Q9C585 (UBP8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 8
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 8
Short name=AtUBP8
Ubiquitin thioesterase 8
Ubiquitin-specific-processing protease 8

Gene names

Name:	UBP8
Ordered Locus Names:	At5g22030
ORF Names:	T6G21.4

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	871 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. Contains 1 DUSP domain.
Sequence caution	The sequence AED92970.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AED92971.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE98798.1 differs from that shown. Reason: Probable cloning artifact leading to an insertion into the sequence. The sequence CAC34496.1 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
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 – 871	871	Ubiquitin carboxyl-terminal hydrolase 8		PRO_0000313035
Regions
	Domain	4 – 99	96	DUSP
Sites
	Active site	288	1	Nucleophile By similarity
	Active site	828	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	263	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	414	1	N → P in AAG42753. Ref.4
	Sequence conflict	618	1	E → K in BAE98798. Ref.3
	Sequence conflict	703	1	L → F in AAG42753. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9C585 [UniParc]. Last modified September 1, 2009. Version 2. Checksum: A669206C1AA3C5F6	FASTA	871	98,171
	10 20 30 40 50 60 MNGTSPDESP DSTTQRIDSF NGEQRVYFVP LRWWKDAQDS MPSESVEKRE ILYTASCGSS 70 80 90 100 110 120 YGGPMKLINN IFNSDILFDL RREGDALQNG ETGEASVSGR DFALVSSDMW LQALKWYHDD 130 140 150 160 170 180 KNTEKGVKSF SAGGVDRGDV YPVQLRLSVL QETNSLAVKI CKKDNSVECF RRACKIFSLD 190 200 210 220 230 240 SEQLRIWDIS GQTTLFFESD VSNSKDCQQQ ADQEILLELQ IYGLSDSIKL KESKKEDGST 250 260 270 280 290 300 QQTNGITNGM NGGTVFRFGR SNSLSFLGKA GEAGTLGLTG LQNLGNTCFM NSSLQCLAHT 310 320 330 340 350 360 PKLVDFFLGE YSKEINLDNP LGMKGEIALA FGDLLRSLWA PGASTVAPRT FKAKLARFAP 370 380 390 400 410 420 QFSGFNQHDS QELLAFLLDG LHEDLNRVKN KPYVEAKDGD GRPDAEVADE YWRNHVARND 430 440 450 460 470 480 SIIVDVCQGQ YKSTLVCPIC KKVSVMFDPF MYLSLPLPCT SMRTMDLTVM SADGSSLPIP 490 500 510 520 530 540 LTVNVPKFGK FEDLHKALVT ACSLPEEETL LVTEVYNNRI IRFLEEPTDS LTLIRDGDKL 550 560 570 580 590 600 VVYRLKKDAN NSPLIVYMHQ KLEEQFISGK SSPTWKAFGI PLVSRLCDVE NGSDVENLYL 610 620 630 640 650 660 KLLSSFKMPT EFFTENLENP TEEEATDKTD TDGTTSVEDT NSTDVKETTE SLPDPVLRLY 670 680 690 700 710 720 LTDDRGNSIE AEMLKEKPVN KSKRLNVLAR WPVKELDVYD TCLLSSLPEV SKSGTKRPQE 730 740 750 760 770 780 SVSLFKCLEA FLTEEPLGPD DMWYCPGCKE HRQAIKKLDL WRLPEILVIH LKRFSYSRFM 790 800 810 820 830 840 KNKLEAYVDF PLDNLDLSSY ISYKNGQTTY RYMLYAISNH YGSMGGGHYT AYVHHGGDRW 850 860 870 YDFDDSHVHQ ISQEKIKTSA AYVLFYKRLV D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [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]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases 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: NUCLEOTIDE SEQUENCE [MRNA] OF 402-871, GENE FAMILY ORGANIZATION, NOMENCLATURE. Strain: cv. Columbia.
[5]	"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-263, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL589883 Genomic DNA. Translation: CAC34496.1. Sequence problems. CP002688 Genomic DNA. Translation: AED92970.1. Sequence problems. CP002688 Genomic DNA. Translation: AED92971.1. Sequence problems. AK226691 mRNA. Translation: BAE98798.1. Sequence problems. AF302662 mRNA. Translation: AAG42753.1.
IPI	IPI00547490. IPI01019477.
RefSeq	NP_568411.4. NM_122126.5. NP_851052.4. NM_180721.4.
UniGene	At.23027.
3D structure databases
ProteinModelPortal	Q9C585.
SMR	Q9C585. Positions 277-505, 721-871.
ModBase	Search...
Protein family/group databases
MEROPS	C19.A01.
Proteomic databases
PaxDb	Q9C585.
PRIDE	Q9C585.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	832263.
KEGG	ath:AT5G22030.
Organism-specific databases
TAIR	At5g22030.
Phylogenomic databases
eggNOG	COG5560.
InParanoid	Q9C585.
KO	K11835.
PhylomeDB	Q9C585.
Gene expression databases
Genevestigator	Q9C585.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS51283. DUSP. False negative. 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

UBP8_ARATH

Accession

Primary (citable) accession number: Q9C585
Secondary accession number(s): F4K8E0, Q0WVQ0, Q9FPT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 1, 2009
Last modified:	May 29, 2013
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program