wanglab/gogpt-training-data huggingface dataset:
Protein: 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC (EC 3.1.3.45) (KDO 8-P phosphatase) (P67653)
Organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Function: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate.
Interaction partners:
- 2-dehydro-3-deoxyphosphooctonate aldolase
- Arabinose 5-phosphate isomerase KdsD
- 3-deoxy-manno-octulosonate cytidylyltransferase
- 3-deoxy-manno-octulosonate cytidylyltransferase
- Lipopolysaccharide export system protein LptC
- Lipopolysaccharide export system ATP-binding protein LptB
- arabinose-5-phosphate isomerase
- Lipopolysaccharide export system protein LptA
- Arabinose 5-phosphate isomerase GutQ
- Sodium/calcium exchanger membrane region domain-containing protein
Sequence:
MSKAGASLATCYGPVSADVMAKAENIRLLILDVDGVLSDGLIYMGNNGEELKAFNVRDGYGIRCALTSDIEVAIITGRKAKLVEDRCATLGITHLYQGQSNKLIAFSDLLEKLAIAPENVAYVGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCDLLLLAQGKLDEAKGQSI
Protein: Meteorin-like protein (Subfatin) (Q8VE43)
Organism: Mus musculus (Mouse)
Function: Hormone induced following exercise or cold exposure that promotes energy expenditure. Induced either in the skeletal muscle after exercise or in adipose tissue following cold exposure and is present in the circulation. Able to stimulate energy expenditure associated with the browning of the white fat depots and improves glucose tolerance. Does not promote an increase in a thermogenic gene program via direct action on adipocytes, but acts by stimulating several immune cell subtypes to enter the adipose tissue and activate their prothermogenic actions. Stimulates an eosinophil-dependent increase in IL4 expression and promotes alternative activation of adipose tissue macrophages, which are required for the increased expression of the thermogenic and anti-inflammatory gene programs in fat. Required for some cold-induced thermogenic responses, suggesting a role in metabolic adaptations to cold temperatures.
Subcellular location: Secreted {ECO:0000269|PubMed:24393292, ECO:0000269|PubMed:24906147}.
Interaction partners:
Sequence:
MRGAVWAARRRAGQQWPRSPGPGPGPPPPPPLLLLLLLLLGGASAQYSSDLCSWKGSGLTREARSKEVEQVYLRCSAGSVEWMYPTGALIVNLRPNTFSPAQNLTVCIKPFRDSSGANIYLEKTGELRLLVRDIRGEPGQVQCFSLEQGGLFVEATPQQDISRRTTGFQYELMSGQRGLDLHVLSAPCRPCSDTEVLLAICTSDFVVRGFIEDVTHVPEQQVSVIYLRVNRLHRQKSRVFQPAPEDSGHWLGHVTTLLQCGVRPGHGEFLFTGHVHFGEAQLGCAPRFSDFQRMYRKAEEMGINPCEINME
Protein: SEC63 homolog, protein translocation regulator (A6PVC9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWYRLRLLKPQPNIIPTVKKIVLLAGWALFLFLAYKVSKTDREYQEYNPYEVLNLDPGATVAEIKKQYRLLSLKYHPDKGGDEVMFMRIAKAYAALTDEESRKNWEEFGNPDGPQATSFGIALPAWIVDQKNSILVLLVYGLAFMVILPVVVGSWWYRSIR
Protein: G-protein coupled receptor 143 (MOA1) (Ocular albinism type 1 protein homolog) (P70259)
Organism: Mus musculus (Mouse)
Function: Receptor for tyrosine, L-DOPA and dopamine. After binding to L-DOPA, stimulates Ca(2+) influx into the cytoplasm, increases secretion of the neurotrophic factor SERPINF1 and relocalizes beta arrestin at the plasma membrane; this ligand-dependent signaling occurs through a G(q)-mediated pathway in melanocytic cells. Its activity is mediated by G proteins which activate the phosphoinositide signaling pathway. Also plays a role as an intracellular G protein-coupled receptor involved in melanosome biogenesis, organization and transport.
Subcellular location: Melanosome membrane {ECO:0000250|UniProtKB:P51810}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P51810}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P51810}; Multi-pass membrane protein {ECO:0000255}. Note=Distributed throughout the endo-melanosomal system but most of endogenous protein is localized in unpigmented stage II melanosomes. Its expression on the apical cell membrane is sensitive to tyrosine. {ECO:0000250|UniProtKB:P51810}.
Interaction partners:
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Membrane-associated transporter protein
- Tyrosinase
- Uridine 5'-monophosphate synthase
- Melan-A
- P protein
- FERM domain-containing protein 7
- Argininosuccinate synthase
- Dihydroorotate dehydrogenase
Sequence:
MASPRLGIFCCPTWDAATQLVLSFQPRVFHALCLGSGTLRLVLGLLQLLSGRRSVGHRAPATSPAASVHILRAATACDLLGCLGIVIRSTVWIAYPEFIENISNVNATDIWPATFCVGSAMWIQLLYSACFWWLFCYAVDVYLVIRRSAGRSTILLYHIMAWGLAVLLCVEGAVMLYYPSVSRCERGLDHAIPHYVTTYLPLLLVLVANPILFHKTVTSVASLLKGRKGVYTENERLMGAVIKTRFFKIMLVLIACWLSNIINESLLFYLEMQPDIHGGSLKRIQNAARTTWFIMGILNPAQGLLLSLAFYGWTGCSLDVHPPKMVIQWETMTASAAEGTYQTPVRSCVPHQNPRKVVCVGGHTSDEVLSILSEDSDASTVEIHTATGSCNIKEVDSISQAQGEL
Protein: ATP-dependent RNA helicase dbp9 (EC 3.6.4.13) (O60080)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Ribosome production factor 2 homolog
- Nucleolar protein 12
- Ribosome biogenesis protein brx1
- Uncharacterized protein C4F10.09c
- Probable rRNA-processing protein ebp2
- Brix domain-containing protein C1B9.03c
- Ribosome biogenesis protein nsa1
- Ribosomal RNA-processing protein 14-N
- Ribosome biogenesis protein erb1
- Pescadillo homolog
Sequence:
MEKSGGIREESSEKTFSDFNLDPRLQRAIHKCEFEKPTSVQSETIPLALEGKDLVAQARTGSGKTAAYLIPILELLLKQKQIDENQRGIFALLLVPTRELAQQVYNVLEKLTAFCSKHIRFINVATNSSDTVQRPLLLDLPDIVIATPSRCVVHVASGVLPLDKLKFLVIDEADLMLSFGYNEDMKTLSRSLPRGTQSFLMSATLSKNIASLQKLVCRNPFILAVKDKEASGKLTQYVVKCSEQDKFLLAYILLKLRLIKGKILIFVNEINRCYRLKLFLEQFGLKSLVLNSELPVNSRLHILEQYNKGLYQIIIATDESGMMGEIEELENNVDFVEEEVISTDQPTLDKMKDQENADVNDESILAAAKDKSKKKKRVKQDKEYGVARGLDFENVACVLNFDMPSNTKSYIHRIGRTARAGKPGTAMSFVVPKSEVGKHKPTSLESCKKDESVLRRLEKKQISLQPYSFDKNQIDAFRYRMEDALRAVTTVAVSAARAAELKQELLISEKLKSYFAENPDELLSLTHDTVSSVRLGHTQRHLRHVPEYLLPKGMQAVNKDIGFVPFKKNNRRKVFKSRKNPKHRHDPLRSMKRKS
Protein: Ubiquitin conjugation factor E4 B (EC 2.3.2.27) (RING-type E3 ubiquitin transferase E4 B) (Ubiquitin fusion degradation protein 2) (Q9ES00)
Organism: Mus musculus (Mouse)
Function: Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases. May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:11770485, ECO:0000269|PubMed:12504083}. Nucleus {ECO:0000269|PubMed:11435423}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Ubiquilin-1
- Nuclear protein localization protein 4 homolog
- Ubiquilin-2
- Ubiquitin thioesterase OTU1
- E3 ubiquitin-protein ligase CHIP
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- E3 ubiquitin-protein ligase Mdm2
- UV excision repair protein RAD23 homolog B
Sequence:
MEELSADEIRRRRLARLAGGQTSQPTTPLTSPQRENPPGPPIAASAPGPSQSLGLNVHNMTPATSPIGAAGVAHRSQSSEGVSSLSSSPSNSLETQSQSLSRSQSMDIDGVSCEKSMSQVDVDSGIENMEVDENDRREKRSLSDKEPSSGPEVSEEQALQLVCKIFRVSWKDRDRDVIFLSSLSAQFKQNPKEVFSDFKDLIGQILMEVLMMSTQTRDENPFASLTATSQPIATAARSPDRNLMLNTGSSSGTSPMFCNMGSFSTSSLSSLGASGGASNWDSYSDHFTIETCKETDMLNYLIECFDRVGIEEKKAPKMCSQPAVSQLLSNIRSQCISHTALVLQGSLTQPRSLQQPSFLVPYMLCRNLPYGFIQELVRTTHQDEEVFKQIFIPILQGLALAAKECSLESDYFKYPLMALGELCETKFGKTHPMCNLVASLPLWLPKSLSPGSGRELQRLSYLGAFFSFSVFAEDDAKVVEKYFSGPAITLENTRVVSQSLQHYLELGRQELFKILHSILLNGETREAALSYMAALVNANMKKAQMQADDRLVSTDGFMLNLLWVLQQLSTKIKLETVDPTYIFHPRCRITLPNDETRINATMEDVNERLTELYGDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTVEDLKNNESQWKDSPLATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLMLRILDPAYPDVTLPLNSEVPKVFAALPEFYVEDVAEFLFFIVQYSPQVLYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQPRTQKFFEMIENHPLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQFVRYINMLINDTTFLLDESLESLKRIHEVQEEMKNKEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQLDCARFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQSSDH
Protein: Syntaxin-1A (Neuron-specific antigen HPC-1) (O35526)
Organism: Mus musculus (Mouse)
Function: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis. Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane. STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion. Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm. Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:18760330}; Single-pass type IV membrane protein {ECO:0000269|PubMed:18760330}. Synapse, synaptosome {ECO:0000269|PubMed:18760330}. Cell membrane {ECO:0000250|UniProtKB:P32851}. Note=Colocalizes with KCNB1 at the cell membrane. {ECO:0000250|UniProtKB:P32851}.
Interaction partners:
- Syntaxin-binding protein 1
- Synaptosomal-associated protein 25
- Vesicle-associated membrane protein 2
- Alpha-soluble NSF attachment protein
- Vesicle-associated membrane protein 1
- Complexin-1
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Synaptosomal-associated protein 23
- Vesicle-associated membrane protein 3
- Beta-soluble NSF attachment protein
Sequence:
MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLETSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG
Protein: AT19737p (GH26310p) (Kelch like family member 10, isoform A) (Kelch like family member 10, isoform B) (Q6GKZ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cullin 3, isoform F
- RING-box protein 1B
- Male-specific protein scotti
- Succinate--CoA ligase subunit beta, mitochondrial
- Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6
- Cullin homolog 1
- RING-box protein 1A
- Cullin 6
- Protein roadkill
- Kelch-like protein diablo
Sequence:
MSRNQNESNLLDINEDLPFALALPPVSMDSLQLNADGNSPEDKTLGIGRKTILNAHTKSLAPIVSDEALNTLNELREQNLLCDAQISVGEDVFNVHRAIMCSCSSYFRAQFTGFNADTPGCVDGSDAKKNNNFIHIPGVSSCIMNCVIQYAYLRQTNISESNVHELLICADYVGMVGLVKKCKDYLGRILTPENCVSIMGFARFRFLEDLHLKARNYTLRYFTEVAYRNIDILDMSAEDFYSIISDDELNTREEDHVWKLCVKWIDRNPESRKRHVAHLMTGVRLGLMTPKCFMEEVKEHPYVLECEAAKPLIVDTFKFMYDLDFLNPQADELTTPPLAMPRLPHEVIFAIGGWSGGTSKGCIETYDTRADRWVTINAEDPAGPRAYHGTAVLGFKIFSIGGYDGVEYFNTCRVFDAVKKKWNEIAPMHCRRCYVSVTELNGMIYAIGGYDGHNRLNTVERYNPRTNQWSVIPPMNMQRSDASACTLQERIYATGGFNGQECLDSAEYYDPVTNVWTRIPNMNHRRSGVSCVAFRNQLYVIGGFNGTARLSTGERFDPDTQTWHFIREMNHSRSNFGLEIIDDMIFAIGGFNGVSTISHTECYVAETDEWMEATDMNIVRSALSANNIAGLPNKRDYIHKERDRLMEERRQRLMATAMARENVGHGNASQMLVEHNDGAMDDYESPDEVDETDEQEQSARISRTIPPSVGLPNPAVAAETIRDQSQLVSTAQLNRVMEDRGMDNNRSNRVQLRNQRHGSHHEIRRRT
Protein: Short-chain dehydrogenase/reductase ABA4 (EC 1.1.1.-) (Abscisic acid biosynthesis protein 4) (G4N1P8)
Organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
Function: Short-chain dehydrogenase/reductase involved in the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. During pathogen-host interaction, ABA plays a dual role in disease severity by increasing plant susceptibility and accelerating pathogenesis in the fungus itself. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase ABA3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene (By similarity). The cytochrome P450 monooxygenase ABA1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (By similarity). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase ABA2 and the short-chain dehydrogenase/reductase ABA4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (By similarity). ABA2 is responsible for the hydroxylation of carbon atom C-1' and ABA4 might be involved in the oxidation of the C-4' carbon atom (By similarity).
Interaction partners:
Sequence:
MGSIENPEIMASTMLHILPLAGKVYGITGGASGIGLATAQILSRRGATVCIADVDPKAMASAEVYFSGQSGAKYSITKVDISKRSEVNAWVDGIISQFGRLDGAANVAGVIGKIHGAVPVSEMDDDEWDKIVAVNLTGTMYCMRAQLRNIVDGGSIVNVASIHGLKGFANHAAYDASKHGVIGLTKAAAQENGAREIRVNAVAPGAIYTPLMQKNWDITGRPKDAPFDDPSAFRRQGTAMETGNVIAFLLGPDSTFVSGSVYSVDGAWI
Protein: SWI/SNF complex subunit SWI3C homolog (OsSWI3C) (OsSWI3C1) (Transcription regulatory protein SWI3C homolog) (Q53KK6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of a multiprotein complex equivalent of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors (By similarity). May be involved in positive response to drought stress and modulation of root growth through its interaction with NMCP1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:32129897, ECO:0000269|PubMed:32808364}. Nucleus, nucleoplasm {ECO:0000269|PubMed:32129897}.
Interaction partners:
- Actin-related protein 4
- Os04g0382100 protein
- Os07g0609766 protein.
- Os02g0723700 protein
- Expressed protein
- Os06g0255200 protein
- Os01g0884500 protein.
- Histone H4
- Histone H4
- ARID transcription factor
Sequence:
MPRKASSTSDSRLKWRKWKRNPTASPSPSNRSSAAAAAADHSDDSDSAAVNEDDDSAVPEDADDETLAGAEDPVLDLREAEVLPSAEPVSAFPVATRRVVNRPHPSVLAVIAAERSACAGEGSAAVAAAPVLENISYGQQQVLSGVLPDHASLATDTDKPSTYVCTPPNLMEGHGVTKQFQGRLHVVPKHSDWFSPGIVHRLERQVVPQFFSGKSPGNTPEKYMLLRNKVIAKYLENPSKRLAFAECQGLVANTAELYDLSRIVRFLDTWGIINYLASGSVHRGLRMATSLLREEPTGELQLLTAPLKSIDGLILFDRPKCNLQAEDISSLASNSEVVDFDAGLAELDGKIRERLSESSCSYCLQPLTSLHYQSLKEADIALCSDCFHDARYITGHSSLDFQRIDGDNDRSENDGDSWTDQETLLLLEGIEKYNDNWNNIAEHVGTKSKAQCIYHFIRLPVEDGLLENIEVPDASVPFRAETNGYPHLDCNGSTSGNLPQKIPPDNQLPFINSSNPVMSLVGFLASAMGPRVAASCASAALSVLTVDDDSRVNSEGICSDSRGQGPHPNFRDHNGGVSSSISPEKVKHAAMCGLSAAATKAKLFADQEEREIQRLTATVINHQLKRLELKLKQFAEVETLLLKECEQVERIRQRIASDRVRIVSTRLASPGNSLPGGSTSTMSSNPMSMSPRPMGVPGSMPQSSMPAPFANNMQGHGHPQMAFLQQQQRQQMLSFGPRLPLSAIQTQPSPQTSNIMFNPGMPNSVTPNHHQLLRSSSGNNSSVG
Protein: Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I) (P24893)
Organism: Caenorhabditis elegans
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18635357}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00401}.
Interaction partners:
- COX5B-domain-containing protein
- Cytochrome c oxidase subunit 3
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 4
- Cytochrome c domain-containing protein
- Cytochrome oxidase c subunit VIb
- Cytochrome b
- NADH-ubiquinone oxidoreductase chain 5
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MNLYKKYQGGLAVWLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPLMLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTMGHPGSSVDLAIFSLHAAGLSSILGGINFMCTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLATLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISDYYSNSSPEYCMSNYVFGHSYQSEIYFSTTSLKN
Protein: RNA polymerase I-specific transcription initiation factor RRN6 (P32786)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the core factor (CF) complex which is essential for the initiation of rDNA transcription by RNA polymerase I. After binding of UAF (upstream activation factor) to an upstream element of the promoter, CF is recruited in a SPT15/TBP-dependent manner to form a preinitiation complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- RNA polymerase I-specific transcription initiation factor RRN11
- RNA polymerase I-specific transcription initiation factor RRN7
- RNA polymerase I-specific transcription initiation factor RRN3
- RNA polymerase I-specific transcription initiation factor RRN5
- RNA polymerase I-specific transcription initiation factor RRN9
- RNA polymerase I-specific transcription initiation factor RRN10
- Upstream activation factor subunit UAF30
- TATA-box-binding protein
- DNA-directed RNA polymerase I subunit RPA34
- DNA-directed RNA polymerase I subunit RPA12
Sequence:
MSEGQIPSSDVLGSQLGVGVQGASLYCPQENYTTKKQEKPQWLRPVDDTLAEDALDLHIVVKSLLCDTAIRYISDDKVLQESDADDDLITSDIDEDTDNQGDTSIVVNPVIPVVPKDVHFFKKVDVGNDSMFGVNCDTPVSFQDYIPSDLLRNLDDTLQESTNSSRPMQDAFFWDPTVANRLDSQYIQTASDLRNYRDGTEIIAYASGKTGSVLNIAVLTRQNTLHLNRHNNVTSIELHSPIKSIKIPGASESIGRRSNLVGIITENSFQIFRIESVHSRSCDVMVSSSEPLYFVEIDDLQVVDFAFNPWDLQQFAIIDIKGNWSIGRIPKNFNNNNKRKLQLIDNLHGTIFDPEELSSWKRIEWFSHFQKILVFDRSKMIEIDFMNNWQTEVVQAKAWSNIRDYKRIDDKNGILLTSREIIIVGASESNDPVRRISWKHDLDPDDTTLRITVQKVKKPDHILLVAFVYSMRHKRIYMHVFSHRKANLFQSLGCSTVLEIPGGTPTGIETILTLDHIDDESRREEDADENFELVVDFLVKLRNSSEVYYYALSNTQNSEPNKQETPIIVDHPEWASLFNNADEREKESIGALVSQIKLKERERISRVQNLIEHENSHDEDKYLQDLGYRLSIATNELLESWQKTKDESILSGSLSHSKLKNLLENSDSFASIPEFSSLLDQFFQYYQDQDVTFIGFEKLLHLFLHEDVPGLDIFYNKLLQCWVLVSPQAELLTKEIVKDIIWSLARLEKPSLFEPIQNEISRSLSGPYQDIISSWDMDDINEEDESNEFNFDSQFSAPFNGRPPFNLNSQSQIPTIKSSQSSGLARRKRILKTQSQKATPLSQSTQNLSVLPDSMTPAFTLMQPPSSQISFVNDSQPRNSQKAKKKKKRIRGFG
Protein: N-acetylgalactosamine kinase (EC 2.7.1.157) (GalNAc kinase) (Galactokinase 2) (Q01415)
Organism: Homo sapiens (Human)
Function: Acts on GalNAc. Also acts as a galactokinase when galactose is present at high concentrations. May be involved in a salvage pathway for the reutilization of free GalNAc derived from the degradation of complex carbohydrates.
Interaction partners:
- UDP-glucose 4-epimerase
- Galactose-1-phosphate uridylyltransferase
- Galactose mutarotase
- UDP-glucose--hexose-1-phosphate uridylyltransferase
- Interleukin-11 receptor subunit alpha
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
- UDP-N-acetylhexosamine pyrophosphorylase
Sequence:
MATESPATRRVQVAEHPRLLKLKEMFNSKFGSIPKFYVRAPGRVNIIGEHIDYCGYSVLPMAVEQDVLIAVEPVKTYALQLANTNPLYPDFSTSANNIQIDKTKPLWHNYFLCGLKGIQEHFGLSNLTGMNCLVDGNIPPSSGLSSSSALVCCAGLVTLTVLGRNLSKVELAEICAKSERYIGTEGGGMDQSISFLAEEGTAKLIEFSPLRATDVKLPSGAVFVIANSCVEMNKAATSHFNIRVMECRLAAKLLAKYKSLQWDKVLRLEEVQAKLGISLEEMLLVTEDALHPEPYNPEEICRCLGISLEELRTQILSPNTQDVLIFKLYQRAKHVYSEAARVLQFKKICEEAPENMVQLLGELMNQSHMSCRDMYECSCPELDQLVDICRKFGAQGSRLTGAGWGGCTVSMVPADKLPSFLANVHKAYYQRSDGSLAPEKQSLFATKPGGGALVLLEA
Protein: Enterobactin exporter EntS (Protein p43) (P24077)
Organism: Escherichia coli (strain K12)
Function: Component of an export pathway for enterobactin. Overexpression reduces intracellular arabinose concentrations.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01436, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01436}.
Interaction partners:
- Ferric enterobactin-binding periplasmic protein FepB
- Ferric enterobactin transport system permease protein FepG
- Iron
- Ferric enterobactin transport system permease protein FepD
- Enterobactin synthase component E
- Ferric enterobactin transport ATP-binding protein FepC
- Isochorismate synthase EntC
- Enterobactin synthase component F
- 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
- Enterobactin synthase component B
Sequence:
MNKQSWLLNLSLLKTHPAFRAVFLARFISIVSLGLLGVAVPVQIQMMTHSTWQVGLSVTLTGGAMFVGLMVGGVLADRYERKKVILLARGTCGIGFIGLCLNALLPEPSLLAIYLLGLWDGFFASLGVTALLAATPALVGRENLMQAGAITMLTVRLGSVISPMIGGLLLATGGVAWNYGLAAAGTFITLLPLLSLPALPPPPQPREHPLKSLLAGFRFLLASPLVGGIALLGGLLTMASAVRVLYPALADNWQMSAAQIGFLYAAIPLGAAIGALTSGKLAHSARPGLLMLLSTLGSFLAIGLFGLMPMWILGVVCLALFGWLSAVSSLLQYTMLQTQTPEAMLGRINGLWTAQNVTGDAIGAALLGGLGAMMTPVASASASGFGLLIIGVLLLLVLVELRHFRQTPPQVTASDS
Protein: Cytochrome P450 71D13 (EC 1.14.14.99) ((-)-(4S)-Limonene-3-hydroxylase) (Cytochrome P450 isoform PM17) (Q9XHE7)
Organism: Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata)
Function: Hydroxylates (-)-(4S)-limonene to (-)-trans-isopiperitenol, a precursor of (-)-menthol, responsible for the cooling sensation of peppermint.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MELQISSAIIILVVTYTISLLIIKQWRKPKPQENLPPGPPKLPLIGHLHLLWGKLPQHALASVAKQYGPVAHVQLGEVFSVVLSSREATKEAMKLVDPACADRFESIGTKIMWYDNDDIIFSPYSVHWRQMRKICVSELLSARNVRSFGFIRQDEVSRLLGHLRSSAAAGEAVDLTERIATLTCSIICRAAFGSVIRDHEELVELVKDALSMASGFELADMFPSSKLLNLLCWNKSKLWRMRRRVDAILEAIVEEHKLKKSGEFGGEDIIDVLFRMQKDSQIKVPITTNAIKAFIFDTFSAGTETSSTTTLWVMAELMRNPEVMAKAQAEVRAALKGKTDWDVDDVQELKYMKSVVKETMRMHPPIPLIPRSCREECEVNGYTIPNKARIMINVWSMGRNPLYWEKPETFWPERFDQVSRDFMGNDFEFIPFGAGRRICPGLNFGLANVEVPLAQLLYHFDWKLAEGMNPSDMDMSEAEGLTGIRKNNLLLVPTPYDPSS