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Protein

Ubiquitin carboxyl-terminal hydrolase 9

Gene

UBP9

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: 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 sitei312 – 3121NucleophilePROSITE-ProRule annotation
Active sitei852 – 8521Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

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

Protein family/group databases

MEROPSiC19.A03.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:UBP9
Ordered Locus Names:At4g10590
ORF Names:F3H7.7, T4F9.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G10590.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 910910Ubiquitin carboxyl-terminal hydrolase 9PRO_0000313036Add
BLAST

Proteomic databases

PaxDbiQ93Y01.
PRIDEiQ93Y01.

Expressioni

Gene expression databases

ExpressionAtlasiQ93Y01. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G10590.1.

Structurei

3D structure databases

ProteinModelPortaliQ93Y01.
SMRiQ93Y01. Positions 29-227, 301-482, 746-893.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 134116DUSPPROSITE-ProRule annotationAdd
BLAST
Domaini303 – 894592USPAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi231 – 2366Poly-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.
InParanoidiQ93Y01.
KOiK11835.
OMAiIDENRWY.
PhylomeDBiQ93Y01.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR028134. USP.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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.

Q93Y01-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIPNSDFMI ENGVCDFPTT PEEEKRIVSE LITESEDNLK EGNLYFVISK
60 70 80 90 100
RWYTSWEKYV EQSTKEYISG ESSEASRPGP IDNHDIIESE SDVNDPQLRR
110 120 130 140 150
LLMERVDYVL VPQEVWKRLV EWYSGGPPIE RKLICQGFYT RSYSVEVYPL
160 170 180 190 200
CLMLTDGRDE SRTVIRLGKQ ASIRELYEKV CALTGVPQEK AHIWDYFDKR
210 220 230 240 250
KNGLLDSLSY KSLEESSLHM DQDILLEVDG SSSSQSAMSS TGNELALVPL
260 270 280 290 300
EPSRSSVTIA GGPTLSNGHS TTSNFSLFPR ITSEDDGSNS LSILGKGEKG
310 320 330 340 350
GLAGLSNLGN TCFMNSALQC LAHTPPIVEY FLQDYSDDIN RDNPLGMCGE
360 370 380 390 400
LAIAFGDLLK KLWSSGRNSV APRAFKTKLA RFAPQFSGYN QHDSQELLAF
410 420 430 440 450
LLDGLHEDLN KVKRKPYIEL KDSDSRPDDE VAEELWNYHK ARNDSVIVDV
460 470 480 490 500
CQGQYKSTLV CPACGKISIT FDPFMYLSVP LPSTLTRSMT VTVFYCDGSH
510 520 530 540 550
LPMPYTVIVP KNGSIRDLIT ALGTACLLAE DESLLLAEVY DHKIFKYFEN
560 570 580 590 600
PLDSLSSIKD DEHIVAYRLN QMPKGSGKAK LEILHGGQKR PILESVRGRD
610 620 630 640 650
VKLFGTPFVT YVNTEPLSGA DIDAVLSRFL SPLHKVHAPS KIHNGSENGH
660 670 680 690 700
LPDATVDEAS EILSSPDTEI DDASDRELSF RIFLTDERGL NFKPLQSESS
710 720 730 740 750
ISLGIATRVL VEWNEGEHER YDSSYLSDLP EVHKTSFSAK KTRQESISLF
760 770 780 790 800
SCLEAFLAEE PLGPDDMWFC PSCKEHRQAN KKLDLWKLPD ILVFHLKRFT
810 820 830 840 850
YSRYLKNKID TFVNFPVHDL DLSKYVKNKN DQSYLYELYA VSNHYGGLGG
860 870 880 890 900
GHYTAYAKLI DDNEWYHFDD SHVSSVNESE IKNSAAYVLF YRRVRSETET
910
QTVEMSTDMD
Length:910
Mass (Da):102,649
Last modified:December 1, 2001 - v1
Checksum:iE01B0AD928A8EE71
GO

Sequence cautioni

The sequence AAD03434.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB40025.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB78182.1 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: 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.
PIRiT04194.
RefSeqiNP_567363.1. NM_117127.2.
NP_849356.1. NM_179025.1.
UniGeneiAt.10964.
At.67146.

Genome annotation databases

EnsemblPlantsiAT4G10590.1; AT4G10590.1; AT4G10590.
AT4G10590.2; AT4G10590.2; AT4G10590.
GeneIDi826651.
KEGGiath:AT4G10590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT04194.
RefSeqiNP_567363.1. NM_117127.2.
NP_849356.1. NM_179025.1.
UniGeneiAt.10964.
At.67146.

3D structure databases

ProteinModelPortaliQ93Y01.
SMRiQ93Y01. Positions 29-227, 301-482, 746-893.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G10590.1.

Protein family/group databases

MEROPSiC19.A03.

Proteomic databases

PaxDbiQ93Y01.
PRIDEiQ93Y01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G10590.1; AT4G10590.1; AT4G10590.
AT4G10590.2; AT4G10590.2; AT4G10590.
GeneIDi826651.
KEGGiath:AT4G10590.

Organism-specific databases

TAIRiAT4G10590.

Phylogenomic databases

eggNOGiCOG5560.
HOGENOMiHOG000264375.
InParanoidiQ93Y01.
KOiK11835.
OMAiIDENRWY.
PhylomeDBiQ93Y01.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ93Y01.

Gene expression databases

ExpressionAtlasiQ93Y01. baseline and differential.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR028134. USP.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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]
ProtoNetiSearch...

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 nameiUBP9_ARATH
AccessioniPrimary (citable) accession number: Q93Y01
Secondary accession number(s): Q9T0B8, Q9ZSB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 98 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.