| UniProt ID | RAD54_YEAST | |
|---|---|---|
| UniProt AC | P32863 | |
| Protein Name | DNA repair and recombination protein RAD54 | |
| Gene Name | RAD54 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 898 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Involved in DNA repair and mitotic recombination. Functions in the recombinational DNA repair (RAD52) pathway. Dissociates RAD51 from nucleoprotein filaments formed on dsDNA. Could be involved in the turnover of RAD51 protein-dsDNA filaments. Addition of RAD54 overcomes inhibition of DNA strand exchange by RAD51 bound to substrate dsDNA. Species preference in the RAD51 dissociation and DNA strand exchange assays underlines the importance of specific RAD54-RAD51 interactions. RAD51 is unable to release dsDNA upon ATP hydrolysis, leaving it stuck on the heteroduplex DNA product after DNA strand exchange.. | |
| Protein Sequence | MARRRLPDRPPNGIGAGERPRLVPRPINVQDSVNRLTKPFRVPYKNTHIPPAAGRIATGSDNIVGGRSLRKRSATVCYSGLDINADEAEYNSQDISFSQLTKRRKDALSAQRLAKDPTRLSHIQYTLRRSFTVPIKGYVQRHSLPLTLGMKKKITPEPRPLHDPTDEFAIVLYDPSVDGEMIVHDTSMDNKEEESKKMIKSTQEKDNINKEKNSQEERPTQRIGRHPALMTNGVRNKPLRELLGDSENSAENKKKFASVPVVIDPKLAKILRPHQVEGVRFLYRCVTGLVMKDYLEAEAFNTSSEDPLKSDEKALTESQKTEQNNRGAYGCIMADEMGLGKTLQCIALMWTLLRQGPQGKRLIDKCIIVCPSSLVNNWANELIKWLGPNTLTPLAVDGKKSSMGGGNTTVSQAIHAWAQAQGRNIVKPVLIISYETLRRNVDQLKNCNVGLMLADEGHRLKNGDSLTFTALDSISCPRRVILSGTPIQNDLSEYFALLSFSNPGLLGSRAEFRKNFENPILRGRDADATDKEITKGEAQLQKLSTIVSKFIIRRTNDILAKYLPCKYEHVIFVNLKPLQNELYNKLIKSREVKKVVKGVGGSQPLRAIGILKKLCNHPNLLNFEDEFDDEDDLELPDDYNMPGSKARDVQTKYSAKFSILERFLHKIKTESDDKIVLISNYTQTLDLIEKMCRYKHYSAVRLDGTMSINKRQKLVDRFNDPEGQEFIFLLSSKAGGCGINLIGANRLILMDPDWNPAADQQALARVWRDGQKKDCFIYRFISTGTIEEKIFQRQSMKMSLSSCVVDAKEDVERLFSSDNLRQLFQKNENTICETHETYHCKRCNAQGKQLKRAPAMLYGDATTWNHLNHDALEKTNDHLLKNEHHYNDISFAFQYISH | |
| 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 |
|---|---|---|---|---|---|
| 32 | Phosphorylation | RPINVQDSVNRLTKP CCCCHHHHHHCCCCC | 12.28 | 30377154 | |
| 130 | Phosphorylation | IQYTLRRSFTVPIKG HEEEECCCEEECCCC | 20.88 | 21126336 | |
| 132 | Phosphorylation | YTLRRSFTVPIKGYV EEECCCEEECCCCEE | 26.98 | 17563356 | |
| 155 | Phosphorylation | LGMKKKITPEPRPLH ECCCCCCCCCCCCCC | 30.40 | 27214570 | |
| 176 | Phosphorylation | AIVLYDPSVDGEMIV EEEEECCCCCCCEEE | 29.91 | 28889911 | |
| 187 | Phosphorylation | EMIVHDTSMDNKEEE CEEEECCCCCCCHHH | 30.14 | 28889911 | |
| 303 | Phosphorylation | EAEAFNTSSEDPLKS HHHHCCCCCCCCCCC | 32.60 | 27214570 | |
| 316 | Phosphorylation | KSDEKALTESQKTEQ CCCHHHHHHHHHHHH | 38.15 | 30377154 | |
| 318 | Phosphorylation | DEKALTESQKTEQNN CHHHHHHHHHHHHHC | 31.57 | 23749301 | |
| 651 | Phosphorylation | SKARDVQTKYSAKFS CCHHCCCHHHHHHHH | 31.62 | 27017623 | |
| 710 | Ubiquitination | DGTMSINKRQKLVDR CCCCCCCHHHHHHHH | 55.31 | 23749301 | |
| 808 | Ubiquitination | SSCVVDAKEDVERLF HHHCCCHHHHHHHHH | 50.40 | 23749301 | |
| 816 | Phosphorylation | EDVERLFSSDNLRQL HHHHHHHCCHHHHHH | 41.18 | 27214570 |
| 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 RAD54_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD54_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 RAD54_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-132 AND SER-318, ANDMASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-132, AND MASSSPECTROMETRY. | |
