wanglab/gogpt-training-data huggingface dataset:
Protein: DNA-directed RNA polymerase II subunit RPB11-b2 (RNA polymerase II subunit B11-b2) (RPB11b2) (DNA-directed RNA polymerase II subunit J3) (Q9H1A7)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MNAPPAFESFLLFEGEKITINKDTKVPNACLFTINKEDHTLGNIIKSQLLKDPQVLFAGYKVPHPLEHKIIIRVQTTPDYSPQEAFTNAITDLISELSLLEERFRTCLLPLRLLP
Protein: Multiplexin, isoform R (M9ND55)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- SH3 domain-binding glutamic acid-rich protein homolog
Sequence:
MRVLQGVMFALAMICTLLVPVLGSFELVGQSIKDALAEYTLTDIMNNNQFAGIEFGEAEDGFPAFRFLQTADVKSPYRMLLPEKLYEFAILITFRQSSLKGGYLFSVVNPLDTVVQLGVHLSPVVKNSYNVSLVYTQADQNIGRKLASFGVAHVPDKWNSIALQVLSDKVSFYYDCELRNTTLVTREPIELVFDSASTLYIGQAGSIIGGKFEGYLEKINVYGNPDAINVTCMPPPKATIAPTTADDGSIFYEGSGENILFEDSTEANILSDDFWNTGDEATDIFDASGMQPPGQTQYTHERPYRGIKGEKGERGPKGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAKYTGECTCNASDILEAIKDNESLRESLRGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLPGVMGPPGPPGPPGLPENYDESLMVNSMGAFRGTTQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPGGLDGLASANGTKGEKGEKGEKGMRGRRGGTGATGPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSGGREGLKGDKGDRGQDGRDGLPGPPGLPSTGGGDGDSGGVQYIPMPGPPGPPGPPGLPGLSISGPKGEPGVDSRSSFFGDASYYGRPGARSSLDELKALRELQDLRDRPDGTAEPPRQPGHSHKHEETLGLVDGEEPYFSASSSNMNMKIVPGAVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVPIATPAPPTTVAPSMRFDLQSKNLLNSPPPLLNTPTWYPRMLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRDLPVVNTRGDVLFNSWKGIFNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKLIILCVEALSQDRKRKKREIGDGSSHGESESREFKTADEYAAHLENLLL
Protein: Lactate-binding periplasmic protein TTHA0766 (ABC transporter, solute-binding protein) (Extracytoplasmic solute receptor protein TTHA0766) (TRAP transporter lactate-binding subunit P) (Q5SK82)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system involved in the uptake of lactate. This protein specifically binds L-lactate.
Subcellular location: Periplasm {ECO:0000250|UniProtKB:P37676}.
Interaction partners:
Sequence:
MKRVSRRAFLRRLGVGVAATAAFSPLAVAQARRYRWRIQTAWDAGTVGYSLFQKFTERVKELTDGQLEVQPFPAGAVVGTFDMFDAVKTGVLDGMNPFTLYWAGRMPVTAFLSSYALGLDRPDQWETWFYSLGGLDIARRAFAEQGLFYVGPVQHDLNIIHSKKPIRRFEDFKGVKLRVPGGMIAEVFAAAGASTVLLPGGEVYPALERGVIDAADFVGPAVNYNLGFHQVAKYIIMGPPETPAIHQPVDLMDFTINLNRWRSLPKPLQERFIAAVHEYSWIHYAGIQKANLEAWPKYRQAGVEVIRLSNEDVRKFRRLAIPIWFKWAKMDKYSREAFASQLEYMKGIGYVTDEELKGLSL
Protein: Cap-associated protein CAF20 (20 kDa cap-associated protein) (CCR4-associated factor 2) (p20) (P12962)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as an inhibitor of cap-dependent translation. Competes with eIF4G1/TIF4631 and EAP1 for binding to eIF4E/TIF45 and interferes with the formation of the eIF4F complex, inhibiting translation and stabilizing mRNA. Binding affinity for eIF4E/TIF45 is 10-fold less than that of eIF4G1/TIF4631. Required for induction of pseudohyphal growth in response to nitrogen limitation, probably by regulating STE12 translation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- RNA-binding protein SRO9
- Eukaryotic initiation factor 4F subunit p150
- Protein EAP1
- Eukaryotic initiation factor 4F subunit p130
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Suppressor protein MPT5
- ATP-dependent RNA helicase DHH1
- ATP-dependent RNA helicase DED1
- Large ribosomal subunit protein uL6A
Sequence:
MIKYTIDELFQLKPSLTLEVNFDAVEFRAIIEKVKQLQHLKEEEFNSHHVGHFGRRRSSHHHGRPKIKHNKPKVTTDSDGWCTFEAKKKGSGEDDEEETETTPTSTVPVATIAQETLKVKPNNKNISSNRPADTRDIVADKPILGFNAFAALESEDEDDEA
Protein: Succinate dehydrogenase subunit 7B, mitochondrial (Q3E870)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Succinate dehydrogenase subunit 8
- Succinate dehydrogenase subunit 5
- Succinate dehydrogenase subunit 4
- Succinate dehydrogenase subunit 7A
- Succinate dehydrogenase subunit 6
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase subunit 3-1
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
Sequence:
MAFLLNNASISSHLRSSSSQKTGDALSISRRGFHIEPGTREKALLAEDSALKRFKSHKKSVHKLKRIGDVLTVVVVAGCCYEIYVKAVMKKEALAAGKSS
Protein: FI01459p (Q9VF39)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Golgin 104
- GH16843p
Sequence:
MAKNPKKEEDGGNDWAQSDEDDNWDDWGDDDDKFVHVEKEQQPQEKVSSRNDAKGTAENQEKLETPRISAPATASATSSSWGLWGGKLSSVLTTATEGLGTITTQVNQGLNQIIGVPDPEELARINVAEKAEKAAKAPPEENVDDEKESSAAFGLDFVTNLGSKVLNTGLDTLEGIGKKTMTILQDNDPKLMNKRKLLGLEANSPNLSAVLLEAKKEADQMEQSLQQLQLKRQKAQLRFEILFENYCGLVHFEALEILSKESRLKLDTLLDAVSGNARAELQETINEVKELIELEDLDVESEGDYEAEELSERLAATIKDAELGIQFDDIANHWTQSLSWLTSEEATAADLEQAYAKSIHALSEACALEMCKLHKIAELLLVKPHHSTANEVDGVVNLCQQFNGHLQGLSHRFAAVLSGKSETEESKGRVSTFFSEMLSAVQFIEKAYKLFTPILQMGAV
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (Q583D6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLLHGPLAERFNRGASDCHKQMQPSVTLPLMHVRFVSSAKLPQCPVTLDPVVAGPKPIDGPDQQQQQPQRTFVPFKDRLRSTNFSRGEKSDRSATLCGSSVTSQQLSKDAGSLSVSFSTACWRLASSASVRSGDGSPMNNDDGGGGCRTQGQPLRLPTYTGTQQGTSQTTARKQTSKLSFKDRQRSSVSNNHSVSAGEEGSGRDAEPPCNESNTYTPANALTSNDGGQQKHYQRKFKARVQTGALAPPLPPGAPPLLLPGTASPSANYVNYCCHSEQWKDGEAEGTELDNTNNSSERRRDKMLPRASSTRRGSAPRASAETLPPVVDASIPMTDEGGGRLNPSCGGGGGGKHYGDRVGAGGNEGEARDVFSFLPISPRIAAEFPAAEEGSALAATRGNRRRSGFSSLFFSMLKPLKVEYQLPFLVQPSIPLDDETVDEPFGLGSSDCSLTDEGLESLTHSLTSGVGVVETEEHVFIPHYELLKEGRSRAEVILSTVRAVCSGLNLSVLSAPPDTIASCRKCDEGGADETKAADPSPCGRSGRADRRHTREGGVGLSQSSSTNEDTKSVSNVGTIIASEEDDCFTFGVVSTSYPLFPTEDQDKSDCKVAARLLFNAEKGVMLISAEDEVKKYMNKPLKAGTPNGRAEGGKGARCSFERSNIGVSRDSAVQERPQQAQQKGIEKRQEEEEGEETEGLLWRYGGNQESGTLDATLVLPSHGTEKDSTRDRNAFYEEDGSVSRCTCTQQLITKDARGVDYSRYHAHKLYHHCKCCDRRPASFLCLHCLTALCPSHVTRHYNDSIPAVGKSKRGASSVCETMDDEETGRNAVGACSLFINILDIMTSFDRVYWCEPCQSFTWRYTEVYDPLVDQLAATRGTYLEDPVRDIACVGYEVQIKCYGEAQPSFCGRTSAHSSVLRDRPLVNRNALQTDIALFYPPNAGQDVTPTEGGSAAISGTIECGLGSPRLVGSASPLPRCSAMEDTLHVGVTAPKLISLGAKVQGWRATQEDAEAAFVISIPCLSDTPDTGADDDKAEETIAARESNDAVAMAVFCVFDGHGGDAVAKLAASRFESHLRKAVCSVRHDEAEASAVLRRVDQESTTPQYSVSEASPLRPRESGCFPQLSSNDVNSGAALGDVGVRSVSNVTVEMVRQLTEGSADKSVARGSAADHSETSDTCHGLSASPTVSRREMEALRLYFAGIMEEALLSLDDELRSSDEGRRGDYNCTGCTACVVGITTNFILCANIGDSGAAFYTPQDIVPISITHRTTDPGERARINAAGYTLVEHRIEGLLAVSRALGDYDFKQCGGRGPREQAVTAVPDVTIMPVPPAAAVGRWGVVVACDGVWDTLTPHQVHHAIMNTPNDLEVASSATEVVIRAREMAYASQKEGDKSHINTEKYRCGADGERENGGSKTVDNVWGGKCCHGGASGASIDALLLTSAAGIFAQCVAPVDNEEGVGMDNCSLFLIEQR
Protein: Nucleoporin NUP35 (35 kDa nucleoporin) (Nuclear pore complex protein Nup53) (Nucleoporin NUP53) (Nucleoporin npp-19) (Q09601)
Organism: Caenorhabditis elegans
Function: Functions as a component of the nuclear pore complex (NPC) (By similarity). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Thereby required for nuclear import. Required for the proper organization of chromosomes on the mitotic spindle during anaphase.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:35852146}.
Interaction partners:
- Nucleoporin_N domain-containing protein
- Nsp1_C domain-containing protein
- Nuclear pore protein
- Nuclear Pore complex Protein
- Nuclear pore complex protein 5
- Nucleoporin ndc-1
- Nucleoporin Nup54 alpha-helical domain-containing protein
- Nuclear pore complex protein 15
- WD_REPEATS_REGION domain-containing protein
- Nuclear pore complex protein Nup85
Sequence:
MFSHLNQNTSGRHNSMDLNNSSISNFGTPVEQSTPALLFGKRKATVPSSYTASPLNTASAPCSDIFAVSAPAVPQHLKDTPGSKSVHWSPSLVQSGEKSAAQTQNTPANLSFGGNSSFSAPTKPAPQSIQTSSFGGQAMHAPPLRSLRDKVEPAKKISRRNTFTARSTPLSTPITQRVTSRLAEAEEQPMEEEADAADTWVTVFGFQPSQVSILLNLFSRHGEVVSHQTPSKGNFIHMRYSCVTHAQQAISRNGTLLDQDTFIGVVQCTNKDVINGSASGIVARSSNIAAAANRSASMYNSFVENDMADQSVNHNENSVLNSSNVFDANNSLNSSRISVRSGVGMRPLAADQRTNILQGTPSVRKAPDGLLNKFWNTIGLN
Protein: Gastrulation defective protein 1 (O16519)
Organism: Caenorhabditis elegans
Function: Required for initiation of gastrulation.
Interaction partners:
- Pre-mRNA-splicing factor CWC22 homolog
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase mog-1
- Pre-mRNA-processing factor 17
- Protein BUD31 homolog
- peptidylprolyl isomerase
- Pre-mRNA-splicing factor CWC25 homolog
- Splicing factor YJU2
- Peptidyl-prolyl cis-trans isomerase
- Pre-mRNA-splicing factor syf-2
- Pre-mRNA-splicing factor 8 homolog
Sequence:
MDDNTAPKKNSEKKARVFDLQAMFAQTISNAPRTEEPTHVPQSVSVSSKSESGVSSSAVSDDEDDFMPDLPPGFQMQQSEAGPSSSRAEGPEDSDDSDFDETEAISIIKLIPAACEAKISHGTQAISALRVEPPGVRFASGGLDYYVKLFDFQKMDMSMRYDKELLPAESHVINSLAFSPNGETLVVASGEAIIRLLDRAGKQWSETVRGDQYIIDLNITKGHTATVNCVEFNPLNKNEFISCSDDGSLRLWNLDDHKVITKCINKHRKVIKTKGANGKRVSPQVCTFSPDGKWIAAGCDDGSVQAWKYGSQYVNVNYLVRKAHNGSITSIAFSPDSKRLLSRGFDDTLKMWSLDNPKEPLLVKTGLENAFKSTDCGFSPRAEVVFTGTSSPNKDTPGTLQFFDPMTFDLVYKIDYPGISCHRIQWHPRLNQIIAGLSDGTIHVYYDQTMSQRGVMSCVTKPLKRNRASEVVREDMVLSPLSLEMFQPRGEEGEEKEVTGWRIKKYLRMQDNKLRPEFRKPADMPINGKSANGRVAASGGSLHSYLAKQIGTARNAEFLKDTDVRASILKHAKDAEENPLYIDKAYRKTQPKKIFQETAVEPEDQDDEELQPVFKMPRTK
Protein: PITH domain-containing protein 1 (Q9GZP4)
Organism: Homo sapiens (Human)
Function: Promotes megakaryocyte differentiation by up-regulating RUNX1 expression. Regulates RUNX1 expression by activating the proximal promoter of the RUNX1 gene and by enhancing the translation activity of an internal ribosome entry site (IRES) element in the RUNX1 gene.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25134913}.
Interaction partners:
Sequence:
MSHGHSHGGGGCRCAAEREEPPEQRGLAYGLYLRIDLERLQCLNESREGSGRGVFKPWEERTDRSKFVESDADEELLFNIPFTGNVKLKGIIIMGEDDDSHPSEMRLYKNIPQMSFDDTEREPDQTFSLNRDLTGELEYATKISRFSNVYHLSIHISKNFGADTTKVFYIGLRGEWTELRRHEVTICNYEASANPADHRVHQVTPQTHFIS
Protein: Cytochrome c lysine N-methyltransferase 1 (EC 2.1.1.59) (P38818)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Methyltransferase which mediates trimethylation of 'Lys-78' of cytochrome c (CYC1).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10791961}.
Interaction partners:
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Holocytochrome-c synthase
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Cytochrome c isoform 2
- Threonine dehydratase, mitochondrial
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- Cytochrome c isoform 1
- Ribosomal lysine N-methyltransferase 1
- Protein-lysine N-methyltransferase EFM1
- Ribosomal lysine N-methyltransferase 4
Sequence:
MEEVFRFYSNSRNIFIHKSLSLKPSTIDDPKSGYGLFVEPSKFKNDELKSETIQLLRIPKRCTFNINTLLALLGDEDEFSSKEEFQRTNDKIKIALREIMAHPNFSVFLTETNLLIIYFMIFQTIRSRYEIPENIQYYLENVLMSIEVETAMDSIENLATDYGHYPQIFGLRETLNLFKELFHDVLNLSDIKHLYSAIISRCLEIPERADTKSEEFTVHSTLVPIVDFANHEGTQKNAYFDIDPSNNDVLLLLDTKAVQSELTKPIEVFISYSPTEDLFSMLVTYGFTPDFRGNSQFWTVSFDRCFLRNYDGPDKTTNLRLFYKWMHINPVVPLVKYEHNGKTRWFLNDTTPEFDMLLLPFIPSIDDGKIARWAYDSTCHLMFTKIHCLINPEANEHALMIAENYRSLIKEKESNGDDFINLPPLAWSLRYKDTENDCVRQRHICSEDAVAVLKQEEMQDSTKTKSQFTSFFRKFLEFRRSKIIRPTSDSKVASILYQQELEIIADLAKAIDSSSTIFFSDLNVTLDTEPERLPPLRFLDDYIEISADKQEPSPICEDLSYYTPSRFTDFFQEEVSQYAAFFQDD
Protein: Histone-binding protein RBBP4 (Chromatin assembly factor 1 subunit C) (CAF-1 subunit C) (Retinoblastoma-binding protein 4) (RBBP-4) (Q6P3H7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q09028}. Chromosome, telomere {ECO:0000250|UniProtKB:Q09028}.
Interaction partners:
- Polycomb protein suz12-A
- Polycomb protein suz12-B
- Histone-lysine N-methyltransferase EZH2
- Protein lin-9 homolog
- Lin-37 DREAM MuvB core complex component.
- Polycomb protein eed
- Zinc finger protein AEBP2
- Histone deacetylase 1
- Protein lin-54 homolog
- Protein lin-52 homolog
Sequence:
MADKEAAFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTRPEGKDFSVHRLVLGTHTSDEQNHLVIASVQLPNDDAQFDASHYDSEKGEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIATKTPTSDVLVFDYTKHPSKPDPSGECTPDLRLRGHQKEGYGLSWNPNLRSCLLSASDDHTICLWDISTVPKEGKIVDAKTIFTGHTAVVEDVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHAVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIGEEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVWQMAENIYNDEDPEGAADTEVQG
Protein: Type-5 uracil-DNA glycosylase (EC 3.2.2.-) (TTUDGB) (Uracil/hypoxanthine/xanthine DNA glycosylase) (Q5SJ65)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: DNA glycosylase with broad substrate specificity. Can remove uracil from double-stranded DNA containing either a U/G, U/A, U/C or U/T base pair. Can also excise hypoxanthine from double-stranded DNA containing G/I, T/I, and A/I base pairs, xanthine from both double-stranded and single stranded DNA, thymine from G/T mismatched DNA, 5'-hydroxymethyluracil and 5'-fluorouracil.
Interaction partners:
Sequence:
MDREAFVQTLTACRLCPRLVAWREEVVGRKRAFRGEPYWARPVPGFGDPEARILLFGLAPGAHGSNRTGRPFTGDASGAFLYPLLHEAGLSSKPESLPGDDLRLYGVYLTAAVRCAPPKNKPTPEELRACARWTEVELGLLPEVRVYVALGRIALEALLAHFGLRKSAHPFRHGAHYPLPGGRHLLASYHVSRQNTQTGRLTREMFLEVLMEAKRLAGL
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) (Q9WVM8)
Organism: Mus musculus (Mouse)
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) (By similarity).
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Kynurenine 3-monooxygenase
- Kynureninase
- Kynurenine--oxoglutarate transaminase 3
- Kynurenine--oxoglutarate transaminase 1
- 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
- 3-hydroxyanthranilate 3,4-dioxygenase
Sequence:
MNYSRFLTATSLARKPSPIRTTADILSKAPKTLISLAPGSPNPSMFPFKSAAFTVENGSTIRFEDDLIKRALQYSPSYGIPELLSWLKQFQVKLHNPPTVNYPPNQGQMDLCITSGCQDGLCKAFEMLINPGDTILVNEPLFPGTLYAMKPLGCNIINVPSDEHGIIPEGLKKILSQWKPEDSKDPTKKTPKFLYTVPNGNNPTGNSLTGDRKKEIYELARKYDFLIIEDDPYYFLQFSKPWEPTFLSMDVDGRVIRADTFSKTVSSGLRVGFMTGPKTLIQNIVLHTQVSSVHACTLSQLMILQLLHQWGEEGFLAHIDRTIDFYKNQRDSILAAADKWLRGLAEWHVPKAGMFLWIKVKGISDTKQLIEEKAIEREVLLVPGNGFFIDGSAPTSFFRASFSLATPAQMDTAFQRLAQLIKESL
Protein: Mitoguardin 2 (Protein FAM73B) (Q8BK03)
Organism: Mus musculus (Mouse)
Function: Regulator of mitochondrial fusion. Acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of PLD6/MitoPLD dimers. May act by regulating phospholipid metabolism via PLD6/MitoPLD (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q7L4E1}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitoguardin 1
Sequence:
MAFRRTEGMSMIQALAMTVAEIPVFLYTTFGQSAFSQLRLTPGLRKVLFATALGTVALALAAHQLKRRRRKKKQVGPEMGGEQLGTVPMPILMARKVPSVKKGCSSRRVQSPSSKSNDTLSGISSIEPSKHSGSSHSLASMVVVNSSSPTAACSGSWEARGMEESVPTTDGSAESLYVQGMELFEEALQKWEQALSVGQRGDGGSTPTPGDSLQNPDTASEALSEPESQRREFAEKLESLLHRAYHLQEEFGSTFPSDSMLLDLERTLMLPLTEGSLRLRADDEDSLTSEDSFFSATEIFESLQIGEYPLPLSRPAAAYEEALQLVKEGRVPCRTLRTELLGCYSDQDFLAKLHCVRQAFEGLLEERSNQIFFGEVGRQMVTGLMTKAEKSPKGFLESYEEMLSYALRPETWATTRLELEGRGVACMSFFDIVLDFILMDAFEDLENPPSSVLAVLRNRWLSDSFKETALATACWSVLKAKRRLLMVPDGFISHFYSVSEHVSPVLAFGFLGPKPQLSEVCAFFKHQIVQYLRDMFDLDNVRYTSVPALAEDILQLSRRRSEILLGYLGAPVASSIGLNGPLPRENGPLEELQ
Protein: Nuclear transcription factor Y subunit nfya-2 (CAAT box DNA-binding protein subunit nfya-2) (Q5ZEP9)
Organism: Caenorhabditis elegans
Function: Component of the sequence-specific heterotrimeric transcription factor (nfya-2-NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression and control cellular identity in particular tissue types. In association with the components in the nfya-2-NF-Y complex, may repress the expression of the T-box transcription factor tbx-2 throughout larval development, which most likely restricts its expression to certain tissues.
Subcellular location: Nucleus {ECO:0000269|PubMed:17574230}.
Interaction partners:
- Nuclear transcription factor Y subunit nfyc-1
- Nuclear transcription factor Y subunit nfyb-1
- RNA polymerase I associated factor, A49-like protein
Sequence:
MNPRGNPSKMPTQIVLNRRPAAPARPQTTFTSLSQYHMYNTASTSSAPPPPPNQNFGQIREAIRTTQPTTVQLPPDCKLVEYTWQENGESRTVLIPMSNDSTEDDVRSALPQSVLESINQHQNQLRQGNAQAVHYYQKHQNPISHEKPIMVNPRQYKRIIKRREMRQKMEDSGRLPLERQKYMHESRRQHALKRRRTGGRFDANAEAAAASSEPSISSAAPSPPKAPRAPTTYAMIRPATSHPPVNIPKAPAMTYRPVQEEKKSIERISKAQMFTIPKRQQ
Protein: Interleukin 18 binding protein (Q9IW12)
Organism: Ectromelia virus
Interaction partners:
Sequence:
MRILFLIAFMYGCVHSYVNAVETKCPNLDIVTSSGEFHCSGCVEHMPEFSYMYWLAKDMKSDEDTKFIEHLGDGINEDETVRTTDGGITTLRKVLHVTDTNKFAHYRFTCVLTTLDGVSKKNIWLK
Protein: E3 ubiquitin-protein ligase rififylin (EC 2.3.2.27) (RING finger and FYVE-like domain-containing protein 1) (Fring) (RING-type E3 ubiquitin transferase rififylin) (Q6ZQM0)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Also ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate apoptosis downstream of death domain receptors. Also negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. May also play a role in endocytic recycling.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15229288}. Cell membrane {ECO:0000269|PubMed:15229288}; Peripheral membrane protein {ECO:0000269|PubMed:15229288}. Recycling endosome membrane {ECO:0000305|PubMed:15229288}; Peripheral membrane protein {ECO:0000305|PubMed:15229288}. Note=The FYVE-type zinc finger may mediate phosphatidylinositol phosphate-binding and control subcellular localization.
Interaction partners:
Sequence:
MSQPSLWKDSHYFIMWASCCNWFCLDGQPEEAPPPQGARTQAYSNPGYSSFPSPTGSEPSCKACGVHFASTTRKQTCLDCKKNFCMTCSSQEGNGPRLCLLCLRFRATAFQREELMKMKVKDLRDYLSLHDISTEMCREKEELVFLVLGQQPVISEADRTRVPHLPQAFPEQQAFLTQPQTSTVPPTSPGLPSSPAQVTSVPLAQDQETQQAVGHVSQDHEEPIFPESTARVPTEDETQSVDSEDSFVPGRRASLSDLTHLEDIEGLTVRQLKEILARNFVNYKGCCEKWELMERVTRLYKDQKGLQHLVSGNEDQNGGAVPSGLEENLCKICMDSPIDCVLLECGHMVTCTKCGKRMNECPICRQYVIRAVHVFRS
Protein: Mitochondrial oligo U binding protein TBRGG1 (Q584T3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Piwi-like protein 1
- RNA editing associated helicase 2
- REH2-associated factor 1
Sequence:
MVCSTICLFQRGQWGNEGSRGDQRNYDNRGGRGEWGDRGGQRGDNQRDYGDQRNYDNRGGRGEWGDRGGQRGDNQRDYGDQRNYDNRGGRGEWGDRGGQRGDNQRDYGDQRNYDNRGGRGEWGDRGGQRGDNQRDYGDQRNYDNRGGRGEWGDRGGQRGDNQRDYGDQRNYDNRGGRGEWGDRGGQRGDNQRNYDNRGGRGEWGDRGGQRGGNQRDNSNQFGYRNERDGGIGRQRSARDNFGAHDNRASDERGSTDPAVGEVFDEQAAKILYELKRRFKSSKTGKERRDVQREARRIVRRARVDPSTQDEKSVTLLLNCAATFRCYPHTEGIKQATEWMRKNIDGLSPQNVALFTNAIGALSVVDSDTILINEISPAVEACYGQMNPVELVMTLQAFQRGRITENEDLQVSLLQQLVTCVPQMPAPQLSTLAGVLVDTPLRKRDEATWQEIAKTVVSKAASGAENMHSREVITLLKATPRLGVPEDHSFHLVDRAIATVGFHTDEQIGELLEAVSYYRDPQKTCGRELNEKLDKLVDALWARLQKVAPFADAASVTTIMRAAHRSGVDVPRDIVSTLVQAVMRELRYHRFTFRRVASLSEALALQKVPAKELLVMLGDYCIGKRPPREERGENTPVDDHNSGIEERMDIYARFLGDLTKARIALENAHSSNAGNGEPGSSVSQILAQRLEDSVGSAPPRELLKSVRAICTAADDCPFRNRANDGKIIALSEQRIAKEGASFMEGVRKTTMENFLSAVSGIPQAQKVVEVLSHQTR
Protein: Protein NRT1/ PTR FAMILY 4.3 (AtNPF4.3) (Nitrate transporter 1.14) (Q93VV5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GDSL esterase/lipase At5g45910
- CASP-like protein 1E1
- Peptidyl-prolyl cis-trans isomerase FKBP43
Sequence:
MAEINKQSNKWEQEEVSNENNWELAEEESVDWRGRPSNPNKHGGMRAALFVLGLQAFEIMGIAAVGNNLITYVINEMHFPLSKAANIVTNFVGTIFIFALLGGYLSDAFLGSFWTIIIFGFVELSGFILLSVQAHLPQLKPPKCNPLIDQTCEEAKGFKAMIFFMALYLVALGSGCVKPNMIAHGADQFSQSHPKQSKRLSSYFNAAYFAFSMGELIALTLLVWVQTHSGMDIGFGVSAAAMTMGIISLVSGTMYFRNKRPRRSIFTPIAHVIVAAILKRKLASPSDPRMLHGDHHVANDVVPSSTLPHTPRFRFLDKACIKIQDTNTKESPWRLCTVTQVEQVKTLISLVPIFASTIVFNTILAQLQTFSVQQGSSMNTRLSNSFHIPPASLQAIPYIMLIFLVPLYDSFLVPFARKLTGHNSGIPPLTRIGIGLFLSTFSMVSAAMLEKKRRDSSVLDGRILSIFWITPQFLIFGISEMFTAVGLIEFFYKQSAKGMESFLMALTYCSYSFGFYFSSVLVSVVNKITSTSVDSKGWLGENDLNKDRLDLFYWLLAVLSLLNFLSYLFWSRWNIKSSRRNNTNVVGDENI
Protein: N-acetymuramyl-L-alanine amidase-related protein (Q7D4L9)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MPSPRREDGDALRCGDRSAAVTEIRAALTALGMLDHQEEDLTTGRNVALELFDAQLDQAVRAFQQHRGLLVDGIVGEATYRALKEASYRLGARTLYHQFGAPLYGDDVATLQARLQDLGFYTGLVDGHFGLQTHNALMSYQREYGLAADGICGPETLRSLYFLSSRVSGGSPHAIREEELVRSSGPKLSGKRIIIDPGRGGVDHGLIAQGPAGPISEADLLWDLASRLEGRMAAIGMETHLSRPTNRSPSDAERAATANAVGADLMISLRCETQTSLAANGVASFHFGNSHGSVSTIGRNLADFIQREVVARTGLRDCRVHGRTWDLLRLTRMPTVQVDIGYITNPHDRGMLVSTQTRDAIAEGILAAVKRLYLLGKNDRPTGTFTFAELLAHELSVERAGRLGGS