wanglab/gogpt-training-data huggingface dataset:
Protein: Anthranilate synthase component 2 (AS) (ASII) (EC 4.1.3.27) (Anthranilate synthase, GATase component) (Anthranilate synthase, glutamine amidotransferase component) (P9WN35)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Interaction partners:
- Probable para-aminobenzoate synthase component I PABD
- Anthranilate phosphoribosyltransferase
- Anthranilate synthase component 1
- Indole-3-glycerol phosphate synthase
- Salicylate synthase
- Tryptophan synthase beta chain
- Tryptophan synthase alpha chain
- Intracellular chorismate mutase
- Bifunctional aminodeoxychorismate lyase / D-amino acid transaminase
- Chorismate synthase
Sequence:
MRILVVDNYDSFVFNLVQYLGQLGIEAEVWRNDDHRLSDEAAVAGQFDGVLLSPGPGTPERAGASVSIVHACAAAHTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVFHTNVGVLQGLPDPFTATRYHSLTILPKSLPAVLRVTARTSSGVIMAVQHTGLPIHGVQFHPESILTEGGHRILANWLTCCGWTQDDTLVRRLENEVLTAISPHFPTSTASAGEATGRTSA
Protein: Beta-3 adrenergic receptor (Beta-3 adrenoreceptor) (Beta-3 adrenoceptor) (P13945)
Organism: Homo sapiens (Human)
Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Mitochondrial brown fat uncoupling protein 1
- Guanine nucleotide-binding protein G
- Beta-2 adrenergic receptor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Beta-1 adrenergic receptor
- Proto-oncogene tyrosine-protein kinase Src
- Hormone-sensitive lipase
- Fibroblast growth factor 21
Sequence:
MAPWPHENSSLAPWPDLPTLAPNTANTSGLPGVPWEAALAGALLALAVLATVGGNLLVIVAIAWTPRLQTMTNVFVTSLAAADLVMGLLVVPPAATLALTGHWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRCARTAVVLVWVVSAAVSFAPIMSQWWRVGADAEAQRCHSNPRCCAFASNMPYVLLSSSVSFYLPLLVMLFVYARVFVVATRQLRLLRGELGRFPPEESPPAPSRSLAPAPVGTCAPPEGVPACGRRPARLLPLREHRALCTLGLIMGTFTLCWLPFFLANVLRALGGPSLVPGPAFLALNWLGYANSAFNPLIYCRSPDFRSAFRRLLCRCGRRLPPEPCAAARPALFPSGVPAARSSPAQPRLCQRLDGASWGVS
Protein: DNA 5'-3' helicase (EC 5.6.2.3) (D3DMG9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
TGNCELSRNRRIMKLSVDGLLVYFPYEYIYPEQYAYMLELKRSLDAKGHCLLEMPSGTGKTATLLSLIVAYMVEHPETVRKLIYCSRTVPEIEKVIAELQNLMVYYERHCPNPPPFTGLVLSSRKNMCIHPEVSKEREGKAVDGKCYGLTASYIRERHEMDTETPICQYFEGFSLEGKESTLPVGVYSIDDLKEYGRSRNWCPYFLARYAIAHAHIVVYSYHYLLDPKIAQVVSKEMSRESCVVFDEAHNIDNVCIDSMSVKINRRTVERSTNALNHLTKLVQDIREEDTNRLNEEYQRMVQGLKDASVQRDTDMILANPVLPNDVLTEVVPGNIRNADHFLSFLRRFIEYIKTRLRVHHVVQESPAGFLKDISSKICIERKPLRFCAERLSSLLRTLEISDLTEYGALTLITHFATLVSTYTKGFTIIIEPFDDKTPTVSNPILHFSCLDSSIAMAPVFSRFQTVVITSGTLSPMDMYPKILDFDPVVMSSFTMTLARPCLLPMIVSKGNDQVTISSKFETREDTAVIRNYGQLLVEVAKTVPDGIVCFFTSYLYLESVVASWYDQGIVDTLLRYKLLFIETQDNAETSYALMNYVKACDCGRGAVLLAVARGKVSEGVDFDHHYGRAVLMFGIPYVYTQSRILKARLDYLRDQFQIRENDFLTFDAMRHAAQCVGRALRGKTDYGIMIFADKRFSRHDKRSRLPKWIQEHLVDSFCNLSTEEAVQLARRWLRRMAQPFTREDQLGISLLTLAQLENMEQEKLERQAQGKQGVGGEVQEL
Protein: Rpgrip1-like (A0A8I6A999)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
Sequence:
MDILKIMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARTNTGRRKASTTAGLQECLGKGIKVQNVDEAETVQPTLTKYSSGLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSVRFSERRVEELQDRINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKAEVLDQLKTERDQNEKLVQENRDLQLQCLQQKQQLHELQNRMKFFNQESDINVDDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDHELKVEQYVHLLDVRAARIQKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVAFASDVLRASGDKELLTFCTYAFYDFELQTTPIVRGPCPEYNFTSQYLVHVNDLFLQYIQKNTVTLELHQAYSTDYETVAACQLRFHEILEKSGRIFCTTSLVGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKKPEKMQLLSQQAATTAQISSPESTDGNLNELHITVRCCTNLQSRARHLQPHAYVVYKFFDFPDHDTAIIPSSNDPQFDDYMCFPVPMNMDLDRYLKSESLSFYVFDDSDIQENIYIGKVNVPLISLAHDRCISGIFELMDKDKHAAGTIQVILKWKFTYLPPSGSIPTEDLGRFVGREEPEAIQRRPPTSSGTEAVVTPKPKPRQRLTFVDKKVSFVDTMPHPSPEASPPPKDIKHNSPEVGPETENSMPAVACPSKESSVAKVEENMGKTQQGKEDDISFLSEGQLASQSVASSEDETEITEELEPEDEDRSASDSDDCIIPSSVSTDTKKPSEEIRIEIIALSLNDSQITREDTVQRLFIECRFYSLPAEETPMSLPKPKSGQWVYYNYTHVLYLDKENNPAVRDVLKAVLQRRELPHRSVRFTVVSDPPEDEQDLECEDIGVAHLDLVDVFQKGRDIIEQDIDVLDARTDGGSIGKLKVTVEALHALRSVYEQYRKDLEA
Protein: Secretin (P09683)
Organism: Homo sapiens (Human)
Function: Hormone involved in different processes, such as regulation of the pH of the duodenal content, food intake and water homeostasis. Exerts its biological effects by binding to secretin receptor (SCTR), a G-protein coupled receptor expressed in the basolateral domain of several cells. Acts as a key gastrointestinal hormone by regulating the pH of the duodenal content (By similarity). Secreted by S cells of the duodenum in the crypts of Lieberkuehn and regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas (By similarity). Production of bicarbonate is essential to neutralize the pH and ensure no damage is done to the small intestine by the gastric acid (By similarity). In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation (Probable). Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation (By similarity). Also able to stimulate lipolysis in white adipocytes (By similarity). Also plays an important role in cellular osmoregulation: released into the systemic circulation in response to hyperosmolality and acts at different levels in the hypothalamus, pituitary and kidney to regulate water homeostasis (By similarity). Also plays a role in the central nervous system, possibly by acting as a neuropeptide hormone: required for hippocampal synaptic function and neural progenitor cells maintenance (By similarity).
Subcellular location: Secreted {ECO:0000269|Ref.2}.
Interaction partners:
- Secretin receptor
- VIP peptides
- Pro-glucagon
- Pituitary adenylate cyclase-activating polypeptide
- Gastrin
- Gastric inhibitory polypeptide
- Guanine nucleotide-binding protein G
- Somatoliberin
- Glucagon-like peptide 1 receptor
- Somatostatin
Sequence:
MAPRPLLLLLLLLGGSAARPAPPRARRHSDGTFTSELSRLREGARLQRLLQGLVGKRSEQDAENSMAWTRLSAGLLCPSGSNMPILQAWMPLDGTWSPWLPPGPMVSEPAGAAAEGTLRPR
Protein: Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5) (U3I7D9)
Organism: Anas platyrhynchos platyrhynchos (Northern mallard)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000256|HAMAP-Rule:MF_03205}.
Interaction partners:
- Fatty acid desaturase 1
- Elongation of very long chain fatty acids protein 6
- 3-ketoacyl-CoA reductase
- Elongation of very long chain fatty acids protein
- Cytochrome b5 heme-binding domain-containing protein
- Cytochrome b5 heme-binding domain-containing protein
- Very-long-chain enoyl-CoA reductase
- Very-long-chain
- Very-long-chain
- Elongation of very long chain fatty acids protein 7
Sequence:
MTGKDYRMERLDKTINSYLDVWLGPRDPRVKGWLLLENYTPTFIFSVLYLLIVWLGPKYMRNKQPFSCRGILVVYNLGLTLLSLYMFYELVTGVWEGGYNFFCQDTHSGGEADMKIIRVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYHHATMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSAVPAMRPYLWWKKYITQGQLTQFVLTIFQTSCGVVWPCAFPQGWLYFQISYMISLIILFTNFYIQTYNKKASSRRKEYQNGSAATVNGYTNSFSSLENNVKQRKQRKD
Protein: Metacaspase-3 (EC 3.4.22.-) (PfMCA3) (Q8ILT4)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Protease that cleaves specifically after arginine or lysine residues.
Interaction partners:
- Thioredoxin-like protein
Sequence:
MVYNNGSLRGRKKIEEKYIPMNRKSTSLKDPSRTKNNNYIKTLDTYINEEDSPTKILSKGKKNKNENIKKRINEKDNDTDREDAASLNVDYNKNVMKKYNTRGTFIEKVSSSERNIEHNNNIIRKLGSKDYSKARVQTMTTNIGNHNALKKINPKVPSITSRTKSYTKVMNENKYNNNNSNNSNNNNINSMYYSKKLNNKKYSTEHTQSIDNNNITSKRLNNKKTATDKAQSTSRYCISNSVKKSYSTKGYNTDRSQTMSRYTLQNKKDSNTNTNRKGYSTHRGQIIQDNSNINNQAEKKKRNMSLKKKYIKESSNSTITGSNEKKNSNNILKKNSTCDLNYLNKEYNNNNNMHEHAENVYNINDNEGCSSMQIINDEDVQKNVPEFYTINLGSETKNMGENYIFKNRDKKIKPNIYNERNNMDLMEHKLNDDMSYNFADHIKDIECYINQLNESNKCNIYKECDPSKLISPVYDNVNDNILENNQQLNEYEKHNDILTTSYLKYYSHTNNNNHYYNDEDVHLDLGKTNEGFSNVVKNMDNIPWNETNKKESFSNIKKKIDHTDDRHIAYVDNSSMKHTMNDKDQYVKNVPYNNTMEEVLLLNEKRGNILGSLISKNHDAKRATSNNNNINNNKYYYYDNKYSEHGGDSVSSNIGYPHGYKNNNIYNYVNNIKDLSSPLYCNTKTKRAHKFHTDNIMSDQLNKYEDNNKNDGKFFSGNISSKQKGKNNLTNYTTHSSEYRIKSIESNLTKDYRKSLTYNDIPNFLDYNINNTNVQNSDFGDSHYINRNVSYKNSMNSNDDIQNSNNNNNNNNNNNMVNNPNEYLVYTNEKHYVRINNKLYEKTRDNTYIEVDSNSNFDIINDINSSHNSPLDNIKDNTLYHNTNKKEYSDYVSSYSNINKYEDINLPNNIHVSKDGKYLFKNYSVSQNVSDDNSVQDSFFSRTERSNSQNRYDKNGVNHIEQNYYNNSNRRDDIYYYHNQLKKLERLTQQNIKSGKYQRNIPQNDDNDHNDDDSEIKEVKKDKTKIDMNKHLHLNDKKIFNQVKRENTGVHMNASKTIKNMKEVTYRNINNDTNYNNNNVKINYLYSDELGKNKNRDTPLKTKQHGDSLDNKTELKKKIYNDIINNDIINNNIINNDIIKSGAINNNIVNNNLINNYNADNRNVSNSIFTQHINNINNNFYNSDDERINIIDNNKRMDMTKDESDRFRNNYFVELEKRKKNLGKTNNTTPISLSKNETINNMMINKRNFFNNYISDKVRDKILKREISCSVNTVCSSKTNNKTNSNYSSNNNNDNNNNNNNSNPFILDNSIRKSNIIITTSNNAKLINNTIISKGINNNILNINSNKNKSLNSAKINALGLLSSRNDLNYIMNNNRTSNNHINQHLLYNNRNYSVIKIPNVHKEKRSSKIPHNINIKSNLNLEPNIKTYTNIKTPINIKAYTNIKAPTNIKAPINIKASTNIKAPTNVKAPTNVKAPTNVKAPTNVNAPTNVNAPTNANAPTYVNTPTNIKRQEFSNVTLNYKGISKFDINEDKNTTIIPPLHRQSNSNFPFKNTKLNLNSDMYTEKELIKCKSINNSDIYNYLRNTYNKTPSKFYRTVSYRNMSLKKNKSMLENRKRKTEKKEENLMSTFNYTSEVDSKYIVKKAVVVGCNYVSEERSRLYGSVNDAYVFCRALVKYFDFLPENILLLTDSLPSNAYIYEDFDINRKKYINVDEEENIKNNEPLKKKNIFNLFNTNALYTTLKKTNEEELNCNSCKDVEIKNVDISSEKMNFNLWPTRVNILKAVNWLVRDSIPFGSYVFYFAGKSVQVDNMSGWEGEGYDEAFLCSDPFNKISEHNVITAVQLKDLLLSINESAQMTIILDCSGGQTILDPAGTENSLSYIKGCKQKGIWPITNPTNKVHKAIYDITILNNTSMKKYFCRSRYSKLIEVESTSAMIDPLLQSISSLPVAPKAYCLCAATWEQISIEGLFPIIEFARVSQLKKPESYKTGEGHYQNMNKKNIRAEKSNRNGPNGLINKNNNLSKKTNYEKNFNFTLNMMKMLFSNTNNNENKLDEKEKINRLGFNENDSDYIDDNYNSDDNNNNNYYYNYDGEKGFKNFQENLNNVGQKDVIKNKKFKDNYILVSHGVFTYCLIEAIIEFKEKELKYNILEKKNEQFIPMTLKNLINVIQQKMQNIKYNKLKKINQKPEFTIHPGANATNNNYFVHYSKNIHFQNYKCNFINADLSPFLNVNKAWEEINRTTLRNRKSLSLSSTLINTASSKYFTQKNEQFKNSYSLKY
Protein: GDSL esterase/lipase APG (EC 3.1.1.-) (Extracellular lipase APG) (Q9LU14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase BRI1-like 2
- GDSL esterase/lipase At5g62930
- At1g62510
- GDSL esterase/lipase
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- At2g10940/F15K19.1
Sequence:
MDRCTSSFLLLTLVSTLSILQISFAQLVPAIMTFGDSVVDVGNNNYLPTLFRADYPPYGRDFANHKATGRFCNGKLATDITAETLGFTKYPPAYLSPEASGKNLLIGANFASAASGYDDKAALLNHAIPLYQQVEYFKEYKSKLIKIAGSKKADSIIKGAICLLSAGSSDFVQNYYVNPLLYKVYTVDAYGSFLIDNFSTFIKQVYAVGARKIGVTSLPPTGCLPAARTLFGFHEKGCVSRLNTDAQNFNKKLNAAASKLQKQYSDLKIVVFDIYSPLYDLVQNPSKSGFTEATKGCCGTGTVETTSLLCNPKSFGTCSNATQYVFWDSVHPSEAANEILATALIGQGFSLLG
Protein: Receptor-interacting serine/threonine-protein kinase 4 (EC 2.7.11.1) (Ankyrin repeat domain-containing protein 3) (PKC-associated protein kinase) (PKC-regulated protein kinase) (Q9ERK0)
Organism: Mus musculus (Mouse)
Function: Involved in stratified epithelial development (By similarity). It is a direct transcriptional target of TP63. Plays a role in NF-kappa-B activation.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein. Note=At steady state, a minor portion of this protein is membrane-associated. The major portion is cytoplasmic.
Interaction partners:
- WD repeat-containing protein 90
- Keratinocyte differentiation factor 1
- Interferon regulatory factor 6
Sequence:
MEGEGRGRWALGLLRTFDAGEFAGWEKVGSGGFGQVYKVRHVHWKTWLAIKCSPSLHVDDRERMELLEEAKKMEMAKFRYILPVYGICQEPVGLVMEYMETGSLEKLLASEPLPWDLRFRIVHETAVGMNFLHCMSPPLLHLDLKPANILLDAHYHVKISDFGLAKCNGMSHSHDLSMDGLFGTIAYLPPERIREKSRLFDTKHDVYSFAIVIWGVLTQKKPFADEKNILHIMMKVVKGHRPELPPICRPRPRACASLIGLMQRCWHADPQVRPTFQEITSETEDLCEKPDEEVKDLAHEPGEKSSLESKSEARPESSRLKRASAPPFDNDCSLSELLSQLDSGISQTLEGPEELSRSSSECKLPSSSSGKRLSGVSSVDSAFSSRGSLSLSFEREASTGDLGPTDIQKKKLVDAIISGDTSRLMKILQPQDVDLVLDSSASLLHLAVEAGQEECVKWLLLNNANPNLTNRKGSTPLHMAVERKGRGIVELLLARKTSVNAKDEDQWTALHFAAQNGDEASTRLLLEKNASVNEVDFEGRTPMHVACQHGQENIVRTLLRRGVDVGLQGKDAWLPLHYAAWQGHLPIVKLLAKQPGVSVNAQTLDGRTPLHLAAQRGHYRVARILIDLCSDVNICSLQAQTPLHVAAETGHTSTARLLLHRGAGKEALTSEGYTALHLAAQNGHLATVKLLIEEKADVMARGPLNQTALHLAAARGHSEVVEELVSADLIDLSDEQGLSALHLAAQGRHSQTVETLLKHGAHINLQSLKFQGGQSSAATLLRRSKT
Protein: Alpha-methylacyl-CoA racemase (EC 5.1.99.4) (2-arylpropionyl-CoA epimerase) (2-methylacyl-CoA racemase) (P70473)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters. Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), and arylpropionic acids like the anti-inflammatory drug ibuprofen (2-(4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor linear-chain acyl-CoAs.
Subcellular location: Peroxisome {ECO:0000269|PubMed:11060359}. Mitochondrion {ECO:0000269|PubMed:11060359, ECO:0000269|PubMed:7649182}.
Interaction partners:
- Hydroxysteroid dehydrogenase-like protein 2
- Peroxisomal multifunctional enzyme type 2
- Peroxisomal acyl-coenzyme A oxidase 2
- 2-hydroxyacyl-CoA lyase 1
- Peroxisomal acyl-coenzyme A oxidase 3
- Iodotyrosine deiodinase 1
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Peroxisomal bifunctional enzyme
- 2-hydroxyacyl-CoA lyase 2
- Riboflavin kinase.
Sequence:
MALRGVRVLELAGLAPGPFCGMILADFGAEVVLVDRLGSVNHPSHLARGKRSLALDLKRSPGAAVLRRMCARADVLLEPFRCGVMEKLQLGPETLRQDNPKLIYARLSGFGQSGIFSKVAGHDINYVALSGVLSKIGRSGENPYPPLNLLADFGGGGLMCTLGILLALFERTRSGLGQVIDANMVEGTAYLSTFLWKTQAMGLWAQPRGQNLLDGGAPFYTTYKTADGEFMAVGAIEPQFYTLLLKGLGLESEELPSQMSIEDWPEMKKKFADVFARKTKAEWCQIFDGTDACVTPVLTLEEALHHQHNRERGSFITDEEQHACPRPAPQLSRTPAVPSAKRDPSVGEHTVEVLKDYGFSQEEIHQLHSDRIIESNKLKANL
Protein: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) (P00362)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:9175858}.
Interaction partners:
Sequence:
MAVKVGINGFGRIGRNVFRAALKNPDIEVVAVNDLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVISNASCTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDLPHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYSHRVVDLAAYIASKGL
Protein: DNA helicase (EC 3.6.4.12) (Q381H2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cell division cycle 45
- GINS subunit domain-containing protein
- Uncharacterized protein
- GINS subunit domain-containing protein
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- DNA replication complex GINS protein SLD5
- Minichromosome maintenance
- Protein MCM10 homolog
Sequence:
MADGPTQEQTKKAAFAVAATSKYPNYLADRDLCRRFFEEFRDASGGMKYMDMAARVARRETNVFTVDLDDIQLYGQLYLAQRIQMNVMGYREEVYRVVDEIIPEAYFEEDMIDHLILEAQTAGQHLPPLLTRRYELVVMPLTSFSEPVPLRQLKGGLIGTLVVLRGICIAATAVRPKLSMLVSVCEVCAETTFQQVIGDRLTPLMVCQSQRCRLNNTVGRLLPQYKASKFTKHQELRLQELPQYVPRGAIPRTIRVICEGEQTRIATPGQVVKVVGTYCPDPSTGQGHEAFRASTMVKTLFRALRIELERRSYQEAADDLKIQVDNVKQHPDKEVVIEKLTRSVAPEIWGMEDVKKALLCLLVGGSSIANGIRIRSDTNICLMGDPGVAKSQLLKWIASVAPRSIFTTGKGSSGVGLTAAVTRDTYTGEVMLEGGALVLSDRGICCIDEFDKMDDSDRTALHEVMEQQMVSIAKAGIITSLNARTSILAAANPKYGRWRRNLTPSENVNLPPALLSRFDVLWLLLDESNRERDAELSMHVTYVHLHGVAPGTVSDNGFYGLSSDYFGKDFLQAYVGEAKKIHPIVDSSAAKVISDIYCEMRAQSVRHTNVVTARTLLSIIRLSQACARLRFSDRVVEADVREAGRLLDCSKISLQERVDTGGRRMVTTSDAAIFSTIKELARSRGSIDLAEVRPALMIKGIDESHLQRCLNTYADVGVWEVSGNTVHFSLE
Protein: Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23) (OMP decarboxylase) (OMPDCase) (OMPdecase) (Uridine 5'-monophosphate synthase) (UMP synthase) (O13410)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Orotate phosphoribosyltransferase
- Uridylate kinase
- Uridine kinase
- uracil phosphoribosyltransferase
- uracil phosphoribosyltransferase
- ATP-dependent DNA helicase II subunit 2
- Dihydroorotate dehydrogenase
- C2H2 type master regulator of conidiophore development brlA
- Secondary metabolism regulator laeA
- Got1 family protein
Sequence:
MSSKSQLTYGARASKHPNPLAKRLFEIAEAKKTNVTVSADVTTTRELLDLADRLGPYIAVIKTHIDILTDFSVDTINGLNVLAQKHNFLIFEDRKFIDIGNTVQKQYHGGALRISEWAHIINCSVLPGEGIVEALAQTASAQDFPYGPERGLLVLAEMTSKGSLATGEYTKASVDYARKYKNFVMGFVSTRALTEVQSDVSSASEDEDFVVFTTGVNLSSKGDKLGQQYQTPASAIGRGADFIIAGRGIYAAPDPVEAAQRYQKEGWEAYMARVCGKS
Protein: Adiponectin receptor protein 2 (Progestin and adipoQ receptor family member 2) (Progestin and adipoQ receptor family member II) (Q8BQS5)
Organism: Mus musculus (Mouse)
Function: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism. Required for normal body fat and glucose homeostasis. ADIPOQ-binding activates a signaling cascade that leads to increased PPARA activity, and ultimately to increased fatty acid oxidation and glucose uptake. Has intermediate affinity for globular and full-length adiponectin. Required for normal revascularization after chronic ischemia caused by severing of blood vessels.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q86V24}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86V24}. Note=Localized to the cell membrane and intracellular organelles. {ECO:0000250|UniProtKB:Q86V24}.
Interaction partners:
- Adiponectin
- DCC-interacting protein 13-alpha
- Adiponectin receptor protein 1
- Cadherin-13
- Leptin
- Nicotinamide phosphoribosyltransferase
- Resistin
- Peroxisome proliferator-activated receptor alpha
- Resistin-like gamma
- DCC-interacting protein 13-beta
Sequence:
MNEPAKHRLGCTRTPEPDIRLRKGHQLDDTRGSNNDNYQGDLEPSLETPVCSSYYENSPEEPECHDDNSQEDEGFMGMSPLLQAHHAMERMEEFVCKVWEGRWRVIPHDVLPDWLKDNDFLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGCVFFLCLGIFYMFRPNISFVAPLQEKVVFGLFFLGAILCLSFSWLFHTVYCHSEGVSRLFSKLDYSGIALLIMGSFVPWLYYSFYCNPQPCFIYLIVICVLGIAAIIVSQWDMFATPQYRGVRAGVFVGLGLSGIIPTLHYVISEGFLKAATIGQIGWLMLMASLYITGAALYAARIPERFFPGKCDIWFHSHQLFHIFVVAGAFVHFHGVSNLQEFRFMIGGGCTEEDAL
Protein: DNA repair protein REV1 (EC 2.7.7.-) (Rev1-like terminal deoxycytidyl transferase) (Q920Q2)
Organism: Mus musculus (Mouse)
Function: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA polymerase zeta catalytic subunit
- Mitotic spindle assembly checkpoint protein MAD2B
- DNA polymerase eta
- DNA polymerase kappa
- DNA polymerase iota
- Proliferating cell nuclear antigen
- E3 ubiquitin-protein ligase RAD18
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-C
- Polyubiquitin-B
Sequence:
MRRGGWRKRTENDGWEKWGGYMAAKVQKLEEQFRTDAANQKDGTASAIFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSSAPYQLYTKPSAAQKSLNFNPVCKPEDPGPGPSNRAKQLNNRVNHIIKKIETESEVKANGLSSWNEDGVNDDFSFEDLEHTFPGRKQNGVMHPRDTAVIFNGHTHSSNGALKTQDCLVPVGNSVASRLSLDSTQEEKRAEKSNADFRDCTVQHLQHSTRSADALRSPHRTNSLSPSLHSNTKINGAHHSTVQGPSSTKSTSVLTLSKVAPSVPSKPSDCNFISDFYSRSRLHHISTWKCELTEFVNTLQRQSSGIFPGREKLKKVKTGRSSLVVTDTGTMSVLSSPRHQSCVMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTAPLRPGANPQLEWQYYQNRALRGKAADIPDSSVWENQDSTQTNGIDSVLSKAEIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKIMVRKPGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQLVPANSNLSTCSSRPSAQSSLFSGRPHSVRDLFQLQKAKKPTEEEHKEVFLAAVDLEVSSTSRACGLLSPLSAHLAASVSPDTNSGECSRKWNGLHSPVSGQSRLNLSIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQGEPRGKKKEPVNGCSSGVLPHPVGTVLLQIPEPQEPCNSDSKISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQRQGEDTTHQQPTSTSVPKNPLLQLKPPAMKDKRNKRKNLIGSPRKSPLKNKLLSSPAKTLPGAYGSPQKLMDGFLQHEGMASERPLEEVSASTPGAQDLSSLLPGQSSCFRPAAPNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
Protein: CLAVATA3/ESR (CLE)-related protein 17 [Cleaved into: CLE17p] (Q8L9H6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.
Subcellular location: [CLE17p]: Secreted, extracellular space {ECO:0000250|UniProtKB:O49519}.
Interaction partners:
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
Sequence:
MTHVLVRRQGQGKKRRWDVNMTMCFFLFFFVFYVSFQIVLSSSASVGYSRLHLVASPPPPPPRKALRYSTAPFRGPLSRDDIYGDDKRVVHTGPNPLHN
Protein: Cytokine receptor-like factor 3 (Cytokine receptor-like molecule 9) (CREME-9) (Cytokine receptor-related protein 4) (Type I cytokine receptor-like factor p48) (Q8IUI8)
Organism: Homo sapiens (Human)
Function: May play a role in the negative regulation of cell cycle progression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19427400}. Note=The EGFP- and MYC-tagged protein has been shown to be cytoplasmic. {ECO:0000269|PubMed:19427400}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 6 homolog
- Leucine-rich repeat-containing protein 37B
- Arf-GAP with dual PH domain-containing protein 2
- Transcription elongation factor
Sequence:
MRGAMELEPELLLQEARENVEAAQSYRRELGHRLEGLREARRQIKESASQTRDVLKQHFNDLKGTLGKLLDERLVTLLQEVDTIEQETIKPLDDCQKLIEHGVNTAEDLVREGEIAMLGGVGEENEKLWSFTKKASHIQLDSLPEVPLLVDVPCLSAQLDDSILNIVKDHIFKHGTVASRPPVQIEELIEKPGGIIVRWCKVDDDFTAQDYRLQFRKCTSNHFEDVYVGSETEFIVLHIDPNVDYQFRVCARGDGRQEWSPWSVPQIGHSTLVPHEWTAGFEGYSLSSRRNIALRNDSESSGVLYSRAPTYFCGQTLTFRVETVGQPDRRDSIGVCAEKQDGYDSLQRDQAVCISTNGAVFVNGKEMTNQLPAVTSGSTVTFDIEAVTLGTTSNNEGGHFKLRVTISSNNREVVFDWLLDQSCGSLYFGCSFFYPGWKVLVF