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Q8LG98

- OTUBL_ARATH

UniProt

Q8LG98 - OTUBL_ARATH

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Protein
Ubiquitin thioesterase otubain-like
Gene
At1g28120, F13K9.21
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at transcript leveli

Functioni

Possible hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation 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 sitei89 – 891 By similarity
Active sitei92 – 921Nucleophile By similarity
Active sitei288 – 2881 By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. omega peptidase activity Source: InterPro

GO - Biological processi

  1. cellular amino acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciARA:AT1G28120-MONOMER.

Protein family/group databases

MEROPSiC65.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin thioesterase otubain-like (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme otubain-like
Ubiquitin-specific-processing protease otubain-like
Gene namesi
Ordered Locus Names:At1g28120
ORF Names:F13K9.21
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G28120.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306Ubiquitin thioesterase otubain-like
PRO_0000221014Add
BLAST

Proteomic databases

PaxDbiQ8LG98.
PRIDEiQ8LG98.

Expressioni

Gene expression databases

ArrayExpressiQ8LG98.
GenevestigatoriQ8LG98.

Interactioni

Protein-protein interaction databases

BioGridi24940. 2 interactions.
IntActiQ8LG98. 2 interactions.
MINTiMINT-8063619.
STRINGi3702.AT1G28120.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ8LG98.
SMRiQ8LG98. Positions 47-293.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 295215OTU
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase C65 family.
Contains 1 OTU domain.

Phylogenomic databases

eggNOGiNOG267426.
HOGENOMiHOG000019496.
InParanoidiQ8LG98.
KOiK09602.
OMAiVEPMYKE.
PhylomeDBiQ8LG98.

Family and domain databases

InterProiIPR003323. OTU.
IPR019400. Peptidase_C65_otubain.
IPR016615. Ubiquitin_thioesterase_Otubain.
[Graphical view]
PfamiPF10275. Peptidase_C65. 1 hit.
[Graphical view]
PIRSFiPIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8LG98-1 [UniParc]FASTAAdd to Basket

« Hide

MQNQIDMVKD EAEVAASISA IKGEEWGNCS SVEDQPSFQE EEAAKVPYVG    50
DKEPLSSLAA EYQSGSPILL EKIKILDSQY IGIRRTRGDG NCFFRSFMFS 100
YLEHILESQD RAEVDRIKVN VEKCRKTLQN LGYTDFTFED FFALFLEQLD 150
DILQGTEESI SYDELVNRSR DQSVSDYIVM FFRFVTAGDI RTRADFFEPF 200
ITGLSNATVD QFCKSSVEPM GEESDHIHIT ALSDALGVAI RVVYLDRSSC 250
DSGGVTVNHH DFVPVGITNE KDEEASAPFI TLLYRPGHYD ILYPKPSCKV 300
SDNVGK 306
Length:306
Mass (Da):34,434
Last modified:March 1, 2004 - v2
Checksum:i7D8822E69806AC87
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51I → N in AAM60966. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC069471 Genomic DNA. Translation: AAG51478.1.
CP002684 Genomic DNA. Translation: AEE30920.1.
AY136373 mRNA. Translation: AAM97039.1.
BT000164 mRNA. Translation: AAN15483.1.
AY084389 mRNA. Translation: AAM60966.1.
PIRiA86407.
RefSeqiNP_564299.1. NM_102577.3.
UniGeneiAt.43774.

Genome annotation databases

EnsemblPlantsiAT1G28120.1; AT1G28120.1; AT1G28120.
GeneIDi839705.
KEGGiath:AT1G28120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC069471 Genomic DNA. Translation: AAG51478.1 .
CP002684 Genomic DNA. Translation: AEE30920.1 .
AY136373 mRNA. Translation: AAM97039.1 .
BT000164 mRNA. Translation: AAN15483.1 .
AY084389 mRNA. Translation: AAM60966.1 .
PIRi A86407.
RefSeqi NP_564299.1. NM_102577.3.
UniGenei At.43774.

3D structure databases

ProteinModelPortali Q8LG98.
SMRi Q8LG98. Positions 47-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 24940. 2 interactions.
IntActi Q8LG98. 2 interactions.
MINTi MINT-8063619.
STRINGi 3702.AT1G28120.1-P.

Protein family/group databases

MEROPSi C65.001.

Proteomic databases

PaxDbi Q8LG98.
PRIDEi Q8LG98.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G28120.1 ; AT1G28120.1 ; AT1G28120 .
GeneIDi 839705.
KEGGi ath:AT1G28120.

Organism-specific databases

TAIRi AT1G28120.

Phylogenomic databases

eggNOGi NOG267426.
HOGENOMi HOG000019496.
InParanoidi Q8LG98.
KOi K09602.
OMAi VEPMYKE.
PhylomeDBi Q8LG98.

Enzyme and pathway databases

BioCyci ARA:AT1G28120-MONOMER.

Gene expression databases

ArrayExpressi Q8LG98.
Genevestigatori Q8LG98.

Family and domain databases

InterProi IPR003323. OTU.
IPR019400. Peptidase_C65_otubain.
IPR016615. Ubiquitin_thioesterase_Otubain.
[Graphical view ]
Pfami PF10275. Peptidase_C65. 1 hit.
[Graphical view ]
PIRSFi PIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
PROSITEi PS50802. OTU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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.
  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. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiOTUBL_ARATH
AccessioniPrimary (citable) accession number: Q8LG98
Secondary accession number(s): Q9C7E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: June 11, 2014
This is version 86 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

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