SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9FPS7

- UBP20_ARATH

UniProt

Q9FPS7 - UBP20_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Ubiquitin carboxyl-terminal hydrolase 20
Gene
UBP20, At4g17895, T6K21.70
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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.

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 – 1851Nucleophile By similarity
Active sitei435 – 4351Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. ubiquitinyl hydrolase activity Source: InterPro

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process Source: InterPro
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: Chromosome 4

Organism-specific databases

TAIRiAT4G17895.

PTM / Processingi

Molecule processing

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

Proteomic databases

PRIDEiQ9FPS7.

Expressioni

Gene expression databases

GenevestigatoriQ9FPS7.

Structurei

3D structure databases

ProteinModelPortaliQ9FPS7.
SMRiQ9FPS7. Positions 177-473.

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000154757.
InParanoidiQ9FPS7.
KOiK11855.
OMAiIERATIR.
PhylomeDBiQ9FPS7.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[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

MLMAKPDVPS SILPRSSSIL PNSIETLDEN ESIEAQVNNV QSLALSSPNR    50
DRSDDDDNNN NHDSVSIPPP IYDGYSSSSS DESQSVPSPP INLDHDDDEC 100
QIPIRNTSQA LDDIDDDIWG DDDLPETRRP WTPNVSPGFG SDDDDDNDDD 150
NSKNEPRKSL FYGFRQEPEP VTGVGAGLWN LGNSCFLNSV FQCFTHTVPL 200
IESLLSFRYE VPCHCGNEFF CVIRAIRYHI EAALRPERCP IAPYFFFDNL 250
NYFSPDFQRY QQEDAHEFLQ AFLEKLEICG SDRTSFRGDI TSQDVFSGRL 300
ISGLRCCNCD YVSETYEKSV GLSLEIEDVD TLGSALESFT RVEKLDEQLT 350
CDNCNEKVSK EKQLLLDKLP LVATFHLKRF KNNGLYMEKI YKHVKIPLEI 400
DLQPYMRNIQ ENEVSTKYHL YALVEHFGYS VAYGHYSSYV RSAPKIWHHF 450
DDSKVTRIDE DMVLSQDSYI LFYAREGTRW FSSVYEEMQP LVEASLLNSS 500
PKSVLDSSTN GECLSEISYE NGDKASKPCD SAGVCNQHVK TKEDFVSLSN 550
DDVFLSAESS SGEESPMGEL LDPLDPDDSY SPCTEKESDS CLAIERATIR 600
DDFFPLLLDQ NQESSTSSPK LQERTFEMQL LQMEETTKSQ EPWKQPLSSI 650
SNIADSMEAE FVYGDLMKKP SPRARELLDQ AISTNGSPPK KLKTT 695
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.
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi T05075.
RefSeqi NP_567544.1. NM_117899.2.
UniGenei At.21461.

3D structure databases

ProteinModelPortali Q9FPS7.
SMRi Q9FPS7. Positions 177-473.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C19.A16.

Proteomic databases

PRIDEi Q9FPS7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G17895.1 ; AT4G17895.1 ; AT4G17895 .
GeneIDi 827513.
KEGGi ath:AT4G17895.

Organism-specific databases

GeneFarmi 1993. 220.
TAIRi AT4G17895.

Phylogenomic databases

eggNOGi COG5533.
HOGENOMi HOG000154757.
InParanoidi Q9FPS7.
KOi K11855.
OMAi IERATIR.
PhylomeDBi Q9FPS7.

Enzyme and pathway databases

BioCyci ARA:AT4G17895-MONOMER.

Gene expression databases

Genevestigatori Q9FPS7.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2000) [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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-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: September 3, 2014
This is version 70 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