Search Results
Overview
| Uniprot ID | A0A286Y121 |
|---|---|
| Protein Name | DNA repair protein XRCC1 |
| Gene Name | XRCC1 |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 169 | SQKVTVTKLGQFRVK |
| 247 | ESPKGKRKLDLNVEE |
Function
Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes. Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity. Recognizes and binds poly-ADP-ribose chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting its activity
Protein Sequence
10
MPEIRLRHVV
20
SCSSQDSTHC
30
AENLLKADTY
40
RKWRAAKAGE
50
KSISVVLQLE
60
KEEQIHSVDI
70
GNNGSAFVEV
80
LVGSSAGGAS
90
EQDYEVLLVT
100
SSFMSPSESR
110
SGSNPNRVRI
120
FGPDKLVRAA
130
AEKRWDRIKI
140
VCSQPYTKDS
150
PYGLSFIRLH
160
SPPDKEEAEV
170
PSQKVTVTKL
180
GQFRVKEEDE
190
SASSLRPGAL
200
FFGRINKTSP
210
ATTSDPTGPS
220
YAAATLQASS
230
ATASASPISK
240
AVGSTSQPQE
250
SPKGKRKLDL
260
NVEEKKAPSK
270
PSAQLSPPAL
280
KRPKLPAPTR
290
TPAAAPVPAA
300
AQRAVPGKPR
310
GDGTEPRGAR
320
AGPQELGKIL
330
QGVVVVLSGF
340
QNPFRSELRD
350
KALELGAKYR
360
PDWTPDSTHL
370
ICAFANTPKY
380
SQVLGLGGRI
390
VRKEWVLDCH
400
RMRRRLPSRR
410
YLMAGPDSSS
420
EEEGGCPSGS
430
SGDEAPRLPR
440
KTKAKPPPAS
450
GPGSPQKPLS
460
PKETKAASLG
470
PQENSDTEEE
480
QSAGRDDGEE
490
ESGDTEDELR
500
RVAEQREHRP
510
APGQENGEDP
520
YAGSTDENTD
530
NEDRPESPDQ
540
PIPELPDFFQ
550
GKHFFLYGEF
560
PGDERRKLIR
570
YVTAFNGELE
580
DYMSDRVQFV
590
ITAQEWDPSF
600
EEALMDNPSL
610
AFVRPRWIYS
620
CNEKQKLLPH
QLYGVVPQA
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0070522 | ERCC4-ERCC1 complex |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0090734 | site of DNA damage |
| Molecular Function | GO:1990599 | 3' overhang single-stranded DNA endodeoxyribonuclease activity |
| Molecular Function | GO:0160002 | ADP-D-ribose modification-dependent protein binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0032356 | oxidized DNA binding |
| Molecular Function | GO:0072572 | poly-ADP-D-ribose binding |
| Molecular Function | GO:1990165 | single-strand break-containing DNA binding |
| Biological Process | GO:0006284 | base-excision repair |
| Biological Process | GO:0006303 | double-strand break repair via nonhomologous end joining |
| Biological Process | GO:1905765 | negative regulation of protection from non-homologous end joining at telomere |
| Biological Process | GO:1905051 | regulation of base-excision repair |
| Biological Process | GO:0033194 | response to hydroperoxide |
| Biological Process | GO:0000012 | single strand break repair |
| Biological Process | GO:0061819 | telomeric DNA-containing double minutes formation |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.