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Q99LG0

- UBP16_MOUSE

UniProt

Q99LG0 - UBP16_MOUSE

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Protein

Ubiquitin carboxyl-terminal hydrolase 16

Gene

Usp16

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (PubMed:24034696). Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B.1 Publication

Catalytic activityi

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).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi24 – 241Zinc 1UniRule annotation
Metal bindingi26 – 261Zinc 1UniRule annotation
Metal bindingi48 – 481Zinc 2UniRule annotation
Metal bindingi51 – 511Zinc 2UniRule annotation
Metal bindingi73 – 731Zinc 3UniRule annotation
Metal bindingi76 – 761Zinc 3UniRule annotation
Metal bindingi81 – 811Zinc 2UniRule annotation
Metal bindingi89 – 891Zinc 2UniRule annotation
Metal bindingi93 – 931Zinc 3UniRule annotation
Metal bindingi102 – 1021Zinc 3UniRule annotation
Metal bindingi115 – 1151Zinc 1UniRule annotation
Metal bindingi118 – 1181Zinc 1UniRule annotation
Active sitei204 – 2041NucleophileUniRule annotation
Active sitei759 – 7591Proton acceptorUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri46 – 12479UBP-typeUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. histone binding Source: UniProtKB
  3. transcription coactivator activity Source: UniProtKB
  4. ubiquitin binding Source: UniProtKB
  5. ubiquitin-specific protease activity Source: UniProtKB
  6. ubiquitin thiolesterase activity Source: UniProtKB
  7. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. histone deubiquitination Source: UniProtKB
  3. histone H2A K63-linked deubiquitination Source: UniProtKB
  4. mitotic nuclear division Source: UniProtKB
  5. monoubiquitinated histone H2A deubiquitination Source: UniProtKB
  6. positive regulation of transcription, DNA-templated Source: UniProtKB
  7. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  8. positive regulation of translational elongation Source: UniProtKB
  9. protein homotetramerization Source: UniProtKB
  10. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  11. transcription, DNA-templated Source: UniProtKB-KW
  12. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC19.050.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 16UniRule annotation (EC:3.4.19.12UniRule annotation)
Alternative name(s):
Deubiquitinating enzyme 16UniRule annotation
Ubiquitin thioesterase 16UniRule annotation
Ubiquitin-specific-processing protease 16UniRule annotation
Gene namesi
Name:Usp16
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1921362. Usp16.

Subcellular locationi

Nucleus UniRule annotation

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 825825Ubiquitin carboxyl-terminal hydrolase 16PRO_0000367503Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei414 – 4141PhosphoserineBy similarity
Modified residuei520 – 5201Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. Phosphorylation by AURKB enhances the deubiquitinase activity.2 PublicationsUniRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ99LG0.
PRIDEiQ99LG0.

PTM databases

PhosphoSiteiQ99LG0.

Expressioni

Gene expression databases

ExpressionAtlasiQ99LG0. baseline and differential.
GenevestigatoriQ99LG0.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

BioGridi216501. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ99LG0.
SMRiQ99LG0. Positions 22-427, 630-821.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini195 – 824630USPAdd
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the peptidase C19 family. USP16 subfamily.UniRule annotation
Contains 1 UBP-type zinc finger.UniRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri46 – 12479UBP-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5207.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000154755.
HOVERGENiHBG062704.
InParanoidiQ99LG0.
KOiK11844.
OMAiECSIQHC.
TreeFamiTF326075.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
HAMAPiMF_03062. UBP16.
InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99LG0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKKRTKGRS APDTVASESA EPVCRHLRKG LEQGNLKKAL VNVEWNICQD
60 70 80 90 100
CKTDNKVKDK PEEEAEDPSV WLCLKCGHQG CGRDSQEQHA LKHYTTPRSE
110 120 130 140 150
PHYLVLSLDN WSVWCYKCDE EVKYCSSNRL GQVVDYVRKQ AGVRTSKPAE
160 170 180 190 200
KNNGHIELEN KKLEKESKNE QEREKSENLA KETIPMDSAS QITVKGLSNL
210 220 230 240 250
GNTCFFNAVM QNLSQTPVLR ELLKEVKMSG TIVKIEPPDL ALTEPLEVNL
260 270 280 290 300
EPPGPLTLAM SQFLSEMQEN KKRVVTPKEL FSQVCKKATR FKGYQQQDSQ
310 320 330 340 350
ELLRYLLDGM RAEEHQRVSK GILKAFGNST EKLDEEVKNK VKDYEKKKAI
360 370 380 390 400
PSFVDRIFGG ELTSTIMCDE CRTVSLVHES FLDLSLPVLD DQSGKKSIND
410 420 430 440 450
KNVKMTMEEE DKDSEEEKDD SYMKSRSDLP SGTSKHLQKK AKKQAKKQAK
460 470 480 490 500
NQRRQQKIQE RFLHFNELCA TDYTEDNERE ADTALAGEVE VDTDSTHGSQ
510 520 530 540 550
EEATQIELSV NQKDLDGQES MIERTPDVQE SPEDLGVKSA NTESDLGIVT
560 570 580 590 600
PAPECPRDFN GAFLEERTSG ELDIINGLKN LNLNAAVDPD EINIEIPNDS
610 620 630 640 650
HSAPKVYEVM NEDPETAFCT LANREAFSTD ECSIQHCLYQ FTRNEKLQDA
660 670 680 690 700
NKLLCEVCSR RQCNGPKANI KGDRRHVYTN AKKQMLVSLA PPVLTLHLKR
710 720 730 740 750
FQQAGFNLRK VNKHIKFPEI LDLAPFCTLK CKNVAEESTR VLYSLYGVVE
760 770 780 790 800
HSGTMRSGHY TAYAKERTAS CHLSNLVLHG DIPQDCEMES TKGQWFHISD
810 820
THVQAVPITK VLNSQAYLLF YERIL
Length:825
Mass (Da):93,434
Last modified:December 11, 2013 - v2
Checksum:i08E8ED64D233461E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731R → K in BAE35580. (PubMed:16141072)Curated
Sequence conflicti173 – 1731R → K in AAH03278. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28291.1.
RefSeqiNP_077220.2. NM_024258.2.
XP_006523163.1. XM_006523100.1.
UniGeneiMm.152941.

Genome annotation databases

EnsembliENSMUST00000026710; ENSMUSP00000026710; ENSMUSG00000025616.
GeneIDi74112.
KEGGimmu:74112.
UCSCiuc007zuk.2. mouse.
uc012ahp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS28291.1.
RefSeqi NP_077220.2. NM_024258.2.
XP_006523163.1. XM_006523100.1.
UniGenei Mm.152941.

3D structure databases

ProteinModelPortali Q99LG0.
SMRi Q99LG0. Positions 22-427, 630-821.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 216501. 2 interactions.

Protein family/group databases

MEROPSi C19.050.

PTM databases

PhosphoSitei Q99LG0.

Proteomic databases

PaxDbi Q99LG0.
PRIDEi Q99LG0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026710 ; ENSMUSP00000026710 ; ENSMUSG00000025616 .
GeneIDi 74112.
KEGGi mmu:74112.
UCSCi uc007zuk.2. mouse.
uc012ahp.1. mouse.

Organism-specific databases

CTDi 10600.
MGIi MGI:1921362. Usp16.

Phylogenomic databases

eggNOGi COG5207.
GeneTreei ENSGT00670000097750.
HOGENOMi HOG000154755.
HOVERGENi HBG062704.
InParanoidi Q99LG0.
KOi K11844.
OMAi ECSIQHC.
TreeFami TF326075.

Miscellaneous databases

NextBioi 339808.
PROi Q99LG0.
SOURCEi Search...

Gene expression databases

ExpressionAtlasi Q99LG0. baseline and differential.
Genevestigatori Q99LG0.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
HAMAPi MF_03062. UBP16.
InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: UP-REGULATION IN DOWN SYNDROME MODELS.

Entry informationi

Entry nameiUBP16_MOUSE
AccessioniPrimary (citable) accession number: Q99LG0
Secondary accession number(s): G5E860, Q99KM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 11, 2013
Last modified: November 26, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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 (PubMed:24025767).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3