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Q9ZSB5 (UBP10_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. 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 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length923 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 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 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 – 923923Ubiquitin carboxyl-terminal hydrolase 10
PRO_0000313037

Regions

Domain19 – 134116DUSP
Domain304 – 895592USP
Compositional bias232 – 2376Poly-Ser

Sites

Active site3131Nucleophile By similarity
Active site8531Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZSB5 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: BF90A1E6CFB474AF

FASTA923103,699
        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 

« 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: 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.
PIRT04192.
RefSeqNP_192795.3. NM_117125.3.
UniGeneAt.48842.

3D structure databases

ProteinModelPortalQ9ZSB5.
SMRQ9ZSB5. Positions 29-227, 302-483, 747-894.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC19.A02.

Proteomic databases

PaxDbQ9ZSB5.
PRIDEQ9ZSB5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G10570.1; AT4G10570.1; AT4G10570.
GeneID826649.
KEGGath:AT4G10570.

Organism-specific databases

TAIRAT4G10570.

Phylogenomic databases

eggNOGCOG5560.
HOGENOMHOG000264375.
InParanoidQ9ZSB5.
KOK11835.
OMAGRIKRTA.
PhylomeDBQ9ZSB5.

Enzyme and pathway databases

BioCycARA:AT4G10570-MONOMER.

Gene expression databases

GenevestigatorQ9ZSB5.

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 nameUBP10_ARATH
AccessionPrimary (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: June 11, 2014
This is version 84 of the entry and version 2 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