Search Results
Overview
| Uniprot ID | H0UT14 |
|---|---|
| Protein Name | Replication protein A subunit |
| Gene Name | RPA1 |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 163 | PKAYGASKTFGKPGG |
| 88 | 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
MAGQLSEGAI
20
AAIMQQGDTS
30
IKPILQVISI
40
RPITTGNNPP
50
RYRLLMSDGI
60
NTLSSFMLAT
70
QMNSLVEQEQ
80
LAANCICQID
90
RFIVNTLKDG
100
RRVVILMELK
110
VLKSADMVGV
120
KIGNPLPYNE
130
GQGQPQAVPS
140
PVTASSPLTG
150
RPQQQNGSSG
160
VGSSVPKAYG
170
ASKTFGKPGG
180
SGLLHPSGGT
190
QSKVVPIVSL
200
TPYQSKWTIR
210
ARVTNKSQIR
220
TWSNSRGEGK
230
LFSLELVDES
240
GEIRAAAFNE
250
QVDKFFPLIE
260
VNKVYYFSKG
270
SLKIANKQFS
280
AVKNDYEMTF
290
NSETSVVPCE
300
DDHHLPTVQF
310
DFTGIDDLEN
320
KSKDSLVDII
330
GICKSYEDAT
340
KITVKSNNRE
350
VAKRNIYLMD
360
TSGKVVTATL
370
WGEDADKFDG
380
SRQPVIAIKG
390
ARVSDFGGRS
400
LSVLSSSTII
410
MNPDIPEAYK
420
LRGWFDTEGQ
430
TLDGVSISDL
440
KGGALGTSNT
450
NWKTLYEVKS
460
ENLGQGDKAD
470
YFSSVATVVY
480
LRKENCMYQA
490
CPTQECNKKV
500
IDQQNGLYRC
510
EKCDREFPNF
520
KYRMILSANI
530
ADFQENQWVT
540
CFQESAEAIL
550
GQNTAYLGEL
560
KDKNEQAFEE
570
VFQNANFRSF
580
TFKIRVKLET
590
YNDESRVKAT
600
VMDVKPVDYR
610
DYGRRLIMNI
RRNAGM
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005662 | DNA replication factor A complex |
| 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: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: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:0000723 | telomere maintenance |
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.