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Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Deubiquitinating enzyme 7) (Herpesvirus-associated ubiquitin-specific protease) (rHAUSP) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7)

 UBP7_RAT                Reviewed;        1103 AA.
Q4VSI4;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
23-MAY-2018, entry version 99.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7;
EC=3.4.19.12 {ECO:0000269|PubMed:16111684, ECO:0000269|PubMed:16328052};
AltName: Full=Deubiquitinating enzyme 7;
AltName: Full=Herpesvirus-associated ubiquitin-specific protease;
Short=rHAUSP;
AltName: Full=Ubiquitin thioesterase 7;
AltName: Full=Ubiquitin-specific-processing protease 7;
Name=Usp7; Synonyms=Hausp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
TISSUE SPECIFICITY, MUTAGENESIS OF CYS-224, POLYUBIQUITINATION, AND
POLYNEDDYLATION.
TISSUE=Testis;
PubMed=16111684; DOI=10.1016/j.febslet.2005.07.048;
Lee H.-J., Kim M.-S., Kim Y.-K., Oh Y.-K., Baek K.-H.;
"HAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated,
polyneddylated, and dimerized.";
FEBS Lett. 579:4867-4872(2005).
[2]
FUNCTION, CATALYTIC ACTIVITY, UBIQUITINATION, AND MUTAGENESIS OF
CYS-224.
TISSUE=Testis;
PubMed=16328052;
Baek K.H., Lee H.J., Kim M.S., Kim Y.S., Seong M., Lee E.J., Lee M.Y.;
"Molecular cloning of rHAUSP encoding a deubiquitinating enzyme in rat
testis.";
Oncol. Rep. 15:173-177(2006).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Hydrolase that deubiquitinates target proteins such as
FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and
DAXX (PubMed:16111684, PubMed:16328052). Together with DAXX,
prevents MDM2 self-ubiquitination and enhances the E3 ligase
activity of MDM2 towards p53/TP53, thereby promoting p53/TP53
ubiquitination and proteasomal degradation (By similarity).
Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and
enhances p53/TP53-dependent transcription regulation, cell growth
repression and apoptosis (By similarity). Deubiquitinates p53/TP53
and MDM2 and strongly stabilizes p53/TP53 even in the presence of
excess MDM2, and also induces p53/TP53-dependent cell growth
repression and apoptosis (By similarity). Deubiquitination of
FOXO4 in presence of hydrogen peroxide is not dependent on
p53/TP53 and inhibits FOXO4-induced transcriptional activity. In
association with DAXX, is involved in the deubiquitination and
translocation of PTEN from the nucleus to the cytoplasm, both
processes that are counteracted by PML (By similarity).
Deubiquitinates KMT2E preventing KMT2E proteasomal-mediated
degradation (By similarity). Involved in cell proliferation during
early embryonic development (By similarity). Involved in
transcription-coupled nucleotide excision repair (TC-NER) in
response to UV damage: recruited to DNA damage sites following
interaction with KIAA1530/UVSSA and promotes deubiquitination of
ERCC6, preventing UV-induced degradation of ERCC6 (By similarity).
Involved in maintenance of DNA methylation via its interaction
with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1
and DNMT1, preventing their degradation and promoting DNA
methylation by DNMT1 (By similarity). Deubiquitinates alkylation
repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize
ALKBH3, thereby promoting the repair of alkylated DNA lesions (By
similarity). Acts as a chromatin regulator via its association
with the Polycomb group (PcG) multiprotein PRC1-like complex; may
act by deubiquitinating components of the PRC1-like complex (By
similarity). Able to mediate deubiquitination of histone H2B; it
is however unsure whether this activity takes place in vivo (By
similarity). Exhibits a preference towards 'Lys-48'-linked
ubiquitin chains. Increases regulatory T-cells (Treg) suppressive
capacity by deubiquitinating and stabilizing transcription factor
FOXP3 which is crucial for Treg cell function (By similarity).
{ECO:0000250|UniProtKB:Q93009, ECO:0000269|PubMed:16111684,
ECO:0000269|PubMed:16328052}.
-!- 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).
{ECO:0000269|PubMed:16111684, ECO:0000269|PubMed:16328052}.
-!- SUBUNIT: Monomer. Homodimer (PubMed:16111684). Part of a complex
with DAXX, MDM2, RASSF1 and USP7. Part of a complex with DAXX,
MDM2 and USP7. Interacts with MDM2; the interaction is independent
of p53/TP53. Interacts with DAXX; the interaction is direct and
independent of MDM2 and p53/TP53. Component of a complex composed
of KMT2E, OGT and USP7; the complex stabilizes KMT2E, preventing
KMT2E ubiquitination and proteosomal-mediated degradation (By
similarity). Interacts (via MATH domain) with KMT2E (By
similarity). Interacts with OGT (By similarity). Interacts with
FOXO4; the interaction is enhanced in presence of hydrogen
peroxide and occurs independently of p53/TP53. Interacts with
p53/TP53; the interaction is enhanced in response to DNA damage;
the interaction is impaired by TSPYL5. Interacts with PTEN; the
interaction is direct. Interacts with ATXN1 and the strength of
interaction is influenced by the length of the poly-Gln region in
ATXN1. A weaker interaction seen with mutants having longer poly-
Gln regions. Interacts with KIAA1530/UVSSA. Interacts with MEX3C
and antagonizes its ability to degrade mRNA. Interacts with DNMT1
and UHRF1. Interacts with FOXP3. Interacts (via MATH domain) with
RNF220 (By similarity). Associated component of the Polycomb group
(PcG) multiprotein PRC1-like complex (By similarity). Interacts
with EPOP (By similarity). Interacts with OTUD4 and USP9X; the
interaction is direct (By similarity).
{ECO:0000250|UniProtKB:Q6A4J8, ECO:0000250|UniProtKB:Q93009,
ECO:0000269|PubMed:16111684}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93009}.
Cytoplasm {ECO:0000250|UniProtKB:Q93009}. Nucleus, PML body
{ECO:0000250|UniProtKB:Q93009}. Chromosome
{ECO:0000250|UniProtKB:Q93009}. Note=Present in a minority of ND10
nuclear bodies. Association with ICP0/VMW110 at early times of
infection leads to an increased proportion of USP7-containing
ND10. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX
in speckled structures. Colocalized with PML and PTEN in
promyelocytic leukemia protein (PML) nuclear bodies.
{ECO:0000250|UniProtKB:Q93009}.
-!- TISSUE SPECIFICITY: Strongly expressed in the testis, spleen and
brain. Weakly expressed in the stomach, small intestine, skeletal
muscle and uterus. {ECO:0000269|PubMed:16111684}.
-!- DOMAIN: The C-terminus plays a role in its oligomerization.
-!- PTM: Polyneddylated. {ECO:0000269|PubMed:16111684}.
-!- PTM: Not sumoylated. {ECO:0000250}.
-!- PTM: Ubiquitinated at Lys-870 (By similarity). Polyubiquitinated.
{ECO:0000250|UniProtKB:Q93009, ECO:0000269|PubMed:16111684,
ECO:0000269|PubMed:16328052}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY641530; AAT68666.1; -; mRNA.
RefSeq; NP_001019961.1; NM_001024790.1.
UniGene; Rn.72721; -.
ProteinModelPortal; Q4VSI4; -.
SMR; Q4VSI4; -.
BioGrid; 261960; 2.
MINT; Q4VSI4; -.
STRING; 10116.ENSRNOP00000041134; -.
MEROPS; C19.016; -.
iPTMnet; Q4VSI4; -.
PhosphoSitePlus; Q4VSI4; -.
PaxDb; Q4VSI4; -.
PRIDE; Q4VSI4; -.
GeneID; 360471; -.
KEGG; rno:360471; -.
UCSC; RGD:1306915; rat.
CTD; 7874; -.
RGD; 1306915; Usp7.
eggNOG; KOG1863; Eukaryota.
eggNOG; COG5077; LUCA.
HOGENOM; HOG000160240; -.
HOVERGEN; HBG018029; -.
InParanoid; Q4VSI4; -.
KO; K11838; -.
PhylomeDB; Q4VSI4; -.
PRO; PR:Q4VSI4; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:RGD.
GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; ISS:UniProtKB.
GO; GO:0010216; P:maintenance of DNA methylation; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
GO; GO:1901537; P:positive regulation of DNA demethylation; ISS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:RGD.
GO; GO:0051090; P:regulation of DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IDA:RGD.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 2.60.210.10; -; 1.
InterPro; IPR002083; MATH/TRAF_dom.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR008974; TRAF-like.
InterPro; IPR024729; USP7_ICP0-binding_dom.
InterPro; IPR029346; USP_C.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00917; MATH; 1.
Pfam; PF00443; UCH; 1.
Pfam; PF14533; USP7_C2; 1.
Pfam; PF12436; USP7_ICP0_bdg; 1.
SMART; SM00061; MATH; 1.
SUPFAM; SSF49599; SSF49599; 1.
PROSITE; PS50144; MATH; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
Acetylation; Chromosome; Complete proteome; Cytoplasm;
Developmental protein; DNA damage; DNA repair; Hydrolase;
Isopeptide bond; Nucleus; Phosphoprotein; Protease;
Reference proteome; Thiol protease; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 1103 Ubiquitin carboxyl-terminal hydrolase 7.
/FTId=PRO_0000268007.
DOMAIN 69 196 MATH. {ECO:0000255|PROSITE-
ProRule:PRU00129}.
DOMAIN 215 522 USP.
REGION 1 209 Interaction with TSPYL5.
{ECO:0000250|UniProtKB:Q93009}.
REGION 54 209 Interaction with p53/TP53 and MDM2.
{ECO:0000250|UniProtKB:Q93009}.
REGION 71 206 Necessary for nuclear localization.
{ECO:0000250|UniProtKB:Q93009}.
COMPBIAS 4 17 Gln-rich.
ACT_SITE 224 224 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093,
ECO:0000269|PubMed:16111684,
ECO:0000269|PubMed:16328052}.
ACT_SITE 465 465 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:Q6A4J8}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000250|UniProtKB:Q6A4J8}.
MOD_RES 870 870 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q93009}.
MOD_RES 964 964 Phosphoserine.
{ECO:0000250|UniProtKB:Q93009}.
MOD_RES 1085 1085 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q93009}.
MOD_RES 1097 1097 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q93009}.
CROSSLNK 870 870 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q93009}.
CROSSLNK 870 870 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q93009}.
CROSSLNK 883 883 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q93009}.
MUTAGEN 224 224 C->S: Loss of p53/TP53-deubiquitinating
activity. {ECO:0000269|PubMed:16111684,
ECO:0000269|PubMed:16328052}.
SEQUENCE 1103 AA; 128431 MW; A542C4149E241C7C CRC64;
MNHQQQQQQQ QKAGEQQLSE PEDMEMEAGD TDDPPRITQN PVINGNVALS DGHSNAEEDM
EDDTSWRSEA TFQFTVERFS RLSESVLSPP CFVRNLPWKI MVMPRFYPDR PHQKSVGFFL
QCNAESDSTS WSCHAQAVLK IINYRDDDKS FSRRISHLFF HKENDWGFSN FMAWSEVTDP
EKGFIDDDKV TFEVFVQADA PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR
KAVYMMPTEG DDSSKSVPLA LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL
CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV SYIQCKEVDY RSDRREDYYD IQLSIKGKKN
IFESFVDYVA VEQLDGDNKY DAGEHGLQEA EKGVKFLTLP PVLHLQLMRF MYDPQTDQNI
KINDRFEFPE QLPLDEFLQK TDPKDPANYI LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK
FDDDVVSRCT KEEAIEHNYG GHDDDLSVRH CTNAYMLVYI RESKLSEVLQ AVTDHDIPQQ
LVERLQEEKR IEAQKRKERQ EAHLYMQVQI VAEDQFCGHQ GNDMYDEEKV RYTVFKVLKN
SSLAEFVQSL SQTMGFPQDQ IRLWPMQARS NGTKRPAMLD NEADGSKTMI ELSDNENPWT
IFLETVDPEL AASGATLPKF DKDHDVMLFL KMYDPKTRSL NYCGHIYTPI SCKIRDLLPV
MCDRAGFIQD TSLILYEEVK PNLTERIQDY DVSLDKALDE LMDGDIIVFQ KDDPENDNSE
LPTAKEYFRD LYHRVDVIFC DKTIPNDPGF VVTLSNRMNY FQVAKTVAQR LNTDPMLLQF
FKSQGYRDGP GNPLRHNYEG TLRDLLQFFK PRQPKKLYYQ QLKMKITDFE NRRSFKCIWL
NSQFREEEIT LYPDKHGCVR DLLEECKKAV ELGDEASGRL RLLEIVSYKI IGVHQEDELL
ECLSPATSRT FRIEEIPLDQ VNIDKENEML ITVAHFHKEV FGTFGIPFLL RIHQGEHFRE
VMKRIQSLLD IQEKEFEKFK FAIVMMGRHQ YINEDEYEVN LKDFEPQPGN MSHPRPWLGL
DHFNKAPKRS RYTYLEKAIK IHN


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