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Q9Y5K5

- UCHL5_HUMAN

UniProt

Q9Y5K5 - UCHL5_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase isozyme L5

Gene

UCHL5

Organism
Homo sapiens (Human)
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 3 (30 May 2006)
      Previous versions | rss
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    Functioni

    Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1.2 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).

    Enzyme regulationi

    Activated by ADRM1. Inhibited by interaction with NFRKB.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei88 – 881NucleophileCurated
    Active sitei164 – 1641Proton donorBy similarity
    Sitei179 – 1791Important for enzyme activityBy similarity

    GO - Molecular functioni

    1. endopeptidase inhibitor activity Source: UniProtKB
    2. omega peptidase activity Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. proteasome binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. ubiquitin-specific protease activity Source: UniProtKB

    GO - Biological processi

    1. DNA recombination Source: UniProtKB-KW
    2. DNA repair Source: UniProtKB-KW
    3. forebrain morphogenesis Source: Ensembl
    4. lateral ventricle development Source: Ensembl
    5. midbrain development Source: Ensembl
    6. negative regulation of endopeptidase activity Source: GOC
    7. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    8. protein deubiquitination Source: UniProtKB
    9. regulation of proteasomal protein catabolic process Source: UniProtKB
    10. regulation of transcription, DNA-templated Source: UniProtKB-KW
    11. transcription, DNA-templated Source: UniProtKB-KW
    12. transforming growth factor beta receptor signaling pathway Source: Reactome
    13. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation, Ubl conjugation pathway

    Enzyme and pathway databases

    BRENDAi3.4.19.12. 2681.
    ReactomeiREACT_120727. Downregulation of TGF-beta receptor signaling.
    SignaLinkiQ9Y5K5.

    Protein family/group databases

    MEROPSiC12.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase isozyme L5 (EC:3.4.19.12)
    Short name:
    UCH-L5
    Alternative name(s):
    Ubiquitin C-terminal hydrolase UCH37
    Ubiquitin thioesterase L5
    Gene namesi
    Name:UCHL5
    Synonyms:UCH37
    ORF Names:AD-019, CGI-70
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19678. UCHL5.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. Ino80 complex Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. proteasome complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi88 – 881C → A: Abolishes enzymatic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134916228.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329Ubiquitin carboxyl-terminal hydrolase isozyme L5PRO_0000211066Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei47 – 471N6-succinyllysineBy similarity
    Modified residuei158 – 1581N6-acetyllysine1 Publication
    Modified residuei289 – 2891N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9Y5K5.
    PaxDbiQ9Y5K5.
    PRIDEiQ9Y5K5.

    PTM databases

    PhosphoSiteiQ9Y5K5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y5K5.
    BgeeiQ9Y5K5.
    CleanExiHS_UCHL5.
    GenevestigatoriQ9Y5K5.

    Organism-specific databases

    HPAiHPA005908.

    Interactioni

    Subunit structurei

    Component of the 19S (PA700) regulatory complex of the 26S proteasome. Interacts with ADRM1 and NFRKB; in vitro ADRM1 and NFRKB compete for interaction with UCHL5. Component of the INO80 complex; specifically part of a complex module associated with N-terminus of INO80.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTR8Q9H9813EBI-1051183,EBI-769597
    ADRM1Q1618617EBI-1051183,EBI-954387
    INO80EQ8NBZ07EBI-1051183,EBI-769401
    NFRKBQ6P4R89EBI-1051183,EBI-2511210
    PSMA6P609004EBI-1051183,EBI-357793
    PSMD2Q132005EBI-1051183,EBI-357648
    PSMD4P550365EBI-1051183,EBI-359318
    TFPTP0C1Z63EBI-1051183,EBI-1245626

    Protein-protein interaction databases

    BioGridi119509. 186 interactions.
    DIPiDIP-42671N.
    IntActiQ9Y5K5. 58 interactions.
    MINTiMINT-2823912.
    STRINGi9606.ENSP00000356425.

    Structurei

    Secondary structure

    1
    329
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 2410
    Beta strandi28 – 347
    Turni40 – 467
    Beta strandi48 – 569
    Beta strandi65 – 684
    Helixi72 – 754
    Helixi85 – 873
    Helixi88 – 9811
    Helixi109 – 11810
    Helixi123 – 1319
    Helixi134 – 1429
    Helixi159 – 1624
    Beta strandi163 – 1719
    Beta strandi174 – 1785
    Beta strandi182 – 1843
    Beta strandi186 – 1905
    Beta strandi193 – 1953
    Helixi197 – 21317
    Beta strandi218 – 2258
    Helixi227 – 23610
    Helixi257 – 28832
    Helixi293 – 3008
    Helixi301 – 3033
    Beta strandi304 – 3063
    Turni307 – 3115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A7SX-ray2.20A1-228[»]
    3IHRX-ray2.95A1-329[»]
    3RIIX-ray2.00A/B1-228[»]
    3RISX-ray2.40A/B/C/D1-240[»]
    3TB3X-ray2.30A/B1-227[»]
    ProteinModelPortaliQ9Y5K5.
    SMRiQ9Y5K5. Positions 7-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y5K5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni313 – 32917Interaction with ADRM1Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C12 family.Curated

    Phylogenomic databases

    eggNOGiNOG321645.
    HOVERGENiHBG056021.
    KOiK05610.
    PhylomeDBiQ9Y5K5.
    TreeFamiTF313976.

    Family and domain databases

    Gene3Di3.40.532.10. 1 hit.
    InterProiIPR001578. Peptidase_C12_UCH.
    IPR017390. Ubiquitinyl_hydrolase_UCH37.
    [Graphical view]
    PANTHERiPTHR10589. PTHR10589. 1 hit.
    PfamiPF01088. Peptidase_C12. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038120. Ubiquitinyl_hydrolase_UCH37. 1 hit.
    PRINTSiPR00707. UBCTHYDRLASE.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q9Y5K5-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH    50
    GLIFLFKWQP GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC 100
    THQDVHLGET LSEFKEFSQS FDAAMKGLAL SNSDVIRQVH NSFARQQMFE 150
    FDTKTSAKEE DAFHFVSYVP VNGRLYELDG LREGPIDLGA CNQDDWISAV 200
    RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR QLAEEEPMDT 250
    DQGNSMLSAI QSEVAKNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL 300
    KTLAEHQQLI PLVEKAKEKQ NAKKAQETK 329
    Length:329
    Mass (Da):37,607
    Last modified:May 30, 2006 - v3
    Checksum:iDF307347D48C9D0F
    GO
    Isoform 2 (identifier: Q9Y5K5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         246-246: Missing.
         316-329: AKEKQNAKKAQETK → GK

    Show »
    Length:316
    Mass (Da):36,079
    Checksum:i2552C52F2CFC1E9C
    GO
    Isoform 3 (identifier: Q9Y5K5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         246-246: Missing.

    Show »
    Length:328
    Mass (Da):37,478
    Checksum:i2ECFB3AB11D07E72
    GO
    Isoform 4 (identifier: Q9Y5K5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         246-246: Missing.
         316-329: AKEKQNAKKAQETK → FEKHFEKTLLGK

    Note: No experimental confirmation available.

    Show »
    Length:326
    Mass (Da):37,353
    Checksum:iA3570094A7EC96CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61G → V in AAD34065. (PubMed:10810093)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti197 – 1971I → F.2 Publications
    VAR_011613

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei246 – 2461Missing in isoform 2, isoform 3 and isoform 4. 4 PublicationsVSP_005253
    Alternative sequencei316 – 32914AKEKQ…AQETK → GK in isoform 2. 2 PublicationsVSP_005254Add
    BLAST
    Alternative sequencei316 – 32914AKEKQ…AQETK → FEKHFEKTLLGK in isoform 4. 1 PublicationVSP_017062Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF147717 mRNA. Translation: AAD31528.1.
    AF151828 mRNA. Translation: AAD34065.1.
    AF157320 mRNA. Translation: AAF67486.1.
    BT006790 mRNA. Translation: AAP35436.1.
    AL136370 Genomic DNA. Translation: CAI10829.1.
    AL136370 Genomic DNA. Translation: CAI10830.1.
    AL136370 Genomic DNA. Translation: CAI10831.1.
    AL136370 Genomic DNA. Translation: CAI10833.1.
    BC015521 mRNA. Translation: AAH15521.1.
    BC025369 mRNA. Translation: AAH25369.1.
    CCDSiCCDS1378.1. [Q9Y5K5-1]
    CCDS55668.1. [Q9Y5K5-3]
    CCDS55669.1. [Q9Y5K5-2]
    CCDS55670.1. [Q9Y5K5-4]
    RefSeqiNP_001186190.1. NM_001199261.1. [Q9Y5K5-3]
    NP_001186191.1. NM_001199262.1. [Q9Y5K5-4]
    NP_001186192.1. NM_001199263.1. [Q9Y5K5-2]
    NP_057068.1. NM_015984.3. [Q9Y5K5-1]
    UniGeneiHs.145469.

    Genome annotation databases

    EnsembliENST00000367448; ENSP00000356418; ENSG00000116750. [Q9Y5K5-4]
    ENST00000367449; ENSP00000356419; ENSG00000116750. [Q9Y5K5-2]
    ENST00000367454; ENSP00000356424; ENSG00000116750. [Q9Y5K5-3]
    ENST00000367455; ENSP00000356425; ENSG00000116750. [Q9Y5K5-1]
    GeneIDi51377.
    KEGGihsa:51377.
    UCSCiuc001gsm.3. human. [Q9Y5K5-1]
    uc001gso.3. human. [Q9Y5K5-3]
    uc001gsp.3. human. [Q9Y5K5-4]
    uc001gsq.3. human. [Q9Y5K5-2]

    Polymorphism databases

    DMDMi108936023.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF147717 mRNA. Translation: AAD31528.1 .
    AF151828 mRNA. Translation: AAD34065.1 .
    AF157320 mRNA. Translation: AAF67486.1 .
    BT006790 mRNA. Translation: AAP35436.1 .
    AL136370 Genomic DNA. Translation: CAI10829.1 .
    AL136370 Genomic DNA. Translation: CAI10830.1 .
    AL136370 Genomic DNA. Translation: CAI10831.1 .
    AL136370 Genomic DNA. Translation: CAI10833.1 .
    BC015521 mRNA. Translation: AAH15521.1 .
    BC025369 mRNA. Translation: AAH25369.1 .
    CCDSi CCDS1378.1. [Q9Y5K5-1 ]
    CCDS55668.1. [Q9Y5K5-3 ]
    CCDS55669.1. [Q9Y5K5-2 ]
    CCDS55670.1. [Q9Y5K5-4 ]
    RefSeqi NP_001186190.1. NM_001199261.1. [Q9Y5K5-3 ]
    NP_001186191.1. NM_001199262.1. [Q9Y5K5-4 ]
    NP_001186192.1. NM_001199263.1. [Q9Y5K5-2 ]
    NP_057068.1. NM_015984.3. [Q9Y5K5-1 ]
    UniGenei Hs.145469.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3A7S X-ray 2.20 A 1-228 [» ]
    3IHR X-ray 2.95 A 1-329 [» ]
    3RII X-ray 2.00 A/B 1-228 [» ]
    3RIS X-ray 2.40 A/B/C/D 1-240 [» ]
    3TB3 X-ray 2.30 A/B 1-227 [» ]
    ProteinModelPortali Q9Y5K5.
    SMRi Q9Y5K5. Positions 7-312.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119509. 186 interactions.
    DIPi DIP-42671N.
    IntActi Q9Y5K5. 58 interactions.
    MINTi MINT-2823912.
    STRINGi 9606.ENSP00000356425.

    Protein family/group databases

    MEROPSi C12.005.

    PTM databases

    PhosphoSitei Q9Y5K5.

    Polymorphism databases

    DMDMi 108936023.

    Proteomic databases

    MaxQBi Q9Y5K5.
    PaxDbi Q9Y5K5.
    PRIDEi Q9Y5K5.

    Protocols and materials databases

    DNASUi 51377.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367448 ; ENSP00000356418 ; ENSG00000116750 . [Q9Y5K5-4 ]
    ENST00000367449 ; ENSP00000356419 ; ENSG00000116750 . [Q9Y5K5-2 ]
    ENST00000367454 ; ENSP00000356424 ; ENSG00000116750 . [Q9Y5K5-3 ]
    ENST00000367455 ; ENSP00000356425 ; ENSG00000116750 . [Q9Y5K5-1 ]
    GeneIDi 51377.
    KEGGi hsa:51377.
    UCSCi uc001gsm.3. human. [Q9Y5K5-1 ]
    uc001gso.3. human. [Q9Y5K5-3 ]
    uc001gsp.3. human. [Q9Y5K5-4 ]
    uc001gsq.3. human. [Q9Y5K5-2 ]

    Organism-specific databases

    CTDi 51377.
    GeneCardsi GC01M192984.
    HGNCi HGNC:19678. UCHL5.
    HPAi HPA005908.
    MIMi 610667. gene.
    neXtProti NX_Q9Y5K5.
    PharmGKBi PA134916228.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG321645.
    HOVERGENi HBG056021.
    KOi K05610.
    PhylomeDBi Q9Y5K5.
    TreeFami TF313976.

    Enzyme and pathway databases

    BRENDAi 3.4.19.12. 2681.
    Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.
    SignaLinki Q9Y5K5.

    Miscellaneous databases

    ChiTaRSi UCHL5. human.
    EvolutionaryTracei Q9Y5K5.
    GeneWikii Ubiquitin_carboxyl-terminal_hydrolase_L5.
    GenomeRNAii 51377.
    NextBioi 54875.
    PROi Q9Y5K5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5K5.
    Bgeei Q9Y5K5.
    CleanExi HS_UCHL5.
    Genevestigatori Q9Y5K5.

    Family and domain databases

    Gene3Di 3.40.532.10. 1 hit.
    InterProi IPR001578. Peptidase_C12_UCH.
    IPR017390. Ubiquitinyl_hydrolase_UCH37.
    [Graphical view ]
    PANTHERi PTHR10589. PTHR10589. 1 hit.
    Pfami PF01088. Peptidase_C12. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038120. Ubiquitinyl_hydrolase_UCH37. 1 hit.
    PRINTSi PR00707. UBCTHYDRLASE.
    ProtoNeti Search...

    Publicationsi

    1. "Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1."
      Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K., Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.
      Nat. Cell Biol. 8:994-1002(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, MUTAGENESIS OF CYS-88, INTERACTION WITH ADRM1.
    2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PHE-197.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PHE-197.
      Tissue: Adrenal gland.
    4. "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] (ISOFORM 3).
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 3 AND 4).
      Tissue: Lung and Uterus.
    7. "A novel proteasome-interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes."
      Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S.
      EMBO J. 25:4524-4536(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ADRM1, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37."
      Qiu X.-B., Ouyang S.-Y., Li C.-J., Miao S., Wang L., Goldberg A.L.
      EMBO J. 25:5742-5753(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ADRM1, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
      Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
      Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex."
      Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.
      Mol. Cell 31:909-917(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN THE INO80 COMPLEX, INTERACTION WITH NFRKB AND ADRM1, ENZYME REGULATION.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
      Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
      J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
    14. "Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5) catalytic domain."
      Nishio K., Kim S.W., Kawai K., Mizushima T., Yamane T., Hamazaki J., Murata S., Tanaka K., Morimoto Y.
      Biochem. Biophys. Res. Commun. 390:855-860(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-228.
    15. "Crystal structure of UCH37."
      Center for eukaryotic structural genomics (CESG)
      Submitted (AUG-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-328.

    Entry informationi

    Entry nameiUCHL5_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5K5
    Secondary accession number(s): Q5LJA6
    , Q5LJA7, Q8TBS4, Q96BJ9, Q9H1W5, Q9P0I3, Q9UQN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3