P09936 (UCHL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase isozyme L1
Short name=UCH-L1
EC=3.4.19.12
EC=6.-.-.-

Alternative name(s):
Neuron cytoplasmic protein 9.5
PGP 9.5
Short name=PGP9.5
Ubiquitin thioesterase L1

Gene names

Name:

UCHL1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity. Ref.12 Ref.13 Ref.28
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). Ref.20
Subunit structure	Monomer. Homodimer. Interacts with SNCA By similarity. Interacts with COPS5. Ref.14 Ref.19
Subcellular location	Cytoplasm. Endoplasmic reticulum membrane; Lipid-anchor. Note: About 30% of total UCHL1 is associated with membranes in brain. Ref.17
Tissue specificity	Found in neuronal cell bodies and processes throughout the neocortex (at protein level). Expressed in neurons and cells of the diffuse neuroendocrine system and their tumors. Weakly expressed in ovary. Down-regulated in brains from Parkinson disease and Alzheimer disease patients. Ref.5 Ref.12
Post-translational modification	O-glycosylated By similarity.
Involvement in disease	Defects in UCHL1 are the cause of Parkinson disease type 5 (PARK5) [MIM:613643]; also known as Parkinson disease autosomal dominant 5. PARK5 is a complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (resting tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia. Ref.8 Ref.13 Ref.21 Ref.27
Miscellaneous	Oxidation of Met-1, Met-6, Met-12, Met-124 and Met-179 to methionine sulfoxide, and oxidation of Cys-220 to cysteine sulfonic acid have been observed in brains from Alzheimer disease (AD) and Parkinson disease (PD) patients. In AD, UCHL1 was found to be associated with neurofibrillary tangles. In contrast to UCHL3, does not hydrolyze a peptide bond at the C-terminal glycine of NEDD8.
Sequence similarities	Belongs to the peptidase C12 family.
Caution	Ref.8 reports the association of mutation Ile93Met with Parkinson disease. However, according to Ref.27 this association is uncertain and UCHL1 is not a susceptibility gene for Parkinson disease.
Biophysicochemical properties	Kinetic parameters: KM=122 nM for Ub-AMC Ref.8 Ref.11 Ref.21 KM=1.20 µM for ubiquitin ethyl ester Vmax=0.47 µmol/min/mg enzyme toward Ub-AMC Vmax=25 µmol/min/mg enzyme toward ubiquitin ethyl ester
Sequence caution	The sequence CAA28443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Neurodegeneration Parkinson disease Parkinsonism
Molecular function	Hydrolase Ligase Protease Thiol protease
PTM	Acetylation Glycoprotein Lipoprotein Oxidation Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell death Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of MAP kinase activity Inferred from direct assay. Source: BHF-UCL protein deubiquitination Inferred from direct assay. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular function	alpha-2A adrenergic receptor binding Inferred from physical interaction. Source: BHF-UCL cysteine-type endopeptidase activity Inferred from direct assay Ref.11. Source: UniProtKB ligase activity Inferred from electronic annotation. Source: UniProtKB-KW omega peptidase activity Inferred from direct assay. Source: UniProtKB ubiquitin binding Inferred from direct assay. Source: UniProtKB ubiquitin thiolesterase activity Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
COPS5	Q92905	3	EBI-714860,EBI-594661
EGFR	P00533	2	EBI-714860,EBI-297353

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 220

220

Ubiquitin carboxyl-terminal hydrolase isozyme L1

PRO_0000211055

Propeptide

221 – 223

3

Removed in mature form Probable

PRO_0000414311

Regions

Region

5 – 10

6

Interaction with ubiquitin

Region

211 – 216

6

Interaction with ubiquitin

Sites

Active site

90

1

Nucleophile Ref.11 Ref.15 Ref.20

Active site

161

1

Proton donor Ref.11 Ref.15 Ref.20

Site

1

1

Susceptible to oxidation

Site

6

1

Susceptible to oxidation

Site

12

1

Susceptible to oxidation

Site

124

1

Susceptible to oxidation

Site

176

1

Important for enzyme activity

Site

179

1

Susceptible to oxidation

Site

220

1

Susceptible to oxidation

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.16

Lipidation

220

1

S-farnesyl cysteine Ref.17

Natural variations

Natural variant

18

1

S → Y Loss of dimerization ability and impaired ligase activity; confers an antioxidant protective function when expressed at physiological levels in neuroblastoma cells and primary cortical neurons. Ref.13 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28
Corresponds to variant rs5030732 [ dbSNP | Ensembl ].

VAR_015677

Natural variant

93

1

I → M in PARK5; impaired enzymatic hydrolase activity; has about a 50% reduction in catalytic activity compared to wild-type protein. Ref.8 Ref.13 Ref.20 Ref.21 Ref.22

VAR_015678

Experimental info

Mutagenesis

73

1

Q → R: No effect on enzymatic parameters. Ref.11

Mutagenesis

90

1

C → S: Abolishes enzymatic activity. Ref.11 Ref.20 Ref.21

Mutagenesis

97

1

H → Q or N: 2-fold increase in affinity for ubiquitin ethyl ester, slight reduction in enzymatic activity. Ref.11

Mutagenesis

161

1

H → D: 10000-fold decrease in enzymatic activity; no change in affinity for ubiquitin ethyl ester. Ref.11

Mutagenesis

161

1

H → K, Q, N or Y: Abolishes enzymatic activity. Ref.11

Mutagenesis

176

1

D → N: 6-fold decrease in affinity for ubiquitin ethyl ester; 97.5% decrease in enzymatic activity. Ref.11

Mutagenesis

204

1

F → A: Almost complete loss of activity. Ref.20

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

223

Helix Strand Turn

Details...

Helix

10 – 19

10

Beta strand

24 – 30

7

Beta strand

39 – 42

4

Beta strand

46 – 54

9

Helix

57 – 70

14

Turn

71 – 74

4

Helix

90 – 100

11

Turn

101 – 105

5

Helix

113 – 120

8

Turn

121 – 123

3

Helix

126 – 135

10

Helix

137 – 147

11

Beta strand

160 – 168

9

Beta strand

171 – 175

5

Beta strand

179 – 181

3

Beta strand

183 – 187

5

Helix

193 – 206

14

Beta strand

215 – 221

7

Sequences

	Sequence		Length	Mass (Da)
	P09936 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: C9E972AC4DA5DA8A	FASTA	223	24,824
	10 20 30 40 50 60 MQLKPMEINP EMLNKVLSRL GVAGQWRFVD VLGLEEESLG SVPAPACALL LLFPLTAQHE 70 80 90 100 110 120 NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA NNQDKLGFED GSVLKQFLSE 130 140 150 160 170 180 TEKMSPEDRA KCFEKNEAIQ AAHDAVAQEG QCRVDDKVNF HFILFNNVDG HLYELDGRMP 190 200 210 220 FPVNHGASSE DTLLKDAAKV CREFTEREQG EVRFSAVALC KAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Muscle.
[4]	"The structure of the human gene encoding protein gene product 9.5 (PGP9.5), a neuron-specific ubiquitin C-terminal hydrolase." Day I.N.M., Hinks L.J., Thompson R.J. Biochem. J. 268:521-524(1990) [PubMed: 2163617] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-15.
[5]	"Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases." Choi J., Levey A.I., Weintraub S.T., Rees H.D., Gearing M., Chin L.-S., Li L. J. Biol. Chem. 279:13256-13264(2004) [PubMed: 14722078] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15 AND 214-221, SUSCEPTIBILITY TO OXIDATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
[6]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-15; 20-27; 66-78; 84-129; 136-195 AND 214-221, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]	"Molecular cloning of cDNA coding for human PGP 9.5 protein. A novel cytoplasmic marker for neurones and neuroendocrine cells." Day I.N.M., Thompson R.J. FEBS Lett. 210:157-160(1987) [PubMed: 2947814] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-223, PARTIAL PROTEIN SEQUENCE.
[8]	"The ubiquitin pathway in Parkinson's disease." Leroy E., Boyer R., Auburger G., Leube B., Ulm G., Mezey E., Harta G., Brownstein M.J., Jonnalagada S., Chernova T., Dehejia A., Lavedan C., Gasser T., Steinbach P.J., Wilkinson K.D., Polymeropoulos M.H. Nature 395:451-452(1998) [PubMed: 9774100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-223, VARIANT PARK5 MET-93, CHARACTERIZATION OF VARIANT PARK5 MET-93, BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"Neuronal protein gene product 9.5 (IEF SSP 6104) is expressed in cultured human MRC-5 fibroblasts of normal origin and is strongly down-regulated in their SV40 transformed counterparts." Honore B., Rasmussen H.H., Vandekerckhove J., Celis J.E. FEBS Lett. 280:235-240(1991) [PubMed: 1849484] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-25; 79-81; 106-121 AND 134-151.
[10]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-25; 79-91; 106-123 AND 136-151.
[11]	"Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues." Larsen C.N., Price J.S., Wilkinson K.D. Biochemistry 35:6735-6744(1996) [PubMed: 8639624] [Abstract] Cited for: ACTIVE SITE, MUTAGENESIS OF GLN-73; CYS-90; HIS-97; HIS-161 AND ASP-176, BIOPHYSICOCHEMICAL PROPERTIES.
[12]	"Cleavage of the C-terminus of NEDD8 by UCH-L3." Wada H., Kito K., Caskey L.S., Yeh E.T.H., Kamitani T. Biochem. Biophys. Res. Commun. 251:688-692(1998) [PubMed: 9790970] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[13]	"The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility." Liu Y., Fallon L., Lashuel H.A., Liu Z., Lansbury P.T. Jr. Cell 111:209-218(2002) [PubMed: 12408865] [Abstract] Cited for: FUNCTION, CHARACTERIZATION OF VARIANT PARK5 MET-93, CHARACTERIZATION OF VARIANT TYR-18.
[14]	"Interaction and colocalization of PGP9.5 with JAB1 and p27(Kip1)." Caballero O.L., Resto V., Patturajan M., Meerzaman D., Guo M.Z., Engles J., Yochem R., Ratovitski E., Sidransky D., Jen J. Oncogene 21:3003-3010(2002) [PubMed: 12082530] [Abstract] Cited for: INTERACTION WITH COPS5.
[15]	"Mechanistic studies of ubiquitin C-terminal hydrolase L1." Case A., Stein R.L. Biochemistry 45:2443-2452(2006) [PubMed: 16475834] [Abstract] Cited for: ACTIVE SITE.
[16]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Membrane-associated farnesylated UCH-L1 promotes alpha-synuclein neurotoxicity and is a therapeutic target for Parkinson's disease." Liu Z., Meray R.K., Grammatopoulos T.N., Fredenburg R.A., Cookson M.R., Liu Y., Logan T., Lansbury P.T. Jr. Proc. Natl. Acad. Sci. U.S.A. 106:4635-4640(2009) [PubMed: 19261853] [Abstract] Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-220.
[18]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1." Das C., Hoang Q.Q., Kreinbring C.A., Luchansky S.J., Meray R.K., Ray S.S., Lansbury P.T., Ringe D., Petsko G.A. Proc. Natl. Acad. Sci. U.S.A. 103:4675-4680(2006) [PubMed: 16537382] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT.
[20]	"Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation." Boudreaux D.A., Maiti T.K., Davies C.W., Das C. Proc. Natl. Acad. Sci. U.S.A. 107:9117-9122(2010) [PubMed: 20439756] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF VARIANTS TYR-18 AND MET-93 IN COMPLEX WITH UBIQUITIN, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF CYS-90 AND PHE-204.
[21]	"Alterations of structure and hydrolase activity of parkinsonism-associated human ubiquitin carboxyl-terminal hydrolase L1 variants." Nishikawa K., Li H., Kawamura R., Osaka H., Wang Y.-L., Hara Y., Hirokawa T., Manago Y., Amano T., Noda M., Aoki S., Wada K. Biochem. Biophys. Res. Commun. 304:176-183(2003) [PubMed: 12705903] [Abstract] Cited for: CHARACTERIZATION OF VARIANT PARK5 MET-93, CHARACTERIZATION OF VARIANT TYR-18, MUTAGENESIS OF CYS-90, BIOPHYSICOCHEMICAL PROPERTIES.
[22]	"The Ile93Met mutation in the ubiquitin carboxy-terminal-hydrolase-L1 gene is not observed in European cases with familial Parkinson's disease." Harhangi B.S., Farrer M.J., Lincoln S., Bonifati V., Meco G., De Michele G., Brice A., Durr A., Martinez M., Gasser T., Bereznai B., Vaughan J.R., Wood N.W., Hardy J., Oostra B.A., Breteler M.M. Neurosci. Lett. 270:1-4(1999) [PubMed: 10454131] [Abstract] Cited for: VARIANT MET-93.
[23]	"Low frequency of pathogenic mutations in the ubiquitin carboxy-terminal hydrolase gene in familial Parkinson's disease." Lincoln S., Vaughan J., Wood N., Baker M., Adamson J., Gwinn-Hardy K., Lynch T., Hardy J., Farrer M. NeuroReport 10:427-429(1999) [PubMed: 10203348] [Abstract] Cited for: VARIANT TYR-18.
[24]	"The ubiquitin carboxy-terminal hydrolase-L1 gene S18Y polymorphism does not confer protection against idiopathic Parkinson's disease." Mellick G.D., Silburn P.A. Neurosci. Lett. 293:127-130(2000) [PubMed: 11027850] [Abstract] Cited for: VARIANT TYR-18.
[25]	"UCHL1 is a Parkinson's disease susceptibility gene." UCHL1 global genetics consortium Maraganore D.M., Lesnick T.G., Elbaz A., Chartier-Harlin M.-C., Gasser T., Krueger R., Hattori N., Mellick G.D., Quattrone A., Satoh J., Toda T., Wang J., Ioannidis J.P.A., de Andrade M., Rocca W.A. Ann. Neurol. 55:512-521(2004) [PubMed: 15048890] [Abstract] Cited for: VARIANT TYR-18.
[26]	Erratum UCHL1 global genetics consortium Maraganore D.M., Lesnick T.G., Elbaz A., Chartier-Harlin M.-C., Gasser T., Krueger R., Hattori N., Mellick G.D., Quattrone A., Satoh J., Toda T., Wang J., Ioannidis J.P.A., de Andrade M., Rocca W.A. Ann. Neurol. 55:899-899(2004)
[27]	"UCHL-1 is not a Parkinson's disease susceptibility gene." Healy D.G., Abou-Sleiman P.M., Casas J.P., Ahmadi K.R., Lynch T., Gandhi S., Muqit M.M., Foltynie T., Barker R., Bhatia K.P., Quinn N.P., Lees A.J., Gibson J.M., Holton J.L., Revesz T., Goldstein D.B., Wood N.W. Ann. Neurol. 59:627-633(2006) [PubMed: 16450370] [Abstract] Cited for: VARIANT TYR-18, LACK OF ASSOCIATION OF VARIANT TYR-18 WITH PARKINSON DISEASE.
[28]	"The S18Y polymorphic variant of UCH-L1 confers an antioxidant function to neuronal cells." Kyratzi E., Pavlaki M., Stefanis L. Hum. Mol. Genet. 17:2160-2171(2008) [PubMed: 18411255] [Abstract] Cited for: CHARACTERIZATION OF VARIANT TYR-18, ANTIOXYDANT FUNCTION IN NEURONAL CELLS.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Ubiquitin carboxy-terminal hydrolase L1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AC095043 Genomic DNA. Translation: AAY40923.1.
CH471069 Genomic DNA. Translation: EAW92983.1.
BC000332 mRNA. Translation: AAH00332.1.
BC005117 mRNA. Translation: AAH05117.1.
BC006305 mRNA. Translation: AAH06305.1.
X17377 Genomic DNA. Translation: CAA35249.1.
X04741 mRNA. Translation: CAA28443.1. Different initiation.
AF076273 , AF060834, AF076269, AF076270, AF076271, AF076272 Genomic DNA. Translation: AAD09172.1.

IPI

IPI00018352.

PIR

A25856.

RefSeq

NP_004172.2. NM_004181.4.

UniGene

Hs.518731.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ETL	X-ray	2.40	A/B	1-223	[»]
3IFW	X-ray	2.40	A	1-223	[»]
3IRT	X-ray	2.80	A/B	1-223	[»]
3KVF	X-ray	2.80	A	1-223	[»]
3KW5	X-ray	2.83	A	1-223	[»]

ProteinModelPortal

P09936.

SMR

P09936. Positions 1-223.

ModBase

Search...

Protein-protein interaction databases

IntAct

P09936. 14 interactions.

MINT

MINT-1378022.

STRING

P09936.

Protein family/group databases

MEROPS

C12.001.

PTM databases

PhosphoSite

P09936.

Polymorphism databases

DMDM

136681.

2D gel databases

Aarhus/Ghent-2DPAGE

6123. IEF.

DOSAC-COBS-2DPAGE

P09936.

UCD-2DPAGE

P09936.

Proteomic databases

PeptideAtlas

P09936.

PRIDE

P09936.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000284440; ENSP00000284440; ENSG00000154277.

GeneID

7345.

KEGG

hsa:7345.

UCSC

uc003gvo.1. human.

Organism-specific databases

CTD

7345.

GeneCards

GC04P041174.

H-InvDB

HIX0004176.

HGNC

HGNC:12513. UCHL1.

HPA

CAB002580.
HPA005993.

MIM

191342. gene.
613643. phenotype.

neXtProt

NX_P09936.

Orphanet

2828. Young adult-onset Parkinsonism.

PharmGKB

PA37160.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14505.

GeneTree

ENSGT00510000046640.

HOGENOM

HBG436319.

HOVERGEN

HBG075483.

InParanoid

P09936.

OMA

ICRQFTE.

OrthoDB

EOG4RJG2F.

PhylomeDB

P09936.

Enzyme and pathway databases

BRENDA

3.1.2.15. 2681.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.

Gene expression databases

ArrayExpress

P09936.

Bgee

P09936.

CleanEx

HS_UCHL1.

Genevestigator

P09936.

GermOnline

ENSG00000154277. Homo sapiens.

Family and domain databases

InterPro

IPR001578. Peptidase_C12.
[Graphical view]

Gene3D

G3DSA:3.40.532.10. Peptidase_C12. 1 hit.

KO

K05611.

PANTHER

PTHR10589. Peptidase_C12. 1 hit.

Pfam

PF01088. Peptidase_C12. 1 hit.
[Graphical view]

PRINTS

PR00707. UBCTHYDRLASE.

PROSITE

PS00140. UCH_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

28756.

SOURCE

Search...

Entry information

Entry name

UCHL1_HUMAN

Accession

Primary (citable) accession number: P09936
Secondary accession number(s): Q4W5K6, Q71UM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1990
Last modified:	January 25, 2012
This is version 139 of the entry and version 2 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.