E3 ubiquitin-protein ligase SHPRH (SNF2, histone-linker, PHD & RING finger domain-containing helicase; SHPRH ;KIAA2023)

Function: 1) E3 ubiquitin-protein ligase involved in DNA repair 2) upon genotoxic stress, accepts ubiquitin from UBE2N-UBE2V2 E2 complex & transfers it to Lys-164 of PCNA which had been monoubiquitinated by UBE2A/B-RAD18, promoting formation of non-canonical poly-ubiquitin chains linked through Lys-63 3) ubiquitin conjugation, 3rd step. 4) interacts with PCNA, UBE2N & RAD18 Structure: - homodimer - belongs to the SNF2/RAD54 helicase family - contains 1 helicase ATP-binding domain - contains 1 helicase C-terminal domain - contains 1 histone H1 domain - contains 1 PHD-type zinc finger - contains 1 RING-type zinc finger - mediates E3 ubiquitin ligase activity Alternative splicing: named isoforms=5 Expression: broadly expressed

General

ring finger protein E3 ubiquitin ligase; ubiquitin-ligating enzyme E3; N end-recognizing protein

Properties

SIZE: MW = 193 kD entity length = 1683 aa MOTIF: helicase NAME: helicase SITE: 307-389 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 373-380 Histone H1 {438-512} Zn finger PHD-type NAME: Zn finger PHD-type SITE: 658-709 EFFECTOR-BOUND: Zn+2 helicase NAME: helicase SITE: 710-868 MOTIF: DEAQ box {819-822} RING-finger {1432-1479} EFFECTOR-BOUND: Zn+2 FOR-BINDING-OF: DNA motif Helicase C-terminal {1514-1672}

Database Correlations

OMIM 608048 UniProt Q149N8

References

UniProt :accession Q149N8