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Q9ZSB5

- UBP10_ARATH

UniProt

Q9ZSB5 - UBP10_ARATH

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Protein

Ubiquitin carboxyl-terminal hydrolase 10

Gene

UBP10

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei313 – 3131NucleophilePROSITE-ProRule annotation
Active sitei853 – 8531Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: InterPro

GO - Biological processi

  1. protein deubiquitination Source: InterPro
  2. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciARA:AT4G10570-MONOMER.

Protein family/group databases

MEROPSiC19.A02.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:UBP10
Ordered Locus Names:At4g10570
ORF Names:F3H7.5, T4F9.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G10570.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 923923Ubiquitin carboxyl-terminal hydrolase 10PRO_0000313037Add
BLAST

Proteomic databases

PaxDbiQ9ZSB5.
PRIDEiQ9ZSB5.

Expressioni

Gene expression databases

GenevestigatoriQ9ZSB5.

Structurei

3D structure databases

ProteinModelPortaliQ9ZSB5.
SMRiQ9ZSB5. Positions 29-227, 302-483, 747-894.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 134116DUSPPROSITE-ProRule annotationAdd
BLAST
Domaini304 – 895592USPAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi232 – 2376Poly-Ser

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 DUSP domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiCOG5560.
HOGENOMiHOG000264375.
InParanoidiQ9ZSB5.
KOiK11835.
OMAiGRIKRTA.
PhylomeDBiQ9ZSB5.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR028134. USP.
[Graphical view]
PANTHERiPTHR24006:SF360. PTHR24006:SF360. 1 hit.
PfamiPF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZSB5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTIPNSDFML ENGVCDLPFT PEEEKRIVSE LTSESEDNLK QGNLYFVISK
60 70 80 90 100
RWYTSWQEYV ENSANECSTG ESSEAPRPGP IDNHDIIESD SDINDPQLRR
110 120 130 140 150
LLVEGEDYVL VPKQVWKRLV EWYSGGPPIE RKLICQGFYT RSYSVEVYPL
160 170 180 190 200
CLMLTDGRDE SRTVIRLGKQ ASIRELYEKV CAMTGVPQEK AHIWDYFDKR
210 220 230 240 250
KNGLLDPLSY KSLEESSLHM DQDILVEVDG LSSSSQSAMS STGNELALVP
260 270 280 290 300
LEPSRSIVTI AGGPTLSNGH STTSNFSLFP RITSEDDGRD SLSILGKGEK
310 320 330 340 350
GGLAGLSNLG NTCFMNSALQ CLAHTPPIVE YFLQDYSDDI NRDNPLGMCG
360 370 380 390 400
ELAIAFGDLL KKLWSSGRNA VAPRAFKTKL ARFAPQFSGY NQHDSQELLA
410 420 430 440 450
FLLDGLHEDL NKVKRKPYIE LKDSDSRPDD EVAEELWNYH KARNDSVIVD
460 470 480 490 500
VCQGQYKSTL VCPVCGKISI TFDPFMYLSV PLPSTLTRSM TITVFYCDGS
510 520 530 540 550
RLPMPYTVIV PKQGSIRDLI TALGTACCLA EDESLLLAEV YDHKIFRYFE
560 570 580 590 600
IPLDSLSAIK DDEHIVAYRL NQIPKGSRKA KLEILHGGQE RAVLDSVRGS
610 620 630 640 650
DVKLFGTPFV TYVNTEPLSG TDIDAVISGF LSPLHKVHAP SKIHNGSDNG
660 670 680 690 700
HLADATVDQA SGILSSPDTE IDNASDRELS FRIFLTDERG LNIKPLQSES
710 720 730 740 750
SISPGTVTRV LVEWNEGEHE RYDSSYLSDL PEVHKTSFSA KKTRQESISL
760 770 780 790 800
FSCLEAFLAE EPLGPDDMWF CPSCKEHRQA NKKLDLWKLP DILVFHLKRF
810 820 830 840 850
TYSRYLKNKI DTFVNFPVHD LDLSKYVKNK NGQSYLYELY AVSNHYGGLG
860 870 880 890 900
GGHYTAYAKL IDDNKWYHFD DSHVSSVNES EIRNSAAYVL FYRRVRSETE
910 920
TQTAEMSTDM DYSCLNSHND KAS
Length:923
Mass (Da):103,699
Last modified:January 15, 2008 - v2
Checksum:iBF90A1E6CFB474AF
GO

Sequence cautioni

The sequence AAD03433.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BT004132 differs from that shown. Reason: Frameshift at position 921. Curated
The sequence CAB40023.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB78180.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT04192.
RefSeqiNP_192795.3. NM_117125.3.
UniGeneiAt.48842.

Genome annotation databases

EnsemblPlantsiAT4G10570.1; AT4G10570.1; AT4G10570.
GeneIDi826649.
KEGGiath:AT4G10570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRi T04192.
RefSeqi NP_192795.3. NM_117125.3.
UniGenei At.48842.

3D structure databases

ProteinModelPortali Q9ZSB5.
SMRi Q9ZSB5. Positions 29-227, 302-483, 747-894.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C19.A02.

Proteomic databases

PaxDbi Q9ZSB5.
PRIDEi Q9ZSB5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G10570.1 ; AT4G10570.1 ; AT4G10570 .
GeneIDi 826649.
KEGGi ath:AT4G10570.

Organism-specific databases

TAIRi AT4G10570.

Phylogenomic databases

eggNOGi COG5560.
HOGENOMi HOG000264375.
InParanoidi Q9ZSB5.
KOi K11835.
OMAi GRIKRTA.
PhylomeDBi Q9ZSB5.

Enzyme and pathway databases

BioCyci ARA:AT4G10570-MONOMER.

Gene expression databases

Genevestigatori Q9ZSB5.

Family and domain databases

Gene3Di 3.30.2230.10. 1 hit.
InterProi IPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR028134. USP.
[Graphical view ]
PANTHERi PTHR24006:SF360. PTHR24006:SF360. 1 hit.
Pfami PF06337. DUSP. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view ]
SMARTi SM00695. DUSP. 1 hit.
[Graphical view ]
SUPFAMi SSF143791. SSF143791. 1 hit.
PROSITEi PS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiUBP10_ARATH
AccessioniPrimary (citable) accession number: Q9ZSB5
Secondary accession number(s): Q9T0B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: October 1, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3