wanglab/gogpt-training-data huggingface dataset:
Protein: Trafficking protein particle complex III-specific subunit 85 (TRAPP III-specific subunit 85) (Muddled meiosis protein 1) (Sporulation protein GSG1) (Transport protein particle 85 kDa subunit) (P46944)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Specific subunit of the TRAPP III complex that acts as an autophagy-specific guanine nucleotide exchange factor (GEF) for YPT1. TRS85 directs the TRAPP III complex to the phagophore assembly site (PAS) that is involved in autophagosome formation. Required for membrane expansion during autophagy and the CVT pathway. Required for sporulation. Has a role late in meiosis following DNA replication.
Subcellular location: Preautophagosomal structure {ECO:0000269|PubMed:11239471, ECO:0000269|PubMed:20375281}.
Interaction partners:
- Trafficking protein particle complex subunit 23
- Trafficking protein particle complex subunit 20
- TRAPP-associated protein TCA17
- Trafficking protein particle complex subunit BET5
- Trafficking protein particle complex subunit 33
- Trafficking protein particle complex subunit 31
- Trafficking protein particle complex subunit BET3
- Trafficking protein particle complex II-specific subunit 130
- Trafficking protein particle complex II-specific subunit 120
- GTP-binding protein YPT1
Sequence:
MVFSYEHYMNLLFHLDNSKETVPPEIAKRIISNAIAPVITVTSTPLFDKHIQETYKVDSLYMLLRFFGGCVSDRDQANEAKVGQHEHEVCDASDSTDSIPKNKNLEVPNLSKKGSRSRSNSLFQRDSTQSQYIRFTRPLGDLIETRDANDMLFNYHSLEVFLDNYLKLVAANTDEMVPHNLLKKSIYHSFFSLAISSTNNLSPYETFNHPILSLIALDISNGEVYEDARDLLVNFKNLNHNTENFPIFMNTNEMLPVFLLCYNDDSQEEFEKCQALAKKLKKQLFVESILLALWKDSFIYDENSVIQLHQPVMSSLEEILFFLQAPTQTTLSLALINSIYDMLDYLVYDLMIPFMKRKVSFWEETILQPRKSLFNGAKFFKKFMNKNPVNGNHQHNSLTRDSQGNEYFASSSSEFLMRKLADWSMMLSDFKTAYSTYESLMDDLDAFPKYLASCIEWCAVSLLMGAQSIVTVKMIKNDINPLIERALATYENCSRIQRGKGKESNSLDVTEPVRSYETRCMILASELFLSLSNTWTSTPYAIQYLETILDECKLGPCSQIMVWERLSDCYNLRVDPRIKHRVGAMKKDAKDTEDLRGEHKYSTDHFTDEDILSEGLTRRRKAAFFRLIAAKKWAEQKQWRQVSWCLKDIESTYSEIKFLHGNGLILSKLKNQLNLKDVDSAPRPSEKNLTRTSVSFIG
Protein: 60S ribosomal protein L34 (Q8IBY4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 40S ribosomal protein S25
- 60S ribosomal protein L23
- 40S ribosomal protein S26
- 40S ribosomal protein S16, putative
- 60S ribosomal protein L11a, putative
- 60S ribosomal protein L19
- 60S ribosomal protein L35, putative
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS5
- 60S ribosomal protein L7a
Sequence:
MAQRVHYRRHNHYNTKSNKVRPVRTPGGKLTIHVVKKKAGKPKCADCKTAIQGVKALRPADNYRARRKNRTVARAYGGSICARCIRERIMRAFLFEEQKCVRQVLKEKKKQEKKVKKVKKEKKKVNAKEVKKTATDNKKAKKVADKKKGK
Protein: Protein kinase C-binding protein 1 (Zinc finger and MYND domain containing protein 8) (D5LMF5)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MHPQSLADEEIKTEEEVVEGMDVTTRSKGPAVALPEGLPQDHGDSQQSNPGSTERPGQKRRFPSPQHSSNGHSPQDSSTSPSKKKKKPIMINSNNKEQSELRHGPFYYMKQPLTTDPVDVVPQDGRNDFYCWVCHREGQVLCCELCPRVYHAKCLKLTAEPEGDWFCPECEKITVAECIETQSKAMTMLTIEQLSYLLKFALQKMKQPGTEPFQKPVSLEQHPDYAEYIFYPMDLSTLEKNVKKKMYGCTEAFLAEAKWILHNCIIYNGGNHKLTQTAKVIIKICEHEMNEIEVCPECYLAACQKRENWFCEPCSNPHPLVWAKLKGFPFWPAKALRDKDGQVDARFFGQHDRAWVPMNNCYLMSKEIPFSVKKTKSIFNSAMQEMEVYVENIRKRFGVFNYAPFRTPYTPNNQYQMLLDTGNPSAGTAKTDKQEKIKLNFDMTASPKILMSKPLLNSSSGRRISLTDMPRSPMSTNSSVHTGSDVEQEAEKKVASSLFSASEESMDFTDKSTASPKSTKTGHGGGITDSPKPFSPQSTPVSSKQERSATTGSILNLNLDRSKAEMDLQELSESVLQQSTPTPLVSPKRQIRSRFQLNLDKTIESCKAQLGINEISDDVYTAVEHSDSEEYEKTDSSDSEYASDEEPKTKNEHEDGEDKVKAEKESSSSSSSASSFKKKAKPPASADTKDNTKITSTAAEKAADIPSKDKSGPEAPKEGIEKAKSAAKEKLKGKDETDSPTVRLGLDSDSESELVIDLGEDQAGRDGRKHKKEAKETLAKQQESKSPAVSNTSGQPQPETPILTRSATQAIPAVGVTVTTSALATVPVATASTGSPTKKQRPLLPKETVPTVQRVVWNSSSKFQTSSQKRHMQKVQRQQQQQQPVAAATTAAAATAATAVPQSPTGTRYQTRQAVKAVQQKDVIPATTTSTITLVTNAPPLAVAATPSNTLNPPISTDLPIATASADVAADIAKYTSKMMDAIKGTMTEIYNDLSKNTTGSTIAEIRRLRIEIEKLQWLHQQELAEMEHNLELTMAEMRQSLEQERDRLTAEVKKQMELEKQQAVDETKKKQWCANCKKEAIFYCCWNTSYCDYPCQQAHWPEHMKSCTQSATATQQEPDPELSTDKSTQPTSSIQPQSTEGSSTPKEKEVDKSKESVTVRIAGP
Protein: Retinoid isomerohydrolase (EC 3.1.1.64) (All-trans-retinyl-palmitate hydrolase) (Lutein isomerase) (Meso-zeaxanthin isomerase) (EC 5.3.3.22) (Retinal pigment epithelium-specific 65 kDa protein) (Retinol isomerase) (Q9TVB8)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore. Essential for the production of 11-cis retinal for both rod and cone photoreceptors. Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A9C3R9}. Cell membrane {ECO:0000250|UniProtKB:Q28175}; Lipid-anchor {ECO:0000250|UniProtKB:Q28175}. Microsome membrane {ECO:0000250|UniProtKB:Q28175}. Note=Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. Undergoes light-dependent intracellular transport to become more concentrated in the central region of the retina pigment epithelium cells (By similarity). {ECO:0000250|UniProtKB:Q16518, ECO:0000250|UniProtKB:Q28175}.
Interaction partners:
- Retinol dehydrogenase 5
- Lecithin retinol acyltransferase.
- Retinol dehydrogenase 10
- Retinol dehydrogenase 11
- Diacylglycerol O-acyltransferase 1
- Patatin like phospholipase domain containing 4.
- Acyl-CoA wax alcohol acyltransferase 2.
- MER proto-oncogene, tyrosine kinase.
- ATP binding cassette subfamily A member 4.
- Bestrophin
Sequence:
MSIQVEHPAGGYKKLFETVEELSSPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEVTDNALVNVYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAHPHIENDGTVYNIGNCFGKNFSIAYNIVKIPPLQADKEDPISKSEVVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLLKFLSSWSLWGANYMDCFESNETMGVWLHIADKKRKKYLNNKYRTSSFNLFHHINTYEDNEFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKKNARKAPQPEVRRYVLPLNIDKADTGKNLVTLPNTTATATLRSDETIWLEPEVLFSGPRQAFEFPQINYQKSGGKPYTYAYGLGLNHFVPDRLCKLNVKTKETWVWQEPDSYPSEPIFVSHPDALEEDDGVVLSVVVSPGAGQKPAYLLILNAKDLSEVARAEVEINIPVTFHGLFKKS
Protein: DNA polymerase alpha subunit B (Q381U6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA primase large subunit
- DNA primase
- DNA polymerase
- DNA polymerase epsilon catalytic subunit
- DNA polymerase
- DNA polymerase II subunit 2
- DNA polymerase delta subunit 2, putative
- Replication factor C, subunit 5, putative
- DNA polymerase
- Proliferating cell nuclear antigen
Sequence:
MQQSTRWKAAANLDLLLGIHHPAARIVRDYTAGSQINDGGVVDARNSVNFRDTMYCNRQDYGSNTTRRRLAGYYRYMLSKINLWEADGGGVILKGEEENPTDIKQEERDDVPSLQKPNEGSLYRARGILTQLCSPLATEEELLLPWEFFPIVNVDDDDTYAAPIRAMTKDVAPTGGFLRIENEDDDDGGATGGATDASGGEGASYHRNNPHSVSRLSLYTRLTPQFTGLYSGMVVGIVGEPFKRSSSGALTAVLVRRFILPSRPQFPWGIERPIPTALSHFAIPTRIHFCSGPFPRRETGHILSSVTLNALHRGADLLIIGGPLVREFEEYEKDSLKLLQLTFDELLSSYMDTIEETMEKYYASSKNPRTRDRMKVVLVPHRDDVTQIPAIPITMYSLESTDSIWVRSNPCRIAVNGIHIGVCNDDVVGDMREKMVERWPTESGSLRRVVEALVQSRLYAPLYEFPAVKHDLQHIGALRLDFLPPNPEGRLPKEDISTSALTWDAVRLLSAASVLNTLDSDGDTKQEAKRVKQEEDDQLVYPTNFSKCGEEDSTVEWMPHLLFLPSTRPRFAFVTHQHNEEALDDPAAASGVMVVNQEVWCRRTTPRFELRVAEVTVEDSERVVCRGASEVNGVVCGVIHFTNIAAAA
Protein: Embryonic developmental protein tofu-6 (21U-RNA biogenesis fouled up protein 6) (Maternal effect lethal protein 47) (Q09293)
Organism: Caenorhabditis elegans
Function: Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively. Promotes the biogenesis of 21U-RNAs. Required for chromosome segregation and cell division in early embryos. May have a role in DNA replication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Nucleus {ECO:0000269|PubMed:31216475}. Note=Dispersedly distributes throughout the cytoplasm in early embryos (PubMed:31147388). During early embryogenesis, localizes to the nucleus at prophase of cell division, and remains in the cytosol at interphase in 2- and 4-cell embryos (PubMed:31216475). Does not localize to cytoplasmic granules in oocytes and embryos (PubMed:31216475). Localizes to puncta in the perinuclear region in the germline syncytium (PubMed:31147388, PubMed:31216475). Localization to the perinuclear region in the germline is dependent on pid-1, tost-1, pics-1 and erh-2 (PubMed:31216475). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
Interaction partners:
- Protein pid-3
- Protein tost-1
- Eukaryotic translation initiation factor 4E-3
- Enhancer of rudimentary homolog 2
- K Homology domain-containing protein
- Protein pid-1
- Schlafen-like protein 1
- Schlafen-like protein 2
- Twenty One u-rna
- Enhancer of rudimentary homolog
Sequence:
MASSSTAYYLKDAGFHIRNIPKAWNDWNLFHVFQNFGKVSYCRVVGQSNDGQVQLGFVNMMSVADADEVRKNLNDGNLIGENFTLKVTDHKNVGGSLLPMASNSVQKLVSSPPSKSGPVLLSSSWLPLNKDIEVEVVDYLPSSSVAPDLFALTLLRINDSSMKEKYDSMHEKMNAYAQIVPFDSELEIGYDGVFRDAPRSVRRVRRISATKLYLVDFGKIINYEKAKCFQLPKVFQSMPTRVSLCGLDGLTWSPVAIPSFDNIREVVKKWGQMENSTLHAMACGFQGSINMINLFCGKSILADRLQRKGVCEYLPRSQQPHYAYSRETLLQHNNSGVTAQISNDADVVKDLLKKIDGVKNMLRELEL
Protein: E3 ubiquitin-protein ligase TRIM31 (EC 2.3.2.27) (Tripartite motif-containing protein 31) (Q9BZY9)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that acts as a regulator of antiviral immune response and inflammation by mediating ubiquitination of substrates. Acts as a regulator of innate immune defense against viruses by mediating 'Lys-63'-linked ubiquitination of MAVS, promoting MAVS polymerization and formation of three-stranded helical filaments on mitochondria. Acts as a negative regulator of the NLRP3 inflammasome by catalyzing 'Lys-48'-linked ubiquitination of NLRP3, leading to its degradation. Regulator of Src-induced anchorage independent cell growth (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18773414}. Mitochondrion {ECO:0000269|PubMed:18773414, ECO:0000269|PubMed:27992402}. Note=Predominantly expressed in the cytoplasm but a fraction is associated with the mitochondria (PubMed:18773414). Recruited t omitochondria after viral infection (PubMed:27992402). {ECO:0000269|PubMed:18773414, ECO:0000269|PubMed:27992402}.
Interaction partners:
- Mitochondrial antiviral-signaling protein
- Melanoma-associated antigen 1
- Ubiquitin-conjugating enzyme E2 D1
- T-cell receptor-associated transmembrane adapter 1
- NACHT, LRR and PYD domains-containing protein 3
- Trimethyllysine dioxygenase, mitochondrial
- HLA class I histocompatibility antigen, alpha chain F
- Gamma-butyrobetaine dioxygenase
Sequence:
MASGQFVNKLQEEVICPICLDILQKPVTIDCGHNFCLKCITQIGETSCGFFKCPLCKTSVRKNAIRFNSLLRNLVEKIQALQASEVQSKRKEATCPRHQEMFHYFCEDDGKFLCFVCRESKDHKSHNVSLIEEAAQNYQGQIQEQIQVLQQKEKETVQVKAQGVHRVDVFTDQVEHEKQRILTEFELLHQVLEEEKNFLLSRIYWLGHEGTEAGKHYVASTEPQLNDLKKLVDSLKTKQNMPPRQLLEDIKVVLCRSEEFQFLNPTPVPLELEKKLSEAKSRHDSITGSLKKFKDQLQADRKKDENRFFKSMNKNDMKSWGLLQKNNHKMNKTSEPGSSSAGGRTTSGPPNHHSSAPSHSLFRASSAGKVTFPVCLLASYDEISGQGASSQDTKTFDVALSEELHAALSEWLTAIRAWFCEVPSS
Protein: Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (KAT/AadAT) (2-aminoadipate aminotransferase) (2-aminoadipate transaminase) (EC 2.6.1.39) (Alpha-aminoadipate aminotransferase) (AadAT) (Glycine transaminase AADAT) (EC 2.6.1.4) (Kynurenine aminotransferase II) (Kynurenine--glyoxylate transaminase AADAT) (EC 2.6.1.63) (Kynurenine--oxoglutarate aminotransferase II) (Kynurenine--oxoglutarate transaminase 2) (EC 2.6.1.7) (Kynurenine--oxoglutarate transaminase II) (Methionine--glyoxylate transaminase AADAT) (EC 2.6.1.73) (Q8N5Z0)
Organism: Homo sapiens (Human)
Function: Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Kynurenine--oxoglutarate transaminase 1
- Kynurenine 3-monooxygenase
- Kynureninase
- Kynurenine--oxoglutarate transaminase 3
- Kynurenine formamidase
- 2-oxoadipate dehydrogenase complex component E1
- Alpha-aminoadipic semialdehyde dehydrogenase
- Dihydrolipoyl dehydrogenase, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
Sequence:
MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKTIQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQGLCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKPEDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNKFRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQLMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKVKGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQLIKESL
Protein: Checkpoint suppressor homologue (Q9U1H1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
PYDPLVHTNNKPPYSFSSLIFMAIEGSNEKALPVKEIYAWIVQHFPYFKTAPNGWKNSVRHNLSLNKSFVKVEKAPNMGKGSLWRVEPQQRQNLIQALNRSPFFPNSAVDKISPSLKSPS
Protein: Multidrug transporter TPO3 (Drug:H(+) antiporter TPO3) (DHA TPO3) (Polyamine transporter 3) (Q6FQ03)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Involved in the resistance to the imidazole antifungal drugs tioconazole, miconazole, clotrimazole and ketoconazole; to the triazole fluconazole; but not to the antifungals flucytosine or amphotericin B. Plays a role in spermine homeostasis, but spermine accumulation in response to clotrimazole is independent of TPO3.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24576949}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome L complete sequence
Sequence:
MVDQESLVSFSSETSQSINSDIDIESQQQPRQYIPSNEKDGNKERLHLTRTETVKSLQEMGMTQDAPIPDVNAPQTTTKNAIFPEEYTMETPTGLVPVATLQSLGRTSTAISKSRTRQIERSVSRRSQNIAASSNSSNKEELEDEEEVSSDMSNQQPELDPEIEFVTFVTGDPTNPHNWPLWIRWAYTVILSCLVICVAYGSACITGGLFTVQEQYHVGLEAAILSCSLMVIGFSLGPLIWSPVSDLYGRRLAYFISMGLYTIFNIPCALSPNLGGLLVCRFLCGVFSSSGLCLVGGSIADMFPSETRGRAIAFFAFAPYTGPIIGPLVNGFVSVCTRRMDLIFWINMAFAGVMWIIVAFIPETYAPVILKWRAAKLRKETGNPKIMTEQEAQGVSVNEMMKACLIRPLYFAVTEPVLDLTCFYVCLIYSLLYAFFFAFPVVFGELYGYKDNLIGLMFIPILIGATMALATTFYCENEYLKLVKKRKPTPEDRLFGAMIGAPFAAAALWILGATSYKHIIWVGPASSGLAFGYGMVLIYYSLNNYIIDCYVQYASSALATKVFLRSAGGAAFPLFTNQMYHKLGLQWASWLLAFISTAMILLPFGFYYYGKTLRHKLSKKDYSIDTIEGY
Protein: Nucleosome assembly protein 1-like 1-B (xNAP1L-B) (Nucleosome assembly protein 1) (NAP1) (xNAP-1) (Q7ZY81)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as a chaperone for the linker histone to facilitate deposition of histone B4 onto linker DNA. Required for both remodeling of sperm chromatin into nucleosomes, and linker histone binding to nucleosome core dimers. Plays a role in tissue-specific gene regulation. Required for primitive hemopoiesis, acting upstream of tal1/scl (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q4U0Y4}. Nucleus {ECO:0000250|UniProtKB:Q4U0Y4}. Note=Cytoplasmic prior to the midblastula transition, becoming predominantly nuclear subsequently. {ECO:0000250|UniProtKB:Q4U0Y4}.
Interaction partners:
Sequence:
MANIDNKEQTELDQQDMEDVEDVEEEETGEEANSKARQLTAQMMQNPQVLAALQERLDDLVGTPTGYIESLPKVVKRRVNALKNLQVKCAQIEAKFYEEVHELERKYAALYQPFFEKRSDIINASYEPTEEECEWKVDEEEDIAEDLKEKAKLEEEKKDEEKEDPKGIPEFWLTVFKNVDLLSDMVQEHDEPILKHLKDIKVKFSEAGQPMNFMLEFHFEPNEFFTNELLTKTYKMRSEPDESDPFSFDGPEIMGCTGCLIDWKKGKNVTLKTIKKKQKHKGRGTVRTVTKTVPNDSFFNFFSPPEVPENGELDDDAEAILTADFEIGHFLRERIIPRSVLYFTGEAIEDDDDDYDEEGEEADDEEGEEEADEDHDPDFDPKKAQNPAECKQQ
Protein: fMet-Leu-Phe receptor (fMLP receptor) (N-formyl peptide receptor) (FPR) (N-formylpeptide chemoattractant receptor) (P33766)
Organism: Mus musculus (Mouse)
Function: High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors. Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Receptor for TAFA4, mediates its effects on chemoattracting macrophages, promoting phagocytosis and increasing ROS release (By similarity). Receptor for cathepsin CTSG, leading to increased phagocyte chemotaxis (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:8244972}; Multi-pass membrane protein {ECO:0000255}. Note=Internalizes in presence of its ligand, TAFA4. {ECO:0000250|UniProtKB:P21462}.
Interaction partners:
- Annexin A1
- Formyl peptide receptor 2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MDTNMSLLMNKSAVNLMNVSGSTQSVSAGYIVLDVFSYLIFAVTFVLGVLGNGLVIWVAGFRMKHTVTTISYLNLAIADFCFTSTLPFYIASMVMGGHWPFGWFMCKFIYTVIDINLFGSVFLIALIALDRCICVLHPVWAQNHRTVSLAKKVIIVPWICAFLLTLPVIIRLTTVPNSRLGPGKTACTFDFSPWTKDPVEKRKVAVTMLTVRGIIRFIIGFSTPMSIVAICYGLITTKIHRQGLIKSSRPLRVLSFVVAAFFLCWCPFQVVALISTIQVRERLKNMTPGIVTALKITSPLAFFNSCLNPMLYVFMGQDFRERLIHSLPASLERALTEDSAQTSDTGTNLGTNSTSLSENTLNAM
Protein: G-protein coupled receptor 20 (Q99678)
Organism: Homo sapiens (Human)
Function: Orphan receptor with constitutive G(i) signaling activity that activate cyclic AMP.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18347022}; Multi-pass membrane protein {ECO:0000269|PubMed:18347022}.
Interaction partners:
- G-protein coupled receptor 22
- Probable G-protein coupled receptor 21
Sequence:
MPSVSPAGPSAGAVPNATAVTTVRTNASGLEVPLFHLFARLDEELHGTFPGLWLALMAVHGAIFLAGLVLNGLALYVFCCRTRAKTPSVIYTINLVVTDLLVGLSLPTRFAVYYGARGCLRCAFPHVLGYFLNMHCSILFLTCICVDRYLAIVRPEGSRRCRQPACARAVCAFVWLAAGAVTLSVLGVTGSRPCCRVFALTVLEFLLPLLVISVFTGRIMCALSRPGLLHQGRQRRVRAMQLLLTVLIIFLVCFTPFHARQVAVALWPDMPHHTSLVVYHVAVTLSSLNSCMDPIVYCFVTSGFQATVRGLFGQHGEREPSSGDVVSMHRSSKGSGRHHILSAGPHALTQALANGPEA
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FVK2)
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 I complete sequence
- Ribosomal RNA-processing protein 43
- 5'-3' exoribonuclease 1
- Candida glabrata strain CBS138 chromosome E complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome B complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
Sequence:
MSDIYTEFSESVFSERHGQHQYLKMAHANMYGNGGASEVQNVEIQPEADDYEARIKEIEEYYLKTLLNEEPSKRNSGYVGASGIKSVPSLELDDQANPSSSSSDVSIQDISTSPGMMYSKFNTHLVGNSPAVYGAAANNALFNNLNSLNESQYIYGKSINNESLYFRQQQQLQQQQQQQQQQQQLLQQQQLQQQLQLQQQQPTFLDSNVQTNYANQEFVNSQANVTPLNYTNIFNNEISAKPAKTHKINPFLQDKQVSRKSNLEVDIKHHYQANALPLTSENLQKMQDLSIDDMPIESINRKKFHIQKTTVDPTKQINSEPKVKEHQQQQQQQQINKGLYKTELCETFTTKGFCKYGNKCQFAHGLQELKLKKTSNNFRTKPCINWDKLGYCPYGKRCCFKHGDDRDIQIYKKAGTYTANPDGSDASERKLTEVQIKQKNLHANIKKLQKMTW
Protein: Calcium permeable stress-gated cation channel 1 (SpCSC1) (Q09809)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as an osmosensitive calcium-permeable cation channel.
Subcellular location: Vacuole membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAFNGYGIFDSDPRKNPSSDLRTQFWLAFLLGASACVFFCFFRKRWKVLYAPRTTIEGLNLPTLSSSYYKWLMDLVNIPDDVVQNCAGLDGYVFLLFFKMGIKFLSFASLLGVLIIMPVNKHFRGDAFGNITLSMPAKSEYFFSSPLVKKSIVQSPIIANGSELNVGVLGPSLFNPIGNLSDIPGLPQPGDGFLYLYVLFTYFISIFLLYVLFSSTKSIADIRQSYLARQNRLTDRTVFISGLPNELCSTENLKAYFDKLDVGSIDSLSICRNYSYMDILLSKKSKYVKKLEKYWSIYLSNCKKLGISTLPPSNYLSPNRAELESTPEQLLEVPWQHHQCHPLIKTHFFGIFGQKIDAIDFYSAKLYKISQQIENARSFDYPTTGQAFITFESMATAQIVAQTHIDSKSLMGLHIELAPAANDIQWHNTYIGRWHKFFQGWFITLVTFMIILLWTVPVGAIAVFINLDTIRRLWPELGRMIEDLPFLNSLLRTFLPTLVYSLFISISPFLFRWLSSMQGLSSRAEEEIYAVGKNYAYLFVNFFLVYVIAGSTSIWELAKDTTSFAHFLANRLPHQAQFFIDLIVLQGIGMFPLKLIQLGKLSSYFVRRSFVPYSIASKKFETPDSFSVGIFLPQPMFIMLICLCYSIISPLILVFGLIYFIIGFLVYKYELIYQMEHPQHSTGELWSTIFLRMIFGCVIMQLTMMGLMSLRKAYWLSTVIFPLLCFTVISAYNFSTMIRSSMQFVSLYYIRTHQSNTLSSESESRNSESSGSYVHPGFDLSNEELPLIDLNTA
Protein: Long-chain-fatty-acid--CoA ligase 6 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 6) (LACS 6) (Long-chain-fatty-acid--CoA ligase, brain isozyme) (P33124)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid.
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UKU0}; Single-pass type III membrane protein {ECO:0000250}.
Interaction partners:
- Fatty acid synthase
- Carnitine O-palmitoyltransferase 1, liver isoform
- Lipoprotein lipase
- Lysosomal thioesterase PPT2
- Palmitoyl-protein thioesterase 1
- Palmitoyl thioesterase CPT1C
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Fatty acid CoA ligase Acsl3
- Acylglycerol transacylase
- Long-chain-fatty-acid--CoA ligase 4
Sequence:
MQTQEILRILRLPELSDLGQFFRSLSATTLVSMGALAAILAYWLTHRPKALQPPCNLLMQSEEVEDSGGARRSVIGDCTQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEQFIGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSIRYIINTADICTVIVDKPHKAILLLEHVERKETPGLKLVILMEPFDDALRERGKKCGVDIKSMQAIEDSGQENHRVPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTESQWAPTCADVHFSYLPLAHMFERMVQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQAEVRSGIIRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTSKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPCWAQKKGIEGNYQELCKSKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM
Protein: Large ribosomal subunit protein uL22c (50S ribosomal protein L22, chloroplastic) (P0C444)
Organism: Oryza sativa (Rice)
Function: This protein binds specifically to 23S rRNA.
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MTSFKLVKYTPRIKKKKSGLRKLARKVPTDRLLKFERVFKAQKRIHMSVFKVQRVLDEIRWRYYEETVMILNLMPYRASYPILKLVYSAAANATHYRDFDKANLFITKAEVSRSTIMNKFRPRARGRSSPIKKTMCHITIVLNIVKKSK