Skip Header

Contribute Send feedback
Read comments (?) or add your own

P50103 (UCHL1_MONDO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMonodelphis domestica (Gray short-tailed opossum) [Reference proteome]
Taxonomic identifier13616 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Metatheria › Didelphimorphia › Didelphidae › Monodelphis

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

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).

Subunit structure

Monomer. Homodimer. Interacts with COPS5 and SNCA By similarity.

Subcellular location

Cytoplasm. Endoplasmic reticulum membrane; Lipid-anchor By similarity.

Post-translational modification

O-glycosylated By similarity.

Miscellaneous

In contrast to UCHL3, does not hydrolyze a peptide bond at the C-terminal glycine of NEDD8 By similarity.

Sequence similarities

Belongs to the peptidase C12 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 223223Ubiquitin carboxyl-terminal hydrolase isozyme L1
PRO_0000211057
Propeptide221 – 2233Removed in mature form By similarity
PRO_0000421570

Regions

Region5 – 106Interaction with ubiquitin By similarity
Region151 – 1566Interaction with ubiquitin By similarity
Region211 – 2166Interaction with ubiquitin By similarity

Sites

Active site901Nucleophile By similarity
Active site1611Proton donor By similarity
Site11Susceptible to oxidation By similarity
Site61Susceptible to oxidation By similarity
Site121Susceptible to oxidation By similarity
Site1761Important for enzyme activity By similarity
Site1791Susceptible to oxidation By similarity
Site2201Susceptible to oxidation By similarity

Amino acid modifications

Lipidation2201S-farnesyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P50103 [UniParc].

Last modified March 6, 2013. Version 2.
Checksum: 5EC27BD80CADF896

FASTA22324,767
        10         20         30         40         50         60 
MQLKPMEINP EMLNKVLTRL GVGGDWKFVD VLGLEEDVLG TVPAPACALL LLFPLTAQHE 

        70         80         90        100        110        120 
NFRKKQIEEL KGQEVSPKVY FMKQTVGNSC GTIGLIHAVA NNQDKLNFDD GSVLKQFISE 

       130        140        150        160        170        180 
TAKLSPEDRA KCFEKNEAIQ AAHDAVAQEG QCRVDDEVNF HFILFNNVDG HLYELDGRMP 

       190        200        210        220 
FPINHGSNSD ESVLKGAAEI CRQFTEREEG EVRFSAVALC KCA

« Hide

References

[1]"Identification of evolutionary conserved regulatory sequences in the 5' untranscribed region of the neural-specific ubiquitin C-terminal hydrolase (PGP9.5) gene."
Mann D.A., Trowern A.R., Lavender F.L., Whittaker P.A., Thompson R.J.
J. Neurochem. 66:35-46(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U32208 Genomic DNA. Translation: AAA89059.1.
RefSeqXP_001365417.1. XM_001365380.2.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMODT00000026186; ENSMODP00000025726; ENSMODG00000020568.
GeneID100015629.
KEGGmdo:100015629.

Phylogenomic databases

GeneTreeENSGT00510000046640.
KOK05611.

Family and domain databases

Gene3D3.40.532.10. 1 hit.
InterProIPR001578. Peptidase_C12.
[Graphical view]
PANTHERPTHR10589. PTHR10589. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSPR00707. UBCTHYDRLASE.
PROSITEPS00140. UCH_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUCHL1_MONDO
AccessionPrimary (citable) accession number: P50103
Secondary accession number(s): F7APK9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 6, 2013
Last modified: May 29, 2013
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents