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Ubiquitin carboxyl-terminal hydrolase 16 (EC 3.4.19.12) (Deubiquitinating enzyme 16) (Ubiquitin thioesterase 16) (Ubiquitin-processing protease UBP-M) (Ubiquitin-specific-processing protease 16)

 UBP16_HUMAN             Reviewed;         823 AA.
Q9Y5T5; A8MU43; B3KN13; B4DFV8; B4DY37; D3DSD9; Q53GP7; Q53HA0;
Q5VKN8; Q8NEL3; Q9H3E6;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 163.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 16 {ECO:0000255|HAMAP-Rule:MF_03062};
EC=3.4.19.12 {ECO:0000255|HAMAP-Rule:MF_03062};
AltName: Full=Deubiquitinating enzyme 16 {ECO:0000255|HAMAP-Rule:MF_03062};
AltName: Full=Ubiquitin thioesterase 16 {ECO:0000255|HAMAP-Rule:MF_03062};
AltName: Full=Ubiquitin-processing protease UBP-M;
AltName: Full=Ubiquitin-specific-processing protease 16 {ECO:0000255|HAMAP-Rule:MF_03062};
Name=USP16 {ECO:0000255|HAMAP-Rule:MF_03062}; ORFNames=MSTP039;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
PHOSPHORYLATION, AND MUTAGENESIS OF CYS-205.
PubMed=10077596; DOI=10.1073/pnas.96.6.2828;
Cai S.-Y., Babbitt R.W., Marchesi V.T.;
"A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic
chromosomes and blocks cell division.";
Proc. Natl. Acad. Sci. U.S.A. 96:2828-2833(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Grimbert P., Pawlak A., Sahali D.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
HIS-141.
TISSUE=Amygdala, Teratocarcinoma, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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 T.-O., 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. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., 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., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
HIS-141.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-823.
TISSUE=Aorta;
Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S.,
Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J.,
Cao H.Q., Zhao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q.,
Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[9]
PRELIMINARY FUNCTION, AND MUTAGENESIS OF CYS-205.
PubMed=11753566; DOI=10.1038/sj.cdd.4400924;
Mimnaugh E.G., Kayastha G., McGovern N.B., Hwang S.G., Marcu M.G.,
Trepel J., Cai S.-Y., Marchesi V.T., Neckers L.;
"Caspase-dependent deubiquitination of monoubiquitinated nucleosomal
histone H2A induced by diverse apoptogenic stimuli.";
Cell Death Differ. 8:1182-1196(2001).
[10]
FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY,
SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-205.
PubMed=17914355; DOI=10.1038/nature06256;
Joo H.-Y., 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 449:1068-1072(2007).
[11]
CHROMOSOMAL REARRANGEMENT.
PubMed=18925961; DOI=10.1186/1471-2407-8-299;
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 M.-J., Birnbaum D., Chaffanet M.;
"Genome profiling of chronic myelomonocytic leukemia: frequent
alterations of RAS and RUNX1 genes.";
BMC Cancer 8:299-299(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415 AND SER-552, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND THR-554, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-415 AND
SER-552, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
POSSIBLE INVOLVEMENT IN DOWN SYNDROME.
PubMed=24025767; DOI=10.1038/nature12530;
Adorno M., Sikandar S., Mitra S.S., Kuo A., Nicolis Di Robilant B.,
Haro-Acosta V., Ouadah Y., Quarta M., Rodriguez J., Qian D.,
Reddy V.M., Cheshier S., Garner C.C., Clarke M.F.;
"Usp16 contributes to somatic stem-cell defects in Down's syndrome.";
Nature 501:380-384(2013).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-140, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[21]
STRUCTURE BY NMR OF 22-143, ZINC-BINDING, AND DOMAIN.
PubMed=17512543; DOI=10.1016/j.jmb.2007.04.015;
Pai M.-T., Tzeng S.-R., Kovacs J.J., Keaton M.A., Li S.S.-C.,
Yao T.-P., 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. 370:290-302(2007).
-!- FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A
(H2AK119Ub), a specific tag for epigenetic transcriptional
repression, thereby acting as a coactivator. Deubiquitination of
histone H2A is a prerequisite for subsequent phosphorylation at
'Ser-11' of histone H3 (H3S10ph), and is required for chromosome
segregation when cells enter into mitosis. In resting B- and T-
lymphocytes, phosphorylation by AURKB leads to enhance its
activity, thereby maintaining transcription in resting
lymphocytes. Regulates Hox gene expression via histone H2A
deubiquitination. Prefers nucleosomal substrates. Does not
deubiquitinate histone H2B. {ECO:0000255|HAMAP-Rule:MF_03062,
ECO:0000269|PubMed:10077596, ECO:0000269|PubMed:17914355}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
{ECO:0000255|HAMAP-Rule:MF_03062, ECO:0000269|PubMed:17914355}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03062,
ECO:0000269|PubMed:17914355}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17914355}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q9Y5T5-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y5T5-2; Sequence=VSP_036715;
Name=3;
IsoId=Q9Y5T5-3; Sequence=VSP_036714, VSP_036715;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9Y5T5-4; Sequence=VSP_036713;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9Y5T5-5; Sequence=VSP_036716;
-!- TISSUE SPECIFICITY: Present in all the tissues examined including
fetal brain, lung, liver, kidney, and adult heart, brain,
placenta, lung, liver, skeletal muscle, kidney and pancreas.
{ECO:0000269|PubMed:10077596}.
-!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions that form a
pair of cross-braced ring fingers encapsulated within a third zinc
finger in the primary structure. It recognizes the C-terminal tail
of free ubiquitin. {ECO:0000269|PubMed:17512543}.
-!- PTM: Phosphorylated at the onset of mitosis and dephosphorylated
during the metaphase/anaphase transition. Phosphorylation by AURKB
enhances the deubiquitinase activity. {ECO:0000255|HAMAP-
Rule:MF_03062, ECO:0000269|PubMed:10077596}.
-!- DISEASE: Note=A chromosomal aberration involving USP16 is a cause
of Chronic myelomonocytic leukemia. Inversion inv(21) (q21;q22)
with RUNX1/AML1.
-!- MISCELLANEOUS: USP16 may contribute to somatic stem cell defects
observed in Down syndrome. USP16 is triplicated in Down syndrome
and its overexpression may contribute to proliferation defects in
stem cells. Reduction of USP16 levels results in increased
proliferation capacity of Down syndrome fibroblasts
(PubMed:24025767). {ECO:0000305|PubMed:24025767}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP16 subfamily.
{ECO:0000255|HAMAP-Rule:MF_03062}.
-!- SEQUENCE CAUTION:
Sequence=AAG39290.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAG51175.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF126736; AAD20949.1; -; mRNA.
EMBL; AY333928; AAR13293.1; -; mRNA.
EMBL; AK023247; BAG51175.1; ALT_INIT; mRNA.
EMBL; AK302247; BAG63599.1; -; mRNA.
EMBL; AK294284; BAG57569.1; -; mRNA.
EMBL; AK222681; BAD96401.1; -; mRNA.
EMBL; AK222884; BAD96604.1; -; mRNA.
EMBL; AL163249; CAB90432.1; -; Genomic_DNA.
EMBL; AF129075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09927.1; -; Genomic_DNA.
EMBL; CH471079; EAX09929.1; -; Genomic_DNA.
EMBL; BC030777; AAH30777.1; -; mRNA.
EMBL; AF113219; AAG39290.1; ALT_INIT; mRNA.
CCDS; CCDS13583.1; -. [Q9Y5T5-1]
CCDS; CCDS42912.1; -. [Q9Y5T5-2]
RefSeq; NP_001001992.1; NM_001001992.1. [Q9Y5T5-2]
RefSeq; NP_001027582.1; NM_001032410.1. [Q9Y5T5-1]
RefSeq; NP_006438.1; NM_006447.2. [Q9Y5T5-1]
RefSeq; XP_016883746.1; XM_017028257.1. [Q9Y5T5-1]
RefSeq; XP_016883747.1; XM_017028258.1. [Q9Y5T5-2]
RefSeq; XP_016883748.1; XM_017028259.1. [Q9Y5T5-2]
RefSeq; XP_016883749.1; XM_017028260.1. [Q9Y5T5-4]
RefSeq; XP_016883750.1; XM_017028261.1. [Q9Y5T5-4]
UniGene; Hs.99819; -.
PDB; 2I50; NMR; -; A=22-143.
PDBsum; 2I50; -.
ProteinModelPortal; Q9Y5T5; -.
SMR; Q9Y5T5; -.
BioGrid; 115848; 31.
DIP; DIP-53761N; -.
IntAct; Q9Y5T5; 5.
STRING; 9606.ENSP00000334808; -.
MEROPS; C19.021; -.
iPTMnet; Q9Y5T5; -.
PhosphoSitePlus; Q9Y5T5; -.
BioMuta; USP16; -.
DMDM; 6686071; -.
EPD; Q9Y5T5; -.
PaxDb; Q9Y5T5; -.
PeptideAtlas; Q9Y5T5; -.
PRIDE; Q9Y5T5; -.
DNASU; 10600; -.
Ensembl; ENST00000334352; ENSP00000334808; ENSG00000156256. [Q9Y5T5-1]
Ensembl; ENST00000399975; ENSP00000382857; ENSG00000156256. [Q9Y5T5-2]
Ensembl; ENST00000399976; ENSP00000382858; ENSG00000156256. [Q9Y5T5-1]
GeneID; 10600; -.
KEGG; hsa:10600; -.
UCSC; uc002ymw.4; human. [Q9Y5T5-1]
CTD; 10600; -.
DisGeNET; 10600; -.
EuPathDB; HostDB:ENSG00000156256.14; -.
GeneCards; USP16; -.
H-InvDB; HIX0023011; -.
HGNC; HGNC:12614; USP16.
HPA; HPA021140; -.
MIM; 604735; gene.
neXtProt; NX_Q9Y5T5; -.
OpenTargets; ENSG00000156256; -.
PharmGKB; PA37240; -.
eggNOG; KOG1873; Eukaryota.
eggNOG; COG5560; LUCA.
GeneTree; ENSGT00860000133682; -.
HOVERGEN; HBG062704; -.
InParanoid; Q9Y5T5; -.
KO; K11844; -.
OMA; FHISDTS; -.
OrthoDB; EOG091G01WT; -.
PhylomeDB; Q9Y5T5; -.
TreeFam; TF326075; -.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SIGNOR; Q9Y5T5; -.
ChiTaRS; USP16; human.
EvolutionaryTrace; Q9Y5T5; -.
GeneWiki; USP16; -.
GenomeRNAi; 10600; -.
PRO; PR:Q9Y5T5; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000156256; -.
CleanEx; HS_USP16; -.
ExpressionAtlas; Q9Y5T5; baseline and differential.
Genevisible; Q9Y5T5; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; TAS:ProtInc.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
GO; GO:0070537; P:histone H2A K63-linked deubiquitination; IMP:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0045901; P:positive regulation of translational elongation; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.30.40.10; -; 1.
HAMAP; MF_03062; UBP16; 1.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR030849; UBP16.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR001607; Znf_UBP.
Pfam; PF00443; UCH; 1.
Pfam; PF02148; zf-UBP; 1.
SMART; SM00290; ZnF_UBP; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
PROSITE; PS50271; ZF_UBP; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Cell cycle;
Cell division; Chromatin regulator; Chromosomal rearrangement;
Complete proteome; Hydrolase; Isopeptide bond; Metal-binding; Mitosis;
Nucleus; Phosphoprotein; Polymorphism; Protease; Reference proteome;
Thiol protease; Transcription; Transcription regulation;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 823 Ubiquitin carboxyl-terminal hydrolase 16.
/FTId=PRO_0000080643.
DOMAIN 196 822 USP.
ZN_FING 60 125 UBP-type. {ECO:0000255|HAMAP-
Rule:MF_03062}.
ACT_SITE 205 205 Nucleophile.
ACT_SITE 758 758 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03062}.
METAL 24 24 Zinc 1.
METAL 26 26 Zinc 1.
METAL 48 48 Zinc 2.
METAL 51 51 Zinc 2.
METAL 74 74 Zinc 3.
METAL 77 77 Zinc 3.
METAL 82 82 Zinc 2.
METAL 90 90 Zinc 2.
METAL 94 94 Zinc 3.
METAL 103 103 Zinc 3.
METAL 116 116 Zinc 1.
METAL 119 119 Zinc 1.
MOD_RES 189 189 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 531 531 Phosphoserine.
{ECO:0000250|UniProtKB:Q99LG0}.
MOD_RES 552 552 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 554 554 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
CROSSLNK 140 140 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 310 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036713.
VAR_SEQ 1 20 MGKKRTKGKTVPIDDSSETL -> MGSVAV (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036714.
VAR_SEQ 150 150 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_036715.
VAR_SEQ 394 823 SGKKSVNDKNLKKTVEDEDQDSEEEKDNDSYIKERSDIPSG
TSKHLQKKAKKQAKKQAKNQRRQQKIQGKVLHLNDICTIDH
PEDSEYEAEMSLQGEVNIKSNHISQEGVMHKEYCVNQKDLN
GQAKMIESVTDNQKSTEEVDMKNINMDNDLEVLTSSPTRNL
NGAYLTEGSNGEVDISNGFKNLNLNAALHPDEINIEILNDS
HTPGTKVYEVVNEDPETAFCTLANREVFNTDECSIQHCLYQ
FTRNEKLRDANKLLCEVCTRRQCNGPKANIKGERKHVYTNA
KKQMLISLAPPVLTLHLKRFQQAGFNLRKVNKHIKFPEILD
LAPFCTLKCKNVAEENTRVLYSLYGVVEHSGTMRSGHYTAY
AKARTANSHLSNLVLHGDIPQDFEMESKGQWFHISDTHVQA
VPTTKVLNSQAYLLFYERIL -> VRLLNLFYSSRFFFL
(in isoform 5). {ECO:0000303|Ref.2}.
/FTId=VSP_036716.
VARIANT 141 141 Q -> H (in dbSNP:rs2274802).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_020388.
MUTAGEN 205 205 C->S: Loss of enzyme activity.
{ECO:0000269|PubMed:10077596,
ECO:0000269|PubMed:11753566,
ECO:0000269|PubMed:17914355}.
CONFLICT 141 141 Q -> E (in Ref. 8; AAG39290).
{ECO:0000305}.
CONFLICT 297 297 Q -> R (in Ref. 3; BAG51175).
{ECO:0000305}.
CONFLICT 348 348 K -> E (in Ref. 4; BAD96604).
{ECO:0000305}.
CONFLICT 350 350 S -> P (in Ref. 4; BAD96401).
{ECO:0000305}.
CONFLICT 480 481 EY -> DN (in Ref. 7; AAH30777).
{ECO:0000305}.
HELIX 27 30 {ECO:0000244|PDB:2I50}.
HELIX 33 40 {ECO:0000244|PDB:2I50}.
STRAND 45 47 {ECO:0000244|PDB:2I50}.
HELIX 49 52 {ECO:0000244|PDB:2I50}.
TURN 63 65 {ECO:0000244|PDB:2I50}.
STRAND 71 74 {ECO:0000244|PDB:2I50}.
TURN 75 77 {ECO:0000244|PDB:2I50}.
STRAND 80 82 {ECO:0000244|PDB:2I50}.
STRAND 86 88 {ECO:0000244|PDB:2I50}.
HELIX 90 96 {ECO:0000244|PDB:2I50}.
STRAND 105 108 {ECO:0000244|PDB:2I50}.
TURN 109 111 {ECO:0000244|PDB:2I50}.
STRAND 114 116 {ECO:0000244|PDB:2I50}.
TURN 117 120 {ECO:0000244|PDB:2I50}.
STRAND 121 123 {ECO:0000244|PDB:2I50}.
HELIX 130 142 {ECO:0000244|PDB:2I50}.
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


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