wanglab/gogpt-training-data huggingface dataset:
Protein: Accessory gland protein Acp63F (O46200)
Organism: Drosophila melanogaster (Fruit fly)
Function: Responsible for physiological and behavioral changes in mated female flies.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Accessory gland protein Acp53Ea
- Accessory gland protein Acp36DE
- Accessory gland-specific peptide 26Aa
- ACP53C14A
- Accessory gland protein Acp76A
- Accessory gland protein 98AB
- Accessory gland protein Acp62F
- Accessory gland-specific peptide 70A
- Accessory gland-specific peptide 95EF
- Accessory gland-specific peptide 26Ab
Sequence:
MKAIIVFILFISSVHAMSKCNQAIYLNLDPHCGILPDCNLDGPNPSYLKRVSCERKENGKPGFIELIPGKCLHGKPRCSLK
Protein: Flagellum-specific ATP synthase (EC 7.1.2.2) (P52612)
Organism: Escherichia coli (strain K12)
Function: Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum. May be involved in a specialized protein export pathway that proceeds without signal peptide cleavage.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Flagellar biosynthetic protein FlhB
- Flagellar biosynthetic protein FliR
- Flagellar motor switch protein FliM
- Flagellar FliJ protein
- Flagellar motor switch protein FliG
- Flagellar motor switch protein FliN
- Flagellar biosynthetic protein FliP
- Flagellar M-ring protein
- Flagellar protein FliO
- Flagellar biosynthesis protein FlhA
Sequence:
MTTRLTRWLTTLDNFEAKMAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERQNGSETHEVESEVVGFNGQRLFLMPLEEVEGVLPGARVYAKNISAEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPSPDTTETGALITPPFNPLQRTPIEHVLDTGVRPINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALISEQHYARVRTFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWPQLEGYLQQGIFERADWEASLQGLERIFPTVS
Protein: DUF2428 domain-containing protein (Q38DI9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Putative tRNA
Sequence:
MSNEYTTAARLQQHHLSSGSANMDMCVYSKLLEGSSTILQAINALTPLAPKAANIVEREIVNFMRAATPEHRVRCISQITGALREPAFYNQRHKRGCATFLHKLAVHFVFPLLLHSSVRYLHRALATLVRTVYVVSEDLELCFQEAFVTAHIKPWFRDGCRPSLLQHLDSTELSLLKDPIMNWVNCIDGTMCVAVPLFPAVFANTFFDVVPLLGDSLQWMVDNACAGCSQSECGKGNSGMLLGEDLSYVRYGIRVVTTYVHKFLHLLGDVLHEGEEQKMAEVQEDICKLFSSSLRMLSSAVFPKDVLNGAGLLVSSLLTIRTCDASFLLEICRYCGASEVRKESNFTSVADDDGCSKRWTEEYVREFVQLVCSSDPQHEILQRSFSRDSLRRIFYSFTANGRFALMKGLLAHLSTPLRGNIGSVGVLLKPVVPLLDNLSSYAASGRPLVAVYDVIIPAAISYCSALHVPDTRFMAIQTIDSVVRHLSSVFTCIADLLETTLEESVVEGTTRVVKRGVQRAGGVGLLTETDRKALSALCANTSGLMRALSEATEVIMGMWDDSTQHVAGPLYGAYSEILAVHSSVRRCNTLLSQGSGAPNQEVDALDVAETLHVILPIPNERRGKYHALLALLDVVQVPQFLLELRQHRAKCSKEGAADYCSAVTPDDVSEVDALCEFSRMLLGGAINPKVGSAAGEVFAKTANYIRLSSGTETETEKLFFGGVIEPLLKSIVVPGYCAPLHVEDATRISNIVTHMISPCLKRDESYLPTLLSRLATMVESGDCYFRLGQSIVEILHRARVAGRDVSTYIHPRSRLFKVVLSSLQSHSSELRYTALGLCVLTMKKAEPVHYWQCRLMEWYISTNMHSGGDSAAMRNLLEVYKKWAQRLVDSCASKCSNRRRKAEGNETSDQYRDLVTKHFVRTVSYIAPHIGESVEWCRNLSLERRVTAMMIYSCLLRNSTEVFTDTQLHELQEQLLPETLVEGLLECLSSGWVKARECAFGILQTYCKYAASAVFSERRLGNPVAASDAKAGLSHARTYKKAEGEVLRYVLATYFTPAARKAASEDPQRECKRRLELVKLEIAALHGKFVGLCQLGTKKAYQLVKLHPFHGSLSLCAALLSNVKEVCTTADGLQESCNQMLLCCNQALQNCSLLVGGEASGSANEGDVDVDCRGHAFDKGNPCEEASMRAVVNNTWLCIRTAAAAVERVVALVSIDSLDFKVVRGVCYVLVESLLRTKHNGVMRAVRGALKTIAAALLRSRDVTCHTLPSEILEFLLGPDGVTSVSVARMLRRSQGLPHALLAVLEAEDIGVPATLFPQAMKRLLHVATNAHSNEGGPDLCPPNGNDERRTPEADGEIRRSQRSNALNVLKFIFENKSFASRSVSHLEDAFWIAASGFDDPSWGIRNSSLMLFSAVLPRFVGEHPSTGGVGVNTSLHDIAIRAPRAVAFAYEELVKSFTNPSPSLGVFPLLQMLSMLAPDPPHVITKATTVNLEGEEQEQPDSQRIVNAVVRCGSSRNLMIRAACSVALTSLVPPTNLEGLFAEFCSALSASRTAANALHGVLLHLQQFHTFYVGTLRRHVKPRALSSSVTPTVQLLVSRLTVEGLTISQGNSAQEPVLSRACVRCPTIAATFFSVASDALYHATVGMKGIEKKDITDSVRSLVNIGVSTLHSILCTATPLYSLSRAYHAAVVENITLFALLAVHYLSDITTHHGTHDALWVALRDVFACDASKIIMSHTMNHISYLMSKNWWSSEISVGVVKQFAVRMKCDLVHAALTMLRESLGDDRHVKGLSCLELLRMQSQLEFVVTMSKEGLMCLEAHSELFDAVEDLLLRRMDPSAKHFLRNADVHSWAIRFLGLRCTCHMPHNKAVLEIITHYCLPTVNVQTRLAVVDSLNDSFLAGVVTSPAAAATTSTFTKQRSVYLLVLLQLLFDDAYDVRTAACRVVSRLVLAAALPLDHTSCVIALVSLLRSYCSTGELSPVMVKQHLLKNTECCLSGSANKDTCGDDDDEGSDEEGVLFEKEADNMFAEGSLLAFLATVITREGADCVPVFSVYTELVNVSERCGNPAVMYGALLDEPSPCGA
Protein: Ectonucleoside triphosphate diphosphohydrolase 2 (A0A1D5PS27)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MARRAAAVLLLLALGCLLGILLLCLGSGDARGPPSFKYGIVLDAGSSHTAVFIYKWPADKENDTGVVSEHSMCDVEGPGISSYSSKPPAAGKSLEHCLSQAMRDVPKEKHADTPLYLGATAGMRLLRIADPPSSDAVLSAVMATLKSYPFDFRGAKILSGEEEGVFGWITANYLLENFIKRGWLGEWIQSKKKTLGAMDFGGASTQITFETSDAIEDPKNEVMLKLYGQPYKVYTHSFLCYGRDQVLKRLLSKVLQAENYQETVANPCWPTGYRKSLSLSSIYDSPCTEKERPGLPLNTTVVVSGTGNGNLCAVHVNKLFDFTSCSFSHCSFDGVFQPEVSGNFIAFSAFFYTVDFIRTVMERPVHSPSDLKDAAETICATSWNELYQKAPRLEKRLPDYCATSTFVYLLITKGYNFNNRSFPSIAFQKKAGETSIGWALGYMLNLTNMIPAQEPASHRSMLYNYWVILILLFVITTLTALLTAVYLLRRSKSSTI
Protein: COP9 signalosome complex subunit 5 (EC 3.4.-.-) (Q12468)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex is involved in the regulation of the mating pheromone response.
Subcellular location: Cytoplasm. Nucleus. Note=Nuclear localization requires the formation of the CSN complex.
Interaction partners:
- Cop9 signalosome-interactor 1
- COP9 signalosome complex subunit 10
- Cop9 signalosome complex subunit 11
- 26S proteasome regulatory subunit RPN5
- COP9 signalosome complex subunit 9
- RING-box protein HRT1
- Cell division control protein 53
- Cullin-3
- 26S proteasome regulatory subunit RPN7
- Suppressor of kinetochore protein 1
Sequence:
MSLSNKTVKELRQLLKERYTVEDELTESIALSSMRFKPSQEPEFHALSQSSLLKTKLKQQSSTDIPSYTHVLISKLSCEKITHYAVRGGNIEIMGILMGFTLKDNIVVMDCFNLPVVGTETRVNAQLESYEYMVQYIDEMYNHNDGGDGRDYKGAKLNVVGWFHSHPGYDCWLSNIDIQTQDLNQRFQDPYVAIVVDPLKSLEDKILRMGAFRTIESKSDDNSATSYYELETIIFDSELNRALFETKLNLHCVIEDDESEQISLNRLIDSMKQYSYLMDSKNVRTRIKLATTSERVSNENKKNIDYQNRSTRSQFCLNTQRGDSTETSSFGSMFSGDNTSDVDMEDRNLTEFDSTDTSLCINGEPSIHVNRVERSSRSTDNFHNSKKRMNSNQERCHDEGNDMLQRNVLETDYARAKNRILASKIKQYERLRFYKDTFTL
Protein: Probable ubiquitin-conjugating enzyme E2 18 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 18) (Ubiquitin carrier protein 18) (Q9FMM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Interaction partners:
- E3 ubiquitin-protein ligase UPL4
- E3 ubiquitin-protein ligase UPL3
- Probable ubiquitin-conjugating enzyme E2 33
- Ubiquitin-ribosomal protein eS31x fusion protein
- S-adenosylmethionine decarboxylase proenzyme 1
- Ubiquitin-conjugating enzyme E2 34
- Probable ubiquitin-conjugating enzyme E2 26
- Ubiquitin-ribosomal protein eS31y fusion protein
- Ubiquitin-ribosomal protein eL40z fusion protein
- Ubiquitin-ribosomal protein eL40y fusion protein
Sequence:
MTSSSSPSRKALSKIACNRLQKELSEWQVNPPTGFKHRVTDNLQKWVIEVTGAPGTLYANETYNLQVEFPQHYPMEAPQVIFVPPAPLHPHIYSNGHICLDILYDSWSPAMTVSSVCISILSMLSSSPEKQRPTDNDRYVKNCKNGRSPKETRWWFHDDKV
Protein: Tubulin alpha chain (F5H5D3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTAWFNGVEELGRDECFVCLELDPSNGSFLNAKLYISNWILIYFTRTLQLPAPFNTCTSSKSRGEPGCDSKRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAVAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGADSADGEDEGEEY
Protein: Amino acid transporter, putative (Q57Y05)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLFLFHPFVPETLWVKEVPKSANRLQDAMSNSKQQQEVQTPNNLSNEPVQTEDNVKKGRNTFFTKVSLCVATVLPPGGIAASAFNMASTTIGAGIFGMPPVANSTGLIMGMFYLIFISSVTVFTMHNLSVAADRSGAPTFERATRALLGRGAAYVLAGIRALLGFSGCVAYVISVGDILSAILKGTNAPDFLKEKSGNRLLMAVVWACFMLPLTIPRHIDSLRYVSTFAVTFMVYFVIVIVVHSCMNGLSENIKNVSVTKSEDAEIILFNSGFQAIEGMGVFMFAFISQITAYEVYIDMKDRSVRKFVIAAIIANTLCCIMYIITAFFGYMDFGKTATSSILLMYDPVKEPAVMVGMIGVVIKLCVSYALVAMACRNALYDVVGKTADSLPFWKHCVSVITLSFLVLLLSIFIPKITTVFGIAGSVCGGSLGFVFPALLIMYSGGFTWQKVGPLYYITTYVVLLCGVFLIVFGTGSTILDTVRG
Protein: F-box only protein 7 (Q3U7U3)
Organism: Mus musculus (Mouse)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Predominantly cytoplasmic. A minor proportion is detected in the nucleus. Relocates from the cytosol to depolarized mitochondria (By similarity). {ECO:0000250}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- Proteasome inhibitor PI31 subunit
- Serine/threonine-protein kinase PINK1, mitochondrial
- E3 ubiquitin-protein ligase parkin
- Polyamine-transporting ATPase 13A2
- E3 ubiquitin-protein ligase RBX1
- 85/88 kDa calcium-independent phospholipase A2
- Auxilin
- Vacuolar protein sorting-associated protein 35
Sequence:
MKLRVRLQKRTQPLEVPESEPTLGQLRAHLSQVLLPTLGFSSDTRFAITLNNKDALTGDEETLASYGIVSGDLICLVLEDDMPAPNLPSSTDTEHSSLQDNDQPSLAATPSQTNIPDEQGTDSSQGQATPFDAWTDDSMEGPSQNVEAESIQDAMSMEEVSGFHPLEPMLCNETEDGQVPHSLETLYQSAGCSNISDALIVLVHLLMLESGYIPQGTETKAVTMPEKWKSSGVYKLQYTHPLCEGGFAVLTCVPLGNLIIINATIKVNGGIKNVKSVQLQPGSYVAAGVEPGESAAKVYKDLKKLSRLFKDQLVYPLLAFTRQVLNLPDVFGLVVLPLELKLRIFRLLDVHSVLALSAVCHDLLIASNDPLLWRCLYLRDFRDGTVRGPDTDWKELYRKKHIQRKEAQRMRHAMFLPSAHPIPFCPIPVYPRAYLPTSLLPPGIIGGEYDERPILPSVGDPVTSLIPRPGELPGQFRPLRPRFDPVDPLPGPHSLLPGRAIPNNRFPFRPGRGRSADSRLPFL
Protein: Myocyte enhancer factor 2ca (Q6PCS3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- NK2 homeobox 5.
- T-box transcription factor TBX5-A
- GATA-binding protein 4.
- Mitogen-activated protein kinase 14B
- mitogen-activated protein kinase
- Mitogen-activated protein kinase.
- mitogen-activated protein kinase
- mitogen-activated protein kinase
- Mitogen-activated protein kinase 14A
- Mitogen-activated protein kinase 12
Sequence:
MGRKKIQIARIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDIDAEDSGHSPESEDKYRKINEDIDLMISRQRLCAIPQSNYDMPVSIPVSNPNSLIYGHPGASLGNPNLLPLTHPSLQRNSMSPGVTHRPPSAGNTGGLMAADLGSGAGTSTGNGYGNHRNSPGLLVSPGNMSKNLQAKSPPSMNMSLSRKPDLRVLIPPGAKNTMPSINQRISSSQSAQSLSTPVVSVATPTLPGEVMGGYPSAINTSYGTEYSLSSGDLSSLSAFNSSASLHLGSMTGWPQNMQHSGLGHLGNCSSAQLCQSSALSLPSNQNLHIKSEPVSPPRDRASGTPGLYGVPQQTPLRQDSGRSPVDSLSSCGSSYDGSDRDEHRANFHSPVGLMRAAENERQSPSVKRMRLSEAGWAS
Protein: Tetratricopeptide repeat protein 27 (TPR repeat protein 27) (Q6P3X3)
Organism: Homo sapiens (Human)
Interaction partners:
- WD repeat-containing protein 3
- Transducin beta-like protein 3
- WD repeat-containing protein 36
- RNA cytidine acetyltransferase
- Periodic tryptophan protein 2 homolog
- Uncharacterized protein.
- 116 kDa U5 small nuclear ribonucleoprotein component
- HEAT repeat-containing protein 1
- DNA-directed RNA polymerase I subunit RPA2
- Protein AAR2 homolog
Sequence:
MWTPELAILRGFPTEAERQQWKQEGVVGSESGSFLQLLLEGNYEAIFLNSMTQNIFNSTTTAEEKIDSYLEKQVVTFLDYSTDLDTTERQQLIFLLGVSSLQLFVQSNWTGPPVDLHPQDFLSSVLFQQFSEVKGLDAFVLSLLTLDGESIYSLTSKPILLLLARIILVNVRHKLTAIQSLPWWTLRCVNIHQHLLEERSPLLFTLAENCIDQVMKLQNLFVDDSGRYLAIQFHLECAYVFLYYYEYRKAKDQLDIAKDISQLQIDLTGALGKRTRFQENYVAQLILDVRREGDVLSNCEFTPAPTPQEHLTKNLELNDDTILNDIKLADCEQFQMPDLCAEEIAIILGICTNFQKNNPVHTLTEVELLAFTSCLLSQPKFWAIQTSALILRTKLEKGSTRRVERAMRQTQALADQFEDKTTSVLERLKIFYCCQVPPHWAIQRQLASLLFELGCTSSALQIFEKLEMWEDVVICYERAGQHGKAEEILRQELEKKETPSLYCLLGDVLGDHSCYDKAWELSRYRSARAQRSKALLHLRNKEFQECVECFERSVKINPMQLGVWFSLGCAYLALEDYQGSAKAFQRCVTLEPDNAEAWNNLSTSYIRLKQKVKAFRTLQEALKCNYEHWQIWENYILTSTDVGEFSEAIKAYHRLLDLRDKYKDVQVLKILVRAVIDGMTDRSGDVATGLKGKLQELFGRVTSRVTNDGEIWRLYAHVYGNGQSEKPDENEKAFQCLSKAYKCDTQSNCWEKDITSFKEVVQRALGLAHVAIKCSKNKSSSQEAVQMLSSVRLNLRGLLSKAKQLFTDVATGEMSRELADDITAMDTLVTELQDLSNQFRNQY
Protein: Ras-related protein Rab-1B (EC 3.6.5.2) (P10536)
Organism: Rattus norvegicus (Rat)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum (By similarity). Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Required to modulate the compacted morphology of the Golgi. Promotes the recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1918138, ECO:0000269|PubMed:23188820}. Membrane {ECO:0000269|PubMed:1918138}; Lipid-anchor {ECO:0000269|PubMed:1918138}; Cytoplasmic side {ECO:0000269|PubMed:1918138}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23188820}. Note=Targeted by REP1 to membranes of specific subcellular compartments including endoplasmic reticulum, Golgi apparatus, and intermediate vesicles between these two compartments. In the GDP-form, colocalizes with GDI in the cytoplasm (By similarity). Co-localizes with MTMR6 to the endoplasmic reticulum-Golgi intermediate compartment and to the peri-Golgi region (PubMed:23188820). {ECO:0000250|UniProtKB:Q9H0U4, ECO:0000269|PubMed:23188820}.
Interaction partners:
- TBC1 domain family, member 20.
- small monomeric GTPase
- Rab GDP dissociation inhibitor alpha
- Rab GDP dissociation inhibitor beta
- General vesicular transport factor p115
- Trafficking protein particle complex subunit 4
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 8
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 3
Sequence:
MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTVTSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGVPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKSASGGCC
Protein: N-methyltransferase gliN (EC 2.1.1.-) (Gliotoxin biosynthesis protein N) (Q4WMJ1)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. Gliotoxin contributes to pathogenesis during invasive aspergillosis. In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species.
Interaction partners:
- Cytochrome P450 monooxygenase gliC
- O-methyltransferase gliM
- Cytochrome P450 monooxygenase gliF
- Glutathione S-transferase gliG
- Thioredoxin reductase gliT
Sequence:
MTVLPDSENGYLLNYEDQEKRRMNMQHDLIKTYMGKLILAPLPFDQPNLRVLDSGTFNGLWLEDASTLLQSPTLVGTDVSPTAFPAKRPPNTEFHVQSISDPWPTEWRDSFDLVHQKLVIACVPPDEGRQALYRLIDLAKPGTGWVQFTEGSLEHLTPEQRKQYPVLARFQSLVAEMLPHFRWNPRPGKLVRQWLEEYGLQEVQEKVMEIPIGAGNPDPKLGEMAKQNMLEVVSNFRTAATRLPDGTGIRAEDFDPILRDIKVEFETVGGILRFNTVWGRRP
Protein: Probable ketoamine kinase SAOUHSC_02908 (EC 2.7.1.-) (Q2FV31)
Organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)
Function: Ketoamine kinase that phosphorylates ketoamines, such as erythruloselysine and ribuloselysine, on the third carbon of the sugar moiety to generate ketoamine 3-phosphate. Has higher activity on free lysine (erythruloselysine and ribuloselysine), than on ribuloselysine and erythruloselysine residues on glycated proteins.
Interaction partners:
Sequence:
MNEQWLEHLPLKDIKEISPVSGGDVNEAYRVETDTDTFFLLVQRGRKESFYAAEIAGLNEFERAGITAPRVIASGEVNGDAYLVMTYLEEGASGSQRQLGQLVAQLHSQQQEEGKFGFSLPYEGGDISFDNHWQDDWCTIFVDKRLDHLKDELLNRGLWDANDIKVYDKVRRQIVAELEKHQSKPSLLHGDLWGGNYMFLQDGRPALFDPAPLYGDREFDIGITTVFGGFTSEFYDAYNKHYPLAKGASYRLEFYRLYLLMVHLLKFGEMYRDSVAHSMDKILQDTTS
Protein: Rhox homeobox family member 1 (Ovary-, testis- and epididymis-expressed gene protein) (Paired-like homeobox protein PEPP-1) (Q8NHV9)
Organism: Homo sapiens (Human)
Function: Transcription factor maybe involved in reproductive processes. Modulates expression of target genes encoding proteins involved in processes relevant to spermatogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:11980563}.
Interaction partners:
Sequence:
MARSLVHDTVFYCLSVYQVKISPTPQLGAASSAEGHVGQGAPGLMGNMNPEGGVNHENGMNRDGGMIPEGGGGNQEPRQQPQPPPEEPAQAAMEGPQPENMQPRTRRTKFTLLQVEELESVFRHTQYPDVPTRRELAENLGVTEDKVRVWFKNKRARCRRHQRELMLANELRADPDDCVYIVVD
Protein: Protein Smaug homolog 1 (Smaug 1) (mSmaug 1) (Sterile alpha motif domain-containing protein 4A) (Q8CBY1)
Organism: Mus musculus (Mouse)
Function: Acts as a translational repressor of SRE-containing messengers.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16221671}. Cell projection, dendrite {ECO:0000269|PubMed:16221671}. Synapse, synaptosome {ECO:0000269|PubMed:16221671}. Note=Colocalizes throughout the cytoplasm in granules with polyadenylated RNAs, PABPC1 and STAU1. Also frequently colocalizes in cytoplasmic stress granule-like foci with ELAVL1, TIA1 and TIAL1. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner (By similarity). Enriched in synaptoneurosomes. {ECO:0000250}.
Interaction partners:
Sequence:
MMFRDQVGVLAGWFKGWNECEQTVALLSLLKRVSQTQARFLQLCLEHSLADCAELHVLEGEANSPGIINQWQQESKDKVISLLLTHLPLLKPGNLDAKAEYMKLLPKILAHSIEHNQHIEESRQLLSYALIHPATSLEDRSALAMWLNHLEDRTSTSFGSQNRGRSDSVDYGQTHYYHQRQNSDDKLNGWQNSRDSGICISASNWQDKSLGCENGHVPLYSSSSVPATINTIGTGASTILSGQAHHSPLKRSVSLTPPMNVPNQPLGHGWMSHEDLRARGPQCLPSDHAPLSPQSSVASSGSGGSEHLEDQTTARNTFQEEGSGMKDVPAWLKSLRLHKYAALFSQMTYEEMMALTECQLEAQNVTKGARHKIVISIQKLKERQNLLKSLERDIIEGGSLRTPLQELHQMILTPIKAYSSPSTTPEVRCREPSLMESPSPDCKDSAAAVTSATASASAGASGGLQPPQLSSCDGELAVAPLPEGDLPGQFTRVMGKVCTQLLVSRPDEENISSYLQLLDKCLVHEAFTETQKKRLLSWKQQVQKLFRSFPRKTLLDISGYRQQRNRGFGQSNSLPTASSVGSGMGRRNPRQYQIASRNVPSARLGLLGTSGFVSSNQRHTAANPTIMKQGRQNLWFANPGGSNSMPSRTHSSVQKTRSLPVHTSPQNMLMFQQPEFQLPVTEPDINNRLESLCLSMTEHALGDGVDRTSTI
Protein: Islet cell autoantigen 1-like protein (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 15 protein homolog) (Ica69-related protein) (Q3TY65)
Organism: Mus musculus (Mouse)
Interaction partners:
- PRKCA-binding protein
Sequence:
MDSSEQLRAEDNQSVVSRMQKNYWRTKQVFIKATGKKEDEHVVASDAELDAKLEVFHSIQETCNELVKIVEKYQLRLNVISEEENELGLFLKFQAERDSTQAGEMMDAAGKALCSSAKQRLALCTPLSRLKQEVATFSQRAISDTLVTINRMERARTEYRGALLWMKDASQELDPDTFKQMEKFRKVQNQVRNSKDSFDKLKKDVCQKVDLLGASRCNMLSHSLTTYQRTLLGFWEKTAQMMTQIQEACAGFHPYDFLALKRLQDTPGNLTADCTEGQTEGSCLTTDLNKVALSEEEEEERFEREPAVARALPRDSLEGDDFEKEFSFLNSLLSPTSSSASEFTQECQPACGSPCTGLTSQEPSVGPGSLTSSSQFLPSQLFDLGLHADGAFNTPNNGNQDMSAWFNLFADLGPLSNPDAIGHSDDELLNA
Protein: Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB) (P0C356)
Organism: Oryza sativa (Rice)
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00482}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00482}.
Interaction partners:
Sequence:
MELRFPRFSQGLAQDPTTRRIWFGIATAHDFESHDDITEERLYQNIFASHFGQLAIIFLWTSGNLFHVAWQGNFESWIQDPLHVRPIAHAIWDPHFGQPAVEAFTRGGAAGPVNIAYSGVYQWWYTIGLRTNEDLYTGALFLLFLSTLSLIGGWLHLQPKWKPSLSWFKNAESRLNHHLSGLFGVSSLAWTGHLVHVAIPASRGEYVRWNNFLDVLPYPQGLGPLLTGQWNLYAQNPDSSNHLFGTTQGAGTAILTLLGGFHPQTQSLWLTDIAHHHLAIAFIFLIAGHMYRTNFGIGHSIKDLLEAHTPPGGRLGRGHKGLYDTINNSIHFQLGLALASLGVITSLVAQHMYSLPSYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGAIFFIRDYNPEQNEDNVLARMLDHKEAIISHLSWASLFLGFHTLGLYVHNDVMLAFGTPEKQILIEPIFAQWIQSAHGKTTYGFDILLSSTSGPAFNAGRTLWLPGWLNAVNENSNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKHITLWQGNVSQFNESSTYLMGWLRDYLWLNSSQLINGYNPFGMNSLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLAWAHERTPLANLIRWRDKPVALSIVQARLVGLAHFSVGYIFTYAAFLIASTSGKFG
Protein: ABC transporter G family member 3 (ABC transporter ABCG.3) (AtABCG3) (White-brown complex homolog protein 3) (AtWBC3) (Q9ZUU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Probable inactive receptor kinase At5g58300
Sequence:
MEEIQSQSDLYRSSSSSASSPTSRVPSSHFFYVRKPGSLRQPISFEDSPEWEDTPDVDLRMEDEAGGGDSINDATTTPVSPSLSKMNSGSMASPPVPEGGAGTGVVRKIAGASIAWKDLTVTMKGKRKYSDKVVKSSNGYAFPGTMTVIMGPAKSGKSTLLRALAGRLPPSAKMYGEVFVNGSKSHMPYGSYGFVERETQLIGSLTVREFLYYSALLQLPGFLFQKRSVVEDAIQAMSLSDYANKLIGGHCYMKGLRSGERRRVSIARELVMRPHILFIDEPLYHLDSVSALLMMVTLKKLASMGCTLVFTIYQSSTEVFGLFDRICLLSNGNTLFFGETLACLQHFSNAGFPCPIMQSPSDHFLRAINTDFDRIIAMCKNWQDDNGDFSAVNMDTAVAIRTLEATYKSSADADSVEAMIIKLTEREGTQLKSKGKAGAATRVAVLTWRSLLVMSREWKYYWLRLILYMILTLSIGTLYSGLGHSLSSVATRVAAVFVFVSFASLLGIAGIPSLLKEIKIYRSEASNQHSGAFVFLLGQFLGSIPFLFLMSISSSLVFYFMVGLRDDFSLLMYFVLNFFMCLLVNEGLMLFIACIWRDVYWSTLTLISVHVIMMLAAGHFRIRTALPKPVWTYPFAYISFHTYSIEGLLENEYLGEVFAVGEVRSISGYQAIQGNYQISPDTNAKWRNMLVLLAMAFGYRLLVYVLLRFGLNKNVSGRLLLSHKKNNSSR