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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: X-ray repair cross-complementing protein 5

UniprotKB/SwissProt ID: XRCC5_HUMAN (P13010)

Gene Name: XRCC5

Synonyms: G22P2

Organism: Homo sapiens (Human).

Function: Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. The XRCC5/6 dimer probably also acts as a 5'- deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Nucleus, nucleolus. Chromosome.

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Network with metabolic pathway:
Kegg map ID Pathway Link
map03450Non-homologous end-joining
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1JEQ X-ray 2.70 A B1-565Link
1JEY X-ray 2.50 A B1-565Link
1Q2Z NMR - A592-708Link
1RW2 NMR - A566-709Link
3RZ9 X-ray 2.29 A B559-571Link

The S-nitrosylation sites of XRCC5_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1235YSFSESLRKL C VFKKIERHSI   3.66%HC0319483679in vivo
2249KIERHSIHWP C RLTIGSNLSI   4.74%HC0122178444-
3249KIERHSIHWP C RLTIGSNLSI   4.74%HC0120140087in vivo
4296KEDIQKETVY C LNDDDETEVL   2.19%HC1219483679in vivo
5339EQMKYKSEGK C FSVLGFCKSS   4.52%HC1119483679in vivo
6346EGKCFSVLGF C KSSQVQRRFF   3.87%HC0719483679in vivo
7493PNPRFQRLFQ C LLHRALHPRE   3.23%HC0122178444-
8493PNPRFQRLFQ C LLHRALHPRE   3.23%HC0119483679in vivo