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Identification
HMDB Protein ID HMDBP10110
Secondary Accession Numbers
  • 16062
Name Ubiquitin carboxyl-terminal hydrolase 16
Synonyms
  1. Deubiquitinating enzyme 16
  2. Ubiquitin thiolesterase 16
  3. Ubiquitin-processing protease UBP-M
  4. Ubiquitin-specific-processing protease 16
Gene Name USP16
Protein Type Enzyme
Biological Properties
General Function Involved in ubiquitin thiolesterase activity
Specific Function Specifically deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-10' of histone H3, and is required for chromosome segregation when cells enter into mitosis. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B
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 (Probable)
Gene Properties
Chromosome Location Chromosome:2
Locus 21q22.11
SNPs USP16
Gene Sequence
>2472 bp
ATGGGAAAGAAACGGACAAAGGGAAAAACTGTTCCAATCGATGATTCCTCTGAAACTTTA
GAACCTGTGTGCAGACACATTAGAAAAGGATTGGAACAAGGTAATTTGAAAAAGGCTTTA
GTGAATGTGGAATGGAATATCTGCCAAGACTGTAAGACTGACAATAAAGTGAAAGATAAA
GCTGAAGAAGAAACAGAAGAAAAGCCTTCAGTTTGGCTGTGTCTTAAATGTGGCCATCAG
GGCTGTGGCAGAAATTCTCAGGAGCAGCATGCCTTGAAGCACTATCTGACGCCAAGATCT
GAACCTCACTGTCTGGTTCTTAGTTTGGACAACTGGAGTGTATGGTGTTACGTATGTGAT
AATGAGGTCCAGTATTGTAGTTCAAACCAGTTGGGTCAAGTGGTTGATTATGTCAGAAAA
CAAGCCAGCATTACAACTCCAAAGCCAGCAGAGAAAGATAATGGAAATATTGAACTTGAA
AATAAAAAATTAGAAAAAGAGAGTAAGAATGAACAAGAGAGAGAAAAGAAGGAAAACATG
GCTAAAGAGAATCCTCCCATGAATTCTCCTTGCCAAATAACCGTGAAAGGACTCAGTAAT
TTGGGAAACACATGTTTCTTCAATGCAGTTATGCAGAACTTGTCACAAACACCAGTGCTT
AGAGAACTACTAAAAGAAGTGAAAATGTCTGGAACAATTGTAAAAATTGAACCACCTGAT
TTGGCATTAACAGAACCATTAGAAATAAACCTTGAGCCTCCAGGCCCTCTTACTTTAGCC
ATGAGCCAGTTTCTTAATGAGATGCAAGAGACCAAAAAGGGGGTTGTGACACCGAAAGAA
CTCTTTTCTCAGGTCTGTAAAAAAGCAGTGCGGTTTAAAGGCTATCAGCAGCAAGACAGC
CAGGAGCTGCTTCGCTACTTATTGGATGGGATGAGAGCAGAAGAACACCAAAGAGTGAGT
AAAGGAATACTTAAAGCATTTGGTAATTCTACTGAAAAGTTGGATGAAGAACTAAAAAAT
AAAGTTAAAGATTATGAGAAGAAAAAATCAATGCCAAGTTTTGTTGACCGCATCTTTGGT
GGTGAACTAACTAGTATGATCATGTGTGATCAATGCAGAACTGTCTCCTTGGTTCATGAA
TCTTTCCTTGATTTGTCCCTCCCAGTTTTAGATGATCAGAGTGGTAAGAAAAGTGTAAAT
GATAAAAATCTGAAAAAGACAGTGGAGGATGAAGATCAAGATAGTGAGGAAGAAAAAGAT
AACGACAGTTACATAAAAGAGAGAAGTGATATTCCTTCTGGAACAAGTAAGCACTTACAG
AAAAAAGCAAAGAAACAAGCCAAAAAGCAAGCCAAGAACCAACGAAGACAACAAAAAATT
CAAGGAAAAGTTCTTCATTTAAATGATATTTGTACTATTGACCATCCTGAAGACAGTGAA
TATGAAGCTGAAATGTCACTTCAAGGAGAAGTAAATATTAAATCCAACCATATTTCACAA
GAGGGTGTTATGCATAAAGAATATTGTGTCAACCAGAAAGATTTGAATGGCCAAGCAAAA
ATGATCGAAAGTGTAACTGACAATCAAAAATCCACAGAGGAAGTAGATATGAAAAATATC
AACATGGATAATGATCTGGAGGTTTTAACATCTTCTCCCACTAGGAATTTAAATGGTGCC
TACCTAACGGAAGGGAGCAATGGAGAAGTGGACATTTCCAATGGTTTCAAAAACCTAAAT
TTGAATGCTGCTCTTCATCCTGATGAAATAAATATAGAGATTCTGAATGATAGTCATACT
CCTGGAACAAAGGTGTATGAGGTTGTAAATGAAGATCCAGAAACTGCTTTCTGTACTCTT
GCAAACAGGGAAGTTTTCAATACTGATGAGTGTTCAATCCAACATTGTTTATATCAGTTC
ACCCGTAATGAGAAACTTCGAGATGCGAATAAACTGCTTTGTGAAGTATGCACACGGAGA
CAGTGTAATGGACCAAAGGCAAATATAAAAGGTGAAAGGAAGCATGTTTACACCAATGCC
AAAAAGCAGATGCTAATTTCTCTTGCTCCTCCTGTTCTTACTCTTCATTTAAAGAGATTT
CAGCAGGCTGGTTTTAACCTACGCAAAGTTAACAAACACATAAAGTTTCCGGAAATCTTA
GATTTGGCTCCTTTTTGCACCCTTAAATGTAAGAATGTTGCAGAAGAAAATACAAGGGTA
CTCTATTCCTTATATGGAGTTGTTGAACACAGTGGTACTATGAGGTCGGGGCATTACACT
GCCTATGCCAAGGCAAGAACCGCAAATAGTCATCTCTCTAATCTTGTTCTTCACGGTGAT
ATTCCACAAGATTTTGAAATGGAATCAAAAGGGCAGTGGTTTCACATCAGCGACACACAT
GTGCAAGCTGTGCCTACAACTAAAGTACTAAACTCACAAGCGTACCTCCTATTTTATGAG
AGAATACTGTAA
Protein Properties
Number of Residues 823
Molecular Weight 93569.6
Theoretical pI 6.93
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Ubiquitin carboxyl-terminal hydrolase 16
MGKKRTKGKTVPIDDSSETLEPVCRHIRKGLEQGNLKKALVNVEWNICQDCKTDNKVKDK
AEEETEEKPSVWLCLKCGHQGCGRNSQEQHALKHYLTPRSEPHCLVLSLDNWSVWCYVCD
NEVQYCSSNQLGQVVDYVRKQASITTPKPAEKDNGNIELENKKLEKESKNEQEREKKENM
AKENPPMNSPCQITVKGLSNLGNTCFFNAVMQNLSQTPVLRELLKEVKMSGTIVKIEPPD
LALTEPLEINLEPPGPLTLAMSQFLNEMQETKKGVVTPKELFSQVCKKAVRFKGYQQQDS
QELLRYLLDGMRAEEHQRVSKGILKAFGNSTEKLDEELKNKVKDYEKKKSMPSFVDRIFG
GELTSMIMCDQCRTVSLVHESFLDLSLPVLDDQSGKKSVNDKNLKKTVEDEDQDSEEEKD
NDSYIKERSDIPSGTSKHLQKKAKKQAKKQAKNQRRQQKIQGKVLHLNDICTIDHPEDSE
YEAEMSLQGEVNIKSNHISQEGVMHKEYCVNQKDLNGQAKMIESVTDNQKSTEEVDMKNI
NMDNDLEVLTSSPTRNLNGAYLTEGSNGEVDISNGFKNLNLNAALHPDEINIEILNDSHT
PGTKVYEVVNEDPETAFCTLANREVFNTDECSIQHCLYQFTRNEKLRDANKLLCEVCTRR
QCNGPKANIKGERKHVYTNAKKQMLISLAPPVLTLHLKRFQQAGFNLRKVNKHIKFPEIL
DLAPFCTLKCKNVAEENTRVLYSLYGVVEHSGTMRSGHYTAYAKARTANSHLSNLVLHGD
IPQDFEMESKGQWFHISDTHVQAVPTTKVLNSQAYLLFYERIL
GenBank ID Protein 75992941
UniProtKB/Swiss-Prot ID Q9Y5T5
UniProtKB/Swiss-Prot Entry Name UBP16_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_001032410.1
GeneCard ID USP16
GenAtlas ID USP16
HGNC ID HGNC:12614
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. 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 ]
  4. 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 ]
  5. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  6. 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 ]
  7. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed:10830953 ]
  8. Cai SY, Babbitt RW, Marchesi VT: A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):2828-33. [PubMed:10077596 ]
  9. Mimnaugh EG, Kayastha G, McGovern NB, Hwang SG, Marcu MG, Trepel J, Cai SY, Marchesi VT, Neckers L: Caspase-dependent deubiquitination of monoubiquitinated nucleosomal histone H2A induced by diverse apoptogenic stimuli. Cell Death Differ. 2001 Dec;8(12):1182-96. [PubMed:11753566 ]
  10. Joo HY, Zhai L, Yang C, Nie S, Erdjument-Bromage H, Tempst P, Chang C, Wang H: Regulation of cell cycle progression and gene expression by H2A deubiquitination. Nature. 2007 Oct 25;449(7165):1068-72. Epub 2007 Oct 3. [PubMed:17914355 ]
  11. Gelsi-Boyer V, Trouplin V, Adelaide J, Aceto N, Remy V, Pinson S, Houdayer C, Arnoulet C, Sainty D, Bentires-Alj M, Olschwang S, Vey N, Mozziconacci MJ, Birnbaum D, Chaffanet M: Genome profiling of chronic myelomonocytic leukemia: frequent alterations of RAS and RUNX1 genes. BMC Cancer. 2008 Oct 16;8:299. doi: 10.1186/1471-2407-8-299. [PubMed:18925961 ]
  12. Pai MT, Tzeng SR, Kovacs JJ, Keaton MA, Li SS, Yao TP, Zhou P: Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin. J Mol Biol. 2007 Jul 6;370(2):290-302. Epub 2007 Apr 12. [PubMed:17512543 ]