wanglab/gogpt-training-data huggingface dataset:
Protein: Catalase-B (EC 1.11.1.6) (Q55DH8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Its accumulation in prespore cells affords the spores protection from oxidation during prolonged dormancy. Required for normal developmental timing, possibly through a regulatory role in differentiation and morphogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11004503}.
Interaction partners:
- 2-Hydroxyacid oxidase
- Catalase-A
- 3-hydroxyanthranilate 3,4-dioxygenase
- Kynureninase
- Superoxide dismutase 4
- Senescence marker protein-30 family protein
- Rhodanese domain-containing protein
- Superoxide dismutase 5
- SCP2 domain-containing protein
- Defective in tip formation protein A
Sequence:
MNKKLEQLEKFKTNDKNPVYSTTNTGVSLSDDANSLKAGPRGPTLLEDFVLREKITHFDHERIPERIVHARGTGAHGYFLSYKDHSKLTKADFLSKQDKKTPVFIRISTVQGPRGSADTVRDVHGFAVKFYTDEGNYDLVGNNMPVFFIQDASSFPDFVHAVKMEPQNEMPTGGSAHDTFYDFCGLKPESAHSVLWVMSDRGIPISLRHQQGFGVHSYRFINQEGKSTFVKLHWKPLSGTCSLLWDEAQKIAGKDCDYHRRRFWEDIESGDFPQWELGAQLLDEDLQKKFDFDILDPTKLIPEELTPVIPLGRMVIDRNPDNFFAETEQVAFCVSHVVPGIDFSNDPLLQGRIFSYLDTQLSRLGGPNFNEIPINRPVCPFANNQRDGIHRMTINKGGASYFPNSIDKGYPLLKEPSANKGGFRPYPENISGTKSYDRSETFEDHFSQATMFWNSMSQHEKNHIIAAYTFEISKCSRPEVRTRYVNNILVNIDSVLAEKVAKNLGVKIEPTSTKPIKKIMVKPSPALSQPNLLSGDIVSRRISVIIEKGVDYDDVINFKDDMEKRGAMVMLVSSTLAQVECSGGEMLSPKGTIIGNPSIFFDAVYVPKSTEEATKILSDDGNFLHYILEAFKHLKTIAFGGSVSVIKELLRLPQDHGLLLGNGYKDITEQFFYSLAHHRVWERESKVSKIPA
Protein: Complement component C1q receptor (C1q/MBL/SPA receptor) (C1qR) (C1qR(p)) (C1qRp) (CDw93) (Complement component 1 q subcomponent receptor 1) (Matrix-remodeling-associated protein 4) (CD antigen CD93) (Q9NPY3)
Organism: Homo sapiens (Human)
Function: Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24809468, ECO:0000269|PubMed:26848865}; Single-pass type I membrane protein.
Interaction partners:
- Complement C1q subcomponent subunit A
- Mannose-binding protein C
- Calreticulin
- PDZ domain-containing protein GIPC1
- Platelet endothelial cell adhesion molecule
- Complement component 1 Q subcomponent-binding protein, mitochondrial
- Integrin alpha-X
- C5a anaphylatoxin chemotactic receptor 1
Sequence:
MATSMGLLLLLLLLLTQPGAGTGADTEAVVCVGTACYTAHSGKLSAAEAQNHCNQNGGNLATVKSKEEAQHVQRVLAQLLRREAALTARMSKFWIGLQREKGKCLDPSLPLKGFSWVGGGEDTPYSNWHKELRNSCISKRCVSLLLDLSQPLLPSRLPKWSEGPCGSPGSPGSNIEGFVCKFSFKGMCRPLALGGPGQVTYTTPFQTTSSSLEAVPFASAANVACGEGDKDETQSHYFLCKEKAPDVFDWGSSGPLCVSPKYGCNFNNGGCHQDCFEGGDGSFLCGCRPGFRLLDDLVTCASRNPCSSSPCRGGATCVLGPHGKNYTCRCPQGYQLDSSQLDCVDVDECQDSPCAQECVNTPGGFRCECWVGYEPGGPGEGACQDVDECALGRSPCAQGCTNTDGSFHCSCEEGYVLAGEDGTQCQDVDECVGPGGPLCDSLCFNTQGSFHCGCLPGWVLAPNGVSCTMGPVSLGPPSGPPDEEDKGEKEGSTVPRAATASPTRGPEGTPKATPTTSRPSLSSDAPITSAPLKMLAPSGSPGVWREPSIHHATAASGPQEPAGGDSSVATQNNDGTDGQKLLLFYILGTVVAILLLLALALGLLVYRKRRAKREEKKEKKPQNAADSYSWVPERAESRAMENQYSPTPGTDC
Protein: LIM zinc-binding domain-containing protein (Q19641)
Organism: Caenorhabditis elegans
Interaction partners:
- IRG-type G domain-containing protein
- DH domain-containing protein
- Carbohydrate kinase FGGY N-terminal domain-containing protein
- Intermediate filament protein ifa-4
- Chloride intracellular channel exc-4
- RING-type domain-containing protein
Sequence:
MPNCPRCQKAVYFAERVTSIGFDWHRPCLRCENEACKKTLAAGSHSEREGKPYCNRCYGALFGPRGYGHGGTESHTFHQGQTGQV
Protein: AT5g37380/MNJ8_170 (Chaperone DnaJ-domain superfamily protein) (Similarity to DnaJ protein) (Q9FHS7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F13F21.24 protein
- Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- Endosomal targeting BRO1-like domain-containing protein
- Cation/H
Sequence:
MECNKDEATRAKEIAENKFKMKDIAGAKKFALKAQNLYPEIEGVSQMLATLDVYIAAENKVNEDVDWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDRRKSLHSVYQKVSVSSSNNGFCNFAKTTFTTNARTTTPRNNPPAQKTNPPAQKTNPPAQKTNPPAQKNNPPTQKNNPQKPVGTTQKTGRTDNHTTTPNSFTASGSSDQSKSNTFWTVCRRCMMQYEYLRVYVNCNLRCPNCLQSYLAVEVPKPGISSRWSSCSRLKSAANHNTTSGLFNNSKWTFSRTSSAAHAASVVQHAYEKVKKDREQAKATARREKKNAKRKSTTDSSASGSSLKKRKVCLETDIGCSSGREVTYRVTGENGKNMGKLEHGTKESADKLSLRRTQRKISKENVTREVKSR
Protein: HTH-type transcriptional regulator RamB (Regulator of acetate metabolism B) (RamB) (Q8NTD8)
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: During growth on glucose, RamB negatively controls the expression of aceA, aceB, ack and pta genes which are involved in acetate metabolism. RamB is also a negative regulator of rpf2 gene expression during growth on acetate as the sole carbon source.
Interaction partners:
- HTH-type transcriptional activator RamA
- CRP-like cAMP-activated global transcriptional regulator
- Isocitrate lyase
- Malate synthase G
- 2-methylcitrate dehydratase 2
- Resuscitation-promoting factor Rpf2
Sequence:
MGKTYVGSRLRQLRRERDLSQASLAATLGLSASYVNQIEHDVRPLTVPVLLRITEAFGVDATFFSRDDDSRLLAEVQDVMLDREINPANVELQELSEMVYNHPQLARAMVEMHQRYRNVRDKFSIAVDNRTNTPEERRPIAEAVSMPHEEVRDFIYARQNYFDALDRRAEAIAAQLGWQPYDSRAMEDSIARRLQMDHDVTITSSKEESGTLHHFDPETRLLTIHARLNPGQRAFRMATELGYLEANDLIEGIVDDGIWSTPEARTLAIRGVASYFAAAVMLPYKIFHSEAEKSGYDIEYLGQLFGVGYETTAHRLSTLQRPNLRGIPFTFVRVDRAGNMSKRQSATGFHFTHYGGTCPLWNVFETFTNPGQVLRQFAQMPDGRNYLWISRTVRHHEARFGEVDKMFAIGLGCEARHADRTVYSRGFNLQDLSTATPIGSGCRVCTRENCAQRAFPSVHGRINIDAHESTIAPY
Protein: Large ribosomal subunit protein eL36y (60S ribosomal protein L36-2) (Q9M352)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL22z
- Large ribosomal subunit protein eL8y
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein eL29y
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL6x
- Large ribosomal subunit protein eL31z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
Sequence:
MTTPQVKTGLFVGLNKGHVVTRRELAPRPRSRKGKTSKRTIFIRNLIKEVAGQAPYEKRITELLKVGKDKRALKVAKRKLGTHKRAKRKREEMSSVLRKMRSGGGGATEKKK
Protein: Immunoglobulin delta heavy chain (Immunoglobulin delta heavy chain WAH) (P0DOX3)
Organism: Homo sapiens (Human)
Function: Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen. IgD is the major antigen receptor isotype on the surface of most peripheral B cells, where it is coexpressed with IgM. The membrane-bound IgD (mIgD) induces the phosphorylation of CD79A and CD79B by the Src family of protein tyrosine kinases. Soluble IgD (sIgD) concentration in serum is below those of IgG, IgA, and IgM but much higher than that of IgE. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. After the antigen binds to the B cell receptor, the secreted form sIgD is shut off. IgD is a potent inducer of TNF, IL1B, and IL1RN. IgD also induces release of IL6, IL10, and LIF from peripheral blood mononuclear cells. Monocytes seem to be the main producers of cytokines in vitro in the presence of IgD.
Subcellular location: Secreted {ECO:0000303|PubMed:11282392, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:11282392, ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
RLQLQESGPGLVKPSETLSLTCIVSGGPIRRTGYYWGWIRQPPGKGLEWIGGVYYTGSIYYNPSLRGRVTISVDTSRNQFSLNLRSMSAADTAMYYCARGNPPPYYDIGTGSDDGIDVWGQGTTVHVSSAPTKAPDVFPIISGCRHPKDNSPVVLACLITGYHPTSVTVTWYMGTQSQPQRTFPEIQRRDSYYMTSSQLSTPLQQWRQGEYKCVVQHTASKSKKEIFRWPESPKAQASSVPTAQPQAEGSLAKATTAPATTRNTGRGGEEKKKEKEKEEQEERETKTPECPSHTQPLGVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVEEGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTCTLNHPSLPPQRLMALREPAAQAPVKLSLNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPGSTTFWAWSVLRVPAPPSPQPATYTCVVSHEDSRTLLNASRSLEVSYVTDHGPM
Protein: Eukaryotic translation initiation factor 4G2, isoform A (Eukaryotic translation initiation factor 4G2, isoform C) (Q9VCH1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Eukaryotic translation initiation factor 4E1
- Eukaryotic initiation factor 4A
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- eIF-4F 25 kDa subunit
- Polyadenylate-binding protein
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic initiation factor 4B
Sequence:
MFPQQGGGGKGTRPQSTHQQNHNHQAQHHQATHSHHHHLQQQQEQQQSHAVFVPNHSGLHHHQQQHLLQQQQQQHQQQAAVAAAHLQQHIQQQQQQQVQAQAQAHHQPVIFYNTQPSYAAHSAAVNNSANGGGATLQLSAAASSNTLGHPLTGGHHGGANGVAPGSNMPRALSNPTLPPHFQQSAGLIAPAGGNAGGPYISATYIPINQTGPLMGMQPAVTFPTNGAAGASFYAAAPPPPQQKQLPPTAQQQGPGGAPGAAQTPTLAYYQLGPNAQNSAGNNVVSGANTHRGNMRGGQRSTPTAQHTNYFTAYTMAPGNAQRPAPTNVAPMMNSRSGALNGAAAFHHLPHNFGIPSLALGPPAGMTTPILAPAGMQAPPPQPPGGLHTFAPHLQSNSATTLPSVPSVTGVPAVASGFSTTSLPTPSVTTAPQLGANSDKVCKRKYAIPIIHPDTMENVMDGWKRSVFIKKDSNSTLTQHTDLDTALDDNSTLCLYQAPTLMDSGSGSSLLSGAMVDQQMQTVKPASSLKQSVSLEKVPEAVYCKDAVGQDVHPSPPPKSTDKDQISVIVKDILAHSGNAEDHLSFWQYSDVDNVTETHNSLPLVQSDLPDTTDTCQQPVLFQEQAKKQRPKLANKQSTATPASIANDVAEAAASGCPGVSILSRGQSMVTPAGPSTPPPPSRVAQQKSTKSIVTTAVAASVKPTTGSPNRKSSIQAATSTTTSSGASSSTASTPTHASSKLKQQPVNNLQHGKQIPGKVSTPALPPTASRISAAVTLLAGTANITTTTNSSKKQRQAQKRARELEKKKQKSSITSTTSTQGQNNNGKGNGNGNAALEINTNSNNAATVTTTSMSTLTTTTTATAPTTKQETAAVDDKETAQPTTDTLSATSNNTKVSSILRDKKTMLNPKEQLTSHNNNNNNNNEDGIEAKVESDPESDIKDDSMSNITGEKSEKHLANEEIVAKFLQKDSPDTSVVHAETQQLQFLNSSSSVCEEDEPVPVISEGVTKTEENAEAEIKFGDFHEDPRNDTGFICSSTWSSSTISKAAEDDSSQSSRSADNVDCAPKVVEQISEEKSASSTKSSPVHKATGSGPGSPKTKELKSKSPSPIPVPQVPKNYRYSIETLRELAKRRDSRKPPMVPCQKGDCISQLFVSRQQQPQQHHGQHIQQYQHMSFNESLDYVPGKRGRGHGPNKKHHDQHQQMGGSSGMGSGSGGGGGISNSSQRHMDIIRVQLSLKEEIKLSECENAWQPGTLRRVSMAGGQDEDDDVEGVLKKVRGILNKLTPDNFEVLLKEMSSIKMDNEAKMTNVMLLIFEKTISEPNFAPTYARFCKVLFHEIKAENKSLFTSSLITRIQHEFESNVNDANAKSKKLQPTMERINQCSDPAKKAELRAEMEDLEYQFRRRAWGTVRFIGELFKLQSLTNDRVLNCVESLLEHGCEEKLEYMCKLLTTVGHLLESSLPEHYQLRDRIEKIFRRIQDIINRSRGTSHRQQVHIKISSRVRFMMQDVLDLRLRNWDQPATHQSGQQGGRGQRHKQHDDSKDQSHSTGGGRGGGMNQHQQSSTHHQHQKHNQHGHDGGNYFMQKMPNKQHHENQTLSIDPSKLRFSNSSATDDSIAKLGNSSHYQWRNVGNRPVSSTQVNASNAPPPTSLLKRPGQNYKFLPYQQPSAVAGTANAPAGGNKSNVEVNDAFDGKQCQGLITKLVEEALNTREWQPEVLSIWRSHSGSQQSKTLFHLLTDYLHKSTVKRQHRQACGNIFAYLMDKDAVEKEIFEEAYSRFGDDFPDLLVDVPNGWGYVFEFLGPIIHSGHLDLKDVWQRRWLDDFFFAERFVYAFVSYFVQEFGAAYARKLWHNDYKLDRGQLFWSDVRKYREFVQSHSFYFLDNGPGQNQGHAKVKAPTTPRSPVEHVERIRHLLAISCDMAIDYINTNVAINDKFVRQLTRFLCCDFALTVMTNTHNNIKSGGNSKPLQLNTESFRSCCTPLLRLCIDAQEALEIACIDEAVDALQQHFMTEYEDDMAAGETICSTFSVLYESEVIPKESFDKWYKLEMAHSRAYRRPFIDKLRGFIEEM
Protein: Maturase K (Intron maturase) (P0C382)
Organism: Oryza sativa subsp. indica (Rice)
Function: Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- KANL3/Tex30 alpha/beta hydrolase-like domain-containing protein
- NAD
- FHA domain-containing protein
- FHA domain-containing protein
- Histone acetyltransferase
- NAD
- NAD
- Histone-lysine N-methyltransferase SUVR5
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MEKFEGYSEKLKFPRQYFVYPLLFQEYIYVFAHDYGLNGSELVEIIGSNNKKFSSLLVKRLMIRMYQQNFWINLVNHPNQDRLLDYNNFFYSEFYSQILSEGFAIVVEIPFSLREQSCPEEKEIPKFQNLRSIHSIFPFLEDKFLHLHYLAHIEIPYPIHLDILLQLLQYRIQDVPSLHLLRFFLNYYSNWNSFITSMKSIFILKKENKRLFRFLYNSYVSEYEFFLLFLRKQSSCLRLTSSGTFLERIIFSRKMEHFGLMYPAFFRKTIWFVMDPLMHYVRYQGKAILASKGTLLLKKKWKCYLVRLWQYSFSFWTQPQRIHLNQLENSCFDFLGYFSSVPINSLLVRNQMLENSFLIDTQMKKFDTKVPVTPLIGSLAKAQFCTGSGHPISKPIWTDLSDWDILDRFGRICRNLFHYYSGSSKKKTLYRLKYILRLSCARTLARKHKSTVRAFMQWLGSVFLEEFFTEEEQVFSLMFAKTTYFSFRGSHSERIWYLDILRINDLVNPLN
Protein: Glycine betaine monooxygenase oxygenase subunit (EC 1.14.13.251) (Glycine betaine catabolism A) (Q9HTF4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Glycine betaine monooxygenase reductase subunit
- DgcA, Dimethylglycine catabolism
- 4-vinyl reductase 4VR domain-containing protein
- DgcB, Dimethylglycine catabolism
- Sarcosine oxidase delta subunit
- Electron transfer flavoprotein alpha/beta-subunit N-terminal domain-containing protein
- Sarcosine oxidase gamma subunit
- Sarcosine oxidase subunit beta subunit beta)
- Membrane dipeptidase
- HTH-type transcriptional regulator GbdR
Sequence:
MDVTSTLSLGDPLEPARKATADMLRSRDHSFSLPQPFYCDQRLFEIDMQEIFHKEWLIAGMTCEIPAKGNFLTLQIGKNPVLVIRGAEGQVHAFHNVCRHRGSRLCVSEKGKVAKLVCPYHQWTYELDGRLLFAGTEMGADFDMKEYGLKPIQVKTAGGYIFISLAENPPAIDDFLATLEHYMEPYDMENAKVAVQTTIREAANWKLVIENNRECYHCNGSHPELLKTLLEWDDVTDPRASQAFKDQVAACTSAWDAEKIPYAHASFGLRNRIVRMPLLDGTVSMTMDGKQGSKKLMGRIKNPDLGSMRILHLPHSWNHCMGDHLIVFTVWPISAQETLVTTKWLVHKDAVEGVDYDVARLREVWDATNDQDRRLAEENQRGINSDAYQPGPYSKTYEFGVINFLDWYSERMLNNLGEESAHVRKVAGS
Protein: NADPH oxidase 4 (EC 1.6.3.1) (Kidney oxidase-1) (KOX-1) (Kidney superoxide-producing NADPH oxidase) (Renal NAD(P)H-oxidase) (Q9NPH5)
Organism: Homo sapiens (Human)
Function: Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB. May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation. Isoform 3 is not functional. Isoform 5 and isoform 6 display reduced activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15572675, ECO:0000269|PubMed:15927447, ECO:0000269|PubMed:21343298, ECO:0000269|PubMed:26742780}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:16019190, ECO:0000269|PubMed:21343298}; Multi-pass membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q924V1}. Nucleus {ECO:0000269|PubMed:16324151}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus {ECO:0000269|PubMed:23393389}. Nucleus, nucleolus {ECO:0000269|PubMed:23393389}. Cytoplasm {ECO:0000269|PubMed:15721269}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15721269}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:15721269}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15721269}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:15721269}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15721269}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000269|PubMed:15721269}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15721269}.
Interaction partners:
- Cytochrome b-245 light chain
- Neutrophil cytosol factor 2
- Neutrophil cytosol factor 1
- NADPH oxidase 2
- NADPH oxidase 1
- Toll-like receptor 4
- NADPH oxidase 5
- NADPH oxidase 3
- Dual oxidase 1
- Neutrophil cytosol factor 4
Sequence:
MAVSWRSWLANEGVKHLCLFIWLSMNVLLFWKTFLLYNQGPEYHYLHQMLGLGLCLSRASASVLNLNCSLILLPMCRTLLAYLRGSQKVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVNYSEDFVELNAARYRDEDPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSGGLLKYQTNLDTHPPGCISLNRTSSQNISLPEYFSEHFHEPFPEGFSKPAEFTQHKFVKICMEEPRFQANFPQTWLWISGPLCLYCAERLYRYIRSNKPVTIISVMSHPSDVMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQSRNYPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCMLHNKFWQENRPDYVNIQLYLSQTDGIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLSNQNNSYGTRFEYNKESFS
Protein: Lymphocyte cytosolic protein 1 (Q5TBN3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARGSVSDEEMMELREAFAKVDTDGNGYISFNELNDLFKAACLPLPGYRVREITENLMATGDLDQDGRISFDEFIKIFHGLKSTDVAKTFRKAINKKEGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTNDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELSRNE
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (F5H211)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERMRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIRVQQMHRPKLIGEELAQLKEQRVHKTDLERVLEANDGSGMLDEDEEDLQRALALSRQEIDMEDEEADLRRAIQLSMQGSSRNISQDMTQTSGTNLTSEELRKRREAYFEKVRLRLQKYIQQQKQQQQQQQQQQGDLSGQSSHPCERPATSSGALGSDLGDAMSEEDMLQAAVTMSLETVRNDLKTEGKK
Protein: Small ribosomal subunit protein mS31 (28S ribosomal protein S31, mitochondrial) (Q95S88)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MLAVRSSQRLGLRSLLPAAFKNVGLVNYSSSQSKNDDGYSSSDDEKPTKKKEEPVETAAQRLNRLLGTMQATDQLSASDFPRPGDANRKRREAQKQEAAAKNVLTAAKNIASMLGTSESDKKQTESELLAKLLGHGSESSSAATGENQTADVSGYPSGDKELNLSDIIVGMKIDRRQQPQQVEQTRGEYVRRSLASRFKPQNRDGAYQRSQRQTKREAESFTGSVNLYGGEPLGIFKDTQLPISNDILSTWSQLSERELSLQASHPPANYFEQMVLWTDQKKVWRFPINNEQDWEDEHNVDFSEHIFLEQHLEDWCPSKGPIRHFMELVCVGLSKNPYLTAQEKKDHIFWFRDYFQAKKDILRDLISKEPSKSISA
Protein: Neurotrophin-3 (NT-3) (HDNF) (Nerve growth factor 2) (NGF-2) (Neurotrophic factor) (P18280)
Organism: Rattus norvegicus (Rat)
Function: Seems to promote the survival of visceral and proprioceptive sensory neurons.
Subcellular location: Secreted.
Interaction partners:
- BDNF/NT-3 growth factors receptor
- High affinity nerve growth factor receptor
- NT-3 growth factor receptor
- Tumor necrosis factor receptor superfamily member 16
- Neurotrophic factor BDNF precursor form
- Glial cell line-derived neurotrophic factor
- Sortilin
- Ciliary neurotrophic factor
- Insulin-like growth factor 1
- Beta-nerve growth factor
Sequence:
MSILFYVIFLAYLRGIQGNNMDQRSLPEDSLNSLIIKLIQADILKNKLSKQMVDVKENYQSTLPKAEAPREPEQGEATRSEFQPMIATDTELLRQQRRYNSPRVLLSDSTPLEPPPLYLMEDYVGNPVVTNRTSPRRKRYAEHKSHRGEYSVCDSESLWVTDKSSAIDIRGHQVTVLGEIKTGNSPVKQYFYETRCKEARPVKNGCRGIDDKHWNSQCKTSQTYVRALTSENNKLVGWRWIRIDTSCVCALSRKIGRT
Protein: Germacrene A hydroxylase (EC 1.14.14.95) (Germacrene A oxidase) (LsGAO) (D5J9U8)
Organism: Lactuca sativa (Garden lettuce)
Function: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones. Catalyzes three consecutive oxidations of germacrene A to produce germacrene A acid. Could also catalyze the three-step oxidation of non-natural substrate amorphadiene to artemisinic acid.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:D5JBW8}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:D5JBW8}.
Interaction partners:
Sequence:
MELSITTSIALATIVFFLYKLATRPKSTKKQLPEASRLPIIGHMHHLIGTMPHRGVMDLARKHGSLMHLQLGEVSTIVVSSPKWAKEILTTYDITFANRPETLTGEIIAYHNTDIVLAPYGEYWRQLRKLCTLELLSVKKVKSFQSIREEECWNLVKEVKESGSGKPINLSESIFTMIATILSRAAFGKGIKDQREFTEIVKEILRQTGGFDVADIFPSKKFLHHLSGKRARLTSIHKKLDNLINNIVAEHHVSTSSKANETLLDVLLRLKDSAEFPLTADNVKAIILDMFGAGTDTSSATVEWAISELIRCPRAMEKVQAELRQALNGKEKIQEEDIQDLAYLNLVIRETLRLHPPLPLVMPRECREPVNLAGYEIANKTKLIVNVFAINRDPEYWKDAEAFIPERFENNPNNIMGADYEYLPFGAGRRMCPGAALGLANVQLPLANILYHFNWKLPNGASHDQLDMTESFGATVQRKTELLLVPSF
Protein: Ribose-phosphate pyrophosphokinase 2 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase II) (PRS-II) (P09330)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
Interaction partners:
- Phosphoribosyl pyrophosphate synthase-associated protein 1
- Phosphoribosyl pyrophosphate synthase-associated protein 2
- Amidophosphoribosyltransferase
- Ribokinase
- Transketolase
- Ribose-5-phosphate isomerase
- transketolase
- transketolase
- Phosphoglucomutase-1
- Uridine monophosphate synthetase, isoform CRA_a.
Sequence:
MPNIVLFSGSSHQDLSQRVADRLGLELGKVVTKKFSNQETSVEIGESVRGEDVYIIQSGCGEINDNLMELLIMINACKIASSSRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLQWIRENITEWRNCIIVSPDAGGAKRVTSIADRLNVEFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAGATKVYAILTHGIFSGPAISRINNAAFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL
Protein: Trifunctional NAD biosynthesis/regulator protein NadR [Includes: Transcriptional regulator NadR; Nicotinamide mononucleotide adenylyltransferase (NMN adenylyltransferase) (NMN-AT) (NMNAT) (EC 2.7.7.1) (Nicotinamide ribonucleotide adenylyltransferase) (Nicotinamide-nucleotide adenylyltransferase); Ribosylnicotinamide kinase (RNK) (EC 2.7.1.22) (Nicotinamide riboside kinase) (NRK) (NmR-K)] (P27278)
Organism: Escherichia coli (strain K12)
Function: This enzyme has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to the nadB operator sequence in an NAD- and ATP-dependent manner. As NAD levels increase within the cell, the affinity of NadR for the nadB operator regions of nadA, nadB, and pncB increases, repressing the transcription of these genes. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity catalyzes the transfer of the AMP moiety of ATP to nicotinamide ribonucleotide to form NAD(+). The NMN adenylyltransferase domain also functions as the NAD and ATP sensor.
Subcellular location: Cell membrane; Peripheral membrane protein. Cytoplasm {ECO:0000250}.
Interaction partners:
- NAD-dependent protein deacylase
- Nicotinate phosphoribosyltransferase
- NH
- Nicotinate-nucleotide adenylyltransferase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinamide-nucleotide amidohydrolase PncC
- Nicotinamide riboside transporter PnuC
- NAD kinase
- Probable HTH-type transcriptional regulator LgoR
- NAD-capped RNA hydrolase NudC
Sequence:
MSSFDYLKTAIKQQGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRQKKTIGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGFDDTRDRALFEDSAMSQQPTVPDRLRWLLQTFKYQKNIRIHAFNEEGMEPYPHGWDVWSNGIKKFMAEKGIQPDLIYTSEEADAPQYMEHLGIETVLVDPKRTFMSISGAQIRENPFRYWEYIPTEVKPFFVRTVAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGGDEIALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGLRSLGSSVDRKEFQNLLVEMLEENNIEFVRVEEEDYDSRFLRCVELVREMMGEQR
Protein: Serine/threonine-protein kinase PknJ (EC 2.7.11.1) (P9WI67)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: In vitro, phosphorylates various substrates such as EmbR, PepE, MmaA4, Pyk, LldD and GroEL2.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20185505}; Single-pass membrane protein {ECO:0000269|PubMed:20185505}.
Interaction partners:
- Serine/threonine protein phosphatase PstP
- Glycogen accumulation regulator GarA
Sequence:
MAHELSAGSVFAGYRIERMLGAGGMGTVYLARNPDLPRSEALKVLAAELSRDLDFRARFVREADVAAGLDHPNIVAVHQRGQFEGRLWIAMQFVDGGNAEDALRAATMTTARAVYVIGEVAKALDYAHQQGVIHRDIKPANFLLSRAAGGDERVLLSDFGIARALGDTGLTSTGSVLATLAYAAPEVLAGQGFDGRADLYSLGCALFRLLTGEAPFAAGAGAAVAVVAGHLHQPPPTVSDRVPGLSAAMDAVIATAMAKDPMRRFTSAGEFAHAAAAALYGGATDGWVPPSPAPHVISQGAVPGSPWWQHPVGSVTALATPPGHGWPPGLPPLPRRPRRYRRGVAAVAAVMVVAAAAVTAVTMTSHQPRTATPPSAAALSPTSSSTTPPQPPIVTRSRLPGLLPPLDDVKNFVGIQNLVAHEPMLQPQTPNGSINPAECWPAVGGGVPSAYDLGTVIGFYGLTIDEPPTGTAPNQVGQLIVAFRDAATAQRHLADLASIWRRCGGRTVTLFRSEWRRPVELSTSVPEVVDGITTMVLTAQGPVLRVREDHAIAAKNNVLVDVDIMTPDTSRGQQAVIGITNYILAKIPG
Protein: RE16319p (SD26190p) (Q8SXK4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWKMLDMMELSEAELFMFDCDDCSGTPLAPPPQFLIPPPPRPPALAEFTVVPQDCNEEQLAQQQWESDVCQAMPVSGKIYPKYDKPIIKTRKILQY