USP28 Rabbit Polyclonal Antibody (ER1803-52)

UNIPROT #

Q96RU2

PROTEIN NAME

USP28

SYNONYMS

Deubiquitinating enzyme 28 antibody;KIAA1515 antibody;Ubiquitin carboxyl terminal hydrolase 28 antibody;Ubiquitin carboxyl-terminal hydrolase 28 antibody;ubiquitin carboxyl-terminal hydrolase 28 variant 1 antibody;Ubiquitin specific peptidase 28 antibody;Ubiquitin specific processing protease 28 antibody;Ubiquitin specific protease 28 antibody;Ubiquitin thioesterase 28 antibody;Ubiquitin thiolesterase 28 antibody;Ubiquitin-specific-processing protease 28 antibody;UBP28_HUMAN antibody;USP 28 antibody;USP28 antibody;USP28 protein antibody

SEQUENCE SIMILARITIES

Belongs to the peptidase C19 family. USP28 subfamily.

POST-TRANSLATIONAL MODIFICATION

Degraded upon nickel ion level or hypoxia exposure.; Phosphorylated upon DNA damage at Ser-67 and Ser-714, by ATM or ATR. Phosphorylated by PRKD1.

SUBCELLULAR LOCATION

Nucleus.

FUNCTION

Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does not interact with isoform 4 of FBXW7 (FBW7gamma) in the nucleolus, allowing MYC degradation and explaining the selective MYC degradation in the nucleolus. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells.