Overview
| Uniprot ID | Q92878 |
|---|
| Protein Name | DNA repair protein RAD50 |
|---|
| Gene Name | RAD50 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 713 |
RLAPDKLKSTESELK |
Function
Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:15064416, PubMed:21757780, PubMed:27889449, PubMed:28134932, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:15064416, PubMed:21757780, PubMed:27889449, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:15064416, PubMed:27889449, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (PubMed:11741547, PubMed:9590181, PubMed:9651580, PubMed:9705271). Within the complex, RAD50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (PubMed:11741547, PubMed:12805565, PubMed:28134932). RAD50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the MRE11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity). The MRN complex is also required for DNA damage signaling via activation of the ATM and ATR kinases: the nuclease activity of MRE11 is not required to activate ATM and ATR (PubMed:15064416, PubMed:15790808, PubMed:16622404). The MRN complex is also required for the processing of R-loops (PubMed:31537797). In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888)
Protein Sequence
10
MSRIEKMSIL
20
GVRSFGIEDK
30
DKQIITFFSP
40
LTILVGPNGA
50
GKTTIIECLK
60
YICTGDFPPG
70
TKGNTFVHDP
80
KVAQETDVRA
90
QIRLQFRDVN
100
GELIAVQRSM
110
VCTQKSKKTE
120
FKTLEGVITR
130
TKHGEKVSLS
140
SKCAEIDREM
150
ISSLGVSKAV
160
LNNVIFCHQE
170
DSNWPLSEGK
180
ALKQKFDEIF
190
SATRYIKALE
200
TLRQVRQTQG
210
QKVKEYQMEL
220
KYLKQYKEKA
230
CEIRDQITSK
240
EAQLTSSKEI
250
VKSYENELDP
260
LKNRLKEIEH
270
NLSKIMKLDN
280
EIKALDSRKK
290
QMEKDNSELE
300
EKMEKVFQGT
310
DEQLNDLYHN
320
HQRTVREKER
330
KLVDCHRELE
340
KLNKESRLLN
350
QEKSELLVEQ
360
GRLQLQADRH
370
QEHIRARDSL
380
IQSLATQLEL
390
DGFERGPFSE
400
RQIKNFHKLV
410
RERQEGEAKT
420
ANQLMNDFAE
430
KETLKQKQID
440
EIRDKKTGLG
450
RIIELKSEIL
460
SKKQNELKNV
470
KYELQQLEGS
480
SDRILELDQE
490
LIKAERELSK
500
AEKNSNVETL
510
KMEVISLQNE
520
KADLDRTLRK
530
LDQEMEQLNH
540
HTTTRTQMEM
550
LTKDKADKDE
560
QIRKIKSRHS
570
DELTSLLGYF
580
PNKKQLEDWL
590
HSKSKEINQT
600
RDRLAKLNKE
610
LASSEQNKNH
620
INNELKRKEE
630
QLSSYEDKLF
640
DVCGSQDFES
650
DLDRLKEEIE
660
KSSKQRAMLA
670
GATAVYSQFI
680
TQLTDENQSC
690
CPVCQRVFQT
700
EAELQEVISD
710
LQSKLRLAPD
720
KLKSTESELK
730
KKEKRRDEML
740
GLVPMRQSII
750
DLKEKEIPEL
760
RNKLQNVNRD
770
IQRLKNDIEE
780
QETLLGTIMP
790
EEESAKVCLT
800
DVTIMERFQM
810
ELKDVERKIA
820
QQAAKLQGID
830
LDRTVQQVNQ
840
EKQEKQHKLD
850
TVSSKIELNR
860
KLIQDQQEQI
870
QHLKSTTNEL
880
KSEKLQISTN
890
LQRRQQLEEQ
900
TVELSTEVQS
910
LYREIKDAKE
920
QVSPLETTLE
930
KFQQEKEELI
940
NKKNTSNKIA
950
QDKLNDIKEK
960
VKNIHGYMKD
970
IENYIQDGKD
980
DYKKQKETEL
990
NKVIAQLSEC
1000
EKHKEKINED
1010
MRLMRQDIDT
1020
QKIQERWLQD
1030
NLTLRKRNEE
1040
LKEVEEERKQ
1050
HLKEMGQMQV
1060
LQMKSEHQKL
1070
EENIDNIKRN
1080
HNLALGRQKG
1090
YEEEIIHFKK
1100
ELREPQFRDA
1110
EEKYREMMIV
1120
MRTTELVNKD
1130
LDIYYKTLDQ
1140
AIMKFHSMKM
1150
EEINKIIRDL
1160
WRSTYRGQDI
1170
EYIEIRSDAD
1180
ENVSASDKRR
1190
NYNYRVVMLK
1200
GDTALDMRGR
1210
CSAGQKVLAS
1220
LIIRLALAET
1230
FCLNCGIIAL
1240
DEPTTNLDRE
1250
NIESLAHALV
1260
EIIKSRSQQR
1270
NFQLLVITHD
1280
EDFVELLGRS
1290
EYVEKFYRIK
1300
KNIDQCSEIV
1310
KCSVSSLGFN
VH
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0098687 |
chromosomal region |
| Cellular Component |
GO:0000781 |
chromosome, telomeric region |
| Cellular Component |
GO:0000794 |
condensed nuclear chromosome |
| Cellular Component |
GO:0016020 |
membrane |
| Cellular Component |
GO:0030870 |
Mre11 complex |
| Cellular Component |
GO:0016604 |
nuclear body |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0035861 |
site of double-strand break |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0016887 |
ATP hydrolysis activity |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0003691 |
double-stranded telomeric DNA binding |
| Molecular Function |
GO:0051880 |
G-quadruplex DNA binding |
| Molecular Function |
GO:0042802 |
identical protein binding |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Molecular Function |
GO:0043539 |
protein serine/threonine kinase activator activity |
| Molecular Function |
GO:0030674 |
protein-macromolecule adaptor activity |
| Molecular Function |
GO:0043047 |
single-stranded telomeric DNA binding |
| Biological Process |
GO:0070192 |
chromosome organization involved in meiotic cell cycle |
| Biological Process |
GO:0006974 |
DNA damage response |
| Biological Process |
GO:0000729 |
DNA double-strand break processing |
| Biological Process |
GO:0006310 |
DNA recombination |
| Biological Process |
GO:0006281 |
DNA repair |
| Biological Process |
GO:0110025 |
DNA strand resection involved in replication fork processing |
| Biological Process |
GO:0006302 |
double-strand break repair |
| Biological Process |
GO:0000724 |
double-strand break repair via homologous recombination |
| Biological Process |
GO:0035825 |
homologous recombination |
| Biological Process |
GO:0044818 |
mitotic G2/M transition checkpoint |
| Biological Process |
GO:1904354 |
negative regulation of telomere capping |
| Biological Process |
GO:2000781 |
positive regulation of double-strand break repair |
| Biological Process |
GO:0032206 |
positive regulation of telomere maintenance |
| Biological Process |
GO:0062176 |
R-loop processing |
| Biological Process |
GO:0007131 |
reciprocal meiotic recombination |
| Biological Process |
GO:0000019 |
regulation of mitotic recombination |
| Biological Process |
GO:0000723 |
telomere maintenance |
| Biological Process |
GO:0000722 |
telomere maintenance via recombination |
| Biological Process |
GO:0007004 |
telomere maintenance via telomerase |
| Biological Process |
GO:0031860 |
telomeric 3' overhang formation |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.