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Q9FPS3

- UBP24_ARATH

UniProt

Q9FPS3 - UBP24_ARATH

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Protein

Ubiquitin carboxyl-terminal hydrolase 24

Gene

UBP24

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein 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 sitei206 – 2061NucleophilePROSITE-ProRule annotation
Active sitei510 – 5101Proton 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:AT4G30890-MONOMER.
ARA:GQT-738-MONOMER.
ARA:GQT-739-MONOMER.

Protein family/group databases

MEROPSiC19.A14.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 24 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 24
Short name:
AtUBP24
Ubiquitin thioesterase 24
Ubiquitin-specific-processing protease 24
Gene namesi
Name:UBP24
Ordered Locus Names:At4g30890
ORF Names:F6I18.200
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G30890.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Ubiquitin carboxyl-terminal hydrolase 24PRO_0000313050Add
BLAST

Proteomic databases

PaxDbiQ9FPS3.
PRIDEiQ9FPS3.

Expressioni

Gene expression databases

ExpressionAtlasiQ9FPS3. baseline and differential.
GenevestigatoriQ9FPS3.

Structurei

3D structure databases

ProteinModelPortaliQ9FPS3.
SMRiQ9FPS3. Positions 198-549.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini197 – 551355USPAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000084329.
InParanoidiQ9FPS3.
KOiK11841.
OMAiSKIMILH.
PhylomeDBiQ9FPS3.

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.

Q9FPS3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEKKVFVFG SFTEHETRSF FEQKPTKDPQ NSKDKCVGSI QFGSLNLAAE
60 70 80 90 100
NSSVNTNGEL KKGEADGTVK SAGSQERLDA SRPASSDKNN DSDAKLPRKN
110 120 130 140 150
SLRVPEHVVQ NGIIKEISES NKSLNNGVAV KTDPIGLDNL SMSDGESDPV
160 170 180 190 200
YKASSSKFQA LDNEDFSSDS SSGSIQRKKN LKVPTESVPP VKDFTPRGLI
210 220 230 240 250
NAGNLCFLNA TLQALLSCSP FVQLLQKIQL QDIPKADSPT LAAFSEFISE
260 270 280 290 300
LDVPSSSSIR NNVTVVEAGR PFRPAMFEGV LRNFTPDVLN NMSGRPRQED
310 320 330 340 350
AQEFLSFIMD QMHDELLKLK EQSPKVTASK SSVISSANDD GDEWETVGPK
360 370 380 390 400
NKSAVTRTQS FVPSELSEIF GGQLKSVVKA KGTKASATVQ PYLLLHLDIH
410 420 430 440 450
PDGVQGIEDA LHLFSAQEDL EGYRASVTGK TGVVSASKSI KIQKLSKIMI
460 470 480 490 500
LHLMRFSYGS QGSTKLRKGV KFPLELNLNR SHLVSLSNES LRYELVATIT
510 520 530 540 550
HHGWDPSKGH YTTDARRKNG QWLRFDDASV TPIGTKLVLH DQAYVLFYKQ

V
Length:551
Mass (Da):60,440
Last modified:March 1, 2001 - v1
Checksum:iC4211FEC7E931AD9
GO

Sequence cautioni

The sequence AAM83229.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA18204.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAB79807.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF302672 mRNA. Translation: AAG42762.1.
AL022198 Genomic DNA. Translation: CAA18204.1. Sequence problems.
AL161577 Genomic DNA. Translation: CAB79807.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85824.1.
CP002687 Genomic DNA. Translation: AEE85825.1.
CP002687 Genomic DNA. Translation: AEE85826.1.
AY127002 mRNA. Translation: AAM83229.1. Different initiation.
BT000568 mRNA. Translation: AAN18137.1.
PIRiF85361.
RefSeqiNP_001190875.1. NM_001203946.1.
NP_567860.1. NM_119236.3.
NP_974644.1. NM_202915.1.
UniGeneiAt.22252.

Genome annotation databases

EnsemblPlantsiAT4G30890.1; AT4G30890.1; AT4G30890.
AT4G30890.2; AT4G30890.2; AT4G30890.
AT4G30890.3; AT4G30890.3; AT4G30890.
GeneIDi829213.
KEGGiath:AT4G30890.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF302672 mRNA. Translation: AAG42762.1 .
AL022198 Genomic DNA. Translation: CAA18204.1 . Sequence problems.
AL161577 Genomic DNA. Translation: CAB79807.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE85824.1 .
CP002687 Genomic DNA. Translation: AEE85825.1 .
CP002687 Genomic DNA. Translation: AEE85826.1 .
AY127002 mRNA. Translation: AAM83229.1 . Different initiation.
BT000568 mRNA. Translation: AAN18137.1 .
PIRi F85361.
RefSeqi NP_001190875.1. NM_001203946.1.
NP_567860.1. NM_119236.3.
NP_974644.1. NM_202915.1.
UniGenei At.22252.

3D structure databases

ProteinModelPortali Q9FPS3.
SMRi Q9FPS3. Positions 198-549.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C19.A14.

Proteomic databases

PaxDbi Q9FPS3.
PRIDEi Q9FPS3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G30890.1 ; AT4G30890.1 ; AT4G30890 .
AT4G30890.2 ; AT4G30890.2 ; AT4G30890 .
AT4G30890.3 ; AT4G30890.3 ; AT4G30890 .
GeneIDi 829213.
KEGGi ath:AT4G30890.

Organism-specific databases

TAIRi AT4G30890.

Phylogenomic databases

eggNOGi COG5533.
HOGENOMi HOG000084329.
InParanoidi Q9FPS3.
KOi K11841.
OMAi SKIMILH.
PhylomeDBi Q9FPS3.

Enzyme and pathway databases

BioCyci ARA:AT4G30890-MONOMER.
ARA:GQT-738-MONOMER.
ARA:GQT-739-MONOMER.

Miscellaneous databases

PROi Q9FPS3.

Gene expression databases

ExpressionAtlasi Q9FPS3. baseline and differential.
Genevestigatori Q9FPS3.

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.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 274-551.
    Strain: cv. Columbia.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Root.
  6. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  7. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBP24_ARATH
AccessioniPrimary (citable) accession number: Q9FPS3
Secondary accession number(s): O65560, Q8L7U2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 80 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