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Q8C6M1

- UBP20_MOUSE

UniProt

Q8C6M1 - UBP20_MOUSE

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Protein
Ubiquitin carboxyl-terminal hydrolase 20
Gene
Usp20, Kiaa1003, Vdu2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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.

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 sitei154 – 1541Nucleophile By similarity
Active sitei645 – 6451Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri28 – 9265UBP-type
Add
BLAST

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. ubiquitin thiolesterase activity Source: UniProtKB
  3. ubiquitin-specific protease activity Source: InterPro
  4. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. protein K48-linked deubiquitination Source: UniProtKB
  3. protein K63-linked deubiquitination Source: UniProtKB
  4. protein deubiquitination Source: UniProtKB
  5. regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  6. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Endocytosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC19.025.

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
VHL-interacting deubiquitinating enzyme 2
Gene namesi
Name:Usp20
Synonyms:Kiaa1003, Vdu2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1921520. Usp20.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 916916Ubiquitin carboxyl-terminal hydrolase 20
PRO_0000390418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei132 – 1321Phosphoserine1 Publication
Modified residuei134 – 1341Phosphoserine1 Publication
Modified residuei259 – 2591Phosphothreonine By similarity
Modified residuei369 – 3691Phosphoserine1 Publication
Modified residuei378 – 3781Phosphothreonine1 Publication
Modified residuei415 – 4151Phosphoserine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8C6M1.
PaxDbiQ8C6M1.
PRIDEiQ8C6M1.

PTM databases

PhosphoSiteiQ8C6M1.

Expressioni

Gene expression databases

ArrayExpressiQ8C6M1.
BgeeiQ8C6M1.
GenevestigatoriQ8C6M1.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ8C6M1.
SMRiQ8C6M1. Positions 5-99, 143-247, 437-688.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini145 – 687543USP
Add
BLAST
Domaini689 – 78294DUSP 1
Add
BLAST
Domaini791 – 894104DUSP 2
Add
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.

Sequence similaritiesi

Contains 2 DUSP domains.
Contains 1 USP domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5560.
GeneTreeiENSGT00750000117701.
HOGENOMiHOG000286031.
HOVERGENiHBG054196.
InParanoidiQ8C6M1.
KOiK11848.
OMAiADYGQIS.
OrthoDBiEOG7CRTP2.
PhylomeDBiQ8C6M1.
TreeFamiTF352179.

Family and domain databases

Gene3Di3.30.2230.10. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
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.

Q8C6M1-1 [UniParc]FASTAAdd to Basket

« Hide

MGDARDLCPH LDCIGEVTKE DLLLKSKGTC QSCGVAGPNL WACLQVTCPY    50
VGCGESFADH SSIHAQVKKH NLTVNLTTFR VWCYACEREV FLEQRLAVHL 100
ASSSARLSEQ DSPPPSHPLK AVPIAVADEG ESESEDDDLK PRGLTGMKNL 150
GNSCYMNAAL QALSNCPPLT QFFLECGGLV RTDKKPALCK SYQKLISEVW 200
HKKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM DQLHEELKEP 250
MVAAVAALTD ARDSDSSDTD ERRDGDRSPS EDEFLSCDSS SDRGEGDGQG 300
RGGGSSKAEM ELLISDEAGR AISEKERMKD RKFSWGQQRT NSEQVDEDAD 350
VDTAMASLDE QSREAQPPSP RSTSPCQTPE PDNEAHIRSS SRPCSPVHHH 400
HEGHSKLSSS PPRASPVRMG PSYVLKKAQV PSTGGRRRKE QSYRSVISDV 450
FNGSVLSLVQ CLTCDRVSTT VETFQDLSLP IPGKEDLAKL HSAIYQNVPA 500
KPGACGDSYS SQGWLAFIVE YIRRFVVSCT PSWFWGPVVT LEDCLAAFFA 550
ADELKGDNMY SCERCKKLRN GVKYCKVLCL PEILCVHLKR FRHEVMYSFK 600
VSSHVSFPLE GLDLRPFLAK ECTSQVTTYD LLSVICHHGT AGSGHYIAYC 650
QNVINGQWYE FDDQYVTEVH ETVVQNVEAY VLFYRKSSEE AMRERQQVVS 700
LAAMREPSLL RFYVSREWLN KFNTFAEPGP ITNHTFLCSH GGIPPNKYHY 750
IDDLVVILPQ SVWEHLYSRF GGGPAVNHLY VCSICQVEIE ALAKRRRVEI 800
DTFIKLNKAF QAEESPAVIY CISMHWFREW EAFVKGKDSE PPGPIDNSRI 850
AQVKGSGHIQ LKQGADCGQI SEETWTYLSS LYGGGPEIAI RQSVAQLPDP 900
ESLHGEQKIE AETRAL 916
Length:916
Mass (Da):102,140
Last modified:March 1, 2003 - v1
Checksum:iE104BD489E7ED49F
GO

Sequence cautioni

The sequence BAD32361.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171H → T in AAN15803. 1 Publication
Sequence conflicti380 – 3801E → D in AAN15803. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF449715 mRNA. Translation: AAN15803.1.
AK173083 mRNA. Translation: BAD32361.1. Different initiation.
AK054279 mRNA. Translation: BAC35715.1.
AK163663 mRNA. Translation: BAE37447.1.
AL844546 Genomic DNA. Translation: CAM18433.1.
CH466542 Genomic DNA. Translation: EDL08500.1.
BC079674 mRNA. Translation: AAH79674.1.
CCDSiCCDS15893.1.
RefSeqiNP_083122.1. NM_028846.5.
XP_006498455.1. XM_006498392.1.
UniGeneiMm.346654.

Genome annotation databases

EnsembliENSMUST00000102849; ENSMUSP00000099913; ENSMUSG00000026854.
ENSMUST00000170476; ENSMUSP00000127388; ENSMUSG00000026854.
GeneIDi74270.
KEGGimmu:74270.
UCSCiuc008jde.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF449715 mRNA. Translation: AAN15803.1 .
AK173083 mRNA. Translation: BAD32361.1 . Different initiation.
AK054279 mRNA. Translation: BAC35715.1 .
AK163663 mRNA. Translation: BAE37447.1 .
AL844546 Genomic DNA. Translation: CAM18433.1 .
CH466542 Genomic DNA. Translation: EDL08500.1 .
BC079674 mRNA. Translation: AAH79674.1 .
CCDSi CCDS15893.1.
RefSeqi NP_083122.1. NM_028846.5.
XP_006498455.1. XM_006498392.1.
UniGenei Mm.346654.

3D structure databases

ProteinModelPortali Q8C6M1.
SMRi Q8C6M1. Positions 5-99, 143-247, 437-688.
ModBasei Search...

Protein family/group databases

MEROPSi C19.025.

PTM databases

PhosphoSitei Q8C6M1.

Proteomic databases

MaxQBi Q8C6M1.
PaxDbi Q8C6M1.
PRIDEi Q8C6M1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102849 ; ENSMUSP00000099913 ; ENSMUSG00000026854 .
ENSMUST00000170476 ; ENSMUSP00000127388 ; ENSMUSG00000026854 .
GeneIDi 74270.
KEGGi mmu:74270.
UCSCi uc008jde.2. mouse.

Organism-specific databases

CTDi 10868.
MGIi MGI:1921520. Usp20.
Rougei Search...

Phylogenomic databases

eggNOGi COG5560.
GeneTreei ENSGT00750000117701.
HOGENOMi HOG000286031.
HOVERGENi HBG054196.
InParanoidi Q8C6M1.
KOi K11848.
OMAi ADYGQIS.
OrthoDBi EOG7CRTP2.
PhylomeDBi Q8C6M1.
TreeFami TF352179.

Miscellaneous databases

NextBioi 340299.
PROi Q8C6M1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8C6M1.
Bgeei Q8C6M1.
Genevestigatori Q8C6M1.

Family and domain databases

Gene3Di 3.30.2230.10. 2 hits.
3.30.40.10. 1 hit.
InterProi IPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view ]
Pfami PF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view ]
SMARTi SM00695. DUSP. 2 hits.
[Graphical view ]
SUPFAMi SSF143791. SSF143791. 2 hits.
PROSITEi PS51283. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a deubiquitinating enzyme subfamily as substrates of the von Hippel-Lindau tumor suppressor."
    Li Z., Wang D., Na X., Schoen S.R., Messing E.M., Wu G.
    Biochem. Biophys. Res. Commun. 294:700-709(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata and Ovary.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-134 AND THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiUBP20_MOUSE
AccessioniPrimary (citable) accession number: Q8C6M1
Secondary accession number(s): Q69ZT5, Q8CJ72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 101 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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