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Q67XW5

- UBP18_ARATH

UniProt

Q67XW5 - UBP18_ARATH

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Protein

Ubiquitin carboxyl-terminal hydrolase 18

Gene

UBP18

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 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

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. ubiquitinyl hydrolase activity Source: InterPro

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process Source: InterPro
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: Chromosome 4

Organism-specific databases

TAIRiAT4G31670.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
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.

Expressioni

Gene expression databases

GenevestigatoriQ67XW5.

Interactioni

Protein-protein interaction databases

BioGridi14581. 1 interaction.
STRINGi3702.AT4G31670.1-P.

Structurei

3D structure databases

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

Transmembrane

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

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.
OMAiECCSEVE.
PhylomeDBiQ67XW5.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
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 [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. 1 PublicationCurated
Sequence conflicti550 – 5501S → P in BAD44466. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi T05103.
RefSeqi NP_194895.1. NM_119316.4.
UniGenei At.31726.

3D structure databases

ProteinModelPortali Q67XW5.
SMRi Q67XW5. Positions 169-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 14581. 1 interaction.
STRINGi 3702.AT4G31670.1-P.

Protein family/group databases

MEROPSi C19.A08.

Proteomic databases

PaxDbi Q67XW5.
PRIDEi Q67XW5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G31670.1 ; AT4G31670.1 ; AT4G31670 .
GeneIDi 829295.
KEGGi ath:AT4G31670.

Organism-specific databases

TAIRi AT4G31670.

Phylogenomic databases

eggNOGi COG5533.
HOGENOMi HOG000097839.
InParanoidi Q67XW5.
KOi K11855.
OMAi ECCSEVE.
PhylomeDBi Q67XW5.

Enzyme and pathway databases

BioCyci ARA:AT4G31670-MONOMER.

Gene expression databases

Genevestigatori Q67XW5.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR002893. Znf_MYND.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS50235. USP_3. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 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. "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: October 1, 2014
This is version 68 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