Search Results
Overview
| Uniprot ID | A0A5G2QMX3 |
|---|---|
| Protein Name | Replication protein A subunit |
| Gene Name | RPA1 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 156 | SKAYGASKIFGKAGA |
| 160 | GASKIFGKAGATSVV |
| 199 | ICARVTNKSQIRTWS |
| 252 | NKVYYFSKGTLKIAN |
| 256 | YFSKGTLKIANKQFT |
| 260 | GTLKIANKQFTAVKN |
| 324 | KNYEDVTKITVKSTN |
| 328 | DVTKITVKSTNREVS |
| 482 | PTQDCNKKVIDQQNG |
| 570 | FTFRIRVKLETYNDE |
| 81 | RFIVNTLKDGRRVVI |
Function
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage
Protein Sequence
10
FIFHLLQEAA
20
SDFLQVRLCV
30
LNIRPITTGN
40
NPPRYRLLMS
50
DGLNTLSSFM
60
LATQLNPLVE
70
EERLSSNCIC
80
QINRFIVNTL
90
KDGRRVVILM
100
DLEVLKSAEA
110
VGVKIGNPVP
120
YNEGHGQQPV
130
VPPPVSAASP
140
PTSNPQQQNG
150
SSGVGSTVSK
160
AYGASKIFGK
170
AGATSVVNSS
180
GGTQAKVVPI
190
ASLTPYQSKW
200
TICARVTNKS
210
QIRTWSNSRG
220
EGKLFSIELV
230
DESGEIRATA
240
FNEQVDKFFP
250
LIDVNKVYYF
260
SKGTLKIANK
270
QFTAVKNDYE
280
MTFSNETSVM
290
PCEDGHHLPT
300
VQFDFTGIAD
310
LENKSKDSLV
320
DIIGICKNYE
330
DVTKITVKST
340
NREVSKRNIY
350
LMDMSGKVVN
360
ATLWGEDADK
370
FDGSRQPVMA
380
IKGARVSDFG
390
GRSLSILSSS
400
TVIVNPDIPE
410
AYKLRGWFDS
420
EGQALDGVSI
430
SDLKSGGIGG
440
SNTNWKTLYE
450
VKSENLGQGD
460
KPDYFSAVAT
470
VVYLRKENCM
480
YQACPTQDCN
490
KKVIDQQNGL
500
YRCEKCDSEF
510
PNFKYRMILS
520
VNIADFQENQ
530
WVTCFQESAE
540
AILGQSTAYL
550
GELKEKNEQA
560
FEEVFQNANF
570
RSFTFRIRVK
580
LETYNDESRI
590
KGTVMDVKPV
600
DYKEYGRRLI
MSIRKNAAM
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005662 | DNA replication factor A complex |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006284 | base-excision repair |
| Biological Process | GO:0006260 | DNA replication |
| Biological Process | GO:0000724 | double-strand break repair via homologous recombination |
| Biological Process | GO:0051321 | meiotic cell cycle |
| Biological Process | GO:0006298 | mismatch repair |
| Biological Process | GO:0006289 | nucleotide-excision repair |
| Biological Process | GO:1990166 | protein localization to site of double-strand break |
| Biological Process | GO:0007004 | telomere maintenance via telomerase |
| Cellular Component | GO:0000800 | lateral element |
| Cellular Component | GO:0001673 | male germ cell nucleus |
| Cellular Component | GO:0016605 | PML body |
| Cellular Component | GO:0035861 | site of double-strand break |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0140463 | chromatin-protein adaptor activity |
| Molecular Function | GO:0003684 | damaged DNA binding |
| Molecular Function | GO:0098505 | G-rich strand telomeric DNA binding |
| Molecular Function | GO:0043047 | single-stranded telomeric DNA binding |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.