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Protein

Ubiquitin carboxyl-terminal hydrolase isozyme L1

Gene

Uchl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

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).

Kineticsi

  1. KM=116 nM for Ub-AMC1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901NucleophileCurated
Active sitei161 – 1611Proton donorPROSITE-ProRule annotation
Sitei176 – 1761Important for enzyme activityBy similarity

GO - Molecular functioni

  1. alpha-2A adrenergic receptor binding Source: MGI
  2. cysteine-type endopeptidase activity Source: UniProtKB
  3. ligase activity Source: UniProtKB-KW
  4. omega peptidase activity Source: UniProtKB
  5. ubiquitin binding Source: UniProtKB
  6. ubiquitin-specific protease activity Source: MGI

GO - Biological processi

  1. adult walking behavior Source: MGI
  2. axonogenesis Source: MGI
  3. axon target recognition Source: MGI
  4. axon transport of mitochondrion Source: MGI
  5. cell proliferation Source: MGI
  6. eating behavior Source: MGI
  7. muscle fiber development Source: MGI
  8. negative regulation of MAP kinase activity Source: MGI
  9. neuromuscular process Source: MGI
  10. protein deubiquitination Source: UniProtKB
  11. response to ischemia Source: MGI
  12. sensory perception of pain Source: Ensembl
  13. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi3.4.19.12. 3474.

Protein family/group databases

MEROPSiC12.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase isozyme L1 (EC:3.4.19.12, EC:6.-.-.-)
Short name:
UCH-L1
Alternative name(s):
Neuron cytoplasmic protein 9.5
PGP 9.5
Short name:
PGP9.5
Ubiquitin thioesterase L1
Gene namesi
Name:Uchl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:103149. Uchl1.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Endoplasmic reticulum membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

  1. axon Source: MGI
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: MGI
  4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  5. extracellular vesicular exosome Source: MGI
  6. myelin sheath Source: UniProtKB
  7. neuronal cell body Source: MGI
  8. nucleoplasm Source: MGI
  9. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301D → K: Abolishes enzymatic activity and ubiquitin binding. 1 Publication
Mutagenesisi90 – 901C → S: Abolishes enzymatic activity, but does not affect ubiquitin binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220Ubiquitin carboxyl-terminal hydrolase isozyme L1PRO_0000211058Add
BLAST
Propeptidei221 – 2233Removed in mature formBy similarityPRO_0000414313

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi220 – 2201S-farnesyl cysteineBy similarity

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Prenylation

Proteomic databases

MaxQBiQ9R0P9.
PaxDbiQ9R0P9.
PRIDEiQ9R0P9.

2D gel databases

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

PTM databases

PhosphoSiteiQ9R0P9.

Expressioni

Tissue specificityi

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.5 Publications

Gene expression databases

BgeeiQ9R0P9.
CleanExiMM_UCHL1.
ExpressionAtlasiQ9R0P9. baseline and differential.
GenevestigatoriQ9R0P9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi204423. 9 interactions.
IntActiQ9R0P9. 5 interactions.
MINTiMINT-4139420.
STRINGi10090.ENSMUSP00000031131.

Structurei

3D structure databases

ProteinModelPortaliQ9R0P9.
SMRiQ9R0P9. Positions 1-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5 – 106Interaction with ubiquitinBy similarity
Regioni151 – 1566Interaction with ubiquitinBy similarity
Regioni211 – 2166Interaction with ubiquitinBy similarity

Sequence similaritiesi

Belongs to the peptidase C12 family.Curated

Phylogenomic databases

eggNOGiNOG327708.
GeneTreeiENSGT00510000046640.
HOVERGENiHBG075483.
InParanoidiQ9R0P9.
KOiK05611.
OMAiMEWKPME.
OrthoDBiEOG7S7SFK.
PhylomeDBiQ9R0P9.
TreeFamiTF316166.

Family and domain databases

Gene3Di3.40.532.10. 1 hit.
InterProiIPR001578. Peptidase_C12_UCH.
IPR030297. UCHL1.
[Graphical view]
PANTHERiPTHR10589. PTHR10589. 1 hit.
PTHR10589:SF19. PTHR10589:SF19. 1 hit.
PfamiPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSiPR00707. UBCTHYDRLASE.
PROSITEiPS00140. UCH_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R0P9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLKPMEINP EMLNKVLAKL GVAGQWRFAD VLGLEEETLG SVPSPACALL
60 70 80 90 100
LLFPLTAQHE NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA
110 120 130 140 150
NNQDKLEFED GSVLKQFLSE TEKLSPEDRA KCFEKNEAIQ AAHDSVAQEG
160 170 180 190 200
QCRVDDKVNF HFILFNNVDG HLYELDGRMP FPVNHGASSE DSLLQDAAKV
210 220
CREFTEREQG EVRFSAVALC KAA
Length:223
Mass (Da):24,838
Last modified:May 1, 2000 - v1
Checksum:iF1402BF7B0C077EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491E → K in AAD51029 (PubMed:12559414).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025313 mRNA. Translation: BAA84083.1.
AF172334 mRNA. Translation: AAD51029.1.
AK013729 mRNA. Translation: BAB28976.1.
BC039177 mRNA. Translation: AAH39177.1.
CCDSiCCDS19315.1.
RefSeqiNP_035800.2. NM_011670.2.
UniGeneiMm.29807.

Genome annotation databases

EnsembliENSMUST00000031131; ENSMUSP00000031131; ENSMUSG00000029223.
GeneIDi22223.
KEGGimmu:22223.
UCSCiuc008xpf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025313 mRNA. Translation: BAA84083.1.
AF172334 mRNA. Translation: AAD51029.1.
AK013729 mRNA. Translation: BAB28976.1.
BC039177 mRNA. Translation: AAH39177.1.
CCDSiCCDS19315.1.
RefSeqiNP_035800.2. NM_011670.2.
UniGeneiMm.29807.

3D structure databases

ProteinModelPortaliQ9R0P9.
SMRiQ9R0P9. Positions 1-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204423. 9 interactions.
IntActiQ9R0P9. 5 interactions.
MINTiMINT-4139420.
STRINGi10090.ENSMUSP00000031131.

Chemistry

BindingDBiQ9R0P9.

Protein family/group databases

MEROPSiC12.001.

PTM databases

PhosphoSiteiQ9R0P9.

2D gel databases

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

Proteomic databases

MaxQBiQ9R0P9.
PaxDbiQ9R0P9.
PRIDEiQ9R0P9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031131; ENSMUSP00000031131; ENSMUSG00000029223.
GeneIDi22223.
KEGGimmu:22223.
UCSCiuc008xpf.2. mouse.

Organism-specific databases

CTDi7345.
MGIiMGI:103149. Uchl1.

Phylogenomic databases

eggNOGiNOG327708.
GeneTreeiENSGT00510000046640.
HOVERGENiHBG075483.
InParanoidiQ9R0P9.
KOiK05611.
OMAiMEWKPME.
OrthoDBiEOG7S7SFK.
PhylomeDBiQ9R0P9.
TreeFamiTF316166.

Enzyme and pathway databases

BRENDAi3.4.19.12. 3474.

Miscellaneous databases

ChiTaRSiUchl1. mouse.
NextBioi302243.
PROiQ9R0P9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0P9.
CleanExiMM_UCHL1.
ExpressionAtlasiQ9R0P9. baseline and differential.
GenevestigatoriQ9R0P9.

Family and domain databases

Gene3Di3.40.532.10. 1 hit.
InterProiIPR001578. Peptidase_C12_UCH.
IPR030297. UCHL1.
[Graphical view]
PANTHERiPTHR10589. PTHR10589. 1 hit.
PTHR10589:SF19. PTHR10589:SF19. 1 hit.
PfamiPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSiPR00707. UBCTHYDRLASE.
PROSITEiPS00140. UCH_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiUCHL1_MOUSE
AccessioniPrimary (citable) accession number: Q9R0P9
Secondary accession number(s): Q9R122
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.