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Protein

Ubiquitin carboxyl-terminal hydrolase 20

Gene

UBP20

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (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 sitei185 – 1851NucleophilePROSITE-ProRule annotation
Active sitei435 – 4351Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: GO_Central
  2. ubiquitin-specific protease activity Source: GO_Central

GO - Biological processi

  1. proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  2. protein deubiquitination Source: GO_Central
  3. regulation of proteasomal protein catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciARA:AT4G17895-MONOMER.

Protein family/group databases

MEROPSiC19.A16.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 20 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 20
Short name:
AtUBP20
Ubiquitin thioesterase 20
Ubiquitin-specific-processing protease 20
Gene namesi
Name:UBP20
Ordered Locus Names:At4g17895
ORF Names:T6K21.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G17895.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 695695Ubiquitin carboxyl-terminal hydrolase 20PRO_0000313046Add
BLAST

Proteomic databases

PRIDEiQ9FPS7.

Expressioni

Gene expression databases

GenevestigatoriQ9FPS7.

Structurei

3D structure databases

ProteinModelPortaliQ9FPS7.
SMRiQ9FPS7. Positions 177-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini176 – 476301USPAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi51 – 150100Asp-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000154757.
InParanoidiQ9FPS7.
KOiK11855.
PhylomeDBiQ9FPS7.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FPS7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMAKPDVPS SILPRSSSIL PNSIETLDEN ESIEAQVNNV QSLALSSPNR
60 70 80 90 100
DRSDDDDNNN NHDSVSIPPP IYDGYSSSSS DESQSVPSPP INLDHDDDEC
110 120 130 140 150
QIPIRNTSQA LDDIDDDIWG DDDLPETRRP WTPNVSPGFG SDDDDDNDDD
160 170 180 190 200
NSKNEPRKSL FYGFRQEPEP VTGVGAGLWN LGNSCFLNSV FQCFTHTVPL
210 220 230 240 250
IESLLSFRYE VPCHCGNEFF CVIRAIRYHI EAALRPERCP IAPYFFFDNL
260 270 280 290 300
NYFSPDFQRY QQEDAHEFLQ AFLEKLEICG SDRTSFRGDI TSQDVFSGRL
310 320 330 340 350
ISGLRCCNCD YVSETYEKSV GLSLEIEDVD TLGSALESFT RVEKLDEQLT
360 370 380 390 400
CDNCNEKVSK EKQLLLDKLP LVATFHLKRF KNNGLYMEKI YKHVKIPLEI
410 420 430 440 450
DLQPYMRNIQ ENEVSTKYHL YALVEHFGYS VAYGHYSSYV RSAPKIWHHF
460 470 480 490 500
DDSKVTRIDE DMVLSQDSYI LFYAREGTRW FSSVYEEMQP LVEASLLNSS
510 520 530 540 550
PKSVLDSSTN GECLSEISYE NGDKASKPCD SAGVCNQHVK TKEDFVSLSN
560 570 580 590 600
DDVFLSAESS SGEESPMGEL LDPLDPDDSY SPCTEKESDS CLAIERATIR
610 620 630 640 650
DDFFPLLLDQ NQESSTSSPK LQERTFEMQL LQMEETTKSQ EPWKQPLSSI
660 670 680 690
SNIADSMEAE FVYGDLMKKP SPRARELLDQ AISTNGSPPK KLKTT
Length:695
Mass (Da):78,633
Last modified:March 1, 2001 - v1
Checksum:i8FD6265E169892D2
GO

Sequence cautioni

The sequence CAA17132.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene At4g17890 has been split into 2 genes: At4g17890 and At4g17895.Curated
The sequence CAB78791.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene At4g17890 has been split into 2 genes: At4g17890 and At4g17895.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302668 mRNA. Translation: AAG42758.1.
AL021889 Genomic DNA. Translation: CAA17132.1. Sequence problems.
AL161547 Genomic DNA. Translation: CAB78791.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83963.1.
PIRiT05075.
RefSeqiNP_567544.1. NM_117899.2.
UniGeneiAt.21461.

Genome annotation databases

EnsemblPlantsiAT4G17895.1; AT4G17895.1; AT4G17895.
GeneIDi827513.
KEGGiath:AT4G17895.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302668 mRNA. Translation: AAG42758.1.
AL021889 Genomic DNA. Translation: CAA17132.1. Sequence problems.
AL161547 Genomic DNA. Translation: CAB78791.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83963.1.
PIRiT05075.
RefSeqiNP_567544.1. NM_117899.2.
UniGeneiAt.21461.

3D structure databases

ProteinModelPortaliQ9FPS7.
SMRiQ9FPS7. Positions 177-473.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC19.A16.

Proteomic databases

PRIDEiQ9FPS7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G17895.1; AT4G17895.1; AT4G17895.
GeneIDi827513.
KEGGiath:AT4G17895.

Organism-specific databases

GeneFarmi1993. 220.
TAIRiAT4G17895.

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000154757.
InParanoidiQ9FPS7.
KOiK11855.
PhylomeDBiQ9FPS7.

Enzyme and pathway databases

BioCyciARA:AT4G17895-MONOMER.

Gene expression databases

GenevestigatoriQ9FPS7.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are required for the resistance to the amino acid analog canavanine."
    Yan N., Doelling J.H., Falbel T.G., Durski A.M., Vierstra R.D.
    Plant Physiol. 124:1828-1843(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION, NOMENCLATURE.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.

Entry informationi

Entry nameiUBP20_ARATH
AccessioniPrimary (citable) accession number: Q9FPS7
Secondary accession number(s): O49688
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2001
Last modified: March 4, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.