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Q08DA3 (UBP16_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length826 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B By similarity. HAMAP-Rule MF_03062

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 By similarity. HAMAP-Rule MF_03062

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_processhistone deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

monoubiquitinated histone H2A deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

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 sequence or structural similarity. 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 – 826826Ubiquitin carboxyl-terminal hydrolase 16 HAMAP-Rule MF_03062
PRO_0000367501

Regions

Domain195 – 825631USP
Zinc finger60 – 12566UBP-type HAMAP-Rule MF_03062

Sites

Active site2041Nucleophile By similarity
Active site7601Proton acceptor By similarity
Metal binding241Zinc 1 By similarity
Metal binding261Zinc 1 By similarity
Metal binding481Zinc 2 By similarity
Metal binding511Zinc 2 By similarity
Metal binding741Zinc 3 By similarity
Metal binding771Zinc 3 By similarity
Metal binding821Zinc 2 By similarity
Metal binding901Zinc 2 By similarity
Metal binding941Zinc 3 By similarity
Metal binding1031Zinc 3 By similarity
Metal binding1161Zinc 1 By similarity
Metal binding1191Zinc 1 By similarity

Amino acid modifications

Modified residue4141Phosphoserine By similarity
Modified residue5511Phosphoserine By similarity

Experimental info

Sequence conflict7711S → N in AAI23862. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q08DA3 [UniParc].

Last modified December 11, 2013. Version 2.
Checksum: 54A141CB98B711CE

FASTA82694,050
        10         20         30         40         50         60 
MGKKRTKGKT VPIDDSSESL EPVCRHIRKG LEQGNLKKAL VNVEWNICQD CKTDNKVKDK 

        70         80         90        100        110        120 
SEEETEENPS VWLCLKCGHQ GCGRNSQEQH ALKHYMKPRS EPHCLVLSLD NWSVWCYLCD 

       130        140        150        160        170        180 
DEVHYCNSNR LGQVVDYVRK QAGNTTPESA EDNGNIELEN KKLEKESKNE QEREKKENMA 

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

       250        260        270        280        290        300 
ALTEPLEINL EPPGPLTLAM SQFLNEMQET KKGIVTPREL FSQVCKKAVR FKGYQQQDSQ 

       310        320        330        340        350        360 
ELLRYLLDGM RAEEHQRVSK GILKAFDNST EKVDEELKNK VKEYEKKKSV PSFVDRIFGG 

       370        380        390        400        410        420 
ELTSTIMCDE CRTVSLVHES FLDLSLPVLD DQSGKKSIND KNLKKTMEDE DKDSEEEKDN 

       430        440        450        460        470        480 
DSYLKERNDI PSGTSKHLQK KAKKQAKKQA KNQRRQQKIQ GKVLHLNDVY AIDHPEDNEC 

       490        500        510        520        530        540 
EVEMSLQREA DIKSNHISQE EVAPKEYCVN QKDLNGHEKM IESITDNQKS TEEAAMKNVS 

       550        560        570        580        590        600 
VDNDLEVLAS SATECPRNLN GAYLKEGSNG EVDISSGFEN LNLNAALQPD EINIEILDDD 

       610        620        630        640        650        660 
PTPGTKVYEV VNEDPETAFC TLANREAFNT DECSVQHCLY QFTRNEKLRD ANKLLCEVCT 

       670        680        690        700        710        720 
RRQYSGPKAN MKGERKHIYT NAKKQMLISL APPVLTLHFK RFQQAGFNLR KVNKHIKFPE 

       730        740        750        760        770        780 
ILDLAPFCTL KCKNVAEEHT RVLYSLYGVV EHSGTMRSGH YTAYAKTRTA STHLSNLVLH 

       790        800        810        820 
GDIPQDFEME STKGQWFHIS DTHVQAVPTT KVLSSQAYLL FYERIL 

« Hide

References

[1]"A whole-genome assembly of the domestic cow, Bos taurus."
Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.
Genome Biol. 10:R42.01-R42.10(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hereford.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DAAA02000172 Genomic DNA. No translation available.
DAAA02000173 Genomic DNA. No translation available.
BC123861 mRNA. Translation: AAI23862.1.
RefSeqNP_001070335.1. NM_001076867.1.
UniGeneBt.51616.

3D structure databases

ProteinModelPortalQ08DA3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000026801.

Protein family/group databases

MEROPSC19.021.

Proteomic databases

PRIDEQ08DA3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000026801; ENSBTAP00000026801; ENSBTAG00000020122.
GeneID519992.
KEGGbta:519992.

Organism-specific databases

CTD10600.

Phylogenomic databases

eggNOGCOG5207.
GeneTreeENSGT00750000117419.
HOGENOMHOG000154755.
HOVERGENHBG062704.
InParanoidQ08DA3.
KOK11844.
TreeFamTF326075.

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

NextBio20872996.

Entry information

Entry nameUBP16_BOVIN
AccessionPrimary (citable) accession number: Q08DA3
Secondary accession number(s): F1N2B1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 11, 2013
Last modified: April 16, 2014
This is version 56 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