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Q0VA64

- UBP16_XENTR

UniProt

Q0VA64 - UBP16_XENTR

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Protein

Ubiquitin carboxyl-terminal hydrolase 16

Gene

usp16

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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.UniRule annotation

Catalytic activityi

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).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi21 – 211Zinc 1UniRule annotation
Metal bindingi23 – 231Zinc 1UniRule annotation
Metal bindingi45 – 451Zinc 2UniRule annotation
Metal bindingi48 – 481Zinc 2UniRule annotation
Metal bindingi71 – 711Zinc 3UniRule annotation
Metal bindingi74 – 741Zinc 3UniRule annotation
Metal bindingi79 – 791Zinc 2UniRule annotation
Metal bindingi87 – 871Zinc 2UniRule annotation
Metal bindingi91 – 911Zinc 3UniRule annotation
Metal bindingi100 – 1001Zinc 3UniRule annotation
Metal bindingi113 – 1131Zinc 1UniRule annotation
Metal bindingi116 – 1161Zinc 1UniRule annotation
Active sitei205 – 2051NucleophileUniRule annotation
Active sitei798 – 7981Proton acceptorUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri43 – 12280UBP-typeUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. histone binding Source: UniProtKB
  3. transcription coactivator activity Source: UniProtKB
  4. ubiquitin binding Source: UniProtKB
  5. ubiquitin-specific protease activity Source: UniProtKB
  6. ubiquitin thiolesterase activity Source: UniProtKB
  7. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. histone deubiquitination Source: UniProtKB
  2. mitotic nuclear division Source: UniProtKB
  3. positive regulation of transcription, DNA-templated Source: UniProtKB
  4. protein homotetramerization Source: UniProtKB
  5. transcription, DNA-templated Source: UniProtKB-KW
  6. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 16UniRule annotation (EC:3.4.19.12UniRule annotation)
Alternative name(s):
Deubiquitinating enzyme 16UniRule annotation
Ubiquitin thioesterase 16UniRule annotation
Ubiquitin-specific-processing protease 16UniRule annotation
Gene namesi
Name:usp16
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
ProteomesiUP000008143: Unplaced

Organism-specific databases

XenbaseiXB-GENE-1007164. usp16.

Subcellular locationi

Nucleus UniRule annotation

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 864864Ubiquitin carboxyl-terminal hydrolase 16PRO_0000367507Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini196 – 863668USPAdd
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the peptidase C19 family. USP16 subfamily.UniRule annotation
Contains 1 UBP-type zinc finger.UniRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri43 – 12280UBP-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5560.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000154755.
HOVERGENiHBG062704.
InParanoidiQ0VA64.
KOiK11844.
OMAiQCEDGEC.
TreeFamiTF326075.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
HAMAPiMF_03062. UBP16.
InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0VA64-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKKRGKNLP AQDSLDAEPV CKHLRKALDE GSVKKALVNV EWTVCQECQA
60 70 80 90 100
DNKEKNNSDD ELVEDPSVWL CLKCGHRGCG RNSASQHALN HYNTPRSEPH
110 120 130 140 150
CLVLSVDMWS AWCYLCDNEV PYNRSSRLGQ LVDYLQRKAK AKSKSTDSAA
160 170 180 190 200
LDEEVKAEIV AENEVKIEDQ EEKPKGQAKW DKASSTQNNS TEPTVKGLSN
210 220 230 240 250
LGNTCFFNAV MQNLSQTPAV RELLNEAKTL KKPVTVPLPD SSSPTNVEVH
260 270 280 290 300
LEQQPGPLTL AMWQFLTEMQ ETKKGVVTPK EVFSQVCKKA IRFKGYQQQD
310 320 330 340 350
SQELLRYLLD GMRGEEIQRV SLAMSKSLQN TLDEEEIKKI VKDSEKRRTI
360 370 380 390 400
PNFVDHLFGG ELTSTIMCEE CHTVSLVHEP FLDLSLPVLD DVIVKKNSQK
410 420 430 440 450
SSAPAPERKE EEENDDGYIK ERDEASPGAS KHLQKKAKKA AKKQAKNQRR
460 470 480 490 500
QLKMQGKTVL LTDVAKQECS EDEEEIAPNN TESEANTRPD DEVPIADGLN
510 520 530 540 550
TMKSDLSALE NGSETIESAM ERVTEDTDLD TSGHNTESVE MNAMELVRNM
560 570 580 590 600
ENNNNNNTDV NKTLERTEGS GVDSMEATAA VDNGNADTVC VDDTEAANGL
610 620 630 640 650
LDCSAASMDN ELTNSLNRLK LSSDIEPTQV EIEILPDQQQ PHTQIYEVIN
660 670 680 690 700
EDPKTAFSTL SERKDLPLDG YSVLSCLYQF THKETLTGNN KLLCNVCTRK
710 720 730 740 750
QASRLNNSNK GEKTFVYTNA KKQMLVSDPS PILTLHLKRF QQNGFNLRKI
760 770 780 790 800
NRHIKFPEVL DLAPFCTSKC KNIPAGESRL LYSLYGVIEH SGSMRSGHYT
810 820 830 840 850
AFVKLRRPNQ QLCEMVLKGV IPEVSGSEPG QGSWYHISDS HVQAVSLSRV
860
LSSQAYLLFY ERML
Length:864
Mass (Da):96,666
Last modified:December 11, 2013 - v2
Checksum:i8600F3A72FCAF9C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061V → M in AAI21231. 1 PublicationCurated
Sequence conflicti405 – 4051A → V in AAI21231. 1 PublicationCurated
Sequence conflicti452 – 4521L → Q in AAI21231. 1 PublicationCurated
Sequence conflicti495 – 4951I → T in AAI21231. 1 PublicationCurated
Sequence conflicti515 – 5151T → A in AAI21231. 1 PublicationCurated
Sequence conflicti529 – 5291L → I in AAI21231. 1 PublicationCurated
Sequence conflicti548 – 5481R → G in AAI21231. 1 PublicationCurated
Sequence conflicti572 – 5721V → G in AAI21231. 1 PublicationCurated
Sequence conflicti714 – 7141T → K in AAI21231. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAMC01089338 Genomic DNA. No translation available.
AAMC01089339 Genomic DNA. No translation available.
BC121230 mRNA. Translation: AAI21231.1.
RefSeqiNP_001072158.1. NM_001078690.1.
UniGeneiStr.20151.

Genome annotation databases

EnsembliENSXETT00000043701; ENSXETP00000043701; ENSXETG00000020255.
GeneIDi447956.
KEGGixtr:447956.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAMC01089338 Genomic DNA. No translation available.
AAMC01089339 Genomic DNA. No translation available.
BC121230 mRNA. Translation: AAI21231.1 .
RefSeqi NP_001072158.1. NM_001078690.1.
UniGenei Str.20151.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSXETT00000043701 ; ENSXETP00000043701 ; ENSXETG00000020255 .
GeneIDi 447956.
KEGGi xtr:447956.

Organism-specific databases

CTDi 10600.
Xenbasei XB-GENE-1007164. usp16.

Phylogenomic databases

eggNOGi COG5560.
GeneTreei ENSGT00670000097750.
HOGENOMi HOG000154755.
HOVERGENi HBG062704.
InParanoidi Q0VA64.
KOi K11844.
OMAi QCEDGEC.
TreeFami TF326075.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
HAMAPi MF_03062. UBP16.
InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiUBP16_XENTR
AccessioniPrimary (citable) accession number: Q0VA64
Secondary accession number(s): F7BZB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 11, 2013
Last modified: November 26, 2014
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3