKSTPDNSLPPNFINNHSNVFRRSFHTCNFSLKSAASLYCDTQDILLNVNSQNLTSTLEKYKKMHLQNPNNFSLDFTLSIFERLRKDSSLQLTTKDINTLFSTIALSPTKLSMASKHSKNLVSERMLYLSLMYKSLVDLKTIDSFSLKLLFLKFMICSCMVKGESNFFLDNRIFLLERIMNRYGIPMTIDTFLLMQFILAKSNRWSEVWRRWDNLRKAGVVFNERLYNHVYLLAFESKNERVINYVLTNIFEDMVSQSPPIPASKLMATSLKKCVQSLPEKYAHSFPSVRNYIAKMENSMTH
Protein: Aminoaldehyde dehydrogenase 1 (SlAMADH1) (EC 1.2.1.-) (4-trimethylammoniobutyraldehyde dehydrogenase AMADH1) (EC 1.2.1.47) (Aminobutyraldehyde dehydrogenase AMADH1) (EC 1.2.1.19) (Betaine aldehyde dehydrogenase AMADH1) (EC 1.2.1.8) (Gamma-guanidinobutyraldehyde dehydrogenase AMADH1) (EC 1.2.1.54) (Q56R04)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively. Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively. Catalyzes with low efficiency the oxidation of betaine aldehyde to glycine betaine.
Interaction partners:
- Choline monooxygenase, chloroplastic
- aldehyde dehydrogenase
- Aldedh domain-containing protein
- Delta-1-pyrroline-5-carboxylate synthase
- Delta-1-pyrroline-5-carboxylate synthase
- Formate--tetrahydrofolate ligase
Sequence:
MANRNVPIPRRQLYIGGEWREPVKKNRIPIINPATEEIIGDIPAATAEDVDIAVEAARKAIARDDWGSTTGAQRAKYLRAIAAKVLEKKSVLATLESLDSGKTLYESAADMDDVAGCFEYYAGLAEALDSRRMTPVNLNSDSYKSYVLREPLGVVGLITPWNYPLLMAIWKVAPALAAGCAAILKPSELASITCLELGEICREIGLPSGALNILTGLGPEAGGPLASHPHVDKISFTGSGPTGSKIMTAAAQLVKPVSLELGGKSPIVVFDDIDNLDIAAEWTLFGIFANTGQVCSATSRLIVQENIASAFMDRLLKWTKNIKISDPLEEDCKLGPVVSAGQYEKVLKFISNAKSEGATILCGGERPQHLKKGYYVQPTIITDVNTSMEIWKEEVFGPVLCVKTFKTEEQAIELANDTKYGLGAAVMSKDVKRCERFTKAFQTGIIWINCSQPTFNELPWGGKKRSGFGRDLGKWGLENFLNIKQVTEYTSAEPLAFYKSPSKN
Protein: Arylamine N-acetyltransferase 2 (EC 2.3.1.5) (Arylamide acetylase 2) (N-acetyltransferase type 2) (AT-2) (NAT-2) (N-hydroxyarylamine O-acetyltransferase) (EC 2.3.1.118) (P50298)
Organism: Rattus norvegicus (Rat)
Function: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Acetylates only arylamines.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2E1
- Xanthine dehydrogenase/oxidase
- Arylamine N-acetyltransferase 1
- Carboxylesterase 1C
- Carboxylesterase 1D
- arylamine N-acetyltransferase
Sequence:
MDIEAYFERIGYQSSRNKLDLEELTEILQHQIRAIPFENLNIHCGESMELNLEVIFDQVVRKKRGGWCLQVNHLLYWALTKMGFEATMLGGYVFNTPANKYSSGMIHLLVQVTLSGKDYIVDAGFGRSYQMWEPLELTSGKDQPQVPAIFRLTEENGTWYLDQIRREQYVPNQEFVNSDLLEKNKYRKIYSFTLEPRTIEDFESINTYLQTSPASLFTSKSFCSLQTLEGVHCLVGSTLTYRRFSYKDNIDLVEFKSLTEEEIEDVLKTIFGVSLERKLVPKHGDRFFTI
Protein: Baruol synthase (AtBARS1) (EC 5.4.99.57) (Pentacyclic triterpene synthase 2) (AtPEN2) (O23390)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts oxidosqualene to baruol (90%) and 22 minor products.
Interaction partners:
- Squalene epoxidase 2, mitochondrial
- Squalene epoxidase 5
- Squalene epoxidase 1
- Squalene epoxidase 3
- Squalene epoxidase 6
- Squalene epoxidase 4
- Camelliol C synthase
- Arabidiol synthase
- Lupeol synthase 1
- Amyrin synthase LUP2
Sequence:
MWRLRIGAKAKDNTHLFTTNNYVGRQIWEFDANAGSPEELAEVEEARRNFSNNRSRFKASADLLWRMQFLREKKFEQKIPRVIVEDAEKITYEDAKTALRRGLLYFTALQADDGHWPAENAGSIFFNAPFVICLYITGHLEKIFTHEHRVELLRYMYNHQNEDGGWGLHVESPSNMFCSVINYICLRILGVEAGHDDKGSACARARKWILDHGGATYSPLIGKAWLSVLGVYDWSGCKPIPPEFWFLPSFFPVNGGTLWIYLRDIFMGLSYLYGKNFVATSTPLILQLREEIYPEPYTNISWRQARNRCAKEDLYYPQSFLQDLFWKGVHVFSENILNRWPFNNLIRQRALRTTMELVHYHDEATRYITGGSVPKVIAVFHMLACWVEDPESDYFKKHLARVPDFIWIGEDGLKIQSFGSQVWDTALSLHVFIDGFDDDVDEEIRSTLLKGYDYLEKSQVTENPPGDYMKMFRHMAKGGWTFSDQDQGWPVSDCTAESLECCLFFESMSSEFIGKKMDVEKLYDAVDFLLYLQSDNGGITAWQPADGKLVEFIEDAVVEHEYVECTGSAIVALAQFNKQFPGYKKEEVERFITKGVKYIEDLQMVDGSWYGNWGVCFIYGTFFAVRGLVAAGKCYNNCEAIRRAVRFILDTQNTEGGWGESYLSCPRKKYIPLIGNKTNVVNTGQALMVLIMGNQMKRDPLPVHRAAKVLINSQMDNGDFPQQEIMGVFKMNVMLHFPTYRNMFTLWALTHYTKALRGL
Protein: Multidrug export protein EmrA (P27303)
Organism: Escherichia coli (strain K12)
Function: Part of the tripartite efflux system EmrAB-TolC, which confers resistance to antibiotics such as CCCP, FCCP, 2,4-dinitrophenol and nalidixic acid. EmrA is a drug-binding protein that provides a physical link between EmrB and TolC.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:12482849, ECO:0000269|PubMed:1409590}; Single-pass membrane protein {ECO:0000269|PubMed:12482849, ECO:0000269|PubMed:1409590}; Periplasmic side {ECO:0000269|PubMed:12482849, ECO:0000269|PubMed:1409590}.
Interaction partners:
- Multidrug export protein EmrB
- Outer membrane protein TolC
- Probable multidrug resistance protein EmrY
- Macrolide export protein MacA
- Multidrug efflux pump subunit AcrA
- Transcriptional repressor MprA
- Macrolide export ATP-binding/permease protein MacB
- Probable aminoglycoside efflux pump
- Multidrug resistance protein MdtB
- Multidrug export protein AcrF
Sequence:
MSANAETQTPQQPVKKSGKRKRLLLLLTLLFIIIAVAIGIYWFLVLRHFEETDDAYVAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTALASSVRQTHQLMINSKQLQANIEVQKIALAKAQSDYNRRVPLGNANLIGREELQHARDAVTSAQAQLDVAIQQYNANQAMILGTKLEDQPAVQQAATEVRNAWLALERTRIISPMTGYVSRRAVQPGAQISPTTPLMAVVPATNMWVDANFKETQIANMRIGQPVTITTDIYGDDVKYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDQKQLEQYPLRIGLSTLVSVNTTNRDGQVLANKVRSTPVAVSTAREISLAPVNKLIDDIVKANAG
Protein: Myotubularin-related protein 14 (E7F0C5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Myotubularin 1.
- 1-phosphatidylinositol 3-phosphate 5-kinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase.
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR8
- Myotubularin-related protein 6.
- Myotubularin-related protein 1a.
- Myotubularin-related protein 7a.
- Coiled-coil domain-containing 78
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Myotubularin-related protein 12
Sequence:
MMMASRSEELTDLIDVFSKSQYRAKEVTPGVERIEKRYLELFDRDYKYSIIHNTNGEVCGHYPRKIVFLEYECSDNNKESFESTVQISKLQDLVNRSKMARCRGRFVCPVILYNGKHVCRSSTLAGWGELYGRTGYNYIFSGGTDDSLGEAEEVLEDDCAVRNGDSQLFDKVRGSDIKLLKYLSVRYICDLMVENKKVKFGLNVTSSEKVDKAQRYADFTLLSVPYPGCEFFREYKDRDYTAEGLVFNWNQDFVDAPLTIPVCFTRNLNINWSEYQSWDLVQQTQNYLKLLLHIINSDDENGLLVHCISGWDRTPLFVSLLRLSLWADGAIHASLEPSEILYLTIAYDWFLFGHMLPDRLSKGEEIFFFCFNFLKHIVCESFSVVKKQRRKNSHFKDADFTVDDLCQLKSRDRGSVTSLSSDFSLITEDASASPSLQAEATDLITLGPQASNGRKGMPLAAHSVLWNRPITSEERIPNVINEPSPLGSFKSSSSSSSNHSDQNATRTGSTPLAVPGRRPVVEYARSGSSVSTDYGSWQIVSGCGSIHDLPPVPSESPLPFSFQDEGPSGRMCTFVPERQVRLEAVREMFLSAYSSTVGLKSSSPSPSGALSGLLEQFARGVGLRGTNAII
Protein: Pleckstrin homology domain-containing family M member 3 (PH domain-containing family M member 3) (Differentiation-associated protein) (Q8BM47)
Organism: Mus musculus (Mouse)
Function: Involved in skeletal muscle differentiation. May act as a scaffold protein for AKT1 during muscle differentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19028694}. Golgi apparatus {ECO:0000269|PubMed:19028694}. Cell membrane {ECO:0000269|PubMed:19028694}. Note=Before differentiation of muscle cells, localized to the cytosol. During muscle differentiation shuttles to the plasma membrane. {ECO:0000269|PubMed:19028694}.
Interaction partners:
Sequence:
MEALEVDDISPALEVTEDFFSTFDSKLEKAVQQAEVYGIQEVPELVGHEVLGNIADNGALRSVASLGKGTMIWDHCKSRLLETKAQNVFPAKEQLMVQRGTAPDNLSWMAQKEASTFNFFNICQRRRDRPRSVNDLLDETTTFKPGHARSRSDVTHVDWRVVLSTMPLQQQQQQQQASLQGIHFPGPSFLLSSPSKVEDAQGNTEHKQTFPNILKKGYLEIRKNHDSYWQSCYAELSPYNLNFYSLDSSGNQNLYATYQLSHFQSISVLGNLEARMVDTVLYDNSQLQLKAESPWEALDWGQKLWEVVHAAVPNYMGRQGEMANSPGLIHHGDCAQNHCLQKKSSGLLASPVLDSPKQYQNILKSGTLYRLTVQNNWKAFTFVLSKAYLMAFHPGKLDEDPLLSYNVDVCLAVQIDNLDGCDSCFQVIFPQDVLRLRAETRQRAQEWMEALKTAANAARSSEQNLQVTLRNKPKDQLDGRELRKNKRQSVTTSFLSILTTLSLERGLTAQSFKCAGCQRSIGLSNGKAKVCNYSGWYYCSSCHVDDSFLIPARIVHNWDTSKYKVSKQAKEFLEYVYEEPLIDIQQENPMLYLHAEPLATVVRLRQRLKSLRAYLFSCRAAVAEDLRRRIFPREYLLQQIHLYSLADLQQVIEGKLAPFLGKVIKFATAHVYSCSLCSQKGFICEICNNGEILYPFEDISTSRCESCGAVFHSECKEKSVPCPRCVRRELQKKQKSFWRQLNVDESLEEACAMFELSYQST
Protein: Ribosomal protein L37 (B5FY56)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Interaction partners:
Sequence:
MTKGTSSFGKRRNKTHTLCRRCGSKAYHLQKSTCGKCGYPAKRKRNYNWSAKAKRRNTTGTGRMRHLKRVYRRFRNGFREGTTPKPKRAAFAASSSS
Protein: Flagellar hook protein FlgE (P75937)
Organism: Escherichia coli (strain K12)
Subcellular location: Bacterial flagellum basal body {ECO:0000250}.
Interaction partners:
- Flagellar hook-associated protein 1
- Flagellar hook-associated protein 2
- Flagellar motor switch protein FliM
- Basal-body rod modification protein FlgD
- Flagellar motor switch protein FliG
- Flagellar L-ring protein
- Flagellar basal body rod protein FlgB
- Flagellar basal-body rod protein FlgF
- Flagellar hook-associated protein 3
- Flagellar M-ring protein
Sequence:
MAFSQAVSGLNAAATNLDVIGNNIANSATYGFKSGTASFADMFAGSKVGLGVKVAGITQDFTDGTTTNTGRGLDVAISQNGFFRLVDSNGSVFYSRNGQFKLDENRNLVNMQGLQLTGYPATGTPPTIQQGANPTNISIPNTLMAAKTTTTASMQINLNSSDPLPTVTPFSASNADSYNKKGSVTVFDSQGNAHDMSVYFVKTGDNNWQVYTQDSSDPNSIAKTATTLEFNANGTLVDGAMANNIATGAINGAEPATFSLSFLNSMQQNTGANNIVATTQNGYKPGDLVSYQINDDGTVVGNYSNEQTQLLGQIVLANFANNEGLASEGDNVWSATQSSGVALLGTAGTGNFGTLTNGALEASNVDLSKELVNMIVAQRNYQSNAQTIKTQDQILNTLVNLR