Hmdb loader
Identification
HMDB Protein ID HMDBP10138
Secondary Accession Numbers
  • 16094
Name Ubiquitin carboxyl-terminal hydrolase 3
Synonyms
  1. Deubiquitinating enzyme 3
  2. Ubiquitin thiolesterase 3
  3. Ubiquitin-specific-processing protease 3
Gene Name USP3
Protein Type Enzyme
Biological Properties
General Function Involved in ubiquitin thiolesterase activity
Specific Function Hydrolase that deubiquitinates monoubiquitinated target proteins such as histone H2A and H2B. Required for proper progression through S phase and subsequent mitotic entry. May regulate the DNA damage response (DDR) checkpoint through deubiquitination of H2A at DNA damage sites. Associates with the chromatin
Pathways Not Available
Reactions Not Available
GO Classification
Function
ion binding
cation binding
metal ion binding
hydrolase activity, acting on ester bonds
binding
catalytic activity
hydrolase activity
transition metal ion binding
zinc ion binding
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. Nucleus
Gene Properties
Chromosome Location Chromosome:1
Locus 15q22.3
SNPs USP3
Gene Sequence
>1563 bp
ATGGAGTGTCCACACCTGAGCTCCAGCGTCTGCATTGCTCCGGACTCAGCCAAGTTCCCC
AACGGCTCCCCGTCGTCCTGGTGCTGCAGCGTGTGCCGGTCCAACAAAAGCCCTTGGGTC
TGTTTGACTTGTTCAAGTGTCCACTGTGGAAGGTATGTGAATGGCCATGCAAAAAAACAT
TATGAAGATGCACAAGTACCTTTAACCAACCATAAGAAATCAGAAAAGCAAGATAAAGTT
CAGCACACAGTATGTATGGATTGCAGTAGCTACAGTACATACTGTTATCGCTGTGATGAT
TTTGTGGTTAATGACACCAAGCTGGGACTGGTACAGAAAGTCAGAGAACACTTACAGAAC
TTGGAAAACTCAGCTTTCACAGCTGACAGGCATAAGAAAAGAAAACTTTTGGAAAACTCA
ACACTAAACAGCAAGTTATTAAAAGTAAATGGAAGCACCACTGCCATTTGTGCCACAGGC
CTTCGGAATTTGGGGAACACATGTTTCATGAATGCCATCCTTCAGTCACTCAGTAACATT
GAGCAGTTTTGCTGTTATTTCAAAGAACTGCCCGCCGTGGAGTTAAGGAATGGGAAAACA
GCAGGAAGGCGGACATACCACACCAGGAGCCAAGGGGATAACAATGTGTCTTTGGTAGAA
GAGTTTAGAAAGACACTCTGTGCTTTATGGCAAGGCAGCCAGACTGCATTTAGCCCAGAG
TCCTTATTTTATGTTGTTTGGAAGATTATGCCAAACTTTAGGGGCTATCAACAGCAGGAC
GCCCATGAATTCATGCGCTACCTTTTGGACCACCTACACTTGGAACTTCAGGGCGGTTTC
AACGGTGTTTCCCGCTCAGCAATTCTGCAGGAGAATTCTACTCTGTCTGCAAGTAACAAG
TGTTGCATAAATGGAGCATCTACTGTTGTCACGGCTATATTCGGAGGCATTCTCCAAAAT
GAGGTTAACTGCCTCATATGTGGGACAGAATCTAGAAAGTTTGATCCATTCCTAGACCTT
TCATTAGATATTCCAAGTCAGTTCAGAAGTAAGCGCTCTAAGAATCAAGAAAATGGACCA
GTTTGTTCGTTACGAGATTGTCTTCGCAGTTTTACCGACTTAGAAGAACTTGATGAGACA
GAGTTATATATGTGCCATAAATGCAAAAAGAAACAAAAGTCCACAAAAAAGTTTTGGATT
CAAAAACTACCCAAGGTGCTATGCTTACATTTGAAAAGATTTCATTGGACAGCATATTTA
AGAAATAAAGTTGATACATACGTAGAATTTCCACTGAGAGGCCTAGACATGAAATGCTAC
TTACTAGAGCCTGAGAACAGTGGCCCGGAGAGCTGCCTGTATGACCTCGCCGCTGTGGTG
GTGCACCATGGTTCCGGGGTTGGTTCTGGACATTACACAGCATACGCAACTCACGAAGGC
CGCTGGTTCCACTTCAATGACAGTACTGTAACACTGACTGACGAGGAGACTGTGGTGAAG
GCGAAGGCCTACATCCTTTTCTACGTGGAACACCAGGCCAAAGCTGGATCGGATAAACTT
TAA
Protein Properties
Number of Residues 520
Molecular Weight 58896.6
Theoretical pI 8.23
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Ubiquitin carboxyl-terminal hydrolase 3
MECPHLSSSVCIAPDSAKFPNGSPSSWCCSVCRSNKSPWVCLTCSSVHCGRYVNGHAKKH
YEDAQVPLTNHKKSEKQDKVQHTVCMDCSSYSTYCYRCDDFVVNDTKLGLVQKVREHLQN
LENSAFTADRHKKRKLLENSTLNSKLLKVNGSTTAICATGLRNLGNTCFMNAILQSLSNI
EQFCCYFKELPAVELRNGKTAGRRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSPE
SLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILQENSTLSASNK
CCINGASTVVTAIFGGILQNEVNCLICGTESRKFDPFLDLSLDIPSQFRSKRSKNQENGP
VCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFHWTAYL
RNKVDTYVEFPLRGLDMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAYATHEG
RWFHFNDSTVTLTDEETVVKAKAYILFYVEHQAKAGSDKL
GenBank ID Protein 55770886
UniProtKB/Swiss-Prot ID Q9Y6I4
UniProtKB/Swiss-Prot Entry Name UBP3_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_006537.2
GeneCard ID USP3
GenAtlas ID USP3
HGNC ID HGNC:12626
References
General References
  1. 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 ]
  2. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed:16572171 ]
  5. Sloper-Mould KE, Eyre HJ, Wang XW, Sutherland GR, Baker RT: Characterization and chromosomal localization of USP3, a novel human ubiquitin-specific protease. J Biol Chem. 1999 Sep 17;274(38):26878-84. [PubMed:10480896 ]
  6. Nicassio F, Corrado N, Vissers JH, Areces LB, Bergink S, Marteijn JA, Geverts B, Houtsmuller AB, Vermeulen W, Di Fiore PP, Citterio E: Human USP3 is a chromatin modifier required for S phase progression and genome stability. Curr Biol. 2007 Nov 20;17(22):1972-7. Epub 2007 Nov 1. [PubMed:17980597 ]