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A8HAL1 (UBP16_DANRE) 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
ORF Names:si:dkey-121n8.2
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length815 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. 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

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
   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

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

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 – 815815Ubiquitin carboxyl-terminal hydrolase 16 HAMAP-Rule MF_03062
PRO_0000367505

Regions

Domain208 – 814607USP
Zinc finger46 – 12681UBP-type HAMAP-Rule MF_03062

Sites

Active site2171Nucleophile By similarity
Active site7521Proton acceptor By similarity
Metal binding241Zinc 1 By similarity
Metal binding261Zinc 1 By similarity
Metal binding481Zinc 2 By similarity
Metal binding511Zinc 2 By similarity
Metal binding761Zinc 3 By similarity
Metal binding791Zinc 3 By similarity
Metal binding841Zinc 2 By similarity
Metal binding911Zinc 2 By similarity
Metal binding951Zinc 3 By similarity
Metal binding1041Zinc 3 By similarity
Metal binding1171Zinc 1 By similarity
Metal binding1201Zinc 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
A8HAL1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 50CF71DC500EE191

FASTA81590,450
        10         20         30         40         50         60 
MGKKKVKDRS AGTDSSSETA GPSCTHIRKG TENSVLKKAC LNEHWSSCQD CEQDKPEEKQ 

        70         80         90        100        110        120 
ILEDQTDGES PAVWMCLKCG HRGCGRSGNQ HAIKHYETPR SEPHCLVLSL DVWSVWCYIC 

       130        140        150        160        170        180 
DDEVQYSSTG QLAQLITNIR KQVLTAPDKR NASKKSWKED ISVMNSAEQT QDEEKGKKGK 

       190        200        210        220        230        240 
QKSSSKQEDS PKSHQSAAAG SSAVVSVRGL SNLGNTCFFN AVVQSLSQTQ YLRELLKQIA 

       250        260        270        280        290        300 
EEKSSFSITP ALSSELDPLQ IQLERPGSLT LAMCQLMNEI QETKKGVVTP KELFTQVCKK 

       310        320        330        340        350        360 
APRFKGFQQQ DSQELLRYLL DGMRAEEAKR VNSGILEALK SSGKNFEAEQ TKKIVKEYEK 

       370        380        390        400        410        420 
DGAPKNFVDR VFGGAMSSTV MCKECKTVSL VTEMFLDLSL PVADEAYRKK NQKKAVQHRH 

       430        440        450        460        470        480 
SVSDDGDQDT SSLANGNEDM PTGTGSKYQQ KKAKKQAKKQ AKNQRRQQKQ GGKVTLDAIT 

       490        500        510        520        530        540 
NQSSTDPADS SMQTQTVSVN GSADAQPADT NQEDLSLEKH NEDQDDEEPE QEQAASVNNR 

       550        560        570        580        590        600 
FTALSEDQTT EDIAEQVNED EDEIEQNCAE EEELVEELNT MSLTTPSEGD VENGEDTLED 

       610        620        630        640        650        660 
VKEYTVVNRD PELAFRALAS RTAPVKQECS VESCLYQFTE VEHLTENNRL MCVTCTKQQP 

       670        680        690        700        710        720 
GYKDGCKKAV YRDALKQMLI SDPPVVLTLH LKRFQQVAYS VCKVNRHVQF PQILDLAPFC 

       730        740        750        760        770        780 
SLNCTGVKEG ETQVLYSLYG IVEHSGTMRS GHYTAYVKSR PSTHNCVQNG TAAASGDAEA 

       790        800        810 
SKGSWFHISD SSVHPVPEAK VQSSQAYLLF YEKIS 

« Hide

References

[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR854897 Genomic DNA. Translation: CAP09451.1.
RefSeqNP_001139569.1. NM_001146097.1.
UniGeneDr.24329.
Dr.99665.

3D structure databases

ProteinModelPortalA8HAL1.
SMRA8HAL1. Positions 22-142.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000085645; ENSDARP00000080080; ENSDARG00000060633.
GeneID569700.
KEGGdre:569700.

Organism-specific databases

CTD10600.

Phylogenomic databases

eggNOGCOG5560.
GeneTreeENSGT00750000117419.
HOGENOMHOG000154755.
HOVERGENHBG062704.
KOK11844.
OMACKNVAEE.
OrthoDBEOG7J9VNZ.
PhylomeDBA8HAL1.
TreeFamTF326075.

Gene expression databases

BgeeA8HAL1.

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

NextBio20889807.
PROA8HAL1.

Entry information

Entry nameUBP16_DANRE
AccessionPrimary (citable) accession number: A8HAL1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 56 of the entry and version 1 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