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Q9Y5K5

- UCHL5_HUMAN

UniProt

Q9Y5K5 - UCHL5_HUMAN

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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

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. 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
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: 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
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.

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.
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. 196 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.
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. 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

        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:
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. 196 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.
GeneTreei ENSGT00510000046560.
HOVERGENi HBG056021.
InParanoidi Q9Y5K5.
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

Bgeei Q9Y5K5.
CleanExi HS_UCHL5.
ExpressionAtlasi Q9Y5K5. baseline and differential.
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

« 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. "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 29, 2014
This is version 129 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