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Q9WUP7 (UCHL5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. 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 isozyme L5

Short name=UCH-L5
EC=3.4.19.12
Alternative name(s):
Ubiquitin C-terminal hydrolase UCH37
Ubiquitin thioesterase L5
Gene names
Name:Uchl5
Synonyms:Uch37
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1 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).

Enzyme regulation

Activated by ADRM1. Inhibited by interaction with NFRKB By similarity.

Subunit structure

Component of the 19S (PA700) regulatory complex of the 26S proteasome. Interacts with ADRM1 and NFRKB. Component of the INO80 complex; specifically part of a complex module associated with N-terminus of INO80 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus By similarity.

Sequence similarities

Belongs to the peptidase C12 family.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

forebrain morphogenesis

Inferred from mutant phenotype PubMed 21048919. Source: BHF-UCL

lateral ventricle development

Inferred from mutant phenotype PubMed 21048919. Source: BHF-UCL

midbrain development

Inferred from mutant phenotype PubMed 21048919. Source: BHF-UCL

protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of proteasomal protein catabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentIno80 complex

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionendopeptidase inhibitor activity

Inferred from electronic annotation. Source: Ensembl

omega peptidase activity

Inferred from electronic annotation. Source: InterPro

ubiquitin thiolesterase activity

Traceable author statement. Source: Reactome

ubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WUP7-1)

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: Q9WUP7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     246-246: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Ubiquitin carboxyl-terminal hydrolase isozyme L5
PRO_0000211067

Regions

Region313 – 32917Interaction with ADRM1 By similarity

Sites

Active site881Nucleophile By similarity
Active site1641Proton donor By similarity
Site1791Important for enzyme activity By similarity

Amino acid modifications

Modified residue471N6-succinyllysine Ref.5
Modified residue1581N6-acetyllysine Ref.5
Modified residue2891N6-succinyllysine Ref.5

Natural variations

Alternative sequence2461Missing in isoform 2.
VSP_005255

Experimental info

Sequence conflict201E → K in AAD31534. Ref.1
Sequence conflict241G → R in AAD31534. Ref.1
Sequence conflict1041D → E in BAB25312. Ref.1

Sequences

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

Last modified September 26, 2001. Version 2.
Checksum: 1EAB5223FB707917

FASTA32937,617
        10         20         30         40         50         60 
MSSNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ESFEKLKPVH GLIFLFKWQP 

        70         80         90        100        110        120 
GEEPAGSVVQ DSRLETIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS 

       130        140        150        160        170        180 
FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTPAKEE DAFHFVSYVP VNGRLYELDG 

       190        200        210        220        230        240 
LREGPIDLGA CNQDDWITAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR 

       250        260        270        280        290        300 
QLAEEEPMDT DQGSTVLSAI QSEVARNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL 

       310        320 
KTLAEHQQLI PLVEKAKEKQ NAKKAQETK 

« Hide

Isoform 2 [UniParc].

Checksum: 55483B16ADC1E720
Show »

FASTA32837,488

References

« Hide 'large scale' references
[1]Xu W., DeMartino G.N., Slaughter C.A., Cohen R.E.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Identification of a novel mouse ubiquitin C-terminal hydrolase: cloning, expression and functional characterization."
Li T.W., Sun B., Mustafa F.B., Lee M.K., Teo T.S.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Embryonic liver, Pancreas and Thymus.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: Czech II.
Tissue: Mammary gland.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-158, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-47 AND LYS-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF148447 mRNA. Translation: AAD31534.1.
AF175903 mRNA. Translation: AAD50311.1.
AK017925 mRNA. Translation: BAB31005.1.
AK011117 mRNA. Translation: BAB27412.1.
AK007860 mRNA. Translation: BAB25312.1.
BC006891 mRNA. Translation: AAH06891.1.
CCDSCCDS15346.1. [Q9WUP7-1]
RefSeqNP_001153338.1. NM_001159866.1. [Q9WUP7-2]
NP_062508.2. NM_019562.2. [Q9WUP7-1]
UniGeneMm.261004.

3D structure databases

ProteinModelPortalQ9WUP7.
SMRQ9WUP7. Positions 7-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207842. 1 interaction.
IntActQ9WUP7. 1 interaction.

Protein family/group databases

MEROPSC12.005.

PTM databases

PhosphoSiteQ9WUP7.

2D gel databases

REPRODUCTION-2DPAGEQ9WUP7.

Proteomic databases

MaxQBQ9WUP7.
PaxDbQ9WUP7.
PRIDEQ9WUP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018333; ENSMUSP00000018333; ENSMUSG00000018189. [Q9WUP7-1]
GeneID56207.
KEGGmmu:56207.
UCSCuc007cxe.2. mouse. [Q9WUP7-1]
uc007cxf.2. mouse. [Q9WUP7-2]

Organism-specific databases

CTD51377.
MGIMGI:1914848. Uchl5.

Phylogenomic databases

eggNOGNOG321645.
GeneTreeENSGT00510000046560.
HOGENOMHOG000203918.
HOVERGENHBG056021.
InParanoidQ9WUP7.
KOK05610.
OMADEDAFHF.
OrthoDBEOG7M3J11.
PhylomeDBQ9WUP7.
TreeFamTF313976.

Gene expression databases

BgeeQ9WUP7.
CleanExMM_UCHL5.
GenevestigatorQ9WUP7.

Family and domain databases

Gene3D3.40.532.10. 1 hit.
InterProIPR001578. Peptidase_C12_UCH.
IPR017390. Ubiquitinyl_hydrolase_UCH37.
[Graphical view]
PANTHERPTHR10589. PTHR10589. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PIRSFPIRSF038120. Ubiquitinyl_hydrolase_UCH37. 1 hit.
PRINTSPR00707. UBCTHYDRLASE.
ProtoNetSearch...

Other

ChiTaRSUCHL5. mouse.
NextBio312039.
PROQ9WUP7.
SOURCESearch...

Entry information

Entry nameUCHL5_MOUSE
AccessionPrimary (citable) accession number: Q9WUP7
Secondary accession number(s): Q9CVJ4, Q9CXZ3, Q9R107
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot