USP33

Protein-coding gene in the species Homo sapiens
USP33
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2UZG

Identifiers
AliasesUSP33, VDU1, ubiquitin specific peptidase 33
External IDsOMIM: 615146; MGI: 2159711; HomoloGene: 8996; GeneCards: USP33; OMA:USP33 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for USP33
Genomic location for USP33
Band1p31.1Start77,695,987 bp[1]
End77,759,852 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for USP33
Genomic location for USP33
Band3|3 H3Start152,052,115 bp[2]
End152,099,254 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • cerebellar vermis

  • Brodmann area 23

  • retinal pigment epithelium

  • pons

  • lateral nuclear group of thalamus

  • mucosa of paranasal sinus

  • parietal pleura

  • primary visual cortex

  • endothelial cell

  • middle temporal gyrus
Top expressed in
  • neural layer of retina

  • ventromedial nucleus

  • lobe of cerebellum

  • ventral tegmental area

  • mammillary body

  • dorsomedial hypothalamic nucleus

  • pontine nuclei

  • habenula

  • lateral hypothalamus

  • dorsal tegmental nucleus
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • cysteine-type peptidase activity
  • zinc ion binding
  • metal ion binding
  • peptidase activity
  • ubiquitin binding
  • protein binding
  • thiol-dependent deubiquitinase
  • cysteine-type endopeptidase activity
  • hydrolase activity
  • G protein-coupled receptor binding
Cellular component
  • cytoplasm
  • cell body
  • centrosome
  • Golgi apparatus
  • VCB complex
  • focal adhesion
  • nucleoplasm
  • microtubule organizing center
  • autophagosome
  • perinuclear region of cytoplasm
  • cytoskeleton
  • cytosol
Biological process
  • endocytosis
  • protein K48-linked deubiquitination
  • ubiquitin-dependent protein catabolic process
  • regulation of G protein-coupled receptor signaling pathway
  • centrosome duplication
  • cellular response to starvation
  • protein stabilization
  • negative regulation of protein binding
  • proteolysis
  • axon guidance
  • regulation of autophagy
  • protein K63-linked deubiquitination
  • positive regulation of protein binding
  • cell migration
  • protein deubiquitination
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23032

170822

Ensembl

ENSG00000077254

ENSMUSG00000025437

UniProt

Q8TEY7

Q8R5K2

RefSeq (mRNA)

NM_015017
NM_201624
NM_201626

NM_001076676
NM_001252486
NM_133247
NM_001355666

RefSeq (protein)
NP_055832
NP_963918
NP_963920
NP_001364359
NP_001364360

NP_001364361
NP_001364362
NP_001364363
NP_001364364
NP_001364365
NP_001364366
NP_001364367
NP_001364368

NP_001070144
NP_001239415
NP_573510
NP_001342595

Location (UCSC)Chr 1: 77.7 – 77.76 MbChr 3: 152.05 – 152.1 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ubiquitin carboxyl-terminal hydrolase 33 is an enzyme that in humans is encoded by the USP33 gene.[5][6]

Interactions

USP33 has been shown to interact with DIO2,[7] SELENBP1[8] and Von Hippel–Lindau tumor suppressor.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000077254 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025437 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Puente XS, Sánchez LM, Overall CM, López-Otín C (Jul 2003). "Human and mouse proteases: a comparative genomic approach". Nat Rev Genet. 4 (7): 544–558. doi:10.1038/nrg1111. PMID 12838346. S2CID 2856065.
  6. ^ "Entrez Gene: USP33 ubiquitin specific peptidase 33".
  7. ^ Curcio-Morelli C, Zavacki AM, Christofollete M, Gereben B, de Freitas BC, Harney JW, Li Z, Wu G, Bianco AC (Jul 2003). "Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation". J. Clin. Invest. 112 (2): 189–196. doi:10.1172/JCI18348. PMC 164294. PMID 12865408.
  8. ^ Jeong JY, Wang Y, Sytkowski AJ (Feb 2009). "Human selenium binding protein-1 (hSP56) interacts with VDU1 in a selenium-dependent manner". Biochem. Biophys. Res. Commun. 379 (2): 583–588. doi:10.1016/j.bbrc.2008.12.110. PMID 19118533.
  9. ^ Li Z, Na X, Wang D, Schoen SR, Messing EM, Wu G (Feb 2002). "Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein". J. Biol. Chem. 277 (7): 4656–4662. doi:10.1074/jbc.M108269200. PMID 11739384.

Further reading

  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (3): 197–205. doi:10.1093/dnares/6.3.197. PMID 10470851.
  • Li Z, Na X, Wang D, Schoen SR, Messing EM, Wu G (2002). "Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein". J. Biol. Chem. 277 (7): 4656–4662. doi:10.1074/jbc.M108269200. PMID 11739384.
  • Li Z, Wang D, Na X, Schoen SR, Messing EM, Wu G (2002). "Identification of a deubiquitinating enzyme subfamily as substrates of the von Hippel-Lindau tumor suppressor". Biochem. Biophys. Res. Commun. 294 (3): 700–709. doi:10.1016/S0006-291X(02)00534-X. PMID 12056827.
  • Curcio-Morelli C, Zavacki AM, Christofollete M, Gereben B, de Freitas BC, Harney JW, Li Z, Wu G, Bianco AC (2003). "Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation". J. Clin. Invest. 112 (2): 189–196. doi:10.1172/JCI18348. PMC 164294. PMID 12865408.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Allen MD, Bycroft M (2007). "The solution structure of the ZnF UBP domain of USP33/VDU1". Protein Sci. 16 (9): 2072–2075. doi:10.1110/ps.072967807. PMC 2206988. PMID 17766394.
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