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Q8IY92 (SLX4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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, KIAA1784, KIAA1987
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1834 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. Ref.7 Ref.8 Ref.9 Ref.10

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. Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus. Note: Localizes to sites of DNA dammage. Ref.7 Ref.8

Involvement in disease

Fanconi anemia complementation group P (FANCP) [MIM:613951]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. Some individuals affected by Fanconi anemia of complementation group P have skeletal anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15

Sequence similarities

Belongs to the SLX4 family.

Contains 1 BTB (POZ) domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IY92-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8IY92-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-312: Missing.
     313-316: QHVN → MFSF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18341834Structure-specific endonuclease subunit SLX4
PRO_0000186219

Regions

Domain691 – 76474BTB
Region1 – 669669Interaction with SLX4IP, ERCC4 and MSH2
Region684 – 18341151Interaction with PLK1 and TERF2-TERF2IP
Region1328 – 1648321Interaction with MUS81
Region1632 – 1834203Interaction with SLX1
Coiled coil801 – 87070 Potential
Compositional bias520 – 5234Poly-Pro
Compositional bias796 – 85661Glu-rich
Compositional bias1710 – 172112Poly-Ser

Amino acid modifications

Modified residue2871Phosphoserine Ref.6
Modified residue10441Phosphoserine Ref.13
Modified residue14691Phosphoserine Ref.5 Ref.6

Natural variations

Alternative sequence1 – 312312Missing in isoform 2.
VSP_035295
Alternative sequence313 – 3164QHVN → MFSF in isoform 2.
VSP_035296
Natural variant381L → F. Ref.16
Corresponds to variant rs141167501 [ dbSNP | Ensembl ].
VAR_068982
Natural variant1411G → W. Ref.16
Corresponds to variant rs137976282 [ dbSNP | Ensembl ].
VAR_068983
Natural variant1971V → A. Ref.16
Corresponds to variant rs147826749 [ dbSNP | Ensembl ].
VAR_068984
Natural variant2041R → C. Ref.16
Corresponds to variant rs79842542 [ dbSNP | Ensembl ].
VAR_068985
Natural variant2371R → Q. Ref.16
Corresponds to variant rs138615800 [ dbSNP | Ensembl ].
VAR_068986
Natural variant2841H → R. Ref.16
VAR_068987
Natural variant3781P → T Polymorphism that does not modify the functional properties of the protein. Ref.16
VAR_068988
Natural variant3851P → T. Ref.16
Corresponds to variant rs115694169 [ dbSNP | Ensembl ].
VAR_068989
Natural variant3861M → V. Ref.16
Corresponds to variant rs113490934 [ dbSNP | Ensembl ].
VAR_068990
Natural variant4241A → V. Ref.16
VAR_068991
Natural variant4571N → K. Ref.16
Corresponds to variant rs74319927 [ dbSNP | Ensembl ].
VAR_068992
Natural variant4581K → E. Ref.16
Corresponds to variant rs149126845 [ dbSNP | Ensembl ].
VAR_068993
Natural variant5051A → T. Ref.16
VAR_068994
Natural variant5061S → N. Ref.16
VAR_068995
Natural variant5681V → M. Ref.16
VAR_068996
Natural variant5791L → P. Ref.16
VAR_068997
Natural variant6711L → S. Ref.3 Ref.16
Corresponds to variant rs77985244 [ dbSNP | Ensembl ].
VAR_068998
Natural variant7871E → K Polymorphism that does not modify the functional properties of the protein. Ref.16
Corresponds to variant rs140600202 [ dbSNP | Ensembl ].
VAR_068999
Natural variant8701A → V. Ref.16
Corresponds to variant rs149584080 [ dbSNP | Ensembl ].
VAR_069000
Natural variant8941V → G. Ref.16
Corresponds to variant rs145137472 [ dbSNP | Ensembl ].
VAR_069001
Natural variant9291P → L. Ref.16
Corresponds to variant rs117707719 [ dbSNP | Ensembl ].
VAR_069002
Natural variant9421E → Q. Ref.16
Corresponds to variant rs114014006 [ dbSNP | Ensembl ].
VAR_069003
Natural variant9521A → M Requires 2 nucleotide substitutions. Ref.3 Ref.16
VAR_069004
Natural variant9751P → L. Ref.16
Corresponds to variant rs114472821 [ dbSNP | Ensembl ].
VAR_069005
Natural variant10071Q → K. Ref.16
Corresponds to variant rs138798067 [ dbSNP | Ensembl ].
VAR_069006
Natural variant10601R → W. Ref.16
VAR_069007
Natural variant11221P → L. Ref.3 Ref.16
Corresponds to variant rs714181 [ dbSNP | Ensembl ].
VAR_019326
Natural variant11231S → Y. Ref.16
Corresponds to variant rs144647122 [ dbSNP | Ensembl ].
VAR_069008
Natural variant12211A → V. Ref.3 Ref.16
Corresponds to variant rs3827530 [ dbSNP | Ensembl ].
VAR_019729
Natural variant12711S → F. Ref.16
Corresponds to variant rs3810813 [ dbSNP | Ensembl ].
VAR_019327
Natural variant12861A → V. Ref.16
Corresponds to variant rs149011965 [ dbSNP | Ensembl ].
VAR_069009
Natural variant12871V → G. Ref.16
VAR_069010
Natural variant13421S → G. Ref.16
Corresponds to variant rs140051968 [ dbSNP | Ensembl ].
VAR_069011
Natural variant13671A → T.
Corresponds to variant rs17136464 [ dbSNP | Ensembl ].
VAR_046337
Natural variant14211I → F. Ref.16
Corresponds to variant rs141567438 [ dbSNP | Ensembl ].
VAR_069012
Natural variant14761T → S. Ref.16
VAR_069013
Natural variant15501R → W Polymorphism that does not modify the functional properties of the protein. Ref.16
Corresponds to variant rs77021998 [ dbSNP | Ensembl ].
VAR_069014
Natural variant16771P → S.
Corresponds to variant rs7196345 [ dbSNP | Ensembl ].
VAR_046338
Natural variant16941A → V. Ref.16
VAR_069015
Natural variant18141R → C. Ref.16
VAR_069016
Natural variant18341N → S Polymorphism that does not modify the functional properties of the protein. Ref.16
Corresponds to variant rs111738042 [ dbSNP | Ensembl ].
VAR_069017

Secondary structure

... 1834
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 2, 2008. Version 3.
Checksum: 9131E88628DB15D5

FASTA1,834200,012
        10         20         30         40         50         60 
MKLSVNEAQL GFYLGSLSHL SACPGIDPRS SEDQPESLKT GQMMDESDED FKELCASFFQ 

        70         80         90        100        110        120 
RVKKHGIKEV SGERKTQKAA SNGTQIRSKL KRTKQTATKT KTLQGPAEKK PPSGSQAPRT 

       130        140        150        160        170        180 
KKQRVTKWQA SEPAHSVNGE GGVLASAPDP PVLRETAQNT QTGNQQEPSP NLSREKTREN 

       190        200        210        220        230        240 
VPNSDSQPPP SCLTTAVPSP SKPRTAQLVL QRMQQFKRAD PERLRHASEE CSLEAAREEN 

       250        260        270        280        290        300 
VPKDPQEEMM AGNVYGLGPP APESDAAVAL TLQQEFARVG ASAHDDSLEE KGLFFCQICQ 

       310        320        330        340        350        360 
KNLSAMNVTR REQHVNRCLD EAEKTLRPSV PQIPECPICG KPFLTLKSRT SHLKQCAVKM 

       370        380        390        400        410        420 
EVGPQLLLQA VRLQTAQPEG SSSPPMFSFS DHSRGLKRRG PTSKKEPRKR RKVDEAPSED 

       430        440        450        460        470        480 
LLVAMALSRS EMEPGAAVPA LRLESAFSER IRPEAENKSR KKKPPVSPPL LLVQDSETTG 

       490        500        510        520        530        540 
RQIEDRVALL LSEEVELSST PPLPASRILK EGWERAGQCP PPPERKQSFL WEGSALTGAW 

       550        560        570        580        590        600 
AMEDFYTARL VPPLVPQRPA QGLMQEPVPP LVPPEHSELS ERRSPALHGT PTAGCGSRGP 

       610        620        630        640        650        660 
SPSASQREHQ ALQDLVDLAR EGLSASPWPG SGGLAGSEGT AGLDVVPGGL PLTGFVVPSQ 

       670        680        690        700        710        720 
DKHPDRGGRT LLSLGLLVAD FGAMVNNPHL SDVQFQTDSG EVLYAHKFVL YARCPLLIQY 

       730        740        750        760        770        780 
VNNEGFSAVE DGVLTQRVLL GDVSTEAART FLHYLYTADT GLPPGLSSEL SSLAHRFGVS 

       790        800        810        820        830        840 
ELVHLCEQVP IATDSEGKPW EEKEAENCES RAENFQELLR SMWADEEEEA ETLLKSKDHE 

       850        860        870        880        890        900 
EDQENVNEAE MEEIYEFAAT QRKLLQEERA AGAGEDADWL EGGSPVSGQL LAGVQVQKQW 

       910        920        930        940        950        960 
DKVEEMEPLE PGRDEAATTW EKMGQCALPP PQGQHSGARG AEAPEQEAPE EALGHSSCSS 

       970        980        990       1000       1010       1020 
PSRDCQAERK EGSLPHSDDA GDYEQLFSST QGEISEPSQI TSEPEEQSGA VRERGLEVSH 

      1030       1040       1050       1060       1070       1080 
RLAPWQASPP HPCRFLLGPP QGGSPRGSHH TSGSSLSTPR SRGGTSQVGS PTLLSPAVPS 

      1090       1100       1110       1120       1130       1140 
KQKRDRSILT LSKEPGHQKG KERRSVLECR NKGVLMFPEK SPSIDLTQSN PDHSSSRSQK 

      1150       1160       1170       1180       1190       1200 
SSSKLNEEDE VILLLDSDEE LELEQTKMKS ISSDPLEEKK ALEISPRSCE LFSIIDVDAD 

      1210       1220       1230       1240       1250       1260 
QEPSQSPPRS EAVLQQEDEG ALPENRGSLG RRGAPWLFCD RESSPSEAST TDTSWLVPAT 

      1270       1280       1290       1300       1310       1320 
PLASRSRDCS SQTQISSLRS GLAVQAVTQH TPRASVGNRE GNEVAQKFSV IRPQTPPPQT 

      1330       1340       1350       1360       1370       1380 
PSSCLTPVSP GTSDGRRQGH RSPSRPHPGG HPHSSPLAPH PISGDRAHFS RRFLKHSPPG 

      1390       1400       1410       1420       1430       1440 
PSFLNQTPAG EVVEVGDSDD EQEVASHQAN RSPPLDSDPP IPIDDCCWHM EPLSPIPIDH 

      1450       1460       1470       1480       1490       1500 
WNLERTGPLS TSSPSRRMNE AADSRDCRSP GLLDTTPIRG SCTTQRKLQE KSSGAGSLGN 

      1510       1520       1530       1540       1550       1560 
SRPSFLNSAL WDVWDGEEQR PPETPPPAQM PSAGGAQKPE GLETPKGANR KKNLPPKVPI 

      1570       1580       1590       1600       1610       1620 
TPMPQYSIME TPVLKKELDR FGVRPLPKRQ MVLKLKEIFQ YTHQTLDSDS EDESQSSQPL 

      1630       1640       1650       1660       1670       1680 
LQAPHCQTLA SQTYKPSRAG VHAQQEATTG PGAHRPKGPA KTKGPRHQRK HHESITPPSR 

      1690       1700       1710       1720       1730       1740 
SPTKEAPPGL NDDAQIPASQ ESVATSVDGS DSSLSSQSSS SCEFGAAFES AGEEEGEGEV 

      1750       1760       1770       1780       1790       1800 
SASQAAVQAA DTDEALRCYI RSKPALYQKV LLYQPFELRE LQAELRQNGL RVSSRRLLDF 

      1810       1820       1830 
LDTHCITFTT AATRREKLQG RRRQPRGKKK VERN 

« Hide

Isoform 2 [UniParc].

Checksum: A3C234F1E746C5FA
Show »

FASTA1,522165,903

References

« Hide 'large scale' references
[1]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
Nagase T., Kikuno R., Ohara O.
DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-669 (ISOFORM 2).
Tissue: Brain.
[3]"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 668-1834 (ISOFORMS 1/2), VARIANTS SER-671; MET-952; LEU-1122 AND VAL-1221.
Tissue: Brain.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1612-1834 (ISOFORMS 1/2).
Tissue: Brain.
[5]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-1469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair."
Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., Elledge S.J., Harper J.W.
Cell 138:63-77(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SLX4IP; ERCC4; SLX1A; MSH2; MUS81; PLK1; TERF2 AND TERF2IP, SUBCELLULAR LOCATION.
[8]"Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases."
Fekairi S., Scaglione S., Chahwan C., Taylor E.R., Tissier A., Coulon S., Dong M.-Q., Ruse C., Yates J.R. III, Russell P., Fuchs R.P., McGowan C.H., Gaillard P.-H.L.
Cell 138:78-89(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ERCC4; SLX1A AND MUS81, SUBCELLULAR LOCATION.
[9]"Coordination of structure-specific nucleases by human SLX4/BTBD12 is required for DNA repair."
Munoz I.M., Hain K., Declais A.-C., Gardiner M., Toh G.W., Sanchez-Pulido L., Heuckmann J.M., Toth R., Macartney T., Eppink B., Kanaar R., Ponting C.P., Lilley D.M.J., Rouse J.
Mol. Cell 35:116-127(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ERCC4; SLX1A AND MUS81-EME1.
[10]"Drosophila MUS312 and the vertebrate ortholog BTBD12 interact with DNA structure-specific endonucleases in DNA repair and recombination."
Andersen S.L., Bergstralh D.T., Kohl K.P., LaRocque J.R., Moore C.B., Sekelsky J.
Mol. Cell 35:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ERCC4.
[11]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1044, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"SLX4, a coordinator of structure-specific endonucleases, is mutated in a new Fanconi anemia subtype."
Stoepker C., Hain K., Schuster B., Hilhorst-Hofstee Y., Rooimans M.A., Steltenpool J., Oostra A.B., Eirich K., Korthof E.T., Nieuwint A.W., Jaspers N.G., Bettecken T., Joenje H., Schindler D., Rouse J., de Winter J.P.
Nat. Genet. 43:138-141(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FANCP.
[15]"Mutations of the SLX4 gene in Fanconi anemia."
Kim Y., Lach F.P., Desetty R., Hanenberg H., Auerbach A.D., Smogorzewska A.
Nat. Genet. 43:142-146(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FANCP.
[16]"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: VARIANTS PHE-38; TRP-141; ALA-197; CYS-204; GLN-237; ARG-284; THR-378; THR-385; VAL-386; VAL-424; LYS-457; GLU-458; THR-505; ASN-506; MET-568; PRO-579; SER-671; LYS-787; VAL-870; GLY-894; LEU-929; GLN-942; MET-952; LEU-975; LYS-1007; TRP-1060; LEU-1122; TYR-1123; VAL-1221; PHE-1271; VAL-1286; GLY-1287; GLY-1342; PHE-1421; SER-1476; TRP-1550; VAL-1694; CYS-1814 AND SER-1834, CHARACTERIZATION OF VARIANTS THR-378; LYS-787; TRP-1550 AND CYS-1814, NO ASSOCIATION WITH BREAST CANCER.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC006111 Genomic DNA. No translation available.
AB075867 mRNA. Translation: BAB85573.1.
AB058687 mRNA. Translation: BAB47413.1.
AL442083 mRNA. Translation: CAH10659.1.
RefSeqNP_115820.2. NM_032444.2.
UniGeneHs.143681.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4M7CX-ray2.05C/D1014-1025[»]
ProteinModelPortalQ8IY92.
SMRQ8IY92. Positions 676-790.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124097. 34 interactions.
IntActQ8IY92. 157 interactions.

PTM databases

PhosphoSiteQ8IY92.

Polymorphism databases

DMDM205371796.

Proteomic databases

PaxDbQ8IY92.
PRIDEQ8IY92.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294008; ENSP00000294008; ENSG00000188827. [Q8IY92-1]
GeneID84464.
KEGGhsa:84464.
UCSCuc002cvp.2. human. [Q8IY92-1]

Organism-specific databases

CTD84464.
GeneCardsGC16M003632.
H-InvDBHIX0202244.
HGNCHGNC:23845. SLX4.
HPAHPA049421.
MIM613278. gene.
613951. phenotype.
neXtProtNX_Q8IY92.
Orphanet84. Fanconi anemia.
PharmGKBPA134983583.
HUGESearch...
Search...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44550.
HOGENOMHOG000095273.
InParanoidQ8IY92.
KOK10484.
OMAHKFVLYA.
OrthoDBEOG7ZKSDH.
PhylomeDBQ8IY92.
TreeFamTF106446.

Gene expression databases

BgeeQ8IY92.
CleanExHS_BTBD12.
GenevestigatorQ8IY92.

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

ChiTaRSSLX4. human.
GeneWikiSLX4.
GenomeRNAi84464.
NextBio74266.
PROQ8IY92.
SOURCESearch...

Entry information

Entry nameSLX4_HUMAN
AccessionPrimary (citable) accession number: Q8IY92
Secondary accession number(s): Q69YT8, Q8TF15, Q96JP1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM