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Q67XW5 (UBP18_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. 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 18

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 18
Short name=AtUBP18
Ubiquitin thioesterase 18
Ubiquitin-specific-processing protease 18
Gene names
Name:UBP18
Ordered Locus Names:At4g31670
ORF Names:F28M20.140
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length631 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).

Subcellular location

Membrane; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 MYND-type zinc finger.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   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

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 631631Ubiquitin carboxyl-terminal hydrolase 18
PRO_0000313044

Regions

Transmembrane10 – 3021Helical; Potential
Domain168 – 474307USP
Zinc finger61 – 9838MYND-type

Sites

Active site1771Nucleophile By similarity
Active site4331Proton acceptor By similarity

Experimental info

Sequence conflict4321G → S in BAD43230. Ref.4
Sequence conflict5501S → P in BAD44466. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q67XW5 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 4C875C228588A0BE

FASTA63170,753
        10         20         30         40         50         60 
MHEVGFPLDL SVFTRLIATL FFLAVGVFYF LKNTAAKYFD IGAAAAGGFD RDFMAVDAED 

        70         80         90        100        110        120 
CSVCGNFSTK KCSRCKSVRY CSAECQRSDW SSGHQRNCRD YGITTLTPSA KNGLRFRASP 

       130        140        150        160        170        180 
FGDSSASSIA LISERGQNKS SLKPREVLFP YEEFVEYFNW DNPELAPCGL MNCGNSCFAN 

       190        200        210        220        230        240 
VILQCLSWTR PLVAYLLEKG HKRECMRNDW CFLCEFQTHV ERASQSRFPF SPMNIISRLT 

       250        260        270        280        290        300 
NIGGTLGYGR QEDAHEFMRY AIDMMQSVCL DEFGGEKIVP PRSQETTLIQ YIFGGLLQSQ 

       310        320        330        340        350        360 
VQCTVCNHVS DQYENMMDLI VEMHGDAGSL EECLDQFTAE EWLHGDNMYK CDRCSDYVKA 

       370        380        390        400        410        420 
CKRLTIRRAP NILTIALKRY QGGRYGKLNK RISFPETLDL NPYMSEGGDG SDVYKLYAVI 

       430        440        450        460        470        480 
VHLDMLNASF FGHYICYIKD FCGNWYRIDD SEIESVELED VLSQRAYMLL YSRIQARSSS 

       490        500        510        520        530        540 
SCLRSEVKDE KKTDTLDTES CVKELVESSM VGAIESRSST HATIEDPVCE QSPSPSPSPS 

       550        560        570        580        590        600 
PSPSPSPSPS VLASECCSEV ERIDTLDSES NSSIDDSATD HQEDVANGNK DPEVKYQAAD 

       610        620        630 
SWSDPTTSTP LVCTKSKPPV RDMDTKMIDA Q 

« 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]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT05103.
RefSeqNP_194895.1. NM_119316.4.
UniGeneAt.31726.

3D structure databases

ProteinModelPortalQ67XW5.
SMRQ67XW5. Positions 169-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14581. 1 interaction.
STRING3702.AT4G31670.1-P.

Protein family/group databases

MEROPSC19.A08.

Proteomic databases

PaxDbQ67XW5.
PRIDEQ67XW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G31670.1; AT4G31670.1; AT4G31670.
GeneID829295.
KEGGath:AT4G31670.

Organism-specific databases

TAIRAT4G31670.

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000097839.
InParanoidQ67XW5.
KOK11855.
OMAECCSEVE.
PhylomeDBQ67XW5.

Enzyme and pathway databases

BioCycARA:AT4G31670-MONOMER.

Gene expression databases

GenevestigatorQ67XW5.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR002893. Znf_MYND.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS50235. USP_3. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBP18_ARATH
AccessionPrimary (citable) accession number: Q67XW5
Secondary accession number(s): O81780, Q682A0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: June 11, 2014
This is version 66 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