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Q9FPS9 (UBP15_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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 15

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 15
Short name=AtUBP15
Ubiquitin thioesterase 15
Ubiquitin-specific-processing protease 15
Gene names
Name:UBP15
Ordered Locus Names:At1g17110
ORF Names:F20D23.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length924 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.

Sequence caution

The sequence AAD50020.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9FPS9-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 924924Ubiquitin carboxyl-terminal hydrolase 15
PRO_0000313041

Regions

Transmembrane7 – 2721Helical; Potential
Domain438 – 744307USP
Zinc finger130 – 16738MYND-type
Compositional bias172 – 1776Poly-Ser

Sites

Active site4471Nucleophile By similarity
Active site7031Proton acceptor By similarity

Experimental info

Sequence conflict1061R → K in AAG42756. Ref.1
Sequence conflict3901I → V in AAG42756. Ref.1
Sequence conflict5361Q → P in AAG42756. Ref.1
Sequence conflict5681R → H in AAG42756. Ref.1
Sequence conflict599 – 6002SL → FF in AAG42756. Ref.1
Sequence conflict6051T → I in AAG42756. Ref.1

Sequences

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

Last modified January 15, 2008. Version 2.
Checksum: 32BD93822243271C

FASTA924103,677
        10         20         30         40         50         60 
MLEPRGADIP ILFLVLVVLP VVAYILLGKW SNISEKRVRA NLLAQMAAEE ALRAETVVNA 

        70         80         90        100        110        120 
DRGVRFESVA TENRAQRTRT KTVSAGGGAV RAEFDAGARE TVAEQRSDSV TATCGVTVVA 

       130        140        150        160        170        180 
PVNNNELHVC ARCFGPAKTR CSRCKSVRYC SGKCQIIHWR VAHKDECVPV ESCSSSSERV 

       190        200        210        220        230        240 
SFEKDSVLYD HGMDSTMYSN NTTQAAKGKT SKSSVDFASL GISQNDITPQ INTQGRKSVG 

       250        260        270        280        290        300 
KQHSSKANRE SCRRDSATVF DSSDEAASAG GDNKTSHIKH KSRGNSYAAE TNPRRHSVDS 

       310        320        330        340        350        360 
SAVQMNGQSF VSGMQESHKH ENNLGVRSSF GCPNTQYPSN GTRTATLPRT GINKSGEQSC 

       370        380        390        400        410        420 
TETSKKGQVA AVSKTVRSKD TGISEESNGI SSTMGIMKMM GLRNSTKHDD RYKNLKMLFP 

       430        440        450        460        470        480 
YEEFLKFFQC EVFDLSPRGL VNCGNSCYAN AVLQSLTCTK PLVAYLLRRS HSRSCSGKDW 

       490        500        510        520        530        540 
CLMCELEQHV MMLRESGGPL SASRILSHMR SINCQIGDGS QEDAHEFLRL LVASMQSICL 

       550        560        570        580        590        600 
ERLGGETKVD PRLQETTLVQ HMFGGRLRSK VKCLRCDHES ERYENIMDLT LEIYGWVESL 

       610        620        630        640        650        660 
QDALTQFTRP EDLDGENMYR CSRCAGYVRA RKELSIHEAP NILTIVLKRF QEGRYGKINK 

       670        680        690        700        710        720 
CISFPEMLDM IPFMTRTGDV PPLYMLYAVI VHLDTLNASF SGHYISYVKD LRGNWYRIDD 

       730        740        750        760        770        780 
SEIHPVPMTQ VMSEGAYMLF YMRSYPRPQR GEHNGKAPVH HSQPRNEMKE QRKPVNRFKP 

       790        800        810        820        830        840 
RADHKNTESS SSEWSLFTSS DEASFTTEST RDSFSTIDYT DVCHVVDSSS PFAIFNNVYH 

       850        860        870        880        890        900 
NVEPSPHNTV ACRMFSGTKP ETRYFVEQET NHNNTVVLDA TPSLYPIPAP YPPHDYYDQS 

       910        920 
MYVNYETNPE FNNGQDQDRT YSYW 

« Hide

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.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF302665 mRNA. Translation: AAG42756.1.
AC007651 Genomic DNA. Translation: AAD50020.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE29542.1.
PIRH86306.
RefSeqNP_564014.1. NM_101571.2.
UniGeneAt.48199.

3D structure databases

ProteinModelPortalQ9FPS9.
SMRQ9FPS9. Positions 128-172, 439-741.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid23521. 3 interactions.
STRING3702.AT1G17110.1-P.

Protein family/group databases

MEROPSC19.096.

Proteomic databases

PaxDbQ9FPS9.
PRIDEQ9FPS9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G17110.1; AT1G17110.1; AT1G17110. [Q9FPS9-1]
GeneID838281.
KEGGath:AT1G17110.

Organism-specific databases

TAIRAT1G17110.

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000242869.
InParanoidQ9FPS9.
KOK11855.
PhylomeDBQ9FPS9.
ProtClustDBCLSN2917013.

Enzyme and pathway databases

BioCycARA:AT1G17110-MONOMER.
ARA:GQT-1818-MONOMER.

Gene expression databases

GenevestigatorQ9FPS9.

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 nameUBP15_ARATH
AccessionPrimary (citable) accession number: Q9FPS9
Secondary accession number(s): Q9SHG9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: April 16, 2014
This is version 80 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