Mouse Anti-SMURF1 Monoclonal Antibody (1E8) (CBMAB-0144-LY)

SMURF1

This gene encodes a ubiquitin ligase that is specific for receptor-regulated SMAD proteins in the bone morphogenetic protein (BMP) pathway. This protein plays a key roll in the regulation of cell motility, cell signalling, and cell polarity. Alternative splicing results in multiple transcript variants encoding different isoforms. E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway. Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway. Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA. Promotes ubiquitination and subsequent proteasomal degradation of MAVS.

KIAA1625

E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway. Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway. Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA. Promotes ubiquitination and subsequent proteasomal degradation of MAVS (PubMed:23087404).
Plays a role in dendrite formation by melanocytes (PubMed:23999003).

Biological Process BMP signaling pathwayManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process cell differentiationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process ectoderm developmentManual Assertion Based On ExperimentTAS:UniProtKB
Biological Process engulfment of target by autophagosomeManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process negative regulation of BMP signaling pathwayManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process negative regulation of transforming growth factor beta receptor signaling pathwayManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process positive regulation of axon extensionIEA:Ensembl
Biological Process positive regulation of dendrite extensionManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of ubiquitin-dependent protein catabolic processManual Assertion Based On ExperimentIMP:CACAO
Biological Process proteasome-mediated ubiquitin-dependent protein catabolic processManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process protein export from nucleusManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process protein localization to cell surfaceManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process protein localization to plasma membraneManual Assertion Based On ExperimentTAS:ParkinsonsUK-UCL
Biological Process protein polyubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process protein targeting to vacuole involved in autophagyManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process protein ubiquitinationManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process receptor catabolic processManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process substrate localization to autophagosomeManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process ubiquitin-dependent protein catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process ubiquitin-dependent SMAD protein catabolic processManual Assertion Based On ExperimentIDA:BHF-UCL
Biological Process Wnt signaling pathway, planar cell polarity pathwayTAS:Reactome

Cytoplasm
Cell membrane

Auto-ubiquitinated in presence of NDFIP1 (PubMed:23087404).
Ubiquitinated by the SCF(FBXL15) complex at Lys-381 and Lys-383, leading to its degradation by the proteasome. Lys-383 is the primary ubiquitination site.