P39001 · UME6_YEAST
- ProteinTranscriptional regulatory protein UME6
- GeneUME6
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids836 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Binds to the URS1 site (5'-AGCCGCCGA-3') and recruits the RPD3 histone deacetylase complex to the promoters to negatively regulate the expression of many genes including CAR1 (arginase), several required for sporulation, mating type switching, inositol metabolism, and oxidative carbon metabolism. Recruits also the ISW2 chromatin remodeling complex to promoters in a second gene repression pathway. Associates with the master regulator of meiosis IME1 in order to activate the expression of meiosis genes. Has both a positive and negative role in regulating phospholipid biosynthesis.
Miscellaneous
Present with 217 molecules/cell in log phase SD medium.
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 771-798 | Zn2-C6 fungal-type | ||||
Sequence: CWICRLRKKKCTEERPHCFNCERLKLDC |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscriptional regulatory protein UME6
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP39001
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 99 | Impairs meiotic genes expression and sporulation, reduces interactions with IME1 and RIM11, and reduces phosphorylation. | ||||
Sequence: T → N or A | ||||||
Mutagenesis | 99-107 | Impairs meiotic genes expression and sporulation, reduces the interaction with IME1, and abolishes phosphorylation. | ||||
Sequence: TPVHTPSGS → APVHAPSGA | ||||||
Mutagenesis | 99-109 | Impairs meiotic genes expression, sporulation and interactions with IME1 and RIM11, and abolishes phosphorylation. | ||||
Sequence: TPVHTPSGSPS → APVHAPAGAPA | ||||||
Mutagenesis | 103 | Impairs meiotic genes expression and sporulation, reduces interaction with IME, and reduces phosphorylation. | ||||
Sequence: T → A | ||||||
Mutagenesis | 107 | Impairs meiotic genes expression and sporulation, reduces interaction with IME, and reduces phosphorylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 523 | Impairs SIN3-binding and gene repression activity. | ||||
Sequence: A → S | ||||||
Mutagenesis | 524 | Impairs gene repression activity. | ||||
Sequence: A → T | ||||||
Mutagenesis | 525 | Impairs gene repression activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 526 | Impairs gene repression activity. | ||||
Sequence: V → Q | ||||||
Mutagenesis | 527 | Impairs SIN3-binding and gene repression activity. | ||||
Sequence: L → P | ||||||
Mutagenesis | 528 | Impairs SIN3-binding and gene repression activity. | ||||
Sequence: S → P | ||||||
Mutagenesis | 530 | Impairs SIN3-binding and gene repression activity. | ||||
Sequence: M → T or V | ||||||
Mutagenesis | 635 | Impairs gene repression activity. | ||||
Sequence: K → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 18 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000114987 | 1-836 | Transcriptional regulatory protein UME6 | |||
Sequence: MLDKARSQSKHMDESNAAASLLSMETTANNHHYLHNKTSRATLMNSSQDGKKHAEDEVSDGANSRHPTISSASIESLKTTYDENPLLSIMKSTCAPNNTPVHTPSGSPSLKVQSGGDIKDDPKENDTTTTTNTTLQDRRDSDNAVHAAASPLAPSNTPSDPKSLCNGHVAQATDPQISGAIQPQYTATNEDVFPYSSTSTNSNTATTTIVAGAKKKIHLPPPQAPAVSSPGTTAAGSGAGTGSGIRSRTGSDLPLIITSANKNNGKTTNSPMSILSRNNSTNNNDNNSIQSSDSRESSNNNEIGGYLRGGTKRGGSPSNDSQVQHNVHDDQCAVGVAPRNFYFNKDREITDPNVKLDENESKINISFWLNSKYRDEAYSLNESSSNNASSNTDTPTNSRHANTSSSITSRNNFQHFRFNQIPSQPPTSASSFTSTNNNNPQRNNINRGEDPFATSSRPSTGFFYGDLPNRNNRNSPFHTNEQYIPPPPPKYINSKLDGLRSRLLLGPNSASSSTKLDDDLGTAAAVLSNMRSSPYRTHDKPISNVNDMNNTNALGVPASRPHSSSFPSKGVLRPILLRIHNSEQQPIFESNNSTAVFDEDQDQNQDLSPYHLNLNSKKVLDPTFESRTRQVTWNKNGKRIDRRLSAPEQQQQLEVPPLKKSRRSVGNARVASQTNSDYNSLGESSTSSAPSSPSLKASSGLAYTADYPNATSPDFAKSKGKNVKPKAKSKAKQSSKKRPNNTTSKSKANNSQESNNATSSTSQGTRSRTGCWICRLRKKKCTEERPHCFNCERLKLDCHYDAFKPDFVSDPKKKQMKLEEIKKKTKEAKRRAMKKK | ||||||
Modified residue | 114 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 141 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 150 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 228 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 316 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 318 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 645 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by RIM11 and MCK1.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6. Interacts with RIM11, MCK1 and IME1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P39001 | IME1 P21190 | 3 | EBI-20086, EBI-9199 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-77 | Disordered | ||||
Sequence: MLDKARSQSKHMDESNAAASLLSMETTANNHHYLHNKTSRATLMNSSQDGKKHAEDEVSDGANSRHPTISSASIESL | ||||||
Compositional bias | 12-48 | Polar residues | ||||
Sequence: MDESNAAASLLSMETTANNHHYLHNKTSRATLMNSSQ | ||||||
Compositional bias | 63-77 | Polar residues | ||||
Sequence: NSRHPTISSASIESL | ||||||
Compositional bias | 92-112 | Polar residues | ||||
Sequence: STCAPNNTPVHTPSGSPSLKV | ||||||
Region | 92-168 | Disordered | ||||
Sequence: STCAPNNTPVHTPSGSPSLKVQSGGDIKDDPKENDTTTTTNTTLQDRRDSDNAVHAAASPLAPSNTPSDPKSLCNGH | ||||||
Compositional bias | 150-168 | Polar residues | ||||
Sequence: SPLAPSNTPSDPKSLCNGH | ||||||
Region | 218-332 | Disordered | ||||
Sequence: HLPPPQAPAVSSPGTTAAGSGAGTGSGIRSRTGSDLPLIITSANKNNGKTTNSPMSILSRNNSTNNNDNNSIQSSDSRESSNNNEIGGYLRGGTKRGGSPSNDSQVQHNVHDDQC | ||||||
Compositional bias | 228-305 | Polar residues | ||||
Sequence: SSPGTTAAGSGAGTGSGIRSRTGSDLPLIITSANKNNGKTTNSPMSILSRNNSTNNNDNNSIQSSDSRESSNNNEIGG | ||||||
Compositional bias | 314-328 | Polar residues | ||||
Sequence: GGSPSNDSQVQHNVH | ||||||
Region | 381-464 | Disordered | ||||
Sequence: NESSSNNASSNTDTPTNSRHANTSSSITSRNNFQHFRFNQIPSQPPTSASSFTSTNNNNPQRNNINRGEDPFATSSRPSTGFFY | ||||||
Region | 508-594 | SIN3-binding | ||||
Sequence: NSASSSTKLDDDLGTAAAVLSNMRSSPYRTHDKPISNVNDMNNTNALGVPASRPHSSSFPSKGVLRPILLRIHNSEQQPIFESNNST | ||||||
Region | 636-766 | Disordered | ||||
Sequence: NGKRIDRRLSAPEQQQQLEVPPLKKSRRSVGNARVASQTNSDYNSLGESSTSSAPSSPSLKASSGLAYTADYPNATSPDFAKSKGKNVKPKAKSKAKQSSKKRPNNTTSKSKANNSQESNNATSSTSQGTR | ||||||
Compositional bias | 666-699 | Polar residues | ||||
Sequence: GNARVASQTNSDYNSLGESSTSSAPSSPSLKASS | ||||||
Compositional bias | 736-766 | Polar residues | ||||
Sequence: KKRPNNTTSKSKANNSQESNNATSSTSQGTR |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length836
- Mass (Da)91,124
- Last updated1996-10-01 v2
- Checksum0DDA0A6B4A157182
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 12-48 | Polar residues | ||||
Sequence: MDESNAAASLLSMETTANNHHYLHNKTSRATLMNSSQ | ||||||
Compositional bias | 63-77 | Polar residues | ||||
Sequence: NSRHPTISSASIESL | ||||||
Compositional bias | 92-112 | Polar residues | ||||
Sequence: STCAPNNTPVHTPSGSPSLKV | ||||||
Sequence conflict | 101 | in Ref. 3; BAA04890 | ||||
Sequence: V → G | ||||||
Compositional bias | 150-168 | Polar residues | ||||
Sequence: SPLAPSNTPSDPKSLCNGH | ||||||
Compositional bias | 228-305 | Polar residues | ||||
Sequence: SSPGTTAAGSGAGTGSGIRSRTGSDLPLIITSANKNNGKTTNSPMSILSRNNSTNNNDNNSIQSSDSRESSNNNEIGG | ||||||
Compositional bias | 314-328 | Polar residues | ||||
Sequence: GGSPSNDSQVQHNVH | ||||||
Sequence conflict | 363 | in Ref. 1; AAA34471 | ||||
Sequence: I → V | ||||||
Sequence conflict | 443 | in Ref. 1; AAA34471 | ||||
Sequence: N → T | ||||||
Sequence conflict | 465 | in Ref. 1; AAA34471 | ||||
Sequence: G → D | ||||||
Compositional bias | 666-699 | Polar residues | ||||
Sequence: GNARVASQTNSDYNSLGESSTSSAPSSPSLKASS | ||||||
Compositional bias | 736-766 | Polar residues | ||||
Sequence: KKRPNNTTSKSKANNSQESNNATSSTSQGTR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L32186 EMBL· GenBank· DDBJ | AAA34471.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L24539 EMBL· GenBank· DDBJ | AAC14472.1 EMBL· GenBank· DDBJ | Unassigned DNA | ||
D23663 EMBL· GenBank· DDBJ | BAA04890.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z68194 EMBL· GenBank· DDBJ | CAA92346.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006938 EMBL· GenBank· DDBJ | DAA12048.1 EMBL· GenBank· DDBJ | Genomic DNA |