Consists of 31 Exons with a total transcription length of 4,013bps.

The coding region of the gene starts from exon 1 to exon 31 (200^th bps to 3508^th bps). The length of the transcript is 3308 bps.

None

HAUSP encodes for 1102 amino acids and its molecular weight is approximately 135kDa. MALDI-TOF/MS analysis has revealed four structural domains which are mainly involved in protein-protein interaction and deubiquitination activity.
N-terminal MATH (TRAF-like) domain (62-205aa) represented in brown colour is responsible for interaction with p53, MDM2 and EBNA1. N-terminal domain of USP7 complexed with Mdm2 at peptide 147-150 and with p53 at position 359-362 and 364-367 respectively.
Ubiquitin processing protease domain represented in yellow colour is a large family of cysteine proteases responsible for the cleavage of ubiquitin conjugates. Catalytic domain consists of approximately 350 amino acids, comprising three conserved domain architectures Finger, Palm, and Thumb. It has highly conserved Cys, Asp(I), His, and Asn/Asp(II) domains, which are responsible for deubiquitination activities.
ICP0 binding domain represented in green colour is located in the C-terminal region at position 599-801 amino acids. N-terminal polyglutamine (poly Q) region at position 4-10 amino acids which is conserved among mouse, rat and human.

HAUSP is expressed in wide variety of cell types including brain, liver, placenta, lung, ovary and melanocytes.

HAUSP primarily localized in Nucleus.

Herpesvirus-associated ubiquitin-specific protease was identified as a novel p53-interacting protein. HAUSP binds and stabilizes p53 through deubiquitination. It also strongly interacts with MDM2, hence playing an important role in the p53-MDM2 pathway resulting in p53-dependent cell growth repression and apoptosis. The tumor suppressor p53 protein is a transcription factor that responds to many cellular stress signals and is regulated primarily through ubiquitination and subsequent degradation. HAUSP contains an N-terminal TRAF-like domain in which p53 and MDM2 binds at the same site implied that HAUSP may function as a tumor suppressor by stabilizing p53.
HAUSP also interacts with the Epstein-Barr nuclear antigen 1 (EBNA1) protein of the Epstein-Barr virus (EBV), which is responsible for EBV latent infection and cellular transformation. Interaction of EBNA1 with USP7 occurs at same N-terminal TRAF-like domain at which p53 also binds to USP7. Through interactions with p53, MDM2 and EBNA1, HAUSP plays a role in cell proliferation, apoptosis and EBV-mediated immortalization.

Human HAUSP shows 98.6% amino acid homology with both rat HAUSP and mouse HAUSP.