Identification |
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Name | E3 ubiquitin-protein ligase RSP5 |
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Synonyms | - Reverses SPT-phenotype protein 5
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Gene Name | RSP5 |
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Enzyme Class | Not Available |
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Biological Properties |
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General Function | ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway |
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Specific Function | E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general amino acid permease GAP1 as well as other cell surface proteins like GAP1, FUR4, MAL61, PMA1 and STE2. The RSP5-BUL1/2 complex is also necessary for the heat-shock element (HSE)-mediated gene expression, nitrogen starvation GLN3-dependent transcription, pressure-induced differential regulation of the two tryptophan permeases TAT1 and TAT2 and sorting efficiency into multivesicular bodies. Also acts on RBP1. Plays a role in tolerance to o-dinitrobenzene. Involved in actin cytoskeleton organization and dynamics. Ubiquitinates the LAS17-binding proteins LSB1 and PIN3/LSB2 without directing them for degradation and affects LAS17 levels in a SLA1-dependent and LSB1/2-independent manner. |
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Cellular Location | Not Available |
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SMPDB Pathways | Stress-activated signalling pathways: pheromone stress test 1 | PW012843 | |
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KEGG Pathways | Not Available |
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SMPDB Reactions | Not Available |
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KEGG Reactions | Not Available |
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Metabolites | |
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GO Classification | Function |
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ubiquitin-dependent protein catabolic process | extrinsic component of cytoplasmic side of plasma membrane | protein polyubiquitination | ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway | actin cortical patch | protein ubiquitination | protein ubiquitination involved in ubiquitin-dependent protein catabolic process | ubiquitin ligase complex | regulation of dolichol biosynthetic process | nucleus | ligase activity | regulation of ergosterol biosynthetic process | mitochondrion organization | phosphatidylinositol binding | regulation of mRNA export from nucleus | cytoplasm | ubiquitin protein ligase activity | regulation of multivesicular body size | positive regulation of transcription from RNA polymerase II promoter | ubiquitin-protein transferase activity | regulation of phosphate metabolic process | cellular bud tip | cellular response to UV | regulation of ribosomal large subunit export from nucleus | endosome membrane | chromatin assembly or disassembly | regulation of rRNA processing | Golgi apparatus | late endosome to vacuole transport via multivesicular body sorting pathway | regulation of tRNA export from nucleus | positive regulation of endocytosis | positive regulation of fatty acid biosynthetic process | regulation of tRNA processing | regulation of protein localization | positive regulation of proteasomal ubiquitin-dependent protein catabolic process | regulation of ubiquinone biosynthetic process | regulation of actin cytoskeleton organization | positive regulation of receptor-mediated endocytosis | response to drug | regulation of initiation of mating projection growth | proteasome-mediated ubiquitin-dependent protein catabolic process | ribophagy | ubiquitin binding | protein autoubiquitination | ubiquitin-dependent endocytosis | regulation of nitrogen utilization | protein monoubiquitination |
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Gene Properties |
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Chromosome Location | Not Available |
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Locus | |
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Gene Sequence | >2430 bp
ATGCCTTCATCCATATCCGTCAAGTTAGTGGCTGCAGAGTCATTATATAAGAGGGACGTA
TTCCGTTCCCCGGATCCGTTTGCTGTTCTGACTATTGATGGTTACCAAACCAAATCTACA
TCCGCAGCGAAGAAAACGTTAAATCCCTACTGGAATGAGACTTTCAAATTCGACGATATC
AATGAAAATTCTATTTTAACCATCCAAGTCTTTGATCAAAAGAAATTTAAAAAGAAGGAT
CAAGGGTTTCTTGGCGTGGTTAACGTCCGCGTGGGTGATGTTTTGGGCCATTTGGATGAA
GATACTGCTACATCGAGTGGTAGACCTCGCGAAGAAACTATTACTCGTGATTTAAAAAAA
TCTAATGACGGAATGGCCGTCAGCGGTAGGTTGATTGTTGTTTTATCAAAACTACCTTCG
TCAAGTCCGCATTCACAAGCTCCTTCTGGCCATACTGCATCTTCTAGTACGAATACAAGT
TCAACTACTCGAACAAATGGTCATTCTACTTCCTCCACCCGTAATCATTCAACGTCTCAT
CCTTCCAGAGGCACCGCGCAAGCAGTAGAATCAACTCTTCAAAGCGGTACAACAGCTGCT
ACTAATACGGCAACAACCAGTCACCGTTCCACCAATTCCACATCCAGTGCTACCAGACAA
TACTCTTCGTTTGAAGACCAGTATGGTCGTTTACCCCCTGGTTGGGAGAGAAGGACCGAT
AACTTTGGTCGTACATATTACGTCGATCATAACACAAGGACTACCACTTGGAAACGTCCA
ACGCTCGATCAAACAGAAGCCGAACGTGGCAACCAATTAAATGCAAATACTGAGTTAGAG
AGAAGGCAGCATAGGGGAAGAACTTTACCTGGTGGATCATCAGATAATTCCTCTGTAACA
GTTCAAGTGGGAGGTGGTTCCAATATACCTCCTGTTAATGGTGCAGCAGCAGCAGCGTTT
GCAGCTACAGGTGGTACCACATCTGGTTTAGGCGAATTACCTTCAGGCTGGGAGCAGCGA
TTTACTCCAGAAGGAAGAGCTTATTTCGTTGACCATAATACTAGAACAACCACTTGGGTG
GATCCAAGGAGACAACAGTATATACGTACTTATGGCCCTACAAATACCACCATTCAGCAA
CAACCGGTCTCCCAATTAGGTCCTTTGCCTTCTGGATGGGAAATGAGATTGACCAATACG
GCACGTGTATATTTCGTTGACCACAATACAAAAACAACGACCTGGGATGACCCAAGACTT
CCATCATCGCTAGACCAAAATGTTCCACAATACAAGCGTGACTTCAGACGTAAGGTTATT
TATTTCAGGTCCCAGCCCGCTCTTAGAATATTGCCGGGACAATGTCATATTAAAGTACGT
AGAAAGAACATTTTTGAGGATGCTTATCAAGAAATTATGAGACAAACCCCAGAAGATTTA
AAGAAAAGATTAATGATCAAGTTTGATGGTGAGGAAGGTTTAGATTACGGTGGTGTTTCC
AGAGAATTTTTCTTTTTATTATCACATGAGATGTTTAATCCATTTTATTGTTTGTTTGAA
TATTCTGCGTATGACAACTATACCATTCAAATAAATCCTAACAGTGGCATCAACCCCGAA
CATTTGAACTATTTCAAATTCATTGGTAGAGTTGTGGGTCTTGGTGTTTTCCATAGAAGA
TTTTTGGATGCATTCTTTGTAGGTGCACTTTACAAAATGATGCTACGTAAAAAAGTCGTA
TTGCAAGATATGGAAGGTGTTGACGCAGAGGTGTATAACTCATTAAACTGGATGCTTGAG
AATAGTATAGATGGTGTCTTGGATCTGACGTTCAGTGCCGACGATGAAAGATTCGGTGAA
GTTGTAACAGTGGATTTGAAGCCAGATGGGAGAAATATTGAAGTTACTGATGGTAATAAG
AAAGAATATGTCGAATTATATACCCAATGGAGAATTGTTGATAGAGTTCAAGAACAATTT
AAGGCATTCATGGATGGTTTTAACGAATTAATCCCCGAAGACTTAGTAACTGTGTTTGAT
GAGCGTGAACTAGAACTATTGATCGGTGGTATTGCGGAAATTGACATTGAAGATTGGAAG
AAACACACTGATTATCGTGGTTACCAAGAGTCAGACGAGGTCATTCAATGGTTTTGGAAG
TGTGTCAGTGAATGGGATAATGAACAAAGAGCCCGTTTATTGCAGTTCACCACTGGTACT
TCTCGTATACCTGTCAACGGGTTTAAAGATTTGCAAGGCTCTGATGGTCCAAGAAGATTC
ACTATTGAAAAAGCTGGTGAAGTACAACAATTGCCAAAATCTCACACATGTTTTAACAGA
GTTGATTTGCCACAATACGTTGATTATGACAGCATGAAACAGAAGCTAACATTGGCCGTG
GAAGAAACCATAGGGTTTGGTCAAGAATGA |
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Protein Properties |
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Pfam Domain Function | Not Available |
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Protein Residues | 809 |
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Protein Molecular Weight | 91815.63 |
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Protein Theoretical pI | Not Available |
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PDB File | show |
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Signalling Regions | Not Available |
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Transmembrane Regions | Not Available |
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Protein Sequence | >E3 ubiquitin-protein ligase RSP5
MPSSISVKLVAAESLYKRDVFRSPDPFAVLTIDGYQTKSTSAAKKTLNPYWNETFKFDDI
NENSILTIQVFDQKKFKKKDQGFLGVVNVRVGDVLGHLDEDTATSSGRPREETITRDLKK
SNDGMAVSGRLIVVLSKLPSSSPHSQAPSGHTASSSTNTSSTTRTNGHSTSSTRNHSTSH
PSRGTAQAVESTLQSGTTAATNTATTSHRSTNSTSSATRQYSSFEDQYGRLPPGWERRTD
NFGRTYYVDHNTRTTTWKRPTLDQTEAERGNQLNANTELERRQHRGRTLPGGSSDNSSVT
VQVGGGSNIPPVNGAAAAAFAATGGTTSGLGELPSGWEQRFTPEGRAYFVDHNTRTTTWV
DPRRQQYIRTYGPTNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRL
PSSLDQNVPQYKRDFRRKVIYFRSQPALRILPGQCHIKVRRKNIFEDAYQEIMRQTPEDL
KKRLMIKFDGEEGLDYGGVSREFFFLLSHEMFNPFYCLFEYSAYDNYTIQINPNSGINPE
HLNYFKFIGRVVGLGVFHRRFLDAFFVGALYKMMLRKKVVLQDMEGVDAEVYNSLNWMLE
NSIDGVLDLTFSADDERFGEVVTVDLKPDGRNIEVTDGNKKEYVELYTQWRIVDRVQEQF
KAFMDGFNELIPEDLVTVFDERELELLIGGIAEIDIEDWKKHTDYRGYQESDEVIQWFWK
CVSEWDNEQRARLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKAGEVQQLPKSHTCFNR
VDLPQYVDYDSMKQKLTLAVEETIGFGQE |
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References |
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External Links | Resource | Link |
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Saccharomyces Genome Database | RSP5 | Uniprot ID | P39940 | Uniprot Name | RSP5 | PDB ID | 3OLM |
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General Reference | Not Available |
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