You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
| Identification |
|---|
| HMDB Protein ID
| HMDBP10137 |
| Secondary Accession Numbers
| |
| Name
| Ubiquitin carboxyl-terminal hydrolase 15 |
| Synonyms
|
- Deubiquitinating enzyme 15
- Ubiquitin thiolesterase 15
- Ubiquitin-specific-processing protease 15
- Unph-2
- Unph4
|
| Gene Name
| USP15 |
| Protein Type
| Enzyme |
| Biological Properties |
|---|
| General Function
| Involved in ubiquitin thiolesterase activity |
| Specific Function
| Protease that degrades 'Lys-48'-linked polyubiquitin chains. Protects target proteins against proteasomal degradation. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway |
| 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
|
- Cytoplasmic
|
| Gene Properties |
|---|
| Chromosome Location
| Chromosome:1 |
| Locus
| 12q14 |
| SNPs
| USP15 |
| Gene Sequence
|
>2946 bp
ATGGCGGAAGGCGGAGCGGCGGATCTGGACACCCAGCGGTCTGACATCGCGACGCTGCTC
AAAACCTCGCTCCGGAAAGGGGACACCTGGTACCTAGTCGATAGTCGCTGGTTCAAACAG
TGGAAAAAATATGTTGGCTTTGACAGTTGGGACAAATACCAGATGGGAGATCAAAATGTG
TATCCTGGACCCATTGATAACTCTGGACTTCTCAAAGATGGTGATGCCCAGTCACTTAAG
GAACACCTTATTGATGAATTGGATTACATACTGTTGCCAACTGAAGGTTGGAATAAACTT
GTCAGCTGGTACACATTGATGGAAGGTCAAGAGCCAATAGCACGAAAGGTGGTTGAACAG
GGTATGTTTGTAAAGCACTGCAAAGTAGAAGTATATCTCACAGAATTGAAGCTATGTGAA
AATGGAAACATGAATAATGTTGTAACTCGAAGATTTAGCAAAGCTGACACAATAGATACA
ATTGAAAAGGAAATAAGAAAAATCTTCAGTATTCCAGATGAAAAGGAGACCAGATTGTGG
AACAAATACATGAGTAACACATTTGAACCACTGAATAAACCAGACAGCACCATTCAGGAT
GCTGGTTTATACCAAGGACAGGTATTAGTGATAGAACAGAAAAATGAAGATGGAACATGG
CCAAGGGGTCCTTCTACTCCTAAGTCCCCAGGTGCATCCAATTTTTCAACTTTACCAAAG
ATCTCTCCTTCATCTCTATCAAATAATTATAACAACATGAACAACAGAAATGTGAAAAAC
TCAAATTACTGTCTTCCATCATATACCGCTTATAAGAACTATGATTATTCGGAACCTGGA
AGAAACAATGAACAGCCAGGCCTCTGTGGCCTAAGTAACTTGGGAAATACGTGTTTCATG
AACTCAGCTATTCAGTGTTTGAGCAACACACCTCCACTTACTGAGTATTTCCTCAATGAT
AAGTATCAAGAAGAACTGAATTTTGACAATCCCTTAGGAATGAGAGGTGAAATAGCTAAA
TCTTATGCCGAACTGATCAAGCAAATGTGGTCTGGAAAGTTTAGCTACGTCACCCCAAGA
GCCTTTAAGACACAGGTAGGACGTTTTGCACCTCAGTTCTCTGGATATCAGCAGCAAGAC
TGTCAAGAACTGTTAGCTTTCCTATTAGATGGATTACATGAGGATTTGAATAGAATTAGG
AAAAAACCATATATACAATTAAAAGATGCAGATGGAAGGCCAGATAAGGTGGTTGCCGAA
GAAGCCTGGGAAAACCATTTAAAACGAAATGATTCTATCATAGTAGATATATTTCATGGC
CTTTTCAAATCAACTTTAGTTTGTCCTGAGTGTGCTAAGATTTCAGTAACATTTGATCCT
TTTTGTTACTTGACACTTCCATTGCCCATGAAAAAAGAACGCACCTTGGAAGTTTACTTA
GTTAGAATGGATCCGCTTACCAAACCTATGCAGTACAAAGTGGTTGTCCCCAAAATTGGA
AACATATTAGATCTTTGTACAGCATTGTCTGCTTTGTCAGGAATACCTGCAGATAAGATG
ATAGTTACTGATATATACAATCATAGATTTCACAGAATATTCGCTATGGATGAAAACCTT
AGTAGTATTATGGAACGGGATGATATTTATGTGTTTGAAATTAACATCAATAGGACAGAA
GATACAGAGCACGTGATTATTCCTGTTTGCCTAAGAGAAAAATTCAGACACTCGAGTTAT
ACCCACCATACTGGTTCTTCACTTTTTGGTCAGCCCTTTCTTATGGCTGTACCACGAAAC
AATACTGAAGACAAACTTTATAATCTCCTGCTCTTGAGAATGTGCCGATATGTCAAAATA
TCTACTGAAACTGAAGAAACTGAAGGATCCCTACACTGCTGTAAGGACCAAAATATTAAT
GGGAATGGCCCAAATGGCATACATGAAGAAGGCTCACCAAGTGAAATGGAAACAGATGAG
CCAGATGATGAATCCAGCCAGGATCAAGAACTTCCCTCAGAGAATGAAAACAGTCAGTCT
GAAGATTCAGTTGGAGGAGATAATGATTCTGAAAATGGATTATGTACTGAGGATACTTGC
AAAGGTCAACTCACGGGACACAAAAAACGATTGTTTACATTCCAGTTCAACAACTTAGGC
AATACTGATATCAACTACATCAAAGATGATACCAGGCATATAAGATTTGATGATAGGCAG
CTTAGGCTAGATGAAAGATCTTTTCTTGCTTTGGATTGGGATCCTGATTTGAAAAAAAGA
TATTTTGATGAAAATGCTGCTGAGGACTTTGAAAAACATGAAAGTGTGGAGTATAAACCT
CCTAAAAAACCCTTTGTGAAATTAAAAGATTGCATTGAACTTTTTACAACAAAAGAAAAG
CTAGGTGCTGAAGATCCCTGGTATTGTCCGAATTGTAAAGAACATCAGCAAGCCACAAAG
AAATTGGATTTATGGTCCCTGCCTCCAGTACTTGTAGTACATCTCAAGCGATTTTCTTAC
AGTCGATACATGAGAGACAAGTTGGATACCTTAGTTGATTTTCCTATCAATGACTTGGAT
ATGTCGGAATTCTTAATTAATCCAAATGCAGGTCCTTGCCGCTATAATCTGATTGCTGTT
TCCAACCACTATGGAGGGATGGGAGGAGGACACTATACTGCTTTTGCAAAAAATAAAGAT
GATGGAAAATGGTACTATTTTGATGACAGTAGTGTCTCCACTGCATCTGAAGACCAAATT
GTGTCCAAAGCAGCATATGTACTCTTCTACCAGAGACAAGACACTTTCAGTGGAACTGGC
TTTTTTCCTCTTGACCGAGAAACTAAAGGTGCTTCAGCTGCCACTGGCATCCCATTAGAA
AGTGATGAAGATAGCAATGATAATGACAATGATATAGAAAATGAAAACTGTATGCACACT
AACTAA
|
| Protein Properties |
|---|
| Number of Residues
| 981 |
| Molecular Weight
| 112418.1 |
| Theoretical pI
| 4.84 |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
|
| Protein Sequence
|
>Ubiquitin carboxyl-terminal hydrolase 15
MAEGGAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKQWKKYVGFDSWDKYQMGDQNV
YPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYTLMEGQEPIARKVVEQ
GMFVKHCKVEVYLTELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFSIPDEKETRLW
NKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQKNEDGTWPRGPSTPKSPGASNFSTLPK
ISPSSLSNNYNNMNNRNVKNSNYCLPSYTAYKNYDYSEPGRNNEQPGLCGLSNLGNTCFM
NSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPR
AFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQLKDADGRPDKVVAE
EAWENHLKRNDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERTLEVYL
VRMDPLTKPMQYKVVVPKIGNILDLCTALSALSGIPADKMIVTDIYNHRFHRIFAMDENL
SSIMERDDIYVFEININRTEDTEHVIIPVCLREKFRHSSYTHHTGSSLFGQPFLMAVPRN
NTEDKLYNLLLLRMCRYVKISTETEETEGSLHCCKDQNINGNGPNGIHEEGSPSEMETDE
PDDESSQDQELPSENENSQSEDSVGGDNDSENGLCTEDTCKGQLTGHKKRLFTFQFNNLG
NTDINYIKDDTRHIRFDDRQLRLDERSFLALDWDPDLKKRYFDENAAEDFEKHESVEYKP
PKKPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSY
SRYMRDKLDTLVDFPINDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKD
DGKWYYFDDSSVSTASEDQIVSKAAYVLFYQRQDTFSGTGFFPLDRETKGASAATGIPLE
SDEDSNDNDNDIENENCMHTN
|
| External Links |
|---|
| GenBank ID Protein
| 5231133 |
| UniProtKB/Swiss-Prot ID
| Q9Y4E8 |
| UniProtKB/Swiss-Prot Entry Name
| UBP15_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| AF153604 |
| GeneCard ID
| USP15 |
| GenAtlas ID
| USP15 |
| HGNC ID
| HGNC:12613 |
| References |
|---|
| General References
| - Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
- 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 ]
- 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 ]
- 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 ]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed:12168954 ]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed:9628581 ]
- Baker RT, Wang XW, Woollatt E, White JA, Sutherland GR: Identification, functional characterization, and chromosomal localization of USP15, a novel human ubiquitin-specific protease related to the UNP oncoprotein, and a systematic nomenclature for human ubiquitin-specific proteases. Genomics. 1999 Aug 1;59(3):264-74. [PubMed:10444327 ]
- Angelats C, Wang XW, Jermiin LS, Copeland NG, Jenkins NA, Baker RT: Isolation and characterization of the mouse ubiquitin-specific protease Usp15. Mamm Genome. 2003 Jan;14(1):31-46. [PubMed:12532266 ]
- Hetfeld BK, Helfrich A, Kapelari B, Scheel H, Hofmann K, Guterman A, Glickman M, Schade R, Kloetzel PM, Dubiel W: The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1. Curr Biol. 2005 Jul 12;15(13):1217-21. [PubMed:16005295 ]
- Huang X, Langelotz C, Hetfeld-Pechoc BK, Schwenk W, Dubiel W: The COP9 signalosome mediates beta-catenin degradation by deneddylation and blocks adenomatous polyposis coli destruction via USP15. J Mol Biol. 2009 Aug 28;391(4):691-702. doi: 10.1016/j.jmb.2009.06.066. Epub 2009 Jul 1. [PubMed:19576224 ]
- Vos RM, Altreuter J, White EA, Howley PM: The ubiquitin-specific peptidase USP15 regulates human papillomavirus type 16 E6 protein stability. J Virol. 2009 Sep;83(17):8885-92. doi: 10.1128/JVI.00605-09. Epub 2009 Jun 24. [PubMed:19553310 ]
- de Jong RN, Ab E, Diercks T, Truffault V, Daniels M, Kaptein R, Folkers GE: Solution structure of the human ubiquitin-specific protease 15 DUSP domain. J Biol Chem. 2006 Feb 24;281(8):5026-31. Epub 2005 Nov 18. [PubMed:16298993 ]
|
