USP8

USP8

Identifiers

USP8, HumORF8, SPG59, UBPY, ubiquitin specific peptidase 8, PITA4

External IDs

OMIM: 603158; MGI: 1934029; GeneCards: USP8

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1WHB, 2A9U, 2GFO, 2GWF, 3N3K

Enzyme activity
EC #	BRENDA	ExPASy	KEGG	MetaCyc
3.4.19.12	↗	↗	↗	↗

Gene location (Human)

Chr.	Chromosome 15 (human)

Band	15q21.2	Start	50,424,380 bp
Band	15q21.2	End	50,514,421 bp

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)

Band	2\|2 F1	Start	126,549,248 bp
Band	2\|2 F1	End	126,601,217 bp

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

Achilles tendon

sural nerve

epithelium of colon

ventricular zone

testicle

rectum

monocyte

caput epididymis

corpus epididymis

gallbladder

Top expressed in

spermatid

seminiferous tubule

spermatocyte

tail of embryo

genital tubercle

right kidney

stroma of bone marrow

zygote

deep cerebellar nuclei

medial vestibular nucleus

More reference expression data

n/a

Gene ontology
Molecular function	cysteine-type peptidase activity SH3 domain binding thiol-dependent deubiquitinase peptidase activity protein binding cysteine-type endopeptidase activity hydrolase activity cadherin binding
Cellular component	cytoplasm endosome membrane plasma membrane extrinsic component of endosome membrane midbody endosome membrane extrinsic component of plasma membrane nucleus postsynaptic density dendritic spine early endosome cytosol glutamatergic synapse
Biological process	protein K48-linked deubiquitination ubiquitin-dependent protein catabolic process mitotic cytokinesis endosome organization proteolysis protein K63-linked deubiquitination cell cycle cell population proliferation protein deubiquitination cellular response to dexamethasone stimulus cellular response to nerve growth factor stimulus positive regulation of canonical Wnt signaling pathway Ras protein signal transduction regulation of protein stability regulation of protein localization regulation of protein catabolic process at postsynapse, modulating synaptic transmission
Sources:Amigo / QuickGO

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


9101


84092


ENSG00000138592


ENSMUSG00000027363


P40818


Q80U87

RefSeq (mRNA)


NM_001128610 NM_001128611 NM_001283049 NM_005154


NM_001252580 NM_019729

RefSeq (protein)


NP_001122082 NP_001269978 NP_005145


NP_001239509 NP_062703

Location (UCSC)

Chr 15: 50.42 – 50.51 Mb

Chr 2: 126.55 – 126.6 Mb

PubMed search

View/Edit Human

View/Edit Mouse

Ubiquitin carboxyl-terminal hydrolase 8 is an enzyme that in humans is encoded by the USP8 gene.

Interactions

USP8 has been shown to interact with RNF41 and STAM2.

Diseases

In a few cases of Morbus Cushing's disease, a mutation of USP8 has been found.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000138592 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027363 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Puente XS, Sánchez LM, Overall CM, López-Otín C (July 2003). "Human and mouse proteases: a comparative genomic approach". Nature Reviews. Genetics. 4 (7): 544–58. doi:10.1038/nrg1111. PMID 12838346. S2CID 2856065.
↑ Janssen JW, Schleithoff L, Bartram CR, Schulz AS (April 1998). "An oncogenic fusion product of the phosphatidylinositol 3-kinase p85beta subunit and HUMORF8, a putative deubiquitinating enzyme". Oncogene. 16 (13): 1767–72. doi:10.1038/sj.onc.1201695. PMID 9582025.
↑ "Entrez Gene: USP8 ubiquitin specific peptidase 8".
↑ Wu X, Yen L, Irwin L, Sweeney C, Carraway KL (September 2004). "Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8". Molecular and Cellular Biology. 24 (17): 7748–57. doi:10.1128/MCB.24.17.7748-7757.2004. PMC 506982. PMID 15314180.
↑ Kaneko T, Kumasaka T, Ganbe T, Sato T, Miyazawa K, Kitamura N, Tanaka N (November 2003). "Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain". The Journal of Biological Chemistry. 278 (48): 48162–8. doi:10.1074/jbc.M306677200. PMID 13129930.
↑ Kato M, Miyazawa K, Kitamura N (December 2000). "A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP". The Journal of Biological Chemistry. 275 (48): 37481–7. doi:10.1074/jbc.M007251200. PMID 10982817.

Further reading

D'Andrea A, Pellman D (1999). "Deubiquitinating enzymes: a new class of biological regulators". Critical Reviews in Biochemistry and Molecular Biology. 33 (5): 337–52. doi:10.1080/10409239891204251. PMID 9827704.
Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, et al. (1995). "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research. 1 (5): 223–9. doi:10.1093/dnares/1.5.223. PMID 7584044.
Naviglio S, Mattecucci C, Matoskova B, Nagase T, Nomura N, Di Fiore PP, Draetta GF (June 1998). "UBPY: a growth-regulated human ubiquitin isopeptidase". The EMBO Journal. 17 (12): 3241–50. doi:10.1093/emboj/17.12.3241. PMC 1170662. PMID 9628861.
Kato M, Miyazawa K, Kitamura N (December 2000). "A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP". The Journal of Biological Chemistry. 275 (48): 37481–7. doi:10.1074/jbc.M007251200. PMID 10982817.
Gnesutta N, Ceriani M, Innocenti M, Mauri I, Zippel R, Sturani E, et al. (October 2001). "Cloning and characterization of mouse UBPy, a deubiquitinating enzyme that interacts with the ras guanine nucleotide exchange factor CDC25(Mm)/Ras-GRF1". The Journal of Biological Chemistry. 276 (42): 39448–54. doi:10.1074/jbc.M103454200. hdl:2434/28853. PMID 11500497.
Kaneko T, Kumasaka T, Ganbe T, Sato T, Miyazawa K, Kitamura N, Tanaka N (November 2003). "Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain". The Journal of Biological Chemistry. 278 (48): 48162–8. doi:10.1074/jbc.M306677200. PMID 13129930.
Soares L, Seroogy C, Skrenta H, Anandasabapathy N, Lovelace P, Chung CD, et al. (January 2004). "Two isoforms of otubain 1 regulate T cell anergy via GRAIL". Nature Immunology. 5 (1): 45–54. doi:10.1038/ni1017. PMID 14661020. S2CID 27005972.
Wu X, Yen L, Irwin L, Sweeney C, Carraway KL (September 2004). "Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8". Molecular and Cellular Biology. 24 (17): 7748–57. doi:10.1128/MCB.24.17.7748-7757.2004. PMC 506982. PMID 15314180.
Berruti G, Martegani E (January 2005). "The deubiquitinating enzyme mUBPy interacts with the sperm-specific molecular chaperone MSJ-1: the relation with the proteasome, acrosome, and centrosome in mouse male germ cells". Biology of Reproduction. 72 (1): 14–21. doi:10.1095/biolreprod.104.030866. PMID 15342353.
Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (June 2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Molecular & Cellular Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
Row PE, Prior IA, McCullough J, Clague MJ, Urbé S (May 2006). "The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation". The Journal of Biological Chemistry. 281 (18): 12618–24. doi:10.1074/jbc.M512615200. PMID 16520378.
Mizuno E, Kobayashi K, Yamamoto A, Kitamura N, Komada M (August 2006). "A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes". Traffic. 7 (8): 1017–31. doi:10.1111/j.1600-0854.2006.00452.x. PMID 16771824.
Avvakumov GV, Walker JR, Xue S, Finerty PJ, Mackenzie F, Newman EM, Dhe-Paganon S (December 2006). "Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)". The Journal of Biological Chemistry. 281 (49): 38061–70. doi:10.1074/jbc.M606704200. PMID 17035239.

v t e PDB gallery
1whb: Solution structure of the Rhodanese-like domain in human ubiquitin specific protease 8 (UBP8) 2a9u: Structure of the N-terminal domain of Human Ubiquitin carboxyl-terminal hydrolase 8 (USP8) 2gfo: Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-terminal Hydrolase 8 2gwf: Structure of a USP8-NRDP1 complex

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