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Protein

Ubiquitin carboxyl-terminal hydrolase 18

Gene

UBP18

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 sitei177 – 1771NucleophilePROSITE-ProRule annotation
Active sitei433 – 4331Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri61 – 9838MYND-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT4G31670-MONOMER.

Protein family/group databases

MEROPSiC19.A08.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 18 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 18
Short name:
AtUBP18
Ubiquitin thioesterase 18
Ubiquitin-specific-processing protease 18
Gene namesi
Name:UBP18
Ordered Locus Names:At4g31670
ORF Names:F28M20.140
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G31670.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3021HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 631631Ubiquitin carboxyl-terminal hydrolase 18PRO_0000313044Add
BLAST

Proteomic databases

PaxDbiQ67XW5.
PRIDEiQ67XW5.

Interactioni

Protein-protein interaction databases

BioGridi14581. 1 interaction.
STRINGi3702.AT4G31670.1.

Structurei

3D structure databases

ProteinModelPortaliQ67XW5.
SMRiQ67XW5. Positions 169-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 474307USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri61 – 9838MYND-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000097839.
InParanoidiQ67XW5.
KOiK11855.
OMAiPYMSEGG.
PhylomeDBiQ67XW5.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS50235. USP_3. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q67XW5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHEVGFPLDL SVFTRLIATL FFLAVGVFYF LKNTAAKYFD IGAAAAGGFD
60 70 80 90 100
RDFMAVDAED CSVCGNFSTK KCSRCKSVRY CSAECQRSDW SSGHQRNCRD
110 120 130 140 150
YGITTLTPSA KNGLRFRASP FGDSSASSIA LISERGQNKS SLKPREVLFP
160 170 180 190 200
YEEFVEYFNW DNPELAPCGL MNCGNSCFAN VILQCLSWTR PLVAYLLEKG
210 220 230 240 250
HKRECMRNDW CFLCEFQTHV ERASQSRFPF SPMNIISRLT NIGGTLGYGR
260 270 280 290 300
QEDAHEFMRY AIDMMQSVCL DEFGGEKIVP PRSQETTLIQ YIFGGLLQSQ
310 320 330 340 350
VQCTVCNHVS DQYENMMDLI VEMHGDAGSL EECLDQFTAE EWLHGDNMYK
360 370 380 390 400
CDRCSDYVKA CKRLTIRRAP NILTIALKRY QGGRYGKLNK RISFPETLDL
410 420 430 440 450
NPYMSEGGDG SDVYKLYAVI VHLDMLNASF FGHYICYIKD FCGNWYRIDD
460 470 480 490 500
SEIESVELED VLSQRAYMLL YSRIQARSSS SCLRSEVKDE KKTDTLDTES
510 520 530 540 550
CVKELVESSM VGAIESRSST HATIEDPVCE QSPSPSPSPS PSPSPSPSPS
560 570 580 590 600
VLASECCSEV ERIDTLDSES NSSIDDSATD HQEDVANGNK DPEVKYQAAD
610 620 630
SWSDPTTSTP LVCTKSKPPV RDMDTKMIDA Q
Length:631
Mass (Da):70,753
Last modified:January 15, 2008 - v2
Checksum:i4C875C228588A0BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti432 – 4321G → S in BAD43230 (Ref. 4) Curated
Sequence conflicti550 – 5501S → P in BAD44466 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031004 Genomic DNA. Translation: CAA19756.1.
AL161579 Genomic DNA. Translation: CAB79885.1.
CP002687 Genomic DNA. Translation: AEE85943.1.
AY142532 mRNA. Translation: AAN13075.1.
AK175467 mRNA. Translation: BAD43230.1.
AK176703 mRNA. Translation: BAD44466.1.
PIRiT05103.
RefSeqiNP_194895.1. NM_119316.4.
UniGeneiAt.31726.

Genome annotation databases

EnsemblPlantsiAT4G31670.1; AT4G31670.1; AT4G31670.
GeneIDi829295.
KEGGiath:AT4G31670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031004 Genomic DNA. Translation: CAA19756.1.
AL161579 Genomic DNA. Translation: CAB79885.1.
CP002687 Genomic DNA. Translation: AEE85943.1.
AY142532 mRNA. Translation: AAN13075.1.
AK175467 mRNA. Translation: BAD43230.1.
AK176703 mRNA. Translation: BAD44466.1.
PIRiT05103.
RefSeqiNP_194895.1. NM_119316.4.
UniGeneiAt.31726.

3D structure databases

ProteinModelPortaliQ67XW5.
SMRiQ67XW5. Positions 169-472.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14581. 1 interaction.
STRINGi3702.AT4G31670.1.

Protein family/group databases

MEROPSiC19.A08.

Proteomic databases

PaxDbiQ67XW5.
PRIDEiQ67XW5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G31670.1; AT4G31670.1; AT4G31670.
GeneIDi829295.
KEGGiath:AT4G31670.

Organism-specific databases

TAIRiAT4G31670.

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000097839.
InParanoidiQ67XW5.
KOiK11855.
OMAiPYMSEGG.
PhylomeDBiQ67XW5.

Enzyme and pathway databases

BioCyciARA:AT4G31670-MONOMER.

Miscellaneous databases

PROiQ67XW5.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS50235. USP_3. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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 nameiUBP18_ARATH
AccessioniPrimary (citable) accession number: Q67XW5
Secondary accession number(s): O81780, Q682A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: June 24, 2015
This is version 73 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

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.