UBP16_HUMAN
ID UBP16_HUMAN Reviewed; 823 AA.
AC Q9Y5T5; A8MU43; B3KN13; B4DFV8; B4DY37; D3DSD9; Q53GP7; Q53HA0; Q5VKN8;
AC Q8NEL3; Q9H3E6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 16 {ECO:0000255|HAMAP-Rule:MF_03062};
DE EC=3.4.19.12 {ECO:0000255|HAMAP-Rule:MF_03062};
DE AltName: Full=Deubiquitinating enzyme 16 {ECO:0000255|HAMAP-Rule:MF_03062};
DE AltName: Full=Ubiquitin thioesterase 16 {ECO:0000255|HAMAP-Rule:MF_03062};
DE AltName: Full=Ubiquitin-processing protease UBP-M;
DE AltName: Full=Ubiquitin-specific-processing protease 16 {ECO:0000255|HAMAP-Rule:MF_03062};
GN Name=USP16 {ECO:0000255|HAMAP-Rule:MF_03062}; ORFNames=MSTP039;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP PHOSPHORYLATION, AND MUTAGENESIS OF CYS-205.
RX PubMed=10077596; DOI=10.1073/pnas.96.6.2828;
RA Cai S.-Y., Babbitt R.W., Marchesi V.T.;
RT "A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic
RT chromosomes and blocks cell division.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2828-2833(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Grimbert P., Pawlak A., Sahali D.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP HIS-141.
RC TISSUE=Amygdala, Teratocarcinoma, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT HIS-141.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-823.
RC TISSUE=Aorta;
RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y.,
RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y.,
RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PRELIMINARY FUNCTION, AND MUTAGENESIS OF CYS-205.
RX PubMed=11753566; DOI=10.1038/sj.cdd.4400924;
RA Mimnaugh E.G., Kayastha G., McGovern N.B., Hwang S.G., Marcu M.G.,
RA Trepel J., Cai S.-Y., Marchesi V.T., Neckers L.;
RT "Caspase-dependent deubiquitination of monoubiquitinated nucleosomal
RT histone H2A induced by diverse apoptogenic stimuli.";
RL Cell Death Differ. 8:1182-1196(2001).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-205.
RX PubMed=17914355; DOI=10.1038/nature06256;
RA Joo H.-Y., Zhai L., Yang C., Nie S., Erdjument-Bromage H., Tempst P.,
RA Chang C., Wang H.;
RT "Regulation of cell cycle progression and gene expression by H2A
RT deubiquitination.";
RL Nature 449:1068-1072(2007).
RN [11]
RP CHROMOSOMAL REARRANGEMENT.
RX PubMed=18925961; DOI=10.1186/1471-2407-8-299;
RA Gelsi-Boyer V., Trouplin V., Adelaide J., Aceto N., Remy V., Pinson S.,
RA Houdayer C., Arnoulet C., Sainty D., Bentires-Alj M., Olschwang S., Vey N.,
RA Mozziconacci M.-J., Birnbaum D., Chaffanet M.;
RT "Genome profiling of chronic myelomonocytic leukemia: frequent alterations
RT of RAS and RUNX1 genes.";
RL BMC Cancer 8:299-299(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415 AND SER-552, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND THR-554, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-415 AND SER-552, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP POSSIBLE INVOLVEMENT IN DOWN SYNDROME.
RX PubMed=24025767; DOI=10.1038/nature12530;
RA Adorno M., Sikandar S., Mitra S.S., Kuo A., Nicolis Di Robilant B.,
RA Haro-Acosta V., Ouadah Y., Quarta M., Rodriguez J., Qian D., Reddy V.M.,
RA Cheshier S., Garner C.C., Clarke M.F.;
RT "Usp16 contributes to somatic stem-cell defects in Down's syndrome.";
RL Nature 501:380-384(2013).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-140, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP STRUCTURE BY NMR OF 22-143, ZINC-BINDING, AND DOMAIN.
RX PubMed=17512543; DOI=10.1016/j.jmb.2007.04.015;
RA Pai M.-T., Tzeng S.-R., Kovacs J.J., Keaton M.A., Li S.S.-C., Yao T.-P.,
RA Zhou P.;
RT "Solution structure of the Ubp-M BUZ domain, a highly specific protein
RT module that recognizes the C-terminal tail of free ubiquitin.";
RL J. Mol. Biol. 370:290-302(2007).
CC -!- FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A
CC (H2AK119Ub), a specific tag for epigenetic transcriptional repression,
CC thereby acting as a coactivator. Deubiquitination of histone H2A is a
CC prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3
CC (H3S10ph), and is required for chromosome segregation when cells enter
CC into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB
CC leads to enhance its activity, thereby maintaining transcription in
CC resting lymphocytes. Regulates Hox gene expression via histone H2A
CC deubiquitination. Prefers nucleosomal substrates. Does not
CC deubiquitinate histone H2B. {ECO:0000255|HAMAP-Rule:MF_03062,
CC ECO:0000269|PubMed:10077596, ECO:0000269|PubMed:17914355}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03062,
CC ECO:0000269|PubMed:17914355};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03062,
CC ECO:0000269|PubMed:17914355}.
CC -!- INTERACTION:
CC Q9Y5T5-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-16813369, EBI-1055254;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17914355}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9Y5T5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5T5-2; Sequence=VSP_036715;
CC Name=3;
CC IsoId=Q9Y5T5-3; Sequence=VSP_036714, VSP_036715;
CC Name=4;
CC IsoId=Q9Y5T5-4; Sequence=VSP_036713;
CC Name=5;
CC IsoId=Q9Y5T5-5; Sequence=VSP_036716;
CC -!- TISSUE SPECIFICITY: Present in all the tissues examined including fetal
CC brain, lung, liver, kidney, and adult heart, brain, placenta, lung,
CC liver, skeletal muscle, kidney and pancreas.
CC {ECO:0000269|PubMed:10077596}.
CC -!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions that form a pair of
CC cross-braced ring fingers encapsulated within a third zinc finger in
CC the primary structure. It recognizes the C-terminal tail of free
CC ubiquitin. {ECO:0000269|PubMed:17512543}.
CC -!- PTM: Phosphorylated at the onset of mitosis and dephosphorylated during
CC the metaphase/anaphase transition. Phosphorylation by AURKB enhances
CC the deubiquitinase activity. {ECO:0000255|HAMAP-Rule:MF_03062,
CC ECO:0000269|PubMed:10077596}.
CC -!- DISEASE: Note=A chromosomal aberration involving USP16 is a cause of
CC Chronic myelomonocytic leukemia. Inversion inv(21) (q21;q22) with
CC RUNX1/AML1.
CC -!- MISCELLANEOUS: USP16 may contribute to somatic stem cell defects
CC observed in Down syndrome. USP16 is triplicated in Down syndrome and
CC its overexpression may contribute to proliferation defects in stem
CC cells. Reduction of USP16 levels results in increased proliferation
CC capacity of Down syndrome fibroblasts (PubMed:24025767).
CC {ECO:0000305|PubMed:24025767}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP16 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03062}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG39290.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG51175.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF126736; AAD20949.1; -; mRNA.
DR EMBL; AY333928; AAR13293.1; -; mRNA.
DR EMBL; AK023247; BAG51175.1; ALT_INIT; mRNA.
DR EMBL; AK302247; BAG63599.1; -; mRNA.
DR EMBL; AK294284; BAG57569.1; -; mRNA.
DR EMBL; AK222681; BAD96401.1; -; mRNA.
DR EMBL; AK222884; BAD96604.1; -; mRNA.
DR EMBL; AL163249; CAB90432.1; -; Genomic_DNA.
DR EMBL; AF129075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09927.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09929.1; -; Genomic_DNA.
DR EMBL; BC030777; AAH30777.1; -; mRNA.
DR EMBL; AF113219; AAG39290.1; ALT_INIT; mRNA.
DR CCDS; CCDS13583.1; -. [Q9Y5T5-1]
DR CCDS; CCDS42912.1; -. [Q9Y5T5-2]
DR RefSeq; NP_001001992.1; NM_001001992.1. [Q9Y5T5-2]
DR RefSeq; NP_001027582.1; NM_001032410.1. [Q9Y5T5-1]
DR RefSeq; NP_006438.1; NM_006447.2. [Q9Y5T5-1]
DR RefSeq; XP_016883746.1; XM_017028257.1. [Q9Y5T5-1]
DR RefSeq; XP_016883747.1; XM_017028258.1. [Q9Y5T5-2]
DR RefSeq; XP_016883748.1; XM_017028259.1. [Q9Y5T5-2]
DR RefSeq; XP_016883749.1; XM_017028260.1. [Q9Y5T5-4]
DR RefSeq; XP_016883750.1; XM_017028261.1. [Q9Y5T5-4]
DR PDB; 2I50; NMR; -; A=22-143.
DR PDBsum; 2I50; -.
DR AlphaFoldDB; Q9Y5T5; -.
DR BMRB; Q9Y5T5; -.
DR SMR; Q9Y5T5; -.
DR BioGRID; 115848; 55.
DR DIP; DIP-53761N; -.
DR IntAct; Q9Y5T5; 13.
DR STRING; 9606.ENSP00000334808; -.
DR BindingDB; Q9Y5T5; -.
DR ChEMBL; CHEMBL4630865; -.
DR MEROPS; C19.021; -.
DR iPTMnet; Q9Y5T5; -.
DR PhosphoSitePlus; Q9Y5T5; -.
DR BioMuta; USP16; -.
DR DMDM; 6686071; -.
DR EPD; Q9Y5T5; -.
DR jPOST; Q9Y5T5; -.
DR MassIVE; Q9Y5T5; -.
DR MaxQB; Q9Y5T5; -.
DR PaxDb; Q9Y5T5; -.
DR PeptideAtlas; Q9Y5T5; -.
DR PRIDE; Q9Y5T5; -.
DR ProteomicsDB; 86497; -. [Q9Y5T5-1]
DR ProteomicsDB; 86498; -. [Q9Y5T5-2]
DR ProteomicsDB; 86499; -. [Q9Y5T5-3]
DR ProteomicsDB; 86500; -. [Q9Y5T5-4]
DR ProteomicsDB; 86501; -. [Q9Y5T5-5]
DR Antibodypedia; 6359; 360 antibodies from 34 providers.
DR DNASU; 10600; -.
DR Ensembl; ENST00000334352.8; ENSP00000334808.4; ENSG00000156256.15. [Q9Y5T5-1]
DR Ensembl; ENST00000399975.7; ENSP00000382857.3; ENSG00000156256.15. [Q9Y5T5-2]
DR Ensembl; ENST00000399976.7; ENSP00000382858.2; ENSG00000156256.15. [Q9Y5T5-1]
DR GeneID; 10600; -.
DR KEGG; hsa:10600; -.
DR MANE-Select; ENST00000399976.7; ENSP00000382858.2; NM_006447.3; NP_006438.1.
DR UCSC; uc002ymw.4; human. [Q9Y5T5-1]
DR CTD; 10600; -.
DR DisGeNET; 10600; -.
DR GeneCards; USP16; -.
DR HGNC; HGNC:12614; USP16.
DR HPA; ENSG00000156256; Low tissue specificity.
DR MIM; 604735; gene.
DR neXtProt; NX_Q9Y5T5; -.
DR OpenTargets; ENSG00000156256; -.
DR PharmGKB; PA37240; -.
DR VEuPathDB; HostDB:ENSG00000156256; -.
DR eggNOG; KOG1873; Eukaryota.
DR GeneTree; ENSGT00940000156013; -.
DR HOGENOM; CLU_007938_1_0_1; -.
DR InParanoid; Q9Y5T5; -.
DR OMA; DGMRTEE; -.
DR OrthoDB; 278083at2759; -.
DR PhylomeDB; Q9Y5T5; -.
DR TreeFam; TF326075; -.
DR PathwayCommons; Q9Y5T5; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q9Y5T5; -.
DR SIGNOR; Q9Y5T5; -.
DR BioGRID-ORCS; 10600; 15 hits in 1128 CRISPR screens.
DR ChiTaRS; USP16; human.
DR EvolutionaryTrace; Q9Y5T5; -.
DR GeneWiki; USP16; -.
DR GenomeRNAi; 10600; -.
DR Pharos; Q9Y5T5; Tbio.
DR PRO; PR:Q9Y5T5; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9Y5T5; protein.
DR Bgee; ENSG00000156256; Expressed in oocyte and 207 other tissues.
DR ExpressionAtlas; Q9Y5T5; baseline and differential.
DR Genevisible; Q9Y5T5; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
DR GO; GO:0070537; P:histone H2A K63-linked deubiquitination; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0140014; P:mitotic nuclear division; IEA:UniProtKB-UniRule.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0045901; P:positive regulation of translational elongation; IMP:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR HAMAP; MF_03062; UBP16; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR030849; UBP16.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cell cycle; Cell division;
KW Chromatin regulator; Chromosomal rearrangement; Hydrolase; Isopeptide bond;
KW Metal-binding; Mitosis; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Transcription;
KW Transcription regulation; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..823
FT /note="Ubiquitin carboxyl-terminal hydrolase 16"
FT /id="PRO_0000080643"
FT DOMAIN 196..822
FT /note="USP"
FT ZN_FING 22..142
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 146..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Nucleophile"
FT ACT_SITE 758
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03062"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99LG0"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 554
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..310
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036713"
FT VAR_SEQ 1..20
FT /note="MGKKRTKGKTVPIDDSSETL -> MGSVAV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036714"
FT VAR_SEQ 150
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036715"
FT VAR_SEQ 394..823
FT /note="SGKKSVNDKNLKKTVEDEDQDSEEEKDNDSYIKERSDIPSGTSKHLQKKAKK
FT QAKKQAKNQRRQQKIQGKVLHLNDICTIDHPEDSEYEAEMSLQGEVNIKSNHISQEGVM
FT HKEYCVNQKDLNGQAKMIESVTDNQKSTEEVDMKNINMDNDLEVLTSSPTRNLNGAYLT
FT EGSNGEVDISNGFKNLNLNAALHPDEINIEILNDSHTPGTKVYEVVNEDPETAFCTLAN
FT REVFNTDECSIQHCLYQFTRNEKLRDANKLLCEVCTRRQCNGPKANIKGERKHVYTNAK
FT KQMLISLAPPVLTLHLKRFQQAGFNLRKVNKHIKFPEILDLAPFCTLKCKNVAEENTRV
FT LYSLYGVVEHSGTMRSGHYTAYAKARTANSHLSNLVLHGDIPQDFEMESKGQWFHISDT
FT HVQAVPTTKVLNSQAYLLFYERIL -> VRLLNLFYSSRFFFL (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_036716"
FT VARIANT 141
FT /note="Q -> H (in dbSNP:rs2274802)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_020388"
FT MUTAGEN 205
FT /note="C->S: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10077596,
FT ECO:0000269|PubMed:11753566, ECO:0000269|PubMed:17914355"
FT CONFLICT 141
FT /note="Q -> E (in Ref. 8; AAG39290)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="Q -> R (in Ref. 3; BAG51175)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="K -> E (in Ref. 4; BAD96604)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="S -> P (in Ref. 4; BAD96401)"
FT /evidence="ECO:0000305"
FT CONFLICT 480..481
FT /note="EY -> DN (in Ref. 7; AAH30777)"
FT /evidence="ECO:0000305"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:2I50"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:2I50"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2I50"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2I50"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2I50"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2I50"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2I50"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2I50"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2I50"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:2I50"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:2I50"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2I50"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2I50"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:2I50"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:2I50"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:2I50"
SQ SEQUENCE 823 AA; 93570 MW; C7D4175649BA3E31 CRC64;
MGKKRTKGKT VPIDDSSETL EPVCRHIRKG LEQGNLKKAL VNVEWNICQD CKTDNKVKDK
AEEETEEKPS VWLCLKCGHQ GCGRNSQEQH ALKHYLTPRS EPHCLVLSLD NWSVWCYVCD
NEVQYCSSNQ LGQVVDYVRK QASITTPKPA EKDNGNIELE NKKLEKESKN EQEREKKENM
AKENPPMNSP CQITVKGLSN LGNTCFFNAV MQNLSQTPVL RELLKEVKMS GTIVKIEPPD
LALTEPLEIN LEPPGPLTLA MSQFLNEMQE TKKGVVTPKE LFSQVCKKAV RFKGYQQQDS
QELLRYLLDG MRAEEHQRVS KGILKAFGNS TEKLDEELKN KVKDYEKKKS MPSFVDRIFG
GELTSMIMCD QCRTVSLVHE SFLDLSLPVL DDQSGKKSVN DKNLKKTVED EDQDSEEEKD
NDSYIKERSD IPSGTSKHLQ KKAKKQAKKQ AKNQRRQQKI QGKVLHLNDI CTIDHPEDSE
YEAEMSLQGE VNIKSNHISQ EGVMHKEYCV NQKDLNGQAK MIESVTDNQK STEEVDMKNI
NMDNDLEVLT SSPTRNLNGA YLTEGSNGEV DISNGFKNLN LNAALHPDEI NIEILNDSHT
PGTKVYEVVN EDPETAFCTL ANREVFNTDE CSIQHCLYQF TRNEKLRDAN KLLCEVCTRR
QCNGPKANIK GERKHVYTNA KKQMLISLAP PVLTLHLKRF QQAGFNLRKV NKHIKFPEIL
DLAPFCTLKC KNVAEENTRV LYSLYGVVEH SGTMRSGHYT AYAKARTANS HLSNLVLHGD
IPQDFEMESK GQWFHISDTH VQAVPTTKVL NSQAYLLFYE RIL
