Q9WUP7 (UCHL5_MOUSE) 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 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).
Enzyme regulation	Activated by ADRM1. Inhibited by interaction with NFRKB By similarity.
Subunit structure	Component of the 19S (PA700) regulatory complex of the 26S proteasome. Interacts with ADRM1 and NFRKB. Component of the INO80 complex; specifically part of a complex module associated with N-terminus of INO80 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus By similarity.
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
Molecular function	Hydrolase Protease Thiol protease
PTM	Acetylation
Technical term	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 mutant phenotype PubMed 21048919. Source: BHF-UCL lateral ventricle development Inferred from mutant phenotype PubMed 21048919. Source: BHF-UCL midbrain development Inferred from mutant phenotype PubMed 21048919. Source: BHF-UCL protein deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB regulation of proteasomal protein catabolic process Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	Ino80 complex Inferred from electronic annotation. Source: Compara cytosol Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB proteasome complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	endopeptidase inhibitor activity Inferred from electronic annotation. Source: Compara omega peptidase activity Inferred from electronic annotation. Source: InterPro ubiquitin thiolesterase activity Traceable author statement. Source: Reactome ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9WUP7-1)

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: Q9WUP7-2)

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

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_0000211067
Regions
	Region	313 – 329	17	Interaction with ADRM1 By similarity
Sites
	Active site	88	1	Nucleophile By similarity
	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 By similarity
Natural variations
	Alternative sequence	246	1	Missing in isoform 2.		VSP_005255
Experimental info
	Sequence conflict	20	1	E → K in AAD31534. Ref.1
	Sequence conflict	24	1	G → R in AAD31534. Ref.1
	Sequence conflict	104	1	D → E in BAB25312. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: 1EAB5223FB707917	FASTA	329	37,617
	10 20 30 40 50 60 MSSNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ESFEKLKPVH GLIFLFKWQP 70 80 90 100 110 120 GEEPAGSVVQ DSRLETIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS 130 140 150 160 170 180 FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTPAKEE DAFHFVSYVP VNGRLYELDG 190 200 210 220 230 240 LREGPIDLGA CNQDDWITAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR 250 260 270 280 290 300 QLAEEEPMDT DQGSTVLSAI QSEVARNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL 310 320 KTLAEHQQLI PLVEKAKEKQ NAKKAQETK
	Isoform 2 [UniParc]. Checksum: 55483B16ADC1E720	FASTA	328	37,488
	10 20 30 40 50 60 MSSNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ESFEKLKPVH GLIFLFKWQP 70 80 90 100 110 120 GEEPAGSVVQ DSRLETIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS 130 140 150 160 170 180 FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTPAKEE DAFHFVSYVP VNGRLYELDG 190 200 210 220 230 240 LREGPIDLGA CNQDDWITAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR 250 260 270 280 290 300 QLAEEPMDTD QGSTVLSAIQ SEVARNQMLI EEEVQKLKRY KIENIRRKHN YLPFIMELLK 310 320 TLAEHQQLIP LVEKAKEKQN AKKAQETK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Xu W., DeMartino G.N., Slaughter C.A., Cohen R.E. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Identification of a novel mouse ubiquitin C-terminal hydrolase: cloning, expression and functional characterization." Li T.W., Sun B., Mustafa F.B., Lee M.K., Teo T.S. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[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] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Embryonic liver, Pancreas and Thymus.
[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] (ISOFORM 2). Strain: Czech II. Tissue: Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF148447 mRNA. Translation: AAD31534.1. AF175903 mRNA. Translation: AAD50311.1. AK017925 mRNA. Translation: BAB31005.1. AK011117 mRNA. Translation: BAB27412.1. AK007860 mRNA. Translation: BAB25312.1. BC006891 mRNA. Translation: AAH06891.1.
IPI	IPI00124938. IPI00230763.
RefSeq	NP_001153338.1. NM_001159866.1. NP_062508.2. NM_019562.2.
UniGene	Mm.261004.
3D structure databases
ProteinModelPortal	Q9WUP7.
SMR	Q9WUP7. Positions 7-312.
ModBase	Search...
Protein family/group databases
MEROPS	C12.005.
PTM databases
PhosphoSite	Q9WUP7.
2D gel databases
REPRODUCTION-2DPAGE	Q9WUP7.
Proteomic databases
PaxDb	Q9WUP7.
PRIDE	Q9WUP7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000018333; ENSMUSP00000018333; ENSMUSG00000018189.
GeneID	56207.
KEGG	mmu:56207.
UCSC	uc007cxe.2. mouse. uc007cxf.2. mouse.
Organism-specific databases
CTD	51377.
MGI	MGI:1914848. Uchl5.
Phylogenomic databases
eggNOG	NOG321645.
GeneTree	ENSGT00510000046560.
HOGENOM	HOG000203918.
HOVERGEN	HBG056021.
InParanoid	Q9WUP7.
KO	K05610.
OMA	QMFEFDT.
OrthoDB	EOG4RBQK0.
Gene expression databases
Bgee	Q9WUP7.
CleanEx	MM_UCHL5.
Genevestigator	Q9WUP7.
GermOnline	ENSMUSG00000018189. Mus musculus.
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. mouse.
NextBio	312039.
SOURCE	Search...

Entry information

Entry name

UCHL5_MOUSE

Accession

Primary (citable) accession number: Q9WUP7
Secondary accession number(s): Q9CVJ4, Q9CXZ3, Q9R107

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	September 26, 2001
Last modified:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program