Q8IY92 (SLX4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Structure-specific endonuclease subunit SLX4

Alternative name(s):
BTB/POZ domain-containing protein 12

Gene names

Name:	SLX4
Synonyms:	BTBD12, KIAA1784, KIAA1987

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1834 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Fanconi anemia
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA double-strand break processing involved in repair via single-strand annealing Inferred from mutant phenotype Ref.9. Source: UniProtKB double-strand break repair via homologous recombination Inferred from mutant phenotype Ref.9Ref.7. Source: UniProtKB nucleotide-excision repair Inferred from mutant phenotype Ref.8. Source: UniProtKB
Cellular_component	Slx1-Slx4 complex Inferred from direct assay Ref.9Ref.7Ref.8. Source: UniProtKB
Molecular_function	enzyme activator activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EME1	Q96AY2	4	EBI-2370740,EBI-2370825
ERCC1	P07992	6	EBI-2370740,EBI-750962
ERCC4	Q92889	10	EBI-2370740,EBI-2370770
MSH2	P43246	5	EBI-2370740,EBI-355888
MUS81	Q96NY9	8	EBI-2370740,EBI-2370806
PLK1	P53350	6	EBI-2370740,EBI-476768
SLX1A	Q9BQ83	10	EBI-2370740,EBI-2370858
SLX4IP	Q5VYV7	4	EBI-2370740,EBI-2370881
TERF2	Q15554	5	EBI-2370740,EBI-706637
TERF2IP	Q9NYB0	4	EBI-2370740,EBI-750109

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1834	1834	Structure-specific endonuclease subunit SLX4		PRO_0000186219
Regions
	Domain	691 – 764	74	BTB
	Region	1 – 669	669	Interaction with SLX4IP, ERCC4 and MSH2
	Region	684 – 1834	1151	Interaction with PLK1 and TERF2-TERF2IP
	Region	1328 – 1648	321	Interaction with MUS81
	Region	1632 – 1834	203	Interaction with SLX1
	Coiled coil	801 – 870	70	Potential
	Compositional bias	520 – 523	4	Poly-Pro
	Compositional bias	796 – 856	61	Glu-rich
	Compositional bias	1710 – 1721	12	Poly-Ser
Amino acid modifications
	Modified residue	287	1	Phosphoserine Ref.6
	Modified residue	1044	1	Phosphoserine Ref.13
	Modified residue	1469	1	Phosphoserine Ref.5 Ref.6
Natural variations
	Alternative sequence	1 – 312	312	Missing in isoform 2.		VSP_035295
	Alternative sequence	313 – 316	4	QHVN → MFSF in isoform 2.		VSP_035296
	Natural variant	38	1	L → F. Ref.16 Corresponds to variant rs141167501 [ dbSNP | Ensembl ].		VAR_068982
	Natural variant	141	1	G → W. Ref.16 Corresponds to variant rs137976282 [ dbSNP | Ensembl ].		VAR_068983
	Natural variant	197	1	V → A. Ref.16 Corresponds to variant rs147826749 [ dbSNP | Ensembl ].		VAR_068984
	Natural variant	204	1	R → C. Ref.16 Corresponds to variant rs79842542 [ dbSNP | Ensembl ].		VAR_068985
	Natural variant	237	1	R → Q. Ref.16 Corresponds to variant rs138615800 [ dbSNP | Ensembl ].		VAR_068986
	Natural variant	284	1	H → R. Ref.16		VAR_068987
	Natural variant	378	1	P → T Polymorphism that does not modify the functional properties of the protein. Ref.16		VAR_068988
	Natural variant	385	1	P → T. Ref.16 Corresponds to variant rs115694169 [ dbSNP | Ensembl ].		VAR_068989
	Natural variant	386	1	M → V. Ref.16 Corresponds to variant rs113490934 [ dbSNP | Ensembl ].		VAR_068990
	Natural variant	424	1	A → V. Ref.16		VAR_068991
	Natural variant	457	1	N → K. Ref.16 Corresponds to variant rs74319927 [ dbSNP | Ensembl ].		VAR_068992
	Natural variant	458	1	K → E. Ref.16 Corresponds to variant rs149126845 [ dbSNP | Ensembl ].		VAR_068993
	Natural variant	505	1	A → T. Ref.16		VAR_068994
	Natural variant	506	1	S → N. Ref.16		VAR_068995
	Natural variant	568	1	V → M. Ref.16		VAR_068996
	Natural variant	579	1	L → P. Ref.16		VAR_068997
	Natural variant	671	1	L → S. Ref.3 Ref.16 Corresponds to variant rs77985244 [ dbSNP | Ensembl ].		VAR_068998
	Natural variant	787	1	E → K Polymorphism that does not modify the functional properties of the protein. Ref.16 Corresponds to variant rs140600202 [ dbSNP | Ensembl ].		VAR_068999
	Natural variant	870	1	A → V. Ref.16 Corresponds to variant rs149584080 [ dbSNP | Ensembl ].		VAR_069000
	Natural variant	894	1	V → G. Ref.16 Corresponds to variant rs145137472 [ dbSNP | Ensembl ].		VAR_069001
	Natural variant	929	1	P → L. Ref.16 Corresponds to variant rs117707719 [ dbSNP | Ensembl ].		VAR_069002
	Natural variant	942	1	E → Q. Ref.16 Corresponds to variant rs114014006 [ dbSNP | Ensembl ].		VAR_069003
	Natural variant	952	1	A → M Requires 2 nucleotide substitutions. Ref.3 Ref.16		VAR_069004
	Natural variant	975	1	P → L. Ref.16 Corresponds to variant rs114472821 [ dbSNP | Ensembl ].		VAR_069005
	Natural variant	1007	1	Q → K. Ref.16 Corresponds to variant rs138798067 [ dbSNP | Ensembl ].		VAR_069006
	Natural variant	1060	1	R → W. Ref.16		VAR_069007
	Natural variant	1122	1	P → L. Ref.3 Ref.16 Corresponds to variant rs714181 [ dbSNP | Ensembl ].		VAR_019326
	Natural variant	1123	1	S → Y. Ref.16 Corresponds to variant rs144647122 [ dbSNP | Ensembl ].		VAR_069008
	Natural variant	1221	1	A → V. Ref.3 Ref.16 Corresponds to variant rs3827530 [ dbSNP | Ensembl ].		VAR_019729
	Natural variant	1271	1	S → F. Ref.16 Corresponds to variant rs3810813 [ dbSNP | Ensembl ].		VAR_019327
	Natural variant	1286	1	A → V. Ref.16 Corresponds to variant rs149011965 [ dbSNP | Ensembl ].		VAR_069009
	Natural variant	1287	1	V → G. Ref.16		VAR_069010
	Natural variant	1342	1	S → G. Ref.16 Corresponds to variant rs140051968 [ dbSNP | Ensembl ].		VAR_069011
	Natural variant	1367	1	A → T. Corresponds to variant rs17136464 [ dbSNP | Ensembl ].		VAR_046337
	Natural variant	1421	1	I → F. Ref.16 Corresponds to variant rs141567438 [ dbSNP | Ensembl ].		VAR_069012
	Natural variant	1476	1	T → S. Ref.16		VAR_069013
	Natural variant	1550	1	R → W Polymorphism that does not modify the functional properties of the protein. Ref.16 Corresponds to variant rs77021998 [ dbSNP | Ensembl ].		VAR_069014
	Natural variant	1677	1	P → S. Corresponds to variant rs7196345 [ dbSNP | Ensembl ].		VAR_046338
	Natural variant	1694	1	A → V. Ref.16		VAR_069015
	Natural variant	1814	1	R → C. Ref.16		VAR_069016
	Natural variant	1834	1	N → S Polymorphism that does not modify the functional properties of the protein. Ref.16 Corresponds to variant rs111738042 [ dbSNP | Ensembl ].		VAR_069017

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 2, 2008. Version 3. Checksum: 9131E88628DB15D5	FASTA	1,834	200,012
	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
	Isoform 2 [UniParc]. Checksum: A3C234F1E746C5FA	FASTA	1,522	165,903
	10 20 30 40 50 60 MFSFRCLDEA EKTLRPSVPQ IPECPICGKP FLTLKSRTSH LKQCAVKMEV GPQLLLQAVR 70 80 90 100 110 120 LQTAQPEGSS SPPMFSFSDH SRGLKRRGPT SKKEPRKRRK VDEAPSEDLL VAMALSRSEM 130 140 150 160 170 180 EPGAAVPALR LESAFSERIR PEAENKSRKK KPPVSPPLLL VQDSETTGRQ IEDRVALLLS 190 200 210 220 230 240 EEVELSSTPP LPASRILKEG WERAGQCPPP PERKQSFLWE GSALTGAWAM EDFYTARLVP 250 260 270 280 290 300 PLVPQRPAQG LMQEPVPPLV PPEHSELSER RSPALHGTPT AGCGSRGPSP SASQREHQAL 310 320 330 340 350 360 QDLVDLAREG LSASPWPGSG GLAGSEGTAG LDVVPGGLPL TGFVVPSQDK HPDRGGRTLL 370 380 390 400 410 420 SLGLLVADFG AMVNNPHLSD VQFQTDSGEV LYAHKFVLYA RCPLLIQYVN NEGFSAVEDG 430 440 450 460 470 480 VLTQRVLLGD VSTEAARTFL HYLYTADTGL PPGLSSELSS LAHRFGVSEL VHLCEQVPIA 490 500 510 520 530 540 TDSEGKPWEE KEAENCESRA ENFQELLRSM WADEEEEAET LLKSKDHEED QENVNEAEME 550 560 570 580 590 600 EIYEFAATQR KLLQEERAAG AGEDADWLEG GSPVSGQLLA GVQVQKQWDK VEEMEPLEPG 610 620 630 640 650 660 RDEAATTWEK MGQCALPPPQ GQHSGARGAE APEQEAPEEA LGHSSCSSPS RDCQAERKEG 670 680 690 700 710 720 SLPHSDDAGD YEQLFSSTQG EISEPSQITS EPEEQSGAVR ERGLEVSHRL APWQASPPHP 730 740 750 760 770 780 CRFLLGPPQG GSPRGSHHTS GSSLSTPRSR GGTSQVGSPT LLSPAVPSKQ KRDRSILTLS 790 800 810 820 830 840 KEPGHQKGKE RRSVLECRNK GVLMFPEKSP SIDLTQSNPD HSSSRSQKSS SKLNEEDEVI 850 860 870 880 890 900 LLLDSDEELE LEQTKMKSIS SDPLEEKKAL EISPRSCELF SIIDVDADQE PSQSPPRSEA 910 920 930 940 950 960 VLQQEDEGAL PENRGSLGRR GAPWLFCDRE SSPSEASTTD TSWLVPATPL ASRSRDCSSQ 970 980 990 1000 1010 1020 TQISSLRSGL AVQAVTQHTP RASVGNREGN EVAQKFSVIR PQTPPPQTPS SCLTPVSPGT 1030 1040 1050 1060 1070 1080 SDGRRQGHRS PSRPHPGGHP HSSPLAPHPI SGDRAHFSRR FLKHSPPGPS FLNQTPAGEV 1090 1100 1110 1120 1130 1140 VEVGDSDDEQ EVASHQANRS PPLDSDPPIP IDDCCWHMEP LSPIPIDHWN LERTGPLSTS 1150 1160 1170 1180 1190 1200 SPSRRMNEAA DSRDCRSPGL LDTTPIRGSC TTQRKLQEKS SGAGSLGNSR PSFLNSALWD 1210 1220 1230 1240 1250 1260 VWDGEEQRPP ETPPPAQMPS AGGAQKPEGL ETPKGANRKK NLPPKVPITP MPQYSIMETP 1270 1280 1290 1300 1310 1320 VLKKELDRFG VRPLPKRQMV LKLKEIFQYT HQTLDSDSED ESQSSQPLLQ APHCQTLASQ 1330 1340 1350 1360 1370 1380 TYKPSRAGVH AQQEATTGPG AHRPKGPAKT KGPRHQRKHH ESITPPSRSP TKEAPPGLND 1390 1400 1410 1420 1430 1440 DAQIPASQES VATSVDGSDS SLSSQSSSSC EFGAAFESAG EEEGEGEVSA SQAAVQAADT 1450 1460 1470 1480 1490 1500 DEALRCYIRS KPALYQKVLL YQPFELRELQ AELRQNGLRV SSRRLLDFLD THCITFTTAA 1510 1520 TRREKLQGRR RQPRGKKKVE RN

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.

Web resources

SLX4 structure-specific endonuclease subunit homolog (S. cerevisiae) (SLX4)

Leiden Open Variation Database (LOVD)

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.
IPI	IPI00291796. IPI00412364.
RefSeq	NP_115820.2. NM_032444.2.
UniGene	Hs.143681.
3D structure databases
ProteinModelPortal	Q8IY92.
SMR	Q8IY92. Positions 675-788.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IY92. 155 interactions.
PTM databases
PhosphoSite	Q8IY92.
Polymorphism databases
DMDM	205371796.
Proteomic databases
PaxDb	Q8IY92.
PRIDE	Q8IY92.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000294008; ENSP00000294008; ENSG00000188827.
GeneID	84464.
KEGG	hsa:84464.
UCSC	uc002cvp.2. human.
Organism-specific databases
CTD	84464.
GeneCards	GC16M003632.
H-InvDB	HIX0202244.
HGNC	HGNC:23845. SLX4.
MIM	613278. gene. 613951. phenotype.
neXtProt	NX_Q8IY92.
Orphanet	84. Fanconi anemia.
PharmGKB	PA134983583.
HUGE	Search... Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG44550.
HOGENOM	HOG000095273.
InParanoid	Q8IY92.
KO	K10484.
OMA	HKFVLYA.
OrthoDB	EOG4S1T8J.
Gene expression databases
Bgee	Q8IY92.
CleanEx	HS_BTBD12.
Genevestigator	Q8IY92.
GermOnline	ENSG00000188827. Homo sapiens.
Family and domain databases
Gene3D	3.30.710.10. 1 hit.
InterPro	IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. IPR013069. BTB_POZ. [Graphical view]
Pfam	PF00651. BTB. 1 hit. [Graphical view]
SMART	SM00225. BTB. 1 hit. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
PROSITE	PS50097. BTB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SLX4. human.
GenomeRNAi	84464.
NextBio	74266.
SOURCE	Search...

Entry information

Entry name

SLX4_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.