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P15374

- UCHL3_HUMAN

UniProt

P15374 - UCHL3_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase isozyme L3

Gene

UCHL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.5 Publications

    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).3 Publications

    Enzyme regulationi

    Inhibited by monoubiquitin and diubiquitin.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei95 – 951Nucleophile
    Active sitei169 – 1691Proton donorCurated
    Sitei184 – 1841Important for enzyme activityBy similarity

    GO - Molecular functioni

    1. peptidase activity Source: UniProtKB
    2. protein binding Source: IntAct
    3. ubiquitin binding Source: UniProtKB
    4. ubiquitin-specific protease activity Source: InterPro
    5. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. protein catabolic process Source: UniProtKB
    2. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    SABIO-RKP15374.

    Protein family/group databases

    MEROPSiC12.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase isozyme L3 (EC:3.4.19.12)
    Short name:
    UCH-L3
    Alternative name(s):
    Ubiquitin thioesterase L3
    Gene namesi
    Name:UCHL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:12515. UCHL3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi33 – 331D → A: Decreased interaction with diubiquitin. No accumulation of free diubiquitin. Decreased levels of polyubiquitinated lysozyme. 2 Publications
    Mutagenesisi95 – 951C → A: Increased interaction with diubiquitin. 3 Publications
    Mutagenesisi95 – 951C → S: Abolishes enzymatic activity. Increased interaction with diubiquitin. 3 Publications

    Organism-specific databases

    PharmGKBiPA37162.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 230230Ubiquitin carboxyl-terminal hydrolase isozyme L3PRO_0000211061Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP15374.
    PaxDbiP15374.
    PeptideAtlasiP15374.
    PRIDEiP15374.

    2D gel databases

    OGPiP15374.
    REPRODUCTION-2DPAGEIPI00011250.

    PTM databases

    PhosphoSiteiP15374.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, skeletal muscle, and testis.1 Publication

    Gene expression databases

    BgeeiP15374.
    CleanExiHS_UCHL3.
    GenevestigatoriP15374.

    Organism-specific databases

    HPAiHPA019678.

    Interactioni

    Subunit structurei

    Preferentially binds diubiquitin; the interaction does not hydrolyze diubiquitin but, in vitro, inhibits the hydrolyzing activity on other substrates.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SMAD1Q157972EBI-954554,EBI-1567153

    Protein-protein interaction databases

    BioGridi113194. 57 interactions.
    DIPiDIP-29135N.
    IntActiP15374. 10 interactions.
    MINTiMINT-2863935.
    STRINGi9606.ENSP00000366819.

    Structurei

    Secondary structure

    1
    230
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2210
    Beta strandi29 – 335
    Helixi39 – 424
    Beta strandi49 – 579
    Helixi60 – 7617
    Helixi92 – 943
    Helixi95 – 10511
    Helixi106 – 1105
    Helixi118 – 1269
    Helixi131 – 1399
    Helixi142 – 15211
    Beta strandi155 – 1573
    Beta strandi168 – 1769
    Beta strandi179 – 1835
    Beta strandi187 – 1893
    Beta strandi191 – 1955
    Turni198 – 2003
    Helixi201 – 21515
    Beta strandi223 – 2297

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UCHX-ray1.80A1-230[»]
    1XD3X-ray1.45A/C1-230[»]
    ProteinModelPortaliP15374.
    SMRiP15374. Positions 2-230.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15374.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni8 – 136Interaction with ubiquitin
    Regioni152 – 1598Interaction with ubiquitin
    Regioni219 – 2246Interaction with ubiquitin

    Sequence similaritiesi

    Belongs to the peptidase C12 family.Curated

    Phylogenomic databases

    eggNOGiNOG327708.
    HOGENOMiHOG000182400.
    HOVERGENiHBG075483.
    KOiK05609.
    OMAiYETFRTE.
    OrthoDBiEOG7S7SFK.
    PhylomeDBiP15374.
    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.

    P15374-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMDPE LLSMVPRPVC    50
    AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL 100
    IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERARYLEN YDAIRVTHET 150
    SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGETSDET 200
    LLEDAIEVCK KFMERDPDEL RFNAIALSAA 230
    Length:230
    Mass (Da):26,183
    Last modified:April 1, 1990 - v1
    Checksum:i8ACACE6E1D86FD55
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30496 mRNA. Translation: AAA36791.1.
    BT019359 mRNA. Translation: AAV38166.1.
    CR456855 mRNA. Translation: CAG33136.1.
    AK313665 mRNA. Translation: BAG36417.1.
    AL137244 Genomic DNA. Translation: CAI12419.1.
    CH471093 Genomic DNA. Translation: EAW80542.1.
    BC018125 mRNA. Translation: AAH18125.1.
    CCDSiCCDS9453.1.
    PIRiA40085.
    RefSeqiNP_001257881.1. NM_001270952.1.
    NP_005993.1. NM_006002.4.
    UniGeneiHs.162241.

    Genome annotation databases

    EnsembliENST00000377595; ENSP00000366819; ENSG00000118939.
    GeneIDi7347.
    KEGGihsa:7347.
    UCSCiuc001vjq.4. human.

    Polymorphism databases

    DMDMi136682.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30496 mRNA. Translation: AAA36791.1 .
    BT019359 mRNA. Translation: AAV38166.1 .
    CR456855 mRNA. Translation: CAG33136.1 .
    AK313665 mRNA. Translation: BAG36417.1 .
    AL137244 Genomic DNA. Translation: CAI12419.1 .
    CH471093 Genomic DNA. Translation: EAW80542.1 .
    BC018125 mRNA. Translation: AAH18125.1 .
    CCDSi CCDS9453.1.
    PIRi A40085.
    RefSeqi NP_001257881.1. NM_001270952.1.
    NP_005993.1. NM_006002.4.
    UniGenei Hs.162241.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UCH X-ray 1.80 A 1-230 [» ]
    1XD3 X-ray 1.45 A/C 1-230 [» ]
    ProteinModelPortali P15374.
    SMRi P15374. Positions 2-230.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113194. 57 interactions.
    DIPi DIP-29135N.
    IntActi P15374. 10 interactions.
    MINTi MINT-2863935.
    STRINGi 9606.ENSP00000366819.

    Chemistry

    BindingDBi P15374.
    ChEMBLi CHEMBL6195.

    Protein family/group databases

    MEROPSi C12.003.

    PTM databases

    PhosphoSitei P15374.

    Polymorphism databases

    DMDMi 136682.

    2D gel databases

    OGPi P15374.
    REPRODUCTION-2DPAGE IPI00011250.

    Proteomic databases

    MaxQBi P15374.
    PaxDbi P15374.
    PeptideAtlasi P15374.
    PRIDEi P15374.

    Protocols and materials databases

    DNASUi 7347.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377595 ; ENSP00000366819 ; ENSG00000118939 .
    GeneIDi 7347.
    KEGGi hsa:7347.
    UCSCi uc001vjq.4. human.

    Organism-specific databases

    CTDi 7347.
    GeneCardsi GC13P076123.
    HGNCi HGNC:12515. UCHL3.
    HPAi HPA019678.
    MIMi 603090. gene.
    neXtProti NX_P15374.
    PharmGKBi PA37162.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327708.
    HOGENOMi HOG000182400.
    HOVERGENi HBG075483.
    KOi K05609.
    OMAi YETFRTE.
    OrthoDBi EOG7S7SFK.
    PhylomeDBi P15374.
    TreeFami TF316166.

    Enzyme and pathway databases

    SABIO-RK P15374.

    Miscellaneous databases

    ChiTaRSi UCHL3. human.
    EvolutionaryTracei P15374.
    GeneWikii UCHL3.
    GenomeRNAii 7347.
    NextBioi 28762.
    PROi P15374.
    SOURCEi Search...

    Gene expression databases

    Bgeei P15374.
    CleanExi HS_UCHL3.
    Genevestigatori P15374.

    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. "The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase."
      Wilkinson K.D., Lee K., Deshpande S., Duerksen-Hughes P., Boss J.M., Pohl J.
      Science 246:670-673(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Lung.
    8. Cited for: FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-95.
    9. "Molecular profiling of the immune response in colon cancer using protein microarrays: occurrence of autoantibodies to ubiquitin C-terminal hydrolase L3."
      Nam M.J., Madoz-Gurpide J., Wang H., Lescure P., Schmalbach C.E., Zhao R., Misek D.E., Kuick R., Brenner D.E., Hanash S.M.
      Proteomics 3:2108-2115(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS TUMOR-ASSOCIATED ANTIGEN BY MASS SPECTROMETRY.
    10. "Substrate profiling of deubiquitin hydrolases with a positional scanning library and mass spectrometry."
      Mason D.E., Ek J., Peters E.C., Harris J.L.
      Biochemistry 43:6535-6544(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Ubiquitin dimers control the hydrolase activity of UCH-L3."
      Setsuie R., Sakurai M., Sakaguchi Y., Wada K.
      Neurochem. Int. 54:314-321(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH UBIQUITIN, FUNCTION, ENZYME REGULATION, MUTAGENESIS OF ASP-33 AND CYS-95.
    14. "Skeletal muscles of Uchl3 knockout mice show polyubiquitinated protein accumulation and stress responses."
      Setsuie R., Suzuki M., Tsuchiya Y., Wada K.
      Neurochem. Int. 56:911-918(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, MUTAGENESIS OF ASP-33 AND CYS-95.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Mutant ubiquitin (UBB(+1)) associated with neurodegenerative disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3)."
      Dennissen F.J., Kholod N., Hermes D.J., Kemmerling N., Steinbusch H.W., Dantuma N.P., van Leeuwen F.W.
      FEBS Lett. 585:2568-2574(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes."
      Iphofer A., Kummer A., Nimtz M., Ritter A., Arnold T., Frank R., van den Heuvel J., Kessler B.M., Jansch L., Franke R.
      ChemBioChem 13:1416-1420(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, LINKAGE SPECIFICITY.
    18. "Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8-A resolution."
      Johnston S.C., Larsen C.N., Cook W.J., Wilkinson K.D., Hill C.P.
      EMBO J. 16:3787-3796(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    19. "Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate."
      Misaghi S., Galardy P.J., Meester W.J.N., Ovaa H., Ploegh H.L., Gaudet R.
      J. Biol. Chem. 280:1512-1520(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH UBIQUITIN VINYLMETHYLESTER, ENZYME ACTIVITY.

    Entry informationi

    Entry nameiUCHL3_HUMAN
    AccessioniPrimary (citable) accession number: P15374
    Secondary accession number(s): B2R970, Q5TBK8, Q6IBE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 147 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Identified as a tumor-specific antigen in colon cancer.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3