wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxisomal ATPase PEX1 (EC 3.6.4.-) (Peroxin-1) (AtPEX1) (Peroxisome biogenesis protein 1) (Q9FNP1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel (By similarity). Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21487094}. Peroxisome membrane {ECO:0000269|PubMed:21487094}. Note=Localizes to the peroxisome when interacting with the PEX6/APEM9 complex. {ECO:0000269|PubMed:21487094}.
Interaction partners:
- Peroxisomal ATPase PEX6
- CWZF3/5/7 THD domain-containing protein
- Peroxisome biogenesis protein 12
- Peroxisome biogenesis protein 5
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis factor 10
- Peroxisome biogenesis protein 7
- Mitochondrial fission 1 protein A
- Peroxisome biogenesis protein 22
- Peroxisome biogenesis protein 19-1
Sequence:
MSRNRQIIIPDDVMETEAVVNTVAGVDCFVSLPRQLLHALQSTSSSPLPPLLPVELRSGDRRWSVAWSGSSSSSSAIEIARVFAESISLPDGTVVKVRVLPNVPKATLVTVEPETEDDWEVLELNAELAEAAILSQVRILHETMKFPLWLHDRTVIRFSVVSTFPSKGVVQLVPGTEVAVAPKRRDRNLKAKKSQEKECNNVKALLRVQETDRSAFHEADVKGFELRVALTSIAYIHPETAKKHSLESLQLISVSPRIPLKGSAKKDEALNMKNSEASKVAENGTSSAKKEPRQAILRLVFSDLAAKGHLMMVESLRLYLGAGLHSWVYLRGCNVNEDKEIPALSLSPCVFKISENEKVLDKGTDRLGNNNSVRKSSHPPSGLSTYVDVVDWSVHDKVVTALSSEGLHDEGNHDKNKKGLEYLTRLWSLAQLDAMASVTGVDVSSLIVGRETFFHFEVRGLESYKSIDGQPSVNDRWESGKKDKHTPLEILYVMTVSDESLLGDKFAGYDLSLDRSEKSDNVVHIEPVLEKMNLGEPIYLKSAKETHCNKGVSPDISSLTWMGPIVSDVIKRMTVLLSPAAGMWFSKFKIPSPGHILIYGPPGSGKTILARAAAKYFEEQKDLLAHVILVSCSTLALEKVQHIHHVLSSVIAEGLEHAPSVIILDDLDSIISSSSDTEGTQASVGVTMLTKFLTDVIDDYGEYRNSSCGIGPLAFVASVQSLEQIPQTLSSSGRFDFHVQLAAPATSERGAILKHEIQKRLLDCSEDILLNLAAKCEGYDAYDLEILVDRAVHAAIGRHLPLESNISKYNLVKEDFTRAMHDFVPVAMRDITKSASEGGRLGWEDVGGVTDIKNAIKEMIELPSKFPKIFAKSPLRLRSNVLLYGPPGCGKTHIVGAAAAACSLRFISVKGPELLNKYIGASEQAVRDIFSKAAAAAPCILFFDEFDSIAPKRGHDNTGVTDRVVNQFLTELDGVEVLTGVFVFAATSRPDLLDPALLRPGRLDRLLLCDFPSPPERLEILTVLSRKLLMADDIDLEPIALMTEGFSGADLQALLSDAQLAAVHEYLNREDKPETGTTPIITDPLLKSIASKTKPSVSETEKQKLYDIYSQFLDSRKSSREAKGKRATLA
Protein: Early growth response protein 1 (EGR-1) (Nerve growth factor-induced protein A) (NGFI-A) (Transcription factor Zif268) (Zinc finger protein Krox-24) (P08154)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (By similarity). Binds double-stranded target DNA, irrespective of the cytosine methylation status (By similarity). Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia. Plays a role in the regulation of cell survival, proliferation and cell death. Activates expression of p53/TP53 and TGFB1, and thereby helps prevent tumor formation. Required for normal progress through mitosis and normal proliferation of hepatocytes after partial hepatectomy. Mediates responses to ischemia and hypoxia; regulates the expression of proteins such as IL1B and CXCL2 that are involved in inflammatory processes and development of tissue damage after ischemia. Regulates biosynthesis of luteinizing hormone (LHB) in the pituitary (By similarity). Regulates the amplitude of the expression rhythms of clock genes: BMAL1, PER2 and NR1D1 in the liver via the activation of PER1 (clock repressor) transcription. Regulates the rhythmic expression of core-clock gene BMAL1 in the suprachiasmatic nucleus (SCN) (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:1859855}. Cytoplasm {ECO:0000250|UniProtKB:P18146}.
Interaction partners:
- Protein c-Fos
- Transcription factor Jun
- Mitogen-activated protein kinase 3
- E3 SUMO-protein ligase EGR2
- Protein FosB
- Mitogen-activated protein kinase 1
- NGFI-A-binding protein 1
- Ngfi-A binding protein 2
- Histone lysine acetyltransferase CREBBP
- Nuclear receptor subfamily 4 group A member 1
Sequence:
MDNYPKLEEMMLLSNGAPQFLGAAGTPEGSGGNNSSSSSSSSSGGGGGGGSNSGSSAFNPQGEPSEQPYEHLTTESFSDIALNNEKALVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPTSSSSAPSPAASSSSSASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPATKGGFQVPMIPDYLFPQQQGDLSLGTPDQKPFQGLENRTQQPSLTPLSTIKAFATQSGSQDLKALNNTYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKADKSVVASSAASSLSSYPSPVATSYPSPATTSFPSPVPTSYSSPGSSTYPSPAHSGFPSPSVATTYASVPPAFPAQVSTFQSAGVSNSFSTSTGLSDMTATFSPRTIEIC
Protein: Legumain (EC 3.4.22.34) (Asparaginyl endopeptidase) (AEP) (Protease, cysteine 1) (Q99538)
Organism: Homo sapiens (Human)
Function: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity). May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.
Subcellular location: Lysosome {ECO:0000269|PubMed:9872320}.
Interaction partners:
- Cystatin-M
- Cathepsin B
- Cathepsin S
- HLA class II histocompatibility antigen gamma chain
- Procathepsin L
- Protein-glutamine gamma-glutamyltransferase E
- Pro-cathepsin H
- Cubilin
- Protein SET
- Cathepsin Z
Sequence:
MVWKVAVFLSVALGIGAVPIDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIVVMMYDDIAYSEDNPTPGIVINRPNGTDVYQGVPKDYTGEDVTPQNFLAVLRGDAEAVKGIGSGKVLKSGPQDHVFIYFTDHGSTGILVFPNEDLHVKDLNETIHYMYKHKMYRKMVFYIEACESGSMMNHLPDNINVYATTAANPRESSYACYYDEKRSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKTISTMKVMQFQGMKRKASSPVPLPPVTHLDLTPSPDVPLTIMKRKLMNTNDLEESRQLTEEIQRHLDARHLIEKSVRKIVSLLAASEAEVEQLLSERAPLTGHSCYPEALLHFRTHCFNWHSPTYEYALRHLYVLVNLCEKPYPLHRIKLSMDHVCLGHY
Protein: GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (EC 2.4.1.131) (Asparagine-linked glycosylation protein 11 homolog) (Glycolipid 2-alpha-mannosyltransferase) (Q54DM9)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53954}; Single-pass membrane protein {ECO:0000250|UniProtKB:P53954}.
Interaction partners:
- Probable Dol-P-Man:Man
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Alpha-1,3/1,6-mannosyltransferase ALG2
- Dolichol-phosphate mannosyltransferase subunit 1
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Mannosyltransferase
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
Sequence:
MDELIMMVFVLFTIVLLLTVSMTLAALISTIVVLVVPLIICIIALLIALRIKYGSKKDLSEVSIGFFHPYCTAGGGGERVLWCAIKSIQEEYPYVRCVVYTGDKESDDEIFNKVKKTFDIELGRDNLEFIRLKKRKWVEASTYPRFTLIGQSLGSMILGWEALTKFVPTIFLDSMGYAFTFPIFSLIGGSTVACYVHYPTISSDMISSVKSSSYSFNNDVSISSNKFKTISKLIYYNIFSKIYQIVGSFSKLVMVNGTWTGNHIRDIWKKQFGYDLFIVYPPVDVKGRKQLKLGWMDGTRKNMILSIAQFRPEKNHQLQLRTLAHLLEKYPSHREQPLNTKLVLVGGVRDQADRDRVEQLRNLSKELNIEDHVEFQIGISSDQLNQLLSEASVGIHTMYNEHFGIGVVELMAAGVIPVANNSAGPKEDIVRHEDTGFLASTIQEYAEYIHEILAYREKYVEMQKKARDSTDRFSESNFSNQFLKYIKPLINQSLRNNNSSSKKRN
Protein: Uncharacterized protein (Q585A3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein L30 ferredoxin-like fold domain-containing protein
- Uncharacterized protein
- Large ribosomal subunit protein mL46
- Uncharacterized protein
- KOW domain-containing protein
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Large ribosomal subunit protein uL29m
Sequence:
MCCLYTSDVFFWSSLVVSPLPRIVRCVSAPQIRSIPCGSGDFSVMKRSLIARWQSGVHTPHGVVYRGAKMKNWPEQRIPENFKFTEEQRFRTKAIPRDVGTIPRNFVLGVLYRHQPCEVGGLWEHCTNDPEIVLDSKRHLREVLKQAREEGFVTFERDAISNEWLCFLTRERYEEVQRIVTAKSEAVDAHSGLRGAAATETSTYAEKFREMNVEAKEAHARRLEEEVANTTRYLRRFQQREIDYLPYTDLNGKVNFMWWYETRDVQQRADEVLTDSSSSKALAGEEEHKAGSQLEATTASTS
Protein: Trehalose-binding lipoprotein LpqY (SugABC transporter substrate-binding protein LpqY) (SugABC transporter SBP LpqY) (P9WGU9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ABC transporter complex LpqY-SugA-SugB-SugC, which is highly specific for uptake of trehalose. Involved in the recycling of extracellular trehalose released from trehalose-containing molecules synthesized by M.tuberculosis. Trehalose uptake is essential for virulence.
Subcellular location: Cell inner membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000269|PubMed:35775983}.
Interaction partners:
- Trehalose transport system permease protein SugB
- Trehalose import ATP-binding protein SugC
- Trehalose transport system permease protein SugA
- Trehalose import ATP-binding protein SugC
- Probable transmembrane protein
- Probable sugar-transport integral membrane protein ABC transporter UspB
- Probable sugar-transport integral membrane protein ABC transporter UspA
- Probable sugar-transport integral membrane protein ABC transporter
- Trehalose import ATP-binding protein SugC
- Probable Sn-glycerol-3-phosphate transport integral membrane protein ABC transporter UgpE
Sequence:
MVMSRGRIPRLGAAVLVALTTAAAACGADSQGLVVSFYTPATDGATFTAIAQRCNQQFGGRFTIAQVSLPRSPNEQRLQLARRLTGNDRTLDVMALDVVWTAEFAEAGWALPLSDDPAGLAENDAVADTLPGPLATAGWNHKLYAAPVTTNTQLLWYRPDLVNSPPTDWNAMIAEAARLHAAGEPSWIAVQANQGEGLVVWFNTLLVSAGGSVLSEDGRHVTLTDTPAHRAATVSALQILKSVATTPGADPSITRTEEGSARLAFEQGKAALEVNWPFVFASMLENAVKGGVPFLPLNRIPQLAGSINDIGTFTPSDEQFRIAYDASQQVFGFAPYPAVAPGQPAKVTIGGLNLAVAKTTRHRAEAFEAVRCLRDQHNQRYVSLEGGLPAVRASLYSDPQFQAKYPMHAIIRQQLTDAAVRPATPVYQALSIRLAAVLSPITEIDPESTADELAAQAQKAIDGMGLLP
Protein: Small ribosomal subunit protein uS19m (30S ribosomal protein S19, chloroplastic) (P92813)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Small ribosomal subunit protein uS14c
- Os08g0513300 protein
- Small ribosomal subunit protein bS18c
- Os02g0102400 protein
- Small ribosomal subunit protein uS2c
- Large ribosomal subunit protein bL36c
- Large ribosomal subunit protein uL2m
- Small ribosomal subunit protein uS11c
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein uL16m
Sequence:
MPRRSIWKGSFVDAFLFRIKKNRESLMSRKIWSRRSSILPEFVDCSVLIYNGKTFVRCKITEGKVGHKFGEFAFTRRRRPYQTNRGKGRKGKK
Protein: Helicase-like transcription factor (EC 2.3.2.27) (EC 3.6.4.-) (P113) (RING-type E3 ubiquitin transferase HLTF) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3) (Sucrose nonfermenting protein 2-like 3) (TNF-response element-binding protein) (Q6PCN7)
Organism: Mus musculus (Mouse)
Function: Has both helicase and E3 ubiquitin ligase activities. Possesses intrinsic ATP-dependent nucleosome-remodeling activity. This activity may be required for transcriptional activation or repression of specific target promoters (By similarity). These may include the SERPINE1, to which this protein can bind directly. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:9427542}. Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Nuclear localization is stimulated by progesterone. {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase RAD18
- Ubiquitin-conjugating enzyme E2 N
- Ubiquitin-conjugating enzyme E2 variant 2
- Proliferating cell nuclear antigen
- DNA repair protein RAD51 homolog 1
- Protein S100-A10
- Fanconi anemia group M protein homolog
- Structure-specific endonuclease subunit MUS81
- DNA repair protein RAD52 homolog
- DNA polymerase zeta catalytic subunit
Sequence:
MSYTFTRGPVWKYSQSVQYGSHENIPRLSYSTFLPHFEFQDIIPPDDFLTSDEEQDLVLFGTMRGQVVGLRYYTGVVNNNEMVALQREPNNPYDKNAIKVNNVNGNQVGHIKREIAAAVAYIMDNKLAQVEGVVPFGASNTFTMPLYMTFWGKEENRNVVLEQLKKHGFKLGPTPKTLGSSLENAWGSGRAGPSYSRPAHVAVQMTTDQLKTEFDKLFEDLKEDDRTVEMEPAEAIETPLLPHQKQALAWMIARENSKELPPFWEQRNDLYYNTITNFSVKERPENVHGGILADDMGLGKTLTAIAVILTNFDDGRPLLSKRGKKNHPGKEYKDETIKRRGSNMDKKEDGHSESSTCGEEPSISGTPEKSSCTLSQLSSVCPKRRKISVQYIESSDSEEIETSELPQKMKGKLKNVQLNTKSRVKGSSKVKEDSKFALTFFASATQRKMLKKGMSMMECSEACDTGERTRATLIICPLSVLSNWIDQFGQHVKSEVHLNFYVYYGPDRIRDSAWLSKQDIILTTYNILTHDYGTKDDSPLHSIKWLRVILDEGHAIRNPNAQQTKAVLELEAERRWVLTGTPIQNSLKDLWSLLSFLKLKPFIDREWWYRIIQRPVTTGDEGGLRRLQSLIKNITLRRTKTSKIKGKPVLELPERKVFIQHITLSEEERKIYQSVKNEGKAAIGRYFTEGTVLAHYADVLGLLLRLRQICCHTHLLTNGMSSSGPSRSDTPEELRKMLIEKMKIILSSGSDEECAICLDSLTFPVITHCAHVFCKPCICQVIHSEQPHAKCPLCRNEIHGDNLLECPPEELACDSDKESSMEWKSSSKINALMHALIELRTKDPNIKSLVVSQFTTFLSLIETPLKASGFVFTRLDGSMAQKKRVESIQRFQNTEAGSPTIMLLSLKAGGVGLNLCAASRVFLMDPAWNPAAEDQCFDRCHRLGQKQEVIITKFIVKDSVEENMLKIQNTKRDLAAGAFGTKKTDANDMKQAKINEIRTLIDL
Protein: Spalt 2 protein (Q90ZW5)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRRKQAKPQHLKSDEELQAEVVSEHAVPGEGADDGDSGNESRSGSEETNVCEKCCAEFFKWTDFLEHKKNCTKNPLVLIVNEDEAAPPPAEEFPEPSPASSPSDQAESEAAEEGVQPENSESSEVKSTEKEEEPMEVETAEKSFQNQGTSNTATPLPQLPEPSPMTSYTMPNTNVTLETLLSTKVAVAQFSQSARSAASASISSGVTAVAIPMILEQLMALQQQQIHQLQLIEQIRSQVAMMNRQPLRPALNPVVAAPGVTGQASNQLQGFATSAAIQLTAVLPPAIMGQAAGAQPPAFDGSQHISRPTSGASTPNISSSGSSAPPESSAPCSSNAITSVTPVSVSNTTISASQPQNASTPPSIGHGSLTSISNLPNPLLPQTSSNSVIFPNPLVSIAATANALDPLSALMKHRKGKPPNVSVFEPKSSSEDPFFKHKCRFCAKVFGSDSALQIHLRSHTGERPFKCNICGNRFSTKGNLKVHFQRHKEKYPHIQMNPYPVPEYLDNVPTCSGIPYGMSLPPEKPVTTWLDSKPVLPTIPTSIGLQLPPTIPGVNSYGDSPSITPMSRSPQRPSPASSECTSLSPSLNTSESGVPVSAESPQPVQSSSSVTKAEPISLPPASTRLGDHSLSGQVSTASTSSIPTIVTDSSVSTSLPNPVLPAVSDQFKAKFPFGGLLDSMQTSETSKLQQLVENIDKKMTDPNQCVICHRVLSCQSALKMHYRTHTGERPFKCKICGRAFTTKGNLKTHFGVHRAKPPLRVQHSCPICQKKFTNAVVLQQHIRMHMGGQIPNTPLPEGFQDAMDSELSYDEKNIDTLSNFDDDIDENSMEEDPELKDMASDSAKPLISYSGSCPSSPPSVISSIAALENQMKMIDSVMNCQQLTSLKSIENGSGESDHLSNDSSSAVGDLESQSAGSPAMSESSSSMQALSPVNSNSESFRSKSPGLSNQEEPQEIQLKTEKPDSPPPATENGGALDLTSTNPGRPVIKEEAPFSLLFLNRERGPSQSTPSLVTSTAPTMIKMEVNGHSKPISLGEVPSLPAGIQVPAAPQTVMSPGITPMLAPPPRRTPKQHNCQSCGKTFSSASALQIHERTHTGEKPFGCTICGRAFTTKGNLKVHMGTHMWNNAPARRGRRLSVENPMALLGGDALKFSEMFQKDLAARAMNVDPSFWNQYAAAITNGLAMKNNEISVIQNGGIPQLPVSLGGGAIPPLSNLTSGMDKARTGSSPPIVGLDKTSSETGASRPFTRFIEDNKEIGIN
Protein: tRNA-splicing endonuclease subunit Sen34 (EC 4.6.1.16) (A0A590UJW4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR017250}.
Interaction partners:
Sequence:
MLVVEVANGRSLVWGAEAVQALRERLGVGGRTVGALPRGPRQNSRLGLPLLLMPEEARLLAEIGAVTLVSAPRPDSRHHSLALTSFKRQQEESFQEQSALAAEARETRRQELLEKITEGQAAKKQKLEQASGASSSQEAGSSQAAKEDETSDGQASGEQEEAGPSSSQAGPSNGVAPLPRSALLVQLATARPRPVKARPLDWRVQSKDWPHAGRPAHELRYSIYRDLWERGFFLSAAGKFGGDFLVYPGDPLRFHAHYIAQCWAPEDTIPLQDLVAAGRLGTSVRKTLLLCSPQPDGFKSQEVSINLVYKCS
Protein: LD19767p (Q95RM4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYKQTSKNQRDSSINQIQNMKKLKKKFNRGSFDPNKKHLEKIFKKQSKLKQNDLQLDIDEKHFLQNSQTTSGLAIKANSNENALQADIPSQPPTVTSQIENNFRNSIYPVQPSVIQQTQVLLAEKKSGSEPERSKLDIFKKISKPRTPRPDIGATLVPPGTGVSVFGSTMTPSALISLPSGTTITPTPSLGLNSENKNVPSMKINPCNIFDGTIPLTKAGVEMSIIDSPKPKKRGRKPGGKNVIKQTNVVSQPLINKVERKKSSQAITLPLSSSPMIITQSSLNVSPPTEPLNLCNTEQPSNNFLSNLYAKEKKDRKKYKSLPENVMQLDKSCSPEKASTLHNSIRPTKQNNDVQCSDKFVTISNALSNASIYPGIQTGMVPLLPLLQFPPRPGLIPTGPGLFPAVTGLVGFGNHGNRIPISPFIDYPGPEESVADTVRCPPIKDSPVTDSDQFLSRSSTQTDLQMDRNYCNVAPLVPDSMKFAECKSVSCASTILENPSAQATSKINTKPLLEASGNPDDPIEVSDDSDESMHNRQMVQRKTPISSPTYVKTSFAELNPSSFTSAASNGEEKSKMDLRNIVSLSSNEPLKKFKKLVKQSFPDVKSVPHTPASHSSFPQFNLPNFMGGDKFSLAGGADLIPLSRVSDSEYSSKIVPFSSLGGTIPNQIKISEEHNIFFYLF
Protein: SCRIB overlapping open reading frame protein (oSCRIB) (C0HLS1)
Organism: Homo sapiens (Human)
Function: Represses translation of the downstream SCRIB protein. Translation of oSCRIB hinders SCRIB translation but does not completely abolish it, probably due to leaky scanning which allows the ribosome to bypass the weaker oSCRIB start codon and initiate translation at the stronger SCRIB start codon.
Interaction partners:
Sequence:
MRTEPRPPAPSPPSAAAGARAAHPHHAQVHPAVALQPARGVGGQAALFAAGRAGGDLPLQPQPGGAAARRQPAARAAQAFFPAAELAQAGPERQRDPAVASRGGQLHAAGGAGRVPERYP
Protein: DNA replication licensing factor MCM7 (EC 3.6.4.12) (Minichromosome maintenance protein 7) (AtMCM7) (Protein PROLIFERA) (P43299)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells (By similarity). Required for megagametophyte and embryo development.
Subcellular location: Nucleus {ECO:0000269|PubMed:19357199}. Cytoplasm {ECO:0000269|PubMed:19357199}. Note=Localized in the nucleus during G1, S and G2 phases of the cell cycle, and released into the cytoplasmic compartment during mitosis.
Interaction partners:
- DNA replication licensing factor MCM6
- Origin of replication complex subunit 6
- Cell division control protein 6 homolog
- Mini-chromosome maintenance complex-binding protein
- Origin of replication complex subunit 5
- DNA replication licensing factor MCM3
- Probable DNA helicase MCM8
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM5
- Minichromosome maintenance 10
Sequence:
MKDHDFDGDKGLAKGFLENFADANGRSKYMEILQEVSNRKIRAIQVDLDDLFNYKDESEEFLGRLTENTRRYVSIFSAAVDELLPEPTEAFPDDDHDILMTQRADDGTDNPDVSDPHQQIPSEIKRYYEVYFKAPSKGRPSTIREVKASHIGQLVRISGIVTRCSDVKPLMAVAVYTCEDCGHEIYQEVTSRVFMPLFKCPSSRCRLNSKAGNPILQLRASKFLKFQEAKMQELAEHVPKGHIPRSMTVHLRGELTRKVSPGDVVEFSGIFLPIPYTGFKALRAGLVADTYLEATSVTHFKKKYEEYEFQKDEEEQIARLAEDGDIYNKLSRSLAPEIYGHEDIKKALLLLLVGAPHRQLKDGMKIRGDVHICLMGDPGVAKSQLLKHIINVAPRGVYTTGKGSSGVGLTAAVMRDQVTNEMVLEGGALVLADMGICAIDEFDKMDESDRTAIHEVMEQQTVSIAKAGITTSLNARTAVLAAANPAWGRYDLRRTPAENINLPPALLSRFDLLWLILDRADMDSDLELAKHVLHVHQTEESPALGFEPLEPNILRAYISAARRLSPYVPAELEEYIATAYSSIRQEEAKSNTPHSYTTVRTLLSILRISAALARLRFSESVAQSDVDEALRLMQMSKISLYADDRQKAGLDAISDTYSIIRDEAARSKKTHVSYANALNWISRKGYSEAQLKECLEEYAALNVWQIDPHTFDIRFI
Protein: Hexokinase-1 (EC 2.7.1.1) (Hexokinase PI) (Hexokinase-A) (P04806)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate.
Interaction partners:
- Glucokinase-1
- Hexokinase-2
- Phosphoglucomutase 2
- Glucose-6-phosphate isomerase
- Invertase 2
- ATP-dependent 6-phosphofructokinase subunit alpha
- Glucose-6-phosphate 1-dehydrogenase
- Low glucose sensor SNF3
- Fructose-1,6-bisphosphatase
- High glucose sensor RGT2
Sequence:
MVHLGPKKPQARKGSMADVPKELMDEIHQLEDMFTVDSETLRKVVKHFIDELNKGLTKKGGNIPMIPGWVMEFPTGKESGNYLAIDLGGTNLRVVLVKLSGNHTFDTTQSKYKLPHDMRTTKHQEELWSFIADSLKDFMVEQELLNTKDTLPLGFTFSYPASQNKINEGILQRWTKGFDIPNVEGHDVVPLLQNEISKRELPIEIVALINDTVGTLIASYYTDPETKMGVIFGTGVNGAFYDVVSDIEKLEGKLADDIPSNSPMAINCEYGSFDNEHLVLPRTKYDVAVDEQSPRPGQQAFEKMTSGYYLGELLRLVLLELNEKGLMLKDQDLSKLKQPYIMDTSYPARIEDDPFENLEDTDDIFQKDFGVKTTLPERKLIRRLCELIGTRAARLAVCGIAAICQKRGYKTGHIAADGSVYNKYPGFKEAAAKGLRDIYGWTGDASKDPITIVPAEDGSGAGAAVIAALSEKRIAEGKSLGIIGA
Protein: Regulator of ribosome biosynthesis (Q08746)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for ribosome biogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10688653}.
Interaction partners:
- Ribosome biogenesis protein RLP24
- Nucleolar GTP-binding protein 2
- Ribosome assembly factor MRT4
- rRNA-processing protein CGR1
- Proteasome-interacting protein CIC1
- Ribosome biogenesis protein RLP7
- Ribosome biogenesis protein RPF2
- Ribosome biogenesis protein 15
- Nucleolar GTP-binding protein 1
- rRNA-processing protein EBP2
Sequence:
MSAEDYKNLPVTVEKPIPVVYDLGNLAAFDSNVLDKNDLDSSNARREEKIKSLTRDNVQLLINQLLSLPMKTTTESVGGTGGQSSVMTLLQLPDPTTDLPREKPLPKAKAMTKWEKFAAKKGIKPKERAGKMIYDEASGEWVPKWGYKGANKKLDDQWLVEVDDKVKGTDNELIDPRTLNRAERKRLVKKNEKQQRRNMKNAL
Protein: Type I acyl-CoA thioesterase mpaH' (EC 3.1.1.-) (Mycophenolic acid biosynthesis cluster protein H') (A0A0B5LB55)
Organism: Penicillium brevicompactum
Function: Type I acyl-CoA thioesterase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893. MpaH' acts as a peroxisomal acyl-CoA hydrolase that converts MPA-CoA into the final product MPA. The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable).
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:31209052}. Note=The mpaH' location in peroxisomes is required for the unique cooperation between biosynthetic and beta-oxidation catabolism machineries to produce final MPA. {ECO:0000269|PubMed:31209052}.
Interaction partners:
Sequence:
MSTEKFTITEHLVPGSHIREYPGSTVNQEDVLKIHVKQYTPKREGPVPDDAITFIATHGVGLPKELYEPLWDELLDQASGFHIRAIWMADVASMNQSGIHNEDKLSMDCSWMDHARDLLLMINHFRDQMPRPLVGIGHSFGGNIITNLAYLHPRLFTTLLLLDPLIQLSPPSLGFGTDAPSAINYTLWRDDVWPSREVAIRANRAIMQGMDPRCLDRMTKHFFRDLPTPLYPDVEAIKALFGTTADSTTTPVTLTTPKYHELVAQIRQNFNARDPKTGRIEVPRDTHADMDPLVAYIPLYRPEPRSTFRRLETLRPSCLWVIAGATFLNIDEIREGVKICGSGIGGSGGVPDGRVREVVLPGFGHLMPFQEVKTVAETCIVWLQQEMDRFRQTERQWKEDRDGKSHLAVEENWYKVLKPIPSGRKKRNDKGKL
Protein: Probable S-methylmethionine permease (Q47689)
Organism: Escherichia coli (strain K12)
Function: Transporter for the intake of S-methylmethionine.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Homocysteine S-methyltransferase
- Cystathionine gamma-synthase
- HTH-type transcriptional regulator MetR
- Methionine aminotransferase
Sequence:
MQTTQQNAPLKRTMKTRHLIMLSLGGVIGTGLFFNTGYIISTTGAAGTLLAYLIGALVVWLVMQCLGELSVAMPETGAFHVYAARYLGPATGYTVAWLYWLTWTVALGSSFTAAGFCMQYWFPQVPVWVWCVVFCAIIFGLNVISTRFFAEGEFWFSLVKVVTIIAFIILGGAAIFGFIPMQDGSPAPGLSNITAEGWFPHGGLPILMTMVAVNFAFSGTELIGIAAGETENPRKVIPVAIRTTIARLIIFFIGTVFVLAALIPMQQVGVEKSPFVLVFEKVGIPYAADIFNFVILTAILSAANSGLYASGRMLWSLSNERTLPACFARVTKNGVPLTALSVSMLGGVLALFSSVVAPDTVFVALSAISGFAVVAVWLSICASHFVFRRRHLQQGKALSELHYRAPWYPLVPVLGFVLCLVACVGLAFDPAQRIALWCGLPFVALCYGAYFLTQPRNAKQEPEHVAE