UniProt ID | SUS1_YEAST | |
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UniProt AC | Q6WNK7 | |
Protein Name | Transcription and mRNA export factor SUS1 {ECO:0000255|HAMAP-Rule:MF_03046} | |
Gene Name | SUS1 {ECO:0000255|HAMAP-Rule:MF_03046} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 96 | |
Subcellular Localization | Nucleus, nucleoplasm. Nucleus, nuclear pore complex. Cytoplasm, P-body. The nucleoplasm localization requires the presence of UBP8 and SGF11 to bind part of SUS1 to the SAGA complex. | |
Protein Description | Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is involved in RNA polymerase II-dependent regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). Within the SAGA complex, participates in a subcomplex with SGF11, SGF73 and UBP8 required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. SUS1 has also a role in mRNP biogenesis and maintenance of genome integrity through preventing RNA-mediated genome instability. Has a role in response to DNA damage induced by methyl methane sulfonate (MMS) and replication arrest induced by hydroxyurea. May also be involved in cytoplasmic mRNA decay by interaction with components of P-bodies.. | |
Protein Sequence | MTMDTAQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDLTKSEMNINESTNFTQILSTVEPKALEMVSDSTRETVLKQIREFLEEIVDTQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
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30 | Ubiquitination | ELISNELKARLLQEG HHCCHHHHHHHHHCC | 25.86 | 23749301 | |
46 | Phosphorylation | VDKVKDLTKSEMNIN HHHHHHHCHHHCCCC | 42.53 | 26447709 | |
48 | Phosphorylation | KVKDLTKSEMNINES HHHHHCHHHCCCCCC | 36.52 | 26447709 | |
55 | Phosphorylation | SEMNINESTNFTQIL HHCCCCCCCCHHHHH | 24.94 | 26447709 | |
56 | Phosphorylation | EMNINESTNFTQILS HCCCCCCCCHHHHHH | 28.33 | 26447709 | |
59 | Phosphorylation | INESTNFTQILSTVE CCCCCCHHHHHHCCC | 19.44 | 26447709 | |
68 | Ubiquitination | ILSTVEPKALEMVSD HHHCCCHHHHHHCCH | 52.69 | 22106047 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of SUS1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of SUS1_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of SUS1_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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