UniProt ID | XRCC3_HUMAN | |
---|---|---|
UniProt AC | O43542 | |
Protein Name | DNA repair protein XRCC3 | |
Gene Name | XRCC3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 346 | |
Subcellular Localization | Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Mitochondrion. Accumulates in discrete nuclear foci prior to DNA damage, and these foci persist throughout the time course of DNA repair. | |
Protein Description | Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD21 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C.. | |
Protein Sequence | MDLDLLDLNPRIIAAIKKAKLKSVKEVLHFSGPDLKRLTNLSSPEVWHLLRTASLHLRGSSILTALQLHQQKERFPTQHQRLSLGCPVLDALLRGGLPLDGITELAGRSSAGKTQLALQLCLAVQFPRQHGGLEAGAVYICTEDAFPHKRLQQLMAQQPRLRTDVPGELLQKLRFGSQIFIEHVADVDTLLECVNKKVPVLLSRGMARLVVIDSVAAPFRCEFDSQASAPRARHLQSLGATLRELSSAFQSPVLCINQVTEAMEEQGAAHGPLGFWDERVSPALGITWANQLLVRLLADRLREEEAALGCPARTLRVLSAPHLPPSSCSYTISAEGVRGTPGTQSH | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MDLDLLDL -------CCCCHHCC | 11.87 | 22814378 | |
17 | 2-Hydroxyisobutyrylation | PRIIAAIKKAKLKSV HHHHHHHHHHHCCCH | 41.79 | - | |
18 | Ubiquitination | RIIAAIKKAKLKSVK HHHHHHHHHHCCCHH | 44.64 | - | |
23 | Phosphorylation | IKKAKLKSVKEVLHF HHHHHCCCHHHHHHH | 49.19 | - | |
25 | Ubiquitination | KAKLKSVKEVLHFSG HHHCCCHHHHHHHCC | 49.55 | - | |
36 | Ubiquitination | HFSGPDLKRLTNLSS HHCCCCHHHHCCCCC | 53.38 | - | |
39 | Phosphorylation | GPDLKRLTNLSSPEV CCCHHHHCCCCCHHH | 37.84 | 27732954 | |
42 | Phosphorylation | LKRLTNLSSPEVWHL HHHHCCCCCHHHHHH | 46.01 | 24719451 | |
43 | Phosphorylation | KRLTNLSSPEVWHLL HHHCCCCCHHHHHHH | 28.39 | 27732954 | |
52 | Phosphorylation | EVWHLLRTASLHLRG HHHHHHHHHHHHHCC | 22.14 | 24719451 | |
72 | Ubiquitination | ALQLHQQKERFPTQH HHHHHHHHHCCCCHH | 44.26 | - | |
172 | Ubiquitination | VPGELLQKLRFGSQI CCHHHHHHHHHCCEE | 41.41 | 2190698 | |
177 | Phosphorylation | LQKLRFGSQIFIEHV HHHHHHCCEEEEEEE | 19.86 | - | |
189 | Phosphorylation | EHVADVDTLLECVNK EEECCHHHHHHHHHC | 32.84 | - | |
196 | Ubiquitination | TLLECVNKKVPVLLS HHHHHHHCCCCHHHH | 34.45 | - | |
197 | Ubiquitination | LLECVNKKVPVLLSR HHHHHHCCCCHHHHC | 46.71 | - | |
225 | Phosphorylation | PFRCEFDSQASAPRA CEECCCCCCCCCCHH | 32.73 | 17525332 | |
241 | Phosphorylation | HLQSLGATLRELSSA HHHHHHHHHHHHHHH | 25.26 | - |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of XRCC3_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 XRCC3_HUMAN !! |
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Phosphorylation | |
Reference | PubMed |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY. |