wanglab/gogpt-training-data huggingface dataset:
Protein: Chaperonin GroEL (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin-60) (Cpn60) (GroEL protein) (P0A6F5)
Organism: Escherichia coli (strain K12)
Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates. Rapid binding of ATP, followed by slower binding of the non-native substrate protein and GroES to the cis open ring of GroEL initiates productive folding of the non-native protein inside a highly stable GroEL-ATP-GroES complex. Binding of ATP and GroES induces conformational changes that result in the release of the substrate protein into a nano-cage compartment, within the GroEL central cavity, for folding in isolation. To discharge GroES and substrate protein, ATP hydrolysis in the cis ring is required to form a GroEL-ADP-GroES complex with decreased stability. Finally, binding of ATP to the opposite trans ring of GroEL results in disassembly of the cis-ternary complex, which opens the cage and allows release of the folded protein. Proteins released in non-native form may be rapidly rebound by another GroEL complex until all of the initially bound polypeptide reaches native form. Can rescue kinetically trapped intermediates. GroEL shows ATPase activity. ATP hydrolysis moves the reaction cycle forward but is not required for substrate folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:20094032, ECO:0000269|PubMed:22380631}. Note=Uniformly located in the cytoplasm (PubMed:20094032). Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase (PubMed:22380631); polar localization depends on the minCDE operon. Foci form near midcell (Probable). {ECO:0000269|PubMed:20094032, ECO:0000269|PubMed:22380631, ECO:0000305}.
Interaction partners:
- Chaperone protein DnaK
- Protein GrpE
- Co-chaperonin GroES
- Chaperone protein HtpG
- Chaperone protein DnaJ
- Chaperone protein ClpB
- ATP-dependent protease ATPase subunit HslU
- RNA polymerase sigma factor RpoH
- ATP-dependent Clp protease proteolytic subunit
- Trigger factor
Sequence:
MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGGMGGMGGMM
Protein: C3H1-type domain-containing protein (Q580V0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGRGKGRGKNIDITKSFFQQAGSLGRVSVQLSPTRVISVGEDEISPTNGSRAALQLWRDDGTEVALKLCQNWRQGTCNSQGACSNAHVLAYHSQMPMPNMVGVMNAFTPIPMPSTGPRDNSEKSVSPKCLHRPQLPHQQPQGAVVDPGRAAEHKVNSNTTNTTSHGTLIPAPRSQQNNRQLYAANNSSAPSGVRATNTTWGREALGPENHYGSQQQTHNPQPQPQHQPQQQQQQQQQQQQQQQQLATQPRGAWNVLQPNDDGRRQAAGVVLSAAYLDKLNQRPKDKCELVKQKAANSQNSSSFSGNNSLNRGSAPRHQPSRSPTGPRREDTWASVAALNHSNGASVIWGDGGVQMWDLMLNNTAASPTPSQTSGVNQPALGRDLNSAALRPNSGQLWSSLASNGRQRSVNNNAVPSATINNNNNSSINSGGFISVNTSPNIGNNNSPQQCSSNNGNGGITGGSRTSSATASSEALKNQLLRALVGGGAEADELTSPPPPPPLPRAEVAHSRVSSGIVSINTGAPSVGCAAEGMKSGVLLSLLGNDGDGGVMHGMMPPQPPPLQDGTHKIQHLMALLTTE
Protein: High mobility group protein HMGI-C (High mobility group AT-hook protein 2) (P52927)
Organism: Mus musculus (Mouse)
Function: Functions as a transcriptional regulator. Functions in cell cycle regulation through CCNA2. Plays an important role in chromosome condensation during the meiotic G2/M transition of spermatocytes. Plays a role in postnatal myogenesis, is involved in satellite cell activation. Positively regulates IGF2 expression through PLAG1 and in a PLAG1-independent manner (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:14668482}.
Interaction partners:
- Insulin-like growth factor 2 mRNA-binding protein 2
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 2
- Cellular tumor antigen p53
- High mobility group protein HMG-I/HMG-Y
- Mothers against decapentaplegic homolog 4
- SNW domain-containing protein 1
- Protein lin-28 homolog B
- Mothers against decapentaplegic homolog 1
- Insulin-like growth factor 2 mRNA-binding protein 3
Sequence:
MSARGEGAGQPSTSAQGQPAAPVPQKRGRGRPRKQQQEPTCEPSPKRPRGRPKGSKNKSPSKAAQKKAETIGEKRPRGRPRKWPQQVVQKKPAQETEETSSQESAEED
Protein: Hepatitis A virus cellular receptor 1 (Hepatitis A virus cellular receptor 1 isoform X1) (A0A2R8QGQ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTDLHSWFLSSWILCCLTICRCSDIIVQSFEGDNVTLPCKYDSRYHGKCEICWMRGDIPSRGCGEEIIASDGDKVSTRNSDRYDLAGPIQHGDVSLTIFNIDKTDSGKYGCRVHVPGWFNDEKYYVHLIVDDAIIPTTLETTSMSSSTSEHETTGVYTTAMTEAPATTPPDPLVTTISGLLTPESQTTETSGDNKTRKEISSTISPSYAPRSSTAGMWLSNTTSVEPSVSVVYHESSSAESKDNVTVSAVLVPVLLLLLALIAIAAAFMWKQKKKTRASLEVRQNSEISVIYSNSGSSVGLYNREMAVENVYQIQAESEYEQWH
Protein: Protein SBE22 (P38814)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With SBE2, is involved in cell wall integrity and polarity processes like bud growth, through the transport of CHS3 and UTR2 to sites of growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Golgi apparatus {ECO:0000250}.
Interaction partners:
- Uncharacterized protein YFR012W-A
- Protein DCV1
- Uncharacterized protein YGR146C-A
Sequence:
MTSIQERGTSAHLHSLKEGEASDRSSEMLPKQRSIIGSHVQRPPSQTTLGRSRAGSNTMNKVSGLDIARRPSENLLSNMNCSDNGNGGNMLNSFVNSALPPPKVNPAQTRRERPASNSSIGTKTTEVFSSTSASSSLGDTSDEGEGSDADKSKINTFPSILMEKATQGRGADGNGMRSASNNTIVEATTDGSKMALQKSMSFDDTAAEKTMNKSRHSYQEQFSSKKSQSSLLNSKQRSRAKSQTCSSTGYNNSSILKTFGISSKISNSSDRIEASSLEFNVPSQKPLNCKPLTPSQKYRLRKEQSEMNLRNTIKRKEKFYDSQEQILELQEGDVDDSLIWNVPMASLSTNSFLASAKPDDMNNLAGKNDLSEYTGGLVNDNSEISYTKQNHRYSNISFASTTSNASLLDFNEMPTSPIPGLNKVTDFQFIQDTTKSLASVYLHSSNRLSRSKLSERTKSSDFLPIELKEAQNQGMEDLILVSENKLDVVSHSRPSWLPPKDRQEKKLHERQINKSMSVASLDQLGKNKDREEKLIRDETNRQKYVLLLDRDITRNSSLQSLSKMVWDTPFSDETRSTIYSEILQSKTRFITKNYIQPFHELQELLTKMGDFPKNKEIEISQLIETSLRRKVSGLHDICPDLMLLLKIKSISSQGIVTGDELLFHHFLVSESFQNLGLNEIWNIVNLVQMTCFNDLCKEKFDAKVLERKGVVAGYLSQNEEFKDEFNTECINSTTWWNILERIDHKLFMWIMDIIVVNNSQSYKNSPINEDEFVNKDWEYYRSKKVVINYKILISFALNVLLNYHFGFTDLRSLCNVNDQRFCIPVFINDEFVDADTVNAVFIKKWAHYYKKF
Protein: Transcription activator GAGA (Adh transcription factor 2) (GAGA factor) (GAF) (Neural conserved at 70F) (Trithorax-like protein) (Q08605)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional activator that functions by regulating chromatin structure. Overcomes the repressive effects of chromatin by promoting the open chromatin conformation in promoter gene regions, thereby allowing access to other transcription factors. Binds to DNA Polycomb response elements (PREs) at the bithorax complex and to the proximal region of the engrailed promoter, and positively regulates transcription of many genes including homeotic ones. Binds to the DNA sequence (GA)n, with optimal binding to the pentamer 5'-GAGAG-3'. Binds DNA as an oligomer. May also act as a transcriptional repressor, maintaining the repressed state of genes including lolal, and down-regulating its own transcription. Required for dosage compensation in males and may be involved in oogenesis. Also has a role in nuclear division.
Subcellular location: Nucleus {ECO:0000269|PubMed:33720012, ECO:0000269|PubMed:7504178, ECO:0000269|PubMed:9241251}. Chromosome {ECO:0000269|PubMed:33720012, ECO:0000269|PubMed:8107823}.
Interaction partners:
- Modifier of mdg4
- Boundary element associated factor
- Protein tramtrack, alpha isoform
- Centrosome-associated zinc finger protein Cp190
- Zinc finger protein su
- Polycomb group protein Pc
- CTCF
- Nucleosome-remodeling factor subunit NURF301
- Deformed wings
- Pipsqueak, isoform M
Sequence:
MSLPMNSLYSLTWGDYGTSLVSAIQLLRCHGDLVDCTLAAGGRSFPAHKIVLCAASPFLLDLLKNTPCKHPVVMLAGVNANDLEALLEFVYRGEVSVDHAQLPSLLQAAQCLNIQGLAPQTVTKDDYTTHSIQLQHMIPQHHDQDQLIATIATAPQQTVHAQVVEDIHHQGQILQATTQTNAAGQQQTIVTTDAAKHDQAVIQAFLPARKRKPRVKKMSPTAPKISKVEGMDTIMGTPTSSHGSGSVQQVLGENGAEGQLLSSTPIIKSEGQKVETIVTMDPNNMIPVTSANAATGEITPAQGATGSSGGNTSGVLSTPKAKRAKHPPGTEKPRSRSQSEQPATCPICYAVIRQSRNLRRHLELRHFAKPGVKKEKKTTSGKKSSSGSSGSGSGALSSSGSVPQVQTVQSLHTLQGVQVKKDPDAQQQQQQQQQQQQQQQQAMTVSGATGGQVQQQVQQVQQQVQQQQQQQQQQQQQLQHHQIIDSSGNITTATTSAQAAAAAQQQAAGQQQQLVAQSDGSESGAPLSIAQVQTLQGHQIIGNLNQVNMTDFQQQQPQQQQQQQQQQQQQQQQQQQTQQTL
Protein: Glutathione S-transferase omega-like 2 (EC 2.5.1.18) (Extracellular mutant protein 4) (Glutathione-dependent dehydroascorbate reductase) (EC 1.8.5.1) (P36156)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB). May be involved in cell wall organization and biogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16936141}.
Interaction partners:
- Ubiquitin-activating enzyme E1 1
- Glutathione S-transferase 2
- Glutathione S-transferase 1
- Glutaredoxin-2
Sequence:
MSKQWASGTNGAFKRQVSSFRETISKQHPIYKPAKGRYWLYVSLACPWAHRTLITRALKGLTSVIGCSVVHWHLDEKGWRFLDMEKQLEDSEDFLEHWHDVAGGIRTAKEDSSKSFAEIKNDSQRFMVDATNEPHYGYKRISDLYYKSDPQYSARFTVPVLWDLETQTIVNNESSEIIRILNSSAFDEFVDDDHKKTDLVPAQLKTQIDDFNSWVYDSINNGVYKTGFAEKAEVYESEVNNVFEHLDKVEKILSDKYSKLKAKYGEEDRQKILGEFFTVGDQLTEADIRLYTTVIRFDPVYVQHFKCNFTSIRAGYPFIHLWVRNLYWNYDAFRYTTDFDHIKLHYTRSHTRINPLGITPLGPKPDIRPL
Protein: Large ribosomal subunit protein bL32m (39S ribosomal protein L32, mitochondrial) (L32mt) (MRP-L32) (Heart-expressed gene 1 protein) (Q9DCI9)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BYC8}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein bL36m
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS16m
Sequence:
MAPSLLLLSLPWPVRPGPLQRCWELLQRQLQQSWSRFVSPPWAPALAVQRPSILTELAHDTCENKENSSFLDSIFWMAAPKNRRTIEVNRCRRRNPQKLIKIKNNIDICPECGHLKQKHVLCGYCYEKVRQETTKIRQQIGAQEGGPFRAPSVETMVLYTGEKPSEKDQGKRIVERNIKRPSWFTQN
Protein: 5-hydroxytryptamine receptor 5B (5-HT-5B) (5-HT5B) (Serotonin receptor 5B) (P31387)
Organism: Mus musculus (Mouse)
Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins. Probably involved in anxiety and depression.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P47898}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 5A
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
Sequence:
MEVSNLSGATPGLAFPPGPESCSDSPSSGRSMGSTPGGLILPGREPPFSAFTVLVVTLLVLLIAATFLWNLLVLVTILRVRAFHRVPHNLVASTAVSDVLVAVLVMPLSLVSELSAGRRWQLGRSLCHVWISFDVLCCTASIWNVAAIALDRYWTITRHLQYTLRTRSRASALMIAITWALSALIALAPLLFGWGEAYDARLQRCQVSQEPSYAVFSTCGAFYLPLAVVLFVYWKIYKAAKFRFGRRRRAVVPLPATTQAKEAPPESEMVFTARRRATVTFQTSGDSWREQKEKRAAMMVGILIGVFVLCWIPFFLTELISPLCACSLPPIWKSIFLWLGYSNSFFNPLIYTAFNKNYNNAFKSLFTKQR
Protein: Syntaxin binding protein 3 (A0A8I6AMM9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAPPVTERGLKSVVWRKIKTTVFDDCRKEGEWKIMLLDDFTTRLLSSCCKMTDLLEEGVTVIENIYKNREPVRQMKALYFISPTPKSSHCSTESFHACSDDFCPDSLFNKIKASCSKSIRRCKEINISFIPHESQVYTLDVPDAFYYCYSPDPSNAGRKEAVMEAMAEQIVTVCATLDENPGVRYKSKPLDNASKLAQLVEKKLEDYYKIDENGLIKGKTQSQLLIIDRGFDPVSTVLHELTFQAMAYDLLPIEKDTYKYKTDGKEKEAVLEEDDDLWVRVRHRHIAVVLEEIPKLMKEISSTKKATEGKTSLSALTQLMKKMPHFRKQISKQVVHLNLAEDCMNKFKLNIEKLCKTEQDLALGTDAEGQRVKDSMLVLLPVLLNKNHDNCDKIRAVLLYIFGVNGTTEENLDRLIHNVKIEDDSDMIRNWSHLGVPIVPPSQQAKPPRKDRSAEETFQLSRWTPFIKDIMEDAIDNRLDSKEWPYCSRCPAVWNGSGAVSARQKPRTNYLELDRKNGSRLIIFVIGGITYSEMRCAYEVSQAHKSCEVIIGSTHILTPRKLLDDIKMLNKSKDKVSFLKDE
Protein: Copper transport protein (Q8T8R3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU367022}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367022}.
Interaction partners:
Sequence:
MDHHGVDASEGHVHHHEGHHSPEMTHHGNHGEHTKHGHHEGGAHDMSMAMFFHTGDSETILFKFWRTESAMALTLSCLLIFMVAVLYEALKFFREWLFSWDRKRLEGGRDQYNRPRRYREANYNYNQPTYPPRTNQQSGTQHTHHHVQENTPPAGRTTKLKVFCSGMHILQTFLHVLQVLISFLLMLVFMTFNVWLCVAVLLGAGVGYYIFCAFRTNVQEHCN
Protein: Glutathione-independent glyoxalase DJR-1.1 (EC 4.2.1.130) (Protein DJ-1 homolog 1) (P90994)
Organism: Caenorhabditis elegans
Function: Catalyzes the conversion of methylglyoxal (MG) or glyoxal (GO) to D-lactate or glycolic acid respectively in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against glyoxal-induced cell death.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22523093}. Nucleus {ECO:0000269|PubMed:22523093}. Note=Ubiquitously localized throughout the whole cells with higher expression in the nucleus. {ECO:0000269|PubMed:22523093}.
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Serine/threonine-protein kinase pink-1, mitochondrial
- Glyoxalase 1
- Leucine-rich repeat serine/threonine-protein kinase 1
- Probable cation-transporting ATPase catp-6
- Superoxide dismutase 2, mitochondrial
- Superoxide dismutase 1, mitochondrial
- Superoxide dismutase
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- FMN hydroxy acid dehydrogenase domain-containing protein
Sequence:
MAQKSALIILAAEGAEEMEVIITGDVLARGEIRVVYAGLDGAEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLAESLLVRDVLKSQVESGGLIGAICAAPIALLSHGVKAELVTSHPSVKEKLEKGGYKYSEDRVVVSGKIITSRGPGTAFEFALKIVELLEGKDKATSLIAPMLLKL
Protein: Inwardly rectifying potassium channel 2, isoform D (A0A0B4LHI9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
- ATP-binding cassette sub-family C member Sur
- KCNQ potassium channel, isoform F
Sequence:
MRFNFSTHSAAPTSTTIPTTTQANGGEQATQPLKKAIEADPDSLDSVISNPQSYPITIVPNRPTSYYGLSQNGKPFPRQPSCRSRNFRPGSMRRVRRRAVFKNGDCNVVQKHLQRRRVRFLQDMYTTMVDWQWRWTLLAFALSFILSWLFFALIWWLIIYTHGDLEEPHLPENQEESGWAPCVSAIDGFTSCFLFSIETQHTIGYGVRTTSPECPEAIFMMCFQSIYGVMSSAFMAGIVFAKMTRAKQRAQTLLFSKHAVICQRDGTLSLMFRVGDMRKSHIIGAGVRAQLIRTKSTKEGEVMTQYFTELEIGTDDSGSDLFFIWPMVIEHKIDENSPLYNLNATDMLQDKFEIVVILEGTVESTGQSTQARSSYINTEILWGHRFDPVVLYNKDLQAYEIDYARFNETTQVDTPLCSARELNEIYKIQEGFRTPAETTFTMRQLSHNHSDQAS
Protein: Calcium/potassium channel (CAKC), putative (Q38F65)
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:
MSKSRAVVKFGGDQSKERVSFRNFFDVLNQRHSNVSVSGLAVTLLFELLSISIYVEASFYAHPTSIYDFNWKTGRFITVAIINAIFFSEWIVMLWVEEQKVRYCLSLLSIVNALTCLPMVIVGIGAIVKPTWQSVWVPLFLRVWWLRKCILVLLDYPQVAKWMMDIRRDICRFLITMLAVLSTCVGIQQFVETLAGNYMDPFSSLYCMVTTFGTIGYGDVSPQTAPGRFLMIGFLVVALSYFLPLFQRLAQIGRDHLNYNECHSCWGRRPHVIFSGIFTGLGAEIILMNFYAGWRKYLGVRVVLLSPVDFPPEVRLLADIPWLRNRVVLMIGDSAKQVDLIRADAANAEAIFLFGDTGSAAYHADYQVIQQSLAIRQFDPELPQHLYLRSERHTRHVASYAASVVEVERLLHHLLGLGAAVPGAVPLIMNLLRTYEPLKVKGTASRPWIEEYEWSLQNDIHCLEMQQTFRGYSFHSLARLLLQHNVTPIGIIDENGEVQLNPHRISSSAVKLVVVAKALRSARSALEAAEEAHSQTSFGEHTGEVEGKEPCIYGMDREAAAGAYYTSDFPGREAKSGVEALQLVDDAYDFENHFVVIDLSMAKAKAPETEGAREGSLSSAAMDVFHVMRSIRQSYPQNDIVLLTKDTSFSAYFGRYWNSVPGAIPVKYIDGCGLNANDLRRCNLKRSAGIIIFFSGDIGGASTGGLSLLVFLSVASILPSSHNIPVVVELDSTQYLSLFPPYADDPYLCSRAESDFVFEPNYVIGNALSRHMFFPSVHRTYFMDEFVDIIDMMVSGVDERTPSLGRLPLLFTTDSLHIYQDVVEYCLKLCYLPIGLHRCISDPETPYINGQRFVLTNPPGDLIVDQKCDAVFYLLPAS
Protein: Histone deacetylase (EC 3.5.1.98) (M9NEF2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
Sequence:
MSSPDDRIPIHDLPSEAGSDERLLHITPATLTLDFKPHPAVDIDQQIMELKKSQELQKQRLINSFQEQSKQMELEHKLQLEHKYQELRNESMVTAAAAAVAQEQHRQQLHQQQQQHQQQQQQQQHQQQQQQQQARGRDGMKLKQNCSANASPEVKQILNCFILSRKSQAAASNGTTTTSPYRNRGVVKSSSGESLPAGTVTSAHPYKIPQPPPSLLKYESDFPLRKTASEPNLLKIRLKQSVIERKARIGGPAGARRHERLLQAAQRRQQKNSVLTNCNSTPDSGPNSPPSAAALAVGVVGSRGSPTSAPIQEENEEGSQYQPGQRSSINDLPLFSSPSLPNISLGRPHLPNSAQAHAQVNAQVAAQAQAQAQAQAQAHAMFAALAAAQGGCGQPGYYNPLGMAFVGRQPAPLAMIPATGIAPQQPSPVVRSASATSTSSSQASLVGDVAPPQAHAASTILPSSSSYMQQLGSVAGSGVNLHAAAVAAAAAAAAAAGSLPPTNSHGHGHGSHAHPHPHAHGHGHGHGHGIYAGHQHNVPITDAQVAQVHLHKQGHRPLGRTQSAPLPLGHPMLTGAVQLNVVQTHYENSEAERQAYEHQVVNQKVRQTVLTRSGAAAAAAAAAGVSVVREAQLKEEDDDSAAEVMDLTDKKKPPKTVLTSTIATSTSQNLPEALAAAAAAAAYRAPHNASSNSASATKSGIKLRDQEYLQQQREQLLLLQQEEELAKSLMRPLSRTLSSPLVPLGPHGLSQIPDTGQQPAPIATSSSADHIPPVNLSLPHRQHRQLMSTLYASQLRNHQPSASGSPPHKVTTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQCQLSRPKLENTLSASFVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRMPEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLGFNVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGKVVLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHWPCVRMLEHTVGLSALETLKVEHDESETINAMAGLSMQSMHRTLSRDDSEEPMDQDETK
Protein: HTH-type transcriptional repressor AllR (Negative regulator of allantoin and glyoxylate utilization operons) (Q9HZ60)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Formimidoylglutamase
- Probable transcriptional regulator
- Probable transcriptional regulator
- Transcriptional regulator PcaR
Sequence:
MSKHSPTDRLLQILIALGQAPEALSAKELSLTLGQPLSSTYRHLKTLLRWGLAEEQAGQGRYLPGPACLQLAKKFDREASLIGLAKPELKRLADLSQESVALMVASNQQAICLELFDSPQPLRCCYQKGLAQPLLHGASAKALLAHLEDERREELYLAQELSAERIDKLEQELRLIREQGYAVSQGEIDEGVWGISVPLLDSRQRLHGALSLMAPALRAQSRSECLRQWTLDAAARLSARLD
Protein: Ferric/cupric reductase transmembrane component B (EC 1.-.-.-) (Ferric reductase B) (Ferrireductase B) (Ferric-chelate reductase B) (Metalloreductase freB) (Q4WR75)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Ferric reductase involved in adaptation to iron starvation and which is most likely part of the reductive iron assimilatory system (RIA), a siderophore-independent high affinity iron uptake mechanism.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P36033}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Iron transport multicopper oxidase fetC
Sequence:
MLLVSCLIILLHLQNALSQIIPPNERCVTAVYTAYEYLSFSGQPNKGLWAPRCRNRLHVLSIYAASDLYCSDAEREAGFAQLDDQCRQYAGVDLIPRQEFAPNLTHEAISQMRVVEFGELPKKGPLDTPILISKSYYSRVFRTIDAWQFELWSHYAFGYLGYAYWTVVIAAGALHKLVLHAISVKRAPSLPPFPFLLLIYYWIQTNLIIPAPLASSRRRLLWWTFPGRIHAIVVLLFWILSIVLCLIGYRTFSDNIYWPDISAQLLRYVADRTGILSFANVPLLWLFAGRNNIFIWATGWSYSTFNIFHRHVAWIATLQAVVHTILYTVLFIQSGNAWKKMQKPYLLWGTLAMLAMILVFPFAVDWFRRRTYETFLVLHILFSVVALVGCFYHVIIFEDHEYWFYLWPAVVIWVSDRVLRLIRIVYCNLHVQLGSRSRFQCTECVAAYDKDADIIHLELTPGSGLQPAPGQYYFLYQPFRLTGWESHPFTLGYWSYNDGAPSTQCRSLKRDTTTDVSEIPLLPDTPSSGSDYGSIDTSTDPPERKLALRFWIRPYDGWTRHLRDQCLQSPTRIIQPNILLEGPYGEQCPLWKYESVLLIAGGTGIAAAVPYIQDHILRSSTGQTSTQSIHLVWTARQPALLRDIAGRELKQALSRKDFRVSFYVTSESASQGAIMDGVEFACGRPDLQAIITAHAEEARLGSSSVLVLVCGPSGMAGLARAAVHQAMRWGCRSLRYVEESFDW
Protein: DNA/RNA-binding protein Alba-like domain-containing protein (Q385X2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA/RNA-binding protein Alba-like domain-containing protein
- DNA/RNA-binding protein Alba-like domain-containing protein
Sequence:
MSEKGGDDSRSSQVRVSVKRRNFSYVDSIKVRLSGGKPEVTISALGKAISDAVAVAEILKNQGLIDVKKITTSRGAAESDGDAVNDKIEILITKSKDFDTIYAEQQKRKLENADKKE
Protein: Interferon C (C1IRY5)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MPCQLQGQLVRITHNLLRDMGGNFPLERLQENVFMAFPATAFASSGAPQLGSSGAKAIYETLKNIDILFEADDPPTQWDQQKLENFQNIVYRQIEESKCMMGSVDTSDYLIRTEGLNTYFGNIAAVLKEKNFSYC
Protein: protein-disulfide reductase (EC 1.8.1.8) (Q9ZR86)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MAEAAPAAGGGIGDILATSDRDFLVRNSGEQVKISSVEASPVAIYFSASWCPPCRRFTPKLIEVYEKLASQGKSFEVVFASADRNEEAFNEYFAKMPWLAVPFSDSEGREALDGQFKVSGIPHLVILDAKTGEVYTEDGVEFVSEYGVEAYPFTPDRINELKEQEKAEKENQTIQSVLVTSTRDYLISNKGDKVPISELEGKYVGLCFVVDGFPPLAEFTEVLAKIYEKLKEVGEKFEVVAVSLDSEESSFNESFAKMPWLAIPQGDIKCQTLVRYFELSSLPTLVLIGPDGKTLNNNVADIIDDHGFEAWEGFPFSAEKLEILAEKAKIKAASQTLESILISGHLDFVIGKDGAKVPVSELVGKTVLVYFSGKWCPPCRAFLPTLVKEYNKIKEKNSDFEIVFISSDEDQSSFDDFFSEMPWLAVPWEDERKASLKKTFKIRGIPSLVAIGPTGQTVSRDAKSQLMIHGADAFPFTEERLEELQKKLDEMAKGWPQKLKHELHDEHELVLLRRGTYRCDGCNEMGSSWSYRCDECDFDLHPKCALGEEKMGEEAPAGYVCEGGVCRKA
Protein: At1g17080/F6I1.24 (F20D23.22 protein) (F6I1.24/F6I1.24) (Ribosomal protein L18ae family) (Q9SHG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein eL29y
- Large ribosomal subunit protein eL36y
- Large ribosomal subunit protein eL8y
- Small ribosomal subunit protein eS25x
- Small ribosomal subunit protein uS10y
- Large ribosomal subunit protein uL1x
- Large ribosomal subunit protein uL22z
- Large ribosomal subunit protein eL31z
- Large ribosomal subunit protein eL19z
- Large ribosomal subunit protein uL2my, C-terminal part
Sequence:
MGHGEEDKSKGFASEEGNQHHQYGTFQGVSNYPPPQNSAPVTGFPQPSAPPGVYDSGAPYYAHGYQTVPVHGGVAEGRPVRQRRLPCCGIGLGWFLFIVGFFLGAIPWYVGLFIMMFGRRIDYREKPGYIACTIAAILATIAVILGVSKGADDW
Protein: Elongation factor Ts, mitochondrial (EF-Ts) (EF-TsMt) (P43896)
Organism: Bos taurus (Bovine)
Function: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Subcellular location: Mitochondrion.
Interaction partners:
- Elongation factor Tu, mitochondrial
- Ribosome-recycling factor, mitochondrial
- Protein RRP5 homolog
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL9m
Sequence:
MSLLRSLRLCLVARTGSCPLSALGPGPLLPSLQAGLPLLQSPQQWHTFHSGSWLSSASSKELLMKLRRKTGYSFINCKKALETCGGDLKQAESWLHKQAQKEGWSKAARLHGRKTKEGLIGLLQEGDTTVLVEVNCETDFVSRNLKFQQLVQQVALGTLLHCQNLKDQLSTYSKGFLNSSELSELPAGPEREGSLKDQLALAIGKLGENMILKRAAWVKVPAGFYVGSYVHGAMHSPSLHNLVLGKYGALVICETSELKANLADLGRRLGQHVVGMAPLSVGSLDDEPGGEAETKMLSQPYLLDPSITLGQYVQPHGVSVVDFVRFECGEGEDAADAE