SLX1_SCHPO - dbPTM
SLX1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLX1_SCHPO
UniProt AC Q9P7M3
Protein Name Structure-specific endonuclease subunit slx1 {ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000303|PubMed:14528010, ECO:0000312|EMBL:CAB76036.1}
Gene Name slx1 {ECO:0000312|EMBL:CAB76036.1}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 271
Subcellular Localization Nucleus, nucleolus . Associates with chromatin at rDNA repeat protrusions.
Protein Description Catalytic subunit 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 stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. It is also required for suppression of methyl methanesulfonate (MMS) and UV-C irradiation hypersensitivity of the structural maintenance of chromosome (SMC) protein mutant, smc6-74, by overexpression of brc1. Has Holliday junction resolvase activity in vitro..
Protein Sequence MDLCNFYCCYLLKSNRTQSSGAVYIGSTPDPPRRLRQHNGEIVGGASKTKHGRPWSISCLVYGFPNKVSALKFEWNWQNLGISRYTKDCDFRSKKQKTIMYCLKGLKHLVDSDTWRRWPLNITFLNKTAFSKWNQLGKTYGNINVYFDEEWLNGFHEKVIQKTYDHKLCLRKTISEPVKCNLCYECIESDELRANCPFTDCNSINHLTCLASSFLTEECQVLPIEGMCTKCKRVLRWREFLSTVFTTSLETDERDFESENRIEIIDLELEK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster

Oops, there are no PTM records of SLX1_SCHPO !!

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SLX1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLX1_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SLX1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HUS2_SCHPOrqh1genetic
14528010
SLX4_SCHPOslx4physical
14528010
DNM1_SCHPOdnm1genetic
18818364
YBPD_SCHPOSPBC16H5.13genetic
18818364
BDC1_SCHPObdc1genetic
18818364
ASK1_SCHPOask1genetic
18818364
HIR1_SCHPOhip1genetic
18818364
RL16B_SCHPOrpl1601genetic
18818364
SWC5_SCHPOswc5genetic
18818364
VPH2_SCHPOvph2genetic
18818364
SLX4_SCHPOslx4physical
26787556

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLX1_SCHPO

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Related Literatures of Post-Translational Modification

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