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P57080 (UBP25_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 25

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 25
Ubiquitin thioesterase 25
Ubiquitin-specific-processing protease 25
Short name=mUSP25
Gene names
Name:Usp25
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1055 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains By similarity. Ref.4

The muscle-specific isoform (USP25m)may have a role in the regulation of muscular differentiation and function. Ref.4

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

Homodimer or oligomer By similarity. Interacts with ACTA1 (via its C-terminus); the interaction occurs for all isoforms but is strongest for isoform USP25min muscle differentiating cells. Interacts (isoform USP25monly) with MYBPC1; the interaction prevents proteasomal degradation of MYBPC1. Interacts (isoform USP25monly) with FLNC (via filament repeats 17-18, 20-21 and 24). Interacts with GAPDH. Interacts with SUMO3; the interaction sumoylates efficiently USP25. Interacts with SUMO2; the interaction sumoylates efficiently USP25. Interacts with SUMO1; the interaction only weakly sumoylates USP25. Interacts with SYK; phosphorylates USP25 and regulates USP25 intracellular levels By similarity.

Subcellular location

Cytoplasm. Nucleus. Note: The longer muscle-specific isoform (USP25m)Some transient punctuate nuclear location in myotubes during myocyte development. Ref.4

Tissue specificity

Highly expressed in testis especially in primary and secondary spematocytes and in immature spermatids. Also found in brain, skeletal muscle, liver and heart. Ref.1

Developmental stage

At E13.5 and E16.5, expression in the brain correlates with the proliferate ventricular zone and post-mitotic neurons of the intermediate zone, particularly in the forebrain. More marked expression at E16.5 in the telencephalic septum and in the pallium. In myocytes, expressed throughout differentiation of myotubes. Ref.1 Ref.4

Post-translational modification

Acetylated By similarity.

Sumoylation impairs binding to and hydrolysis of ubiquitin chains. Sumoylated preferentially with SUMO2 or SUMO3. Desumoylated by SENP1. Regulated by ubiquitination on the same residue By similarity.

Preferentially monoubiquitinated but can also be polyubiquitinated. Autodeubiquitinated. Ubiquitination activates the enzymatic activity either by preventing sumoylation or by allowing novel interactions By similarity.

Phosphorylation in the C-terminal by SYK regulates USP25 cellular levels By similarity.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 UBA-like domain.

Contains 2 UIM (ubiquitin-interacting motif) repeats.

Contains 1 USP domain.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A longer muscle-specific isoform, USP25m, also exists.
Isoform 1 (identifier: P57080-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10551055Ubiquitin carboxyl-terminal hydrolase 25
PRO_0000080654

Regions

Domain14 – 5744UBA-like
Repeat97 – 11620UIM 1
Repeat123 – 14018UIM 2
Domain169 – 658490USP
Region77 – 10226SUMO interaction domain (SIM)
Motif89 – 957Required for SUMO paralog-specific binding

Sites

Active site1781Nucleophile By similarity
Active site6081Proton acceptor By similarity

Amino acid modifications

Modified residue7401Phosphotyrosine By similarity
Cross-link99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Experimental info

Sequence conflict3941E → K in AAF32264. Ref.1
Sequence conflict4961P → L in AAF32264. Ref.1
Sequence conflict6831P → L in AAF32264. Ref.1
Sequence conflict8411H → L in AAF32264. Ref.1

Secondary structure

......... 1055
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 103E34EC3FA8A72B

FASTA1,055121,420
        10         20         30         40         50         60 
MTVEQNVLQQ SAAQKHQQTF LNQLREITGI NDAQILQQAL KDSNGNLELA VAFLTAKNAK 

        70         80         90        100        110        120 
TPPQEETGYY QTALPGNDRY ISVGSQADAN VIDLTGDDKD DLQRAIALSL AESNRAFRET 

       130        140        150        160        170        180 
GITDEEQAIS RVLEASIAEN KACLKRTPIE VWRDSRNPYD RKRQEKAPVG LKNVGNTCWF 

       190        200        210        220        230        240 
SAVIQSLFNL LEFRRLVLNY KPPSNAQDLP RNQKEHRNLP FMRELRYLFA LLVGTKRKYV 

       250        260        270        280        290        300 
DPSRAVEILK DAFKSNDSQQ QDVSEFTHKL LDWLEDAFQM KAEEETDEEK PKNPMVELFY 

       310        320        330        340        350        360 
GRFLAMGVLE GKKFENTEMF GQYPLQVNGF KDLHECLEAA MIEGEIESLH SDNSGKSGQE 

       370        380        390        400        410        420 
HWFTELPPVL TFELSRFEFN QALGRPEKIH NKLEFPQVLY LDRYMHRNRE ITRIKREEIK 

       430        440        450        460        470        480 
RLKDYLTVLQ QRLERYLSYG SGPKRFPLVD VLQYALEFAS SKPVCTSPVD DIDASSSASG 

       490        500        510        520        530        540 
PLPSQSLPST TEQQGPCASD LPGSSSPASG AALPLRSVIH KPFTQSRIPP DLPMHPAPRH 

       550        560        570        580        590        600 
ITEEELCVLE SCLHRWRTEI ENDTRDLQES ISRIHRTIEL MYSDKSMIQV PYRLHAVLVH 

       610        620        630        640        650        660 
EGQANAGHYW AYIFDHRESR WMKYNDIAVT KSSWEELVRD SFGGYRNASA YCLMYIDDKA 

       670        680        690        700        710        720 
QFLIQEEFNK ETGQALVGME TLPPDLRDFV EEDNQRFEKE LEEWDTQLAQ RSLQEKLLAA 

       730        740        750        760        770        780 
PKLREAEASA TTAQAGGADY LEQPSRSDLS KHWKEETLRV IAKASHDLED KGPETVLQSA 

       790        800        810        820        830        840 
IKLEYSRLVK LAQEDTPPET DYRLHHVLVY FIQNQAPKKI IEKTLLEQFG DRNLSFDERC 

       850        860        870        880        890        900 
HNIMKVAQAK LEMIKPEEVN LEEYEEWHAD YKKFRETTMY LITGLENFQR ESYIDSLLFL 

       910        920        930        940        950        960 
LCAYQNNKEL LSKGPYRGHD GELISHYRRE CLLKLNEQAA ELFESGEDGD VNNGLIIMNE 

       970        980        990       1000       1010       1020 
FIVPFLPLLL VDDMEEKDIL AVEDMRNRWC SYLGQEMEAN LQEKLTDFLP KLLDCSTEIK 

      1030       1040       1050 
GFHEPPKLPS YSAHELCERF ARIMLSLSRT PADGR 

« Hide

References

« Hide 'large scale' references
[1]"USP25, a novel gene encoding a deubiquitinating enzyme, is located in the gene-poor region 21q11.2."
Valero R., Marfany G., Gonzalez-Angulo O., Gonzalez-Gonzalez G., Puelles L., Gonzalez-Duarte R.
Genomics 62:395-405(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"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].
Strain: C57BL/6.
Tissue: Brain.
[3]"Solution structure of RSGI RUH-013, a UBA domain in mouse."
RIKEN structural genomics initiative (RSGI)
Submitted (SEP-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-67.
[4]"The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins."
Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G., Marfany G.
Cell. Mol. Life Sci. 63:723-734(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE, POSSIBLE FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF170563 mRNA. Translation: AAF32264.1.
BC048171 mRNA. Translation: AAH48171.1.
BC063059 mRNA. Translation: AAH63059.1.
CCDSCCDS28275.1. [P57080-1]
RefSeqNP_038946.2. NM_013918.2. [P57080-1]
UniGeneMm.40986.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VDLNMR-A1-67[»]
ProteinModelPortalP57080.
SMRP57080. Positions 1-138, 169-407, 592-677.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP57080. 2 interactions.

Protein family/group databases

MEROPSC19.041.

PTM databases

PhosphoSiteP57080.

Proteomic databases

MaxQBP57080.
PaxDbP57080.
PRIDEP57080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023580; ENSMUSP00000023580; ENSMUSG00000022867. [P57080-1]
GeneID30940.
KEGGmmu:30940.
UCSCuc007zsb.1. mouse. [P57080-1]

Organism-specific databases

CTD29761.
MGIMGI:1353655. Usp25.

Phylogenomic databases

eggNOGCOG5077.
GeneTreeENSGT00390000016082.
HOGENOMHOG000007956.
HOVERGENHBG056030.
InParanoidP57080.
KOK11849.
OMASRSVIHK.
OrthoDBEOG761BSZ.
PhylomeDBP57080.
TreeFamTF329035.

Gene expression databases

ArrayExpressP57080.
BgeeP57080.
CleanExMM_USP25.
GenevestigatorP57080.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR003903. Ubiquitin-int_motif.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view]
SMARTSM00726. UIM. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS50330. UIM. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP25. mouse.
EvolutionaryTraceP57080.
NextBio307378.
PROP57080.
SOURCESearch...

Entry information

Entry nameUBP25_MOUSE
AccessionPrimary (citable) accession number: P57080
Secondary accession number(s): Q80ZT9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 13, 2004
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot