wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxiredoxin Q, chloroplastic (EC 1.11.1.24) (Thioredoxin peroxidase) (Thioredoxin-dependent peroxiredoxin Q) (F4JBC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000256|ARBA:ARBA00004456}.
Interaction partners:
Sequence:
MAASSSSFTLCNHTTLRTLPLRKTLVTKTQFSVPTKSSESNFFGSTLTHSSYISPVSSSSLKGLIFAKQVNKGQAAPDFTLKDQNGKPVSLKKYKGKPVVLYFYPADETPGCTKQACAFRDSYEKFKKAGAEVIGISGDDSASHKAFASKYKLPYTLLSDEGNKVRKDWGVPGDLFGALPGRQTYVLDKNGVVQLIYNNQFQPEKHIDETLKFLKAA
Protein: Probable cytochrome P450 6a20 (EC 1.14.-.-) (CYPVIA20) (Q9V773)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Glutathione S transferase E9
Sequence:
MAVMIVLLIGVITFVAWYVHQHFNYWKRRGIPHDEPKIPYGNTSELMKTVHFADIFKRTYNKLRNKTDGPFVGFYMYFKRMVVVTDIDFAKTVLIREFDKFHDRGVFHNERDDPLSANLVNIDGQKWKTLRQKLTPTFTSGKMKTMFPTILTVGDELIRVFGETASADSDSMEITNVVARFTADVIGSCAFGLDCHSLSDPKAKFVQMGTTAITERRHGKSMDLLLFGAPELAAKLRMKATVQEVEDFYMNIIRDTVDYRVKNNVKRHDFVDMLIEMKLKFDNGDKENGLTFNEIAAQAFIFFLAGFETSSTTMGFALYELACHQDIQDKLRTEINTVLKQHNGKLDYDSMREMTYLEKVIDETMRKRPVVGHLIRVATQHYQHTNPKYNIEKGTGVIVPTLAIHHDPEFYPEPEKFIPERFDEDQVQQRPACTFLPFGDGPRNCIGLRFGRMQVIVGMALLIHNFKFEFHPTKTVVPLEYRTDDFLLSSKGGIHLKVTRV
Protein: Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta (PP2A subunit B isoform PR48) (Protein phosphatase 2A 48 kDa regulatory subunit) (Q9Y5P8)
Organism: Homo sapiens (Human)
Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
Subcellular location: Nucleus {ECO:0000269|PubMed:10629059}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Cell division control protein 6 homolog
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Ryanodine receptor 2
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Apoptosis regulator Bcl-2
- Protein phosphatase 1 regulatory subunit 1A
Sequence:
MPPGKVLQPVLKMKVDELFLYWLSEASTQRMLQDCLRRIKAPGRDQPTPGDGEQPGAWPTAPLAAPRPSGLEPPGTPGPGPALPLGAASSPRNAPHVRGTRRSAGTRVVQTRKEEPLPPATSQSIPTFYFPRGRPQDSVNVDAVISKIESTFARFPHERATMDDMGLVAKACGCPLYWKGPLFYGAGGERTGSVSVHKFVAMWRKILQNCHDDAAKFVHLLMSPGCNYLVQEDFVPFLQDVVNTHPGLSFLKEASEFHSRYITTVIQRIFYAVNRSWSGRITCAELRRSSFLQNVALLEEEADINQLTEFFSYEHFYVIYCKFWELDTDHDLLIDADDLARHNDHALSTKMIDRIFSGAVTRGRKVQKEGKISYADFVWFLISEEDKKTPTSIEYWFRCMDLDGDGALSMFELEYFYEEQCRRLDSMAIEALPFQDCLCQMLDLVKPRTEGKITLQDLKRCKLANVFFDTFFNIEKYLDHEQKEQISLLRDGDSGGPELSDWEKYAAEEYDILVAEETAGEPWEDGFEAELSPVEQKLSALRSPLAQRPFFEAPSPLGAVDLYEYACGDEDLEPL
Protein: Fatty acid 2-hydroxylase (EC 1.14.18.-) (Fatty acid alpha-hydroxylase) (Q5MPP0)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydroxylation of free fatty acids at the C-2 position to produce 2-hydroxy fatty acids, which are building blocks of sphingolipids and glycosphingolipids common in neural tissue and epidermis. FA2H is stereospecific for the production of (R)-2-hydroxy fatty acids. Plays an essential role in the synthesis of galactosphingolipids of the myelin sheath. Responsible for the synthesis of sphingolipids and glycosphingolipids involved in the formation of epidermal lamellar bodies critical for skin permeability barrier (By similarity). Participates in the synthesis of glycosphingolipids and a fraction of type II wax diesters in sebaceous gland, specifically regulating hair follicle homeostasis. Involved in the synthesis of sphingolipids of plasma membrane rafts, controlling lipid raft mobility and trafficking of raft-associated proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15658937}; Multi-pass membrane protein {ECO:0000269|PubMed:15658937}. Microsome membrane {ECO:0000269|PubMed:15658937}; Multi-pass membrane protein {ECO:0000269|PubMed:15658937}.
Interaction partners:
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- RNA-binding protein 39
- Bifunctional coenzyme A synthase
- Cholesterol 25-hydroxylase
- Pantothenate kinase 2
- Methylsterol monooxygenase 1
Sequence:
MAPAPPPAASFTPAEVQRRLAAGACWVRRGASLYDLTSFVRHHPGGEQLLLARAGQDISADLDGPPHRHSDNARRWLEQYYVGELRADPQDPTENGAVASAETQKTDPALEPQFKVVDWDKDLVDWQKPLLWQVGHLGEKYDEWVHQPVARPIRLFHSDLIEAFSKTVWYSVPIIWVPLVLYLSWSYYRTLTQDNIRLFASLTREYSMMMPESVFIGLFVLGMLFWTFVEYVIHRFLFHMKPPSNSHYLIMLHFVMHGQHHKAPFDGSRLVFPPVPASLVIAFFYVFLRLILPETVGGIIFAGGLLGYVLYDMTHYYLHFGSPHKGSYLYNMKAHHVKHHFEYQKSGFGISTKLWDYFFHTLIPEEAHPKMQ
Protein: Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase (EC 2.4.1.144) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III) (GNT-III) (GlcNAc-T III) (N-acetylglucosaminyltransferase III) (Q10470)
Organism: Mus musculus (Mouse)
Function: It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains, called bisecting N-acetylglucosamine (GlcNAc). It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. The addition of this bisecting GlcNAc residue alters not only the composition, but also the conformation of the N-glycan. The introduction of the bisecting GlcNAc residue results in the suppression of further processing and elongation of N-glycans, precluding the formation of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is unable to use the bisected oligosaccharide as a substrate (By similarity). Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location. Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation (By similarity). In brain, addition of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal targeting in response to oxidative stress and further degradation which increases its location to early endosome and the APP cleavage.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
Sequence:
MKMRRYKLFLMFCMAGLCLISFLHFFKTLSYVTFPRELASLSPNLISSFFWNNAPVTPQASPEPGDPDLLRTPLYSHSPLLQPLSPSKATEELHRVDFVLPEDTTEYFVRTKAGGVCFKPGTRMLEKPSPGRTEEKTEVSEGSSARGPARRPMRHVLSSRERLGSRGTRRKWVECVCLPGWHGPSCGVPTVVQYSNLPTKERLVPREVPRRVINAININHEFDLLDVRFHELGDVVDAFVVCDSNFTAYGEPRPLKFREMLTNGTFEYIRHKVLYVFLDHFPPGGRQDGWIADDYLRTFLTQDGVSRLRNLRPDDVFIIDDADEIPARDGVLFLKLYDGWTEPFAFHMRKSLYGFFWKQPGTLEVVSGCTMDMLQAVYGLDGIRLRRRQYYTMPNFRQYENRTGHILVQWSLGSPLHFAGWHCSWCFTPEGIYFKLVSAQNGDFPRWGDYEDKRDLNYIRSLIRTGGWFDGTQQEYPPADPSEHMYAPKYLLKNYDQFRYLLENPYREPKSTVEGGRQNQGSDGRSSAVRGKLDTAEG
Protein: Sialic acid binding Ig-like lectin H (G3X9N0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLLSRLLPLLWVLKWASGNCFILPREVIGTYPSLTLELQSVTVQEGLCVLVPCHLIEYPMNRWSDAAFGYWFHEGENTHPDSLVATNKPYQLVQKEMQSRFHFSGDCSLDIRDAQKGDNGSYFFRLEKGGKTWNFCEERISVHVTDLTHSPNISIPQTLELGRPTNVMCSVPWACERGTPPIFSWMSAALISLGPTTTLSSVLTLTPRLQDHGTNLTCQVTFPGAGVTVQKTIQLNVTWKPRPLADVVQVAMGEAAIKFLLLGICFFFLSKRSHTKRVERPATHMDQAHAVMD
Protein: Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)] (G8BAW7)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Function: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase.
Interaction partners:
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Uncharacterized protein
- AMP-dependent synthetase/ligase domain-containing protein
- 3-oxoacyl-[acyl-carrier-protein] synthase
- 3-oxoacyl-[acyl-carrier-protein] reductase
- [acyl-carrier-protein] S-malonyltransferase
- Octanoyltransferase
- AMP-dependent synthetase/ligase domain-containing protein
- AMP-dependent synthetase/ligase domain-containing protein
- Acyl-CoA desaturase
Sequence:
MKPEIEQELSHTLLTELLAYQFASPVRWIETQDVFLKQHNTERVIEIGPSPTLAGMASRTIKAKYQSYDAALSLQRQVLCYSKDAKEIYYTPDPAEPPAAEEPKAETGKESAPAASAAAAAATQPAAAVAPPPQSAGPVESIPDEPVKASLLIHVLVAQKLKKPLDAVPMSKAIKDLVNGKSTVQNEILGDLGKEFGSTPEKPEETPLEELAEQFQDTFSGSLGKTSTSLIGRLMSSKMPGGFSITNARKYLESRFGLGPGRQDSVLLTALCNEPASRLGSEGDAKSFLDTMAQKYASHAGISLSSPSAGGASSGAGAAVVDSAALDALIAENKKLARQQLETLARYLQVDLTKGEKAFIKEKEATTVLQQELDLWEAEHGEFYAKGIKPVFSPLKSRTYDSYWNWARQDLLSMWFDILFGKLTSVDRETINQCIQIMNRANPTLIKFMQYHVELCPTYRGETYKLGKRLGEQLIENCKQILGQSPVYKDVSRITGPKTTVSAKGDIVYEEANKESVRKFEQYVFEMAQGGSMTKMKQSSIQEDLARVYKAISKQASRDSKLELQKVYDQLLKVVEGSTEIETEQTTQDALAIPTGSNTPTEEDELSTASDDDEIASLPDKTSIAQPVSSTIPNKTIPFLHIQSKSESGNWEYDRKLSSIYLDGLESAAINGLTFKDKYVLVTGAGAGSIGAEILQGLISGGAKVIVTTSRYSKKVTEYYQNMYARYGAAGSTLIVVPFNQGSKQDVDALVEYIYNDQKKGGLGWDLDVIIPFAAIPENGNGIDNIDSKSEFAHRIMLTNLLRLLGAVKARKTTDTRPAQCILPLSPNHGTFGFDGLYSESKISLETLFNRWYSEDWGTKLTICGAIIGWTRGTGLMSANNIIAEGIEKLGVRTFSQKEMAFNILGLLTPEIVNLCQEEPVMADLNGGLQFIDNLKEFTSKLRNDLTETADIRRAVSIESAIEQKVVNGDNVDSNYNKVTVRPRANMKFDFPTLKSYDEIKQIAPDLEGMLDLENVVVVTGFAEVGPWGNARTRWEMESKGEFSLEGAIEMAWIMGMIKYHNGNLKGKPYSGWIDAKTQTPVDDKDIKAKYEEEILEHSGIRLIEPELFNGYDPKKKQMIQEVVIQHDLEPFECSKETAEQYKHEHGDKCEISEIEESGEYSVRILKGATLFIPKALRFDRLVAGQIPTGWDARTYGIPEDTINQVDPITLYVLVATVEALLSAGITDPYEFYKYVHVSEVGNCSGSGMGGVSALRGMFKDRYADKPVQNDILQESFINTMSAWVNMLLLSASGPIKTPVGACATAVESVDIGIETILSGKAKVVMVGGYDDFQEEGSYEFANMNATSSAIDEFKHGRTPKEMSRPTTTTRNGFMEAQGSGIQVIMSADLALKMGVPIHAVLAMSATATDKIGRSVPAPGKGILTTAREHHGNLKYPSPLLNVKYRKRQLSKRLDQIKSWESSELNYLQEEAHLAKEEFGEEFSEAEFLRERTEEIYRESKRQVADAKKQWGNAFYKSDPRIAPLRGALATFNLTIDDIGVASFHGTSTVANDKNESATIDSMMKHLGRSEGNPVFGVFQKYLTGHPKGAAGAWMLNGAIQILESGIVPGNRNADNVDKVLEQYEYVLYPSRSIQTDGIKAVSVTSFGFGQKGAQAVVVHPDYLYAVLDRSTYEDYAKRVTARNKKTYRYMHNAITRNTMFVAKDKAPYSDELTMDVYLDPLARVSKTKNEFVFTKKSVQSDKSYVSNIANSTAKALSSLNKSSKGVGVDVELLSELNIDNETFLERNFTPEEIKYCQNSANPQASFTGTWSAKEATFKALGVSSQGGGASLKEIEIVRDGNGAPQVVLNDNAKAAAKAAGVKNVNVSISHDDFQATAVALSEF
Protein: ABC-type glutathione-S-conjugate transporter (EC 7.6.2.3) (Q7KTC5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Vacuole membrane {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
Interaction partners:
Sequence:
MADDTSSPMDRFCGSTFWNATETWYTNDPDFTPCFEQTALVWTPCAFYWAFVIFDFYYLKASLDRNIPWNKLNVSKALVNLGLLVITALDLIMALVKKGGDSELPLYDLDVWGPIIKFATFLLLFIFIPLNRKYGVQTTGCQFIFWFLLTVLSIPRCRTEVRLDAERQKILNSQQPSEQDFSWEEYQFVSFFIFFTFTSIMLILNCFADGMPRQTKYQRGENEIPELSASFLSRITYQWFDKMALKGYRNPLEEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKNYKNKARVEPKAQFSNGNVTFENPHGEKNGRKKGMASIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLTSEANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRINKFLNSEELDPNSVLHDSSKPHPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQHLQEGNEEEEELNQIKRQISSTADVPELLGTVEKAIKLARTESLSDSISVTSADSLMGGGGSLRRRTKRQDSHDSVASAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDMYLGVYGAFGFGQVFSYIGSVVIVYLGALIGTRKIFIQLFGNILHAPQAYFDIKPRARILDRLANDIYKLDVVLPELIRVFNSQVFRVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPWELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSMAKDANLV
Protein: RNA-binding protein 24 (RNA-binding motif protein 24) (M0R7T6)
Organism: Rattus norvegicus (Rat)
Function: Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation. Plays a major role in pre-mRNA alternative splicing regulation (By similarity). Mediates preferentially muscle-specific exon inclusion in numerous mRNAs important for striated cardiac and skeletal muscle cell differentiation (By similarity). Binds to intronic splicing enhancer (ISE) composed of stretches of GU-rich motifs localized in flanking intron of exon that will be included by alternative splicing (By similarity). Involved in embryonic stem cell (ESC) transition to cardiac cell differentiation by promoting pre-mRNA alternative splicing events of several pluripotency and/or differentiation genes (By similarity). Plays a role in the regulation of mRNA stability (By similarity). Binds to 3'-untranslated region (UTR) AU-rich elements in target transcripts, such as CDKN1A and MYOG, leading to maintain their stabilities (By similarity). Involved in myogenic differentiation by regulating MYOG levels (By similarity). Binds to multiple regions in the mRNA 3'-UTR of TP63 isoform 2, hence inducing its destabilization (By similarity). Promotes also the destabilization of the CHRM2 mRNA via its binding to a region in the coding sequence (By similarity). Plays a role in the regulation of mRNA translation (By similarity). Mediates repression of p53/TP53 mRNA translation through its binding to U-rich element in the 3'-UTR, hence preventing EIF4E from binding to p53/TP53 mRNA and translation initiation (By similarity). Binds to a huge amount of mRNAs (By similarity). Required for embryonic heart development, sarcomer and M-band formation in striated muscles (By similarity). Together with RBM20, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6GQD3}. Cytoplasm {ECO:0000250|UniProtKB:D3Z4I3}.
Interaction partners:
- RNA binding protein fox-1 homolog 1
- RNA binding protein fox-1 homolog 2
Sequence:
MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGDIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQLHPALIQRPFGIPAHYVYPQAFVQPGVVIPHVQPTAAAASTTPYIDYTGAAYAQYSAAAAAAAAAAAYDQYPYAASPAATGYVTTGGYSYAVQQPITAAAPGTAAAAAAAAAAAAAFGQYQPQQLQTDRMQ
Protein: Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic (EC 1.2.1.12) (NAD-dependent glyceraldehydephosphate dehydrogenase C subunit 1) (P25858)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism. Required for full fertility. Involved in response to oxidative stress by mediating plant responses to abscisic acid (ABA) and water deficits through the activation of PLDDELTA and production of phosphatidic acid (PA), a multifunctional stress signaling lipid in plants. Associates with FBA6 to the outer mitochondrial membrane, in a redox-dependent manner, leading to binding and bundling of actin. Actin binding and bundling occurs under oxidizing conditions and is reversible under reducing conditions. May be part of a redox-dependent retrograde signal transduction network for adaptation upon oxidative stress. Binds DNA in vitro. Together with DNA polymerase II subunit B3-1 (DPB3-1) and GAPC2, enhances heat tolerance and promotes the expression of heat-inducible genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32651385}. Nucleus {ECO:0000269|PubMed:32651385}. Note=Accumulates in the nucleus under heat stress. {ECO:0000269|PubMed:32651385}.
Interaction partners:
- Triosephosphate isomerase, chloroplastic
- Phosphoribulokinase, chloroplastic
- Triosephosphate isomerase, cytosolic
- Phosphoglycerate kinase 3, cytosolic
- Phosphoglycerate kinase 1, chloroplastic
- Phosphoglycerate kinase 2, chloroplastic
- Transketolase-1, chloroplastic
- Transketolase-2, chloroplastic
- Glucose-6-phosphate isomerase, cytosolic
- transaldolase
Sequence:
MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHNELKIKDEKTLLFGEKPVTVFGIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSSRVVDLIVHMSKA
Protein: 3'-5' exoribonuclease 1 (EC 3.1.13.1) (3'-5' exonuclease ERI1) (Eri-1 homolog) (Histone mRNA 3'-end-specific exoribonuclease) (Histone mRNA 3'-exonuclease 1) (Protein 3'hExo) (HEXO) (Q8IV48)
Organism: Homo sapiens (Human)
Function: RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16912046}. Nucleus {ECO:0000269|PubMed:16912046}. Nucleus, nucleolus {ECO:0000269|PubMed:16912046}.
Interaction partners:
- Histone RNA hairpin-binding protein
- Endoribonuclease Dicer
- Heterogeneous nuclear ribonucleoprotein Q
- 5'-3' exoribonuclease 1
- Death effector domain-containing protein
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- U7 snRNA-associated Sm-like protein LSm11
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
- Y-box-binding protein 1
Sequence:
MEDPQSKEPAGEAVALALLESPRPEGGEEPPRPSPEETQQCKFDGQETKGSKFITSSASDFSDPVYKEIAITNGCINRMSKEELRAKLSEFKLETRGVKDVLKKRLKNYYKKQKLMLKESNFADSYYDYICIIDFEATCEEGNPPEFVHEIIEFPVVLLNTHTLEIEDTFQQYVRPEINTQLSDFCISLTGITQDQVDRADTFPQVLKKVIDWMKLKELGTKYKYSLLTDGSWDMSKFLNIQCQLSRLKYPPFAKKWINIRKSYGNFYKVPRSQTKLTIMLEKLGMDYDGRPHCGLDDSKNIARIAVRMLQDGCELRINEKMHAGQLMSVSSSLPIEGTPPPQMPHFRK
Protein: Calcium up-regulated protein A (Q55FW5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May play an important role in stabilizing and/or regulating the cell membrane during Ca(2+) stress or certain stages of development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14871937}. Membrane {ECO:0000269|PubMed:14871937}; Peripheral membrane protein {ECO:0000269|PubMed:14871937}. Note=Associates with the cell membrane during Ca(2+) stress and cell aggregation.
Interaction partners:
Sequence:
MINIEDISKSSNESEEKQLKSTSTSSKPKYPFAAKSLFKGSNNIIPYYLSTSNTFQCVASESIQTWLLSDDGHIFTSSGNFVLDVSSGGYFVELVQLNSNSKTQIWTIDTTNNKIQNQGNGKYLDIDNLNICVAPLNGNATQKWTTFRRAPIPTGNWGYFQSKKLDSNNNYWGLSVLNNSTSYNTSVVMNKVQAKSIGQIWQMTNDGHILSRLDGNLVLDIGPSINGSKTNYYLNTNVYKANDLMQQWGINENNQIFNQYYPNLCIGFVGELGVDSTVNCVLAQPTSASDINFQWIANPTYSLNQIVSEVPEPFPAYTSGDLLASYQYLSNDATNGYTDDIRSLYTSINVSLEHFYVNVSNATCPSSIHSTEDFSNVQNQIKNELTYAINVRLVFDNYSDFYSKLFSQGSTNLTNLANLINVI
Protein: Guanine nucleotide exchange factor subunit RIC1 (Protein RIC1) (Ribosome control protein 1) (Ric1p) (P40395)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates YPT6 by exchanging bound GDP for free GTP. It is thereby required for efficient fusion of endosome-derived vesicles with the Golgi. The RIC1-RGP1 participates in the recycling of SNC1, presumably by mediating fusion of endosomal vesicles with the Golgi compartment. May also be indirectly involved in the transcription of both ribosomal protein genes and ribosomal RNA.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10990452, ECO:0000269|PubMed:11160819, ECO:0000269|PubMed:11689439, ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:10990452, ECO:0000269|PubMed:11160819, ECO:0000269|PubMed:11689439, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Guanine nucleotide exchange factor subunit RGP1
- GTP-binding protein YPT6
- Protein LTV1
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit beta
- Translation initiation factor eIF2B subunit alpha
- GTP-binding protein GTR1
- Translation initiation factor eIF2B subunit gamma
- Protein MEH1
Sequence:
MFIKQSEKNTPKCLYKKKGKVRVLLTGSCKKLNTWKMHLWPVSPPQLLRIPPRNAELGEGTKIDDCNILQSMTLPQANVLIMLTPTRVLIYNFKPMALVASHERTMASLKEFGDNRSMKRSAPYNDIIEGLISKKDSQYLLWHQGKLIFYVMTDKNFLLTYQILKNCTNEIIFKEYGIPVIEPLLMSEEEANSAEYDYNNDDDTLTVFDKNSSSRIIQNGFGITKEKGFLHFLSNQENIDELPVKKLELRLKVVLKFDYEIIDMIGIKTFSKVGDGRYEEVLIVLFPHGLQILTISDFKVSKSSLVEVKKGSKTIVCNKQLMVLSHDSVEKQTIVSIIDIEKQAVEAIPLTDTPDELLTCLEVNGYLVVVYKEKIICFDTRIKKVSHSWKPPFVIKLCDKINDKILLLVSEDSVNIHFYTEFGNLLFATYFDEDDYNGDNNNDNSKDKNEKKAAEYKISDFVCLDKSLITVSHSGKYQVWKLWEEIKQTQFDFRNPKCYVLTNTNNDVIIYSPVTSSSINNDNLQVIKLPTKTFNNHIAFVKINSSLRLFATYVSNKNILLIHNLETNMWSSFADQNVLDLHWLGDNYLVCHMKNDDGSTNLKCLQIPLQEANPDVELSDYVMWEYNVPENTIVFSLHVNTLSRYKLLKMKSKNHNASEKQPDALLKTAEIILVTDTQTIVFDVISTVHPCGLNIIKKFYQYLKINIPIDVLPNKIEWIINMKEGLLFFADRKFIKLGKVDGGGWQTLTLLDNIEKIIDVIRDEIFVVQGHNYVVYSLEDLWDDKKPLVSIPIEEDLYPISTTPETATTHTLHCIFNARFSKLVVKHQIYLDQLILAKLEDNTDLEDISHNYRFLKPYKFALEKILSTKILRSDSLDDILKLIKMYDNTDPEHNISPPTHSGMLEIISNCLRKIETKYWNHLFTNLKMTPRDLLALCIEENEAKMLGVLLLVFLNYDEKDLGDDLHFKKSDLGTEESKALNDNSTKKSEKSVTNLLKDEELMLKVLELLVTSAANATDPIKATDSWDMCFQLIRLLKELDRENNTQLVQKALERFK