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Q9FPS7

- UBP20_ARATH

UniProt

Q9FPS7 - UBP20_ARATH

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Protein

Ubiquitin carboxyl-terminal hydrolase 20

Gene

UBP20

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.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 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 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.
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

        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.
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: October 1, 2014
This is version 71 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