Q9SCJ9 (UBP26_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 26
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 26
Short name=AtUBP26
Ubiquitin thioesterase 26
Ubiquitin-specific-processing protease 26

Gene names

Name:	UBP26
Synonyms:	SUP32
Ordered Locus Names:	At3g49600
ORF Names:	T9C5.190

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	1067 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. Deubiquitinates H2BK143ub1 of histone H2B. Ref.2
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).
Subcellular location	Nucleus Ref.2.
Tissue specificity	Expressed in seedlings, roots, stems, leaves and inflorescences. Ref.2
Sequence similarities	Belongs to the peptidase C19 family. Contains 3 DUSP domains. Contains 1 ubiquitin-like domain.
Sequence caution	The sequence CAB62464.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Domain	Repeat
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	seed development Inferred from mutant phenotype PubMed 18723879. Source: TAIR ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleolus Inferred from direct assay PubMed 15496452. 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 – 1067	1067	Ubiquitin carboxyl-terminal hydrolase 26		PRO_0000293492
Regions
	Domain	503 – 595	93	DUSP 1
	Domain	610 – 711	102	DUSP 2
	Domain	738 – 861	124	DUSP 3
	Domain	948 – 1031	84	Ubiquitin-like
	Compositional bias	392 – 432	41	Ser-rich
Sites
	Active site	115	1	Nucleophile
	Active site	359	1	Proton acceptor By similarity
Experimental info
	Mutagenesis	115	1	C → S: Loss of activity. Ref.2
	Sequence conflict	935	1	E → G in AAG42764. Ref.1
	Sequence conflict	989	1	G → E in AAG42764. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9SCJ9 [UniParc]. Last modified May 3, 2011. Version 3. Checksum: C0338D496C035573	FASTA	1,067	119,934
	10 20 30 40 50 60 MSRPNTRNKN KRQRPDAVDS SSQILRKIHE ANDVTDDDIN QLFMIWKPVC QGCRVNTRDN 70 80 90 100 110 120 PNCFCGLVPP LNGSRKSGLW QKTSEIIQSL GPDPTLDRRD SESTPAGLTN LGATCYANSI 130 140 150 160 170 180 LQCLYMNTAF REGVFSVEVH VLKQNPVLDQ IARLFAQLHA SQKSFVDSDA FVKTLELDNG 190 200 210 220 230 240 VQQDTHEFLT LLLSLLERCL LHSGVKAKTI VQDLFSGSVS HVTTCSKCGR DSEASSKMED 250 260 270 280 290 300 FYALELNVKG LKSLDASLND YLSLEQLNGD NQYFCGSCNA RVDATRCIKL RTLPPVITFQ 310 320 330 340 350 360 LKRCIFLPKT TAKKKITSSF SFPQVLDMGS RLAESSQNKL TYDLSAVLIH KGSAVNSGHY 370 380 390 400 410 420 VAHIKDEKTG LWWEFDDEHV SELGKRPCNE ASSSTPQSES NGTASSGNIT DGIQSGSSDC 430 440 450 460 470 480 RSAIKSEVFS SSDAYMLMYS LRCDKQENQE GQKENPIDIT KGEVKQLKGG YLPKHLSEWI 490 500 510 520 530 540 NNMNAVFLES CKQYNLRKEK ELNALTERRQ EVRTILSEAA VQSLEEQYFW ISTDWLRLWA 550 560 570 580 590 600 DTTLPPALDN TPLLCSHGKV HASKVNCMKR ISELAWIKLE SKFNGGPKLG KGDYCRDCLM 610 620 630 640 650 660 DGARMVVSSD SYRDRRTFMK SIANDVLSGK CEDGMYYISR AWLQQWIKRK NLDAPTEADA 670 680 690 700 710 720 GPTNAITCNH GELMPEQAPG AKRVVVPENF WSFLFEDALK VMSEDTLDCT CFPVDSSQCC 730 740 750 760 770 780 HCTEVLSEVA CFEDSLRTLK VKQRQNHEKL ATGKGIPLTP QSRYFLLPSP WLVQWRIYIN 790 800 810 820 830 840 MTGKNSSSAP EPERLDGVIN TLKCKKHTRL LERLPELVCR RGSYFQKNPS TDKLTIIPEL 850 860 870 880 890 900 DWKYFCDEWG GLMENGISAF IEVGNTDQSS SPDVIDLEKD SSPDDNMDVD AQQLILRASP 910 920 930 940 950 960 EICEECIGER ESCELMQKLS YSEGDVFVCF VRGKEAPKAM LEASDSSFEV DRRTSKRSRR 970 980 990 1000 1010 1020 TNYGNLTSLK VSATTTVYQL KMMIWELLGV MKENQELHKG SKVIDQESAT LADMNIFPGD 1030 1040 1050 1060 RLWVRDTEMH EHRDIADELC EKKPGAQDIE EGFRGTLLTG NISSEAC

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.
[2]	"Control of DNA methylation and heterochromatic silencing by histone H2B deubiquitination." Sridhar V.V., Kapoor A., Zhang K., Zhu J., Zhou T., Hasegawa P.M., Bressan R.A., Zhu J.-K. Nature 447:735-738(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-115, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF302674 mRNA. Translation: AAG42764.1. AL132964 Genomic DNA. Translation: CAB62464.1. Sequence problems. CP002686 Genomic DNA. Translation: AEE78564.1.
IPI	IPI00546690.
PIR	T46237.
RefSeq	NP_566922.1. NM_114820.3.
UniGene	At.22294.
3D structure databases
HSSP	HSSP built from PDB template 2AYN based on UniProtKB P54578.
ProteinModelPortal	Q9SCJ9.
SMR	Q9SCJ9. Positions 107-390, 961-1025.
ModBase	Search...
Protein family/group databases
MEROPS	C19.068.
Proteomic databases
PaxDb	Q9SCJ9.
PRIDE	Q9SCJ9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G49600.1; AT3G49600.1; AT3G49600.
GeneID	824122.
KEGG	ath:AT3G49600.
Organism-specific databases
TAIR	At3g49600.
Phylogenomic databases
eggNOG	COG5077.
HOGENOM	HOG000090485.
InParanoid	Q9SCJ9.
KO	K11858.
OMA	EECIGER.
Gene expression databases
Genevestigator	Q9SCJ9.
Family and domain databases
InterPro	IPR006615. Pept_C19_DUSP. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR019955. Ubiquitin_supergroup. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
SMART	SM00695. DUSP. 1 hit. [Graphical view]
PROSITE	PS51283. DUSP. 3 hits. PS00299. UBIQUITIN_1. False negative. PS50053. UBIQUITIN_2. 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

UBP26_ARATH

Accession

Primary (citable) accession number: Q9SCJ9
Secondary accession number(s): Q9FPS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	May 3, 2011
Last modified:	May 1, 2013
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program