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Q6P1D7 (SLX4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structure-specific endonuclease subunit SLX4
Alternative name(s):
BTB/POZ domain-containing protein 12
Gene names
Name:Slx4
Synonyms:Btbd12
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1565 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Subunit structure

Forms a heterodimer with SLX1A/GIYD1. Interacts with ERCC4; catalytic subunit of the ERCC4-ERCC1 endonuclease. Interacts with MUS81; catalytic subunit of the MUS81-EME1 endonuclease. Interacts with MSH2; component of the MSH2-MSH3 mismatch repair complex. Interacts with TERF2-TERF2IP. Interacts with PLK1 and SLX4IP By similarity.

Subcellular location

Nucleus By similarity. Note: Localizes to sites of DNA dammage By similarity.

Sequence similarities

Belongs to the SLX4 family.

Contains 1 BTB (POZ) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15651565Structure-specific endonuclease subunit SLX4
PRO_0000383567

Regions

Domain506 – 57974BTB
Region499 – 15651067Interaction with PLK1 and TERF2-TERF2IP By similarity
Region1120 – 1413294Interaction with MUS81 By similarity
Region1406 – 1565160Interaction with SLX1 By similarity

Amino acid modifications

Modified residue1111Phosphoserine By similarity
Modified residue8451Phosphoserine By similarity
Modified residue12541Phosphoserine By similarity

Experimental info

Mutagenesis2021P → T: Does not modify the functional properties of the protein. Ref.2
Mutagenesis6021E → K: Does not modify the functional properties of the protein. Ref.2
Mutagenesis13241Q → W: Does not modify the functional properties of the protein. Ref.2
Mutagenesis15451R → C: Does not modify the functional properties of the protein. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6P1D7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: AB4CB4EB57CA6394

FASTA1,565172,412
        10         20         30         40         50         60 
MVPESAPNGN SQPLPSCFTT TGVPSPSKPR VSELVLQRMK QFKRADPERL RHASEESPQK 

        70         80         90        100        110        120 
TALGDDVPRS PPEETVGENE YKLDATDSDA AMALALQQEF RREEASSHHD SLEEKGLFFC 

       130        140        150        160        170        180 
QMCQKNLSAM NVTRREQHVN RCLDEAEKAQ RPASPRIPDC PICGKPFLTT KSRISHLKQC 

       190        200        210        220        230        240 
AVRMEVGPQL LLQAVRLQTA QPEVDGSPQV PSFSNNVGGL KRKGVTTKRE PRRRKVNKPE 

       250        260        270        280        290        300 
APSEDLLVAM ALSRSEVEHC PVVPPLRLEN AFSEKIRLGA EKKSRKKRPP VCPPQLVTQD 

       310        320        330        340        350        360 
SETTGRQIED RVAQLLSEEA ELSCTPPLLA SKISKEELEP AGWRARLPEG KRNFLWELSA 

       370        380        390        400        410        420 
LTGAWAEESF YTVGLFPPIV SQCPSKEPQL PLELPKQGEP SPRRPPASQS SLPVSHSPKI 

       430        440        450        460        470        480 
RLLSSSQRER QALQDLVDLA VEGLSSSPQP GSRGVPTGLD LVPSSLPLTG FVLPCKKTLK 

       490        500        510        520        530        540 
KDDSASLSLG LLVTDFGAMV NNPHLSDVQF QLDSGEVLYA HKFVLYARCP LLIQYVSTES 

       550        560        570        580        590        600 
FSSEEDGDLT QRALLSDVSS EAAHAFLNYL YMADTDMPPS LVPDLRSLAL RFGVSDLVQL 

       610        620        630        640        650        660 
CEQVPAVVDL EGEQPEETSE DCESRAETFL ELLRSVWVDN EEEVETLLKP ELCEEERERV 

       670        680        690        700        710        720 
NEAEMEEIYE FAATQRKLLQ WGRAADPDGS TNPHGEDGAV SEPSLAGVQS NRQLENTEHM 

       730        740        750        760        770        780 
ESSGLEKEEA LASWEQEGHS TPLQDQCPDW AGKAEAQDAL GEATDDPSFC SRHRRGKECL 

       790        800        810        820        830        840 
PLHPNKAHGC KQPLPSNPRV SSELSQITVD HEEQSDHVRE TQADMAQAPT PHSCSLVSQS 

       850        860        870        880        890        900 
SVDGSPSQSW LHLYHTSHLS PSVSQSHSSI SRVASPRSLS PTTPTKQRRG SNIVTLRKDA 

       910        920        930        940        950        960 
GHHRGQQSSP IAGHRNRGIL ISPAKSPPID LTQSVPEPLS PRAQDPLHFV KKEDEVILLL 

       970        980        990       1000       1010       1020 
DSDEELEHTK TESVSKDSPE GRKVPEFSPR SSELFSVIDV EEDHEHFQSP LKREAGLQHG 

      1030       1040       1050       1060       1070       1080 
EEGQLGNQSA LGCRDIPWLL CSQKTSLDED SATDTSWLVP ATPGVSRSRD CSSQTQIKSL 

      1090       1100       1110       1120       1130       1140 
KTRIPSDETA QQTPRPNLER RTMLETAQQF SVIMPHTQPI TLGAFDSGRQ AYRSPSHPYP 

      1150       1160       1170       1180       1190       1200 
RHHRLSSSQP SCPGPDFTRW SQKSSAPRPC LPNLPAADDV VEVGDSDDEV ASHQGNSSPV 

      1210       1220       1230       1240       1250       1260 
LDGDPPGPMG DYCWNEPLSP IPIDHLNLER TGPLTTSSPS SQVLEALHSD DCHSPGLGTT 

      1270       1280       1290       1300       1310       1320 
PIRGSCGTLR ESQERSSLAG SPEALWDDWN EEEGQSPEAP PVAQMLSTRT RKPDRPETPK 

      1330       1340       1350       1360       1370       1380 
GANQKKNLPP KVPITPMPRY SIMETPVLKK ELDRFGVRAL PKRQMVLKLK EIFQYTHQTL 

      1390       1400       1410       1420       1430       1440 
ESDSEDEVQS PQIPAELPCR QASTTETCNP SRLPTGEPSH PDGDAQLPAS QESMATSVDG 

      1450       1460       1470       1480       1490       1500 
SDNSFSSKSS SAEFGAAFEY SDEDKDEEVG VTASQAAIQA ADTEEAVRRY IRSKPALHRQ 

      1510       1520       1530       1540       1550       1560 
VLRYQPVELA ELQAELKQNG IPVAMGKLSD ILDAQCITFT TAAARKEKLK HKRRQPSGRK 


KKDQK 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[2]"Analysis of the novel Fanconi anemia gene SLX4/FANCP in familial breast cancer cases."
Bakker J.L., van Mil S.E., Crossan G., Sabbaghian N., De Leeneer K., Poppe B., Adank M., Gille H., Verheul H., Meijers-Heijboer H., de Winter J.P., Claes K., Tischkowitz M., Waisfisz Q.
Hum. Mutat. 34:70-73(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PRO-202; GLU-602; GLN-1324 AND ARG-1545.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC065125 mRNA. Translation: AAH65125.1.
RefSeqNP_803423.2. NM_177472.5.
UniGeneMm.29935.

3D structure databases

ProteinModelPortalQ6P1D7.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ6P1D7.

Proteomic databases

PaxDbQ6P1D7.
PRIDEQ6P1D7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040790; ENSMUSP00000038871; ENSMUSG00000039738.
GeneID52864.
KEGGmmu:52864.
UCSCuc007xzg.1. mouse.

Organism-specific databases

CTD84464.
MGIMGI:106299. Slx4.

Phylogenomic databases

eggNOGNOG44550.
GeneTreeENSGT00390000014091.
HOGENOMHOG000095273.
InParanoidQ6P1D7.
KOK10484.
OMAHKFVLYA.
OrthoDBEOG7ZKSDH.
PhylomeDBQ6P1D7.
TreeFamTF106446.

Gene expression databases

ArrayExpressQ6P1D7.
BgeeQ6P1D7.
GenevestigatorQ6P1D7.

Family and domain databases

Gene3D3.30.710.10. 1 hit.
InterProIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR018574. Structure-sp_endonuc_su_Slx4.
[Graphical view]
PfamPF00651. BTB. 1 hit.
PF09494. Slx4. 1 hit.
[Graphical view]
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio309663.
PROQ6P1D7.
SOURCESearch...

Entry information

Entry nameSLX4_MOUSE
AccessionPrimary (citable) accession number: Q6P1D7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot