| UniProt ID | EXOS1_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y3B2 | |
| Protein Name | Exosome complex component CSL4 | |
| Gene Name | EXOSC1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 195 | |
| Subcellular Localization | Nucleus, nucleolus . Nucleus . Cytoplasm . | |
| Protein Description | Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8.. | |
| Protein Sequence | MAPPVRYCIPGERLCNLEEGSPGSGTYTRHGYIFSSLAGCLMKSSENGALPVVSVVRETESQLLPDVGAIVTCKVSSINSRFAKVHILYVGSMPLKNSFRGTIRKEDVRATEKDKVEIYKSFRPGDIVLAKVISLGDAQSNYLLTTAENELGVVVAHSESGIQMVPISWCEMQCPKTHTKEFRKVARVQPEFLQT | |
| 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 |
|---|---|---|---|---|---|
| 6 | Methylation | --MAPPVRYCIPGER --CCCCCEEEECCCE | 26.78 | - | |
| 6 | Dimethylation | --MAPPVRYCIPGER --CCCCCEEEECCCE | 26.78 | - | |
| 21 | Phosphorylation | LCNLEEGSPGSGTYT EECCCCCCCCCCCEE | 29.39 | 30266825 | |
| 24 | Phosphorylation | LEEGSPGSGTYTRHG CCCCCCCCCCEECCC | 31.20 | 30266825 | |
| 26 | Phosphorylation | EGSPGSGTYTRHGYI CCCCCCCCEECCCEE | 24.34 | 30266825 | |
| 27 | Phosphorylation | GSPGSGTYTRHGYIF CCCCCCCEECCCEEE | 12.80 | 30266825 | |
| 28 | Phosphorylation | SPGSGTYTRHGYIFS CCCCCCEECCCEEEH | 18.94 | 30266825 | |
| 32 | Phosphorylation | GTYTRHGYIFSSLAG CCEECCCEEEHHHHH | 7.83 | 20090780 | |
| 44 | Phosphorylation | LAGCLMKSSENGALP HHHHHHCCCCCCCCC | 28.99 | 21406692 | |
| 45 | Phosphorylation | AGCLMKSSENGALPV HHHHHCCCCCCCCCE | 29.57 | 21406692 | |
| 54 | Phosphorylation | NGALPVVSVVRETES CCCCCEEEEEEECHH | 18.35 | 24719451 | |
| 74 | Ubiquitination | VGAIVTCKVSSINSR CCEEEEEEEHHCCCC | 35.47 | - | |
| 84 | Acetylation | SINSRFAKVHILYVG HCCCCCEEEEEEEEC | 31.47 | 26051181 | |
| 89 | Phosphorylation | FAKVHILYVGSMPLK CEEEEEEEECCCCCC | 11.36 | - | |
| 92 | Phosphorylation | VHILYVGSMPLKNSF EEEEEECCCCCCCCC | 13.74 | 23186163 | |
| 96 | Ubiquitination | YVGSMPLKNSFRGTI EECCCCCCCCCCCCC | 44.68 | - | |
| 98 | Phosphorylation | GSMPLKNSFRGTIRK CCCCCCCCCCCCCCH | 18.09 | 27422710 | |
| 113 | Ubiquitination | EDVRATEKDKVEIYK HHHCCCHHHCEEHHH | 59.50 | - | |
| 113 | Acetylation | EDVRATEKDKVEIYK HHHCCCHHHCEEHHH | 59.50 | 23749302 | |
| 115 | Ubiquitination | VRATEKDKVEIYKSF HCCCHHHCEEHHHHC | 53.48 | - | |
| 119 | Phosphorylation | EKDKVEIYKSFRPGD HHHCEEHHHHCCCCC | 6.25 | 29514088 | |
| 120 | Ubiquitination | KDKVEIYKSFRPGDI HHCEEHHHHCCCCCE | 49.10 | 21890473 | |
| 121 | Phosphorylation | DKVEIYKSFRPGDIV HCEEHHHHCCCCCEE | 14.98 | 29514088 | |
| 180 | Ubiquitination | QCPKTHTKEFRKVAR CCCCCCCHHHHHHHH | 47.45 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of EXOS1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EXOS1_HUMAN !! | ||||||
* 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 EXOS1_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY. | |
