Q9Y5K5 (UCHL5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase isozyme L5
Short name=UCH-L5
EC=3.4.19.12

Alternative name(s):
Ubiquitin C-terminal hydrolase UCH37
Ubiquitin thioesterase L5

Gene names

Name:	UCHL5
Synonyms:	UCH37
ORF Names:	AD-019, CGI-70

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.10
Catalytic activity	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 regulation	Activated by ADRM1. Inhibited by interaction with NFRKB. Ref.1 Ref.8 Ref.10
Subunit structure	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. Ref.1 Ref.7 Ref.8 Ref.10 Ref.13
Subcellular location	Cytoplasm. Nucleus. Note: Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus. Ref.10
Sequence similarities	Belongs to the peptidase C12 family.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW forebrain morphogenesis Inferred from electronic annotation. Source: Compara lateral ventricle development Inferred from electronic annotation. Source: Compara midbrain development Inferred from electronic annotation. Source: Compara negative regulation of transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome protein deubiquitination Inferred from direct assay Ref.10. Source: UniProtKB regulation of proteasomal protein catabolic process Inferred from mutant phenotype PubMed 18162577. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	Ino80 complex Inferred from direct assay Ref.13. Source: UniProtKB cytosol Inferred from direct assay Ref.10. Source: UniProtKB proteasome complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	endopeptidase inhibitor activity Inferred from mutant phenotype PubMed 18162577. Source: UniProtKB omega peptidase activity Inferred from electronic annotation. Source: InterPro proteasome binding Inferred from direct assay PubMed 18162577Ref.10. Source: UniProtKB ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTR8	Q9H981	3	EBI-1051183,EBI-769597
ADRM1	Q16186	7	EBI-1051183,EBI-954387
INO80E	Q8NBZ0	7	EBI-1051183,EBI-769401
NFRKB	Q6P4R8	9	EBI-1051183,EBI-2511210
TFPT	P0C1Z6	3	EBI-1051183,EBI-1245626

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q9Y5K5-1)

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.

Isoform 2 (identifier: Q9Y5K5-2)

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

Isoform 3 (identifier: Q9Y5K5-3)

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

Isoform 4 (identifier: Q9Y5K5-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 329

329

Ubiquitin carboxyl-terminal hydrolase isozyme L5

PRO_0000211066

Regions

Region

313 – 329

17

Interaction with ADRM1

Sites

Active site

88

1

Nucleophile Probable

Active site

164

1

Proton donor By similarity

Site

179

1

Important for enzyme activity By similarity

Amino acid modifications

Modified residue

158

1

N6-acetyllysine Ref.11

Natural variations

Alternative sequence

246

1

Missing in isoform 2, isoform 3 and isoform 4.

VSP_005253

Alternative sequence

316 – 329

14

AKEKQ…AQETK → GK in isoform 2.

VSP_005254

Alternative sequence

316 – 329

14

AKEKQ…AQETK → FEKHFEKTLLGK in isoform 4.

VSP_017062

Natural variant

197

1

I → F. Ref.2 Ref.3

VAR_011613

Experimental info

Mutagenesis

88

1

C → A: Abolishes enzymatic activity. Ref.1

Sequence conflict

6

1

G → V in AAD34065. Ref.2

Secondary structure

1

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329

Helix Strand Turn

Details...

Helix

15 – 24

10

Beta strand

28 – 34

7

Turn

40 – 46

7

Beta strand

48 – 56

9

Beta strand

65 – 68

4

Helix

72 – 75

4

Helix

85 – 87

3

Helix

88 – 98

11

Helix

109 – 118

10

Helix

123 – 131

9

Helix

134 – 142

9

Helix

159 – 162

4

Beta strand

163 – 171

9

Beta strand

174 – 178

5

Beta strand

182 – 184

3

Beta strand

186 – 190

5

Beta strand

193 – 195

3

Helix

197 – 213

17

Beta strand

218 – 225

8

Helix

227 – 236

10

Helix

257 – 288

32

Helix

293 – 300

8

Helix

301 – 303

3

Beta strand

304 – 306

3

Turn

307 – 311

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 30, 2006. Version 3. Checksum: DF307347D48C9D0F	FASTA	329	37,607
	10 20 30 40 50 60 MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP 70 80 90 100 110 120 GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS 130 140 150 160 170 180 FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTSAKEE DAFHFVSYVP VNGRLYELDG 190 200 210 220 230 240 LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR 250 260 270 280 290 300 QLAEEEPMDT DQGNSMLSAI QSEVAKNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL 310 320 KTLAEHQQLI PLVEKAKEKQ NAKKAQETK
	Isoform 2 [UniParc]. Checksum: 2552C52F2CFC1E9C	FASTA	316	36,079
	10 20 30 40 50 60 MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP 70 80 90 100 110 120 GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS 130 140 150 160 170 180 FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTSAKEE DAFHFVSYVP VNGRLYELDG 190 200 210 220 230 240 LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR 250 260 270 280 290 300 QLAEEPMDTD QGNSMLSAIQ SEVAKNQMLI EEEVQKLKRY KIENIRRKHN YLPFIMELLK 310 TLAEHQQLIP LVEKGK
	Isoform 3 [UniParc]. Checksum: 2ECFB3AB11D07E72	FASTA	328	37,478
	10 20 30 40 50 60 MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP 70 80 90 100 110 120 GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS 130 140 150 160 170 180 FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTSAKEE DAFHFVSYVP VNGRLYELDG 190 200 210 220 230 240 LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR 250 260 270 280 290 300 QLAEEPMDTD QGNSMLSAIQ SEVAKNQMLI EEEVQKLKRY KIENIRRKHN YLPFIMELLK 310 320 TLAEHQQLIP LVEKAKEKQN AKKAQETK
	Isoform 4 [UniParc]. Checksum: A3570094A7EC96CB	FASTA	326	37,353
	10 20 30 40 50 60 MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP 70 80 90 100 110 120 GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS 130 140 150 160 170 180 FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTSAKEE DAFHFVSYVP VNGRLYELDG 190 200 210 220 230 240 LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR 250 260 270 280 290 300 QLAEEPMDTD QGNSMLSAIQ SEVAKNQMLI EEEVQKLKRY KIENIRRKHN YLPFIMELLK 310 320 TLAEHQQLIP LVEKFEKHFE KTLLGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract] 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, 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, 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, MASS SPECTROMETRY.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00219512.
IPI00219513.
IPI00299313.
IPI00549820.

RefSeq

NP_001186190.1. NM_001199261.1.
NP_001186191.1. NM_001199262.1.
NP_001186192.1. NM_001199263.1.
NP_057068.1. NM_015984.3.

UniGene

Hs.145469.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3A7S	X-ray	2.20	A	1-228	[»]
3IHR	X-ray	2.95	A	2-329	[»]
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	[»]

ProteinModelPortal

Q9Y5K5.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42671N.

IntAct

Q9Y5K5. 54 interactions.

MINT

MINT-2823912.

STRING

9606.ENSP00000356425.

Protein family/group databases

MEROPS

C12.005.

PTM databases

PhosphoSite

Q9Y5K5.

Polymorphism databases

DMDM

108936023.

Proteomic databases

PaxDb

Q9Y5K5.

PRIDE

Q9Y5K5.

Protocols and materials databases

DNASU

51377.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367448; ENSP00000356418; ENSG00000116750.
ENST00000367449; ENSP00000356419; ENSG00000116750.
ENST00000367454; ENSP00000356424; ENSG00000116750.
ENST00000367455; ENSP00000356425; ENSG00000116750.

GeneID

51377.

KEGG

hsa:51377.

UCSC

uc001gsm.3. human.
uc001gso.3. human.
uc001gsp.3. human.
uc001gsq.3. human.

Organism-specific databases

CTD

51377.

GeneCards

GC01M192984.

HGNC

HGNC:19678. UCHL5.

HPA

HPA005908.

MIM

610667. gene.

neXtProt

NX_Q9Y5K5.

PharmGKB

PA134916228.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG321645.

HOVERGEN

HBG056021.

KO

K05610.

OrthoDB

EOG4RBQK0.

PhylomeDB

Q9Y5K5.

Enzyme and pathway databases

BRENDA

3.4.19.12. 2681.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q9Y5K5.

Bgee

Q9Y5K5.

CleanEx

HS_UCHL5.

Genevestigator

Q9Y5K5.

GermOnline

ENSG00000116750. Homo sapiens.

Family and domain databases

Gene3D

3.40.532.10. 1 hit.

InterPro

IPR001578. Peptidase_C12.
IPR017390. Ubiquitinyl_hydrolase_UCH37.
[Graphical view]

PANTHER

PTHR10589. PTHR10589. 1 hit.

Pfam

PF01088. Peptidase_C12. 1 hit.
[Graphical view]

PIRSF

PIRSF038120. Ubiquitinyl_hydrolase_UCH37. 1 hit.

PRINTS

PR00707. UBCTHYDRLASE.

PROSITE

PS00140. UCH_1. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

UCHL5. human.

EvolutionaryTrace

Q9Y5K5.

GenomeRNAi

51377.

NextBio

54875.

SOURCE

Search...

Entry information

Entry name

UCHL5_HUMAN

Accession

Primary (citable) accession number: Q9Y5K5
Secondary accession number(s): Q5LJA6 , Q5LJA7, Q8TBS4, Q96BJ9, Q9H1W5, Q9P0I3, Q9UQN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	May 30, 2006
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.