Overview
| Uniprot ID | Q8IY92 |
| Protein Name | Structure-specific endonuclease subunit SLX4 |
| Gene Name | SLX4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 1093 |
RSILTLSKEPGHQKG |
Function
Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures originating from replication and recombination intermediates and from DNA damage. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5'-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products. Interacts with the structure-specific ERCC4-ERCC1 endonuclease and promotes the cleavage of bubble structures. Interacts with the structure-specific MUS81-EME1 endonuclease and promotes the cleavage of 3'-flap and replication fork-like structures. SLX4 is required for recovery from alkylation-induced DNA damage and is involved in the resolution of DNA double-strand breaks
Protein Sequence
10
MKLSVNEAQL
20
GFYLGSLSHL
30
SACPGIDPRS
40
SEDQPESLKT
50
GQMMDESDED
60
FKELCASFFQ
70
RVKKHGIKEV
80
SGERKTQKAA
90
SNGTQIRSKL
100
KRTKQTATKT
110
KTLQGPAEKK
120
PPSGSQAPRT
130
KKQRVTKWQA
140
SEPAHSVNGE
150
GGVLASAPDP
160
PVLRETAQNT
170
QTGNQQEPSP
180
NLSREKTREN
190
VPNSDSQPPP
200
SCLTTAVPSP
210
SKPRTAQLVL
220
QRMQQFKRAD
230
PERLRHASEE
240
CSLEAAREEN
250
VPKDPQEEMM
260
AGNVYGLGPP
270
APESDAAVAL
280
TLQQEFARVG
290
ASAHDDSLEE
300
KGLFFCQICQ
310
KNLSAMNVTR
320
REQHVNRCLD
330
EAEKTLRPSV
340
PQIPECPICG
350
KPFLTLKSRT
360
SHLKQCAVKM
370
EVGPQLLLQA
380
VRLQTAQPEG
390
SSSPPMFSFS
400
DHSRGLKRRG
410
PTSKKEPRKR
420
RKVDEAPSED
430
LLVAMALSRS
440
EMEPGAAVPA
450
LRLESAFSER
460
IRPEAENKSR
470
KKKPPVSPPL
480
LLVQDSETTG
490
RQIEDRVALL
500
LSEEVELSST
510
PPLPASRILK
520
EGWERAGQCP
530
PPPERKQSFL
540
WEGSALTGAW
550
AMEDFYTARL
560
VPPLVPQRPA
570
QGLMQEPVPP
580
LVPPEHSELS
590
ERRSPALHGT
600
PTAGCGSRGP
610
SPSASQREHQ
620
ALQDLVDLAR
630
EGLSASPWPG
640
SGGLAGSEGT
650
AGLDVVPGGL
660
PLTGFVVPSQ
670
DKHPDRGGRT
680
LLSLGLLVAD
690
FGAMVNNPHL
700
SDVQFQTDSG
710
EVLYAHKFVL
720
YARCPLLIQY
730
VNNEGFSAVE
740
DGVLTQRVLL
750
GDVSTEAART
760
FLHYLYTADT
770
GLPPGLSSEL
780
SSLAHRFGVS
790
ELVHLCEQVP
800
IATDSEGKPW
810
EEKEAENCES
820
RAENFQELLR
830
SMWADEEEEA
840
ETLLKSKDHE
850
EDQENVNEAE
860
MEEIYEFAAT
870
QRKLLQEERA
880
AGAGEDADWL
890
EGGSPVSGQL
900
LAGVQVQKQW
910
DKVEEMEPLE
920
PGRDEAATTW
930
EKMGQCALPP
940
PQGQHSGARG
950
AEAPEQEAPE
960
EALGHSSCSS
970
PSRDCQAERK
980
EGSLPHSDDA
990
GDYEQLFSST
1000
QGEISEPSQI
1010
TSEPEEQSGA
1020
VRERGLEVSH
1030
RLAPWQASPP
1040
HPCRFLLGPP
1050
QGGSPRGSHH
1060
TSGSSLSTPR
1070
SRGGTSQVGS
1080
PTLLSPAVPS
1090
KQKRDRSILT
1100
LSKEPGHQKG
1110
KERRSVLECR
1120
NKGVLMFPEK
1130
SPSIDLTQSN
1140
PDHSSSRSQK
1150
SSSKLNEEDE
1160
VILLLDSDEE
1170
LELEQTKMKS
1180
ISSDPLEEKK
1190
ALEISPRSCE
1200
LFSIIDVDAD
1210
QEPSQSPPRS
1220
EAVLQQEDEG
1230
ALPENRGSLG
1240
RRGAPWLFCD
1250
RESSPSEAST
1260
TDTSWLVPAT
1270
PLASRSRDCS
1280
SQTQISSLRS
1290
GLAVQAVTQH
1300
TPRASVGNRE
1310
GNEVAQKFSV
1320
IRPQTPPPQT
1330
PSSCLTPVSP
1340
GTSDGRRQGH
1350
RSPSRPHPGG
1360
HPHSSPLAPH
1370
PISGDRAHFS
1380
RRFLKHSPPG
1390
PSFLNQTPAG
1400
EVVEVGDSDD
1410
EQEVASHQAN
1420
RSPPLDSDPP
1430
IPIDDCCWHM
1440
EPLSPIPIDH
1450
WNLERTGPLS
1460
TSSPSRRMNE
1470
AADSRDCRSP
1480
GLLDTTPIRG
1490
SCTTQRKLQE
1500
KSSGAGSLGN
1510
SRPSFLNSAL
1520
WDVWDGEEQR
1530
PPETPPPAQM
1540
PSAGGAQKPE
1550
GLETPKGANR
1560
KKNLPPKVPI
1570
TPMPQYSIME
1580
TPVLKKELDR
1590
FGVRPLPKRQ
1600
MVLKLKEIFQ
1610
YTHQTLDSDS
1620
EDESQSSQPL
1630
LQAPHCQTLA
1640
SQTYKPSRAG
1650
VHAQQEATTG
1660
PGAHRPKGPA
1670
KTKGPRHQRK
1680
HHESITPPSR
1690
SPTKEAPPGL
1700
NDDAQIPASQ
1710
ESVATSVDGS
1720
DSSLSSQSSS
1730
SCEFGAAFES
1740
AGEEEGEGEV
1750
SASQAAVQAA
1760
DTDEALRCYI
1770
RSKPALYQKV
1780
LLYQPFELRE
1790
LQAELRQNGL
1800
RVSSRRLLDF
1810
LDTHCITFTT
1820
AATRREKLQG
1830
RRRQPRGKKK
VERN
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0000781 |
chromosome, telomeric region |
| Cellular Component |
GO:0000228 |
nuclear chromosome |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0033557 |
Slx1-Slx4 complex |
| Molecular Function |
GO:0003677 |
DNA binding |
| Molecular Function |
GO:0008047 |
enzyme activator activity |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0010792 |
DNA double-strand break processing involved in repair via single-strand annealing |
| Biological Process |
GO:0006281 |
DNA repair |
| Biological Process |
GO:0006260 |
DNA replication |
| Biological Process |
GO:0000724 |
double-strand break repair via homologous recombination |
| Biological Process |
GO:1904357 |
negative regulation of telomere maintenance via telomere lengthening |
| Biological Process |
GO:0006289 |
nucleotide-excision repair |
| Biological Process |
GO:1904431 |
positive regulation of t-circle formation |
| Biological Process |
GO:0032206 |
positive regulation of telomere maintenance |
| Biological Process |
GO:0000712 |
resolution of meiotic recombination intermediates |
| Biological Process |
GO:0072429 |
response to intra-S DNA damage checkpoint signaling |
| Biological Process |
GO:0090656 |
t-circle formation |
| Biological Process |
GO:0061820 |
telomeric D-loop disassembly |
Reference
PMID: N/A