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Reviewed, UniProtKB/Swiss-Prot Q9R0P9 (UCHL1_MOUSE)

Last modified June 16, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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):
    Ubiquitin thioesterase L1
    Neuron cytoplasmic protein 9.5
    PGP 9.5
      Short name=PGP9.5
Gene names
Name: Uchl1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Homodimer. Interacts with COPS5 and SNCA By similarity.

Subcellular location

Cytoplasm. 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 aand olfactory bulb. Highly expressed in senescent pituitary. Ref.6 Ref.1 Ref.2 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.6 Ref.1

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

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
   Molecular functionHydrolase
Ligase
Protease
Thiol protease
   PTMGlycoprotein
Oxidation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processadult walking behavior

Inferred from mutant phenotype. Source: MGI

axon target recognition

Inferred from mutant phenotype. Source: MGI

axon transport of mitochondrion

Inferred from mutant phenotype. Source: MGI

cell proliferation

Inferred from mutant phenotype. Source: MGI

eating behavior

Inferred from genetic interaction. Source: MGI

neuromuscular process

Inferred from mutant phenotype. Source: MGI

protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

response to stress Ref.7

Inferred from mutant phenotype. Source: MGI

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentaxon

Inferred from direct assay. Source: MGI

cell soma

Inferred from direct assay. Source: MGI

cytosol Ref.6

Inferred from direct assay. Source: MGI

   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 Ref.6

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin thiolesterase activity Ref.6

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 223223Ubiquitin carboxyl-terminal hydrolase isozyme L1
PRO_0000211058

Regions

Region37 – 5418Ubiquitin binding Potential
Region170 – 1789Ubiquitin binding Potential

Sites

Active site901
Active site1611 By similarity
Active site1761 By similarity
Site11Susceptible to oxidation By similarity
Site61Susceptible to oxidation By similarity
Site121Susceptible to oxidation By similarity
Site1791Susceptible to oxidation By similarity
Site2201Susceptible to oxidation 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
Q9R0P9-1 [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: 10471497] [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: 12559414] [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: 16141072] [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: 15489334] [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, 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: 12913066] [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: 14695319] [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: 15911766] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB025313 mRNA. Translation: BAA84083.1.
AF172334 mRNA. Translation: AAD51029.1.
AK013729 mRNA. Translation: BAB28976.1.
BC039177 mRNA. Translation: AAH39177.1.
IPIIPI00313962.
RefSeqNP_035800.2.
UniGeneMm.29807

3D structure databases

HSSPHSSP built from PDB template 1UCH based on UniProtKB P15374.
SMRQ9R0P9. Positions 1-223.
ModBaseSearch...

2-D gel databases

REPRODUCTION-2DPAGEQ9R0P9.

Proteomic databases

PRIDEQ9R0P9.

Genome annotation databases

EnsemblENSMUSG00000029223. Mus musculus. [Contig view]
GeneID22223.
KEGGmmu:22223.

Organism-specific databases

MGIMGI:103149. Uchl1.

Phylogenomic databases

HOVERGENQ9R0P9.
OMAQ9R0P9. CRQFTER.

Enzyme and pathway databases

BRENDA3.4.19.12. 244.

Gene expression databases

ArrayExpressQ9R0P9.
BgeeQ9R0P9.
CleanExMM_UCHL1.
GermOnlineENSMUSG00000029223. Mus musculus.

Family and domain databases

InterProIPR001578. Peptidase_C12.
[Graphical view]
Gene3DG3DSA:3.40.532.10. Peptidase_C12. 1 hit.
PANTHERPTHR10589. Peptidase_C12. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSPR00707. UBCTHYDRLASE.
ProDomPD350662. Peptidase_C12. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00140. UCH_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio302243.
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: June 16, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents