Property Summary

NCBI Gene PubMed Count 38
Grant Count 54
R01 Count 38
Funding $3,754,652.64
PubMed Score 54.86
PubTator Score 42.23

Knowledge Summary

Patent

No data available

Expression

  Differential Expression (1)

Disease log2 FC p
osteosarcoma -1.736 0.000

Gene RIF (49)

PMID Text
26453996 SLX4 (FANCP) and XPF (FANCQ) proteins interact with each other and play a vital role in the Fanconi anemia (FA) DNA repair pathway. Study has revealed that the global minor allele, SLX4(Y546C), is defective in this interaction.
25722289 SUMOylation and PARylation cooperate to recruit and stabilize SLX4 at DNA damage sites.
25533188 The SLX4 complex is a SUMO E3 ligase that SUMOylates SLX4 itself and the XPF subunit of the DNA repair/recombination XPF-ERCC1 endonuclease.
25533185 The interactions of SLX4 with SUMO and ubiquitin increase its affinity for factors recognizing different DNA lesions or telomeres, helping to direct the SLX4 complex in distinct functional contexts.
25496524 Vpr recruits the SLX4 endonuclease complex and Vpr-induced inappropriate activation of this complex leads to cell cycle arrest at the G2 phase.
25496524 HIV-1 Vpr-mediated cell cycle G2/M arrest requires human SLX4, MUS81, and EME1 proteins in cells
25496524 HIV-1 Vpr-mediated cell cycle G2/M arrest requires human SLX4, MUS81, and EME1 proteins in cells
25496524 HIV-1 Vpr-mediated cell cycle G2/M arrest requires human SLX4, MUS81, and EME1 proteins in cells
25496524 HIV-1 Vpr-mediated cell cycle G2/M arrest requires human SLX4, MUS81, and EME1 proteins in cells
25496524 HIV-1 Vpr-mediated cell cycle G2/M arrest requires human SLX4, MUS81, and EME1 proteins in cells
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AA Sequence

MKLSVNEAQLGFYLGSLSHLSACPGIDPRSSEDQPESLKTGQMMDESDEDFKELCASFFQRVKKHGIKEV      1 - 70
SGERKTQKAASNGTQIRSKLKRTKQTATKTKTLQGPAEKKPPSGSQAPRTKKQRVTKWQASEPAHSVNGE     71 - 140
GGVLASAPDPPVLRETAQNTQTGNQQEPSPNLSREKTRENVPNSDSQPPPSCLTTAVPSPSKPRTAQLVL    141 - 210
QRMQQFKRADPERLRHASEECSLEAAREENVPKDPQEEMMAGNVYGLGPPAPESDAAVALTLQQEFARVG    211 - 280
ASAHDDSLEEKGLFFCQICQKNLSAMNVTRREQHVNRCLDEAEKTLRPSVPQIPECPICGKPFLTLKSRT    281 - 350
SHLKQCAVKMEVGPQLLLQAVRLQTAQPEGSSSPPMFSFSDHSRGLKRRGPTSKKEPRKRRKVDEAPSED    351 - 420
LLVAMALSRSEMEPGAAVPALRLESAFSERIRPEAENKSRKKKPPVSPPLLLVQDSETTGRQIEDRVALL    421 - 490
LSEEVELSSTPPLPASRILKEGWERAGQCPPPPERKQSFLWEGSALTGAWAMEDFYTARLVPPLVPQRPA    491 - 560
QGLMQEPVPPLVPPEHSELSERRSPALHGTPTAGCGSRGPSPSASQREHQALQDLVDLAREGLSASPWPG    561 - 630
SGGLAGSEGTAGLDVVPGGLPLTGFVVPSQDKHPDRGGRTLLSLGLLVADFGAMVNNPHLSDVQFQTDSG    631 - 700
EVLYAHKFVLYARCPLLIQYVNNEGFSAVEDGVLTQRVLLGDVSTEAARTFLHYLYTADTGLPPGLSSEL    701 - 770
SSLAHRFGVSELVHLCEQVPIATDSEGKPWEEKEAENCESRAENFQELLRSMWADEEEEAETLLKSKDHE    771 - 840
EDQENVNEAEMEEIYEFAATQRKLLQEERAAGAGEDADWLEGGSPVSGQLLAGVQVQKQWDKVEEMEPLE    841 - 910
PGRDEAATTWEKMGQCALPPPQGQHSGARGAEAPEQEAPEEALGHSSCSSPSRDCQAERKEGSLPHSDDA    911 - 980
GDYEQLFSSTQGEISEPSQITSEPEEQSGAVRERGLEVSHRLAPWQASPPHPCRFLLGPPQGGSPRGSHH    981 - 1050
TSGSSLSTPRSRGGTSQVGSPTLLSPAVPSKQKRDRSILTLSKEPGHQKGKERRSVLECRNKGVLMFPEK   1051 - 1120
SPSIDLTQSNPDHSSSRSQKSSSKLNEEDEVILLLDSDEELELEQTKMKSISSDPLEEKKALEISPRSCE   1121 - 1190
LFSIIDVDADQEPSQSPPRSEAVLQQEDEGALPENRGSLGRRGAPWLFCDRESSPSEASTTDTSWLVPAT   1191 - 1260
PLASRSRDCSSQTQISSLRSGLAVQAVTQHTPRASVGNREGNEVAQKFSVIRPQTPPPQTPSSCLTPVSP   1261 - 1330
GTSDGRRQGHRSPSRPHPGGHPHSSPLAPHPISGDRAHFSRRFLKHSPPGPSFLNQTPAGEVVEVGDSDD   1331 - 1400
EQEVASHQANRSPPLDSDPPIPIDDCCWHMEPLSPIPIDHWNLERTGPLSTSSPSRRMNEAADSRDCRSP   1401 - 1470
GLLDTTPIRGSCTTQRKLQEKSSGAGSLGNSRPSFLNSALWDVWDGEEQRPPETPPPAQMPSAGGAQKPE   1471 - 1540
GLETPKGANRKKNLPPKVPITPMPQYSIMETPVLKKELDRFGVRPLPKRQMVLKLKEIFQYTHQTLDSDS   1541 - 1610
EDESQSSQPLLQAPHCQTLASQTYKPSRAGVHAQQEATTGPGAHRPKGPAKTKGPRHQRKHHESITPPSR   1611 - 1680
SPTKEAPPGLNDDAQIPASQESVATSVDGSDSSLSSQSSSSCEFGAAFESAGEEEGEGEVSASQAAVQAA   1681 - 1750
DTDEALRCYIRSKPALYQKVLLYQPFELRELQAELRQNGLRVSSRRLLDFLDTHCITFTTAATRREKLQG   1751 - 1820
RRRQPRGKKKVERN                                                           1821 - 1834
//

Text Mined References (48)

PMID Year Title
27084631 2016 Disruption of SLX4-MUS81 Function Increases the Relative Biological Effectiveness of Proton Radiation.
26453996 2015 Physical interaction between SLX4 (FANCP) and XPF (FANCQ) proteins and biological consequences of interaction-defective missense mutations.
25852190 2015 Integrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapy.
25772364 2015 SUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage.
25755297 2015 System-wide Analysis of SUMOylation Dynamics in Response to Replication Stress Reveals Novel Small Ubiquitin-like Modified Target Proteins and Acceptor Lysines Relevant for Genome Stability.
25722289 2015 SUMOylation and PARylation cooperate to recruit and stabilize SLX4 at DNA damage sites.
25533188 2015 The SLX4 complex is a SUMO E3 ligase that impacts on replication stress outcome and genome stability.
25533185 2015 Noncovalent interactions with SUMO and ubiquitin orchestrate distinct functions of the SLX4 complex in genome maintenance.
25496524 2014 How SLX4 cuts through the mystery of HIV-1 Vpr-mediated cell cycle arrest.
25416956 2014 A proteome-scale map of the human interactome network.
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