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Q9FPS3 (UBP24_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:UBP24
Ordered Locus Names:At4g30890
ORF Names:F6I18.200
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length551 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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).

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleus

Inferred from direct assay Ref.5. Source: TAIR

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 551551Ubiquitin carboxyl-terminal hydrolase 24
PRO_0000313050

Regions

Domain197 – 551355USP

Sites

Active site2061Nucleophile By similarity
Active site5101Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9FPS3 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: C4211FEC7E931AD9

FASTA55160,440
        10         20         30         40         50         60 
MSEKKVFVFG SFTEHETRSF FEQKPTKDPQ NSKDKCVGSI QFGSLNLAAE NSSVNTNGEL 

        70         80         90        100        110        120 
KKGEADGTVK SAGSQERLDA SRPASSDKNN DSDAKLPRKN SLRVPEHVVQ NGIIKEISES 

       130        140        150        160        170        180 
NKSLNNGVAV KTDPIGLDNL SMSDGESDPV YKASSSKFQA LDNEDFSSDS SSGSIQRKKN 

       190        200        210        220        230        240 
LKVPTESVPP VKDFTPRGLI NAGNLCFLNA TLQALLSCSP FVQLLQKIQL QDIPKADSPT 

       250        260        270        280        290        300 
LAAFSEFISE LDVPSSSSIR NNVTVVEAGR PFRPAMFEGV LRNFTPDVLN NMSGRPRQED 

       310        320        330        340        350        360 
AQEFLSFIMD QMHDELLKLK EQSPKVTASK SSVISSANDD GDEWETVGPK NKSAVTRTQS 

       370        380        390        400        410        420 
FVPSELSEIF GGQLKSVVKA KGTKASATVQ PYLLLHLDIH PDGVQGIEDA LHLFSAQEDL 

       430        440        450        460        470        480 
EGYRASVTGK TGVVSASKSI KIQKLSKIMI LHLMRFSYGS QGSTKLRKGV KFPLELNLNR 

       490        500        510        520        530        540 
SHLVSLSNES LRYELVATIT HHGWDPSKGH YTTDARRKNG QWLRFDDASV TPIGTKLVLH 

       550 
DQAYVLFYKQ V 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis."
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.
J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRF85361.
RefSeqNP_001190875.1. NM_001203946.1.
NP_567860.1. NM_119236.3.
NP_974644.1. NM_202915.1.
UniGeneAt.22252.

3D structure databases

ProteinModelPortalQ9FPS3.
SMRQ9FPS3. Positions 198-549.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC19.A14.

Proteomic databases

PaxDbQ9FPS3.
PRIDEQ9FPS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G30890.1; AT4G30890.1; AT4G30890.
AT4G30890.2; AT4G30890.2; AT4G30890.
AT4G30890.3; AT4G30890.3; AT4G30890.
GeneID829213.
KEGGath:AT4G30890.

Organism-specific databases

TAIRAT4G30890.

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000084329.
InParanoidQ9FPS3.
KOK11841.
OMASKIMILH.
PhylomeDBQ9FPS3.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorQ9FPS3.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9FPS3.

Entry information

Entry nameUBP24_ARATH
AccessionPrimary (citable) accession number: Q9FPS3
Secondary accession number(s): O65560, Q8L7U2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2001
Last modified: May 14, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names