Q9ZSB5 (UBP10_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 10
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 10
Short name=AtUBP10
Ubiquitin thioesterase 10
Ubiquitin-specific-processing protease 10

Gene names

Name:	UBP10
Ordered Locus Names:	At4g10570
ORF Names:	F3H7.5, T4F9.30

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	923 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 DUSP domain.
Sequence caution	The sequence AAD03433.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BT004132 differs from that shown. Reason: Frameshift at position 921. The sequence CAB40023.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78180.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
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 – 923	923	Ubiquitin carboxyl-terminal hydrolase 10		PRO_0000313037
Regions
	Domain	19 – 134	116	DUSP
	Compositional bias	232 – 237	6	Poly-Ser
Sites
	Active site	313	1	Nucleophile By similarity
	Active site	853	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZSB5 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: BF90A1E6CFB474AF	FASTA	923	103,699
	10 20 30 40 50 60 MTIPNSDFML ENGVCDLPFT PEEEKRIVSE LTSESEDNLK QGNLYFVISK RWYTSWQEYV 70 80 90 100 110 120 ENSANECSTG ESSEAPRPGP IDNHDIIESD SDINDPQLRR LLVEGEDYVL VPKQVWKRLV 130 140 150 160 170 180 EWYSGGPPIE RKLICQGFYT RSYSVEVYPL CLMLTDGRDE SRTVIRLGKQ ASIRELYEKV 190 200 210 220 230 240 CAMTGVPQEK AHIWDYFDKR KNGLLDPLSY KSLEESSLHM DQDILVEVDG LSSSSQSAMS 250 260 270 280 290 300 STGNELALVP LEPSRSIVTI AGGPTLSNGH STTSNFSLFP RITSEDDGRD SLSILGKGEK 310 320 330 340 350 360 GGLAGLSNLG NTCFMNSALQ CLAHTPPIVE YFLQDYSDDI NRDNPLGMCG ELAIAFGDLL 370 380 390 400 410 420 KKLWSSGRNA VAPRAFKTKL ARFAPQFSGY NQHDSQELLA FLLDGLHEDL NKVKRKPYIE 430 440 450 460 470 480 LKDSDSRPDD EVAEELWNYH KARNDSVIVD VCQGQYKSTL VCPVCGKISI TFDPFMYLSV 490 500 510 520 530 540 PLPSTLTRSM TITVFYCDGS RLPMPYTVIV PKQGSIRDLI TALGTACCLA EDESLLLAEV 550 560 570 580 590 600 YDHKIFRYFE IPLDSLSAIK DDEHIVAYRL NQIPKGSRKA KLEILHGGQE RAVLDSVRGS 610 620 630 640 650 660 DVKLFGTPFV TYVNTEPLSG TDIDAVISGF LSPLHKVHAP SKIHNGSDNG HLADATVDQA 670 680 690 700 710 720 SGILSSPDTE IDNASDRELS FRIFLTDERG LNIKPLQSES SISPGTVTRV LVEWNEGEHE 730 740 750 760 770 780 RYDSSYLSDL PEVHKTSFSA KKTRQESISL FSCLEAFLAE EPLGPDDMWF CPSCKEHRQA 790 800 810 820 830 840 NKKLDLWKLP DILVFHLKRF TYSRYLKNKI DTFVNFPVHD LDLSKYVKNK NGQSYLYELY 850 860 870 880 890 900 AVSNHYGGLG GGHYTAYAKL IDDNKWYHFD DSHVSSVNES EIRNSAAYVL FYRRVRSETE 910 920 TQTAEMSTDM DYSCLNSHND KAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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]. Strain: cv. Columbia.
[4]	"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: GENE FAMILY ORGANIZATION, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF118222 Genomic DNA. Translation: AAD03433.1. Sequence problems. AL049523 Genomic DNA. Translation: CAB40023.1. Sequence problems. AL161517 Genomic DNA. Translation: CAB78180.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE82900.1. BT004132 mRNA. No translation available.
IPI	IPI00521385.
PIR	T04192.
RefSeq	NP_192795.3. NM_117125.3.
UniGene	At.48842.
3D structure databases
HSSP	HSSP built from PDB template 2GFO based on UniProtKB P40818.
ProteinModelPortal	Q9ZSB5.
SMR	Q9ZSB5. Positions 29-227, 302-483, 747-894.
ModBase	Search...
Protein family/group databases
MEROPS	C19.A02.
Proteomic databases
PaxDb	Q9ZSB5.
PRIDE	Q9ZSB5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G10570.1; AT4G10570.1; AT4G10570.
GeneID	826649.
KEGG	ath:AT4G10570.
Organism-specific databases
TAIR	At4g10570.
Phylogenomic databases
eggNOG	COG5560.
HOGENOM	HOG000264375.
InParanoid	Q9ZSB5.
KO	K11835.
OMA	ENSANEC.
PhylomeDB	Q9ZSB5.
ProtClustDB	CLSN2689389.
Gene expression databases
Genevestigator	Q9ZSB5.
Family and domain databases
InterPro	IPR006615. Pept_C19_DUSP. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF06337. DUSP. 1 hit. PF00443. UCH. 1 hit. [Graphical view]
SMART	SM00695. DUSP. 1 hit. [Graphical view]
PROSITE	PS51283. DUSP. 1 hit. 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

UBP10_ARATH

Accession

Primary (citable) accession number: Q9ZSB5
Secondary accession number(s): Q9T0B6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	May 1, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program