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Protein

Ubiquitin carboxyl-terminal hydrolase 20

Gene

USP20

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).By similarity

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531NucleophilePROSITE-ProRule annotation
Active sitei642 – 6421Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri28 – 9265UBP-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Endocytosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 20 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 20
Ubiquitin thioesterase 20
Ubiquitin-specific-processing protease 20
Gene namesi
Name:USP20
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 913913Ubiquitin carboxyl-terminal hydrolase 20PRO_0000390419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311PhosphoserineBy similarity
Modified residuei133 – 1331PhosphoserineBy similarity
Modified residuei257 – 2571PhosphothreonineBy similarity
Modified residuei367 – 3671PhosphoserineBy similarity
Modified residuei376 – 3761PhosphothreonineBy similarity
Modified residuei412 – 4121PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated via a VHL-dependent pathway for proteasomal degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

Interacts with VHL, leading to its ubiquitination and subsequent degradation. Interacts with CCP110, DIO2 and HIF1A (By similarity).By similarity

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000022065.

Structurei

3D structure databases

ProteinModelPortaliQ5R5Z6.
SMRiQ5R5Z6. Positions 5-97.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini144 – 684541USPAdd
BLAST
Domaini686 – 77994DUSP 1PROSITE-ProRule annotationAdd
BLAST
Domaini788 – 891104DUSP 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The UBP-type zinc finger binds 3 zinc ions. However, it does not bind ubiquitin, probably because the conserved Arg in position 55 is replaced by a Glu residue (By similarity).By similarity

Sequence similaritiesi

Contains 2 DUSP domains.PROSITE-ProRule annotation
Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri28 – 9265UBP-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOGENOMiHOG000286031.
HOVERGENiHBG054196.
InParanoidiQ5R5Z6.
KOiK11848.

Family and domain databases

Gene3Di3.30.2230.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 2 hits.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 2 hits.
PROSITEiPS51283. DUSP. 2 hits.
PS00972. 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.

Q5R5Z6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDSRDLCPH LDSIGEVTKE DLLLKSMGTC QSCGVTGPNL WACLQVACPY
60 70 80 90 100
VGCGESFADH STIHAQAKKH NLTVNLTTFR LWCYACEKEV FLEQRLAAPL
110 120 130 140 150
LGSSKFSEQD SPPPSHPLKA VPIAVADEGE SESEDDDLKP RGLTGMKNLG
160 170 180 190 200
NSCYMNAALQ ALSNCPPLTQ FFLECGGLVR TDKKPALCKS YQKLVSEVWH
210 220 230 240 250
KKRPSYVVPT SLSHGIKLVN PMFRGYAQQD TQEFLRCLMD QLHEELKEPV
260 270 280 290 300
VATVALTEAR DSDSSDTDEK REGDRSPSED EFLSCDSSSD RGEGDGQGRG
310 320 330 340 350
GGSSQAETEL LIPDEASRAI SEKERMKDRK FSWGQQRTNS EQVDEDADVD
360 370 380 390 400
TTMAALDDQP AEAQPPSPRS SSPCRTPEPD NDAHLCSSSR PCSPVHHHEG
410 420 430 440 450
HAKLSSSPPR ASPVRMAPSY VLKKAQVLSA GSRRRKEQRY RSVISDIFDG
460 470 480 490 500
SILSLVQCLT CDRVSATVET FQDLSLPIPG KEDLAKLHSA IYQNVPAKPG
510 520 530 540 550
TCGDSYAAQG WLAFIVEYIR RFVVSCTPSW FWGPVVTLED CLAAFFAADE
560 570 580 590 600
LKGDNMYSCE RCKKLRNGVK YCKVLRLPEI LCIHLKRFRH EVMYSFKINS
610 620 630 640 650
HVSFPLEGLD LRPFLAKECT SQITTYDLLS VICHHGTAGS GHYIAYCQNV
660 670 680 690 700
INGQWYEFDD QYVTEVHETV VQNAEGYVLF YRKSSEEAVR ERQQVVSLAA
710 720 730 740 750
MREPSLLRFY VSREWLNKFN TFAEPGPITN QTFLCSHGGI PPHKYHYIDD
760 770 780 790 800
LVVILPQNVW EHLYNRFGGG PAVNHLYVCS ICQVEIEALA KRRRIEIDTF
810 820 830 840 850
IKLNKAFQAE ESPGIIYCIS MQWFREWEAF VKGKDNEPPG PIDNSRIAQV
860 870 880 890 900
KGSGHVQLKQ GADYGQISEE TWTYLNSLYG GGPEIAIRQS VAQPLGPESL
910
HGEQKIEAEA RAV
Length:913
Mass (Da):101,851
Last modified:December 21, 2004 - v1
Checksum:i54CA311FD1D3E626
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860704 mRNA. Translation: CAH92820.1.
RefSeqiNP_001126647.1. NM_001133175.1.

Genome annotation databases

GeneIDi100173645.
KEGGipon:100173645.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860704 mRNA. Translation: CAH92820.1.
RefSeqiNP_001126647.1. NM_001133175.1.

3D structure databases

ProteinModelPortaliQ5R5Z6.
SMRiQ5R5Z6. Positions 5-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000022065.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100173645.
KEGGipon:100173645.

Organism-specific databases

CTDi10868.

Phylogenomic databases

HOGENOMiHOG000286031.
HOVERGENiHBG054196.
InParanoidiQ5R5Z6.
KOiK11848.

Family and domain databases

Gene3Di3.30.2230.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 2 hits.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 2 hits.
PROSITEiPS51283. DUSP. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiUBP20_PONAB
AccessioniPrimary (citable) accession number: Q5R5Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: December 21, 2004
Last modified: June 24, 2015
This is version 63 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.