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Protein

Structure-specific endonuclease subunit SLX4

Gene

SLX4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  • 5'-flap endonuclease activity Source: InterPro
  • enzyme activator activity Source: UniProtKB

GO - Biological processi

  • DNA double-strand break processing involved in repair via single-strand annealing Source: UniProtKB
  • DNA repair Source: UniProtKB
  • DNA replication Source: InterPro
  • double-strand break repair via homologous recombination Source: UniProtKB
  • nucleotide-excision repair Source: UniProtKB
  • positive regulation of catalytic activity Source: GOC
  • response to intra-S DNA damage checkpoint signaling Source: MGI
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Structure-specific endonuclease subunit SLX4
Alternative name(s):
BTB/POZ domain-containing protein 12
Gene namesi
Name:SLX4
Synonyms:BTBD12, KIAA1784, KIAA1987
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:23845. SLX4.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: HPA
  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • Slx1-Slx4 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Fanconi anemia complementation group P (FANCP)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:613951

Keywords - Diseasei

Fanconi anemia

Organism-specific databases

MIMi613951. phenotype.
Orphaneti84. Fanconi anemia.
PharmGKBiPA134983583.

Polymorphism and mutation databases

BioMutaiSLX4.
DMDMi205371796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18341834Structure-specific endonuclease subunit SLX4PRO_0000186219Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei287 – 2871Phosphoserine1 Publication
Modified residuei1044 – 10441Phosphoserine1 Publication
Modified residuei1469 – 14691Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8IY92.
PaxDbiQ8IY92.
PRIDEiQ8IY92.

PTM databases

PhosphoSiteiQ8IY92.

Expressioni

Gene expression databases

BgeeiQ8IY92.
CleanExiHS_BTBD12.
GenevisibleiQ8IY92. HS.

Organism-specific databases

HPAiHPA049421.
HPA066238.

Interactioni

Subunit structurei

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EME1Q96AY24EBI-2370740,EBI-2370825
ERCC1P079926EBI-2370740,EBI-750962
ERCC4Q9288910EBI-2370740,EBI-2370770
MSH2P432465EBI-2370740,EBI-355888
MUS81B3KX633EBI-10175993,EBI-10175987
MUS81Q96NY98EBI-2370740,EBI-2370806
PLK1P533507EBI-2370740,EBI-476768
SLX1BQ9BQ8310EBI-2370740,EBI-2370858
SLX4IPQ5VYV74EBI-2370740,EBI-2370881
TERF2Q155545EBI-2370740,EBI-706637
TERF2IPQ9NYB04EBI-2370740,EBI-750109

Protein-protein interaction databases

BioGridi124097. 35 interactions.
IntActiQ8IY92. 158 interactions.
STRINGi9606.ENSP00000294008.

Structurei

Secondary structure

1
1834
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi668 – 68215Combined sources
Turni683 – 6864Combined sources
Beta strandi693 – 6964Combined sources
Beta strandi702 – 7054Combined sources
Helixi707 – 7137Combined sources
Helixi715 – 72410Combined sources
Beta strandi726 – 7305Combined sources
Beta strandi733 – 7397Combined sources
Helixi745 – 75713Combined sources
Helixi764 – 7663Combined sources
Helixi767 – 77610Combined sources
Helixi780 – 7878Combined sources
Helixi1016 – 10194Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4M7CX-ray2.05C/D1014-1025[»]
4UYIX-ray1.86A668-796[»]
ProteinModelPortaliQ8IY92.
SMRiQ8IY92. Positions 668-788.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini691 – 76474BTBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 669669Interaction with SLX4IP, ERCC4 and MSH2Add
BLAST
Regioni684 – 18341151Interaction with PLK1 and TERF2-TERF2IPAdd
BLAST
Regioni1328 – 1648321Interaction with MUS81Add
BLAST
Regioni1632 – 1834203Interaction with SLX1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili801 – 87070Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi520 – 5234Poly-Pro
Compositional biasi796 – 85661Glu-richAdd
BLAST
Compositional biasi1710 – 172112Poly-SerAdd
BLAST

Sequence similaritiesi

Belongs to the SLX4 family.Curated
Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG44550.
GeneTreeiENSGT00390000014091.
HOGENOMiHOG000095273.
InParanoidiQ8IY92.
KOiK10484.
OMAiHKFVLYA.
OrthoDBiEOG7ZKSDH.
PhylomeDBiQ8IY92.
TreeFamiTF106446.

Family and domain databases

InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR018574. Structure-sp_endonuc_su_Slx4.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
PF09494. Slx4. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IY92-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MKLSVNEAQL GFYLGSLSHL SACPGIDPRS SEDQPESLKT GQMMDESDED
60 70 80 90 100
FKELCASFFQ RVKKHGIKEV SGERKTQKAA SNGTQIRSKL KRTKQTATKT
110 120 130 140 150
KTLQGPAEKK PPSGSQAPRT KKQRVTKWQA SEPAHSVNGE GGVLASAPDP
160 170 180 190 200
PVLRETAQNT QTGNQQEPSP NLSREKTREN VPNSDSQPPP SCLTTAVPSP
210 220 230 240 250
SKPRTAQLVL QRMQQFKRAD PERLRHASEE CSLEAAREEN VPKDPQEEMM
260 270 280 290 300
AGNVYGLGPP APESDAAVAL TLQQEFARVG ASAHDDSLEE KGLFFCQICQ
310 320 330 340 350
KNLSAMNVTR REQHVNRCLD EAEKTLRPSV PQIPECPICG KPFLTLKSRT
360 370 380 390 400
SHLKQCAVKM EVGPQLLLQA VRLQTAQPEG SSSPPMFSFS DHSRGLKRRG
410 420 430 440 450
PTSKKEPRKR RKVDEAPSED LLVAMALSRS EMEPGAAVPA LRLESAFSER
460 470 480 490 500
IRPEAENKSR KKKPPVSPPL LLVQDSETTG RQIEDRVALL LSEEVELSST
510 520 530 540 550
PPLPASRILK EGWERAGQCP PPPERKQSFL WEGSALTGAW AMEDFYTARL
560 570 580 590 600
VPPLVPQRPA QGLMQEPVPP LVPPEHSELS ERRSPALHGT PTAGCGSRGP
610 620 630 640 650
SPSASQREHQ ALQDLVDLAR EGLSASPWPG SGGLAGSEGT AGLDVVPGGL
660 670 680 690 700
PLTGFVVPSQ DKHPDRGGRT LLSLGLLVAD FGAMVNNPHL SDVQFQTDSG
710 720 730 740 750
EVLYAHKFVL YARCPLLIQY VNNEGFSAVE DGVLTQRVLL GDVSTEAART
760 770 780 790 800
FLHYLYTADT GLPPGLSSEL SSLAHRFGVS ELVHLCEQVP IATDSEGKPW
810 820 830 840 850
EEKEAENCES RAENFQELLR SMWADEEEEA ETLLKSKDHE EDQENVNEAE
860 870 880 890 900
MEEIYEFAAT QRKLLQEERA AGAGEDADWL EGGSPVSGQL LAGVQVQKQW
910 920 930 940 950
DKVEEMEPLE PGRDEAATTW EKMGQCALPP PQGQHSGARG AEAPEQEAPE
960 970 980 990 1000
EALGHSSCSS PSRDCQAERK EGSLPHSDDA GDYEQLFSST QGEISEPSQI
1010 1020 1030 1040 1050
TSEPEEQSGA VRERGLEVSH RLAPWQASPP HPCRFLLGPP QGGSPRGSHH
1060 1070 1080 1090 1100
TSGSSLSTPR SRGGTSQVGS PTLLSPAVPS KQKRDRSILT LSKEPGHQKG
1110 1120 1130 1140 1150
KERRSVLECR NKGVLMFPEK SPSIDLTQSN PDHSSSRSQK SSSKLNEEDE
1160 1170 1180 1190 1200
VILLLDSDEE LELEQTKMKS ISSDPLEEKK ALEISPRSCE LFSIIDVDAD
1210 1220 1230 1240 1250
QEPSQSPPRS EAVLQQEDEG ALPENRGSLG RRGAPWLFCD RESSPSEAST
1260 1270 1280 1290 1300
TDTSWLVPAT PLASRSRDCS SQTQISSLRS GLAVQAVTQH TPRASVGNRE
1310 1320 1330 1340 1350
GNEVAQKFSV IRPQTPPPQT PSSCLTPVSP GTSDGRRQGH RSPSRPHPGG
1360 1370 1380 1390 1400
HPHSSPLAPH PISGDRAHFS RRFLKHSPPG PSFLNQTPAG EVVEVGDSDD
1410 1420 1430 1440 1450
EQEVASHQAN RSPPLDSDPP IPIDDCCWHM EPLSPIPIDH WNLERTGPLS
1460 1470 1480 1490 1500
TSSPSRRMNE AADSRDCRSP GLLDTTPIRG SCTTQRKLQE KSSGAGSLGN
1510 1520 1530 1540 1550
SRPSFLNSAL WDVWDGEEQR PPETPPPAQM PSAGGAQKPE GLETPKGANR
1560 1570 1580 1590 1600
KKNLPPKVPI TPMPQYSIME TPVLKKELDR FGVRPLPKRQ MVLKLKEIFQ
1610 1620 1630 1640 1650
YTHQTLDSDS EDESQSSQPL LQAPHCQTLA SQTYKPSRAG VHAQQEATTG
1660 1670 1680 1690 1700
PGAHRPKGPA KTKGPRHQRK HHESITPPSR SPTKEAPPGL NDDAQIPASQ
1710 1720 1730 1740 1750
ESVATSVDGS DSSLSSQSSS SCEFGAAFES AGEEEGEGEV SASQAAVQAA
1760 1770 1780 1790 1800
DTDEALRCYI RSKPALYQKV LLYQPFELRE LQAELRQNGL RVSSRRLLDF
1810 1820 1830
LDTHCITFTT AATRREKLQG RRRQPRGKKK VERN
Length:1,834
Mass (Da):200,012
Last modified:September 2, 2008 - v3
Checksum:i9131E88628DB15D5
GO
Isoform 2 (identifier: Q8IY92-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,522
Mass (Da):165,903
Checksum:iA3C234F1E746C5FA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381L → F.1 Publication
Corresponds to variant rs141167501 [ dbSNP | Ensembl ].
VAR_068982
Natural varianti141 – 1411G → W.1 Publication
Corresponds to variant rs137976282 [ dbSNP | Ensembl ].
VAR_068983
Natural varianti197 – 1971V → A.1 Publication
Corresponds to variant rs147826749 [ dbSNP | Ensembl ].
VAR_068984
Natural varianti204 – 2041R → C.1 Publication
Corresponds to variant rs79842542 [ dbSNP | Ensembl ].
VAR_068985
Natural varianti237 – 2371R → Q.1 Publication
Corresponds to variant rs138615800 [ dbSNP | Ensembl ].
VAR_068986
Natural varianti284 – 2841H → R.1 Publication
VAR_068987
Natural varianti378 – 3781P → T Polymorphism; does not modify the functional properties of the protein. 1 Publication
VAR_068988
Natural varianti385 – 3851P → T.1 Publication
Corresponds to variant rs115694169 [ dbSNP | Ensembl ].
VAR_068989
Natural varianti386 – 3861M → V.1 Publication
Corresponds to variant rs113490934 [ dbSNP | Ensembl ].
VAR_068990
Natural varianti424 – 4241A → V.1 Publication
VAR_068991
Natural varianti457 – 4571N → K.1 Publication
Corresponds to variant rs74319927 [ dbSNP | Ensembl ].
VAR_068992
Natural varianti458 – 4581K → E.1 Publication
Corresponds to variant rs149126845 [ dbSNP | Ensembl ].
VAR_068993
Natural varianti505 – 5051A → T.1 Publication
VAR_068994
Natural varianti506 – 5061S → N.1 Publication
VAR_068995
Natural varianti568 – 5681V → M.1 Publication
VAR_068996
Natural varianti579 – 5791L → P.1 Publication
VAR_068997
Natural varianti671 – 6711L → S.2 Publications
Corresponds to variant rs77985244 [ dbSNP | Ensembl ].
VAR_068998
Natural varianti787 – 7871E → K Polymorphism; does not modify the functional properties of the protein. 1 Publication
Corresponds to variant rs140600202 [ dbSNP | Ensembl ].
VAR_068999
Natural varianti870 – 8701A → V.1 Publication
Corresponds to variant rs149584080 [ dbSNP | Ensembl ].
VAR_069000
Natural varianti894 – 8941V → G.1 Publication
Corresponds to variant rs145137472 [ dbSNP | Ensembl ].
VAR_069001
Natural varianti929 – 9291P → L.1 Publication
Corresponds to variant rs117707719 [ dbSNP | Ensembl ].
VAR_069002
Natural varianti942 – 9421E → Q.1 Publication
Corresponds to variant rs114014006 [ dbSNP | Ensembl ].
VAR_069003
Natural varianti952 – 9521A → M Requires 2 nucleotide substitutions. 2 Publications
VAR_069004
Natural varianti975 – 9751P → L.1 Publication
Corresponds to variant rs114472821 [ dbSNP | Ensembl ].
VAR_069005
Natural varianti1007 – 10071Q → K.1 Publication
Corresponds to variant rs138798067 [ dbSNP | Ensembl ].
VAR_069006
Natural varianti1060 – 10601R → W.1 Publication
VAR_069007
Natural varianti1122 – 11221P → L.2 Publications
Corresponds to variant rs714181 [ dbSNP | Ensembl ].
VAR_019326
Natural varianti1123 – 11231S → Y.1 Publication
Corresponds to variant rs144647122 [ dbSNP | Ensembl ].
VAR_069008
Natural varianti1221 – 12211A → V.2 Publications
Corresponds to variant rs3827530 [ dbSNP | Ensembl ].
VAR_019729
Natural varianti1271 – 12711S → F.1 Publication
Corresponds to variant rs3810813 [ dbSNP | Ensembl ].
VAR_019327
Natural varianti1286 – 12861A → V.1 Publication
Corresponds to variant rs149011965 [ dbSNP | Ensembl ].
VAR_069009
Natural varianti1287 – 12871V → G.1 Publication
VAR_069010
Natural varianti1342 – 13421S → G.1 Publication
Corresponds to variant rs140051968 [ dbSNP | Ensembl ].
VAR_069011
Natural varianti1367 – 13671A → T.
Corresponds to variant rs17136464 [ dbSNP | Ensembl ].
VAR_046337
Natural varianti1421 – 14211I → F.1 Publication
Corresponds to variant rs141567438 [ dbSNP | Ensembl ].
VAR_069012
Natural varianti1476 – 14761T → S.1 Publication
VAR_069013
Natural varianti1550 – 15501R → W Polymorphism; does not modify the functional properties of the protein. 1 Publication
Corresponds to variant rs77021998 [ dbSNP | Ensembl ].
VAR_069014
Natural varianti1677 – 16771P → S.
Corresponds to variant rs7196345 [ dbSNP | Ensembl ].
VAR_046338
Natural varianti1694 – 16941A → V.1 Publication
VAR_069015
Natural varianti1814 – 18141R → C.1 Publication
VAR_069016
Natural varianti1834 – 18341N → S Polymorphism; does not modify the functional properties of the protein. 1 Publication
Corresponds to variant rs111738042 [ dbSNP | Ensembl ].
VAR_069017

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 312312Missing in isoform 2. 1 PublicationVSP_035295Add
BLAST
Alternative sequencei313 – 3164QHVN → MFSF in isoform 2. 1 PublicationVSP_035296

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC006111 Genomic DNA. No translation available.
AB075867 mRNA. Translation: BAB85573.1.
AB058687 mRNA. Translation: BAB47413.1.
AL442083 mRNA. Translation: CAH10659.1.
CCDSiCCDS10506.2. [Q8IY92-1]
RefSeqiNP_115820.2. NM_032444.2. [Q8IY92-1]
UniGeneiHs.143681.

Genome annotation databases

EnsembliENST00000294008; ENSP00000294008; ENSG00000188827. [Q8IY92-1]
GeneIDi84464.
KEGGihsa:84464.
UCSCiuc002cvp.2. human. [Q8IY92-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

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

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC006111 Genomic DNA. No translation available.
AB075867 mRNA. Translation: BAB85573.1.
AB058687 mRNA. Translation: BAB47413.1.
AL442083 mRNA. Translation: CAH10659.1.
CCDSiCCDS10506.2. [Q8IY92-1]
RefSeqiNP_115820.2. NM_032444.2. [Q8IY92-1]
UniGeneiHs.143681.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4M7CX-ray2.05C/D1014-1025[»]
4UYIX-ray1.86A668-796[»]
ProteinModelPortaliQ8IY92.
SMRiQ8IY92. Positions 668-788.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124097. 35 interactions.
IntActiQ8IY92. 158 interactions.
STRINGi9606.ENSP00000294008.

PTM databases

PhosphoSiteiQ8IY92.

Polymorphism and mutation databases

BioMutaiSLX4.
DMDMi205371796.

Proteomic databases

MaxQBiQ8IY92.
PaxDbiQ8IY92.
PRIDEiQ8IY92.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294008; ENSP00000294008; ENSG00000188827. [Q8IY92-1]
GeneIDi84464.
KEGGihsa:84464.
UCSCiuc002cvp.2. human. [Q8IY92-1]

Organism-specific databases

CTDi84464.
GeneCardsiGC16M003632.
GeneReviewsiSLX4.
H-InvDBHIX0202244.
HGNCiHGNC:23845. SLX4.
HPAiHPA049421.
HPA066238.
MIMi613278. gene.
613951. phenotype.
neXtProtiNX_Q8IY92.
Orphaneti84. Fanconi anemia.
PharmGKBiPA134983583.
HUGEiSearch...
Search...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44550.
GeneTreeiENSGT00390000014091.
HOGENOMiHOG000095273.
InParanoidiQ8IY92.
KOiK10484.
OMAiHKFVLYA.
OrthoDBiEOG7ZKSDH.
PhylomeDBiQ8IY92.
TreeFamiTF106446.

Miscellaneous databases

ChiTaRSiSLX4. human.
GeneWikiiSLX4.
GenomeRNAii84464.
NextBioi74266.
PROiQ8IY92.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IY92.
CleanExiHS_BTBD12.
GenevisibleiQ8IY92. HS.

Family and domain databases

InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR018574. Structure-sp_endonuc_su_Slx4.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
PF09494. Slx4. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. Cited for: INVOLVEMENT IN FANCP.
  15. Cited for: INVOLVEMENT IN FANCP.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. 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.

Entry informationi

Entry nameiSLX4_HUMAN
AccessioniPrimary (citable) accession number: Q8IY92
Secondary accession number(s): Q69YT8, Q8TF15, Q96JP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: September 2, 2008
Last modified: June 24, 2015
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.