UniProt ID | RAD23_YEAST | |
---|---|---|
UniProt AC | P32628 | |
Protein Name | UV excision repair protein RAD23 | |
Gene Name | RAD23 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 398 | |
Subcellular Localization | Nucleus . Cytoplasm . | |
Protein Description | Plays a central role both in proteasomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes.. | |
Protein Sequence | MVSLTFKNFKKEKVPLDLEPSNTILETKTKLAQSISCEESQIKLIYSGKVLQDSKTVSECGLKDGDQVVFMVSQKKSTKTKVTEPPIAPESATTPGRENSTEASPSTDASAAPAATAPEGSQPQEEQTATTERTESASTPGFVVGTERNETIERIMEMGYQREEVERALRAAFNNPDRAVEYLLMGIPENLRQPEPQQQTAAAAEQPSTAATTAEQPAEDDLFAQAAQGGNASSGALGTTGGATDAAQGGPPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARYPQLREHIMANPEVFVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEGSFQVDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD | |
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 |
---|---|---|---|---|---|
7 | Ubiquitination | -MVSLTFKNFKKEKV -CCCEEECCCCCCCC | 57.13 | 17644757 | |
10 | Ubiquitination | SLTFKNFKKEKVPLD CEEECCCCCCCCCCC | 70.21 | 22817900 | |
11 | Ubiquitination | LTFKNFKKEKVPLDL EEECCCCCCCCCCCC | 59.64 | 22817900 | |
13 | Acetylation | FKNFKKEKVPLDLEP ECCCCCCCCCCCCCC | 59.02 | 24489116 | |
13 | Ubiquitination | FKNFKKEKVPLDLEP ECCCCCCCCCCCCCC | 59.02 | 23749301 | |
28 | Ubiquitination | SNTILETKTKLAQSI CCCHHHHHHHHHHHC | 34.00 | 22817900 | |
30 | Ubiquitination | TILETKTKLAQSISC CHHHHHHHHHHHCCC | 43.30 | 23749301 | |
43 | Ubiquitination | SCEESQIKLIYSGKV CCCHHHEEEEECCCC | 22.61 | 17644757 | |
49 | Acetylation | IKLIYSGKVLQDSKT EEEEECCCCCCCCCC | 33.56 | 24489116 | |
49 | Ubiquitination | IKLIYSGKVLQDSKT EEEEECCCCCCCCCC | 33.56 | 23749301 | |
55 | Ubiquitination | GKVLQDSKTVSECGL CCCCCCCCCHHHCCC | 62.32 | 23749301 | |
56 | Phosphorylation | KVLQDSKTVSECGLK CCCCCCCCHHHCCCC | 32.96 | 27017623 | |
58 | Phosphorylation | LQDSKTVSECGLKDG CCCCCCHHHCCCCCC | 32.19 | 27017623 | |
63 | Ubiquitination | TVSECGLKDGDQVVF CHHHCCCCCCCEEEE | 44.97 | 17644757 | |
73 | Phosphorylation | DQVVFMVSQKKSTKT CEEEEEEEECCCCCC | 25.21 | 27017623 | |
75 | Ubiquitination | VVFMVSQKKSTKTKV EEEEEEECCCCCCCC | 40.98 | 17644757 | |
76 | Ubiquitination | VFMVSQKKSTKTKVT EEEEEECCCCCCCCC | 56.58 | 22817900 | |
79 | Ubiquitination | VSQKKSTKTKVTEPP EEECCCCCCCCCCCC | 54.14 | 22817900 | |
81 | Ubiquitination | QKKSTKTKVTEPPIA ECCCCCCCCCCCCCC | 49.03 | 23749301 | |
83 | Phosphorylation | KSTKTKVTEPPIAPE CCCCCCCCCCCCCCC | 44.31 | 28889911 | |
91 | Phosphorylation | EPPIAPESATTPGRE CCCCCCCCCCCCCCC | 29.83 | 19795423 | |
93 | Phosphorylation | PIAPESATTPGRENS CCCCCCCCCCCCCCC | 42.68 | 19795423 | |
94 | Phosphorylation | IAPESATTPGRENST CCCCCCCCCCCCCCC | 24.38 | 24930733 | |
100 | Phosphorylation | TTPGRENSTEASPST CCCCCCCCCCCCCCC | 23.91 | 22369663 | |
101 | Phosphorylation | TPGRENSTEASPSTD CCCCCCCCCCCCCCC | 47.34 | 22369663 | |
104 | Phosphorylation | RENSTEASPSTDASA CCCCCCCCCCCCCCC | 17.10 | 22369663 | |
106 | Phosphorylation | NSTEASPSTDASAAP CCCCCCCCCCCCCCC | 36.10 | 22369663 | |
107 | Phosphorylation | STEASPSTDASAAPA CCCCCCCCCCCCCCC | 38.68 | 22369663 | |
110 | Phosphorylation | ASPSTDASAAPAATA CCCCCCCCCCCCCCC | 27.98 | 22369663 | |
116 | Phosphorylation | ASAAPAATAPEGSQP CCCCCCCCCCCCCCC | 44.87 | 22369663 | |
121 | Phosphorylation | AATAPEGSQPQEEQT CCCCCCCCCCHHHHC | 36.71 | 22369663 | |
128 | Phosphorylation | SQPQEEQTATTERTE CCCHHHHCCCCCCCC | 29.29 | 23749301 | |
130 | Phosphorylation | PQEEQTATTERTESA CHHHHCCCCCCCCCC | 32.36 | 22369663 | |
131 | Phosphorylation | QEEQTATTERTESAS HHHHCCCCCCCCCCC | 22.47 | 22369663 | |
134 | Phosphorylation | QTATTERTESASTPG HCCCCCCCCCCCCCC | 28.23 | 22369663 | |
136 | Phosphorylation | ATTERTESASTPGFV CCCCCCCCCCCCCEE | 27.23 | 22369663 | |
138 | Phosphorylation | TERTESASTPGFVVG CCCCCCCCCCCEEEE | 44.40 | 22369663 | |
139 | Phosphorylation | ERTESASTPGFVVGT CCCCCCCCCCEEEEC | 27.44 | 22369663 | |
146 | Phosphorylation | TPGFVVGTERNETIE CCCEEEECCCCHHHH | 21.84 | 29136822 |
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 RAD23_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD23_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 RAD23_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94; SER-121; SER-136;SER-138 AND THR-139, AND MASS SPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND MASSSPECTROMETRY. |