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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

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
  • interstrand cross-link repair Source: GO_Central
  • meiotic DNA double-strand break processing Source: GO_Central
  • nucleotide-excision repair Source: UniProtKB
  • positive regulation of t-circle formation Source: BHF-UCL
  • resolution of meiotic recombination intermediates Source: GO_Central
  • response to intra-S DNA damage checkpoint signaling Source: MGI
  • t-circle formation Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Enzyme and pathway databases

BioCyciZFISH:G66-31599-MONOMER.
ReactomeiR-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-6783310. Fanconi Anemia Pathway.
SIGNORiQ8IY92.

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
Proteomesi
  • UP000005640 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

DisGeNETi84464.
MalaCardsiSLX4.
MIMi613951. phenotype.
OpenTargetsiENSG00000188827.
Orphaneti84. Fanconi anemia.
PharmGKBiPA134983583.

Polymorphism and mutation databases

BioMutaiSLX4.
DMDMi205371796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001862191 – 1834Structure-specific endonuclease subunit SLX4Add BLAST1834

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei169PhosphoserineCombined sources1
Modified residuei287PhosphoserineCombined sources1
Cross-linki291Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1028PhosphoserineCombined sources1
Modified residuei1044PhosphoserineCombined sources1
Modified residuei1070PhosphoserineCombined sources1
Cross-linki1112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1121PhosphoserineBy similarity1
Modified residuei1135PhosphoserineBy similarity1
Cross-linki1179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1180Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1185PhosphoserineCombined sources1
Modified residuei1464PhosphoserineBy similarity1
Modified residuei1469PhosphoserineCombined sources1
Cross-linki1575Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1610PhosphoserineBy similarity1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8IY92.
MaxQBiQ8IY92.
PaxDbiQ8IY92.
PeptideAtlasiQ8IY92.
PRIDEiQ8IY92.

PTM databases

iPTMnetiQ8IY92.
PhosphoSitePlusiQ8IY92.

Expressioni

Gene expression databases

BgeeiENSG00000188827.
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
MUS81Q96NY910EBI-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. 46 interactors.
IntActiQ8IY92. 162 interactors.
STRINGi9606.ENSP00000294008.

Structurei

Secondary structure

11834
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi668 – 682Combined sources15
Turni683 – 686Combined sources4
Beta strandi693 – 696Combined sources4
Beta strandi702 – 705Combined sources4
Helixi707 – 713Combined sources7
Helixi715 – 724Combined sources10
Beta strandi726 – 730Combined sources5
Beta strandi733 – 739Combined sources7
Helixi745 – 757Combined sources13
Helixi764 – 766Combined sources3
Helixi767 – 776Combined sources10
Helixi780 – 787Combined sources8
Helixi1016 – 1019Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M7CX-ray2.05C/D1014-1025[»]
4UYIX-ray1.86A668-796[»]
4ZOUX-ray2.15A669-787[»]
ProteinModelPortaliQ8IY92.
SMRiQ8IY92.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini691 – 764BTBPROSITE-ProRule annotationAdd BLAST74

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 669Interaction with SLX4IP, ERCC4 and MSH21 PublicationAdd BLAST669
Regioni684 – 1834Interaction with PLK1 and TERF2-TERF2IP1 PublicationAdd BLAST1151
Regioni1328 – 1648Interaction with MUS81Add BLAST321
Regioni1632 – 1834Interaction with SLX1Add BLAST203

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili801 – 870Sequence analysisAdd BLAST70

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi520 – 523Poly-Pro4
Compositional biasi796 – 856Glu-richAdd BLAST61
Compositional biasi1710 – 1721Poly-SerAdd BLAST12

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFPH. Eukaryota.
ENOG410XPS5. LUCA.
GeneTreeiENSGT00390000014091.
HOGENOMiHOG000095273.
InParanoidiQ8IY92.
KOiK10484.
OMAiHKFVLYA.
OrthoDBiEOG091G10TA.
PhylomeDBiQ8IY92.
TreeFamiTF106446.

Family and domain databases

InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06898238L → F.1 PublicationCorresponds to variant rs141167501dbSNPEnsembl.1
Natural variantiVAR_068983141G → W.1 PublicationCorresponds to variant rs137976282dbSNPEnsembl.1
Natural variantiVAR_068984197V → A.1 PublicationCorresponds to variant rs147826749dbSNPEnsembl.1
Natural variantiVAR_068985204R → C.1 PublicationCorresponds to variant rs79842542dbSNPEnsembl.1
Natural variantiVAR_068986237R → Q.1 PublicationCorresponds to variant rs138615800dbSNPEnsembl.1
Natural variantiVAR_068987284H → R.1 Publication1
Natural variantiVAR_068988378P → T Polymorphism; does not modify the functional properties of the protein. 1 Publication1
Natural variantiVAR_068989385P → T.1 PublicationCorresponds to variant rs115694169dbSNPEnsembl.1
Natural variantiVAR_068990386M → V.1 PublicationCorresponds to variant rs113490934dbSNPEnsembl.1
Natural variantiVAR_068991424A → V.1 PublicationCorresponds to variant rs551823420dbSNPEnsembl.1
Natural variantiVAR_068992457N → K.1 PublicationCorresponds to variant rs74319927dbSNPEnsembl.1
Natural variantiVAR_068993458K → E.1 PublicationCorresponds to variant rs149126845dbSNPEnsembl.1
Natural variantiVAR_068994505A → T.1 Publication1
Natural variantiVAR_068995506S → N.1 Publication1
Natural variantiVAR_068996568V → M.1 PublicationCorresponds to variant rs371825444dbSNPEnsembl.1
Natural variantiVAR_068997579L → P.1 PublicationCorresponds to variant rs772504776dbSNPEnsembl.1
Natural variantiVAR_068998671L → S.2 PublicationsCorresponds to variant rs77985244dbSNPEnsembl.1
Natural variantiVAR_068999787E → K Polymorphism; does not modify the functional properties of the protein. 1 PublicationCorresponds to variant rs140600202dbSNPEnsembl.1
Natural variantiVAR_069000870A → V.1 PublicationCorresponds to variant rs149584080dbSNPEnsembl.1
Natural variantiVAR_069001894V → G.1 PublicationCorresponds to variant rs145137472dbSNPEnsembl.1
Natural variantiVAR_069002929P → L.1 PublicationCorresponds to variant rs117707719dbSNPEnsembl.1
Natural variantiVAR_069003942E → Q.1 PublicationCorresponds to variant rs114014006dbSNPEnsembl.1
Natural variantiVAR_069004952A → M Requires 2 nucleotide substitutions. 2 Publications1
Natural variantiVAR_069005975P → L.1 PublicationCorresponds to variant rs114472821dbSNPEnsembl.1
Natural variantiVAR_0690061007Q → K.1 PublicationCorresponds to variant rs138798067dbSNPEnsembl.1
Natural variantiVAR_0690071060R → W.1 PublicationCorresponds to variant rs144273492dbSNPEnsembl.1
Natural variantiVAR_0193261122P → L.2 PublicationsCorresponds to variant rs714181dbSNPEnsembl.1
Natural variantiVAR_0690081123S → Y.1 PublicationCorresponds to variant rs144647122dbSNPEnsembl.1
Natural variantiVAR_0197291221A → V.2 PublicationsCorresponds to variant rs3827530dbSNPEnsembl.1
Natural variantiVAR_0193271271S → F.1 PublicationCorresponds to variant rs3810813dbSNPEnsembl.1
Natural variantiVAR_0690091286A → V.1 PublicationCorresponds to variant rs149011965dbSNPEnsembl.1
Natural variantiVAR_0690101287V → G.1 Publication1
Natural variantiVAR_0690111342S → G.1 PublicationCorresponds to variant rs140051968dbSNPEnsembl.1
Natural variantiVAR_0463371367A → T.Corresponds to variant rs17136464dbSNPEnsembl.1
Natural variantiVAR_0690121421I → F.1 PublicationCorresponds to variant rs141567438dbSNPEnsembl.1
Natural variantiVAR_0690131476T → S.1 PublicationCorresponds to variant rs372321470dbSNPEnsembl.1
Natural variantiVAR_0690141550R → W Polymorphism; does not modify the functional properties of the protein. 1 PublicationCorresponds to variant rs77021998dbSNPEnsembl.1
Natural variantiVAR_0463381677P → S.Corresponds to variant rs7196345dbSNPEnsembl.1
Natural variantiVAR_0690151694A → V.1 PublicationCorresponds to variant rs761226343dbSNPEnsembl.1
Natural variantiVAR_0690161814R → C.1 PublicationCorresponds to variant rs767720336dbSNPEnsembl.1
Natural variantiVAR_0690171834N → S Polymorphism; does not modify the functional properties of the protein. 1 PublicationCorresponds to variant rs111738042dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0352951 – 312Missing in isoform 2. 1 PublicationAdd BLAST312
Alternative sequenceiVSP_035296313 – 316QHVN → MFSF in isoform 2. 1 Publication4

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_032444.3. [Q8IY92-1]
UniGeneiHs.143681.

Genome annotation databases

EnsembliENST00000294008; ENSP00000294008; ENSG00000188827. [Q8IY92-1]
GeneIDi84464.
KEGGihsa:84464.
UCSCiuc002cvp.3. 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_032444.3. [Q8IY92-1]
UniGeneiHs.143681.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M7CX-ray2.05C/D1014-1025[»]
4UYIX-ray1.86A668-796[»]
4ZOUX-ray2.15A669-787[»]
ProteinModelPortaliQ8IY92.
SMRiQ8IY92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124097. 46 interactors.
IntActiQ8IY92. 162 interactors.
STRINGi9606.ENSP00000294008.

PTM databases

iPTMnetiQ8IY92.
PhosphoSitePlusiQ8IY92.

Polymorphism and mutation databases

BioMutaiSLX4.
DMDMi205371796.

Proteomic databases

EPDiQ8IY92.
MaxQBiQ8IY92.
PaxDbiQ8IY92.
PeptideAtlasiQ8IY92.
PRIDEiQ8IY92.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294008; ENSP00000294008; ENSG00000188827. [Q8IY92-1]
GeneIDi84464.
KEGGihsa:84464.
UCSCiuc002cvp.3. human. [Q8IY92-1]

Organism-specific databases

CTDi84464.
DisGeNETi84464.
GeneCardsiSLX4.
GeneReviewsiSLX4.
H-InvDBHIX0202244.
HGNCiHGNC:23845. SLX4.
HPAiHPA049421.
HPA066238.
MalaCardsiSLX4.
MIMi613278. gene.
613951. phenotype.
neXtProtiNX_Q8IY92.
OpenTargetsiENSG00000188827.
Orphaneti84. Fanconi anemia.
PharmGKBiPA134983583.
HUGEiSearch...
Search...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFPH. Eukaryota.
ENOG410XPS5. LUCA.
GeneTreeiENSGT00390000014091.
HOGENOMiHOG000095273.
InParanoidiQ8IY92.
KOiK10484.
OMAiHKFVLYA.
OrthoDBiEOG091G10TA.
PhylomeDBiQ8IY92.
TreeFamiTF106446.

Enzyme and pathway databases

BioCyciZFISH:G66-31599-MONOMER.
ReactomeiR-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-6783310. Fanconi Anemia Pathway.
SIGNORiQ8IY92.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000188827.
CleanExiHS_BTBD12.
GenevisibleiQ8IY92. HS.

Family and domain databases

InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/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...

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: November 30, 2016
This is version 131 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

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 one 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.