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Q9R0P9 (UCHL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase isozyme L1

Short name=UCH-L1
EC=3.4.19.12
EC=6.-.-.-
Alternative name(s):
Neuron cytoplasmic protein 9.5
PGP 9.5
Short name=PGP9.5
Ubiquitin thioesterase L1
Gene names
Name:Uchl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity. Ref.6

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).

Subunit structure

Monomer. Homodimer. Interacts with COPS5 and SNCA By similarity.

Subcellular location

Cytoplasm. Endoplasmic reticulum membrane; Lipid-anchor By similarity Ref.6.

Tissue specificity

Expressed in brain, where it is found in neurons but not in oligodendrocytes or astrocytes. Found in the ganglion cell layer and the inner nuclear layer of the retina (at protein level). Expressed in brain and testis. In the brain, expression is at its lowest in replaceable neurons of hippocampus and olfactory bulb. Highly expressed in senescent pituitary. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8

Post-translational modification

O-glycosylated By similarity.

Disruption phenotype

Mice show sensory ataxia at an early stage, followed by motor ataxia at a later stage. They have reduced levels of monoubiquitin in the nervous system, and increased resistance to retinal ischemia. Ref.1 Ref.6

Miscellaneous

In contrast to UCHL3, does not hydrolyze a peptide bond at the C-terminal glycine of NEDD8 By similarity.

Sequence similarities

Belongs to the peptidase C12 family.

Biophysicochemical properties

Kinetic parameters:

KM=116 nM for Ub-AMC Ref.6

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
   Molecular functionHydrolase
Ligase
Protease
Thiol protease
   PTMGlycoprotein
Lipoprotein
Oxidation
Prenylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from mutant phenotype PubMed 11555633PubMed 3340629. Source: MGI

axon target recognition

Inferred from mutant phenotype PubMed 8474599. Source: MGI

axon transport of mitochondrion

Inferred from mutant phenotype PubMed 2558488. Source: MGI

axonogenesis

Inferred from mutant phenotype PubMed 1630580. Source: MGI

cell proliferation

Inferred from mutant phenotype PubMed 12638230. Source: MGI

eating behavior

Inferred from genetic interaction PubMed 11555633. Source: MGI

muscle fiber development

Inferred from genetic interaction PubMed 8007658. Source: MGI

negative regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

neuromuscular process

Inferred from mutant phenotype PubMed 3340629PubMed 7555927. Source: MGI

protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

response to ischemia

Inferred from mutant phenotype Ref.7. Source: MGI

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from direct assay PubMed 11466438PubMed 12074562PubMed 12107488PubMed 12866128PubMed 14973275PubMed 21606356PubMed 8896700. Source: MGI

cytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

cytosol

Inferred from direct assay Ref.6. Source: MGI

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from direct assay PubMed 11549719PubMed 23284756. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

omega peptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin binding

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from direct assay Ref.6. Source: MGI

ubiquitin-specific protease activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Ubiquitin carboxyl-terminal hydrolase isozyme L1
PRO_0000211058
Propeptide221 – 2233Removed in mature form By similarity
PRO_0000414313

Regions

Region5 – 106Interaction with ubiquitin By similarity
Region151 – 1566Interaction with ubiquitin By similarity
Region211 – 2166Interaction with ubiquitin By similarity

Sites

Active site901Nucleophile Probable
Active site1611Proton donor By similarity
Site11Susceptible to oxidation By similarity
Site61Susceptible to oxidation By similarity
Site121Susceptible to oxidation By similarity
Site1761Important for enzyme activity By similarity
Site1791Susceptible to oxidation By similarity
Site2201Susceptible to oxidation By similarity

Amino acid modifications

Lipidation2201S-farnesyl cysteine By similarity

Experimental info

Mutagenesis301D → K: Abolishes enzymatic activity and ubiquitin binding. Ref.6
Mutagenesis901C → S: Abolishes enzymatic activity, but does not affect ubiquitin binding. Ref.6
Sequence conflict1491E → K in AAD51029. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9R0P9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F1402BF7B0C077EA

FASTA22324,838
        10         20         30         40         50         60 
MQLKPMEINP EMLNKVLAKL GVAGQWRFAD VLGLEEETLG SVPSPACALL LLFPLTAQHE 

        70         80         90        100        110        120 
NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA NNQDKLEFED GSVLKQFLSE 

       130        140        150        160        170        180 
TEKLSPEDRA KCFEKNEAIQ AAHDSVAQEG QCRVDDKVNF HFILFNNVDG HLYELDGRMP 

       190        200        210        220 
FPVNHGASSE DSLLQDAAKV CREFTEREQG EVRFSAVALC KAA 

« Hide

References

« Hide 'large scale' references
[1]"Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice."
Saigoh K., Wang Y.-L., Suh J.G., Yamanishi T., Sakai Y., Kiyosawa H., Harada T., Ichihara N., Wakana S., Kikuchi T., Wada K.
Nat. Genet. 23:47-51(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
Tissue: Brain.
[2]"Age-related alterations in the protein expression profile of C57BL/6J mouse pituitaries."
Marzban G., Grillari J., Reisinger E., Hemetsberger T., Grabherr R., Katinger H.
Exp. Gerontol. 37:1451-1460(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10, TISSUE SPECIFICITY.
Strain: C57BL/6J.
Tissue: Pituitary.
[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].
Strain: C57BL/6J.
Tissue: Hippocampus.
[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].
Tissue: Retina.
[5]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 20-27; 66-78; 116-123; 136-153 AND 158-199, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron."
Osaka H., Wang Y.-L., Takada K., Takizawa S., Setsuie R., Li H., Sato Y., Nishikawa K., Sun Y.-J., Sakurai M., Harada T., Hara Y., Kimura I., Chiba S., Namikawa K., Kiyama H., Noda M., Aoki S., Wada K.
Hum. Mol. Genet. 12:1945-1958(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-30 AND CYS-90, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, DISRUPTION PHENOTYPE.
[7]"Role of ubiquitin carboxy terminal hydrolase-L1 in neural cell apoptosis induced by ischemic retinal injury in vivo."
Harada T., Harada C., Wang Y.-L., Osaka H., Amanai K., Tanaka K., Takizawa S., Setsuie R., Sakurai M., Sato Y., Noda M., Wada K.
Am. J. Pathol. 164:59-64(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Replaceable neurons and neurodegenerative disease share depressed UCHL1 levels."
Lombardino A.J., Li X.-C., Hertel M., Nottebohm F.
Proc. Natl. Acad. Sci. U.S.A. 102:8036-8041(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025313 mRNA. Translation: BAA84083.1.
AF172334 mRNA. Translation: AAD51029.1.
AK013729 mRNA. Translation: BAB28976.1.
BC039177 mRNA. Translation: AAH39177.1.
RefSeqNP_035800.2. NM_011670.2.
UniGeneMm.29807.

3D structure databases

ProteinModelPortalQ9R0P9.
SMRQ9R0P9. Positions 1-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204423. 7 interactions.
IntActQ9R0P9. 5 interactions.
MINTMINT-4139420.
STRING10090.ENSMUSP00000031131.

Chemistry

BindingDBQ9R0P9.

Protein family/group databases

MEROPSC12.001.

PTM databases

PhosphoSiteQ9R0P9.

2D gel databases

REPRODUCTION-2DPAGEIPI00313962.
Q9R0P9.
UCD-2DPAGEQ9R0P9.

Proteomic databases

PaxDbQ9R0P9.
PRIDEQ9R0P9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031131; ENSMUSP00000031131; ENSMUSG00000029223.
GeneID22223.
KEGGmmu:22223.
UCSCuc008xpf.2. mouse.

Organism-specific databases

CTD7345.
MGIMGI:103149. Uchl1.

Phylogenomic databases

eggNOGNOG327708.
GeneTreeENSGT00510000046640.
HOVERGENHBG075483.
InParanoidQ9R0P9.
KOK05611.
OMAKSHENGH.
OrthoDBEOG7S7SFK.
PhylomeDBQ9R0P9.
TreeFamTF316166.

Enzyme and pathway databases

BRENDA3.4.19.12. 3474.

Gene expression databases

ArrayExpressQ9R0P9.
BgeeQ9R0P9.
CleanExMM_UCHL1.
GenevestigatorQ9R0P9.

Family and domain databases

Gene3D3.40.532.10. 1 hit.
InterProIPR001578. Peptidase_C12_UCH.
[Graphical view]
PANTHERPTHR10589. PTHR10589. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSPR00707. UBCTHYDRLASE.
PROSITEPS00140. UCH_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUCHL1. mouse.
NextBio302243.
PROQ9R0P9.
SOURCESearch...

Entry information

Entry nameUCHL1_MOUSE
AccessionPrimary (citable) accession number: Q9R0P9
Secondary accession number(s): Q9R122
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 125 of the entry and version 1 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