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Q9FPS0 (UBP27_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 27

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 27
Short name=AtUBP27
Ubiquitin thioesterase 27
Ubiquitin-specific-processing protease 27
Gene names
Name:UBP27
Ordered Locus Names:At4g39370
ORF Names:F23K16.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length494 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 USP domain.

Sequence caution

The sequence CAB52824.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB80600.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   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

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9FPS0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9FPS0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     314-361: TEIEKLRSCG...LIIARFPKLL → VVNLSQLLML...AQELWRRGPM
     362-494: Missing.
Note: Derived from EST data. May be due to an intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Ubiquitin carboxyl-terminal hydrolase 27
PRO_0000313052

Regions

Transmembrane30 – 5021Helical; Potential
Domain74 – 494421USP

Sites

Active site831Nucleophile By similarity
Active site4401Proton acceptor By similarity

Natural variations

Alternative sequence314 – 36148TEIEK…FPKLL → VVNLSQLLMLLYFSFVHASR LYLTRVSWKRFQSDGNRKAQ ELWRRGPM in isoform 2.
VSP_029992
Alternative sequence362 – 494133Missing in isoform 2.
VSP_029993

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: B8CBDF5799FA9FA6

FASTA49455,771
        10         20         30         40         50         60 
MVSRRGSETK AIVCVLTDRI RISNQWVSHL SFAGLLGVAG FVFAQQHGLF RNLNNLKLFS 

        70         80         90        100        110        120 
GREKDSGDDS FLVPGLQNLG NNCFLNVILQ ALASCKDFRS FLQWVLEDAR GSLAGEQEEQ 

       130        140        150        160        170        180 
LPLTFALSAL LQELGTVGSR RSVSNPRKVM VTLTDYAKNF NLTSQQDAAE ALLHLISSLQ 

       190        200        210        220        230        240 
EEIVVCYRPS QSSNLSDILF SRNLRMLAPS EGLHGLMELK RWHKHLRGPF DGILGSTLMC 

       250        260        270        280        290        300 
RTCSSQISLE FQFFHTLPLS PLLHHGGYNI MSGCTLEHCL KKFLNTEKVE NYFCYRCWHG 

       310        320        330        340        350        360 
AALKYLSVIG AAETEIEKLR SCGGEDQCDC KTSLHLQRMP WSNSYSHILK QLIIARFPKL 

       370        380        390        400        410        420 
LCIQVQRASF NMFEEFKLSG HIAFPLVLNL SLFTPSSIGV NIEERIEMSS EYQKPEASKN 

       430        440        450        460        470        480 
HGMYRLVTVV EHFGRTGSGH YTVYRSVRVF SQEEEEEDCD EDLSWFSISD SEVCRVSESD 

       490 
VLGAEASLLF YERL 

« Hide

Isoform 2 [UniParc].

Checksum: EBD855CB345C1129
Show »

FASTA36140,770

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION, NOMENCLATURE (ISOFORM 1).
Strain: cv. Columbia.
[2]"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.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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] (ISOFORM 1).
Strain: cv. Columbia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF302675 mRNA. Translation: AAG42765.1.
AL078620 Genomic DNA. Translation: CAB52824.1. Sequence problems.
AL161595 Genomic DNA. Translation: CAB80600.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE87061.1.
CP002687 Genomic DNA. Translation: AEE87062.1.
AF370208 mRNA. Translation: AAK44023.1.
AY133770 mRNA. Translation: AAM91704.1.
PIRB85466.
RefSeqNP_568058.1. NM_120097.2.
NP_974714.1. NM_202985.1.
UniGeneAt.3432.

3D structure databases

ProteinModelPortalQ9FPS0.
SMRQ9FPS0. Positions 75-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G39370.1-P.

Protein family/group databases

MEROPSC19.002.

Proteomic databases

PaxDbQ9FPS0.
PRIDEQ9FPS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G39370.1; AT4G39370.1; AT4G39370. [Q9FPS0-1]
GeneID830092.
KEGGath:AT4G39370.

Organism-specific databases

TAIRAT4G39370.

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000070653.
InParanoidQ9FPS0.
KOK11851.
PhylomeDBQ9FPS0.
ProtClustDBCLSN2689838.

Enzyme and pathway databases

BioCycARA:AT4G39370-MONOMER.
ARA:GQT-496-MONOMER.
ARA:GQT-497-MONOMER.

Gene expression databases

GenevestigatorQ9FPS0.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9FPS0.

Entry information

Entry nameUBP27_ARATH
AccessionPrimary (citable) accession number: Q9FPS0
Secondary accession number(s): Q3E9N3, Q9SVC0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 76 of the entry and version 1 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