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Q00981

- UCHL1_RAT

UniProt

Q00981 - UCHL1_RAT

Protein

Ubiquitin carboxyl-terminal hydrolase isozyme L1

Gene

Uchl1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      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 By similarity.By similarity

    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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1 – 11Susceptible to oxidationBy similarity
    Sitei6 – 61Susceptible to oxidationBy similarity
    Sitei12 – 121Susceptible to oxidationBy similarity
    Active sitei90 – 901NucleophilePROSITE-ProRule annotation
    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: Ensembl
    2. ligase activity Source: UniProtKB-KW
    3. omega peptidase activity Source: Ensembl
    4. ubiquitin-specific protease activity Source: InterPro
    5. ubiquitin thiolesterase activity Source: Ensembl

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Ligase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    BRENDAi3.4.19.12. 5301.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 14

    Organism-specific databases

    RGDi3928. Uchl1.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cytosol Source: Ensembl
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. neuronal cell body Source: Ensembl
    5. nucleus Source: Ensembl
    6. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 220220Ubiquitin carboxyl-terminal hydrolase isozyme L1PRO_0000211060Add
    BLAST
    Propeptidei221 – 2233Removed in mature formBy similarityPRO_0000414315

    Amino acid modifications

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

    Post-translational modificationi

    O-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein, Lipoprotein, Oxidation, Prenylation

    Proteomic databases

    PaxDbiQ00981.
    PRIDEiQ00981.

    2D gel databases

    World-2DPAGE0004:Q00981.

    PTM databases

    PhosphoSiteiQ00981.

    Expressioni

    Gene expression databases

    GenevestigatoriQ00981.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. Interacts with COPS5 By similarity. Interacts with SNCA.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi248179. 1 interaction.
    IntActiQ00981. 1 interaction.
    STRINGi10116.ENSRNOP00000056108.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00981.
    SMRiQ00981. 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.
    HOGENOMiHOG000182400.
    HOVERGENiHBG075483.
    KOiK05611.
    OMAiKSHENGH.
    OrthoDBiEOG7S7SFK.
    PhylomeDBiQ00981.

    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.

    Q00981-1 [UniParc]FASTAAdd to Basket

    « Hide

    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:July 5, 2005 - v2
    Checksum:iF1402BF7B0C077EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381T → I in BAA01541. (PubMed:1331034)Curated
    Sequence conflicti96 – 961I → M in BAA01541. (PubMed:1331034)Curated
    Sequence conflicti105 – 1073KLE → NLG in BAA01541. (PubMed:1331034)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10699 mRNA. Translation: BAA01541.1.
    BC060573 mRNA. Translation: AAH60573.1.
    PIRiJX0222.
    RefSeqiNP_058933.2. NM_017237.3.
    UniGeneiRn.107213.

    Genome annotation databases

    EnsembliENSRNOT00000003248; ENSRNOP00000003248; ENSRNOG00000002343.
    GeneIDi29545.
    KEGGirno:29545.
    UCSCiRGD:3928. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10699 mRNA. Translation: BAA01541.1 .
    BC060573 mRNA. Translation: AAH60573.1 .
    PIRi JX0222.
    RefSeqi NP_058933.2. NM_017237.3.
    UniGenei Rn.107213.

    3D structure databases

    ProteinModelPortali Q00981.
    SMRi Q00981. Positions 1-223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248179. 1 interaction.
    IntActi Q00981. 1 interaction.
    STRINGi 10116.ENSRNOP00000056108.

    Chemistry

    BindingDBi Q00981.

    Protein family/group databases

    MEROPSi C12.001.

    PTM databases

    PhosphoSitei Q00981.

    2D gel databases

    World-2DPAGE 0004:Q00981.

    Proteomic databases

    PaxDbi Q00981.
    PRIDEi Q00981.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000003248 ; ENSRNOP00000003248 ; ENSRNOG00000002343 .
    GeneIDi 29545.
    KEGGi rno:29545.
    UCSCi RGD:3928. rat.

    Organism-specific databases

    CTDi 7345.
    RGDi 3928. Uchl1.

    Phylogenomic databases

    eggNOGi NOG327708.
    GeneTreei ENSGT00510000046640.
    HOGENOMi HOG000182400.
    HOVERGENi HBG075483.
    KOi K05611.
    OMAi KSHENGH.
    OrthoDBi EOG7S7SFK.
    PhylomeDBi Q00981.

    Enzyme and pathway databases

    BRENDAi 3.4.19.12. 5301.

    Miscellaneous databases

    NextBioi 609557.
    PROi Q00981.

    Gene expression databases

    Genevestigatori Q00981.

    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. "cDNA cloning and tissue distribution of a rat ubiquitin carboxyl-terminal hydrolase PGP9.5."
      Kajimoto Y., Hashimoto T., Shirai Y., Nishino N., Kuno T., Tanaka C.
      J. Biochem. 112:28-32(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "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: Pituitary.
    3. Lubec G., Boddul S., Afjehi-Sadat L., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 20-27; 84-123 AND 132-199, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Spinal cord.
    4. "Cytosolic O-glycosylation is abundant in nerve terminals."
      Cole R.N., Hart G.W.
      J. Neurochem. 79:1080-1089(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
    5. "The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility."
      Liu Y., Fallon L., Lashuel H.A., Liu Z., Lansbury P.T. Jr.
      Cell 111:209-218(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNCA.

    Entry informationi

    Entry nameiUCHL1_RAT
    AccessioniPrimary (citable) accession number: Q00981
    Secondary accession number(s): Q6P9V8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3