Ubiquitin carboxyl-terminal hydrolase 25

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P57080 (UBP25_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1055 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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 USP25m in muscle differentiating cells. Interacts (isoform USP25m only) with MYBPC1; the interaction prevents proteasomal degradation of MYBPC1. Interacts (isoform USP25m only) 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 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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
Molecular function	Hydrolase Protease Thiol protease
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein K48-linked deubiquitination Inferred from electronic annotation. Source: Compara protein K63-linked deubiquitination Inferred from electronic annotation. Source: Compara ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity Ref.1. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome complex Inferred from sequence or structural similarity Ref.1. Source: MGI
Molecular_function	ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from sequence or structural similarity Ref.1. Source: MGI
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1055

1055

Ubiquitin carboxyl-terminal hydrolase 25

PRO_0000080654

Regions

Domain

14 – 57

UBA-like

Repeat

97 – 116

UIM 1

Repeat

123 – 140

UIM 2

Region

77 – 102

SUMO interaction domain (SIM)

Motif

89 – 95

Required for SUMO paralog-specific binding

Sites

Active site

178

Nucleophile By similarity

Active site

608

Proton acceptor By similarity

Amino acid modifications

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Experimental info

Sequence conflict

394

E → K in AAF32264. Ref.1

Sequence conflict

496

P → L in AAF32264. Ref.1

Sequence conflict

683

P → L in AAF32264. Ref.1

Sequence conflict

841

H → L in AAF32264. Ref.1

Secondary structure

1055

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform 1 [UniParc].

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

1,055

121,420

        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' referencesShow '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.

IPI

IPI00331006.

RefSeq

NP_038946.2. NM_013918.2.

UniGene

Mm.40986.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VDL	NMR	-	A	1-67	[»]

ProteinModelPortal

P57080.

SMR

P57080. Positions 1-138, 169-407, 592-677.

ModBase

Search...

Protein family/group databases

MEROPS

C19.041.

PTM databases

PhosphoSite

P57080.

Proteomic databases

PaxDb

P57080.

PRIDE

P57080.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000023580; ENSMUSP00000023580; ENSMUSG00000022867.

GeneID

30940.

KEGG

mmu:30940.

UCSC

uc007zsb.1. mouse.

Organism-specific databases

CTD

29761.

MGI

MGI:1353655. Usp25.

Phylogenomic databases

eggNOG

COG5077.

GeneTree

ENSGT00390000016082.

HOGENOM

HOG000007956.

HOVERGEN

HBG056030.

InParanoid

P57080.

K11849.

OMA

DAFQMKA.

OrthoDB

EOG49S65J.

Gene expression databases

ArrayExpress

P57080.

Bgee

P57080.

CleanEx

MM_USP25.

Genevestigator

P57080.

GermOnline

ENSMUSG00000022867. Mus musculus.

Family and domain databases

InterPro

IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR009060. UBA-like.
IPR003903. Ubiquitin-int_motif.
[Graphical view]

Pfam

PF00443. UCH. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view]

SMART

SM00726. UIM. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.

PROSITE

PS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
PS50330. UIM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

USP25. mouse.

EvolutionaryTrace

P57080.

NextBio

307378.

SOURCE

Search...

Entry information

Entry name

UBP25_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents