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Q99LG0 (UBP16_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 92. 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
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 lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

General annotation (Comments)

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 By similarity.

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).

Subunit structure

Homotetramer By similarity.

Subcellular location

Nucleus By similarity.

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.

Post-translational modification

Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. The phosphorylated form of the protein is also enzymatically active By similarity.

Sequence similarities

Belongs to the peptidase C19 family. USP16 subfamily.

Contains 1 UBP-type zinc finger.

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_processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

histone H2A K63-linked deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-dependent

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

response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-dependent

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
PRO_0000367503

Regions

Zinc finger46 – 12479UBP-type

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 binding871Zinc 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 Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q99LG0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 72CD1A102365E8E1

FASTA82593,406
        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 QEKEKSENLA 

       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

[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]"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.
[3]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK160038 mRNA. Translation: BAE35580.1.
BC003278 mRNA. Translation: AAH03278.1.
BC004577 mRNA. Translation: AAH04577.1.
IPIIPI00116875.
RefSeqNP_077220.2. NM_024258.2.
UniGeneMm.152941.

3D structure databases

ProteinModelPortalQ99LG0.
SMRQ99LG0. Positions 22-427, 630-821.
ModBaseSearch...

Protein family/group databases

MEROPSC19.050.

PTM databases

PhosphoSiteQ99LG0.

Proteomic databases

PaxDbQ99LG0.
PRIDEQ99LG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID74112.
KEGGmmu:74112.
UCSCuc012ahp.1. mouse.

Organism-specific databases

CTD10600.
MGIMGI:1921362. Usp16.

Phylogenomic databases

eggNOGCOG5207.
HOGENOMHOG000154755.
HOVERGENHBG062704.
InParanoidQ99LG0.
KOK11844.
OrthoDBEOG495ZRD.

Gene expression databases

GenevestigatorQ99LG0.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEPS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio339808.
SOURCESearch...

Entry information

Entry nameUBP16_MOUSE
AccessionPrimary (citable) accession number: Q99LG0
Secondary accession number(s): Q99KM0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 1, 2001
Last modified: May 29, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents