Q9FPS3 (UBP24_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	UBP24
Ordered Locus Names:	At4g30890
ORF Names:	F6I18.200

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	551 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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 process	Ubl conjugation pathway
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleus Inferred from direct assay PubMed 18433157. Source: TAIR
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 551	551	Ubiquitin carboxyl-terminal hydrolase 24		PRO_0000313050
Sites
	Active site	206	1	Nucleophile By similarity
	Active site	510	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	85	1	Phosphoserine Ref.6
	Modified residue	143	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9FPS3 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: C4211FEC7E931AD9	FASTA	551	60,440
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, MASS SPECTROMETRY. Strain: cv. Columbia.
[6]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	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.
IPI	IPI00539881.
PIR	F85361.
RefSeq	NP_001190875.1. NM_001203946.1. NP_567860.1. NM_119236.3. NP_974644.1. NM_202915.1.
UniGene	At.22252.
3D structure databases
HSSP	HSSP built from PDB template 2AYN based on UniProtKB P54578.
ProteinModelPortal	Q9FPS3.
SMR	Q9FPS3. Positions 198-549.
ModBase	Search...
Protein family/group databases
MEROPS	C19.A14.
Proteomic databases
PaxDb	Q9FPS3.
PRIDE	Q9FPS3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G30890.1; AT4G30890.1; AT4G30890. AT4G30890.2; AT4G30890.2; AT4G30890. AT4G30890.3; AT4G30890.3; AT4G30890.
GeneID	829213.
KEGG	ath:AT4G30890.
Organism-specific databases
TAIR	At4g30890.
Phylogenomic databases
eggNOG	COG5533.
HOGENOM	HOG000084329.
InParanoid	Q9FPS3.
KO	K11841.
OMA	KIMILHL.
PhylomeDB	Q9FPS3.
ProtClustDB	CLSN2689694.
Gene expression databases
ArrayExpress	Q9FPS3.
Genevestigator	Q9FPS3.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBP24_ARATH

Accession

Primary (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 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program