Hmdb loader

Showing Protein Ubiquitin carboxyl-terminal hydrolase 5 (HMDBP10125)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP10125
Secondary Accession Numbers
  • 16081
Name Ubiquitin carboxyl-terminal hydrolase 5
Synonyms
  1. Deubiquitinating enzyme 5
  2. Isopeptidase T
  3. Ubiquitin thiolesterase 5
  4. Ubiquitin-specific-processing protease 5
Gene Name USP5
Protein Type Enzyme
Biological Properties
General Function Involved in ubiquitin thiolesterase activity
Specific Function Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys- 63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of TP53/p53 and an increase in TP53/p53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated TP53/p53 but not with MDM2 for proteasomal recognition
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. Cytoplasmic
Gene Properties
Chromosome Location Chromosome:1
Locus 12p13
SNPs USP5
Gene Sequence 
>2577 bp
ATGGCGGAGCTGAGTGAGGAGGCGCTGCTGTCAGTATTACCGACGATCCGGGTCCCTAAG
GCTGGAGACCGGGTCCACAAAGACGAGTGCGCCTTCTCCTTCGACACGCCGGAGTCTGAG
GGGGGCCTCTACATCTGTATGAACACGTTTCTGGGCTTTGGGAAACAGTATGTGGAGAGA
CATTTCAATAAGACCGGCCAGCGAGTCTACTTGCACCTCCGGCGGACCCGGCGCCCGAAA
GAGGAGGACCCTGCTACAGGCACTGGAGACCCACCCCGGAAGAAGCCCACGCGGCTGGCT
ATTGGTGTTGAAGGCGGATTTGACCTTAGCGAGGAGAAGTTTGAATTAGACGAGGATGTG
AAGATTGTCATTTTGCCAGATTACCTGGAGATTGCCCGGGATGGACTGGGGGGACTGCCT
GACATTGTCAGAGATCGGGTGACCAGTGCAGTGGAGGCCCTACTGTCGGCCGACTCAGCC
TCCCGCAAGCAGGAGGTGCAGGCATGGGATGGGGAAGTACGGCAGGTGTCTAAGCATGCC
TTCAGCCTCAAGCAGTTGGACAACCCTGCTCGAATCCCTCCCTGTGGCTGGAAGTGCTCC
AAGTGTGACATGAGAGAGAACCTGTGGCTCAACCTGACTGATGGCTCCATCCTCTGTGGG
CGACGCTACTTCGATGGCAGTGGGGGCAACAACCACGCTGTGGAGCACTACCGAGAGACA
GGCTACCCGTTAGCTGTCAAGCTGGGCACCATCACCCCTGATGGAGCTGACGTGTACTCA
TATGATGAGGATGACATGGTCCTGGACCCCAGCCTGGCTGAGCACCTGTCCCACTTCGGC
ATCGACATGCTGAAGATGCAGAAGACAGACAAGACGATGACTGAGTTGGAGATAGACATG
AACCAGCGGATTGGTGAATGGGAGCTGATCCAGGAGTCAGGTGTGCCACTCAAGCCCCTG
TTTGGGCCTGGCTACACAGGCATCCGGAACCTGGGTAACAGCTGCTACCTCAACTCTGTG
GTCCAGGTGCTCTTCAGCATCCCTGACTTCCAGAGGAAGTATGTGGATAAGCTGGAGAAG
ATCTTCCAGAATGCCCCGACGGACCCTACCCAGGATTTCAGCACCCAGGTGGCCAAGCTG
GGCCATGGCCTTCTCTCCGGGGAGTATTCCAAGCCAGTACCGGAGTCGGGCGATGGGGAG
CGGGTGCCAGAACAGAAGGAAGTTCAAGATGGCATTGCCCCTCGGATGTTCAAGGCCCTC
ATCGGCAAGGGCCACCCTGAATTCTCCACCAACCGGCAGCAGGATGCCCAGGAGTTCTTC
CTTCACCTTATCAACATGGTGGAGAGGAATTGCCGGAGCTCTGAAAATCCTAATGAAGTG
TTCCGCTTCTTGGTGGAGGAAAAGATCAAGTGCCTGGCCACAGAGAAGGTGAAGTACACC
CAGCGAGTTGACTACATCATGCAGCTGCCTGTGCCCATGGATGCAGCCCTTAACAAAGAG
GAGCTTCTGGAGTACGAGGAGAAGAAGCGGCAAGCCGAAGAGGAGAAGATGGCACTGCCA
GAACTGGTTCGGGCCCAGGTGCCCTTCAGCTCTTGCCTGGAGGCCTACGGGGCCCCTGAG
CAGGTCGATGACTTCTGGAGCACGGCCCTGCAGGCCAAGTCAGTAGCTGTCAAGACCACA
CGATTTGCCTCATTCCCTGACTACCTGGTCATCCAGATCAAGAAGTTCACCTTCGGCTTA
GACTGGGTGCCCAAGAAACTGGATGTGTCCATCGAGATGCCAGAGGAGCTCGACATCTCC
CAGTTGAGGGGCACAGGGCTGCAGCCCGGAGAGGAGGAGCTGCCAGACATTGCCCCACCC
CTGGTCACTCCGGATGAGCCCAAAGGTAGCCTTGGTTTCTATGGCAACGAAGACGAAGAC
TCCTTCTGCTCCCCTCACTTCTCCTCTCCGACATCGCCCATGCTGGATGAATCAGTCATC
ATCCAGCTGGTGGAGATGGGATTCCCTATGGACGCCTGCCGCAAAGCTGTCTACTACACG
GGCAACAGCGGGGCTGAGGCCGCCATGAACTGGGTCATGTCACACATGGATGATCCAGAT
TTTGCAAACCCCCTCATCCTGCCTGGCTCTAGTGGGCCGGGCTCCACAAGCGCAGCAGCC
GACCCCCCTCCTGAGGACTGTGTGACCACCATTGTCTCCATGGGCTTCTCCCGGGACCAG
GCCTTGAAAGCGCTGCGGGCCACGAACAATAGTTTAGAACGGGCTGTGGACTGGATCTTC
AGTCACATTGACGACCTGGATGCTGAAGCTGCCATGGACATCTCAGAGGGCCGCTCAGCT
GCCGACTCCATCTCTGAGTCTGTGCCAGTGGGACCTAAAGTCCGGGATGGTCCTGGAAAG
TATCAGCTCTTTGCCTTCATTAGTCACATGGGCACCTCTACCATGTGTGGTCACTACGTC
TGCCACATCAAGAAAGAAGGCAGATGGGTGATCTACAATGACCAGAAAGTGTGTGCCTCC
GAGAAGCCGCCCAAGGACCTGGGCTACATCTACTTCTACCAGAGAGTGGCCAGCTAA
Protein Properties
Number of Residues 858
Molecular Weight 95785.4
Theoretical pI 4.65
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Ubiquitin carboxyl-terminal hydrolase 5
MAELSEEALLSVLPTIRVPKAGDRVHKDECAFSFDTPESEGGLYICMNTFLGFGKQYVER
HFNKTGQRVYLHLRRTRRPKEEDPATGTGDPPRKKPTRLAIGVEGGFDLSEEKFELDEDV
KIVILPDYLEIARDGLGGLPDIVRDRVTSAVEALLSADSASRKQEVQAWDGEVRQVSKHA
FSLKQLDNPARIPPCGWKCSKCDMRENLWLNLTDGSILCGRRYFDGSGGNNHAVEHYRET
GYPLAVKLGTITPDGADVYSYDEDDMVLDPSLAEHLSHFGIDMLKMQKTDKTMTELEIDM
NQRIGEWELIQESGVPLKPLFGPGYTGIRNLGNSCYLNSVVQVLFSIPDFQRKYVDKLEK
IFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPESGDGERVPEQKEVQDGIAPRMFKAL
IGKGHPEFSTNRQQDAQEFFLHLINMVERNCRSSENPNEVFRFLVEEKIKCLATEKVKYT
QRVDYIMQLPVPMDAALNKEELLEYEEKKRQAEEEKMALPELVRAQVPFSSCLEAYGAPE
QVDDFWSTALQAKSVAVKTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELDIS
QLRGTGLQPGEEELPDIAPPLVTPDEPKGSLGFYGNEDEDSFCSPHFSSPTSPMLDESVI
IQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFANPLILPGSSGPGSTSAAA
DPPPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDDLDAEAAMDISEGRSA
ADSISESVPVGPKVRDGPGKYQLFAFISHMGTSTMCGHYVCHIKKEGRWVIYNDQKVCAS
EKPPKDLGYIYFYQRVAS
GenBank ID Protein 148727331
UniProtKB/Swiss-Prot ID P45974
UniProtKB/Swiss-Prot Entry Name UBP5_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_001098536.1
GeneCard ID USP5
GenAtlas ID USP5
HGNC ID HGNC:12628
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. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  5. 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 ]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  7. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed:9074930 ]
  8. Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. Genome Res. 1996 Apr;6(4):314-26. [PubMed:8723724 ]
  9. Falquet L, Paquet N, Frutiger S, Hughes GJ, Hoang-Van K, Jaton JC: cDNA cloning of a human 100 kDa de-ubiquitinating enzyme: the 100 kDa human de-ubiquitinase belongs to the ubiquitin C-terminal hydrolase family 2 (UCH2). FEBS Lett. 1995 Dec 4;376(3):233-7. [PubMed:7498549 ]
  10. Falquet L, Paquet N, Frutiger S, Hughes GJ, Hoang-Van K, Jaton JC: A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro. FEBS Lett. 1995 Feb 6;359(1):73-7. [PubMed:7851534 ]
  11. Reyes-Turcu FE, Shanks JR, Komander D, Wilkinson KD: Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T. J Biol Chem. 2008 Jul 11;283(28):19581-92. doi: 10.1074/jbc.M800947200. Epub 2008 May 15. [PubMed:18482987 ]
  12. Dayal S, Sparks A, Jacob J, Allende-Vega N, Lane DP, Saville MK: Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53. J Biol Chem. 2009 Feb 20;284(8):5030-41. doi: 10.1074/jbc.M805871200. Epub 2008 Dec 19. [PubMed:19098288 ]
  13. Reyes-Turcu FE, Horton JR, Mullally JE, Heroux A, Cheng X, Wilkinson KD: The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin. Cell. 2006 Mar 24;124(6):1197-208. [PubMed:16564012 ]