Reviewed, UniProtKB/Swiss-Prot Q08DA3 (UBP16_BOVIN)

Names and origin

Protein names

Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 16
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 16
    Ubiquitin-specific-processing protease 16
    Deubiquitinating enzyme 16

Gene names

Name:

USP16

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	826 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
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 process	Cell cycle Cell division Mitosis Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Chromatin regulator Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW histone 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 protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	cysteine-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 826	826	Ubiquitin carboxyl-terminal hydrolase 16		PRO_0000367501
Regions
	Zinc finger	60 – 125	66	UBP-type
Sites
	Active site	204	1	By similarity
	Active site	752	1	By similarity
	Active site	760	1	By similarity
	Metal binding	24	1	Zinc 1 By similarity
	Metal binding	26	1	Zinc 1 By similarity
	Metal binding	48	1	Zinc 2 By similarity
	Metal binding	51	1	Zinc 2 By similarity
	Metal binding	74	1	Zinc 3 By similarity
	Metal binding	77	1	Zinc 3 By similarity
	Metal binding	82	1	Zinc 2 By similarity
	Metal binding	88	1	Zinc 2 By similarity
	Metal binding	90	1	Zinc 2 By similarity
	Metal binding	94	1	Zinc 3 By similarity
	Metal binding	103	1	Zinc 3 By similarity
	Metal binding	116	1	Zinc 1 By similarity
	Metal binding	119	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	414	1	Phosphoserine By similarity
	Modified residue	551	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q08DA3-1 [UniParc]. Last modified October 31, 2006. Version 1. Checksum: 89A15CD698B711DA	FASTA	826	94,077
	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 NTHLSNLVLH 790 800 810 820 GDIPQDFEME STKGQWFHIS DTHVQAVPTT KVLSSQAYLL FYERIL

References

[1]	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
EMBLGenBankDDBJ	BC123861 mRNA. Translation: AAI23862.1.
IPI	IPI00706867.
RefSeq	NP_001070335.1.
UniGene	Bt.51616
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	C19.021.
Genome annotation databases
Ensembl	ENSBTAT00000026801; ENSBTAP00000026801; ENSBTAG00000020122; Bos taurus. [Genome view]
GeneID	519992.
KEGG	bta:519992.
Organism-specific databases
CTD	519992.
Phylogenomic databases
HOVERGEN	Q08DA3.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR001607. Znf_UBP. [Graphical view]
Pfam	PF00443. UCH. 1 hit. PF02148. zf-UBP. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. PS50271. ZF_UBP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBP16_BOVIN

Accession

Primary (citable) accession number: Q08DA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	October 31, 2006
Last modified:	September 1, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)