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Q6PAW2 (UBP16_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length901 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. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B By similarity. Ref.2

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
Gene Ontology (GO)
   Biological_processanterior/posterior pattern specification

Inferred from mutant phenotype Ref.2. 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

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 – 901901Ubiquitin carboxyl-terminal hydrolase 16 HAMAP-Rule MF_03062
PRO_0000367506

Regions

Domain197 – 900704USP
Zinc finger43 – 12280UBP-type HAMAP-Rule MF_03062

Sites

Active site2061Nucleophile By similarity
Active site8351Proton acceptor By similarity
Metal binding211Zinc 1 By similarity
Metal binding231Zinc 1 By similarity
Metal binding451Zinc 2 By similarity
Metal binding481Zinc 2 By similarity
Metal binding711Zinc 3 By similarity
Metal binding741Zinc 3 By similarity
Metal binding791Zinc 2 By similarity
Metal binding871Zinc 2 By similarity
Metal binding911Zinc 3 By similarity
Metal binding1001Zinc 3 By similarity
Metal binding1131Zinc 1 By similarity
Metal binding1161Zinc 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6PAW2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: EAC737894C997ABA

FASTA901101,293
        10         20         30         40         50         60 
MVKKRGTNLP AQDFLDAEPV CKHLRKALDD GSVKRALVNV EWTMCQDCQA DNKEKNNSED 

        70         80         90        100        110        120 
ESAEDPSVWL CLKCGHRGCG RNSVAQHALN HYNTPRSEPH CLVLNVDMWS AWCYLCDNEV 

       130        140        150        160        170        180 
PYNRTSRLGQ LVDYLQRKAK AKNKNSNSVV SNEEVKTEIV TENEVKKIQY QDEKPDVQAK 

       190        200        210        220        230        240 
QEKASSTQKI STEPTVKGLS NLGNTCFFNA VMQNLSQTPA LSELLNEVKT FRKPVTVLLP 

       250        260        270        280        290        300 
DSSSPKILEV NLEQQPGPLT LAMWQFLTEM HETKKGVVTP KELFSQVCKK AIRFKGYQQQ 

       310        320        330        340        350        360 
DSQELLRYLL DGMRGEEIQR VTLAMSKSLQ STLDEEEIKK IVKDYEKRRT IPNFVDCLFG 

       370        380        390        400        410        420 
GELTSTIMCE ECHTVSLVHE PFLDLSLPVL DDLIVKKNSK STPPARERKE EEEEEENDDD 

       430        440        450        460        470        480 
RYVKERDEVS PGASKHLQKK AKKAAKKQAK NQRRQQKWQG KTVLFTDLAK QECSEDEEEV 

       490        500        510        520        530        540 
SQTKTNTRPD NETPTADGLN TMETDLSTLE NGNEESADGL NTMETDLSTL ENGNEEMAGG 

       550        560        570        580        590        600 
FKTMEMDLST LENGSETIKS AVEGITEHTD LDSSVHNNVG SVETNALVGN MENNNNIEVN 

       610        620        630        640        650        660 
KTPERTAGSG GDSMEAMAAV ENGNADAVNV DDTEAVNGLI DSANMDHELT NSLNRLQLSS 

       670        680        690        700        710        720 
DLEPTQVEIE ILPDKEQPHT QVYEVVNEDP KTAFSTLSNR KDLPIDEFSV LSCLYQFTHK 

       730        740        750        760        770        780 
ETLTGNNKLL CNVCTRKQAS RLNNSNKGEK KFVYTNAKKQ MLVSNPSPIL TLHLKRFQQN 

       790        800        810        820        830        840 
GFNLRKINRH IKFPEVLDLA PFCTAKCKNV PEGESRLLYS LYGVIEHSGS MRSGHYTAFV 

       850        860        870        880        890        900 
KLRHPNQQLC KMLFTGVIPE VSGSEPGQGS WYHISDSHVQ AVSLSRVLSS QAYLLFYERM 


L 

« Hide

References

« Hide 'large scale' references
[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[2]"Regulation of cell cycle progression and gene expression by H2A deubiquitination."
Joo H.-Y., Zhai L., Yang C., Nie S., Erdjument-Bromage H., Tempst P., Chang C., Wang H.
Nature 449:1068-1072(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC060022 mRNA. Translation: AAH60022.1.
RefSeqNP_001083244.1. NM_001089775.1.
UniGeneXl.32808.

3D structure databases

ProteinModelPortalQ6PAW2.
SMRQ6PAW2. Positions 19-139.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID398823.
KEGGxla:398823.

Organism-specific databases

CTD10600.
XenbaseXB-GENE-1007170. usp16.

Phylogenomic databases

HOVERGENHBG062704.
KOK11844.

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...

Entry information

Entry nameUBP16_XENLA
AccessionPrimary (citable) accession number: Q6PAW2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 62 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