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Ubiquitin carboxyl-terminal hydrolase 25 (EC 3.4.19.12) (Deubiquitinating enzyme 25) (Ubiquitin thioesterase 25) (Ubiquitin-specific-processing protease 25) (mUSP25)

 UBP25_MOUSE             Reviewed;        1055 AA.
P57080; Q80ZT9;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
20-JUN-2018, entry version 147.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 25;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 25;
AltName: Full=Ubiquitin thioesterase 25;
AltName: Full=Ubiquitin-specific-processing protease 25;
Short=mUSP25;
Name=Usp25;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
TISSUE=Kidney;
PubMed=10644437; DOI=10.1006/geno.1999.6025;
Valero R., Marfany G., Gonzalez-Angulo O., Gonzalez-Gonzalez G.,
Puelles L., Gonzalez-Duarte R.;
"USP25, a novel gene encoding a deubiquitinating enzyme, is located in
the gene-poor region 21q11.2.";
Genomics 62:395-405(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
STRUCTURE BY NMR OF 1-67.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-013, a UBA domain in mouse.";
Submitted (SEP-2004) to the PDB data bank.
[5]
ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE, POSSIBLE FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=16501887; DOI=10.1007/s00018-005-5533-1;
Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G.,
Marfany G.;
"The ubiquitin-specific protease USP25 interacts with three sarcomeric
proteins.";
Cell. Mol. Life Sci. 63:723-734(2006).
-!- 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). {ECO:0000250}.
-!- FUNCTION: The muscle-specific isoform (USP25m) may have a role in
the regulation of muscular differentiation and function.
-!- 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: 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16501887}.
Nucleus {ECO:0000269|PubMed:16501887}. Note=The longer muscle-
specific isoform (USP25m) Some transient punctuate nuclear
location in myotubes during myocyte development.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A longer muscle-specific isoform, USP25m, also exists.;
Name=1;
IsoId=P57080-1; Sequence=Displayed;
-!- 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.
{ECO:0000269|PubMed:10644437}.
-!- 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. {ECO:0000269|PubMed:10644437,
ECO:0000269|PubMed:16501887}.
-!- PTM: Acetylated. {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: Preferentially monoubiquitinated but can also be
polyubiquitinated. Autodeubiquitinated. Ubiquitination activates
the enzymatic activity either by preventing sumoylation or by
allowing novel interactions (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylation in the C-terminal by SYK regulates USP25
cellular levels. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF170563; AAF32264.1; -; mRNA.
EMBL; BC048171; AAH48171.1; -; mRNA.
EMBL; BC063059; AAH63059.1; -; mRNA.
CCDS; CCDS28275.1; -. [P57080-1]
RefSeq; NP_038946.2; NM_013918.2. [P57080-1]
UniGene; Mm.40986; -.
PDB; 1VDL; NMR; -; A=1-67.
PDBsum; 1VDL; -.
ProteinModelPortal; P57080; -.
SMR; P57080; -.
BioGrid; 206017; 1.
IntAct; P57080; 2.
STRING; 10090.ENSMUSP00000023580; -.
MEROPS; C19.041; -.
iPTMnet; P57080; -.
PhosphoSitePlus; P57080; -.
EPD; P57080; -.
MaxQB; P57080; -.
PaxDb; P57080; -.
PeptideAtlas; P57080; -.
PRIDE; P57080; -.
Ensembl; ENSMUST00000023580; ENSMUSP00000023580; ENSMUSG00000022867. [P57080-1]
GeneID; 30940; -.
KEGG; mmu:30940; -.
UCSC; uc007zsb.1; mouse. [P57080-1]
CTD; 29761; -.
MGI; MGI:1353655; Usp25.
eggNOG; KOG1863; Eukaryota.
eggNOG; COG5077; LUCA.
GeneTree; ENSGT00390000016082; -.
HOGENOM; HOG000007956; -.
HOVERGEN; HBG056030; -.
InParanoid; P57080; -.
KO; K11849; -.
OMA; WAYIFDH; -.
OrthoDB; EOG091G00QR; -.
PhylomeDB; P57080; -.
TreeFam; TF329035; -.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
ChiTaRS; Usp25; mouse.
EvolutionaryTrace; P57080; -.
PRO; PR:P57080; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022867; -.
CleanEx; MM_USP25; -.
Genevisible; P57080; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000502; C:proteasome complex; ISS:MGI.
GO; GO:0051117; F:ATPase binding; ISO:MGI.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; ISS:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:1904293; P:negative regulation of ERAD pathway; ISO:MGI.
GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
GO; GO:0071108; P:protein K48-linked deubiquitination; ISO:MGI.
GO; GO:0070536; P:protein K63-linked deubiquitination; ISO:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:MGI.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR009060; UBA-like_sf.
InterPro; IPR003903; UIM_dom.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 1.
Pfam; PF02809; UIM; 2.
SMART; SM00726; UIM; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF54001; SSF54001; 2.
PROSITE; PS50330; UIM; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein;
Protease; Reference proteome; Repeat; Thiol protease; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 1055 Ubiquitin carboxyl-terminal hydrolase 25.
/FTId=PRO_0000080654.
DOMAIN 14 57 UBA-like.
DOMAIN 97 116 UIM 1. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 123 140 UIM 2. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 169 658 USP.
REGION 77 102 SUMO interaction domain (SIM).
MOTIF 89 95 Required for SUMO paralog-specific
binding.
ACT_SITE 178 178 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
ACT_SITE 608 608 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UHP3}.
MOD_RES 740 740 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9UHP3}.
CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q9UHP3}.
CONFLICT 394 394 E -> K (in Ref. 1; AAF32264).
{ECO:0000305}.
CONFLICT 496 496 P -> L (in Ref. 1; AAF32264).
{ECO:0000305}.
CONFLICT 683 683 P -> L (in Ref. 1; AAF32264).
{ECO:0000305}.
CONFLICT 841 841 H -> L (in Ref. 1; AAF32264).
{ECO:0000305}.
HELIX 9 12 {ECO:0000244|PDB:1VDL}.
HELIX 17 27 {ECO:0000244|PDB:1VDL}.
HELIX 33 43 {ECO:0000244|PDB:1VDL}.
HELIX 47 55 {ECO:0000244|PDB:1VDL}.
SEQUENCE 1055 AA; 121420 MW; 103E34EC3FA8A72B CRC64;
MTVEQNVLQQ SAAQKHQQTF LNQLREITGI NDAQILQQAL KDSNGNLELA VAFLTAKNAK
TPPQEETGYY QTALPGNDRY ISVGSQADAN VIDLTGDDKD DLQRAIALSL AESNRAFRET
GITDEEQAIS RVLEASIAEN KACLKRTPIE VWRDSRNPYD RKRQEKAPVG LKNVGNTCWF
SAVIQSLFNL LEFRRLVLNY KPPSNAQDLP RNQKEHRNLP FMRELRYLFA LLVGTKRKYV
DPSRAVEILK DAFKSNDSQQ QDVSEFTHKL LDWLEDAFQM KAEEETDEEK PKNPMVELFY
GRFLAMGVLE GKKFENTEMF GQYPLQVNGF KDLHECLEAA MIEGEIESLH SDNSGKSGQE
HWFTELPPVL TFELSRFEFN QALGRPEKIH NKLEFPQVLY LDRYMHRNRE ITRIKREEIK
RLKDYLTVLQ QRLERYLSYG SGPKRFPLVD VLQYALEFAS SKPVCTSPVD DIDASSSASG
PLPSQSLPST TEQQGPCASD LPGSSSPASG AALPLRSVIH KPFTQSRIPP DLPMHPAPRH
ITEEELCVLE SCLHRWRTEI ENDTRDLQES ISRIHRTIEL MYSDKSMIQV PYRLHAVLVH
EGQANAGHYW AYIFDHRESR WMKYNDIAVT KSSWEELVRD SFGGYRNASA YCLMYIDDKA
QFLIQEEFNK ETGQALVGME TLPPDLRDFV EEDNQRFEKE LEEWDTQLAQ RSLQEKLLAA
PKLREAEASA TTAQAGGADY LEQPSRSDLS KHWKEETLRV IAKASHDLED KGPETVLQSA
IKLEYSRLVK LAQEDTPPET DYRLHHVLVY FIQNQAPKKI IEKTLLEQFG DRNLSFDERC
HNIMKVAQAK LEMIKPEEVN LEEYEEWHAD YKKFRETTMY LITGLENFQR ESYIDSLLFL
LCAYQNNKEL LSKGPYRGHD GELISHYRRE CLLKLNEQAA ELFESGEDGD VNNGLIIMNE
FIVPFLPLLL VDDMEEKDIL AVEDMRNRWC SYLGQEMEAN LQEKLTDFLP KLLDCSTEIK
GFHEPPKLPS YSAHELCERF ARIMLSLSRT PADGR


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