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Q6PAW2

- UBP16_XENLA

UniProt

Q6PAW2 - UBP16_XENLA

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Protein

Ubiquitin carboxyl-terminal hydrolase 16

Gene

usp16

Organism
Xenopus laevis (African clawed frog)
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 sitei206 – 2061NucleophileUniRule annotation
Active sitei835 – 8351Proton 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. anterior/posterior pattern specification Source: UniProtKB
  2. histone deubiquitination Source: UniProtKB
  3. mitotic nuclear division Source: UniProtKB
  4. positive regulation of transcription, DNA-templated Source: UniProtKB
  5. protein homotetramerization Source: UniProtKB
  6. transcription, DNA-templated Source: UniProtKB-KW
  7. 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 laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-1007170. 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 – 901901Ubiquitin carboxyl-terminal hydrolase 16PRO_0000367506Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ6PAW2.
SMRiQ6PAW2. Positions 19-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini197 – 900704USPAdd
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

HOVERGENiHBG062704.
KOiK11844.

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.

Q6PAW2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKKRGTNLP AQDFLDAEPV CKHLRKALDD GSVKRALVNV EWTMCQDCQA
60 70 80 90 100
DNKEKNNSED ESAEDPSVWL CLKCGHRGCG RNSVAQHALN HYNTPRSEPH
110 120 130 140 150
CLVLNVDMWS AWCYLCDNEV PYNRTSRLGQ LVDYLQRKAK AKNKNSNSVV
160 170 180 190 200
SNEEVKTEIV TENEVKKIQY QDEKPDVQAK QEKASSTQKI STEPTVKGLS
210 220 230 240 250
NLGNTCFFNA VMQNLSQTPA LSELLNEVKT FRKPVTVLLP DSSSPKILEV
260 270 280 290 300
NLEQQPGPLT LAMWQFLTEM HETKKGVVTP KELFSQVCKK AIRFKGYQQQ
310 320 330 340 350
DSQELLRYLL DGMRGEEIQR VTLAMSKSLQ STLDEEEIKK IVKDYEKRRT
360 370 380 390 400
IPNFVDCLFG GELTSTIMCE ECHTVSLVHE PFLDLSLPVL DDLIVKKNSK
410 420 430 440 450
STPPARERKE EEEEEENDDD RYVKERDEVS PGASKHLQKK AKKAAKKQAK
460 470 480 490 500
NQRRQQKWQG KTVLFTDLAK QECSEDEEEV SQTKTNTRPD NETPTADGLN
510 520 530 540 550
TMETDLSTLE NGNEESADGL NTMETDLSTL ENGNEEMAGG FKTMEMDLST
560 570 580 590 600
LENGSETIKS AVEGITEHTD LDSSVHNNVG SVETNALVGN MENNNNIEVN
610 620 630 640 650
KTPERTAGSG GDSMEAMAAV ENGNADAVNV DDTEAVNGLI DSANMDHELT
660 670 680 690 700
NSLNRLQLSS DLEPTQVEIE ILPDKEQPHT QVYEVVNEDP KTAFSTLSNR
710 720 730 740 750
KDLPIDEFSV LSCLYQFTHK ETLTGNNKLL CNVCTRKQAS RLNNSNKGEK
760 770 780 790 800
KFVYTNAKKQ MLVSNPSPIL TLHLKRFQQN GFNLRKINRH IKFPEVLDLA
810 820 830 840 850
PFCTAKCKNV PEGESRLLYS LYGVIEHSGS MRSGHYTAFV KLRHPNQQLC
860 870 880 890 900
KMLFTGVIPE VSGSEPGQGS WYHISDSHVQ AVSLSRVLSS QAYLLFYERM

L
Length:901
Mass (Da):101,293
Last modified:July 5, 2004 - v1
Checksum:iEAC737894C997ABA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC060022 mRNA. Translation: AAH60022.1.
RefSeqiNP_001083244.1. NM_001089775.1.
UniGeneiXl.32808.

Genome annotation databases

GeneIDi398823.
KEGGixla:398823.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC060022 mRNA. Translation: AAH60022.1 .
RefSeqi NP_001083244.1. NM_001089775.1.
UniGenei Xl.32808.

3D structure databases

ProteinModelPortali Q6PAW2.
SMRi Q6PAW2. Positions 19-139.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 398823.
KEGGi xla:398823.

Organism-specific databases

CTDi 10600.
Xenbasei XB-GENE-1007170. usp16.

Phylogenomic databases

HOVERGENi HBG062704.
KOi K11844.

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

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiUBP16_XENLA
AccessioniPrimary (citable) accession number: Q6PAW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 5, 2004
Last modified: October 1, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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