wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha/beta-Hydrolases superfamily protein (F4JBL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Prolyl endopeptidase
- Prolyl endopeptidase
- Dihydroorotase, mitochondrial
- Acylamino-acid-releasing enzyme
Sequence:
MDSSQGSTQQKIVILNSHNENLVGLLHETGSTEIVVLCHGFRSNKNFEIMKNVAVAIEREGISAFRFDFSGNGYVFLSCIILNKLVFVLTLGLWCFHSFRESEGSFYYGNYNYEADDLHSVIQYFSNLNRVVTIILGHSKGGDVVLLYASKYHDIPNVINLSGRYDLKKGIGERLGEDFLERIKQQGYIDVKDGIVIALRFSCTVIRTLVLLSMYWFVTGDSGYRVTEESLMDRLNTDMHEACLKIDKECRVLTVHGSGDETVPVEDAKEFAKIIPNHELQIVEGADHCYTNYQSQLVLTVMEFIKSHCEEKNDKTCN
Protein: RNA helicase (EC 3.6.4.13) (Q56TY6)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MLSKRNREGSRGAMGCGEKNPYTGRVLSSRYHALRGVREKLPIFAAKQKIQRLISRYQTLLLVGETGSGKTTQVPQFVLEMNPEHAIACTQPRRVAAISVSERVAEELDVTLGEEVGYCIRFDDTSSDRTRLKYLTDGMLLREAMGDPMLQRYSVIILDEAHERTVHTDILIGAVKDLLHRRPDLRVVVMSATLEERRFQSYFPEAPLVHVSGRMYDVEVYNSRLPEANYLEASIRTAMQIHLYEGPGDILIFLTGEDEIEQAVERLRLGIPMAEHTNADCHKGPVAVLPLYSALPPKEQRKVFQAAPEGTRKIVVATNVAETSLTIDGVVFVIDSGFSKQKVYNPKLRVESLLVTPISQASARQRCGRAGRTRPGKCFRLYTAKAFDTLLQQQTYPEILRCNLGSVILHMKMMGIEDLVNFDFVEPPAPETLMRALELLNYLGAINDDGDMTKFGRRVADFPLEPEMAAMLLHSPEYGCSDDIARICAMMSVQSPFVTPRNDQRGCAMRCRDQFYHPTGDHLALLNVFNAFYEGSNQSGSWASENYLNPRVMKQSVSIYRQLIGIMRRLNLSICSTYSAAQWGGAGDGESDEYANEVRRAVLRGYFTKVALSLPTKNQFLTLKDNVKCLLFPSTFLNRRPKFVVFNELVLTTNTYIRTVTSVSDEWLLEVNPLYFDPSEFEGVSRQVFEELHRRNNRNNAAERDQNKDCLTGHKRRRGGDAPDNGDDDDDDDSS
Protein: Coatomer subunit epsilon (Epsilon-coat protein) (Epsilon-COP) (Q28104)
Organism: Bos taurus (Bovine)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit alpha
- Coatomer subunit delta
- Coatomer subunit beta'
- Coatomer subunit beta
- Coatomer subunit gamma-1
- Coatomer subunit zeta-1
- Protein SEC13 homolog
- Coatomer subunit gamma-2
- Coatomer subunit zeta
- ADP-ribosylation factor 1
Sequence:
MAPPAPGPASGGSGEVDELFDVKNAFYIGSYQQCINEAQRVKPSSPERDVERDVFLYRAYLAQRKYGVVLDEIKPSSAPELQAVRMFAEYLASDSRRDAIVAELDREMSRSVDVTNTTFLLMAASIYFYDQNPDAALRTLHQGDSLECMAMTVQILLKLDRLDLARKELKKMQDQDEDATLTQLATAWVSLAAGGEKLQDAYYIFQEMADKCSPTLLLLNGQAACHMAQGRWEAAEGVLQEALDKDSGHPETLINLVVLSQHLGKPPEVTNRYLSQLKDAHRSHPFIKEYRAKENDFDRLVLQYAPSA
Protein: Leucine aminopeptidase 1 (EC 3.4.11.-) (Leucyl aminopeptidase 1) (LAP1) (Q8J2N2)
Organism: Aspergillus sojae
Function: Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MRFLPCIATLAATASALAIGDHIRSDDQYVLELGPGETKVVTEAEKWALRAEGKRFFDITGRTSSLELASNKKQKLAVTYPDSVQHNETVQNLINSLDKKNFETVLQPFSEFHNRYYKSDNGKKSSEWLQGKIQEIISASGAKGVTVEPFKHFFPQSSLIAKIPGKSDKTIVLGAHQDSINLNSPSEGRAPSADDDGSGVVTILEAFRVLLTDEKVAAGEAPNTVEFHFYAGEEGGLLGSQDIFEQYLQKSRDVKAMLQQDMTGYTKGTTDAGKPESIGIITDNVDENLTKFLKIIVDAYCTIPTVDSKCGYGCSDHASATKYGYPAAFAFESAFGDDSPYIHSADDTIETVNFDHVLQHGRLTLGFAYELAFADSL
Protein: cGMP-dependent protein kinase interacting domain-containing protein (G5ECD7)
Organism: Caenorhabditis elegans
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha
- Rho-associated protein kinase let-502
- Serine/threonine-protein kinase pak-1
- Myosin regulatory light chain
- Myosin-11
- Serine/threonine-protein kinase mrck-1
- Myosin-11
- Serine/threonine-protein kinase max-2
- DH domain-containing protein
- Rho GTPase-activating protein 20
Sequence:
MGQDDEDDAHMLQAKQQITFNVVNKRKDQLRRWQSSEMNAEAARRTKRPKVQFQDSDIFLSACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHGADLSIVNSDKELALDLAVDEQCRDYLDDDYKRQMIDLDACRDQELQTMLKDVNMWMSQGEYRDIPHHRTGGTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAELSDLTFTGADVLGVADKECIDYLVELADTVKVQNKRKSPGSGSQPPTSILQEKNHRMPSHEEHVLTSERKRDLQHKDQHSENEFLHSHPSTASVGSTTSSNTNTTTTTIVIGENDISAAQKDSRESSKESAVDDEEYVAEDEMEEAEEDEEEEDVEEEEEEKSEAELKNGKEISPLRSETTSSRSISITRSLDGYTDRSSSGRETSAEMSEAASSASTGTTSSSSRFTSSTPSSQRSAAGSVHTETPRSSMENSSSVGSGDQNVSATIPIVPLSAPPKAVHQSPSSWINRGVPLSSRSSTSSVTRSSSTPVSEIISPPSSIHSQLSFPSVSNTTTTTATVAPTSSTVPSTPVSNVMAATISSTAKNTPSPAGSVTTINATFSKPSSRHPSEEVYRSPSQPTNVPWASLWHNVNNASTGQIRSHIEQLRNASFSSLSSYPRVSAFRSPIKTTASSTSVNSASSPLLLQPHPHPPVIAEYPRGFVPQQINPNKMSRWQSKTVTESEAERRNNSRMQRQHRRSTQGVTKEQLEEASKFATDEVARRNSQVLSTYPNSLHARLASEEKDLSSTSDDLKDGDVSTTATVSLINSPNSNSANVRRKSQGLSISRSNRRATGPVNPEDLAPAMSLRLATAQPYSPASVRSNAGTLPTMTSRFSEKAQSLPPASNGMSSTQPLSTRSAIVAGLSSAPSMRTTAPLSSTATSSRFMPSSSLSSNGSSANQQPSSIYGLQSRPTETNLNYKALFEKERSECERLRREMEEMRRSQTADSYRGASTQLAWRARNASPSAQPHNLSVAKSTSLASFDENERRSMERKISDLELQLKTATNLRMENQRLKEENGALVRVISKMTI
Protein: Stomatin (A0A8I6GAW8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MPDNSKAELGPCGWILVAVSFIFVLITFPISIWICIKIVKEYERVIIFRLGRILQGGAKGPGLFFILPCTDSFIKVDMRTISFDIPPQEVLTKDSVTISVDGVVYYRVQNATLAVANITNADSATRLLAQTTLRNALGTKNLSQILSDREEIAHHMQSTLDDATDDWGIKVERVEIKDVKLPVQLQRAMAAEAEAAREARAKVIAAEGEMNASRALKEASMVITESPAALQLRYLQTLTTIAAEKNSTIVFPLPIDMLQGIMGSHH
Protein: Thylakoid lumenal 29 kDa protein, chloroplastic (TL29) (EC 1.-.-.-) (AtAPx07) (P29) (Probable L-ascorbate peroxidase 4) (P82281)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11034343, ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:19828564}.
Interaction partners:
- Glutathione S-transferase DHAR3, chloroplastic
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase DHAR2
- Monodehydroascorbate reductase 3
- Monodehydroascorbate reductase 2
- Thylakoid lumenal 17.4 kDa protein, chloroplastic
- PsbP domain-containing protein 4, chloroplastic
- Monodehydroascorbate reductase 4, peroxisomal
- Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic
Sequence:
MGGVSFLSTVPSFTNTTNHQHLTTLSSSSHRSAVIRCSKIEPQVSGESLAFHRRDVLKLAGTAVGMELIGNGFINNVGDAKAADLNQRRQRSEFQSKIKILLSTTIKAKPELVPSLLKLALNDAMTYDKATKSGGANGSIRFSSELSRAENEGLSDGLSLIEEVKKEIDSISKGGPISYADIIQLAGQSAVKFTYLASAIRKCGGNEEKGNLLYTAYGSAGQWGLFDRNFGRSDATEADPEGRVPQWGKATVQEMKDKFIAVGLGPRQLAVMSAFLGPDQAATEQLLATDPQVAPWVQKYQRSRETVSQTDYEVDLITAFTKLSCLGQQINFEAYTYPVERINLSKLKL
Protein: Long-chain specific acyl-CoA dehydrogenase, mitochondrial (LCAD) (EC 1.3.8.8) (P51174)
Organism: Mus musculus (Mouse)
Function: Long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, long-chain specific acyl-CoA dehydrogenase can act on saturated and unsaturated acyl-CoAs with 6 to 24 carbons with a preference for 8 to 18 carbons long primary chains.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P15650}.
Interaction partners:
- Trifunctional enzyme subunit beta, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Carnitine O-palmitoyltransferase 2, mitochondrial
- 3-ketoacyl-CoA thiolase B, peroxisomal
- Enoyl-CoA hydratase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- 3-ketoacyl-CoA thiolase A, peroxisomal
- Peroxisomal bifunctional enzyme
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MAARLLLRSLRVLKARSAPRPPPSARCSHSGAEARLETPSAKKLTDVGIRRIFSSEHDIFRESVRKFFQEEVIPHHTEWEKAGEVSREVWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEKFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIVVAVTNREARSPAHGISLFLVENGMKGFIKGRKLHKMGMKAQDTAELFFEDVRLPANALLGEENKGFYYLMQELPQERLLIAELAISACEFMFEETRNYVKQRKAFGKTVAHIQTVQHKLAELKTHICVTRAFVDSCLQLHETKRLDSGSASMAKYWASELQNSVAYECVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKELIARQIVSDS
Protein: Probable ATP-dependent RNA helicase DDX4 (EC 3.6.4.13) (DEAD box protein 4) (Q5W5U4)
Organism: Bos taurus (Bovine)
Function: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q61496}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q61496}.
Interaction partners:
- RAN binding protein 9
- Deleted in azoospermia-like transcript variant 1.
- Synaptonemal complex protein 3
- Stimulated by retinoic acid 8
- Muellerian-inhibiting factor
- Nanos C2HC-type zinc finger 3
- Protein maelstrom homolog
- PR/SET domain 14
- Growth/differentiation factor 9
- Piwi-like protein 2
Sequence:
MGDEDWEAEIIKPHISSYVPVFEKDRYSSGANGDTFNRTPASSSEMGDGSSRRDHFMRSGFASGRSLGNRDPGESNKRENTSTVGGFGVGKSFGNRGFSNNKFEEGDSSGFWRESSIDCEDNQTRNRGFSKRGGYQDGNDSEALGSSRRGGRGSFRGCRGGFGRGSPNSDYEQDEGTQRSGGIFGSRRSALSGAGNGDTFQSRSGGGSGRGGYKGLNEEVITGSGKNSWKSEAEGGESGDTQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDPPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIIQGGRDLMACAQTGSGKTAAFLLPILAHMMRDGITASRFKELQEPECIIVAPTRELINQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDVIGKEKIGLRQVKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAGEFLKSNYLFVAVGQVGGACRDVQQTILQVGQYSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRCGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDSQLAQPLVKVLSDAQQDVPAWLEEIAFSTYGPGFSGNARGNVFASVDTRKNYPGKSSLNTAGFSSTQAPNPVDDESWD
Protein: Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 1 (Q6ZVC0)
Organism: Homo sapiens (Human)
Function: Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis.
Interaction partners:
Sequence:
MNLLYRKTKLEWRQHKEEEAKRSSSKEVAPAGSAGPAAGQGPGVRVRDIASLRRSLRMGFMTMPASQEHTPHPCRSAMAPRSLSCHSVGSMDSVGGGPGGASGGLTEDSSTRRPPAKPRRHPSTKLSMVGPGSGAETPPSKKAGSQKPTPEGRESSRKVPPQKPRRSPNTQLSVSFDESCPPGPSPRGGNLPLQRLTRGSRVAGDPDVGAQEEPVYIEMVGDVFRGGGRSGGGLAGPPLGGGGPTPPAGADSDSEESEAIYEEMKYPLPEEAGEGRANGPPPLTATSPPQQPHALPPHAHRRPASALPSRRDGTPTKTTPCEIPPPFPNLLQHRPPLLAFPQAKSASRTPGDGVSRLPVLCHSKEPAGSTPAPQVPARERETPPPPPPPPAANLLLLGPSGRARSHSTPLPPQGSGQPRGERELPNSHSMICPKAAGAPAAPPAPAALLPGPPKDKAVSYTMVYSAVKVTTHSVLPAGPPLGAGEPKTEKEISVLHGMLCTSSRPPVPGKTSPHGGAMGAAAGVLHHRGCLASPHSLPDPTVGPLTPLWTYPATAAGLKRPPAYESLKAGGVLNKGCGVGAPSPMVKIQLQEQGTDGGAFASISCAHVIASAGTPEEEEEEVGAATFGAGWALQRKVLYGGRKAKELDKVEDGARAWNGSAEGPGKVEREDRGPGTSGIPVRSQGAEGLLARIHHGDRGGSRTALPIPCQTFPACHRNGDFTGGYRLGRSASTSGVRQVVLHTPRPCSQPRDALSQPHPALPLPLPLPPQPARERDGKLLEVIERKRCVCKEIKARHRPDRGLCKQESMPILPSWRRGPEPRKSGTPPCRRQHTVLWDTAI
Protein: Targeting protein for Xklp2 (A2APB8)
Organism: Mus musculus (Mouse)
Function: Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules. Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation. TPX2 is inactivated upon binding to importin-alpha. At the onset of mitosis, GOLGA2 interacts with importin-alpha, liberating TPX2 from importin-alpha, allowing TPX2 to activates AURKA kinase and stimulates local microtubule nucleation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9ULW0}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:27753540}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9ULW0}. Note=During mitosis it is strictly associated with the spindle pole and with the mitotic spindle, whereas during S and G2, it is diffusely distributed throughout the nucleus. Is released from the nucleus in apoptotic cells and is detected on apoptotic microtubules. {ECO:0000250|UniProtKB:Q9ULW0}.
Interaction partners:
- Transcription factor RelB
- Transcription factor p65
- Nuclear factor NF-kappa-B p105 subunit
- Proto-oncogene c-Rel
- Aurora kinase A
- Nuclear factor NF-kappa-B p100 subunit
- Transforming acidic coiled-coil-containing protein 3
- Cytoskeleton-associated protein 2-like
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cyclin-A2
Sequence:
MSQVPTTYSFDAPTDFINFSSLDAEEDTENIDSWFDEKANLENKFLRQRGIGEPFQGKNSLRKAKLQQGFVTPLKAVDNTYHKETEKENLQKQSIPSNDCSSLDAKRAVSGNTPVQPQRRSIRLSAQKDLEQKEKNHVASVEMKAKRCVAPATDCPPQKRMKVSHKKKLEEEEEGSAPATSRKNERETLEKAKGKHTVPGVPPAREKVLKSTEEQEIEKRLRMQQEVVELRRKNEEFKKLALAGPGQPVKKSTSQVTKTVDFHFLTDERIKQHPKNQEEYKEVNFMSELRKHSSTPARGTRGCTIIKPFNLSKGKKRTFDEAASTYVPIAQQVEAFHKRTPNRYHLRNKKDESLLPSKSVNKIARDPQTPILQTKYRTRAVTCKSTAEQEAEELEKLQQYKFKARELDPRIFESGPILPKRAPVKPPTQPVGFDLEIEKRIHERESKKKTEDEQFEFHSRPCPTKILEDVVGVPEKKVIPATVPKSPVFALKNRIRVPIKDEEEEKPVVIKAQPVPHYGVPYKPHIAEARNVEVCPFSFDTRDKERQLQKEKKIKEMQKGEVPKFKALPVPHFDTINLPEKKVKNVTQAEPFSLETDKRGAYKAEMWKHQLEEEQKQQKDAACFKARPNTVIFQEPFVPKKEKKSLAENPSGSLVQEPFQLATERRAKERQELEKKMAEVEAWKLQQLEEVRQQEEEQQKEELARLRKELVHKANPIRKYAAVEVKSSELPLTVPVSPKFSTRFQ
Protein: GTP-binding protein, putative (Q386P6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pescadillo homolog
- Ribosome biogenesis protein BOP1 homolog
- Nucleolar GTP-binding protein 1
- NLE domain-containing protein
- rRNA processing protein, putative
- RNA-binding protein, putative
- Nucleolar complex protein 2
- Nucleolar protein, putative
- Ribosome assembly factor mrt4
- Ribosome biogenesis protein NSA2 homolog
Sequence:
MGGQSKKHGKGGGGGGGHGRNCHPQQRKKLTKDPGVPDLKKVAQNLTRTARNRNRSLFSIPALRGSNKIAAASGEKEPQEQGNEEARVAAERRAMTLLAVQCAEKVHHYEVPQQWIGESENINDMDDDVERRGVDRSLRRFYKEFQKVVENSDVLLQVVDARDPLGCRLNQLERTIRSQFGEDKKKMVMVLNKADLLPSKETVDAWVHFFEEHEGIMCIPFAATAKGASGHTYVANMFRRLRALATSEETGARKAIVVGVIGYPNVGKSSVINALKRKHVVGVGNMPGFTTGNTEVELRSDIRVMDCPGVVAPGEDCGDVVLRNAVKVSDLADPFTPVQRLLQRCAQVTLDPSQQQHSQYLSAGVHPLGLFYSIGSFDPSDVMSFIRLVGQRRGRLLQGGVVDEEGTARMILHDWNDGRIAYYTLPPTSDLFGRTTLTADPGEGLTGCEEYGESGPQLVDGFAQGLQWEGLPTFHLSWSKMKSGVQ
Protein: Eukaryotic translation initiation factor 4 gamma 1 (M0RD03)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Eukaryotic translation initiation factor 4 gamma 1
- Similar to eukaryotic translation initiation factor 4E member 3
- Eukaryotic translation initiation factor 4, gamma 2.
Sequence:
MLTLALDTTFPPSPFAISVGPFLVPSSALSNRCWGDPDVAPNEMNKAPQPTGPPPARSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQGGFRSLQHFYPSRAQPPSSAASRVQSAAPARPGPAPHVYPAGSQVMMIPSQISYSASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQSVQQFPASVAPAPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGSLEPQPNGESPQVAVIIRPDDRSQGAAIGGRPGLPGPEHSPGTESQPSSPSPTPSPPPILEPGSESNLGVLSIPGDTMTTGMIPISVEESTPISCESGEPYCLSPEPTLAEPILEVEVTLSKPIPESEFSSSPLQVSTSLVPHRAETHEPNGVIPSEDLEPEVESSTEPAPPPLSACASESLVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVPSAALASIVSPTPPVAPSDTSAAQEEEIEEDEDEDGEAESEKGGEDLPLDSTPVPAQLSQNLEVAAAPQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEVDPAVPEVENQPPTGSNPSPESEGSAALPQPEEAEETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHITDVVLDKANKTPLRSLDPSRLPGINCGPDFTPSFANLGRPTLSSRGPPRGGPGGELPRGPAGLGPRRSQQGPRKETRKIISSVIMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFAKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRQSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGGDKRRGGPPGPPVNRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDTASEATRPATLNRFSALQQTLPVENTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRGRDPVKREATLPPVSPPKAALAVDEVERKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRLGIESTLERSTIAREHMGRLLHQLLCAGHLSTAQYYQGLYETLELAEDMEIDIPHVWLYLAELITPILQEDGVPMGELFREITKPLRPMGKATSLLLEILGLLCKSMGPKKVGMLWREAGLSWREFLAEGQDVGSFVAEKKVEYTLGEESEAPGQRALAFEELRRQLEKLLKDGGSNQRVFDWIEANLNEQQIASNTLVRALMTTVCYSAIIFETPLRVDVQVLKVRARLLQKYLSDEQKELQALYALQALVVTLEQPANLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFNWLREAEDEESDHN
Protein: Thin, isoform E (A0A0B4LFW8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEQFEQLLTCCVCLDRYRIPKLLPCQHSFCMEPCMEGLVDYVRRQVKCPECRAEHRIPYNGVQAFPTNVTLQRFLELHIEITGELPDPTSGQIMERCGVCSEKAYLSHCAHCEKKICEDCKSAHMDILRREITRFNSQIRRSLHRLQDSLAIIEKNTMSLQTNAISVTEEIDEIYQRITKAIKDRSDQLKGEIDRYLAVELRNLTTLKENLDLEITNITSNCDTVDKYMNETVEWDDCELMDTKEIFLKTVEFLRHFEYENNDYSRRVRFLVSIDPNQLVMNLATFGDLNIAPHSTPSGGSVSSSHLAPPSALQPGLMRSKSDHRLATQFRQQEERSGYNDEPVLGGRKFGERPQRSATQANNDRYGRSGGDYDYENDYDNEGSSGRAGKSSRFRSRFVRSHQNDDSDSEQQQQQRQQELKERKDRVLDSEDVSRGQLSGIIRLSDCSRVVQRLADIGKEKKEKKSDAAAAAQAAVQAAIQAQKAAMQRQQQKNQQNAADEEELARQKRKNAGSSSTGGAATSTSSGGGDTASDQRVAALKNRGGEESDGSSNQAASPVRNSAASTTRAETASATDSDATPTPTIQQSKPPVSAQVAAVKKTQRSGSSDSSASTESSASSAAAAAVAATSTSATAAAPATSSSNSTSQNAKAPSSSRYSTARDTTAVPEKKPFVSRFLPQHSTASTTNGSADKKKAESSSSSEEETSSESESESEPETKAKSSATSSTTNTKSTPNSAASSTTAASSSTTSGSYRDRLEARRASRDDSSSTAAGRSSYATPSSSGYGSGSGTTGGRTRAVPAPHHTSESEDRYGSGTGSRYSGYGSSDLSRSRSSHALKSRDNSPITDRGAGSSRSSGLGGSSTTDSKDGEALSSWARYLKNKYGNKSSKDSAGSSGSARDTHAGSSTSSSAAASSSHAHGYGSGTSGSSGRSTASDVSRRLSLGLPLRQANELASSDDDGSKNGLGSPTSPTVAAAVAAAGITGAAGTIPKQVYLRKRQQLFQLGGRGSEPGSFTWPRGLAVGPDNSIVVADSSNHRVQVFDSNGIFVKEFGEYGNGEGEFDCLAGVAVNRIGQYIIADRYNHRIQVLDPQGRFLRAFGSQGTADGKFNYPWGVTTDALGFIYVCDKENHRVQVFQSDGSFVGKFGSCGRGEGQLEHPHYIAVSNTNRVIVSDSNNHRIQIFDVNGKVLSTVGGEGSDDGQFKFPRGVAVDDQGYIFVADSGNNRIQIFNPDGSFLKTFGSWGSGDSEFKGLEGVAIMSNGNILVCDRENHRVQVF
Protein: Purine-cytosine permease FCY2 (PCP FCY2) (Cytosine/purine transport protein FCY2) (Fluorocytosine resistance protein 2) (P17064)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This permease has a broad specificity towards purines, and also transport cytosine and 5-methylcytosine but neither uracil nor thymine.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Cytosine deaminase
- Inosine-5'-monophosphate dehydrogenase 2
- Mannan polymerase complexes subunit MNN9
- Uracil phosphoribosyltransferase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Bifunctional purine biosynthetic protein ADE5,7
- Epsin-2
- Hypoxanthine-guanine phosphoribosyltransferase
- Epsin-1
- Uridine permease
Sequence:
MLEEGNNVYEIQDLEKRSPVIGSSLENEKKVAASETFTATSEDDQQYIVESSEATKLSWFHKFFASLNAETKGVEPVTEDEKTDDSILNAASMWFSANMVIASYALGALGPMVFGLNFGQSVLVIIFFNIMGLIFVAFFSVFGAELGLRQMILSRYLVGNVTARIFSLINVIACVGWGIVNTSVSAQLLNMVNEGSGHVCPIWAGCLIIIGGTVLVTFFGYSVIHAYEKWSWVPNFAVFLVIIAQLSRSGKFKGGEWVGGATTAGSVLSFGSSIFGFAAGWTTYAADYTVYMPKSTNKYKIFFSLVAGLAFPLFFTMILGAASAMAALNDPTWKAYYDKNAMGGVIYAILVPNSLNGFGQFCCVLLALSTIANNIPNMYTVALSAQALWAPLAKIPRVVWTMAGNAATLGISIPATYYFDGFMENFMDSIGYYLAIYIAISCSEHFFYRRSFSAYNIDDWDNWEHLPIGIAGTAALIVGAFGVALGMCQTYWVGEIGRLIGKYGGDIGFELGASWAFIIYNILRPLELKYFGR
Protein: Optineurin (Q5RI56)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase TBK1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- GABA
- GABA
- Uncharacterized protein LOC100000242
- small monomeric GTPase
- Calcium-binding and coiled-coil domain 2
- Inhibitor of nuclear factor kappa B kinase subunit beta.
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Serine/threonine-protein kinase PLK
Sequence:
MNGDISHPRGSGPGNLGSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQVKELEKSGAECLHTELEALRGQILRIQAEKNDLVAMNSELQLKMGQGSPSNSFIEIRIADDDLKVTKDLSSVPEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAETNASTEVKNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQKKTQDEKNNLNQLKDAYTKLFEDYSELQEEKKKRESCVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETISVFQAQAEIYSSDFYAERAAREKIHEEKERLATQLEYVKKQNSQLQEEMESLGRHSMSEMQRRHVPRGANPQGPTAPNNLPGGRGEWQQQNIPDHACPKCGEVLPDLDSLQIHIMDCII
Protein: Transmembrane protein 215 (A7E1Z1)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRPDDINPRTGLVVALVSVFLVFGFMFTVSGMKGETLGNIPLLAIGPAICLPGIAAIALARKTEGCTKWPENELLWVRKLPCFRKPKDKEVVELLRTPSDLESGKGSSDELAKKAGLRGKQLPQGPGEVPMASSVTTPTPTEEGECQSLVQSGRQEETSRYLDGYCPSASSLAYSALDAKCSAWDRSDRPEPEDSIFFVPQDSIIVCSYKQNSPYDRYCCYINQSQGRWDHETIV
Protein: FUN14 domain-containing protein 2 (Cervical cancer proto-oncogene 3 protein) (HCC-3) (Hepatitis C virus core-binding protein 6) (Q9BWH2)
Organism: Homo sapiens (Human)
Function: Binds directly and specifically 1,2-Diacyl-sn-glycero-3-phospho-(1'-myo-inositol-3',4',5'-bisphosphate) (PIP3) leading to the recruitment of PIP3 to mitochondria and may play a role in the regulation of the platelet activation via AKT/GSK3B/cGMP signaling pathways. May act as transcription factor that regulates SREBP1 (isoform SREBP-1C) expression in order to modulate triglyceride (TG) homeostasis in hepatocytes.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:29786068}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000305|PubMed:29187281}.
Interaction partners:
Sequence:
METSAPRAGSQVVATTARHSAAYRADPLRVSSRDKLTEMAASSQGNFEGNFESLDLAEFAKKQPWWRKLFGQESGPSAEKYSVATQLFIGGVTGWCTGFIFQKVGKLAATAVGGGFFLLQLANHTGYIKVDWQRVEKDMKKAKEQLKIRKSNQIPTEVRSKAEEVVSFVKKNVLVTGGFFGGFLLGMAS