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Ubiquitin carboxyl-terminal hydrolase 2 (EC 3.4.19.12) (41 kDa ubiquitin-specific protease) (Deubiquitinating enzyme 2) (Ubiquitin thioesterase 2) (Ubiquitin-specific-processing protease 2)

 UBP2_HUMAN              Reviewed;         605 AA.
O75604; B0YJB8; E9PPM2; Q8IUM2; Q8IW04; Q96MB9; Q9BQ21;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
27-MAR-2002, sequence version 2.
22-NOV-2017, entry version 166.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 2;
EC=3.4.19.12;
AltName: Full=41 kDa ubiquitin-specific protease;
AltName: Full=Deubiquitinating enzyme 2;
AltName: Full=Ubiquitin thioesterase 2;
AltName: Full=Ubiquitin-specific-processing protease 2;
Name=USP2; Synonyms=UBP41;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Placenta;
Gong L., Yeh E.T.H.;
"Cloning and expression of the human and mouse UBP41.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Prostate cancer;
Rossi S., Graner E., Weinstein L.J., Loda M.;
"Molecular cloning and characterization of USP2b in the human prostate
cancer cell line LNCaP.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Lymph, and Testis;
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).
[8]
FUNCTION, INTERACTION WITH MDM2, AND MUTAGENESIS OF HIS-549.
PubMed=17290220; DOI=10.1038/sj.emboj.7601567;
Stevenson L.F., Sparks A., Allende-Vega N., Xirodimas D.P., Lane D.P.,
Saville M.K.;
"The deubiquitinating enzyme USP2a regulates the p53 pathway by
targeting Mdm2.";
EMBO J. 26:976-986(2007).
[9]
FUNCTION, INTERACTION WITH CCND1, AND MUTAGENESIS OF CYS-276.
PubMed=19917254; DOI=10.1016/j.molcel.2009.10.018;
Shan J., Zhao W., Gu W.;
"Suppression of cancer cell growth by promoting cyclin D1
degradation.";
Mol. Cell 36:469-476(2009).
[10]
FUNCTION, INTERACTION WITH MDM2 AND MDM4, INDUCTION, AND MUTAGENESIS
OF HIS-549.
PubMed=19838211; DOI=10.1038/onc.2009.330;
Allende-Vega N., Sparks A., Lane D.P., Saville M.K.;
"MdmX is a substrate for the deubiquitinating enzyme USP2a.";
Oncogene 29:432-441(2010).
[11]
TISSUE SPECIFICITY.
PubMed=20403044; DOI=10.1111/j.1440-1827.2010.02496.x;
Wang S., Wu H., Liu Y., Sun J., Zhao Z., Chen Q., Guo M., Ma D.,
Zhang Z.;
"Expression of USP2-69 in mesangial cells in vivo and in vitro.";
Pathol. Int. 60:184-192(2010).
[12]
INTERACTION WITH KCNQ1.
PubMed=22024150; DOI=10.1016/j.hrthm.2011.10.026;
Krzystanek K., Rasmussen H.B., Grunnet M., Staub O., Olesen S.P.,
Abriel H., Jespersen T.;
"Deubiquitylating enzyme USP2 counteracts Nedd4-2-mediated
downregulation of KCNQ1 potassium channels.";
Heart Rhythm 9:440-448(2012).
[13]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 251-605.
Structural genomics consortium (SGC);
"Covalent ubiquitin-usp2 complex.";
Submitted (FEB-2009) to the PDB data bank.
[14]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 258-605 IN COMPLEX WITH
UBIQUITIN AND ZINC-BINDING, AND ENZYME REGULATION.
PubMed=16905103; DOI=10.1016/j.str.2006.06.012;
Renatus M., Parrado S.G., D'Arcy A., Eidhoff U., Gerhartz B.,
Hassiepen U., Pierrat B., Riedl R., Vinzenz D., Worpenberg S.,
Kroemer M.;
"Structural basis of ubiquitin recognition by the deubiquitinating
protease USP2.";
Structure 14:1293-1302(2006).
-!- FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target
proteins such as MDM2, MDM4 and CCND1 (PubMed:17290220,
PubMed:19917254, PubMed:19838211). Isoform 1 and isoform 4 possess
both ubiquitin-specific peptidase and isopeptidase activities (By
similarity). Deubiquitinates MDM2 without reversing MDM2-mediated
p53/TP53 ubiquitination and thus indirectly promotes p53/TP53
degradation and limits p53 activity (PubMed:17290220,
PubMed:19838211). Has no deubiquitinase activity against p53/TP53
(PubMed:17290220). Prevents MDM2-mediated degradation of MDM4
(PubMed:17290220). Plays a role in the G1/S cell-cycle progression
in normal and cancer cells (PubMed:19917254). Regulates the
circadian clock by modulating its intrinsic circadian rhythm and
its capacity to respond to external cues (By similarity).
Associates with clock proteins and deubiquitinates core clock
component PER1 but does not affect its overall stability (By
similarity). Regulates the nucleocytoplasmic shuttling and nuclear
retention of PER1 and its repressive role on the clock
transcription factors CLOCK and ARNTL/BMAL1 (By similarity). Plays
a role in the regulation of myogenic differentiation of embryonic
muscle cells (By similarity). {ECO:0000250|UniProtKB:O88623,
ECO:0000250|UniProtKB:Q5U349, ECO:0000269|PubMed:17290220,
ECO:0000269|PubMed:19838211, ECO:0000269|PubMed:19917254}.
-!- FUNCTION: Isoform 4: Circadian clock output effector that
regulates Ca(2+) absorption in the small intestine. Probably
functions by regulating protein levels of the membrane scaffold
protein NHERF4 in a rhythmic manner, and is therefore likely to
control Ca(2+) membrane permeability mediated by the Ca(2+)
channel TRPV6 in the intestine. {ECO:0000250|UniProtKB:O88623}.
-!- 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: Cleavage is inhibited by ubiquitin in a dosage-
dependent manner. Cleavage is blocked by ubiquitin aldehyde.
{ECO:0000269|PubMed:16905103}.
-!- SUBUNIT: Homooligomer (By similarity). Found in trimeric complex
with MDM2 and MDM4 and USP2. Interacts with CCND1; the interaction
is direct and promotes its stabilization by antagonizing
ubiquitin-dependent degradation. Interacts (via N-terminus and C-
terminus) with MDM2. Interacts with MDM4. Interacts with PER1 (By
similarity). Interacts with KCNQ1; counteracts the NEDD4L-specific
down-regulation of I(Ks) and restore plasma membrane localization
of KCNQ1 (PubMed:22024150). Isoform 4: Interacts with PDZD3 and
CLTC (By similarity). {ECO:0000250|UniProtKB:O88623,
ECO:0000250|UniProtKB:Q5U349, ECO:0000269|PubMed:17290220,
ECO:0000269|PubMed:19838211, ECO:0000269|PubMed:19917254,
ECO:0000269|PubMed:22024150}.
-!- INTERACTION:
Q9NYB9-2:ABI2; NbExp=4; IntAct=EBI-743272, EBI-11096309;
Q86V38:ATN1; NbExp=4; IntAct=EBI-743272, EBI-11954292;
Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-743272, EBI-10171416;
Q8IYA8:CCDC36; NbExp=3; IntAct=EBI-743272, EBI-8638439;
Q2TAC2:CCDC57; NbExp=3; IntAct=EBI-743272, EBI-2808286;
Q8WTU0:DDI1; NbExp=4; IntAct=EBI-743272, EBI-748248;
Q08379:GOLGA2; NbExp=5; IntAct=EBI-743272, EBI-618309;
Q9NYA3:GOLGA6A; NbExp=4; IntAct=EBI-743272, EBI-11163335;
Q4V328:GRIPAP1; NbExp=4; IntAct=EBI-743272, EBI-717919;
Q9NSC5:HOMER3; NbExp=5; IntAct=EBI-743272, EBI-748420;
Q9UJC3:HOOK1; NbExp=3; IntAct=EBI-743272, EBI-746704;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-743272, EBI-2125614;
P19012:KRT15; NbExp=5; IntAct=EBI-743272, EBI-739566;
Q6A162:KRT40; NbExp=5; IntAct=EBI-743272, EBI-10171697;
Q969G2:LHX4; NbExp=3; IntAct=EBI-743272, EBI-2865388;
Q9BRK4:LZTS2; NbExp=5; IntAct=EBI-743272, EBI-741037;
Q00987:MDM2; NbExp=4; IntAct=EBI-743272, EBI-389668;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-743272, EBI-742948;
Q9GZM8:NDEL1; NbExp=5; IntAct=EBI-743272, EBI-928842;
I6L9F6:NEFL; NbExp=3; IntAct=EBI-743272, EBI-10178578;
Q8ND90:PNMA1; NbExp=3; IntAct=EBI-743272, EBI-302345;
Q12933:TRAF2; NbExp=6; IntAct=EBI-743272, EBI-355744;
Q9Y4K3:TRAF6; NbExp=3; IntAct=EBI-743272, EBI-359276;
P14373:TRIM27; NbExp=5; IntAct=EBI-743272, EBI-719493;
Q86XT4:TRIM50; NbExp=4; IntAct=EBI-743272, EBI-9867283;
Q8N1B4:VPS52; NbExp=5; IntAct=EBI-743272, EBI-2799833;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88623}.
Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88623}.
Note=Localizes in the spermatid head in late-elongating spermatids
in the thin area between the outer acrosomal membrane and the
plasma membrane. {ECO:0000250|UniProtKB:Q5U349}.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus
{ECO:0000250|UniProtKB:Q5U349}. Membrane
{ECO:0000250|UniProtKB:O88623}; Peripheral membrane protein
{ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O88623}.
Note=Predominantly expressed at membranes.
{ECO:0000250|UniProtKB:O88623}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=USP2a, USP2-69;
IsoId=O75604-1; Sequence=Displayed;
Name=2; Synonyms=USP2b;
IsoId=O75604-2; Sequence=VSP_005256, VSP_005257;
Note=No experimental confirmation available.;
Name=3;
IsoId=O75604-3; Sequence=VSP_039559;
Note=Ref.7 (AAH41366) sequence is in conflict in position:
10:Y->S. {ECO:0000305};
Name=4;
IsoId=O75604-4; Sequence=VSP_039560;
-!- TISSUE SPECIFICITY: Expressed in mesangial cells of the kidney and
in different types of glomerulonephritides (at protein level).
{ECO:0000269|PubMed:20403044}.
-!- INDUCTION: Down-regulated by cisplatin (at protein level).
{ECO:0000269|PubMed:19838211}.
-!- DOMAIN: The different N-terminus extensions of isoform 1 and
isoform 4 determine their respective subcellular localization and
differentiel effect on myoblast fusion and accumulation of muscle-
specific proteins. The different N-terminus extensions of isoform
1 and isoform 4 are not essential for their catalytic activity.
{ECO:0000250|UniProtKB:Q5U349}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP2 subfamily.
{ECO:0000305}.
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EMBL; AF079564; AAC28392.1; -; mRNA.
EMBL; AF440755; AAN65363.1; -; mRNA.
EMBL; AK057225; BAB71388.1; -; mRNA.
EMBL; AK292255; BAF84944.1; -; mRNA.
EMBL; EF445044; ACA06096.1; -; Genomic_DNA.
EMBL; EF445044; ACA06097.1; -; Genomic_DNA.
EMBL; AP003396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67484.1; -; Genomic_DNA.
EMBL; CH471065; EAW67485.1; -; Genomic_DNA.
EMBL; CH471065; EAW67486.1; -; Genomic_DNA.
EMBL; BC002854; AAH02854.1; -; mRNA.
EMBL; BC002955; AAH02955.1; -; mRNA.
EMBL; BC041366; AAH41366.1; -; mRNA.
CCDS; CCDS58189.1; -. [O75604-3]
CCDS; CCDS8422.1; -. [O75604-1]
CCDS; CCDS8423.1; -. [O75604-4]
RefSeq; NP_001230688.1; NM_001243759.1. [O75604-3]
RefSeq; NP_004196.4; NM_004205.4. [O75604-1]
RefSeq; NP_741994.1; NM_171997.2. [O75604-4]
RefSeq; XP_005271778.1; XM_005271721.4. [O75604-1]
RefSeq; XP_005271779.1; XM_005271722.2. [O75604-1]
UniGene; Hs.524085; -.
PDB; 2HD5; X-ray; 1.85 A; A=258-605.
PDB; 2IBI; X-ray; 2.20 A; A=251-605.
PDB; 3NHE; X-ray; 1.26 A; A=258-605.
PDB; 3V6C; X-ray; 1.70 A; A=258-605.
PDB; 3V6E; X-ray; 2.10 A; A=258-605.
PDBsum; 2HD5; -.
PDBsum; 2IBI; -.
PDBsum; 3NHE; -.
PDBsum; 3V6C; -.
PDBsum; 3V6E; -.
ProteinModelPortal; O75604; -.
SMR; O75604; -.
BioGrid; 114553; 106.
CORUM; O75604; -.
DIP; DIP-29134N; -.
IntAct; O75604; 104.
MINT; MINT-4304073; -.
STRING; 9606.ENSP00000260187; -.
BindingDB; O75604; -.
ChEMBL; CHEMBL1293227; -.
MEROPS; C19.013; -.
iPTMnet; O75604; -.
PhosphoSitePlus; O75604; -.
BioMuta; USP2; -.
MaxQB; O75604; -.
PaxDb; O75604; -.
PeptideAtlas; O75604; -.
PRIDE; O75604; -.
DNASU; 9099; -.
Ensembl; ENST00000260187; ENSP00000260187; ENSG00000036672. [O75604-1]
Ensembl; ENST00000455332; ENSP00000407842; ENSG00000036672. [O75604-3]
Ensembl; ENST00000525735; ENSP00000436952; ENSG00000036672. [O75604-4]
GeneID; 9099; -.
KEGG; hsa:9099; -.
UCSC; uc001pwl.5; human. [O75604-1]
CTD; 9099; -.
DisGeNET; 9099; -.
EuPathDB; HostDB:ENSG00000036672.15; -.
GeneCards; USP2; -.
HGNC; HGNC:12618; USP2.
HPA; HPA006777; -.
HPA; HPA007222; -.
MIM; 604725; gene.
neXtProt; NX_O75604; -.
OpenTargets; ENSG00000036672; -.
PharmGKB; PA37244; -.
eggNOG; KOG1868; Eukaryota.
eggNOG; ENOG410XP8T; LUCA.
GeneTree; ENSGT00860000133682; -.
HOGENOM; HOG000231498; -.
HOVERGEN; HBG011164; -.
InParanoid; O75604; -.
KO; K11833; -.
OMA; MRTSYTV; -.
OrthoDB; EOG091G0120; -.
PhylomeDB; O75604; -.
TreeFam; TF106277; -.
Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
ChiTaRS; USP2; human.
EvolutionaryTrace; O75604; -.
GeneWiki; USP2; -.
GenomeRNAi; 9099; -.
PRO; PR:O75604; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000036672; -.
CleanEx; HS_USP2; -.
ExpressionAtlas; O75604; baseline and differential.
Genevisible; O75604; HS.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:FlyBase.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0048512; P:circadian behavior; ISS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 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; Biological rhythms; Cell cycle;
Complete proteome; Cytoplasm; Hydrolase; Membrane; Metal-binding;
Myogenesis; Nucleus; Polymorphism; Protease; Reference proteome;
Thiol protease; Ubl conjugation pathway; Zinc.
CHAIN 1 605 Ubiquitin carboxyl-terminal hydrolase 2.
/FTId=PRO_0000080616.
DOMAIN 267 599 USP.
REGION 1 200 Necessary for interaction with MDM4.
{ECO:0000269|PubMed:19838211}.
REGION 403 503 Necessary for interaction with MDM4.
{ECO:0000269|PubMed:19838211}.
ACT_SITE 276 276 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
ACT_SITE 557 557 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
METAL 425 425 Zinc. {ECO:0000269|PubMed:16905103}.
METAL 428 428 Zinc. {ECO:0000269|PubMed:16905103}.
METAL 476 476 Zinc. {ECO:0000269|PubMed:16905103}.
METAL 479 479 Zinc. {ECO:0000269|PubMed:16905103}.
VAR_SEQ 1 258 MSQLSSTLKRYTESARYTDAHYAKSGYGAYTPSSYGANLAA
SLLEKEKLGFKPVPTSSFLTRPRTYGPSSLLDYDRGRPLLR
PDITGGGKRAESQTRGTERPLGSGLSGGSGFPYGVTNNCLS
YLPINAYDQGVTLTQKLDSQSDLARDFSSLRTSDSYRIDPR
NLGRSPMLARTRKELCTLQGLYQTASCPEYLVDYLENYGRK
GSASQVPSQAPPSRVPEIISPTYRPIGRYTLWETGKGQAPG
PSRSSSPGRDGM -> MLVPGSTRPYSKKRQ (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039559.
VAR_SEQ 1 258 MSQLSSTLKRYTESARYTDAHYAKSGYGAYTPSSYGANLAA
SLLEKEKLGFKPVPTSSFLTRPRTYGPSSLLDYDRGRPLLR
PDITGGGKRAESQTRGTERPLGSGLSGGSGFPYGVTNNCLS
YLPINAYDQGVTLTQKLDSQSDLARDFSSLRTSDSYRIDPR
NLGRSPMLARTRKELCTLQGLYQTASCPEYLVDYLENYGRK
GSASQVPSQAPPSRVPEIISPTYRPIGRYTLWETGKGQAPG
PSRSSSPGRDGM -> MRTSYTVTLPEDPPAAPFPALAKEL
RPRSPLSPSLLLSTFVGLLLNKAK (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_039560.
VAR_SEQ 1 252 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_005256.
VAR_SEQ 253 258 PGRDGM -> MLNKAK (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_005257.
VARIANT 174 174 R -> Q (in dbSNP:rs33929148).
/FTId=VAR_051519.
VARIANT 383 383 N -> S (in dbSNP:rs45533837).
/FTId=VAR_051520.
MUTAGEN 276 276 C->A: Loss of enzymatic activity.
Increases the steady-state level of
CCND1. {ECO:0000269|PubMed:19917254}.
MUTAGEN 549 549 H->A: Loss of enzymatic activity.
Increases the steady-state level of MDM2
and MDM4 that leads to attenuation of
MDM2-mediated degradation of p53/TP53 and
MDM4. Increases the level of p53/TP53 and
MDM4 ubiquitin conjugates.
{ECO:0000269|PubMed:17290220,
ECO:0000269|PubMed:19838211}.
CONFLICT 421 421 S -> G (in Ref. 3; BAB71388).
{ECO:0000305}.
CONFLICT 501 501 H -> R (in Ref. 3; BAB71388).
{ECO:0000305}.
CONFLICT 594 594 L -> H (in Ref. 1; AAC28392).
{ECO:0000305}.
CONFLICT 602 605 PSRM -> TSPI (in Ref. 1; AAC28392).
{ECO:0000305}.
STRAND 272 274 {ECO:0000244|PDB:3V6E}.
HELIX 276 286 {ECO:0000244|PDB:3NHE}.
HELIX 289 296 {ECO:0000244|PDB:3NHE}.
HELIX 299 302 {ECO:0000244|PDB:3NHE}.
HELIX 312 325 {ECO:0000244|PDB:3NHE}.
HELIX 337 346 {ECO:0000244|PDB:3NHE}.
HELIX 348 350 {ECO:0000244|PDB:3NHE}.
STRAND 351 353 {ECO:0000244|PDB:3NHE}.
HELIX 358 373 {ECO:0000244|PDB:3NHE}.
HELIX 392 404 {ECO:0000244|PDB:3NHE}.
HELIX 410 415 {ECO:0000244|PDB:3NHE}.
STRAND 417 425 {ECO:0000244|PDB:3NHE}.
TURN 426 428 {ECO:0000244|PDB:3NHE}.
STRAND 431 443 {ECO:0000244|PDB:3NHE}.
HELIX 455 463 {ECO:0000244|PDB:3NHE}.
STRAND 466 468 {ECO:0000244|PDB:3NHE}.
HELIX 470 472 {ECO:0000244|PDB:3NHE}.
TURN 477 480 {ECO:0000244|PDB:3NHE}.
STRAND 485 493 {ECO:0000244|PDB:3NHE}.
STRAND 496 502 {ECO:0000244|PDB:3NHE}.
HELIX 529 531 {ECO:0000244|PDB:3NHE}.
STRAND 532 536 {ECO:0000244|PDB:2HD5}.
STRAND 540 551 {ECO:0000244|PDB:3NHE}.
STRAND 553 555 {ECO:0000244|PDB:3V6C}.
STRAND 556 563 {ECO:0000244|PDB:3NHE}.
TURN 565 567 {ECO:0000244|PDB:3NHE}.
STRAND 570 574 {ECO:0000244|PDB:3NHE}.
STRAND 577 581 {ECO:0000244|PDB:3NHE}.
HELIX 583 585 {ECO:0000244|PDB:3NHE}.
STRAND 591 598 {ECO:0000244|PDB:3NHE}.
SEQUENCE 605 AA; 68072 MW; AFF4DA9344D21812 CRC64;
MSQLSSTLKR YTESARYTDA HYAKSGYGAY TPSSYGANLA ASLLEKEKLG FKPVPTSSFL
TRPRTYGPSS LLDYDRGRPL LRPDITGGGK RAESQTRGTE RPLGSGLSGG SGFPYGVTNN
CLSYLPINAY DQGVTLTQKL DSQSDLARDF SSLRTSDSYR IDPRNLGRSP MLARTRKELC
TLQGLYQTAS CPEYLVDYLE NYGRKGSASQ VPSQAPPSRV PEIISPTYRP IGRYTLWETG
KGQAPGPSRS SSPGRDGMNS KSAQGLAGLR NLGNTCFMNS ILQCLSNTRE LRDYCLQRLY
MRDLHHGSNA HTALVEEFAK LIQTIWTSSP NDVVSPSEFK TQIQRYAPRF VGYNQQDAQE
FLRFLLDGLH NEVNRVTLRP KSNPENLDHL PDDEKGRQMW RKYLEREDSR IGDLFVGQLK
SSLTCTDCGY CSTVFDPFWD LSLPIAKRGY PEVTLMDCMR LFTKEDVLDG DEKPTCCRCR
GRKRCIKKFS IQRFPKILVL HLKRFSESRI RTSKLTTFVN FPLRDLDLRE FASENTNHAV
YNLYAVSNHS GTTMGGHYTA YCRSPGTGEW HTFNDSSVTP MSSSQVRTSD AYLLFYELAS
PPSRM


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