wanglab/gogpt-training-data huggingface dataset:
Protein: Beta-toxin Ct7 (P0DUH9)
Organism: Centruroides tecomanus (Scorpion) (Centruroides limpidus tecomanus)
Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). Is possibly toxic to mice, freshwater shrimp and crickets.
Subcellular location: Secreted {ECO:0000269|PubMed:23840487}.
Interaction partners:
Sequence:
MKVLILIIASVLLIGVECKDGYPMNSEGCKISCVIGNTFCDTECKMLKASSGYCWTLGLACYCEGLPENVEVWDSATNKCGGK
Protein: NHL domain-containing protein (Q9ZNQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKANMSSSSSTRYRSFFVFPILFAVLFLGLLIPSSADNRHVINFRSPGLYPEGLTWDPRDQHFLVGSLHSRTIHSVSDAGVIETLISDLDLPENSTILGLAVDSTNRRLLACIQSLPPLPPFSALASYDLRSGGRRVFLSPLPSLPGDDEDIARDVANDVAVDFKGNAYVTNSAKNFIWKVDRDGAASIFSKSPLFNSQPVAADADASFRDCGLNGIVYISKGYLLVVQSNTGKVFKVDEDSGNARLVLLNGDLIAADGMTRRRRDGTVMVVSQKKLWLLKSQDSWSEGVVYDEIDLDIEGFPTAVTVAGRDRIYVLYGRVMEGIMGSSYKEEGAREWFGIEEVWSEKEGGEDKIWLYVLIGFGFAYFCFWRFQMKKLITNMDKKIT
Protein: Small ribosomal subunit protein mS29 (37S ribosomal protein S23, mitochondrial) (O59677)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for maintenance of mitochondrial DNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein mS35
Sequence:
MLPKFRSRSSIIKNTERISNILSGGKLTVCGSKLGGLYTFEKCTFNKYYSSSQYQHTGRPVGGNIHSSSNQQRQKNSEAPRINEIPPSTSSVEKSTTIPNSSVVLDHLLNEGENTLEEVKPSEIHPHMSWSSKSEGKMFKIPEELLNKLNGFGALEKQKKSFSFFTSASLLHRKITTELVNVLQRSKDQGTKDGRFLLDGAPGSGRSIALIQAELFALSQPNFIVLPVHNCEGWVNSTSSYGYDEQLKLWVQPDLIKGFLTSVMKTNSDKLKKLKTFESHELLQNECIPAGTDLLSFLHKLIASSNAPKSLEIFLQELNNNTKSNSNMKVLLVIDNISILSVVTKYKDKKNNFLPPKDFYFINLLFKYISGSLTFNRGTVLAATSSQPRVSTPSLDIALGVAHRNPYKSSDETILDSLQSVHILNMEPYTLDESRRMMEYLVSSNVCLEKVDNYLQNHVLSGGNPRKFFDACTRLA
Protein: Multifunctional protein pyr1-3 [Includes: Glutamine-dependent carbamoyl-phosphate synthase (EC 6.3.5.5); Glutamine amidotransferase (GATase) (GLNase) (EC 3.5.1.2); Ammonium-dependent carbamoyl phosphate synthase (CPS) (CPSase) (EC 6.3.4.16); Aspartate carbamoyltransferase (EC 2.1.3.2); Dihydroorotase (EC 3.5.2.3)] (P20054)
Organism: Dictyostelium discoideum (Social amoeba)
Function: This protein is a 'fusion' protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
Subcellular location: Cytoplasm.
Interaction partners:
- Bifunctional protein argC
- Dihydroorotate dehydrogenase
- Amidophosphoribosyltransferase
- Uridine 5'-monophosphate synthase
- Protein transport protein got1 homolog
- Adenylosuccinate synthetase
- asparaginase
- Bifunctional purine biosynthetic protein purD
- Type-1 glutamine synthetase 1
- Type-3 glutamine synthetase
Sequence:
MDILNRKKGCLVLEDGTKLSGYSFGSERSVAGECVFSTGMVGYNESISDPSYTGQILVFSFPLIGNYGVPSFRERDPESGLAVNFESDKAHVQAIICSEYCDEYSHWAAEKSLSEWLKESNIPGLYGIDTRALITKIREKGSLKGKVIIGDFDESKLEFEDINLRNLVAEVSTKEIKEYKAAENNKKTGEKRKNKKVIVLDCGIKNNQIRCLLNRGVDLKVVPWDYDVVANESINDYDGVFISNGPGDPSLCGKAIENIRKVLALPVAKAVFGVCMGNQLLGLAAGAQTHKMAFGNRGLNQPCVDQISGRCHITSQNHGFVIDSNSLPAGSGWKTYFINANDASNEGIYHESKPWFSVQFHPEAMAGPTDTEYLFDNFVDNVCGEQQHKSPMNKSKIIDCPKGINKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEGIKTILINPNIATVQTSPGLADKVYFLPVNASSVQKVIENENPDGILVTFGGQTALNCGIELYKSGILEKYNCKVLGTPIETIIATEDRGIFAEKLSEINERIAPSMACNSLEESLIEAEKIGYPVIVRAAYCLGGLGSGFADNKEQLTALVTEAMATSSQVLVEKSLKGWKEIEYEVLRDSKDNCITVCNMENFDPLGIHTGESIVVAPSQTLSDREYQMLRETAIKTVRHLGVIGECNIQYSLNPYSEEYCIIEVNARLSRSSALASKATGYPLAFISAKVALGYDLAALRNTITKKTTACFEPSLDYLVVKMPRWDLKKFTRVSNKISSSMKSVGEVMSIGRKFEEAIQKAIRMVMDGAVEGFQAGVFPTSDEELEHPTNNRILVLASAFKDGYSIDRVHQLTKIDKWFLTKLKAIIDLENHLSTYKEPSQIPSEILKFSKQQGFSDKQIARAVGTTELNVRDYRKKMGIIPCTKHIDTVAAEFPAQNNYLYMTYNGETNDVNINEKSYITLGSGSYRIGSSVEFDWCAVSCIRTLRSLGLKSIMINFNPETVSTDYDECDYLYFEELSLERVLDIYERGGPNSNHGVILSVGGQIPNNLAIPLSRCNVKVLGTHPDMIDSAENRYKFSRLLDTIGIDQPLWKELTSVSDTKDFCESVGFPCLVRPSYVLSGAAMNVVHSSQDLETFLTEAAAVSRDHPVVISKFIQEAKEIEIDAVADNGRIVLFAISEHVENAGVHSGDATIVCPAQDLDDATILKVEETARKIAEALNVSGPFNIQFIAKNNEIKVIECNLRCSRSFPFVSKTLNINFIELATKIIIKHQYDLPVVNPINYVGVKVPQFSFIRLKGADPVLGVEMASTGEVACFGNTREEAYVKGLISTGFKAPEKNVLLSIGSFKEKHEFLPSAHKLIKLGYTLFGTQGTADFYSENGVPVTQLNWDEEDLGENVIQKKMTENTIHLFINLPSKNKYRRPSSFMSRGYSLRRVAIDFQVPLITNIKCAKLFVDSLSYMKGPMPIENVDWRTSNKIIRLPGLVDVHVHLREPGATHKEDWDSGTATALAGGFTMVGAMPNTNPAIMDDASFELCKSLAASKARCDYGIFIGATFTNTTTAGKFASDAMGMKMYLEETFAPLPLKDDINVWRDHIMNWPGTTPICVHADGRNLAAILLLGWMYDKHMHVCHVSHKEEIDIIRDAKKRGMKLSCEVSPHHLTLCDKDIPRIGAGQSEVRPKLGTEEDLNALWDNIDYIDMIATDHAPHTWEEKCSAKPPPGFPGLETSLPLMLTAVHNGRITIEDLVMKMHTNPIRIFNLPEQPDTYIEVDMEQEWTIPKKPLYSRCGWTPFEGLQVRGKVVKVVLRGQIAFIDGKIIAQKGFGLNLRSKEYQVEKERLLNTTKPIYDKIPTVQSTKNQTTNITSPSLISDSPNKAINKIKSTSTSTTPNTQEQSTQHLPLVGSNLASAVLNKKEDTLQTAFNISDNSLAGKHIFSVKQFNRKQLHALFGIAHEMRILVKRSGGSDLLKGKVLATLFYEPSTRTQCSFTAAMQRLGGSVVTVDNVSSSVAKGESIADTIQTLESYCDAVCMRHPAVGSVESAIQVAKKPIINAGDGVGEHPTQALLDVFTIREELGTVNGLTITVVGDLKHGRTVHSLVRLLANYQVKINYVSPSSLSMPTEIIKELNEKGIEQKEYTNIESILPTTNVLYVTRVQKERFQSIEEYEKVKDSFIITPHTLTKASDNMIVMHPLPRINEISPEVDSDPRAAYFRQMENGLYVRMSLLALVFGAGV
Protein: Protein INCA1 (Inhibitor of CDK interacting with cyclin A1) (Q0VD86)
Organism: Homo sapiens (Human)
Function: Binds to CDK2-bound cyclins and inhibits the kinase activity of CDK2; binding to cyclins is critical for its function as CDK inhibitor. Inhibits cell growth and cell proliferation and may play a role in cell cycle control (By similarity). Required for ING5-mediated regulation of S-phase progression, enhancement of Fas-induced apoptosis and inhibition of cell growth (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15159402, ECO:0000269|PubMed:18756329}. Cytoplasm {ECO:0000269|PubMed:18756329}.
Interaction partners:
- Cyclin-A1
Sequence:
MQVQDDGVNLIPFAKCSRVVSRSPPPRLPSQSLRPMPQRYGDVFWKNLNQRPTPTWLEEQHIPPMLRATGCSQLGLYPPEQLPPPEMLWRRKKRRPCLEGMQQQGLGGVPARVRAVTYHLEDLRRRQSIINELKKAQWGSSGAASEPVVLGEEGCGFPSTNEYPDLEEERATYPQEEDRFLTPGRAQLLWSPWSPLDQEEACASRQLHSLASFSTVTARRNPLHNPWGMELAASEE
Protein: Large ribosomal subunit protein mL65 (28S ribosomal protein S30, mitochondrial) (MRP-S30) (S30mt) (Q9D0G0)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein mS31
Sequence:
MAAARYWKLVPRGRGLSQNAAAKASATAPEVRDLEVVATPVARYPPIVASMTADSKAARQRRVQRWQATVHAAPSVDEKIRILTKMQFKKYVVHPQISALNADRWYQSFTKTVFVSGLPPAPALSPPPPSLDLAALRAAVCDCILQEQVYVRRRRPRSLFDRRQALASSILDQVVRTLVNLLAPLNPVLSTAALDCKRSVDFYWLRGEERIPAGHRKGHIDALRYQINDKPHNQIRISKQLPEFVPLDYSIPTEIPVMKCKPDKLPLFRRQYENSIFTGSKTADPCCYGHTQFHLIPDRLKRERLIRQNQAEQVEAVFRANAIASLFAWTGAQAMYQGFWSEADVTRPFVSQAVITDGKYFSFFCYQLNTLALTVQADQNNPRKNLCWGSQSQPLYETVEDNDVKGFDDGTLLQIVHFLLNKPREDGAQLLASQEKELDLGP
Protein: Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (E3 component of pyruvate complex) (P75393)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes.
Subcellular location: Cytoplasm.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Pyruvate dehydrogenase E1 component subunit alpha
- Pyruvate dehydrogenase E1 component subunit beta
- Probable lipoate-protein ligase A
- Serine hydroxymethyltransferase
- Ribose-phosphate pyrophosphokinase
- NADH oxidase
- Uncharacterized protein MG269 homolog
- Phenylalanine--tRNA ligase beta subunit
Sequence:
MNYDLIIIGAGPAGYVAAEYAGKHKLKTLVVEKEYFGGVCLNVGCIPTKTLLKRAKIVDYLRHAQDYGISINGQVALNWNQLLEQKGKVVSKLVGGVKAIIASAKAETVMGEAKVLDPNTVEVAGKTYTTKSIVVATGSRPRYLTLPGFAEARQNGFVIDSTQALSLEGVPRKLVVVGGGVIGIEFAFLYASLGSEVTILQGVDRILEIFDTEVSDLVAKLLQTKNVKIITNAQVTRANNNEVFYSQNGQEGSVVGDRILVSIGRIPNTECLDGLNLQRDERNRIVLNQDLQTSIPNIYIVGDANAQLMLAHFAYQQGRYAVNHILNKKQVKPAQKLTCPSCIYTNPEVASVGYTEMELKKQGIPYVKTNLVLAHCGKAIADNETNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMGAGLTVFDIANSISPHPTINEMIADVCKKALFDHFK
Protein: RNA 3'-terminal phosphate cyclase-like protein (Q9Y2P8)
Organism: Homo sapiens (Human)
Function: Does not have cyclase activity. Plays a role in 40S-ribosomal-subunit biogenesis in the early pre-rRNA processing steps at sites A0, A1 and A2 that are required for proper maturation of the 18S RNA (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:27474224, ECO:0000269|PubMed:34516797}.
Interaction partners:
- Bystin
- U3 small nucleolar RNA-associated protein 4 homolog
- WD repeat-containing protein 43
- U3 small nucleolar RNA-associated protein 18 homolog
- U3 small nucleolar ribonucleoprotein protein IMP4
- Ribosome biogenesis protein BMS1 homolog
- Nucleolar complex protein 4 homolog
- Neuroguidin
- U3 small nucleolar RNA-associated protein 6 homolog
- HEAT repeat-containing protein 1
Sequence:
MATQAHSLSYAGCNFLRQRLVLSTLSGRPVKIRKIRARDDNPGLRDFEASFIRLLDKITNGSRIEINQTGTTLYYQPGLLYGGSVEHDCSVLRGIGYYLESLLCLAPFMKHPLKIVLRGVTNDQVDPSVDVLKATALPLLKQFGIDGESFELKIVRRGMPPGGGGEVVFSCPVRKVLKPIQLTDPGKIKRIRGMAYSVRVSPQMANRIVDSARSILNKFIPDIYIYTDHMKGVNSGKSPGFGLSLVAETTSGTFLSAELASNPQGQGAAVLPEDLGRNCARLLLEEIYRGGCVDSTNQSLALLLMTLGQQDVSKVLLGPLSPYTIEFLRHLKSFFQIMFKIETKPCGEELKGGDKVLMTCVGIGFSNLSKTLK
Protein: Transcription initiation factor TFIID subunit 8 (TBP-associated factor 8) (A0A0A0MRR3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADAAATAGAGGSGTRSGSKQSTNPADNYHLARRRTLQVVVSSLLTEAGFESAEKASVETLTEMLQSYISEIGRSAKSYCEHTARTQPTLSDIVVTLVEMGFNVDTLPAYAKRSQRMVITAPPVTNQPVTPKALTAGQNRPHPPHIPSHFPEFPDPHTYIKTPVSDEALGLRVV
Protein: GM01572p (Q8T9L4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MTTSYVDGHPVRDHLLSGGQQNQHTHPNNTLHIIFMNASILGNVICRDYSSRLAEIAKDAVSHGDAVNITGHKHFQAPLTVQALQANEINGVPVSEIVVKSNTTQNFTGTKTFARVVVANDINVHDHLNVSHLNGLPLQQLLGHDISLQRLELTETPHLENLHFRRLNGLPFDELLSKISEDGEQPLLLHKQLLIEGNVRFDKALQVQNINGIQWDEYLDRLVRSDSNAEIRGKKTFMADVQINDALQSPHINNLDLSSLLDNTLLRMTPQQISGAYTFDRMMATNVDVNRINGVPKEEFIDTRKDLELKGDLYLKQLNINGSLKFPFVNEAVLKDLKQRVEQVQQLPWRNLIVTGDALWDGEEQSQSQLDYLRQHAVRRVGNQTIAGHVLLKEPYLKDIQSKQSLPIDLNFTHLAEDALLRRSPTNETQVITAPQELQGLVRANTLHLEQDAHFELVNGIDIRRFNASLYRLSSGEAIAADLHFHQAPKIGKLQLEYPEVNGAPIQSIYQQGKGQSWPPVTFKNLLVEQDLNLKTVNNMNLDYFLQHRIPLKGDALEVFGSLTFEHLQLSGKPLLRSINGIQLDNLVFRHSNRTQSITGAKTFRGGVEFTGPGHVMNLNGRELSESFRGSIFRNKDYNIDSLVLDKALFPGGLVLAGLQSQIPNRMRAMEVQSNPLEEFQELLALGNQTSPRRLLYLDHDTESLESTWVKGPFRGSSELQVSLPLGYSAPCQRRTLQAKLLIHERRVLLANSSVSNQLMRLHSGDIRVKVQNHCHRPARRLRSRIRISCRNETHTLGMRQSVEAMELLEMGEMVLLLLGTEEEVRVLRLKRSNCSLTDWQSVLPADGRLMKLVRMGVESRQDLILTSGMSNHRPVLAIHYRDPLNHNFKMLQLIQGSYDLAEMQGNQLLVSCLGCRHIAIFKRYSHSAEILFEPIQQLSFQERIQQLTPFKVGNEQYLLVVTQPEEEHFYLFSYNEVGGWQQRTFGIKKQDQWAWSLVKSGQMLEAAETPILLLCGKKRECSLVKALLG
Protein: Fatty acid elongase 2 (EC 2.3.1.-) (Beta-ketoacyl-CoA synthase) (Elongation of fatty acids protein) (Q57UP7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q4DHY2}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MFPYVTDYSGFAIRKWMIDNVDVAGFLCLLYLGLVWKGPGVVKSLREKNLINATLLQGVFIMWNLFLSTFSVIGMIVVVPAAIAHISNKGLVPALCERDVNMIYDSPVGFWVGVFALSKIPELFDTVLLVLQGKQPPFLHWYHHTTVLIFSWQSYCEGSSTIFVFVAMNLTVHAVMYFYFAMCASGFKAIMRTIAPVITIMQILQMIVGSAVTMYSAYVLYNPQPDGPQTCDVTKASARMGVVMYLSYLYLFAALFVESYLKPKKRTEKSK
Protein: C2 domain-containing protein (Q57Y24)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRSNCAPLGRVKIRILDLTVLSEDASDFVYDGLYVVSRLGPDAQRTNILCNGADSAGGRCWNEVFMFHFEGNPPEFRETAPTLSKSGLDVTVGQHISTYHDGPSLGNPSREYILPQQPHEVKRGLLAPPWMGGSCALPAITLELWRYSLSSDDCLARYQFCIPLEMSSGNIADRVVRLASASSYSVQFALRIRVALSGYDGGALGFENYMPAMSPANLPVLWRH
Protein: Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase) (P70531)
Organism: Rattus norvegicus (Rat)
Function: Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced (By similarity).
Interaction partners:
- Elongation factor 2
- Ribosomal protein S6 kinase beta-1
- Protein kinase AMP-activated non-catalytic subunit gamma 2
- Protein kinase AMP-activated non-catalytic subunit gamma 3
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- Protein kinase C gamma type
- Protein kinase C beta type
- 5'-AMP-activated protein kinase subunit beta-1
- 5'-AMP-activated protein kinase subunit beta-2
Sequence:
MADEDLIFRLEGVDGGGSSGAGRHGDSDTDSDDDEGYFICPITDDHMSNQNVNSKGQGYYNNLLKTECGSTGSPASSFHFKEAWKHAIEKAKHMPDPWAEFHLEDIATEHATRHRYNAVTGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQHWKGASNYVAKRYLEPVDRSVYFEDVQLQMEAKLWGEEYNRHKPPKQVDIMQMCIIELKDRQGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRICQSMGLAPFDLSPREQDAVNQSTKLLQSAKTILRGTEEKCGSPRIRTLSGSRPPLLLRLSENSGDENMSDVTFDSLPSSPSSATPHSQKLDHLHWPVFGDLDNMGPRDHDRMDNHRDSENSGDSGYPSEKRSDLDDPEPREHGHSNGNRRPESDEDSLGSSGRVCVETWNLLNPSRLHLPRPSAVALEVQRLNALDLGRKIGKSVLGKVHLAMVRYHEGGRFCEKDEEWDQESAIFHLEHAADLGELEAIVGLGLMYSQLPHHILADVSLEETEENKTKGFDYLLKAAEAGDRQSMILVARAFDTGLNLSPDRCQDWSEALHWYNTALETTDCDEGGEYDGIQDEPQYALLAREAEMLLTGGFGLDKNPQRSGDLYTQAAEAAMEAMKGRLANQYYEKAEEAWAQMEE
Protein: Catabolic L-serine/threonine dehydratase [Includes: L-serine dehydratase (EC 4.3.1.17) (L-serine deaminase); L-threonine dehydratase (EC 4.3.1.19) (L-threonine deaminase)] (P25379)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Threonine synthase
- Acetolactate synthase small subunit, mitochondrial
- Tryptophan synthase
- Acetolactate synthase catalytic subunit, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Alanine--glyoxylate aminotransferase 1
- Low specificity L-threonine aldolase
- Cystathionine beta-synthase
- Serine hydroxymethyltransferase, mitochondrial
- Threonine dehydratase, mitochondrial
Sequence:
MSIVYNKTPLLRQFFPGKASAQFFLKYECLQPSGSFKSRGIGNLIMKSAIRIQKDGKRSPQVFASSGGNAGFAAATACQRLSLPCTVVVPTATKKRMVDKIRNTGAQVIVSGAYWKEADTFLKTNVMNKIDSQVIEPIYVHPFDNPDIWEGHSSMIDEIVQDLKSQHISVNKVKGIVCSVGGGGLYNGIIQGLERYGLADRIPIVGVETNGCHVFNTSLKIGQPVQFKKITSIATSLGTAVISNQTFEYARKYNTRSVVIEDKDVIETCLKYTHQFNMVIEPACGAALHLGYNTKILENALGSKLAADDIVIIIACGGSSNTIKDLEEALDSMRKKDTPVIEVADNFIFPEKNIVNLKSA
Protein: Carnitine O-palmitoyltransferase 1, muscle isoform (CPT1-M) (EC 2.3.1.21) (Carnitine O-palmitoyltransferase I, muscle isoform) (CPT I) (CPTI-M) (Carnitine palmitoyltransferase 1B) (Carnitine palmitoyltransferase I-like protein) (Q92523)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion outer membrane {ECO:0000305|PubMed:9344464}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Choline/ethanolamine kinase
- Acetyl-CoA carboxylase 2
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Mitochondrial carnitine/acylcarnitine carrier protein
- Carnitine O-palmitoyltransferase 1, liver isoform
- Palmitoyl thioesterase CPT1C
- Putative mitochondrial transporter UCP3
- Long-chain-fatty-acid--CoA ligase 1
- Beta-alanine-activating enzyme
- Fatty acid CoA ligase Acsl3
Sequence:
MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPTSWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTGIFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPRVSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEEYIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALGIVPMCSYQMERMFNTTRIPGKDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDLEMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVALDEESYSYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPIIGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIESSYQVAKALADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREGRTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCLYLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGYGVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS
Protein: Reduced folate transporter (FOLT) (Cyclic dinucleotide:anion antiporter SLC19A1) (Folate:anion antiporter SLC19A1) (Intestinal folate carrier 1) (IFC-1) (Placental folate transporter) (Reduced folate carrier protein) (RFC) (hRFC) (Reduced folate transporter 1) (RFT-1) (Solute carrier family 19 member 1) (hSLC19A1) (P41440)
Organism: Homo sapiens (Human)
Function: Antiporter that mediates the import of reduced folates or a subset of cyclic dinucleotides, driven by the export of organic anions. Mechanistically, acts as a secondary active transporter, which exports intracellular organic anions down their concentration gradients to facilitate the uptake of its substrates. Has high affinity for N5-methyltetrahydrofolate, the predominant circulating form of folate. Also able to mediate the import of antifolate drug methotrexate. Also acts as an importer of immunoreactive cyclic dinucleotides, such as cyclic GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol, and its linkage isomer 3'-3'-cGAMP, thus playing a role in triggering larger immune responses. 5-amino-4-imidazolecarboxamide riboside (AICAR), when phosphorylated to AICAR monophosphate, can serve as an organic anion for antiporter activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10347183, ECO:0000269|PubMed:10787414, ECO:0000269|PubMed:15337749, ECO:0000269|PubMed:16115875, ECO:0000269|PubMed:36071163, ECO:0000269|PubMed:36265513, ECO:0000269|PubMed:36575193, ECO:0000269|PubMed:36745868, ECO:0000269|PubMed:9767079}; Multi-pass membrane protein {ECO:0000269|PubMed:36071163, ECO:0000269|PubMed:36265513, ECO:0000269|PubMed:36575193}. Apical cell membrane {ECO:0000269|PubMed:10787414}; Multi-pass membrane protein {ECO:0000269|PubMed:36071163, ECO:0000269|PubMed:36265513, ECO:0000269|PubMed:36575193}. Basolateral cell membrane {ECO:0000269|PubMed:10787414}; Multi-pass membrane protein {ECO:0000269|PubMed:36071163, ECO:0000269|PubMed:36265513, ECO:0000269|PubMed:36575193}.
Interaction partners:
- Gamma-glutamyl hydrolase
- Thiopurine S-methyltransferase
- Methylenetetrahydrofolate reductase
- Proton-coupled folate transporter
- Methionine synthase reductase
- Dihydrofolate reductase
- Folylpolyglutamate synthase, mitochondrial
- Methionine synthase
- Thymidylate synthase
- C-1-tetrahydrofolate synthase, cytoplasmic
Sequence:
MVPSSPAVEKQVPVEPGPDPELRSWRHLVCYLCFYGFMAQIRPGESFITPYLLGPDKNFTREQVTNEITPVLSYSYLAVLVPVFLLTDYLRYTPVLLLQGLSFVSVWLLLLLGHSVAHMQLMELFYSVTMAARIAYSSYIFSLVRPARYQRVAGYSRAAVLLGVFTSSVLGQLLVTVGRVSFSTLNYISLAFLTFSVVLALFLKRPKRSLFFNRDDRGRCETSASELERMNPGPGGKLGHALRVACGDSVLARMLRELGDSLRRPQLRLWSLWWVFNSAGYYLVVYYVHILWNEVDPTTNSARVYNGAADAASTLLGAITSFAAGFVKIRWARWSKLLIAGVTATQAGLVFLLAHTRHPSSIWLCYAAFVLFRGSYQFLVPIATFQIASSLSKELCALVFGVNTFFATIVKTIITFIVSDVRGLGLPVRKQFQLYSVYFLILSIIYFLGAMLDGLRHCQRGHHPRQPPAQGLRSAAEEKAAQALSVQDKGLGGLQPAQSPPLSPEDSLGAVGPASLEQRQSDPYLAQAPAPQAAEFLSPVTTPSPCTLCSAQASGPEAADETCPQLAVHPPGVSKLGLQCLPSDGVQNVNQ
Protein: Interleukin 17_4 (Interleukin 17d) (Interleukin-17D precursor) (Q5TKT1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Interleukin 17 receptor C.
Sequence:
MRAPVVSTLVLVWLWCCGSAPGERGQKVSRRAPRTRSCLDLPEEILEQMFGRLSVGVLSAFHHTLQLATPERQNLSCGSASRLARDRPRTPVNLLSLSPWAYRISHDPARYPRYLPEAYCLCKGCLSGLNGEESDRFRSTPVYMPTVILRRTVGPCVGGRHSYTESYVSIAVGCTCVPLLEKDSKIQKSKPSVRRVASKNTVSSTFRKNELN
Protein: Ribonuclease HII (RNase HII) (EC 3.1.26.4) (P10442)
Organism: Escherichia coli (strain K12)
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Lipid-A-disaccharide synthase
- Ribonuclease HI
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
- DNA polymerase III subunit alpha
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Beta sliding clamp
- Signal peptidase I
- Thymidylate synthase
- DNA polymerase I
- UDP-3-O-
Sequence:
MIEFVYPHTQLVAGVDEVGRGPLVGAVVTAAVILDPARPIAGLNDSKKLSEKRRLALYEEIKEKALSWSLGRAEPHEIDELNILHATMLAMQRAVAGLHIAPEYVLIDGNRCPKLPMPAMAVVKGDSRVPEISAASILAKVTRDAEMAALDIVFPQYGFAQHKGYPTAFHLEKLAEHGATEHHRRSFGPVKRALGLAS
Protein: Uncharacterized protein YNL018C (P53976)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized membrane protein YNL033W
- Uncharacterized membrane protein YNL019C
Sequence:
MSTSFQEFKAFCNKVGLDFQWLNLQSSKSVPENGSSEGFSAVSDTVQENIRPATEPLNVNQSKDPVSNFFYDVKNAPLWNVYKRNHSGHSSAEACSGVSSRQAPKNIPEAMVKETVLSNHDNVTIINELLPTSSAMHQEESTAMTTSYLLSHSVNDTCNVMFSSSSHNRAMLPSSLVQRNNATTSPTTDSASENNESVPSLTSSVSTSSSVYSSWNPPHSPHISSFPDGNFASLNAEVTCFDFRRTKDSRTKETNESIIPTEIYCPTNSTDHHKHYPSRKSKQDACAPAPCNQNISCSVVSTAEFSQSNHTLTTVVPSYMQQYLDRPQNWFESKMGKYCPLFLRSTKNIDYDSLEFKFERKMIAVQYLLLDEQSEPRRYYNPSNKSIPFWKRPFNFDTMPSYDQLMEEAECRFYSYQYKYEGFQRIEPYSISCPWKNTQREIDLVLDHIHFSLDVGEKKSLNRKGNITLDTLDSKVDPNIQIKPYQIFPSNNLVYEGLPHPAEQSLILSPDTSLIERAFQALIDICKESIPSSNDCSTRNNNSAPQLTVPEPSKPCRLLLVRESRTATELKTNKKLWLHSQRRNIEVTVPMHPSERGTKSWLRKWLSTFVHQ
Protein: Small EDRK-rich factor 2 (Gastric cancer-related protein VRG107) (Protein 4F5-related) (4F5rel) (h4F5rel) (P84101)
Organism: Homo sapiens (Human)
Function: Positive regulator of amyloid protein aggregation and proteotoxicity. Induces conformational changes in amyloid proteins, such as HTT, driving them into compact formations preceding the formation of aggregates.
Interaction partners:
- Myosin light polypeptide 6
- Translation machinery-associated protein 7
- Small ribosomal subunit protein eS19
Sequence:
MTRGNQRELARQKNMKKQSDSVKGKRRDDGLSAAARKQRDSEIMQQKQKKANEKKEEPK
Protein: Heat shock transcription factor, X-linked (Q9UBD0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:15044259}.
Interaction partners:
Sequence:
MEDKRSLSMARCEERNSRGQDHGLERVPFPPQLQSETYLHPADPSPAWDDPGSTGSPNLRLLTEEIAFQPLAEEASFRRPHPDGDVPPQGEDNLLSLPFPQKLWRLVSSNQFSSIWWDDSGACRVINQKLFEKEILKRDVAHKVFATTSIKSFFRQLNLYGFRKRRQCTFRTFTRIFSAKRLVSILNKLEFYCHPYFQRDSPHLLVRMKRRVGVKSAPRHQEEDKPEAAGSCLAPADTEQQDHTSPNENDQVTPQHREPAGPNTQIRSGSAPPATPVMVPDSAVASDNSPVTQPAGEWSEGSQAHVTPVAAVPGPAALPFLYVPGSPTQMNSYGPVVALPTASRSTLAMDTTGLPAPGMLPFCHLWVPVTLVAAGAAQPAASMVMFPHLPALHHHCPHSHRTSQYMPASDGPQAYPDYADQST
Protein: Large ribosomal subunit protein eL8 (50S ribosomal protein L7Ae) (Ribosomal protein L8e) (P54066)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00326}.
Interaction partners:
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS3
- Uncharacterized NOP5 family protein MJ0694
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein uS17
- Probable translation initiation factor IF-2
Sequence:
MAVYVKFKVPEEIQKELLDAVAKAQKIKKGANEVTKAVERGIAKLVIIAEDVKPEEVVAHLPYLCEEKGIPYAYVASKQDLGKAAGLEVAASSVAIINEGDAEELKVLIEKVNVLKQ