Q6A4J8 (UBP7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 7
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 7
Herpesvirus-associated ubiquitin-specific protease
Short name=mHAUSP
Ubiquitin thioesterase 7
Ubiquitin-specific-processing protease 7

Gene names

Name:	Usp7
Synonyms:	Hausp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1103 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. 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. 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. 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. Involved in cell proliferation during early embryonic development. 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. 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. Exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Ref.1 Ref.5 Ref.6
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	Monomer. Homodimer. 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. 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 UBXN6. 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 By similarity. Interacts with p53/TP53. Interacts with DNMT1 and UHRF1. Ref.1 Ref.6
Subcellular location	Nucleus. Cytoplasm By similarity. Nucleus › PML body By similarity. Note: Present in a minority of ND10 nuclear bodies. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX in speckled structures. Colocalized with PML and PTEN in promyelocytic leukemia protein (PML) nuclear bodies By similarity. Ref.5
Tissue specificity	Expressed at high levels in brain, lung, thymus and testis. Expressed at low levels in the liver. Ref.1
Developmental stage	Expressed in embryo at 3.5 and from 7.5 to 10.5 dpc (at protein level).
Domain	The C-terminus plays a role in its oligomerization By similarity.
Post-translational modification	Phosphorylated at positions Ser-19 and Ser-964 By similarity. Polyneddylated By similarity. Not sumoylated By similarity. Polyubiquitinated. Ubiquitinated at Lys-870 By similarity.
Disruption phenotype	Led to early embryonic lethality. Show disorganized germinal layers without the formation of a proamniotic cavity. Many of the surviving cells were trophoblastic giant cells with large nuclei. Ref.5
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 MATH domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Developmental protein Hydrolase Protease Thiol protease
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW protein deubiquitination Inferred from direct assay Ref.6. Source: UniProtKB regulation of sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB transcription-coupled nucleotide-excision repair Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay PubMed 12093161. Source: MGI nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	cysteine-type endopeptidase activity Inferred from mutant phenotype Ref.6. Source: UniProtKB ubiquitin thiolesterase activity Inferred from direct assay Ref.6. Source: UniProtKB ubiquitin-specific protease activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6A4J8-1)

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.

Isoform 2 (identifier: Q6A4J8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: MNHQQQQQQQQKAGEQQLSEPEDMEME → MASSTSPPRS...CPWNEGIEYQ

Isoform 3 (identifier: Q6A4J8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     974-974: E → ECLQ
     1094-1103: YLEKAIKIHN → LGLC

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1103	1103	Ubiquitin carboxyl-terminal hydrolase 7		PRO_0000268006
Regions
	Domain	69 – 196	128	MATH
	Region	1 – 209	209	Interaction with TSPYL5 By similarity
	Region	54 – 209	156	Interaction with p53/TP53 and MDM2 By similarity
	Region	71 – 206	136	Necessary for nuclear localization By similarity
	Compositional bias	4 – 17	14	Gln-rich
Sites
	Active site	224	1	Nucleophile By similarity
	Active site	465	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	19	1	Phosphoserine Ref.4
	Modified residue	870	1	N6-acetyllysine By similarity
	Modified residue	964	1	Phosphoserine By similarity
	Modified residue	1085	1	N6-acetyllysine By similarity
	Modified residue	1097	1	N6-acetyllysine By similarity
	Cross-link	870		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Natural variations
	Alternative sequence	1 – 27	27	MNHQQ…DMEME → MASSTSPPRSPSGGILTQDT IYFPQSNIISELLPWYLRYT PPEVPSTSVITKFILVNCPW NEGIEYQ in isoform 2.		VSP_021952
	Alternative sequence	974	1	E → ECLQ in isoform 3.		VSP_021953
	Alternative sequence	1094 – 1103	10	YLEKAIKIHN → LGLC in isoform 3.		VSP_021954
Experimental info
	Mutagenesis	224	1	C → S: Loss of p53/TP53-deubiquitinating activity. Ref.1 Ref.6
	Sequence conflict	162	1	E → K in BAE22671. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 989DFE733F0D961E	FASTA	1,103	128,475
	10 20 30 40 50 60 MNHQQQQQQQ QKAGEQQLSE PEDMEMEAGD TDDPPRITQN PVINGNVTLS DGHSNAEEDM 70 80 90 100 110 120 EDDTSWRSEA TFQFTVERFS RLSESVLSPP CFVRNLPWKI MVMPRFYPDR PHQKSVGFFL 130 140 150 160 170 180 QCNAESDSTS WSCHAQAVLK IINYRDDDKS FSRRISHLFF HEENDWGFSN FMAWSEVTDP 190 200 210 220 230 240 EKGFIDDDKV TFEVFVQADA PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR 250 260 270 280 290 300 KAVYMMPTEG DDSSKSVPLA LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL 310 320 330 340 350 360 CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV SYIQCKDVDY RSDRREDYYD IQLSIKGKKN 370 380 390 400 410 420 IFESFVDYVA VEQLDGDNKY DAGEHGLQEA EKGVKFLTLP PVLHLQLMRF MYDPQTDQNI 430 440 450 460 470 480 KINDRFEFPE QLPLDEFLQK TDPKDPANYI LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK 490 500 510 520 530 540 FDDDVVSRCT KEEAIEHNYG GHDDDLSVRH CTNAYMLVYI RESKLSEVLQ AVTDHDIPQQ 550 560 570 580 590 600 LVERLQEEKR IEAQKRKERQ EAHLYMQVQI VAEDQFCGHQ GNDMYDEEKV RYTVFKVLKN 610 620 630 640 650 660 SSLAEFVQSL SQTMGFPQDQ IRLWPMQARS NGTKRPAMLD NEADGNKTMI ELSDNENPWT 670 680 690 700 710 720 IFLETVDPEL AASGATLPKF DKDHDVMLFL KMYDPKTRSL NYCGHIYTPI SCKIRDLLPV 730 740 750 760 770 780 MCDRAGFIQD TSLILYEEVK PNLTERIQDY DVSLDKALDE LMDGDIIVFQ KDDPENDNSE 790 800 810 820 830 840 LPTAKEYFRD LYHRVDVIFC DKTIPNDPGF VVTLSNRMNY FQVAKTVAQR LNTDPMLLQF 850 860 870 880 890 900 FKSQGYRDGP GNPLRHNYEG TLRDLLQFFK PRQPKKLYYQ QLKMKITDFE NRRSFKCIWL 910 920 930 940 950 960 NSQFREEEIT LYPDKHGCVR DLLEECKKAV ELGDKASGRL RLLEIVSYKI IGVHQEDELL 970 980 990 1000 1010 1020 ECLSPATSRT FRIEEIPLDQ VDIDKENEML ITVAHFHKEV FGTFGIPFLL RIHQGEHFRE 1030 1040 1050 1060 1070 1080 VMKRIQSLLD IQEKEFEKFK FAIVMMGRHQ YINEDEYEVN LKDFEPQPGN MSHPRPWLGL 1090 1100 DHFNKAPKRS RYTYLEKAIK IHN
	Isoform 2 [UniParc]. Checksum: 38F6764A2D063600	FASTA	1,143	132,749
	10 20 30 40 50 60 MASSTSPPRS PSGGILTQDT IYFPQSNIIS ELLPWYLRYT PPEVPSTSVI TKFILVNCPW 70 80 90 100 110 120 NEGIEYQAGD TDDPPRITQN PVINGNVTLS DGHSNAEEDM EDDTSWRSEA TFQFTVERFS 130 140 150 160 170 180 RLSESVLSPP CFVRNLPWKI MVMPRFYPDR PHQKSVGFFL QCNAESDSTS WSCHAQAVLK 190 200 210 220 230 240 IINYRDDDKS FSRRISHLFF HEENDWGFSN FMAWSEVTDP EKGFIDDDKV TFEVFVQADA 250 260 270 280 290 300 PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR KAVYMMPTEG DDSSKSVPLA 310 320 330 340 350 360 LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL CRVLLDNVEN KMKGTCVEGT 370 380 390 400 410 420 IPKLFRGKMV SYIQCKDVDY RSDRREDYYD IQLSIKGKKN IFESFVDYVA VEQLDGDNKY 430 440 450 460 470 480 DAGEHGLQEA EKGVKFLTLP PVLHLQLMRF MYDPQTDQNI KINDRFEFPE QLPLDEFLQK 490 500 510 520 530 540 TDPKDPANYI LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK FDDDVVSRCT KEEAIEHNYG 550 560 570 580 590 600 GHDDDLSVRH CTNAYMLVYI RESKLSEVLQ AVTDHDIPQQ LVERLQEEKR IEAQKRKERQ 610 620 630 640 650 660 EAHLYMQVQI VAEDQFCGHQ GNDMYDEEKV RYTVFKVLKN SSLAEFVQSL SQTMGFPQDQ 670 680 690 700 710 720 IRLWPMQARS NGTKRPAMLD NEADGNKTMI ELSDNENPWT IFLETVDPEL AASGATLPKF 730 740 750 760 770 780 DKDHDVMLFL KMYDPKTRSL NYCGHIYTPI SCKIRDLLPV MCDRAGFIQD TSLILYEEVK 790 800 810 820 830 840 PNLTERIQDY DVSLDKALDE LMDGDIIVFQ KDDPENDNSE LPTAKEYFRD LYHRVDVIFC 850 860 870 880 890 900 DKTIPNDPGF VVTLSNRMNY FQVAKTVAQR LNTDPMLLQF FKSQGYRDGP GNPLRHNYEG 910 920 930 940 950 960 TLRDLLQFFK PRQPKKLYYQ QLKMKITDFE NRRSFKCIWL NSQFREEEIT LYPDKHGCVR 970 980 990 1000 1010 1020 DLLEECKKAV ELGDKASGRL RLLEIVSYKI IGVHQEDELL ECLSPATSRT FRIEEIPLDQ 1030 1040 1050 1060 1070 1080 VDIDKENEML ITVAHFHKEV FGTFGIPFLL RIHQGEHFRE VMKRIQSLLD IQEKEFEKFK 1090 1100 1110 1120 1130 1140 FAIVMMGRHQ YINEDEYEVN LKDFEPQPGN MSHPRPWLGL DHFNKAPKRS RYTYLEKAIK IHN
	Isoform 3 [UniParc]. Checksum: 3E5FE589370B8006	FASTA	1,100	127,996
	10 20 30 40 50 60 MNHQQQQQQQ QKAGEQQLSE PEDMEMEAGD TDDPPRITQN PVINGNVTLS DGHSNAEEDM 70 80 90 100 110 120 EDDTSWRSEA TFQFTVERFS RLSESVLSPP CFVRNLPWKI MVMPRFYPDR PHQKSVGFFL 130 140 150 160 170 180 QCNAESDSTS WSCHAQAVLK IINYRDDDKS FSRRISHLFF HEENDWGFSN FMAWSEVTDP 190 200 210 220 230 240 EKGFIDDDKV TFEVFVQADA PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR 250 260 270 280 290 300 KAVYMMPTEG DDSSKSVPLA LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL 310 320 330 340 350 360 CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV SYIQCKDVDY RSDRREDYYD IQLSIKGKKN 370 380 390 400 410 420 IFESFVDYVA VEQLDGDNKY DAGEHGLQEA EKGVKFLTLP PVLHLQLMRF MYDPQTDQNI 430 440 450 460 470 480 KINDRFEFPE QLPLDEFLQK TDPKDPANYI LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK 490 500 510 520 530 540 FDDDVVSRCT KEEAIEHNYG GHDDDLSVRH CTNAYMLVYI RESKLSEVLQ AVTDHDIPQQ 550 560 570 580 590 600 LVERLQEEKR IEAQKRKERQ EAHLYMQVQI VAEDQFCGHQ GNDMYDEEKV RYTVFKVLKN 610 620 630 640 650 660 SSLAEFVQSL SQTMGFPQDQ IRLWPMQARS NGTKRPAMLD NEADGNKTMI ELSDNENPWT 670 680 690 700 710 720 IFLETVDPEL AASGATLPKF DKDHDVMLFL KMYDPKTRSL NYCGHIYTPI SCKIRDLLPV 730 740 750 760 770 780 MCDRAGFIQD TSLILYEEVK PNLTERIQDY DVSLDKALDE LMDGDIIVFQ KDDPENDNSE 790 800 810 820 830 840 LPTAKEYFRD LYHRVDVIFC DKTIPNDPGF VVTLSNRMNY FQVAKTVAQR LNTDPMLLQF 850 860 870 880 890 900 FKSQGYRDGP GNPLRHNYEG TLRDLLQFFK PRQPKKLYYQ QLKMKITDFE NRRSFKCIWL 910 920 930 940 950 960 NSQFREEEIT LYPDKHGCVR DLLEECKKAV ELGDKASGRL RLLEIVSYKI IGVHQEDELL 970 980 990 1000 1010 1020 ECLSPATSRT FRIECLQEIP LDQVDIDKEN EMLITVAHFH KEVFGTFGIP FLLRIHQGEH 1030 1040 1050 1060 1070 1080 FREVMKRIQS LLDIQEKEFE KFKFAIVMMG RHQYINEDEY EVNLKDFEPQ PGNMSHPRPW 1090 1100 LGLDHFNKAP KRSRYTLGLC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of murine mHAUSP encoding a deubiquitinating enzyme that regulates the status of p53 ubiquitination." Lim S.-K., Shin J.-M., Kim Y.-S., Baek K.-H. Int. J. Oncol. 24:357-364(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TP53, MUTAGENESIS OF CYS-224.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-545 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 832-1103. Strain: C57BL/6J. Tissue: Egg and Stomach.
[3]	"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] OF 214-1103 (ISOFORM 3). Strain: C57BL/6. Tissue: Brain.
[4]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, MASS SPECTROMETRY. Tissue: Macrophage.
[5]	"Inactivation of HAUSP in vivo modulates p53 function." Kon N., Kobayashi Y., Li M., Brooks C.L., Ludwig T., Gu W. Oncogene 29:1270-1279(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[6]	"Usp7 and Uhrf1 control ubiquitination and stability of the maintenance DNA methyltransferase Dnmt1." Qin W., Leonhardt H., Spada F. J. Cell. Biochem. 112:439-444(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DNMT1 AND UHRF1, MUTAGENESIS OF CYS-224.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF548565 mRNA. Translation: AAQ12339.1. AK075830 mRNA. Translation: BAC35992.1. AK135814 mRNA. Translation: BAE22671.1. BC100666 mRNA. Translation: AAI00667.1.
IPI	IPI00463367. IPI00817018. IPI00969838.
RefSeq	NP_001003918.2. NM_001003918.2.
UniGene	Mm.295330.
3D structure databases
HSSP	HSSP built from PDB template 1NBF based on UniProtKB Q93009.
ProteinModelPortal	Q6A4J8.
SMR	Q6A4J8. Positions 64-555, 561-1084.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38603N.
IntAct	Q6A4J8. 1 interaction.
Protein family/group databases
MEROPS	C19.016.
PTM databases
PhosphoSite	Q6A4J8.
Proteomic databases
PaxDb	Q6A4J8.
PRIDE	Q6A4J8.
Protocols and materials databases
DNASU	252870.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	252870.
KEGG	mmu:252870.
UCSC	uc007ycw.1. mouse. uc007ycx.1. mouse.
Organism-specific databases
CTD	7874.
MGI	MGI:2182061. Usp7.
Phylogenomic databases
eggNOG	COG5077.
HOGENOM	HOG000160240.
HOVERGEN	HBG018029.
KO	K11838.
OrthoDB	EOG4640B4.
Gene expression databases
CleanEx	MM_USP7.
Genevestigator	Q6A4J8.
Family and domain databases
InterPro	IPR002083. MATH. IPR024729. Pept_C19_dom. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR008974. TRAF-like. [Graphical view]
Pfam	PF00917. MATH. 1 hit. PF00443. UCH. 1 hit. PF12436. USP7. 1 hit. [Graphical view]
SMART	SM00061. MATH. 1 hit. [Graphical view]
SUPFAM	SSF49599. Traf_like. 1 hit.
PROSITE	PS50144. MATH. 1 hit. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	USP7. mouse.
NextBio	387363.
SOURCE	Search...

Entry information

Entry name

UBP7_MOUSE

Accession

Primary (citable) accession number: Q6A4J8
Secondary accession number(s): Q3UX92, Q496Y5, Q8BW01

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	September 13, 2004
Last modified:	April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program