SCUBA

SH3RF1 — SH3 domain containing ring finger 1

SH3RF1 belongs to a gene co-expression module in 1 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

SH3RF1's module in each cell type

Cell typeModuleShares the module with
EnterocytesBasal adhesion remodeling
Migration & adhesion
EPB41L2, ETS2, FNDC3B, HERC4, ITGA6, NT5C2, SESTD1, SGMS1 +2 moreView in SCUBA

About the gene

SynonymsKIAA1494, POSH, RNF142, SH3MD2
Chromosome4: 169094259-169270956
Predicted locationIntracellular
Essential geneNo
Protein classEnzymes, Metabolic proteins, Predicted intracellular proteins
Molecular functionTransferase
Biological processHost-virus interaction, Ubl conjugation pathway

Function

Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin- independent endocytosis. Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (By similarity). (Microbial infection) Plays an essential role in the targeting of HIV-1 Gag to the plasma membrane, this function is dependent on it's RING domain, and hence it's E3 ligase activity

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.