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Identification
HMDB Protein ID HMDBP11576
Secondary Accession Numbers
  • 21020
Name Ubiquitin carboxyl-terminal hydrolase 2
Synonyms
  1. 41 kDa ubiquitin-specific protease
  2. Deubiquitinating enzyme 2
  3. Ubiquitin thiolesterase 2
  4. Ubiquitin-specific-processing protease 2
Gene Name USP2
Protein Type Enzyme
Biological Properties
General Function Involved in ubiquitin thiolesterase activity
Specific Function Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells
Pathways Not Available
Reactions Not Available
GO Classification
Function
hydrolase activity, acting on ester bonds
catalytic activity
hydrolase activity
ubiquitin thiolesterase activity
thiolester hydrolase activity
Process
metabolic process
catabolic process
macromolecule catabolic process
cellular macromolecule catabolic process
modification-dependent macromolecule catabolic process
modification-dependent protein catabolic process
ubiquitin-dependent protein catabolic process
Cellular Location
  1. Isoform 4:Nucleus
Gene Properties
Chromosome Location Chromosome:1
Locus 11q23.3
SNPs USP2
Gene Sequence
>1818 bp
ATGTCCCAGCTCTCCTCCACCCTGAAGCGCTACACAGAATCGGCCCGCTACACAGATGCC
CACTATGCCAAGTCGGGCTATGGTGCCTACACCCCGTCCTCCTATGGGGCCAATCTGGCT
GCCTCCTTACTGGAGAAGGAGAAACTTGGTTTCAAGCCGGTCCCCACCAGCAGCTTCCTC
ACCCGTCCCCGTACCTATGGCCCCTCCTCCCTCCTGGACTATGACCGGGGCCGCCCCCTG
CTGAGACCCGACATCACTGGGGGTGGTAAGCGGGCAGAGAGCCAGACCCGGGGTACTGAG
CGGCCTTTAGGCAGTGGCCTCAGCGGGGGCAGCGGATTCCCTTATGGAGTGACCAACAAC
TGCCTCAGCTACCTGCCCATCAATGCCTATGACCAGGGGGTGACCCTAACCCAGAAGCTG
GACAGCCAATCAGACCTGGCCCGGGATTTCTCCAGCCTCCGGACCTCAGATAGCTACCGG
ATAGACCCCAGGAACCTGGGCCGCAGCCCCATGCTGGCCCGGACGCGCAAGGAGCTCTGC
ACCCTGCAGGGGCTCTACCAGACAGCCAGCTGCCCTGAATACCTGGTCGACTACCTGGAG
AACTATGGTCGCAAGGGCAGTGCATCTCAGGTGCCCTCCCAGGCCCCTCCCTCACGAGTC
CCTGAAATCATCAGCCCAACCTACCGACCCATTGGCCGCTACACGCTGTGGGAGACGGGA
AAGGGTCAGGCCCCTGGGCCCAGCCGCTCCAGCTCCCCGGGAAGAGACGGCATGAATTCT
AAGAGTGCCCAGGGTCTGGCTGGTCTTCGAAACCTTGGGAACACGTGCTTCATGAACTCA
ATTCTGCAGTGCCTGAGCAACACTCGGGAGTTGAGAGATTACTGCCTCCAGAGGCTCTAC
ATGCGGGACCTGCACCACGGCAGCAATGCACACACAGCCCTCGTGGAAGAGTTTGCAAAA
CTAATTCAGACCATATGGACTTCATCCCCCAATGATGTGGTGAGCCCATCTGAGTTCAAG
ACCCAGATCCAGAGATACGCACCGCGCTTTGTTGGCTATAATCAGCAGGATGCTCAGGAG
TTCCTTCGCTTTCTTCTGGATGGGCTCCATAACGAGGTGAACCGAGTGACACTGAGACCT
AAGTCCAACCCTGAGAACCTCGATCATCTTCCTGATGACGAGAAAGGCCGACAGATGTGG
AGAAAATATCTAGAACGGGAAGACAGTAGGATCGGGGATCTCTTTGTTGGGCAGCTAAAG
AGCTCGCTGACGTGTACAGATTGTGGTTACTGTTCTACGGTCTTCGACCCCTTCTGGGAC
CTCTCACTGCCCATTGCTAAGCGAGGTTATCCTGAGGTGACATTAATGGACTGCATGAGG
CTCTTCACCAAAGAGGATGTGCTTGATGGAGATGAAAAGCCAACATGCTGTCGCTGCCGA
GGCAGAAAACGGTGTATAAAGAAGTTCTCCATCCAGAGGTTCCCAAAGATCTTGGTGCTC
CATCTGAAGCGGTTCTCAGAATCCAGGATCCGAACCAGCAAGCTCACAACATTTGTGAAC
TTCCCCCTAAGAGACCTGGACTTAAGAGAATTTGCCTCAGAAAACACCAACCATGCTGTT
TACAACCTGTACGCTGTGTCCAATCACTCCGGAACCACCATGGGTGGCCACTATACAGCC
TACTGTCGCAGTCCAGGGACAGGAGAATGGCACACTTTCAACGACTCCAGCGTCACTCCC
ATGTCCTCCAGCCAAGTGCGCACCAGCGACGCCTACCTGCTCTTCTACGAACTGGCCAGC
CCGCCCTCCCGAATGTAG
Protein Properties
Number of Residues 605
Molecular Weight 68071.0
Theoretical pI 9.17
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Ubiquitin carboxyl-terminal hydrolase 2
MSQLSSTLKRYTESARYTDAHYAKSGYGAYTPSSYGANLAASLLEKEKLGFKPVPTSSFL
TRPRTYGPSSLLDYDRGRPLLRPDITGGGKRAESQTRGTERPLGSGLSGGSGFPYGVTNN
CLSYLPINAYDQGVTLTQKLDSQSDLARDFSSLRTSDSYRIDPRNLGRSPMLARTRKELC
TLQGLYQTASCPEYLVDYLENYGRKGSASQVPSQAPPSRVPEIISPTYRPIGRYTLWETG
KGQAPGPSRSSSPGRDGMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLY
MRDLHHGSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQE
FLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKGRQMWRKYLEREDSRIGDLFVGQLK
SSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCR
GRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAV
YNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELAS
PPSRM
GenBank ID Protein 188528692
UniProtKB/Swiss-Prot ID O75604
UniProtKB/Swiss-Prot Entry Name UBP2_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_004205.4
GeneCard ID USP2
GenAtlas ID USP2
HGNC ID HGNC:12618
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed:16554811 ]
  4. Shan J, Zhao W, Gu W: Suppression of cancer cell growth by promoting cyclin D1 degradation. Mol Cell. 2009 Nov 13;36(3):469-76. doi: 10.1016/j.molcel.2009.10.018. [PubMed:19917254 ]
  5. Stevenson LF, Sparks A, Allende-Vega N, Xirodimas DP, Lane DP, Saville MK: The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2. EMBO J. 2007 Feb 21;26(4):976-86. Epub 2007 Feb 8. [PubMed:17290220 ]
  6. Allende-Vega N, Sparks A, Lane DP, Saville MK: MdmX is a substrate for the deubiquitinating enzyme USP2a. Oncogene. 2010 Jan 21;29(3):432-41. doi: 10.1038/onc.2009.330. Epub 2009 Oct 19. [PubMed:19838211 ]
  7. Wang S, Wu H, Liu Y, Sun J, Zhao Z, Chen Q, Guo M, Ma D, Zhang Z: Expression of USP2-69 in mesangial cells in vivo and in vitro. Pathol Int. 2010 Mar;60(3):184-92. doi: 10.1111/j.1440-1827.2010.02496.x. [PubMed:20403044 ]
  8. Renatus M, Parrado SG, D'Arcy A, Eidhoff U, Gerhartz B, Hassiepen U, Pierrat B, Riedl R, Vinzenz D, Worpenberg S, Kroemer M: Structural basis of ubiquitin recognition by the deubiquitinating protease USP2. Structure. 2006 Aug;14(8):1293-302. [PubMed:16905103 ]