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Protein

Ubiquitin carboxyl-terminal hydrolase isozyme L3

Gene

UCHL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.5 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).3 Publications

Enzyme regulationi

Inhibited by monoubiquitin and diubiquitin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Nucleophile
Active sitei169 – 1691Proton donorCurated
Sitei184 – 1841Important for enzyme activityBy similarity

GO - Molecular functioni

  1. peptidase activity Source: UniProtKB
  2. ubiquitin binding Source: UniProtKB
  3. ubiquitin-specific protease activity Source: InterPro

GO - Biological processi

  1. protein catabolic process Source: UniProtKB
  2. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

SABIO-RKP15374.

Protein family/group databases

MEROPSiC12.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase isozyme L3 (EC:3.4.19.12)
Short name:
UCH-L3
Alternative name(s):
Ubiquitin thioesterase L3
Gene namesi
Name:UCHL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:12515. UCHL3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleoplasm Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331D → A: Decreased interaction with diubiquitin. No accumulation of free diubiquitin. Decreased levels of polyubiquitinated lysozyme. 2 Publications
Mutagenesisi95 – 951C → A: Increased interaction with diubiquitin. 3 Publications
Mutagenesisi95 – 951C → S: Abolishes enzymatic activity. Increased interaction with diubiquitin. 3 Publications

Organism-specific databases

PharmGKBiPA37162.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 230230Ubiquitin carboxyl-terminal hydrolase isozyme L3PRO_0000211061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15374.
PaxDbiP15374.
PeptideAtlasiP15374.
PRIDEiP15374.

2D gel databases

OGPiP15374.
REPRODUCTION-2DPAGEIPI00011250.

PTM databases

PhosphoSiteiP15374.

Expressioni

Tissue specificityi

Highly expressed in heart, skeletal muscle, and testis.1 Publication

Gene expression databases

BgeeiP15374.
CleanExiHS_UCHL3.
ExpressionAtlasiP15374. baseline.
GenevestigatoriP15374.

Organism-specific databases

HPAiCAB037139.
CAB037208.
HPA019678.

Interactioni

Subunit structurei

Preferentially binds diubiquitin; the interaction does not hydrolyze diubiquitin but, in vitro, inhibits the hydrolyzing activity on other substrates.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SMAD1Q157972EBI-954554,EBI-1567153

Protein-protein interaction databases

BioGridi113194. 58 interactions.
DIPiDIP-29135N.
IntActiP15374. 10 interactions.
MINTiMINT-2863935.
STRINGi9606.ENSP00000366819.

Structurei

Secondary structure

1
230
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2210Combined sources
Beta strandi29 – 335Combined sources
Helixi39 – 424Combined sources
Beta strandi49 – 579Combined sources
Helixi60 – 7617Combined sources
Helixi92 – 943Combined sources
Helixi95 – 10511Combined sources
Helixi106 – 1105Combined sources
Helixi118 – 1269Combined sources
Helixi131 – 1399Combined sources
Helixi142 – 15211Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi168 – 1769Combined sources
Beta strandi179 – 1835Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi191 – 1955Combined sources
Turni198 – 2003Combined sources
Helixi201 – 21515Combined sources
Beta strandi223 – 2297Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UCHX-ray1.80A1-230[»]
1XD3X-ray1.45A/C1-230[»]
ProteinModelPortaliP15374.
SMRiP15374. Positions 2-230.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15374.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 136Interaction with ubiquitin
Regioni152 – 1598Interaction with ubiquitin
Regioni219 – 2246Interaction with ubiquitin

Sequence similaritiesi

Belongs to the peptidase C12 family.Curated

Phylogenomic databases

eggNOGiNOG327708.
GeneTreeiENSGT00510000046640.
HOGENOMiHOG000182400.
HOVERGENiHBG075483.
InParanoidiP15374.
KOiK05609.
OMAiVYGMEPE.
OrthoDBiEOG7S7SFK.
PhylomeDBiP15374.
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.

P15374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMDPE LLSMVPRPVC
60 70 80 90 100
AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL
110 120 130 140 150
IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERARYLEN YDAIRVTHET
160 170 180 190 200
SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGETSDET
210 220 230
LLEDAIEVCK KFMERDPDEL RFNAIALSAA
Length:230
Mass (Da):26,183
Last modified:April 1, 1990 - v1
Checksum:i8ACACE6E1D86FD55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30496 mRNA. Translation: AAA36791.1.
BT019359 mRNA. Translation: AAV38166.1.
CR456855 mRNA. Translation: CAG33136.1.
AK313665 mRNA. Translation: BAG36417.1.
AL137244 Genomic DNA. Translation: CAI12419.1.
CH471093 Genomic DNA. Translation: EAW80542.1.
BC018125 mRNA. Translation: AAH18125.1.
CCDSiCCDS9453.1.
PIRiA40085.
RefSeqiNP_001257881.1. NM_001270952.1.
NP_005993.1. NM_006002.4.
UniGeneiHs.162241.

Genome annotation databases

EnsembliENST00000377595; ENSP00000366819; ENSG00000118939.
GeneIDi7347.
KEGGihsa:7347.
UCSCiuc001vjq.4. human.

Polymorphism databases

DMDMi136682.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30496 mRNA. Translation: AAA36791.1.
BT019359 mRNA. Translation: AAV38166.1.
CR456855 mRNA. Translation: CAG33136.1.
AK313665 mRNA. Translation: BAG36417.1.
AL137244 Genomic DNA. Translation: CAI12419.1.
CH471093 Genomic DNA. Translation: EAW80542.1.
BC018125 mRNA. Translation: AAH18125.1.
CCDSiCCDS9453.1.
PIRiA40085.
RefSeqiNP_001257881.1. NM_001270952.1.
NP_005993.1. NM_006002.4.
UniGeneiHs.162241.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UCHX-ray1.80A1-230[»]
1XD3X-ray1.45A/C1-230[»]
ProteinModelPortaliP15374.
SMRiP15374. Positions 2-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113194. 58 interactions.
DIPiDIP-29135N.
IntActiP15374. 10 interactions.
MINTiMINT-2863935.
STRINGi9606.ENSP00000366819.

Chemistry

BindingDBiP15374.
ChEMBLiCHEMBL6195.

Protein family/group databases

MEROPSiC12.003.

PTM databases

PhosphoSiteiP15374.

Polymorphism databases

DMDMi136682.

2D gel databases

OGPiP15374.
REPRODUCTION-2DPAGEIPI00011250.

Proteomic databases

MaxQBiP15374.
PaxDbiP15374.
PeptideAtlasiP15374.
PRIDEiP15374.

Protocols and materials databases

DNASUi7347.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377595; ENSP00000366819; ENSG00000118939.
GeneIDi7347.
KEGGihsa:7347.
UCSCiuc001vjq.4. human.

Organism-specific databases

CTDi7347.
GeneCardsiGC13P076123.
HGNCiHGNC:12515. UCHL3.
HPAiCAB037139.
CAB037208.
HPA019678.
MIMi603090. gene.
neXtProtiNX_P15374.
PharmGKBiPA37162.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327708.
GeneTreeiENSGT00510000046640.
HOGENOMiHOG000182400.
HOVERGENiHBG075483.
InParanoidiP15374.
KOiK05609.
OMAiVYGMEPE.
OrthoDBiEOG7S7SFK.
PhylomeDBiP15374.
TreeFamiTF316166.

Enzyme and pathway databases

SABIO-RKP15374.

Miscellaneous databases

ChiTaRSiUCHL3. human.
EvolutionaryTraceiP15374.
GeneWikiiUCHL3.
GenomeRNAii7347.
NextBioi28762.
PROiP15374.
SOURCEiSearch...

Gene expression databases

BgeeiP15374.
CleanExiHS_UCHL3.
ExpressionAtlasiP15374. baseline.
GenevestigatoriP15374.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase."
    Wilkinson K.D., Lee K., Deshpande S., Duerksen-Hughes P., Boss J.M., Pohl J.
    Science 246:670-673(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "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].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Lung.
  8. Cited for: FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-95.
  9. "Molecular profiling of the immune response in colon cancer using protein microarrays: occurrence of autoantibodies to ubiquitin C-terminal hydrolase L3."
    Nam M.J., Madoz-Gurpide J., Wang H., Lescure P., Schmalbach C.E., Zhao R., Misek D.E., Kuick R., Brenner D.E., Hanash S.M.
    Proteomics 3:2108-2115(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS TUMOR-ASSOCIATED ANTIGEN BY MASS SPECTROMETRY.
  10. "Substrate profiling of deubiquitin hydrolases with a positional scanning library and mass spectrometry."
    Mason D.E., Ek J., Peters E.C., Harris J.L.
    Biochemistry 43:6535-6544(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Ubiquitin dimers control the hydrolase activity of UCH-L3."
    Setsuie R., Sakurai M., Sakaguchi Y., Wada K.
    Neurochem. Int. 54:314-321(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH UBIQUITIN, FUNCTION, ENZYME REGULATION, MUTAGENESIS OF ASP-33 AND CYS-95.
  14. "Skeletal muscles of Uchl3 knockout mice show polyubiquitinated protein accumulation and stress responses."
    Setsuie R., Suzuki M., Tsuchiya Y., Wada K.
    Neurochem. Int. 56:911-918(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, MUTAGENESIS OF ASP-33 AND CYS-95.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Mutant ubiquitin (UBB(+1)) associated with neurodegenerative disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3)."
    Dennissen F.J., Kholod N., Hermes D.J., Kemmerling N., Steinbusch H.W., Dantuma N.P., van Leeuwen F.W.
    FEBS Lett. 585:2568-2574(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes."
    Iphofer A., Kummer A., Nimtz M., Ritter A., Arnold T., Frank R., van den Heuvel J., Kessler B.M., Jansch L., Franke R.
    ChemBioChem 13:1416-1420(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, LINKAGE SPECIFICITY.
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8-A resolution."
    Johnston S.C., Larsen C.N., Cook W.J., Wilkinson K.D., Hill C.P.
    EMBO J. 16:3787-3796(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  20. "Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate."
    Misaghi S., Galardy P.J., Meester W.J.N., Ovaa H., Ploegh H.L., Gaudet R.
    J. Biol. Chem. 280:1512-1520(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH UBIQUITIN VINYLMETHYLESTER, ENZYME ACTIVITY.

Entry informationi

Entry nameiUCHL3_HUMAN
AccessioniPrimary (citable) accession number: P15374
Secondary accession number(s): B2R970, Q5TBK8, Q6IBE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: March 4, 2015
This is version 152 of the entry and version 1 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

Miscellaneous

Identified as a tumor-specific antigen in colon cancer.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.