wanglab/gogpt-training-data huggingface dataset:
Protein: GTPase ObgE/CgtA (EC 3.6.5.-) (GTP-binding protein Obg) (Large ribosomal subunit assembly factor ObgE) (P42641)
Organism: Escherichia coli (strain K12)
Function: An abundant, essential GTPase which binds GTP, GDP and ppGpp with moderate affinity. Has high guanosine nucleotide exchange rate constants for GTP and GDP, and a relatively low GTP hydrolysis rate stimulated by the 50S ribosomal subunit. It is estimated there are 34000 molecules in log-phase cells and 5600 molecules in stationary-phase cells. Required for chromosome segregation. Plays a role in the stringent response, perhaps by sequestering 50S ribosomal subunits and decreasing protein synthesis, and a non-essential role in the late steps of ribosome biogenesis, perhaps acting as a checkpoint for correct 50S subunit synthesis (Probable). Overexpression increases bacterial persistence (in exponential and stationary phase) in response to antibiotics. Cells expressing high levels of Obg are more likely to form persister cells upon antibiotic exposure; this requires alarmone (p)ppGpp and acts via induced HokB, depolarizing cells, which probably reduces metabolic activity and induces persistence. The persister phenotype can be separated from the essential phenotype.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:15292126, ECO:0000269|PubMed:33639093}. Note=Low amounts associate with pre-50S ribosomal subunits (PubMed:15292126, PubMed:33639093). Another group also sees association with 30S subunit (PubMed:15836769). {ECO:0000269|PubMed:15292126, ECO:0000269|PubMed:15836769, ECO:0000269|PubMed:33639093}.
Interaction partners:
- Ribosomal silencing factor RsfS
- Ribosomal large subunit pseudouridine synthase D synthase)
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein bL20
- GTPase Der
- Uncharacterized inner membrane transporter YhbE
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL32
Sequence:
MKFVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGKRGKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLADVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVLLHLIDIDPIDGTDPVENARIIISELEKYSQDLATKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWEDKYYLISAASGLGVKDLCWDVMTFIIENPVVQAEEAKQPEKVEFMWDDYHRQQLEEIAEEDDEDWDDDWDEDDEEGVEFIYKR
Protein: U1 small nuclear ribonucleoprotein component SNU71 (P53207)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- U2 small nuclear ribonucleoprotein A'
- Protein LUC7
- Splicing factor MUD2
- Pre-mRNA-processing factor 39
- U1 small nuclear ribonucleoprotein A
- U1 small nuclear ribonucleoprotein 70 kDa homolog
- Pre-mRNA-processing protein PRP40
- Nuclear cap-binding protein subunit 2
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- Protein NAM8
Sequence:
MRDIVFVSPQLYLSSQEGWKSDSAKSGFIPILKNDLQRFQDSLKHIVDARNSLSETLLNSNDDGSIHNSDQNTGLNKDKEASIADNNSANKCATSSSRYQELKQFLPISLDQQIHTVSLQGVSSSFSRGQIESLLDHCLNLALTETQSNSALKVEAWSSFSSFLDTQDIFIRFSKVDEDEAFVNTLNYCKALFAFIRKLHEDFKIELHLDLNTKEYVEDRTGTIPSVKPEKASEFYSVFKNIEDQTDERNSKKEQLDDSSTQYKVDTNTLSDLPSDALDQLCKDIIEFRTKVVSIEKEKKMKSTYEESRRQRHQMQKVFDQIRKNHSGAKGSANTEEEDTNMEDEDEEDDTEDDLALEKRKEERDLEESNRRYEDMLHQLHSNTEPKIKSIRADIMSAENYEEHLEKNRSLYLKELLHLANDVHYDHHRSFKEQEERRDEEDRAKNGNAKELAPIQLSDGKAISAGKAAAITLPEGTVKSENYNADKNVSESSEHVKIKFDFKKAIDHSVESSSEDEGYRESELPPTKPSERSAAEDRLPFTADELNIRLTNLKESRYVDELVREFLGVYEDELVEYILENIRVNQSKQALLNELRETFDEDGETIADRLWSRKEFRLGT
Protein: p44-79 outer membrane protein (Q2GIE6)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MKALSYGKLFWRVCVILSLAMLMTGNSAYAEQDSKISSHSNSKRDGYFYVGLDYSPTFVNIKNFSIGESSGGTKGIYPYLRDGDVVKLEAGRFDWNRPDPWIGFDDNMFVTMGGSAGYGMGNTRIEVEIGYERFKTKGTKGSRDTEDYADTVYLLAKDLAYNVASGKASNLAVALAGVSGKEIVGFADSLKEKHPGIDRQICKRVKGALRRGLLQDDEKAGNCDTGVGTHTVVIKKTEGAQQQQRISLQPYSGPLGLRASLGGRGVEKWPRINNRHSGHVYSSSFLKKAGIVQKDSSGYSYQRDASGTVANDIKELYSEAREIVAKLFLTAIEGAEVIEIKGISSTSFIVNVCSDIVADDFVAVPYACLGLGGNIIEFVEGRSDLRPAYKLKVGLSYQLSQKVNAFADVFYHRVLGNGEYSDLPVRHLVDDHSPEGRSKNAATANFSMKYTGAELGIQLRF
Protein: Zinc finger protein 3 (Zinc finger protein HF.12) (Zinc finger protein HZF3.1) (Zinc finger protein KOX25) (P17036)
Organism: Homo sapiens (Human)
Function: Involved in cell differentiation and/or proliferation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-2
- NADPH oxidase 4
Sequence:
METQADLVSQEPQALLDSALPSKVPAFSDKDSLGDEMLAAALLKAKSQELVTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSLDRETRTENDQEISEDTRSHGVLLGRFQKDISQGLKFKEAYEREVSLKRPLGNSPGERLNRKMPDFGQVTVEEKLTPRGERSEKYNDFGNSFTVNSNLISHQRLPVGDRPHKCDECSKSFNRTSDLIQHQRIHTGEKPYECNECGKAFSQSSHLIQHQRIHTGEKPYECSDCGKTFSCSSALILHRRIHTGEKPYECNECGKTFSWSSTLTHHQRIHTGEKPYACNECGKAFSRSSTLIHHQRIHTGEKPYECNECGKAFSQSSHLYQHQRIHTGEKPYECMECGGKFTYSSGLIQHQRIHTGENPYECSECGKAFRYSSALVRHQRIHTGEKPLNGIGMSKSSLRVTTELNIREST
Protein: Ferritin light chain 1 (Ferritin L subunit 1) (P29391)
Organism: Mus musculus (Mouse)
Function: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25327288}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:25327288}. Autolysosome {ECO:0000269|PubMed:25327288}.
Interaction partners:
- Ferritin heavy chain
- Scavenger receptor class A member 5
- Nuclear receptor coactivator 4
- Ferroportin
- Natural resistance-associated macrophage protein 2
- Iron-responsive element-binding protein 2
- Transferrin receptor protein 1
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Hepcidin
- Cytoplasmic aconitate hydratase
Sequence:
MTSQIRQNYSTEVEAAVNRLVNLHLRASYTYLSLGFFFDRDDVALEGVGHFFRELAEEKREGAERLLEFQNDRGGRALFQDVQKPSQDEWGKTQEAMEAALAMEKNLNQALLDLHALGSARTDPHLCDFLESHYLDKEVKLIKKMGNHLTNLRRVAGPQPAQTGAPQGSLGEYLFERLTLKHD
Protein: RNA binding motif protein 15 (A0A494C001)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKGKERSPVKAKRSRGGEDSTSRGERSKKLGGSGGSNGSSSGKTDSGGGSRRSLHLDKSSSRGGSREYDTGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSAPGGGDGAEYKTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVLYDRPLKIEAVYVSRRRSRSPLDKDTYPPSASVVGASVGGHRHPPGGGGGQRSLSPGGAALGYRDYRLQQLALGRLPPPPPPPLPRDLERERDYPFYERVRPAYSLEPRVGAGAGAAPFREVDEISPEDDQRANRTLFLGNLDITVTESDLRRAFDRFGVITEVDIKRPSRGQTSTYGFLKFENLDMSHRAKLAMSGKIIIRNPIKIGYGKATPTTRLWVGGLGPWVPLAALAREFDRFGTIRTIDYRKGDSWAYIQYESLDAAHAAWTHMRGFPLGGPDRRLRVDFADTEHRYQQQYLQPLPLTHYELVTDAFGHRAPDPLRGARDRTPPLLYRDRDRDLYPDSDWVPPPPPVRERSTRTAATSVPAYEPLDSLDRRRDGWSLDRDRGDRDLPSSRDQPRKRRLPEESGGRHLDRSPESDRPRKRHCAPSPDRSPELSSSRDRYNSDNDRSSRLLLERPSPIRDRRGSLEKSQGDKRDRKNSASAERDRKHRTTAPTEGKSPLKKEDRSDGSAPSTSTASSKLKSPSQKQDGGTAPVASASPKLCLAWQGMLLLKNSNFPSNMHLLQGDLQVASSLLVEGSTGGKVAQLKITQRLRLDQPKLDEVTRRIKVAGPNGYAILLAVPGSSDSRSSSSSAASDTATSTQRPLRNLVSYLKQKQAAGVISLPVGGNKDKENTGVLHAFPPSKLVEQRMKIWNSKL
Protein: Tyrosine-protein kinase ABL2 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 2) (Abelson tyrosine-protein kinase 2) (Abelson-related gene protein) (Tyrosine-protein kinase ARG) (Q4JIM5)
Organism: Mus musculus (Mouse)
Function: Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL or DOK1. Required for adhesion-dependent phosphorylation of ARHGAP35 which promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11752434}.
Interaction partners:
- Abl interactor 1
- Abl interactor 2
- Tyrosine-protein kinase ABL1
- Adapter molecule crk
- Transcription factor ETV6
Sequence:
MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTADAGFNVFTQHDHFASCVEDGFEGDKTGGSSPEVLHRPFGCDAESQALNEAIRWSSKENLLGATESDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNQNGEWSEVRSKNGQGWVPSNYITPVNSLEKHSWYHGPVSRSAAEYLLSSLINGSFLVRESESSPGQLSISLRYEGRVYHYRINTTTDSKVYVTAESRFSTLAELVHHHSTVADGLVTTLHYPAPKCNKPTVYGVSPIHDKWEMERTDITMKHKLGGGQYGEVYVGVWKKYSLTVAVKTFKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTLEPPFYIVTEYMPYGNLLDYLRECSREEVTAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHVVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNTFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYDLLEKGYRMEQPEGCPPKVYELMRACWKWSPADRPSFAETHQAFETMFHDSSISEEVAEELGRTASSSSVVPYLPRLPLLPSKTRTLRKQGENKENLDGGLDAAESLASSSAPAGFIRSTQASSGSPALPRKQRDKSPSSLLEDAKETCFTRDRKGGFFSSFMKKRNAPTPPKRSSSFREMENQPHKKYELTGNFSPVASLQNADGFSVAPSQQEPNLVPAKCYGGSFAQRNLCADDDSGGGGGSGTAGGGWSGITGFFTPRLIKKTLGLRAGKPTASDDTSKPFPRSNSTSSMSSGLPEQDRMAMTLPRNCQRSKLQLERTVSTSSQPEENVDRANDMLPKKSEEGAAPARERPKAKLLPRGATALPLRAPDPAITESDSPGVGVAGVAAAPKGKERNGGTRLGVAGVPEDGEQLGWSSPAKAVAVLPTTHNHKVPVLISPTLKHTPADVQLIGTDSQGNKFKLLSEHQVTSSGDKDRPRRVKPKCAPPPPPVMRLLQHPSTCSDPEEEPTAPPAGQHTPETQEGGKKAAPGPVPSSGKPGRPVMPPPQVPLPTSSISPAKMANGTAGTKVALRKTKQAAEKISADKISKEALLECADLLSSAITEPVPNSQLVDTGHQLLDYCSGYVDSIPQTRNKFAFREAVSKLELSLQELQVSSTAAGVPGTNPVLNNLLSCVQEISDVVQR
Protein: LD41913p (Q9VW28)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- EG:BACR42I17.11 protein
- LP13385p
Sequence:
METLPCANQLQEHQQPQQQHVNLSIDPSLGENVVSIPKELILISLVSQEQSLYNPKHPHYRSTKIKDEKWLEIGSNVGWSDVQCKSKWKAMRDQYCRELKRAKACSKAVKWKYFKELDFLRPYALARNYRGRSGQTSNGAVGTVTPLSLPMTTSFSSNSSSQNLNLSGSIKIEDASASTLLDSCSFSSPSSTDKKPAATFLASHIGAVLQQQQQQQQHQQQMHSQPEANWNYLTDAGGGATPSIIVQCGTANTTTVVDTLYNEIVDCVNAANQSSSAATITSNVSTTSAAHNQSTNAEEEDDDPIHTFLNMESYFEKELITLIQQEDMIYNYGNENYRNAKLKMEVWEEIARKLKKSVKQCRLKWKALRDQYAREHKRLRTLMHIDATSRWKHYNSLSFLQKYIQQKTLESDSQLSMLLPKNDPVRELEDHMTQSHSPPTQQITLESSSSNSQLNLPTLPHLTGPHKAEQQQQQQQQEEQHQQQQQHQQQQQQQQASELCVATYDDMDIENYINGDVHHNDDDVEDDEDEEMETTTAAEQPPQQQDQHVMTYDHEDGPVYMAVPSVGSAMSKQEQLSDGATSLENQQLQSTAEFQKIEIQTPTTPRYQNAATTPSSTSTSRYHSAPITPSKPTHMEYPSSNGHNSGEDDEIGAFFKAVSMKIRNAQLEPVAFTELQIDILRVINEALRNH
Protein: Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 (EC 2.4.1.88) (Forssman glycolipid synthase) (Q95158)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Catalyzes the formation of Forssman glycolipid via the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to GalNAcb-1,3Gala-1,4Galb-1,4GlcCer (Gb4Cer). Forssman glycolipid (also called Forssman antigen; FG) probably serves for adherence of some pathogens such as E.coli uropathogenic strains.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Hexosyltransferase.
- Alpha-galactosidase.
- Beta-hexosaminidase.
- Hexosaminidase subunit beta.
Sequence:
MRCRRLALGLGFSLLSGIALWSLWIYMETWLPFSYVPYYLPCPEIFNMKLQYKGEKPFQPVTRSPHPQPKLLEQRPTELLTLTPWLAPIVSEGTFNPELLQHIYQPLNLTIGLTVFAVGKYTRFVQHFLESAEQFFMQGYQVYYYIFTNDPAGIPRVPLGPGRLLSIIPIQRHSRWEEISTRRMETISRHIAQRAHREVDYLFCVDVDMVFRNPWGPETLGDLVAAIHPGYYAVPRQQFPYERRHISTAFVAENEGDFYYGGAVFGGRVAKVYEFTTGCHMAILADKANGIMAAWQEESHLNRRFISHKPSKVLSPEYLWDDRKPQPPSLKLIRFSTLDKATSWLRS
Protein: GM01240p (Q8T9L6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCPAVLSFKINQKPYPRLLNFTTNEYILCLQTGELNEYTERSEMPAEIMCMALGTVPEGEQRSWFLAVGLADNTVRILSLDPNNCLTPCSMQALPSPAESLCLVEMGHTESTTQGGLDDDAPAQRSGNNKGTIYLNIGLSNGVLLRTVLDPVSGDLADTRTRYLGSRPVKLFRIKMQGSEAVLAMSSRTWLSYYHQNRFHLTPLSYETLEYASGFSSEQCSEGIVAISTNTLRILALEKLGAVFNQVAFPLQYTPRTFVIHPDTGRMLIAETDHNAYTEDTKSARKEQMAEEMRSAAGDEERELAREMANAFINEVLPEDVFSSPKAGLGLWASQIRCLDAMHGQTMFSVPLTQNEAIMSMAMLKFSIAADGRYYLAVGIAKDLQLNPRISQGGCIDIYKIDPTCSSLEFMHRTDIDEIPGALCGFQGRLLAGCGRMLRIYDFGKKKMLRKCENKHIPYQIVNIQAMGHRVYVSDVQESVFFIRYRRAENQLIIFADDTHPRWVTATTLLDYDTIAIADKFGNLSIQRLPHSVTDDVDEDPTGTKSLWDRGLLSGASQKSENICSFHVGEIIMSLQKATLIPGGSEALIYATLSGTVGAFVPFTSREDYDFFQHLEMHMRNENPPLCGRDHLSYRSSYYPVKNVLDGDLCEQYLSIEAAKQKSIAGDMFRTPNQICKKLEDIRTRYAF
Protein: Gigas, isoform B (M9PD17)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSKDKSKFKLFLKSLPAGYVGERTLRPEFERELRPEQPVAQRCRMLKELGDTQLHNFNLDESAITILFNLTNDLIVPNKPAETRQIALSFYKRLIHTQYKNLTIMREKFFLVIQNHEAREDLRHLLELLDTLTDNGKDITNFEEKIGKFMLLWIPAITEANLLTPYLDILVNLIKFNAAHLDKDILVGIVQNACDLSCSVTVNEIGLQCLTILEMVIGYTIFPSEPLPQCITTLCRTVNHAPYCPSSFKIMKNLLGTQLGYHSMKMMCSILNDRALYDDAHLLRGAVFHLNMNIFGSNIIFQVSPMTYATNVLTAFLRALDSRQVIVTFEVILSVRMVITKRQLSEIIWDLICDIMSSIVSNIEYYEEVNINKDRLHHLQINFHENIDCIEKLLQQDRSQILGNVERIYDLIERVADRRPEASVLALIEYRSRRVTATRPDWLQVLAQFVRRYYRMSNVNVRIKTIEALVQIMDQNRACYEEEILSRVVLVHLSHIHLESSVQVRVAVARALSNFATHCDTKRCMDLLDILEALINRPFEHTRHGSSSGEGTLAEVTFGLVNNESEISDIIAAVDGLVKVFAIKLHRLPGIHALKIFNILMDHLELHYERPKIFEHISVVRYKIFAWLLKARANGSYHIGYPEGSTEVVKFSPYLGIDSPLLPQAHPTAISIRRVCKLIVRCLEHDTDYQVFQLVIRELPKVLQNKALVQGNDIEELANTLLKINLVSNNKFKRPTDEFHALVLPAIASLVIYHESLQPQQHYGIITALNSRVLTGIASVCINTMTILILEMPEALMRKLPDVLLQMSKMSDTNALATPVLEFLSLLIHLSKHLFANFTSMHNMYVFAITLPYTKPHRYDHYTVSLAHHVIAGWFLKCKLELRRNCVNYIKSSNAKMLSSDIVNLNSLNEDSSNRKRSTSLTERGSRNNANAWNDLEMRPQMNNGLRNFHAELAETCFDFLARHTYSPCPSMPKRLPAAEFLLKDGVSQTWLVGNNLVTITTSGCPSAPARSGLCERCAQLGKAPSISLNSKSLSDAAPPLSPERERRYTKVSLQHSSGNESAGSTELTSSSSSNSAAAGGHPHRQISNSSTASLDALSRRGSNPEALGSALGEGAHTGSNTSLLGNSLSQSSVSMSPSSGSVVQQPVCVRACTGWAEVLVRRPTGNVSWITRIQNPITNDCFGQELPFNNVVSLFLPTAHGGVFGPDNTIQAPPHTLADPEPEPEAEVNAATAPQASALRSRMVAKARALQRQEEIHSVGGNGNGNGNGNGSGNAPSTGGAAAIPIPRVPASGKRGKEAALCGSVSDGEADDDSLAFEDAQSRARNPVRRVNSSPEMSSSWRQSFLTNKPTPLSQEPVKTTADEPQSLLTLKKKTVQYSTKDMRVSCEAIPEEIAGSTPPSQAAALALQPESGTLPPKQHSADDVSSHVAGGSNLQAGGSTLKLGKPPLSPGQPPLLGTGRVTSFGGTSVPQPGALAKSSSSGSNGTNVGVITSDYDNGNNGNGDMMRGRSKTISVVREVNNGNTRPPPASSFRNFGAAKPPINTKLCMNPSFIFMQLYTTGQLGVTDEPLKVGPENSSAVSLIDLVPPFETHKIGVLYVGQGQCNNEVEILRNSHGSARYVEFLRNIGTLVSLKEAEQNNLFIMLDRNGADGKFAYIWKDDILQVTFHVATLMPTNLQDDPNCNEKKSHIGNDFVKIIYNESGEEYNLNTISGQFNYACVIVEPLDLNSNRVYVKARSEISKFVCHAEYRIVSDRSAPLLARQMALHANLASLVYQSVQKKHPYASNWLERLRKLKRLRSKLIEGLNSQQKSGSASSGIGINASAIGSDMDDQRGDFIKYT
Protein: Aldo-keto reductase ausK (EC 1.1.1.-) (Austinoid biosynthesis clusters protein K) (C8VQ93)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Aldo-keto reductase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Interaction partners:
- FAD-dependent monooxygenase ausM
- Austinoid biosynthesis clusters protein J
- Cytochrome P450 monooxygenase ausI
- Cytochrome P450 monooxygenase ausG
Sequence:
MTGTRILELFGPAPEPPSELGRYRILSPTAGIRVSPLQLGALSIGDAWSTDLGSMDKDSAMELLDAYAAAGGNFIDTANAYQNEQSEMWIGEWMASRGNRDKMVIATKFGTDYRAHELGKGLAVNYSGNHKRSLHMSVRDSLQKLRTSWIDILYLHTWDYTTSIPELMDSLHHLVQRGDVLYLGICNTPAWVVSAANTYAQQQGKTQFSVYQGRWNPLRRELERDILPMARHFGMAVTVYDALGSGKFQSRDMLARRKDQGEGLRAIYGGQQTALEEAMSKALGVVAAQHGIESVTAVALAYLLAKAPYVFPIIGGRKIQHLHDNIEALSLRLSQEEIEYLESVGDFDPGFPYDMAGVDPADTGIATPIVAQAAPMAFVQRSKAIGYAESSKGSQMFG
Protein: Translocon-associated protein subunit alpha (TRAP-alpha) (Signal sequence receptor subunit alpha) (SSR-alpha) (P43307)
Organism: Homo sapiens (Human)
Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Interaction partners:
- Translocon-associated protein subunit gamma
- Translocon-associated protein subunit delta
- Translocon-associated protein subunit beta
- Protein transport protein Sec61 subunit alpha isoform 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Protein transport protein Sec61 subunit beta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Calnexin
Sequence:
MRLLPRLLLLLLLVFPATVLFRGGPRGLLAVAQDLTEDEETVEDSIIEDEDDEAEVEEDEPTDLVEDKEEEDVSGEPEASPSADTTILFVKGEDFPANNIVKFLVGFTNKGTEDFIVESLDASFRYPQDYQFYIQNFTALPLNTVVPPQRQATFEYSFIPAEPMGGRPFGLVINLNYKDLNGNVFQDAVFNQTVTVIEREDGLDGETIFMYMFLAGLGLLVIVGLHQLLESRKRKRPIQKVEMGTSSQNDVDMSWIPQETLNQINKASPRRLPRKRAQKRSVGSDE
Protein: Alpha-conotoxin PIA (P69658)
Organism: Conus purpurascens (Purple cone)
Function: Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This toxin blocks mammalian nAChRs (alpha-6 or -3/beta-2 or -3 > alpha-3/beta-2 > alpha-3/beta-4) when heterologously expressed in Xenopus oocytes. Does not block the muscle nor the major neuronal nAChR alpha-4/beta-2. Discriminates between nAChRs containing alpha-6 and alpha-3 subunits, being selective for alpha-6. Also reduces the frequency of responses from the giant fiber (GF)-dorsal longitudinal muscle pathway in the D.melanogaster GF circuit, but has no effect on the GF-tergo trochanteral muscle pathway.
Subcellular location: Secreted {ECO:0000269|PubMed:28917942}.
Interaction partners:
Sequence:
SDGRDAAANDKATDLIALTARRDPCCSNPVCTVHNPQICG
Protein: Adhesion G protein-coupled receptor E5 (Leukocyte antigen CD97) (CD antigen CD97) [Cleaved into: Adhesion G protein-coupled receptor E5 subunit alpha; Adhesion G protein-coupled receptor E5 subunit beta] (Q9Z0M6)
Organism: Mus musculus (Mouse)
Function: Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10540231}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Adhesion G protein-coupled receptor E5 subunit alpha]: Secreted, extracellular space {ECO:0000305}.
Interaction partners:
- Complement decay-accelerating factor, GPI-anchored
- Complement decay-accelerating factor transmembrane isoform
- Lysophosphatidic acid receptor 1
- Thy-1 membrane glycoprotein
- Guanine nucleotide-binding protein subunit alpha-12
Sequence:
MRGVRCPGLLVVCILLSLSGAGTQKAESKNCAKWCPINSKCVSNRSCVCKPGFSSEKELITNPAESCEDINECLLPGFSCGDFAMCKNSEGSYTCVCNLGYKLLSGAESFVNESENTCQASVNTGTTPVPSRIHTVTTAPGNLPEQTTTVHQTQMGDSEERTPKDVNECISGQNHCHQSTHCINKLGGYSCICRQGWKPVPGSPNGPVSTVCEDVDECSSGQHQCHNSTVCKNTVGSYKCHCRPGWKPTSGSLRGPDTICQEPPFPTWTLLPTAHSQTLLRFSVEVQNLLRDFNPATVNYTIQKLIEAVDKLLEDPMETQTQQVAAQLLSNLEQSLRTLAQFLPKGPFTYTSPSNTELSLMVKEQDNKDVTTVHHGQTWMELDWAVTAGAKISENGSSVAGILSSPNMEKLLGNTPLNLEQRRASLEDFYGSPIPSVSLKLLSNINSVFLTNTNTEKLASNVTFKFDFTSVESIEPRHELICAFWKAHNGNGYWDTDGCSMNGTGFCHCNHLTSFAILMAQYHVQDPRLELITKVGLLLSLICLLLCILTFLLVKPIQSSRTMVHLHLCICLFLGSIIFLVGVENEGGEVGLRCRLVAMMLHFCFLAAFCWMALEGVELYFLVVRVFQGQGLSTWQRCLIGYGVPLLIVAISMAVVKMDGYGHATYCWLDFRKQGFLWSFSGPVAFIIFCNAAIFVITVWKLTKKFSEINPNMKKLRKARVLTITAIAQLLVLGCTWGFGLFLFNPHSTWLSYIFTLLNCLQGLFLYVMLCLLNKKVREEYWKWACMVTGSKYTEFNSSTTGTGTSQTRALRSSESGM
Protein: Two-pore potassium channel 1 (AtTPK1) (Calcium-activated outward-rectifying potassium channel 1) (AtKCO1) (Q8LBL1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Voltage-independent, large conductance and potassium-selective tonoplast ion channel. Regulated by cytoplasmic calcium and pH. Does not mediate slow-vacuolar (SV) ionic currents, but essential to establish VK currents. Has some permeability for Rb(+) and NH(4)(+), but none for Na(+), Cs(+) or Li(+). Involved in intracellular K(+) redistribution and/or K(+) retranslocation between different tissues.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:12148538, ECO:0000269|PubMed:19825594, ECO:0000269|PubMed:21697507}; Multi-pass membrane protein {ECO:0000269|PubMed:12148538, ECO:0000269|PubMed:19825594, ECO:0000269|PubMed:21697507}. Note=Tonoplast.
Interaction partners:
- Protein DMP1
- Two pore calcium channel protein 1
- Potassium channel KAT3
- Anthranilate N-hydroxycinnamoyl/benzoyltransferase-like protein
- Early nodulin-like protein 20
- LOW protein: ankyrin repeat protein
- DNAse I-like superfamily protein
- Fimbrin-1
- Potassium channel SKOR
- Potassium channel GORK channel)
Sequence:
MSSDAARTPLLPTEKIDTMAQDFNLNSRTSSSRKRRLRRSRSAPRGDCMYNDDVKIDEPPPHPSKIPMFSDLNPNLRRVIMFLALYLTIGTLCFYLVRDQISGHKTSGVVDALYFCIVTMTTVGYGDLVPNSSASRLLACAFVFSGMVLVGHLLSRAADYLVEKQEALLVRAFHLRQSFGPTDILKELHTNKLRYKCYATCLVLVVLFIVGTIFLVMVEKMPVISAFYCVCSTVTTLGYGDKSFNSEAGRLFAVFWILTSSICLAQFFLYVAELNTENKQRALVKWVLTRRITNNDLEAADLDEDGVVGAAEFIVYKLKEMGKIDEKDISGIMDEFEQLDYDESGTLTTSDIVLAQTTSQIQR
Protein: Regulator in type III secretion (Q9I326)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Type III secretion protein PcrV
- Type III secretory apparatus protein PcrD
- Translocation protein in type III secretion
- Translocator protein PopB
- Regulatory protein PcrH
- Translocator outer membrane protein PopD
- Type III secretion outer membrane protein PopN
- Type III secretion chaperone SycN
- HTH-type transcriptional regulator ExsA
- Transcriptional antiactivator ExsD
Sequence:
MGDMNEYTEDTLRATVQAAELAIRDSEERGRLLAEMWQGLGLAADAGELLFQAPERELARAAEEELLAELRRMRSSQPTQGEQGTRPRRPTPMRGLLI