wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 4E-1 (eIF4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein) (A0A1U8GR65)
Organism: Capsicum annuum (Capsicum pepper)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. Key component of recessive resistance to potyviruses.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}.
Interaction partners:
Sequence:
MATAEMEKTTTFDEAEKVKLNANEADDEVEEGEIVEETDDTTSYLSKEIATKHPLEHSWTFWFDNPVAKSKQAAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLVVGADLHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHEDEICGAVVSVRGKGEKISLWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV
Protein: MICOS complex subunit MIC13 (Q8R404)
Organism: Mus musculus (Mouse)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Constituent of mature MICOS complex, it is required for the formation of cristae junction (CJ) and maintenance of cristae morphology. Required for the incorporation of MICOS10/MIC10 into the MICOS complex.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5XKP0}; Single-pass membrane protein {ECO:0000255}. Note=Enriched at crista junctions. {ECO:0000250|UniProtKB:Q5XKP0}.
Interaction partners:
- MICOS complex subunit Mic26
- MICOS complex subunit Mic27
- MICOS complex subunit Mic25
- MICOS complex subunit Mic19
- MICOS complex subunit Mic10
- MICOS complex subunit Mic60
- Coiled-coil-helix-coiled-coil-helix domain containing 10
- DnaJ homolog subfamily C member 11
- Metaxin-2
- NADH dehydrogenase 1 alpha subcomplex subunit 7
Sequence:
MVARVWSLMRFLIKGSVAGGAVYLVYDQELLGPSDKSEAALRKAEEVVPPAMYQFSQYVCQQTGLEMPQLPTPPKIKFPNFRDSWNSGIISVMSALSVAPSKAREYSKEGWEYLKEHSK
Protein: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) (EC 1.17.7.4) (Q72G08)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Interaction partners:
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- Bifunctional enzyme IspD/IspF
- 1-deoxy-D-xylulose-5-phosphate synthase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- Geranylgeranyl diphosphate synthase
- Isopentenyl-diphosphate delta-isomerase
- Small ribosomal subunit protein bS1
- Cytidylate kinase
- Ribosomal protein S1, putative
Sequence:
MNVIRARTAGFCMGVSLALRKLDREVDRAEEKAAQGSPRCRIATFGPIIHNPQVLEAYAGMGVRCLRQVDEVEAGDHVVIRAHGVPQQQEKALRSRDAVVVDATCPKVKKAQLGIEEQCRAGRTLLLFGEAEHPEVRGLLSYAGEGALVFGSVDELEGLPLQPETEYFLAAQTTQDRVAFEVARAWLHERLGHEVPVLETICDATRLRQQEAIDIARKVDAMVVVGGFDSGNTRRLADVAAAQGVFTVHVENESQLPVEQLRGCGIIGLTAGASTPKSIIDATQRFLESL
Protein: KCNE3 protein (Potassium voltage-gated channel subfamily E member 3) (Potassium voltage-gated channel, Isk-related family, member 3) (cDNA, FLJ92142, Homo sapiens potassium voltage-gated channel, Isk-related family,member 3 (KCNE3), mRNA) (Q6IAE6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
METTNGTETWYESLHAVLKALNATLHSNLLCRPGPGLGPDNQTEERRASLPGRDDNSYMYILFVMFLFAVTVGSLILGYTRSRKVDKRSDPYHVYIKNRVSMI
Protein: NDR1/HIN1-like protein 6 (Q8LD98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important role in the abiotic stresses-induced abscisic acid (ABA) signaling and biosynthesis. Acts as positive regulator of ABA-mediated seed germination inhibition. Functions downstream of ABF2/AREB1, ABF4/AREB2 and ABF3.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26849212}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:26849212}. Note=Moves from plasma membrane to cytosol under abiotic stress. {ECO:0000269|PubMed:26849212}.
Interaction partners:
- Membrane lipoprotein
- Late embryogenesis abundant
- Non-race specific disease resistance protein
- Tubby-like F-box protein 11
Sequence:
MSQHQKIYPVQDPEAATARPTAPLVPRGSSRSEHGDPSKVPLNQRPQRFVPLAPPKKRRSCCCRCFCYTFCFLLLLVVAVGASIGILYLVFKPKLPDYSIDRLQLTRFALNQDSSLTTAFNVTITAKNPNEKIGIYYEDGSKITVWYMEHQLSNGSLPKFYQGHENTTVIYVEMTGQTQNASGLRTTLEEQQQRTGNIPLRIRVNQPVRVKFGKLKLFEVRFLVRCGVFVDSLATNNVIKIQSSSCKFRLRL
Protein: Phytanoyl-CoA dioxygenase, peroxisomal (EC 1.14.11.18) (Lupus nephritis-associated peptide 1) (Phytanic acid oxidase) (Phytanoyl-CoA alpha-hydroxylase) (PhyH) (O35386)
Organism: Mus musculus (Mouse)
Function: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (By similarity). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl-and 4-methyl-branched acyl-CoAs (By similarity).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:O14832}.
Interaction partners:
- Phytanoyl-CoA hydroxylase-interacting protein
- Peroxisomal targeting signal 2 receptor
- Peroxisomal leader peptide-processing protease
- Peroxisomal targeting signal 1 receptor
- Alkyldihydroxyacetonephosphate synthase, peroxisomal
- 3-ketoacyl-CoA thiolase B, peroxisomal
- Peroxisomal membrane protein PEX13
- Alpha-methylacyl-CoA racemase
Sequence:
MNLTRAGARLQVLLGHLGRPSAPTIVAQPVSGLASPASFQPEQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVSDDDIQRFRAEFERICREEVKPPGIVIMRDVALAKQDYMPSDRMVSKIQDFQEDEELFRYCLLPEILKYVECFTGPNIMALHGMLINKPPDVGKKTSRHPLHQDLHYFPFRPSNLIVCAWTAMEHIDRNNGCLVVLPGTHKGTLKPHDYPKWEGGVNKMYHGIQDYDPNSPRVHLVMEKGDTVFFHPLLIHGSGRNKTQGFRKAISCHFGSSDCQCIDVSGTSQENIAREVVEMAEKKYGFQGVMDFKDTWIFRSRLVKGERINI
Protein: DNA-binding transcriptional dual regulator (Q88F34)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Interaction partners:
- Coproporphyrinogen-III oxidase
- DNA-binding transcriptional dual regulator
Sequence:
MSEPVKLRPHNQAHCKDCSLAPLCLPLSLNLEDMDALDEIVKRGRPLKKGEFLFRQGDSFGSVYAVRSGALKTFSLSDSGEEQITGFHLPSELVGLSGMDTEAYPVSAQAQETTSVCEIPFERLDELSVQLPQLRRQLMRVMSREIRDDQQMMLLLSKKTADERIATFLVNLSARFRARGYSANQFRLSMSRNEIGNYLGLAVETVSRVFTRFQQNGLLRAEGKEVHILDPIQLCALAGGAIEA
Protein: Kynurenine formamidase (KFA) (KFase) (EC 3.5.1.9) (Arylformamidase) (N-formylkynurenine formamidase) (FKF) (P0C8P4)
Organism: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
Interaction partners:
- Kynureninase
- Tryptophan 2,3-dioxygenase
- NAD-dependent formate dehydrogenase delta subunit
- NAD-dependent formate dehydrogenase alpha subunit
- Formate dehydrogenase iron-sulfur subunit
- Arylformamidase
- Formate dehydrogenase alpha subunit
- NAD-dependent formate dehydrogenase gamma subunit
- Formate dehydrogenase subunit C
- NAD-dependent formate dehydrogenase beta subunit
Sequence:
MPQAPQLHDGRRIWDISPAVSPATPVWPGDTPFQHDPAWQLDEHCPVNVGRITMSPHTGAHADAPLHYAADGAPIGAVPLDAYLGPCRVIHCIGAAPRVEPQHIAHALAGTPPRVLLRTYAQAPQGKWDSAFCAVAPETISLLARHGVRLIGIDTPSLDPETSKTMDAHHAVRDHQLAILEGIVLDEVPAGDYELIALPLRLATLDASPVRAVLRELP
Protein: Rho GTPase activating protein 45 (K7EM85)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFSRKKRELMKTPSISKKNRAGSPSPQPSGPHFISGETEAVSRPENPFNELPSDLPKELPRKDGADAVFPGPSLEPPAGSSGVKATGTLKRPTSLSRHASAAGFPLSGAASWTLGRSHRSPLTAASPGELPTEGAGPDVVEDISHLLADVARFAEGLEKLKECVLRDDLLEARRPRAHECLGEALRVMHQIISKYPLLNTVETLTAAGTLIAKVKAFHYESNNDLEKQEFEKALETIAVAFSSTVSEFLMGEVDSSTLLAVPPGDSSQSMESLYGPGSEGTPPSLEDCDAGCLPAEEVDVLLQRCEGGVDAALLYAKNMAKYMKDLISYLEKRTTLEMEFAKGLQKIAHNCRQSVMQEPHMPLLSIYSLALEQDLEFGHSMVQAVGTLQTQTFMQPLTLRRLEHEKRRKEIKEAWHRAQRKLQEAESNLRKAKQGYVQRCEDHDKARFLVAKAEEEQAGSAPGAGSTATKTLDKRRRLEEEAKNKAEEAMATYRTCVADAKTQKQELEDTKVTALRQIQEVIRQSDQTIKSATISYYQMMHMQTAPLPVHFQMLCESSKLYDPGQQYASHVRQLQRDQEPDVHYDFEPHVSANAWSPVMRARKSSFNVSDVARPEAAGSPPEEGGCTEGTPAKDHRAGRGHQVHKSWPLSISDSDSGLDPGPGAGDFKKFERTSSSGTMSSTEELVDPDGGAGASAFEQADLNGMTPELPVAVPSGPFRHEGLSKAARTHRLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCGHKKLQGRLQLFGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHELVGLAKDSLKAEAEAKAASRGRQDGSESEAVAVALAGRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDYPHQARVIETLIVHYGLVFEEEPEETPGGQDESSNQRAEVVVQVPYLEAGEAVVYPLQEAAADGCRESRVVSNDSDSDLEEASELLSSSEASALGHLSFLEQQQSEASLEVASGSHSGSEEQLEATAREDGDGDEDGPAQQLSGFNTNQSNNVLQAPLPPMRLRGGRMTLGSCRERQPEFV
Protein: Rho GTPase activating protein at 1A, isoform D (X2J9V9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}.
Interaction partners:
Sequence:
MSVFDDFQRLWMQRFPQSSLSDAWEQDVRASLERHKVRINELSKELEQETLYVEYLERLLSDVERYRVSGGDPKALFEAASGSCASSNNSNCSSTTNGATQEESNTNLDKDFKSSLNLRESPSSTGAKDKDRLSLNPDNKYTTHTNAVIGGIGSEKVSGPLHSTQITADGKRTGELYLKREEDKCKDSNSEDTDGALQQCITELAASLKAQPDNVAGGRLENDVDIDKPLRKSTSQYVTVIQVKEAKDKESADGTTSSSGIGEPQQQPTPPSTFSRYSEATAPPLSPSLTSYAAHVEAKKKMPPRPPPKNIRRVEPPTIPSQQLSSSPKRETYMINTMPSSSSGSLCIDSLGNSLERNIKPSDILRQKSSDNLDSKYSAKRKTTPELSKFVNVNNPELMEELGRKMVSKADSLEQTRRNDSSPSGCGSLGRTSSTPGRSLTPGRTGVGASPTGSLSKTGKLAMADSSSTSSLERRSCLQAVDADIGTESRESGANQRSVGSKESLTSQGISEIKSYESVSSLSSESAKAVASQQSAAAGGALAECEPYYDSVPLDNGDGEYVFIKPGRTGSSSSRDDLSTPGSSILPLPNVADPESPGRTSNYVNIDFFLQQGIETRSSSLDSDGEYEGPPILRTISHDDQTTTQTTPGAIRKNLVSAILVCGNARGAKIRSILSSIIQSETIYVECLNKMMQYKKAIHATLTTSQPVIREEEENTIFFKIDELYDLHTGFLSDLKTIVSHEGGDVLIGEPFRRLAEMFDLYSAFLHNYKNAIETVKKCSANNPQFKKIVSTIVLNLQTEQSLTLEDLLHKPVARVQINALVFNDLLRETPNAHPDHQPLRQAQKIIQMFLNQFNVVNQRLPIESNRNLRRMVRNSFIVELVDGHRKLRHLFLFNDVIACAKYKALGRDRIDYELKWFIPLKDVSIYEEADPAVELKESSPANISQVKRNLRSVRDQLAMEVANSGSGAFRSGDKYRRKLADLESQLVLATPNLVLRLGNKANNKTITFFLSSDFERTQWIDSILSLKQKCNLPGANTINSLEVTAFIVAMQKGMKTEMGSYLMRNTNDESLLVGDLYMGVHGLEGLEQANDLYICVEVDSYGHYFRKATTKKICRSQTPLWNESFMLELEGSQNVRILLYEAKERPLLKAKHILKLSLSWLTETTQPKSIKLTETLELGCSFRFIPGELFRGSTKPGALFGAKMSQVLKREKRDIPFIIGACIREVERRGMLEVGCYRVSGSASDLAKLKKAFESDAYEAEQLLREVDIHSVTGILKTFLRELPEALFTDQLYPRFFDTFSAFSNNNESTRINELLKVFEELPQANKASITSILDHLIRVHEKETDNKMSLHNLAMVFGPTLLRPGQTQVKQKDPLAASTVDVMAQAGILYCFLQARIKKD
Protein: Vacuolar basic amino acid transporter 1 (Q04301)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transporter required for vacuolar uptake of at least histidine and lysine.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:15572352}; Multi-pass membrane protein {ECO:0000269|PubMed:15572352}.
Interaction partners:
- Vacuolar basic amino acid transporter 3
- Vacuolar amino acid transporter 1
- Uncharacterized membrane protein YJL163C
- Uncharacterized transporter YMR279C
Sequence:
MQTLDETSNLLPPPEEAEAPPLEQKFHEYNLALPKFPILFSLWLGSFLSSLDSTIVANIMNRVAEEFSESSKKQWIATSFLLTNTAFQPLYGKLSDITGRKSALLTAQFFFGLGCLLTCFARNVTEFSIARAICGIGAGGLNAISSIAVSDICTARERGVYQGYANIVFGFGQLLGAPLGGVFIETIGWRALFGIQVPVIMLCSVLAIKNINIKLFHVPPMKERYTLKNLSRIDIFGSLSLVATISGVLFLCSSQLNKLYLALFTIGSFIVFILVERYYATEKILPFELLTRSFCLSSAVTVISSFVVFGEIFRSPIYLQLLQNISVTKTGLFLIFPSISVAVGSLVTGWVLRNTKINLAHCAYQIIFGGMIMQLLGLGLGYFLLSHLNPDYTIYDMLESITFRSNSIWWKLIYVFASVLVSFGYACLLVATLVSIVFTVEKSQQGTMTGVFYLWRSIGNVLGASLTLVSYENSLSSMLWNYMFKTKRDDEYHFTKKQYYSLINDSSYLRGPNFPTDIFVRILDVYKKAFLISYIPNIALAAVGIVLSLYLVKHTYKRSSSS
Protein: R151.8A protein (G5EG26)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Derlin-2
- Histidine kinase/HSP90-like ATPase domain-containing protein
- Double-stranded RNA-specific adenosine deaminase adr-2
- Alanine--glyoxylate aminotransferase
Sequence:
MPASVTHVIFDFDGLLVDTESAYTEANMELLRKYGHVFTMDLKRRQMGKRHDESIRWLINELKIGDLVTPEEYSRQYDELLIEMFKRSPAMPGAEKLVRHLLHTGVPVALCTGSCSRTFPTKLDNHKDWVNMIKLQVLSGDDPEVKHGKPHPDPFLVTMKRFPQVPESADKVLVFEDSYNGVLSALDAGMQCVMVPERSIFDPDSDPEFKNRVTVILNSLEQFKPEDFGLPPY
Protein: Putative serine/threonine-protein kinase receptor (EC 2.7.11.1) (S-receptor kinase) (SRK) (Q09092)
Organism: Brassica oleracea var. viridis (Flowering kale) (Brassica oleracea var. acephala)
Function: Involved in sporophytic self-incompatibility system (the inability of flowering plants to achieve self-fertilization), probably acting in combination with S-locus-specific glycoproteins. Interaction with a ligand in the extracellular domain triggers the protein kinase activity of the cytoplasmic domain.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MKGARNIYHHSYMSFLLVFVVMILIHPALSIYINTLSSTESLTISSNKTLVSPGSIFEVGFFRTNSRWYLGMWYKKVSDRTYVWVANRDNPLSNAIGTLKISGNNLVLLDHSNKPVWWTNLTRGNERSPVVAELLANGNFVMRDSSNNDASEYLWQSFDYPTDTLLPEMKLGYNLKTGLNRFLTSWRSSDDPSSGNFSYKLETQSLPEFYLSRENFPMHRSGPWNGIRFSGIPEDQKLSYMVYNFIENNEEVAYTFRMTNNSFYSRLTLISEGYFQRLTWYPSIRIWNRFWSSPVDPQCDTYIMCGPYAYCDVNTSPVCNCIQGFNPRNIQQWDQRVWAGGCIRRTQLSCSGDGFTRMKKMKLPETTMATVDRSIGVKECKKRCISDCNCTAFANADIRNGGSGCVIWTERLEDIRNYATDAIDGQDLYVRLAAADIAKKRNASGKIISLTVGVSVLLLLIMFCLWKRKQKRAKASAISIANTQRNQNLPMNEMVLSSKREFSGEYKFEELELPLIEMETVVKATENFSSCNKLGQGGFGIVYKGRLLDGKEIAVKRLSKTSVQGTDEFMNEVTLIARLQHINLVQVLGCCIEGDEKMLIYEYLENLSLDSYLFGKTRRSKLNWNERFDITNGVARGLLYLHQDSRFRIIHRDLKVSNILLDKNMIPKISDFGMARIFERDETEANTMKVVGTYGYMSPEYAMYGIFSEKSDVFSFGVIVLEIVSGKKNRGFYNLDYENDLLSYVWSRWKEGRALEIVDPVIVDSLSSQPSIFQPQEVLKCIQIGLLCVQELAEHRPAMSSVVWMFGSEATEIPQPKPPGYCVRRSPYELDPSSSWQCDENESWTVNQYTCSVIDAR
Protein: Frataxin, mitochondrial (Fxn) (EC 1.16.3.1) [Cleaved into: Frataxin intermediate form; Frataxin mature form; Extramitochondrial frataxin] (D3ZYW7)
Organism: Rattus norvegicus (Rat)
Function: Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly. Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release. Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems (By similarity). May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation. May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (By similarity).
Subcellular location: [Frataxin mature form]: Mitochondrion {ECO:0000250|UniProtKB:Q16595}.; SUBCELLULAR LOCATION: [Extramitochondrial frataxin]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q16595}.
Interaction partners:
- Iron-sulfur cluster assembly enzyme ISCU
- Cysteine desulfurase
- LYR motif containing 4
- Selenocysteine lyase
- Ferrochelatase
- Cytoplasmic aconitate hydratase
- Aconitate hydratase, mitochondrial
- Ferredoxin-2, mitochondrial
- Iron-sulfur clusters transporter ABCB7, mitochondrial
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
Sequence:
MWTFGRRAAAGLLPRTASRASAWVRNPRGRERIGTCGRRGLHVTANADAIRHSHLNLHYLGQILNIKKQSVCVVHLRNSGTLGNPSSLDETAYERLAEETLDALAEFFEDLADKPYTLKDYDVSFGDGVLTIKLGGDLGTYVINKQTPLLYLWFSGPCSGPKRYDWTGKNWVYSHDGVSLHELLARELTEALNTKLDLSSLAYSGKGT
Protein: Small ribosomal subunit protein eS19y (40S ribosomal protein S19-2) (Q9LF30)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS28z/eS28y
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein eS21z
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein eS12z
- Small ribosomal subunit protein uS12z
Sequence:
MATGKTVKDVSPHDFVKAYASHLKRSGKIELPLWTDIVKTGRLKELAPYDPDWYYIRAASMARKIYLRGGLGVGAFRRIYGGSKRNGSRPPHFCKSSGGIARHILQQLETMSIVELDTKGGRRITSSGQRDLDQVAGRIAAES
Protein: Transcription factor MafK isoform X1 (V-maf avian musculoaponeurotic fibrosarcoma oncogene homolog K) (A0A0R4IVU1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- BTB and CNC homology 1, basic leucine zipper transcription factor 1 b.
- Nuclear factor, erythroid 2.
- Nuclear factor
- BTB and CNC homology 1, basic leucine zipper transcription factor 1 a.
- Nuclear factor, erythroid 2-like 2b.
- BTB and CNC homology 1, basic leucine zipper transcription factor 2b
- Endoplasmic reticulum membrane sensor NFE2L1
- Endoplasmic reticulum membrane sensor NFE2L1
Sequence:
MQGMTTHFKAGKALKVKKEAGENAPALSDDELVAMSVRELNQHLRGLTKEDVVRLKQRRRTLKNRGYAASCRIKRVTQKEELERQKTELQHEVDKLARENASMRLELDALRAKYEALQCFARTVTRGPPGKVAATSVITIVKSANHSPSSAPFSAQS
Protein: Beta-glucuronidase (EC 3.2.1.31) (Q8VNV4)
Organism: Clostridium perfringens
Interaction partners:
Sequence:
MLYPIITESRQLIDLSGIWKFKLNEGNGLTEELSKAPLEDTIEMAVPSSYNDLVESQEVRDHVGWVWYERNFTIPKTLLNERIVLRFGSATHEAKVYLNGELLVEHKGGFTPFEAEINDLLVSGDNRLTVAVNNIIDETTLPVGLVKEVEVDGKKVIKNSVNFDFFNYAGIHRPVKIYTTPKSYIEDITIVTDFKENNGYVNYEVQAVGKCNIKVTIIDEENNIVAEGEGKEGKLTINNVHLWEPMNAYLYKLKVELLDDEEIIDTYFEEFGVRTVEVKDGKFLINNNPFYFKGFGKHEDSYVNGRGINEAINIKDFNLMKWIGANSFRTSHYPYSEEIMRLADREGIVVIDETPAVGLHLNFMATGFGGDAPKRDTWKEIGTKEAHERILRELVSRDKNHPCVVMWSVANEPDSDSEGAKEYFEPLIKLTKELDPQKRPVTVVTYLMSTPDRCKVGDIVDVLCLNRYYGWYVAGGDLEEAKRMLEDELKGWEERCPKTPIMFTEYGADTVAGLHDTVPVMFTEEYQVEYYKANHEVMDKCKNFVGEQVWNFADFATSQGIIRVQGNKKGIFTRERKPKMIAHSLRERWTNIPEFGYKK
Protein: Transcription factor ATOH8 (Class A basic helix-loop-helix protein 21) (bHLHa21) (Helix-loop-helix protein hATH-6) (hATH6) (Protein atonal homolog 8) (Q96SQ7)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins. Regulates endothelial cell proliferation, migration and tube-like structures formation. Modulates endothelial cell differentiation through NOS3. May be implicated in specification and differentiation of neuronal cell lineages in the brain (By similarity). May participate in kidney development and may be involved in podocyte differentiation (By similarity). During early embryonic development is involved in tissue-specific differentiation processes that are dependent on class II bHLH factors and namely modulates the differentiation program initiated by the pro-endocrine factor NEUROG3 (By similarity). During myogenesis, may play a role during the transition of myoblasts from the proliferative phase to the differentiation phase (By similarity). Positively regulates HAMP transcription in two ways, firstly by acting directly on the HAMP promoter via E-boxes binding and indirectly through increased phosphorylation of SMAD protein complex. Repress NEUROG3-dependent gene activation in a gene-specific manner through at least two mechanisms; requires only either the sequestering of a general partner such as TCF3 through heterodimerization, either also requires binding of the bHLH domain to DNA via a basic motif (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:24463812}. Nucleus speckle {ECO:0000269|PubMed:24463812}. Cytoplasm {ECO:0000250|UniProtKB:Q99NA2}.
Interaction partners:
Sequence:
MKHIPVLEDGPWKTVCVKELNGLKKLKRKGKEPARRANGYKTFRLDLEAPEPRAVATNGLRDRTHRLQPVPVPVPVPVPVAPAVPPRGGTDTAGERGGSRAPEVSDARKRCFALGAVGPGLPTPPPPPPPAPQSQAPGGPEAQPFREPGLRPRILLCAPPARPAPSAPPAPPAPPESTVRPAPPTRPGESSYSSISHVIYNNHQDSSASPRKRPGEATAASSEIKALQQTRRLLANARERTRVHTISAAFEALRKQVPCYSYGQKLSKLAILRIACNYILSLARLADLDYSADHSNLSFSECVQRCTRTLQAEGRAKKRKE
Protein: N-glycosidase YbiA (EC 3.2.2.-) (Riboflavin biosynthesis intermediates N-glycosidase) (P30176)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of the N-glycosidic bond in the first two intermediates of riboflavin biosynthesis, which are highly reactive metabolites, yielding relatively innocuous products. Thus, can divert a surplus of harmful intermediates into relatively harmless products and pre-empt the damage these intermediates would otherwise do. Helps maintain flavin levels. May act on other substrates in vivo. Has no activity against GTP, nucleoside monophosphates or ADP-ribose. Is Required for swarming motility.
Interaction partners:
- Riboflavin biosynthesis protein RibD
- GTP cyclohydrolase-2
- Uncharacterized protein YbiB
Sequence:
MPVRAQRIQHVMQDTIINFYSTSDDYGDFSNFAAWPIKVDGKTWPTSEHYFQAQKFLDEKYREEIRRVSSPMVAARMGRDRSKPLRKNWESVKEQVMRKALRAKFEQHAELRALLLATAPAKLVEHTENDAYWGDGGHGKGKNRLGYLLMELREQLAIEK
Protein: Glycine cleavage system H protein, mitochondrial (Lipoic acid-containing protein) (Q91WK5)
Organism: Mus musculus (Mouse)
Function: The glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST) (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P23434}.
Interaction partners:
- Glycine dehydrogenase
- Aminomethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Dihydrolipoyl dehydrogenase, mitochondrial
- Lipoyl amidotransferase LIPT1, mitochondrial
- Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial
- Lipoyl synthase, mitochondrial
- Alanine--glyoxylate aminotransferase
- Dimethylglycine dehydrogenase, mitochondrial
Sequence:
MSLQVSRSLRVVAYSLRTALTFCSPRPCVPSAAAVRSLRTGSALLSVRKFTEKHEWITTEEGIGTVGISNFAQEALGDVVYCSLPEVGTKLKKQEEFGALESVKAASELYSPLSGEVTEVNEALAENPGLVNKSCYEDGWLIKMTLSDPSEMDELMSEEAYEKYVKSIEE
Protein: Uncharacterized protein (Q38B13)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVLPSLAPSPHSNRFHDVTQDRVEGASVEEIFECVNDSVPAPTVRVLGDEFSTFDQKHERSNKTSDSNVAGRSKPLNGKGGTLPTSAEVEKPFEINKHAVGNISSVVAVDDDDRASSIKFTFVDGESVLSRSPTTTSIVFEVEPSSNMRGTSASSLLSPNRSKLSTDTADGAPLNSCRPAEAVRHGTPASSGLANERRRAGSATPIKRSSVKSCFFEHEVQEQRGLRGNRCSSASSLDSRRGPGGRHSSRSRRSGSGSVTPLSGRREGIRSASRTDGGRRSYGSHRSEGRYTNSDASSYSRGRAGDWKPRYYNNEPPSSNTGSRRPSPHTQLDTPHSQRSRCLLASPRYSDLTVSQHYLMGTNPNVSHATSPALEMFKVHRSSCSPMRVRQKKRQELLAKIEKELTAVRDEMQSLDVELEQAMLSDPHVRLYHMNNRRDRDERRSRLLLYLNLENARNQLLSEDDETEERRLRRRREVERKRSELFERLHQQSSARRHSSQGSTPRRRRTPSSSFDDGLHERLYSDAAKFREWHEERRQRARQEREQMELEELLFTRVLRKVGLDSSERMLTPQEEEECAAVLCTKLLDDPEKLQEYIRPKRLNREQEELLNARLARRSEINLNAIRNQMEVAQMAECTFRPRTNSPQSRNRQEAILSINKPTAASIRRRKANVESGSSTRPPSRRGHSIPRNRTCEKLYNSAKKSEDRLSALKVSSESMKKLQLLKSKLKEDHHFRRRAELDPSLAQRYMDSLVV