wanglab/gogpt-training-data huggingface dataset:
Protein: Heterochromatin protein 5, isoform B (Q9VYY7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI01426p
- Heterochromatin protein 6
Sequence:
MDIFDMVKAAPPPQTINPVDTKLSTPSPIPPDSPIDVNDLLESGNQLDENDLRMSRKSKNVEQCSIDLFDSETSFDHLDESLAKRKRKSVANSKPNKSRKSTVSASTPHNKRPKVSIDDDGEAIEEDQQSMVVVPTKTKAQQKMFSDQQSPNVKRKVRVLLRRLKQTEIDSAVESLANSSFINVPEIVNQSGTSGRSRHKKRKTSPKKQKSSTAQTNFHIKVPLQNGAKKRALNHSLRAHTPPPSLAKSSESTHSALKRSPKPKIKAKRLSSRGRNTDPDLVKRYGAHFFGCVVKVRRTRLPSAKWPDCKPPPIGDGVVRKVYPKKAVSFSEAVEILGSPGGPSRRSTFGSLSSRGAPKPTRLQRVDATGNVLEDIALTSTPLFSSSSGGSRERVRRRSCNGTPVVGRLKLRRLGRLSIDNSSSRSDGGGDNDDDDEEYIVPNDVPGSQRSGTPPPKKKKISFTTTISDDEDEKPVLKKQKDAQKKQPKPLKERSNKKTDKMLNEKETTDKMQTKKEKKTENSPVVEIESSDPDVEIKPPVKEIETNEREGDAHETETNEVERDREEQFVDATEKNTDEAKEKKVVKDMPELKEADNSEEKSEDAREEVLLDEDEKNLEENAAEISDNAVKSLEKPTNEDRVEKVEDEVEHAEEFSDLPTPPQLPSTTDDNEDDVLEIQTSLDDVRQLHTPSSRQSTPKSRSRLDSGDSDCSFKSASDNAKLLAGQAIEETEQKASKAPNDDEDQQTAATIIGDPIDSPELPAELMTPPSAPRTVNGEPTSESRSTATTYYSPMEDPMATLDDVIMDQLSEPNFQLNSSRHAISRGTLDEIMTALES
Protein: Antitoxin YafN (Q47156)
Organism: Escherichia coli (strain K12)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Functions as an mRNA interferase antitoxin; overexpression prevents YafO-mediated cessation of cell growth and inhibition of cell proliferation.
Interaction partners:
- mRNA interferase toxin YafO
- Uncharacterized N-acetyltransferase YafP
- Toxin YoeB
- DNA polymerase IV
- mRNA interferase toxin RelE
- Antitoxin DinJ
- mRNA interferase toxin YafQ
- Antitoxin ChpS
- Antitoxin MqsA
- Antitoxin YefM
Sequence:
MHRILAEKSVNITELRKNPAKYFIDQPVAVLSNNRPAGYLLSASAFEALMDMLAEQEEKKPIKARFRPSAARLEEITRRAEQYLNDMTDDDFNDFKE
Protein: 18S rRNA aminocarboxypropyltransferase (EC 2.5.1.157) (Q381R8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGKSKGPRCDAEGSRCSVPLAMWDFEQCDPNACSGRRLHRRNALRLLKLREPFRGVVLTPTAVETLSPADAGLIAQLGVAVVDCSWNQLDAVPWRQMKMGAPRLLPFLVAANPVNYGRPQELNCAEALAAALAIADRMDDARAVMSYFSWGASFFDINAELLEGYRGCRNAAEVLEFQEQHVEAEKRRSTAQREMDFDNVDLSDVGPLNVKRGKLKNRHAWEVNTEENSSSSDDCGEETDEELGKVDEETSEEEEQVVSECNGV
Protein: Zinc finger protein 337 (Q9Y3M9)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MGPQGARRQAFLAFGDVTVDFTQKEWRLLSPAQRALYREVTLENYSHLVSLGILHSKPELIRRLEQGEVPWGEERRRRPGPCAGIYAEHVLRPKNLGLAHQRQQQLQFSDQSFQSDTAEGQEKEKSTKPMAFSSPPLRHAVSSRRRNSVVEIESSQGQRENPTEIDKVLKGIENSRWGAFKCAERGQDFSRKMMVIIHKKAHSRQKLFTCRECHQGFRDESALLLHQNTHTGEKSYVCSVCGRGFSLKANLLRHQRTHSGEKPFLCKVCGRGYTSKSYLTVHERTHTGEKPYECQECGRRFNDKSSYNKHLKAHSGEKPFVCKECGRGYTNKSYFVVHKRIHSGEKPYRCQECGRGFSNKSHLITHQRTHSGEKPFACRQCKQSFSVKGSLLRHQRTHSGEKPFVCKDCERSFSQKSTLVYHQRTHSGEKPFVCRECGQGFIQKSTLVKHQITHSEEKPFVCKDCGRGFIQKSTFTLHQRTHSEEKPYGCRECGRRFRDKSSYNKHLRAHLGEKRFFCRDCGRGFTLKPNLTIHQRTHSGEKPFMCKQCEKSFSLKANLLRHQWTHSGERPFNCKDCGRGFILKSTLLFHQKTHSGEKPFICSECGQGFIWKSNLVKHQLAHSGKQPFVCKECGRGFNWKGNLLTHQRTHSGEKPFVCNVCGQGFSWKRSLTRHHWRIHSKEKPFVCQECKRGYTSKSDLTVHERIHTGERPYECQECGRKFSNKSYYSKHLKRHLREKRFCTGSVGEASS
Protein: Protein phosphatase 1B (EC 3.1.3.16) (Protein phosphatase 2C isoform beta) (PP2C-beta) (P36993)
Organism: Mus musculus (Mouse)
Function: Enzyme with a broad specificity. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:23088624}. Membrane {ECO:0000269|PubMed:23088624}; Lipid-anchor {ECO:0000269|PubMed:23088624}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000269|PubMed:23088624}.
Interaction partners:
- Ubiquitin-like protein ISG15
- Mitogen-activated protein kinase kinase kinase 7
- Amino acid transporter heavy chain SLC3A1
- E3 ubiquitin-protein ligase ARIH1
- Protein phosphatase 1A
- YEATS domain-containing protein 4
- Prolyl endopeptidase-like
Sequence:
MGAFLDKPKTEKHNAHGAGNGLRYGLSSMQGWRVEMEDAHTAVVGIPHGLDNWSFFAVYDGHAGSRVANYCSTHLLEHITTNEDFRAADKSGSALEPSVESVKTGIRTGFLKIDEYMRNFSDLRNGMDRSGSTAVGVMVSPTHMYFINCGDSRAVLCRNGQVCFSTQDHKPCNPVEKERIQNAGGSVMIQRVNGSLAVSRALGDYDYKCVDGKGPTEQLVSPEPEVYEIVRAEEDEFVVLACDGIWDVMSNEELCEFVKSRLEVSDDLENVCNWVVDTCLHKGSRDNMSVVLVCFSNAPKVSEEAVKRDSELDKHLESRVEEIMQKSGEEGMPDLAHVMRILSAENIPNLPPGGGLAGKRHVIEAVYSRLNPHKDNDGGAGDLEDSLVAL
Protein: Probable purine permease 5 (AtPUP5) (Q9ZUH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- At5g58750
- Rhodanese-like domain-containing protein 11, chloroplastic
- Rhodanese-like/PpiC domain-containing protein 12, chloroplastic
Sequence:
MDETTERPTVSFSYSNWISNIKKSTREAYEAKPFSHWILLFFSGAAMLIAFPASSLLSRLYFSNGGKSKWIISWVAVAGWPITCLILLPTYIFQKIKPTPLNTKLVLSYVVLGFLSAADNLMYAYAYAYLPASTSSLLASSSLAFSALFGYLIVKNPLNASVINSIVVITGAMAIIALDSSSDRYSYISNSQYFAGFFWDIMGSALHGLIFALSELLFVKLLGRRSFHVALEQQVMVSLTAFAFTTIGMVVSNDFQGMSHEAKSFKGGESLYTQVLVWSAVTFQLGVLGATAVLFLASTVMAGVLNAVRVPITSVAAVILMHDPMSGFKILSLVLTFWGFSSYIYGSSSSNSSTQASSSSS
Protein: Uncharacterized protein YdfD (P29010)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Division inhibition protein DicB
- Uncharacterized protein YdfA
- Uncharacterized protein YdfB
- Uncharacterized protein YdfC
Sequence:
MNSAFVLVLTVFLVSGEPVDIAVSVHRTMQECMTAATEQKIPGNCYPVDKVIHQDNIEIPAGL
Protein: Negative regulator of ofd1 (Q9USJ7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for correct translation termination (By similarity). Positive regulator of the stability of the N-terminal transcription factor domain (Sre1N) of sre1 which is released from the membrane and enters the nucleus to activate hypoxic gene expression. Acts also as a direct inhibitor of ofd1. Functions probably by inhibiting the ability of the ofd1 to accelerate Sre1N degradation in absence of oxygen.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Prolyl 3,4-dihydroxylase ofd1
- Sterol regulatory element-binding protein 1
- Sterol regulatory element-binding protein cleavage-activating protein
- Probable oxygen-dependent coproporphyrinogen-III oxidase
- Small ribosomal subunit protein uS12B
- Putative transcription factor sre2
Sequence:
MIGRRPQGLRAAASLKKQQQLEKQKQEASYELSGNSSPSKENGSENVDNGEMEDETMLVYTEEDNISQLWGLYEMSREKLENDDIDASVSLVFGTIHEADRILRNTEDISTLPKDFHAAYSSALLAVSELFEIAQKRLKETNTEESYIDAAIERAQLGLDAPGNESRLFLALARAYLEKVRVLVWRHDNEESLANIPVTQLVNPYIEKAIQYLRPLAQDSTEYFDALTPDSLRPLYILSSYLFQFGDQFSEAFLLDVCSIITALWLKSVVDPNTPAYYKLIAQEAVLNNYTTFAEYYMDLLDNSESNVDDLINKASSWLNNSVDTWNVIYTLDKSPERLLKLADIKMDLAQIVQDEASQDNYLKEACNAIKEAQGSGVELSPDYVEFVEAYSA
Protein: Endothelial PAS domain protein 1a (Endothelial PAS domain-containing protein 1 isoform X3) (F8W2W5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTAEREKKRHPSERRKEKSRDAARCRRSKETEVFYELAHQLPLPHSISSHLDKASIMRLAISFLRTRKLFSSGHTVQQMRSQNLGQMDNLYLKSLEGFVIVVTSDGDMIFLSENVSKFMGLTQVELTGHSIFDFTHPCDHEEIRENLSIKSGPVYGRKGKEMSTSRDFFMRMKCTVTNRGRTVNLKSASWKVLHCTGHLQVCSSRPPQILCGFSEPPLTCITMLCAPIPHPSNVDTPLDSKTFMSRHSMDMKFIYCDERVSSLIGYRPEELLGRSVYEFCHALDSENMTKSHQNLCNKGQVVSGQYRMLAKNGGYVWVETQATVIYNNRNSQPQCIICINYILSSVEEQSVIFSLDQTEALFKPYHTYDMGEIFSQNTSISEPQNNLFTTLKEEPEELAQLAPMPGDAIIALDFERAEFEEATFFSKSSKLPAVGPSWVVDTPPDGSPERNLSSLPSSFTVPQVPPAGKCTPCTTPCLSSCSSCSTPNSPVDCCGSGEWDLKVELTEKLFAPESGATNPTDSQLNLSDLDLETLAPYIPMDGEDFQLHPICLEEPVPDAGPGLSAAVQHSFSSVADLFQPLEKQRQSLHWPPDQLSQYENTNVGCMDDRNTGGPGQTCNFNVPPPHQRFFENFTPVQKGMSLGQRALLNNFKRKRQSEFPLSCSFSDIPKQVVAPHKSTDGMRKRMKPMNDDSCAFSVRKSLSTSVLTDKFPCMQSGLVDPQACSRSVKGCPEDLKQHCTDSFCSNSSRQYNMMPSRKHTGMISQLLAPSFDSYCLPELTRYDCEVNMPLQGNLHLLQGSDLLRALDQST
Protein: Sorting nexin-2 (Transformation-related gene 9 protein) (TRG-9) (O60749)
Organism: Homo sapiens (Human)
Function: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity. Required for retrograde endosome-to-TGN transport of TGN38. Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:16179610, ECO:0000269|PubMed:17101778}; Peripheral membrane protein {ECO:0000269|PubMed:16179610, ECO:0000269|PubMed:17101778}; Cytoplasmic side {ECO:0000269|PubMed:16179610, ECO:0000269|PubMed:17101778}. Cell projection, lamellipodium {ECO:0000269|PubMed:20604901}. Note=Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles (PubMed:18088323). Colocalized with F-actin at the leading edge of lamellipodia in cells in a KALRN-dependent manner (PubMed:20604901). {ECO:0000269|PubMed:18088323, ECO:0000269|PubMed:20604901}.
Interaction partners:
- Sorting nexin-6
- Vacuolar protein sorting-associated protein 26A
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-1
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-5
- Sorting nexin-32
- Vacuolar protein sorting-associated protein 26B
- Sorting nexin-27
- TBC1 domain family member 5
Sequence:
MAAEREPPPLGDGKPTDFEDLEDGEDLFTSTVSTLESSPSSPEPASLPAEDISANSNGPKPTEVVLDDDREDLFAEATEEVSLDSPEREPILSSEPSPAVTPVTPTTLIAPRIESKSMSAPVIFDRSREEIEEEANGDIFDIEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKVGKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESSELPRAVNTQALSGAGILRMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHVSVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSRALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANKPDKIQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAKAIA
Protein: Protein spinster homolog 1 (MSpin1) (Spns1) (Q8R0G7)
Organism: Mus musculus (Mouse)
Function: Plays a critical role in the phospholipid salvage pathway from lysosomes to the cytosol. Mediates the rate-limiting, proton-dependent, lysosomal efflux of lysophospholipids, which can then be reacylated by acyltransferases in the endoplasmic reticulum to form phospholipids. Selective for zwitterionic headgroups such as lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), can also transport lysophosphatidylglycerol (LPG), but not other anionic lysophospholipids, sphingosine, nor sphingomyelin. Transports lysophospholipids with saturated, monounsaturated, and polyunsaturated fatty acids, such as 1-hexadecanoyl-sn-glycero-3-phosphocholine, 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine and 1-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine, respectively. Can also transport lysoplasmalogen (LPC with a fatty alcohol) such as 1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine. Essential player in lysosomal homeostasis. May be involved in necrotic or autophagic cell death (By similarity).
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:36161949}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Major facilitator superfamily domain-containing protein 9
- Putative transporter SVOPL
- Major facilitator superfamily domain-containing protein 10
Sequence:
MAGSDTAPFLSQADDPDDGPAPGHPGLPGPMGNPKSGELEVPDCEGLQRITGLSRGHSTLIVVVLCYINLLNYMDRFTVAGVLTDIEQFFNIGDGSTGLIQTVFISSYMVLAPVFGYLGDRYNRKYLMCGGIAFWSLVTLGSSFIPREHFWLLLLTRGLVGVGEASYSTIAPTLIADLFVADQRSRMLSIFYFAIPVGSGLGYIAGSKVKDVAGDWHWALRVTPGLGVLAVLLLFLVVQEPPRGAVERHSGSPPLSPTSWWADLKALARNPSFVLSSLGFTSVAFVTGSLALWAPAFLLRSRVVLGETPPCLPGDSCSSSDSLIFGLITCLTGVLGVGLGVEISRRLRRFNPRADPLVCAAGLLGSAPFLFLALACARGSIVATYIFIFIGETLLSMNWAIVADILLYVVIPTRRSTAEAFQIVLSHLLGDAGSPYLIGLISDRLRRSWPPSFLSEFRALQFSLMLCAFVGALGGAAFLGTAMFIEDDRRRAQLHVQGLLHESGPSDDRIVVPQRGRSTRVPVSSVLI
Protein: Pentatricopeptide repeat-containing protein 6, mitochondrial (Q9USP3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial RNA-binding protein required for the stability of the atp9 mRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:21727087}.
Interaction partners:
- Mitochondrial cox1 translation regulator ppr4
- Uncharacterized protein C106.19
- Mitochondrial 15S rRNA processing factor ppr3
- Pentatricopeptide repeat-containing protein 5
- Pentatricopeptide repeat-containing protein 7
- Protein mss51
- DNA-directed RNA polymerase, mitochondrial
- Uncharacterized protein PB1E7.11c
- Pentatricopeptide repeat-containing protein 2
- Pentatricopeptide repeat-containing protein 8
Sequence:
MRILGSLPNNIRKCTFKLILQKRYSHTDILKELLYDISDSQKFIPSASPIASNLLRVSSYGKLSSLFIEYSKARSKKEFDQLRTSDFQSILRSVVCPKNGKNIRHRDRDLVSLQIKLILQDADRLGIQFNIVDYTHILRVAMYTGNKHILEYIVARVKEKRIRPSVDYFNAILGVIGGNRWSLSKFQSPAFRGSPVTEPVSGKMLDMIEVDFPNYDLVPNSTTYDYLMVGLSRDGKIREIYDLIDTVWGINENSSSKKVDCGNVTFPTHHTVFSIISALGYLGDVSSAVSLSRKLTSVYKINFPELAWRYIIYWSIASLQFRAPAGHARIKNIELFIRLYSQMYRHCVPIIEIYDTSIKFYMKHGRFGLLEKVCESWTKQFLGSLEKQNNEVKKKHLQLLEKQISKLMRYAETERPHDTKRVSVKWSNVLNQIHSSVGDPAKP
Protein: Lipase 3 (DmLip3) (EC 3.1.1.-) (O46108)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Alpha-amylase-related protein
Sequence:
MTRGALKVTILLVGLGLVLAGSRPISDCGERIEDDGYPMERHEVVTSDNYILTMHRIPYSPKTGESSNRPVAFLMHGMLSSSSDWVLMGPERSLAYMLADAGYDVWMGNARGNTYSKAHKYWPTYWQIFWNFSWNEIGMYDVPAMIDYVLAKTGQQQVQYVGHSQGTTVYLVMVSERPEYNDKIKSAHLLGPAAYMGNMKSPLTRAFAPILGQPNAIVEVCGSMEFMPSNKFKQDLGIEMCQATSPYADMCANEIFLIGGYDTEQLDYELLEHIKATSPAGASVNQNLHFCQEYNSGKFRKFDYTALRNPYEYGSYFPPDYKLKNAKAPVLLYYGANDWMCDVSDVRKLRDELPNMALDYLVPFEKWAHLDFIWGTEARKYVYDEVLKQMQSYE
Protein: Glutamate decarboxylase 4 (GAD 4) (EC 4.1.1.15) (Q9ZPS3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the production of GABA. The calmodulin-binding is calcium-dependent and it is proposed that this may, directly or indirectly, form a calcium regulated control of GABA biosynthesis (By similarity).
Interaction partners:
- Gamma-aminobutyrate transaminase POP2, mitochondrial
- Delta-1-pyrroline-5-carboxylate dehydrogenase 12A1, mitochondrial
- Probable glutamate dehydrogenase 3
- Glutamate dehydrogenase 1
- glutamate dehydrogenase
- Glutamate dehydrogenase 2
- Pantoate--beta-alanine ligase
- Glutamate synthase 1, chloroplastic
- Asparagine synthetase 1
- Ferredoxin-dependent glutamate synthase 2, chloroplastic
Sequence:
MVLSKTVSESDVSIHSTFASRYVRNSLPRFEMPENSIPKEAAYQIINDELMLDGNPRLNLASFVTTWMEPECDKLMMESINKNYVDMDEYPVTTELQNRCVNMIARLFNAPLGDGEAAVGVGTVGSSEAIMLAGLAFKRQWQNKRKAQGLPYDKPNIVTGANVQVCWEKFARYFEVELKEVNLREDYYVMDPVKAVEMVDENTICVAAILGSTLTGEFEDVKLLNDLLVEKNKQTGWDTPIHVDAASGGFIAPFLYPELEWDFRLPLVKSINVSGHKYGLVYAGIGWVVWRTKTDLPDELIFHINYLGADQPTFTLNFSKGSSQVIAQYYQLIRLGFEGYRNVMDNCRENMMVLRQGLEKTGRFKIVSKENGVPLVAFSLKDSSRHNEFEVAHTLRRFGWIVPAYTMPADAQHVTVLRVVIREDFSRTLAERLVADFEKVLHELDTLPARVHAKMANGKVNGVKKTPEETQREVTAYWKKLLETKKTNKNTIC
Protein: Uncharacterized protein (Q388D7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEGLSPPETDECAKPHNRECNTTPSSGSPPSNIPPQQLLCSVRSGMHSNLTESAWESRESNSGYAHEKQSGVDGDACTRYYQRLHRFYEQYNPKNLSRISEYLAAYKGKEEQLMAILVGKYGPEPVDRGPQTNLSCCSGDDSVMHFSGKRYRIPTVVTPQQGNTDCETPYWGNSPLIGERDILGLLSSLETANVELQKCYIGPSAQHPTSSWNGMTYVTRAEIFTPNEETFLGHKWTFTLGSKKVLVHEGSAYHRATFFCTDECQYRGRHERWRLCVYTSSVDSLYLVRVIWDPVVYLEPLPLDRSALSQHSSSEAMPIAGSSVSYQTSCGKGNTEPEQPLISATMINIMTMLENMDKKISGRFDALEARFSFLESKLLGAVDDKQRTEDR
Protein: Flavin-containing monooxygenase 5 (FMO 5) (Dimethylaniline monooxygenase [N-oxide-forming] 5) (EC 1.14.13.8) (Dimethylaniline oxidase 5) (Hepatic flavin-containing monooxygenase 5) (NADPH oxidase) (EC 1.6.3.1) (P97872)
Organism: Mus musculus (Mouse)
Function: Acts as Baeyer-Villiger monooxygenase on a broad range of substrates. Catalyzes the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Active on diverse carbonyl compounds, whereas soft nucleophiles are mostly non- or poorly reactive. In contrast with other forms of FMO it is non- or poorly active on 'classical' substrates such as drugs, pesticides, and dietary components containing soft nucleophilic heteroatoms. Able to oxidize drug molecules bearing a carbonyl group on an aliphatic chain, such as nabumetone and pentoxifylline. Also, in the absence of substrates, shows slow but yet significant NADPH oxidase activity (By similarity). Acts as a positive modulator of cholesterol biosynthesis as well as glucose homeostasis, promoting metabolic aging via pleiotropic effects.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:P49326}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49326}.
Interaction partners:
Sequence:
MAKKRIAVIGAGASGLTCIKCCLEEGLEPVCFERSGDIGGLWRFQEAPEEGRASIYQSVVINTSKEMMCFSDYPIPDHYPNYMHNSQVLEYFRMYAKEFDLLKYIQFKTTVCSVKKQPDFSTSGQWQVVTECEGKQQVDVFDGVLVCTGHHTDAHLPLESFPGIEKFKGKYFHSRDYKNPVEFTGKRVIVIGIGNSGGDLAVEISHTAKQVFLSTRRGAWILNRVGKHGYPIDLLLSSRIMYYLSRICGPSLKNNYMEKQMNQRFDHEMFGLKPKHRALSQHPTVNDDLPNRIIAGLVKVKGNVKEFTETAAVFEDGSREDGIDVVIFATGYSFAFPFLEDSVKVVKNKVSLYKKVFPPNLEKPTLAIIGLIQPLGAIMPISELQGRWATQVFKGLKKLPSQSEMMAEINKAREEMAKRYVDSQRHTIQGDYIDTMEEIADLVGVRPNILPLVFTDPRLALRLLLGPCTPVQYRLQGPGKWAGARKTILTTEDRVRKPLMTRVVERDSSGGSLVTVRVLMLAVAFFAVILAYF
Protein: DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18) (H7BXZ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKGLLGNAFDGHQLLRPLIFCQDHLREGPPIGRGDSQGEELEPQLPSSLSSIPYGFCDHCWTKDVDDPPLVTHPSPGSRDGHMTQAWPVKVVSPLATVIGHVMQASLLAL
Protein: Uncharacterized protein At4g00950 (Q9M160)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT4g00920 protein
- NC domain-containing protein-like protein
- Wall-associated receptor kinase-like protein
- ATPase, F1 complex, OSCP/delta subunit protein
- F-box protein At4g00893
- Dof zinc finger protein DOF4.1
- COP1-interacting protein 4.1
- Receptor-like cytosolic serine/threonine-protein kinase RBK2
- Pentatricopeptide repeat-containing protein At4g20090
- Aluminum-activated malate transporter 10
Sequence:
MEAEKETEQEGNLTVMKLPVLPTKPNTHSHSMSSPIHSSISASVPFSWEEEPGKPKQHSTSSSSSSSSSPLTSYSSSPFETHKSLELPPRLHLLEKDGGSVTKLHSPITVFDGPYSMTTSKRMDSPSFRMMVKGSADCYGSFRSDIDGDLEDLEVGSKQQENLSSGSLAVVKKRGRLGFFGFRRRRALKGKTEFGRGSYVFPSSVDRESEYSRKEEEEEKEDKRFGYDDTDGISCSQSSRFCDVKISSISRTGSFSTLPAPPSSSSKSHFWTNVYAGLKQVVPWKSKKTTV
Protein: NEDD8-activating enzyme E1 catalytic subunit (EC 6.2.1.64) (Ubiquitin-activating enzyme E1 3) (Q09765)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of the dimeric uba3-ula1 E1 enzyme. E1 activates NEDD8/ubl1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-uba3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of ubc12 (By similarity).
Interaction partners:
- NEDD8-conjugating enzyme ubc12
- NEDD8-activating enzyme E1 regulatory subunit
- Ubiquitin-like protein 1
- Ubiquitin-activating enzyme E1 1
- NEDD8-specific protease 1
- RING-box protein pip1
- Defective in cullin neddylation protein 1
- NEDD8-specific protease 2
- Tyrosine--tRNA ligase, mitochondrial
- COP9 signalosome complex subunit 5
Sequence:
MPSSDVCKAGSHRHSGWIQSLKKPGPFNLDAPENPEETLKSAFSSKILIIGAGGLGCEILKDLALSGFRDLSVIDMDTIDITNLNRQFLFNESNIDEPKANVAASMIMKRIPSTVVTPFYGKIQDKTIEFYKEFKLIICGLDSVEARRWINSTLVAIAKTGDLIPLVDGGSEGLKGQARVIIPTITSCYECSLDMLTPKISYPICTLANTPRLPEHCVEWAYLLEWPRVFLNASVDSFSKQEVFEPLDGKNSNFEPDNIRHIDWLVKRSIERANKFQIPSSSINRFFVQGIVKRIIPAVASTNAIIAASCCNEALKILTESNPFLDNYMMYVGEDGAYTYTFNLEKRSDCPVCGVLSEVYDISASSTVTLKDILNHYSKSYNLQNPSVSTAAGTPLYLASPPALQVATSKNLSQPILSITSVDVNLVITDKNLSTSLSVQLREC
Protein: Serine/threonine-protein kinase ULK1 (EC 2.7.11.1) (Autophagy-related protein 1 homolog) (ATG1) (hATG1) (Unc-51-like kinase 1) (O75385)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity. May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences. Plays a role early in neuronal differentiation and is required for granule cell axon formation. May also phosphorylate SESN2 and SQSTM1 to regulate autophagy. Phosphorylates FLCN, promoting autophagy. Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation. Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Preautophagosomal structure {ECO:0000250}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. {ECO:0000250}.
Interaction partners:
- Beclin-1
- RB1-inducible coiled-coil protein 1
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Beclin 1-associated autophagy-related key regulator
- Serine/threonine-protein kinase mTOR
- Nuclear receptor-binding factor 2
- Autophagy-related protein 101
- Autophagy-related protein 13
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Serine/threonine-protein kinase ULK2
Sequence:
MEPGRGGTETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHAMRTLSEDTIRLFLQQIAGAMRLLHSKGIIHRDLKPQNILLSNPAGRRANPNSIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPTIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASPSVRKSPPVPVPSYPSSGSGSSSSSSSTSHLASPPSLGEMQQLQKTLASPADTAGFLHSSRDSGGSKDSSCDTDDFVMVPAQFPGDLVAEAPSAKPPPDSLMCSGSSLVASAGLESHGRTPSPSPPCSSSPSPSGRAGPFSSSRCGASVPIPVPTQVQNYQRIERNLQSPTQFQTPRSSAIRRSGSTSPLGFARASPSPPAHAEHGGVLARKMSLGGGRPYTPSPQVGTIPERPGWSGTPSPQGAEMRGGRSPRPGSSAPEHSPRTSGLGCRLHSAPNLSDLHVVRPKLPKPPTDPLGAVFSPPQASPPQPSHGLQSCRNLRGSPKLPDFLQRNPLPPILGSPTKAVPSFDFPKTPSSQNLLALLARQGVVMTPPRNRTLPDLSEVGPFHGQPLGPGLRPGEDPKGPFGRSFSTSRLTDLLLKAAFGTQAPDPGSTESLQEKPMEIAPSAGFGGSLHPGARAGGTSSPSPVVFTVGSPPSGSTPPQGPRTRMFSAGPTGSASSSARHLVPGPCSEAPAPELPAPGHGCSFADPITANLEGAVTFEAPDLPEETLMEQEHTEILRGLRFTLLFVQHVLEIAALKGSASEAAGGPEYQLQESVVADQISLLSREWGFAEQLVLYLKVAELLSSGLQSAIDQIRAGKLCLSSTVKQVVRRLNELYKASVVSCQGLSLRLQRFFLDKQRLLDRIHSITAERLIFSHAVQMVQSAALDEMFQHREGCVPRYHKALLLLEGLQHMLSDQADIENVTKCKLCIERRLSALLTGICA