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Q93Y01 (UBP9_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. 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 9

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 9
Short name=AtUBP9
Ubiquitin thioesterase 9
Ubiquitin-specific-processing protease 9
Gene names
Name:UBP9
Ordered Locus Names:At4g10590
ORF Names:F3H7.7, T4F9.50
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length910 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Contains 1 USP domain.

Sequence caution

The sequence AAD03434.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB40025.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB78182.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   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 – 910910Ubiquitin carboxyl-terminal hydrolase 9
PRO_0000313036

Regions

Domain19 – 134116DUSP
Domain303 – 894592USP
Compositional bias231 – 2366Poly-Ser

Sites

Active site3121Nucleophile By similarity
Active site8521Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q93Y01 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: E01B0AD928A8EE71

FASTA910102,649
        10         20         30         40         50         60 
MTIPNSDFMI ENGVCDFPTT PEEEKRIVSE LITESEDNLK EGNLYFVISK RWYTSWEKYV 

        70         80         90        100        110        120 
EQSTKEYISG ESSEASRPGP IDNHDIIESE SDVNDPQLRR LLMERVDYVL VPQEVWKRLV 

       130        140        150        160        170        180 
EWYSGGPPIE RKLICQGFYT RSYSVEVYPL CLMLTDGRDE SRTVIRLGKQ ASIRELYEKV 

       190        200        210        220        230        240 
CALTGVPQEK AHIWDYFDKR KNGLLDSLSY KSLEESSLHM DQDILLEVDG SSSSQSAMSS 

       250        260        270        280        290        300 
TGNELALVPL EPSRSSVTIA GGPTLSNGHS TTSNFSLFPR ITSEDDGSNS LSILGKGEKG 

       310        320        330        340        350        360 
GLAGLSNLGN TCFMNSALQC LAHTPPIVEY FLQDYSDDIN RDNPLGMCGE LAIAFGDLLK 

       370        380        390        400        410        420 
KLWSSGRNSV APRAFKTKLA RFAPQFSGYN QHDSQELLAF LLDGLHEDLN KVKRKPYIEL 

       430        440        450        460        470        480 
KDSDSRPDDE VAEELWNYHK ARNDSVIVDV CQGQYKSTLV CPACGKISIT FDPFMYLSVP 

       490        500        510        520        530        540 
LPSTLTRSMT VTVFYCDGSH LPMPYTVIVP KNGSIRDLIT ALGTACLLAE DESLLLAEVY 

       550        560        570        580        590        600 
DHKIFKYFEN PLDSLSSIKD DEHIVAYRLN QMPKGSGKAK LEILHGGQKR PILESVRGRD 

       610        620        630        640        650        660 
VKLFGTPFVT YVNTEPLSGA DIDAVLSRFL SPLHKVHAPS KIHNGSENGH LPDATVDEAS 

       670        680        690        700        710        720 
EILSSPDTEI DDASDRELSF RIFLTDERGL NFKPLQSESS ISLGIATRVL VEWNEGEHER 

       730        740        750        760        770        780 
YDSSYLSDLP EVHKTSFSAK KTRQESISLF SCLEAFLAEE PLGPDDMWFC PSCKEHRQAN 

       790        800        810        820        830        840 
KKLDLWKLPD ILVFHLKRFT YSRYLKNKID TFVNFPVHDL DLSKYVKNKN DQSYLYELYA 

       850        860        870        880        890        900 
VSNHYGGLGG GHYTAYAKLI DDNEWYHFDD SHVSSVNESE IKNSAAYVLF YRRVRSETET 

       910 
QTVEMSTDMD 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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: AAD03434.1. Sequence problems.
AL049523 Genomic DNA. Translation: CAB40025.1. Sequence problems.
AL161517 Genomic DNA. Translation: CAB78182.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82901.1.
CP002687 Genomic DNA. Translation: AEE82902.1.
AY054463 mRNA. Translation: AAK96655.1.
BT010363 mRNA. Translation: AAQ56806.1.
PIRT04194.
RefSeqNP_567363.1. NM_117127.2.
NP_849356.1. NM_179025.1.
UniGeneAt.10964.
At.67146.

3D structure databases

ProteinModelPortalQ93Y01.
SMRQ93Y01. Positions 29-227, 301-482, 746-893.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC19.A03.

Proteomic databases

PaxDbQ93Y01.
PRIDEQ93Y01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G10590.1; AT4G10590.1; AT4G10590.
AT4G10590.2; AT4G10590.2; AT4G10590.
GeneID826651.
KEGGath:AT4G10590.

Organism-specific databases

TAIRAT4G10590.

Phylogenomic databases

eggNOGCOG5560.
HOGENOMHOG000264375.
InParanoidQ93Y01.
KOK11835.
OMADKEHELY.
PhylomeDBQ93Y01.

Enzyme and pathway databases

BioCycARA:AT4G10590-MONOMER.
ARA:GQT-1184-MONOMER.

Gene expression databases

GenevestigatorQ93Y01.

Family and domain databases

Gene3D3.30.2230.10. 1 hit.
InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR028134. USP.
[Graphical view]
PANTHERPTHR24006:SF360. PTHR24006:SF360. 1 hit.
PfamPF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMSSF143791. SSF143791. 1 hit.
PROSITEPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBP9_ARATH
AccessionPrimary (citable) accession number: Q93Y01
Secondary accession number(s): Q9T0B8, Q9ZSB6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 87 of the entry and version 1 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