Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9R0P9

- UCHL1_MOUSE

UniProt

Q9R0P9 - UCHL1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin carboxyl-terminal hydrolase isozyme L1

Gene

Uchl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

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).

Kineticsi

  1. KM=116 nM for Ub-AMC1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901NucleophileCurated
Active sitei161 – 1611Proton donorPROSITE-ProRule annotation
Sitei176 – 1761Important for enzyme activityBy similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. ligase activity Source: UniProtKB-KW
  3. omega peptidase activity Source: UniProtKB
  4. ubiquitin binding Source: UniProtKB
  5. ubiquitin-specific protease activity Source: InterPro
  6. ubiquitin thiolesterase activity Source: MGI

GO - Biological processi

  1. adult walking behavior Source: MGI
  2. axonogenesis Source: MGI
  3. axon target recognition Source: MGI
  4. axon transport of mitochondrion Source: MGI
  5. cell proliferation Source: MGI
  6. eating behavior Source: MGI
  7. muscle fiber development Source: MGI
  8. negative regulation of MAP kinase activity Source: Ensembl
  9. neuromuscular process Source: MGI
  10. protein deubiquitination Source: UniProtKB
  11. response to ischemia Source: MGI
  12. sensory perception of pain Source: Ensembl
  13. ubiquitin-dependent protein catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi3.4.19.12. 3474.

Protein family/group databases

MEROPSiC12.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase isozyme L1 (EC:3.4.19.12, EC:6.-.-.-)
Short name:
UCH-L1
Alternative name(s):
Neuron cytoplasmic protein 9.5
PGP 9.5
Short name:
PGP9.5
Ubiquitin thioesterase L1
Gene namesi
Name:Uchl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:103149. Uchl1.

Subcellular locationi

Cytoplasm 1 Publication. Endoplasmic reticulum membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

  1. axon Source: MGI
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: MGI
  4. endoplasmic reticulum Source: UniProtKB-KW
  5. extracellular vesicular exosome Source: Ensembl
  6. neuronal cell body Source: MGI
  7. nucleus Source: Ensembl
  8. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show sensory ataxia at an early stage, followed by motor ataxia at a later stage. They have reduced levels of monoubiquitin in the nervous system, and increased resistance to retinal ischemia.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301D → K: Abolishes enzymatic activity and ubiquitin binding. 1 Publication
Mutagenesisi90 – 901C → S: Abolishes enzymatic activity, but does not affect ubiquitin binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220Ubiquitin carboxyl-terminal hydrolase isozyme L1PRO_0000211058Add
BLAST
Propeptidei221 – 2233Removed in mature formBy similarityPRO_0000414313

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi220 – 2201S-farnesyl cysteineBy similarity

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Prenylation

Proteomic databases

MaxQBiQ9R0P9.
PaxDbiQ9R0P9.
PRIDEiQ9R0P9.

2D gel databases

REPRODUCTION-2DPAGEIPI00313962.
Q9R0P9.
UCD-2DPAGEQ9R0P9.

PTM databases

PhosphoSiteiQ9R0P9.

Expressioni

Tissue specificityi

Expressed in brain, where it is found in neurons but not in oligodendrocytes or astrocytes. Found in the ganglion cell layer and the inner nuclear layer of the retina (at protein level). Expressed in brain and testis. In the brain, expression is at its lowest in replaceable neurons of hippocampus and olfactory bulb. Highly expressed in senescent pituitary.5 Publications

Gene expression databases

BgeeiQ9R0P9.
CleanExiMM_UCHL1.
ExpressionAtlasiQ9R0P9. baseline and differential.
GenevestigatoriQ9R0P9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi204423. 7 interactions.
IntActiQ9R0P9. 5 interactions.
MINTiMINT-4139420.
STRINGi10090.ENSMUSP00000031131.

Structurei

3D structure databases

ProteinModelPortaliQ9R0P9.
SMRiQ9R0P9. Positions 1-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5 – 106Interaction with ubiquitinBy similarity
Regioni151 – 1566Interaction with ubiquitinBy similarity
Regioni211 – 2166Interaction with ubiquitinBy similarity

Sequence similaritiesi

Belongs to the peptidase C12 family.Curated

Phylogenomic databases

eggNOGiNOG327708.
GeneTreeiENSGT00510000046640.
HOVERGENiHBG075483.
InParanoidiQ9R0P9.
KOiK05611.
OMAiKSHENGH.
OrthoDBiEOG7S7SFK.
PhylomeDBiQ9R0P9.
TreeFamiTF316166.

Family and domain databases

Gene3Di3.40.532.10. 1 hit.
InterProiIPR001578. Peptidase_C12_UCH.
[Graphical view]
PANTHERiPTHR10589. PTHR10589. 1 hit.
PfamiPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSiPR00707. UBCTHYDRLASE.
PROSITEiPS00140. UCH_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R0P9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLKPMEINP EMLNKVLAKL GVAGQWRFAD VLGLEEETLG SVPSPACALL
60 70 80 90 100
LLFPLTAQHE NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA
110 120 130 140 150
NNQDKLEFED GSVLKQFLSE TEKLSPEDRA KCFEKNEAIQ AAHDSVAQEG
160 170 180 190 200
QCRVDDKVNF HFILFNNVDG HLYELDGRMP FPVNHGASSE DSLLQDAAKV
210 220
CREFTEREQG EVRFSAVALC KAA
Length:223
Mass (Da):24,838
Last modified:May 1, 2000 - v1
Checksum:iF1402BF7B0C077EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491E → K in AAD51029. (PubMed:12559414)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB025313 mRNA. Translation: BAA84083.1.
AF172334 mRNA. Translation: AAD51029.1.
AK013729 mRNA. Translation: BAB28976.1.
BC039177 mRNA. Translation: AAH39177.1.
CCDSiCCDS19315.1.
RefSeqiNP_035800.2. NM_011670.2.
UniGeneiMm.29807.

Genome annotation databases

EnsembliENSMUST00000031131; ENSMUSP00000031131; ENSMUSG00000029223.
GeneIDi22223.
KEGGimmu:22223.
UCSCiuc008xpf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB025313 mRNA. Translation: BAA84083.1 .
AF172334 mRNA. Translation: AAD51029.1 .
AK013729 mRNA. Translation: BAB28976.1 .
BC039177 mRNA. Translation: AAH39177.1 .
CCDSi CCDS19315.1.
RefSeqi NP_035800.2. NM_011670.2.
UniGenei Mm.29807.

3D structure databases

ProteinModelPortali Q9R0P9.
SMRi Q9R0P9. Positions 1-223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204423. 7 interactions.
IntActi Q9R0P9. 5 interactions.
MINTi MINT-4139420.
STRINGi 10090.ENSMUSP00000031131.

Chemistry

BindingDBi Q9R0P9.

Protein family/group databases

MEROPSi C12.001.

PTM databases

PhosphoSitei Q9R0P9.

2D gel databases

REPRODUCTION-2DPAGE IPI00313962.
Q9R0P9.
UCD-2DPAGE Q9R0P9.

Proteomic databases

MaxQBi Q9R0P9.
PaxDbi Q9R0P9.
PRIDEi Q9R0P9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031131 ; ENSMUSP00000031131 ; ENSMUSG00000029223 .
GeneIDi 22223.
KEGGi mmu:22223.
UCSCi uc008xpf.2. mouse.

Organism-specific databases

CTDi 7345.
MGIi MGI:103149. Uchl1.

Phylogenomic databases

eggNOGi NOG327708.
GeneTreei ENSGT00510000046640.
HOVERGENi HBG075483.
InParanoidi Q9R0P9.
KOi K05611.
OMAi KSHENGH.
OrthoDBi EOG7S7SFK.
PhylomeDBi Q9R0P9.
TreeFami TF316166.

Enzyme and pathway databases

BRENDAi 3.4.19.12. 3474.

Miscellaneous databases

ChiTaRSi UCHL1. mouse.
NextBioi 302243.
PROi Q9R0P9.
SOURCEi Search...

Gene expression databases

Bgeei Q9R0P9.
CleanExi MM_UCHL1.
ExpressionAtlasi Q9R0P9. baseline and differential.
Genevestigatori Q9R0P9.

Family and domain databases

Gene3Di 3.40.532.10. 1 hit.
InterProi IPR001578. Peptidase_C12_UCH.
[Graphical view ]
PANTHERi PTHR10589. PTHR10589. 1 hit.
Pfami PF01088. Peptidase_C12. 1 hit.
[Graphical view ]
PRINTSi PR00707. UBCTHYDRLASE.
PROSITEi PS00140. UCH_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice."
    Saigoh K., Wang Y.-L., Suh J.G., Yamanishi T., Sakai Y., Kiyosawa H., Harada T., Ichihara N., Wakana S., Kikuchi T., Wada K.
    Nat. Genet. 23:47-51(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    Tissue: Brain.
  2. "Age-related alterations in the protein expression profile of C57BL/6J mouse pituitaries."
    Marzban G., Grillari J., Reisinger E., Hemetsberger T., Grabherr R., Katinger H.
    Exp. Gerontol. 37:1451-1460(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Pituitary.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hippocampus.
  4. "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].
    Tissue: Retina.
  5. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 20-27; 66-78; 116-123; 136-153 AND 158-199, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  6. Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-30 AND CYS-90, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, DISRUPTION PHENOTYPE.
  7. "Role of ubiquitin carboxy terminal hydrolase-L1 in neural cell apoptosis induced by ischemic retinal injury in vivo."
    Harada T., Harada C., Wang Y.-L., Osaka H., Amanai K., Tanaka K., Takizawa S., Setsuie R., Sakurai M., Sato Y., Noda M., Wada K.
    Am. J. Pathol. 164:59-64(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Replaceable neurons and neurodegenerative disease share depressed UCHL1 levels."
    Lombardino A.J., Li X.-C., Hertel M., Nottebohm F.
    Proc. Natl. Acad. Sci. U.S.A. 102:8036-8041(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiUCHL1_MOUSE
AccessioniPrimary (citable) accession number: Q9R0P9
Secondary accession number(s): Q9R122
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3