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This gene encodes a serine protease. The protein has been localized in the endoplasmic reticulum and interacts with an alternatively spliced form of mitogen-activated protein kinase 14. The protein has also been localized to the mitochondria with release to the cytosol following apoptotic stimulus. The protein is thought to induce apoptosis by binding the apoptosis inhibitory protein baculoviral IAP repeat-containing 4. Nuclear localization of this protein has also been observed. Alternate spl

GOLPH2 is widely expressed. Expression levels are high in the colon, prostate, trachea and stomach; expressed at lower level in testis, muscle, lymphoid tissues, white blood cells and spleen. GOLPH2 is predominantly expressed by cells of the epithelial lineage. It is expressed at a low level in normal liver, though expression significantly increases in virus (HBV, HCV) infected liver. Expression does not increase in liver disease due to non viral causes (alcohol induced liver disease, autoimm

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [p

Lamins are nuclear membrane proteins that serve to maintain specific cellular functions, such as DNA replication and chromatin organization. Lamin B receptor (LBR) is an integral protein of the nuclear envelope inner membrane. It is phosphorylated by CDC2 protein kinase in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin. It is phosphorylated by different protein kinases in interphase when the membrane is associated with these

Early endosomes are cytoplasmic compartments that function in receiving and sorting endocytosed proteins for vesicular transport. EEA1 (early endosome antigen 1) is a peripheral membrane protein that co-localizes with the transferrin receptor and Rab5 on early endosomes. EEA1 contains a calmodulin-binding IQ motif and cysteine rich finger motif necessary for its specific localization to the early endosomes. EEA1 has sequence homology to several yeast proteins that have been implicated in mem