Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q6A4J8

- UBP7_MOUSE

UniProt

Q6A4J8 - UBP7_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin carboxyl-terminal hydrolase 7

Gene

Usp7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei224 – 2241NucleophilePROSITE-ProRule annotation
Active sitei465 – 4651Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. ubiquitin-specific protease activity Source: UniProtKB
  3. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. multicellular organismal development Source: UniProtKB-KW
  2. protein deubiquitination Source: UniProtKB
  3. regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  4. transcription-coupled nucleotide-excision repair Source: UniProtKB
  5. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Thiol protease

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.016.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Usp7
Synonyms:Hausp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:2182061. Usp7.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm By similarity. NucleusPML 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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi224 – 2241C → S: Loss of p53/TP53-deubiquitinating activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11031103Ubiquitin carboxyl-terminal hydrolase 7PRO_0000268006Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei870 – 8701N6-acetyllysine; alternateBy similarity
Cross-linki870 – 870Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei964 – 9641PhosphoserineBy similarity
Modified residuei1085 – 10851N6-acetyllysineBy similarity
Modified residuei1097 – 10971N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated at positions Ser-19 and Ser-964.By similarity
Polyneddylated.By similarity
Not sumoylated.By similarity
Polyubiquitinated. Ubiquitinated at Lys-870 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ6A4J8.
PaxDbiQ6A4J8.
PRIDEiQ6A4J8.

PTM databases

PhosphoSiteiQ6A4J8.

Expressioni

Tissue specificityi

Expressed at high levels in brain, lung, thymus and testis. Expressed at low levels in the liver.1 Publication

Developmental stagei

Expressed in embryo at 3.5 and from 7.5 to 10.5 dpc (at protein level).

Gene expression databases

CleanExiMM_USP7.
GenevestigatoriQ6A4J8.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi232963. 4 interactions.
DIPiDIP-38603N.
IntActiQ6A4J8. 2 interactions.
MINTiMINT-4139284.

Structurei

3D structure databases

ProteinModelPortaliQ6A4J8.
SMRiQ6A4J8. Positions 64-1084.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 196128MATHPROSITE-ProRule annotationAdd
BLAST
Domaini215 – 522308USPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 209209Interaction with TSPYL5By similarityAdd
BLAST
Regioni54 – 209156Interaction with p53/TP53 and MDM2By similarityAdd
BLAST
Regioni71 – 206136Necessary for nuclear localizationBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 1714Gln-richAdd
BLAST

Domaini

The C-terminus plays a role in its oligomerization.By similarity

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 MATH domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiCOG5077.
HOGENOMiHOG000160240.
HOVERGENiHBG018029.
InParanoidiQ6A4J8.
KOiK11838.
PhylomeDBiQ6A4J8.

Family and domain databases

InterProiIPR002083. MATH.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR008974. TRAF-like.
IPR028889. UCH/PAN2.
IPR024729. USP7_ICP0-binding_dom.
IPR029346. USP_C.
[Graphical view]
PfamiPF00917. MATH. 1 hit.
PF00443. UCH. 1 hit.
PF14533. USP7_C2. 1 hit.
PF12436. USP7_ICP0_bdg. 1 hit.
[Graphical view]
SMARTiSM00061. MATH. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS50144. MATH. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6A4J8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNHQQQQQQQ QKAGEQQLSE PEDMEMEAGD TDDPPRITQN PVINGNVTLS
60 70 80 90 100
DGHSNAEEDM EDDTSWRSEA TFQFTVERFS RLSESVLSPP CFVRNLPWKI
110 120 130 140 150
MVMPRFYPDR PHQKSVGFFL QCNAESDSTS WSCHAQAVLK IINYRDDDKS
160 170 180 190 200
FSRRISHLFF HEENDWGFSN FMAWSEVTDP EKGFIDDDKV TFEVFVQADA
210 220 230 240 250
PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR KAVYMMPTEG
260 270 280 290 300
DDSSKSVPLA LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL
310 320 330 340 350
CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV SYIQCKDVDY RSDRREDYYD
360 370 380 390 400
IQLSIKGKKN IFESFVDYVA VEQLDGDNKY DAGEHGLQEA EKGVKFLTLP
410 420 430 440 450
PVLHLQLMRF MYDPQTDQNI KINDRFEFPE QLPLDEFLQK TDPKDPANYI
460 470 480 490 500
LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK FDDDVVSRCT KEEAIEHNYG
510 520 530 540 550
GHDDDLSVRH CTNAYMLVYI RESKLSEVLQ AVTDHDIPQQ LVERLQEEKR
560 570 580 590 600
IEAQKRKERQ EAHLYMQVQI VAEDQFCGHQ GNDMYDEEKV RYTVFKVLKN
610 620 630 640 650
SSLAEFVQSL SQTMGFPQDQ IRLWPMQARS NGTKRPAMLD NEADGNKTMI
660 670 680 690 700
ELSDNENPWT IFLETVDPEL AASGATLPKF DKDHDVMLFL KMYDPKTRSL
710 720 730 740 750
NYCGHIYTPI SCKIRDLLPV MCDRAGFIQD TSLILYEEVK PNLTERIQDY
760 770 780 790 800
DVSLDKALDE LMDGDIIVFQ KDDPENDNSE LPTAKEYFRD LYHRVDVIFC
810 820 830 840 850
DKTIPNDPGF VVTLSNRMNY FQVAKTVAQR LNTDPMLLQF FKSQGYRDGP
860 870 880 890 900
GNPLRHNYEG TLRDLLQFFK PRQPKKLYYQ QLKMKITDFE NRRSFKCIWL
910 920 930 940 950
NSQFREEEIT LYPDKHGCVR DLLEECKKAV ELGDKASGRL RLLEIVSYKI
960 970 980 990 1000
IGVHQEDELL ECLSPATSRT FRIEEIPLDQ VDIDKENEML ITVAHFHKEV
1010 1020 1030 1040 1050
FGTFGIPFLL RIHQGEHFRE VMKRIQSLLD IQEKEFEKFK FAIVMMGRHQ
1060 1070 1080 1090 1100
YINEDEYEVN LKDFEPQPGN MSHPRPWLGL DHFNKAPKRS RYTYLEKAIK

IHN
Length:1,103
Mass (Da):128,475
Last modified:September 13, 2004 - v1
Checksum:i989DFE733F0D961E
GO
Isoform 2 (identifier: Q6A4J8-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,143
Mass (Da):132,749
Checksum:i38F6764A2D063600
GO
Isoform 3 (identifier: Q6A4J8-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,100
Mass (Da):127,996
Checksum:i3E5FE589370B8006
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621E → K in BAE22671. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2727MNHQQ…DMEME → MASSTSPPRSPSGGILTQDT IYFPQSNIISELLPWYLRYT PPEVPSTSVITKFILVNCPW NEGIEYQ in isoform 2. 1 PublicationVSP_021952Add
BLAST
Alternative sequencei974 – 9741E → ECLQ in isoform 3. 1 PublicationVSP_021953
Alternative sequencei1094 – 110310YLEKAIKIHN → LGLC in isoform 3. 1 PublicationVSP_021954

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF548565 mRNA. Translation: AAQ12339.1.
AK075830 mRNA. Translation: BAC35992.1.
AK135814 mRNA. Translation: BAE22671.1.
BC100666 mRNA. Translation: AAI00667.1.
CCDSiCCDS49755.1. [Q6A4J8-1]
RefSeqiNP_001003918.2. NM_001003918.2.
UniGeneiMm.295330.

Genome annotation databases

GeneIDi252870.
KEGGimmu:252870.
UCSCiuc007ycx.1. mouse. [Q6A4J8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF548565 mRNA. Translation: AAQ12339.1 .
AK075830 mRNA. Translation: BAC35992.1 .
AK135814 mRNA. Translation: BAE22671.1 .
BC100666 mRNA. Translation: AAI00667.1 .
CCDSi CCDS49755.1. [Q6A4J8-1 ]
RefSeqi NP_001003918.2. NM_001003918.2.
UniGenei Mm.295330.

3D structure databases

ProteinModelPortali Q6A4J8.
SMRi Q6A4J8. Positions 64-1084.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 232963. 4 interactions.
DIPi DIP-38603N.
IntActi Q6A4J8. 2 interactions.
MINTi MINT-4139284.

Protein family/group databases

MEROPSi C19.016.

PTM databases

PhosphoSitei Q6A4J8.

Proteomic databases

MaxQBi Q6A4J8.
PaxDbi Q6A4J8.
PRIDEi Q6A4J8.

Protocols and materials databases

DNASUi 252870.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 252870.
KEGGi mmu:252870.
UCSCi uc007ycx.1. mouse. [Q6A4J8-1 ]

Organism-specific databases

CTDi 7874.
MGIi MGI:2182061. Usp7.

Phylogenomic databases

eggNOGi COG5077.
HOGENOMi HOG000160240.
HOVERGENi HBG018029.
InParanoidi Q6A4J8.
KOi K11838.
PhylomeDBi Q6A4J8.

Miscellaneous databases

ChiTaRSi Usp7. mouse.
NextBioi 387363.
PROi Q6A4J8.
SOURCEi Search...

Gene expression databases

CleanExi MM_USP7.
Genevestigatori Q6A4J8.

Family and domain databases

InterProi IPR002083. MATH.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR008974. TRAF-like.
IPR028889. UCH/PAN2.
IPR024729. USP7_ICP0-binding_dom.
IPR029346. USP_C.
[Graphical view ]
Pfami PF00917. MATH. 1 hit.
PF00443. UCH. 1 hit.
PF14533. USP7_C2. 1 hit.
PF12436. USP7_ICP0_bdg. 1 hit.
[Graphical view ]
SMARTi SM00061. MATH. 1 hit.
[Graphical view ]
SUPFAMi SSF49599. SSF49599. 1 hit.
PROSITEi PS50144. MATH. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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.

Entry informationi

Entry nameiUBP7_MOUSE
AccessioniPrimary (citable) accession number: Q6A4J8
Secondary accession number(s): Q3UX92, Q496Y5, Q8BW01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: September 13, 2004
Last modified: November 26, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3