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Protein

Ubiquitin carboxyl-terminal hydrolase isozyme L5

Gene

UCHL5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • endopeptidase inhibitor activity Source: UniProtKB
  • omega peptidase activity Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • proteasome binding Source: UniProtKB
  • ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:19678. UCHL5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: UniProtKB
  • Ino80 complex Source: UniProtKB
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB-KW
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiUCHL5.
DMDMi108936023.

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

BgeeiQ9Y5K5.
CleanExiHS_UCHL5.
ExpressionAtlasiQ9Y5K5. baseline and differential.
GenevisibleiQ9Y5K5. HS.

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
ADRM1Q1618620EBI-1051183,EBI-954387
INO80EQ8NBZ07EBI-1051183,EBI-769401
NFRKBQ6P4R812EBI-1051183,EBI-2511210
PSMA6P609004EBI-1051183,EBI-357793
PSMD2Q132005EBI-1051183,EBI-357648
PSMD4P550365EBI-1051183,EBI-359318
TFPTP0C1Z63EBI-1051183,EBI-1245626
ZBED1O960063EBI-1051183,EBI-740037

Protein-protein interaction databases

BioGridi119509. 197 interactions.
DIPiDIP-42671N.
IntActiQ9Y5K5. 61 interactions.
MINTiMINT-2823912.
STRINGi9606.ENSP00000356425.

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2410Combined sources
Beta strandi28 – 347Combined sources
Turni40 – 467Combined sources
Beta strandi48 – 569Combined sources
Beta strandi65 – 684Combined sources
Helixi72 – 754Combined sources
Helixi85 – 873Combined sources
Helixi88 – 9811Combined sources
Helixi109 – 11810Combined sources
Helixi123 – 1319Combined sources
Helixi134 – 1429Combined sources
Helixi159 – 1624Combined sources
Beta strandi163 – 1719Combined sources
Beta strandi174 – 1785Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi186 – 1905Combined sources
Beta strandi193 – 1953Combined sources
Helixi197 – 21317Combined sources
Beta strandi218 – 2258Combined sources
Helixi227 – 24317Combined sources
Helixi255 – 28935Combined sources
Helixi293 – 30513Combined sources
Helixi309 – 31810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4UELX-ray2.30A1-329[»]
4UEMX-ray2.82A1-329[»]
4UF5X-ray3.70A1-329[»]
4UF6X-ray3.69A/D/G/J1-329[»]
4WLPX-ray3.10A5-322[»]
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.
GeneTreeiENSGT00510000046560.
HOVERGENiHBG056021.
InParanoidiQ9Y5K5.
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. AlignAdd to basket

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

        10         20         30         40         50
MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH
60 70 80 90 100
GLIFLFKWQP GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC
110 120 130 140 150
THQDVHLGET LSEFKEFSQS FDAAMKGLAL SNSDVIRQVH NSFARQQMFE
160 170 180 190 200
FDTKTSAKEE DAFHFVSYVP VNGRLYELDG LREGPIDLGA CNQDDWISAV
210 220 230 240 250
RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR QLAEEEPMDT
260 270 280 290 300
DQGNSMLSAI QSEVAKNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL
310 320
KTLAEHQQLI PLVEKAKEKQ NAKKAQETK
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:
EMBLi
GenBanki
DDBJi
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.
GeneIDi51377.
KEGGihsa:51377.
UCSCiuc001gsm.3. human. [Q9Y5K5-1]
uc001gso.3. human. [Q9Y5K5-3]
uc001gsp.3. human. [Q9Y5K5-4]
uc001gsq.3. human. [Q9Y5K5-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4UELX-ray2.30A1-329[»]
4UEMX-ray2.82A1-329[»]
4UF5X-ray3.70A1-329[»]
4UF6X-ray3.69A/D/G/J1-329[»]
4WLPX-ray3.10A5-322[»]
ProteinModelPortaliQ9Y5K5.
SMRiQ9Y5K5. Positions 7-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119509. 197 interactions.
DIPiDIP-42671N.
IntActiQ9Y5K5. 61 interactions.
MINTiMINT-2823912.
STRINGi9606.ENSP00000356425.

Protein family/group databases

MEROPSiC12.005.

PTM databases

PhosphoSiteiQ9Y5K5.

Polymorphism and mutation databases

BioMutaiUCHL5.
DMDMi108936023.

Proteomic databases

MaxQBiQ9Y5K5.
PaxDbiQ9Y5K5.
PRIDEiQ9Y5K5.

Protocols and materials databases

DNASUi51377.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51377.
GeneCardsiGC01M192984.
HGNCiHGNC:19678. UCHL5.
HPAiHPA005908.
MIMi610667. gene.
neXtProtiNX_Q9Y5K5.
PharmGKBiPA134916228.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG321645.
GeneTreeiENSGT00510000046560.
HOVERGENiHBG056021.
InParanoidiQ9Y5K5.
KOiK05610.
PhylomeDBiQ9Y5K5.
TreeFamiTF313976.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiUCHL5. human.
EvolutionaryTraceiQ9Y5K5.
GeneWikiiUbiquitin_carboxyl-terminal_hydrolase_L5.
GenomeRNAii51377.
NextBioi54875.
PROiQ9Y5K5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5K5.
CleanExiHS_UCHL5.
ExpressionAtlasiQ9Y5K5. baseline and differential.
GenevisibleiQ9Y5K5. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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.
  16. "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: July 22, 2015
This is version 137 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

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.