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Q99LG0 (UBP16_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 16

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 16
Ubiquitin thioesterase 16
Ubiquitin-specific-processing protease 16
Gene names
Name:Usp16
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length825 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 (Ref.6). Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. Ref.6

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). HAMAP-Rule MF_03062

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_03062

Subcellular location

Nucleus By similarity HAMAP-Rule MF_03062.

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 By similarity. HAMAP-Rule MF_03062

Post-translational modification

Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. Phosphorylation by AURKB enhances the deubiquitinase activity. Ref.6

Miscellaneous

Usp16 acts as a regulator of stem cell self-renewal and its overexpression contributes to somatic stem cell defects observed in Down syndrome models in mouse. Usp16 is triplicated in Ts65D Down syndrome mouse model and its overexpression leads to reduce the self-renewal of haematopoietic stem cells and the expansion of mammary epithelial cells, neural progenitors and fibroblasts. Defects are rescued by down-regulating Usp16 in Ts65D mice by short interfering RNAs (Ref.7).

Sequence similarities

Belongs to the peptidase C19 family. USP16 subfamily.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Chromatin regulator
Hydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

histone H2A K63-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

histone deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

monoubiquitinated histone H2A deubiquitination

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of translational elongation

Inferred from sequence or structural similarity. Source: UniProtKB

protein homotetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.6. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin binding

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 825825Ubiquitin carboxyl-terminal hydrolase 16 HAMAP-Rule MF_03062
PRO_0000367503

Regions

Domain195 – 824630USP
Zinc finger46 – 12479UBP-type HAMAP-Rule MF_03062

Sites

Active site2041Nucleophile By similarity
Active site7591Proton acceptor By similarity
Metal binding241Zinc 1 By similarity
Metal binding261Zinc 1 By similarity
Metal binding481Zinc 2 By similarity
Metal binding511Zinc 2 By similarity
Metal binding731Zinc 3 By similarity
Metal binding761Zinc 3 By similarity
Metal binding811Zinc 2 By similarity
Metal binding891Zinc 2 By similarity
Metal binding931Zinc 3 By similarity
Metal binding1021Zinc 3 By similarity
Metal binding1151Zinc 1 By similarity
Metal binding1181Zinc 1 By similarity

Amino acid modifications

Modified residue4141Phosphoserine By similarity
Modified residue5201Phosphoserine Ref.5

Experimental info

Sequence conflict1731R → K in BAE35580. Ref.1
Sequence conflict1731R → K in AAH03278. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q99LG0 [UniParc].

Last modified December 11, 2013. Version 2.
Checksum: 08E8ED64D233461E

FASTA82593,434
        10         20         30         40         50         60 
MGKKRTKGRS APDTVASESA EPVCRHLRKG LEQGNLKKAL VNVEWNICQD CKTDNKVKDK 

        70         80         90        100        110        120 
PEEEAEDPSV WLCLKCGHQG CGRDSQEQHA LKHYTTPRSE PHYLVLSLDN WSVWCYKCDE 

       130        140        150        160        170        180 
EVKYCSSNRL GQVVDYVRKQ AGVRTSKPAE KNNGHIELEN KKLEKESKNE QEREKSENLA 

       190        200        210        220        230        240 
KETIPMDSAS QITVKGLSNL GNTCFFNAVM QNLSQTPVLR ELLKEVKMSG TIVKIEPPDL 

       250        260        270        280        290        300 
ALTEPLEVNL EPPGPLTLAM SQFLSEMQEN KKRVVTPKEL FSQVCKKATR FKGYQQQDSQ 

       310        320        330        340        350        360 
ELLRYLLDGM RAEEHQRVSK GILKAFGNST EKLDEEVKNK VKDYEKKKAI PSFVDRIFGG 

       370        380        390        400        410        420 
ELTSTIMCDE CRTVSLVHES FLDLSLPVLD DQSGKKSIND KNVKMTMEEE DKDSEEEKDD 

       430        440        450        460        470        480 
SYMKSRSDLP SGTSKHLQKK AKKQAKKQAK NQRRQQKIQE RFLHFNELCA TDYTEDNERE 

       490        500        510        520        530        540 
ADTALAGEVE VDTDSTHGSQ EEATQIELSV NQKDLDGQES MIERTPDVQE SPEDLGVKSA 

       550        560        570        580        590        600 
NTESDLGIVT PAPECPRDFN GAFLEERTSG ELDIINGLKN LNLNAAVDPD EINIEIPNDS 

       610        620        630        640        650        660 
HSAPKVYEVM NEDPETAFCT LANREAFSTD ECSIQHCLYQ FTRNEKLQDA NKLLCEVCSR 

       670        680        690        700        710        720 
RQCNGPKANI KGDRRHVYTN AKKQMLVSLA PPVLTLHLKR FQQAGFNLRK VNKHIKFPEI 

       730        740        750        760        770        780 
LDLAPFCTLK CKNVAEESTR VLYSLYGVVE HSGTMRSGHY TAYAKERTAS CHLSNLVLHG 

       790        800        810        820 
DIPQDCEMES TKGQWFHISD THVQAVPITK VLNSQAYLLF YERIL 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"The Aurora B kinase and the Polycomb protein Ring1B combine to regulate active promoters in quiescent lymphocytes."
Frangini A., Sjoberg M., Roman-Trufero M., Dharmalingam G., Haberle V., Bartke T., Lenhard B., Malumbres M., Vidal M., Dillon N.
Mol. Cell 51:647-661(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[7]"Usp16 contributes to somatic stem-cell defects in Down's syndrome."
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.
Nature 501:380-384(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: UP-REGULATION IN DOWN SYNDROME MODELS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK160038 mRNA. Translation: BAE35580.1.
AC154631 Genomic DNA. No translation available.
CH466521 Genomic DNA. Translation: EDK98336.1.
BC003278 mRNA. Translation: AAH03278.1.
BC004577 mRNA. Translation: AAH04577.1.
RefSeqNP_077220.2. NM_024258.2.
XP_006523163.1. XM_006523100.1.
UniGeneMm.152941.

3D structure databases

ProteinModelPortalQ99LG0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid216501. 2 interactions.

Protein family/group databases

MEROPSC19.050.

PTM databases

PhosphoSiteQ99LG0.

Proteomic databases

PaxDbQ99LG0.
PRIDEQ99LG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026710; ENSMUSP00000026710; ENSMUSG00000025616.
GeneID74112.
KEGGmmu:74112.
UCSCuc007zuk.2. mouse.
uc012ahp.1. mouse.

Organism-specific databases

CTD10600.
MGIMGI:1921362. Usp16.

Phylogenomic databases

eggNOGCOG5207.
GeneTreeENSGT00750000117419.
HOGENOMHOG000154755.
HOVERGENHBG062704.
InParanoidQ99LG0.
KOK11844.
TreeFamTF326075.

Gene expression databases

GenevestigatorQ99LG0.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
HAMAPMF_03062. UBP16.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio339808.
PROQ99LG0.
SOURCESearch...

Entry information

Entry nameUBP16_MOUSE
AccessionPrimary (citable) accession number: Q99LG0
Secondary accession number(s): G5E860, Q99KM0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 11, 2013
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot