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Q9R0P9

- UCHL1_MOUSE

UniProt

Q9R0P9 - UCHL1_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase isozyme L1

Gene

Uchl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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
    Sitei1 – 11Susceptible to oxidationBy similarity
    Sitei6 – 61Susceptible to oxidationBy similarity
    Sitei12 – 121Susceptible to oxidationBy similarity
    Active sitei90 – 901NucleophileCurated
    Active sitei161 – 1611Proton donorPROSITE-ProRule annotation
    Sitei176 – 1761Important for enzyme activityBy similarity
    Sitei179 – 1791Susceptible to oxidationBy similarity
    Sitei220 – 2201Susceptible to oxidationBy similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. ligase activity Source: UniProtKB-KW
    3. omega peptidase activity Source: UniProtKB
    4. ubiquitin binding Source: UniProtKB
    5. ubiquitin-specific protease activity Source: InterPro
    6. ubiquitin thiolesterase 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: Ensembl
    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: Ensembl

    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: Chromosome 5

    Organism-specific databases

    MGIiMGI:103149. Uchl1.

    Subcellular locationi

    Cytoplasm 1 Publication. 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. neuronal cell body Source: MGI
    6. nucleus Source: Ensembl
    7. plasma membrane Source: Ensembl

    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, Oxidation, 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

    ArrayExpressiQ9R0P9.
    BgeeiQ9R0P9.
    CleanExiMM_UCHL1.
    GenevestigatoriQ9R0P9.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi204423. 7 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.
    OMAiKSHENGH.
    OrthoDBiEOG7S7SFK.
    PhylomeDBiQ9R0P9.
    TreeFamiTF316166.

    Family and domain databases

    Gene3Di3.40.532.10. 1 hit.
    InterProiIPR001578. Peptidase_C12_UCH.
    [Graphical view]
    PANTHERiPTHR10589. PTHR10589. 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

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    MQLKPMEINP EMLNKVLAKL GVAGQWRFAD VLGLEEETLG SVPSPACALL    50
    LLFPLTAQHE NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA 100
    NNQDKLEFED GSVLKQFLSE TEKLSPEDRA KCFEKNEAIQ AAHDSVAQEG 150
    QCRVDDKVNF HFILFNNVDG HLYELDGRMP FPVNHGASSE DSLLQDAAKV 200
    CREFTEREQG EVRFSAVALC KAA 223
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025313 mRNA. Translation: BAA84083.1 .
    AF172334 mRNA. Translation: AAD51029.1 .
    AK013729 mRNA. Translation: BAB28976.1 .
    BC039177 mRNA. Translation: AAH39177.1 .
    CCDSi CCDS19315.1.
    RefSeqi NP_035800.2. NM_011670.2.
    UniGenei Mm.29807.

    3D structure databases

    ProteinModelPortali Q9R0P9.
    SMRi Q9R0P9. Positions 1-223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204423. 7 interactions.
    IntActi Q9R0P9. 5 interactions.
    MINTi MINT-4139420.
    STRINGi 10090.ENSMUSP00000031131.

    Chemistry

    BindingDBi Q9R0P9.

    Protein family/group databases

    MEROPSi C12.001.

    PTM databases

    PhosphoSitei Q9R0P9.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00313962.
    Q9R0P9.
    UCD-2DPAGE Q9R0P9.

    Proteomic databases

    MaxQBi Q9R0P9.
    PaxDbi Q9R0P9.
    PRIDEi Q9R0P9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031131 ; ENSMUSP00000031131 ; ENSMUSG00000029223 .
    GeneIDi 22223.
    KEGGi mmu:22223.
    UCSCi uc008xpf.2. mouse.

    Organism-specific databases

    CTDi 7345.
    MGIi MGI:103149. Uchl1.

    Phylogenomic databases

    eggNOGi NOG327708.
    GeneTreei ENSGT00510000046640.
    HOVERGENi HBG075483.
    InParanoidi Q9R0P9.
    KOi K05611.
    OMAi KSHENGH.
    OrthoDBi EOG7S7SFK.
    PhylomeDBi Q9R0P9.
    TreeFami TF316166.

    Enzyme and pathway databases

    BRENDAi 3.4.19.12. 3474.

    Miscellaneous databases

    ChiTaRSi UCHL1. mouse.
    NextBioi 302243.
    PROi Q9R0P9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9R0P9.
    Bgeei Q9R0P9.
    CleanExi MM_UCHL1.
    Genevestigatori Q9R0P9.

    Family and domain databases

    Gene3Di 3.40.532.10. 1 hit.
    InterProi IPR001578. Peptidase_C12_UCH.
    [Graphical view ]
    PANTHERi PTHR10589. PTHR10589. 1 hit.
    Pfami PF01088. Peptidase_C12. 1 hit.
    [Graphical view ]
    PRINTSi PR00707. UBCTHYDRLASE.
    PROSITEi PS00140. UCH_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 128 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