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Q9SCJ9 (UBP26_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 83. 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 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1067 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. 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.

Contains 1 USP domain.

Sequence caution

The sequence CAB62464.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   DomainRepeat
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processseed development

Inferred from mutant phenotype PubMed 18723879. Source: TAIR

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleolus

Inferred from direct assay PubMed 15496452. Source: TAIR

   Molecular_functionubiquitin-specific protease activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10671067Ubiquitin carboxyl-terminal hydrolase 26
PRO_0000293492

Regions

Domain106 – 442337USP
Domain503 – 59593DUSP 1
Domain610 – 711102DUSP 2
Domain738 – 861124DUSP 3
Domain948 – 103184Ubiquitin-like
Compositional bias392 – 43241Ser-rich

Sites

Active site1151Nucleophile
Active site3591Proton acceptor By similarity

Experimental info

Mutagenesis1151C → S: Loss of activity. Ref.2
Sequence conflict9351E → G in AAG42764. Ref.1
Sequence conflict9891G → E in AAG42764. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9SCJ9 [UniParc].

Last modified May 3, 2011. Version 3.
Checksum: C0338D496C035573

FASTA1,067119,934
        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 

« 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.
[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. expand/collapse author list , 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.
PIRT46237.
RefSeqNP_566922.1. NM_114820.3.
UniGeneAt.22294.

3D structure databases

ProteinModelPortalQ9SCJ9.
SMRQ9SCJ9. Positions 107-390, 966-1019.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC19.A35.

Proteomic databases

PaxDbQ9SCJ9.
PRIDEQ9SCJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G49600.1; AT3G49600.1; AT3G49600.
GeneID824122.
KEGGath:AT3G49600.

Organism-specific databases

TAIRAT3G49600.

Phylogenomic databases

eggNOGCOG5077.
HOGENOMHOG000090485.
InParanoidQ9SCJ9.
KOK11858.
OMALADMNIF.

Enzyme and pathway databases

BioCycARA:AT3G49600-MONOMER.

Gene expression databases

GenevestigatorQ9SCJ9.

Family and domain databases

Gene3D3.30.2230.10. 1 hit.
InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMSSF143791. SSF143791. 2 hits.
SSF54236. SSF54236. 1 hit.
PROSITEPS51283. DUSP. 3 hits.
PS50053. UBIQUITIN_2. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBP26_ARATH
AccessionPrimary (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: June 11, 2014
This is version 83 of the entry and version 3 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