Any feedback?
Please rate this page
(sequences.php)
(0/150)

BRENDA support

Sequence of UHRF1_MOUSE

EC Number:2.3.2.27

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
RING-type E3 ubiquitin transferase
Q8VDF2
Mus musculus
782
88304
Reaction
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
Other sequences found for EC No. 2.3.2.27

General information:

Sequence
show sequence in fasta format
  0 MWIQVRTMDG KETHTVNSLS RLTKVQELRK KIEEVFHVEP QLQRLFYRGK QMEDGHTLFD
 60 YDVRLNDTIQ LLVRQSLALP LSTKERDSEL SDSDSGYGVG HSESDKSSTH GEGAAEADDK
120 TVWEDTDLGL YKVNEYVDVR DNIFGAWFEA QVVQVQKRAL SEDEPCSSSA VKTSEDDIMY
180 HVKYDDYPEH GVDIVKAKNV RARARTVIPW ENLEVGQVVM ANYNVDYPRK RGFWYDVEIC
240 RKRQTRTARE LYGNIRLLND SQLNNCRIMF VDEVLMIELP KERRPLIASP SQPPPALRNT
300 GKSGPSCRFC KDDENKPCRK CACHVCGGRE APEKQLLCDE CDMAFHLYCL KPPLTSVPPE
360 PEWYCPSCRT DSSEVVQAGE KLKESKKKAK MASATSSSRR DWGKGMACVG RTTECTIVPA
420 NHFGPIPGVP VGTMWRFRVQ VSESGVHRPH VAGIHGRSND GAYSLVLAGG YEDDVDNGNY
480 FTYTGSGGRD LSGNKRTAGQ SSDQKLTNNN RALALNCHSP INEKGAEAED WRQGKPVRVV
540 RNMKGGKHSK YAPAEGNRYD GIYKVVKYWP ERGKSGFLVW RYLLRRDDTE PEPWTREGKD
600 RTRQLGLTMQ YPEGYLEALA NKEKSRKRPA KALEQGPSSS KTGKSKQKST GPTLSSPRAS
660 KKSKLEPYTL SEQQANLIKE DKGNAKLWDD VLTSLQDGPY QIFLSKVKEA FQCICCQELV
720 FRPVTTVCQH NVCKDCLDRS FRAQVFSCPA CRFELDHSSP TRVNQPLQTI LNQLFPGYGS
780 GR
Download this sequence
in fasta format
Download all sequences for 2.3.2.27
in fasta format
in csv (Excel, OpenOffice) format
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
247215
Fujimori A.,Matsuda Y.,Takemoto Y.,Hashimoto Y.,Kubo E.,Araki R.,Fukumura R.,Mita K.,Tatsumi K.,Muto M.
Cloning and mapping of Np95 gene which encodes a novel nuclear protein associated with cell proliferation.
Mamm. Genome
9
1032-1035
1998
247217
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.
The transcriptional landscape of the mammalian genome.
Science
309
1559-1563
2005
247218
Church D.M.,Goodstadt L.,Hillier L.W.,Zody M.C.,Goldstein S.,She X.,Bult C.J.,Agarwala R.,Cherry J.L.,DiCuccio M.,Hlavina W.,Kapustin Y.,Meric P.,Maglott D.,Birtle Z.,Marques A.C.,Graves T.,Zhou S.,Teague B.,Potamousis K.,Churas C.,Place M.,Herschleb J.,Runnheim R.,Forrest D.,Amos-Landgraf J.,Schwartz D.C.,Cheng Z.,Lindblad-Toh K.,Eichler E.E.,Ponting C.P.
Lineage-specific biology revealed by a finished genome assembly of the mouse.
PLoS Biol.
7
0-0
2009
247219
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
247220
Muto M.,Kanari Y.,Kubo E.,Takabe T.,Kurihara T.,Fujimori A.,Tatsumi K.
Targeted disruption of Np95 gene renders murine embryonic stem cells hypersensitive to DNA damaging agents and DNA replication blocks.
J. Biol. Chem.
277
34549-34555
2002
247221
Muto M.,Utsuyama M.,Horiguchi T.,Kubo E.,Sado T.,Hirokawa K.
The characterization of the monoclonal antibody Th-10a, specific for a nuclear protein appearing in the S phase of the cell cycle in normal thymocytes and its unregulated expression in lymphoma cell lines.
Cell Prolif.
28
645-657
1995
247222
Uemura T.,Kubo E.,Kanari Y.,Ikemura T.,Tatsumi K.,Muto M.
Temporal and spatial localization of novel nuclear protein NP95 in mitotic and meiotic cells.
Cell Struct. Funct.
25
149-159
2000
247223
Miura M.,Watanabe H.,Sasaki T.,Tatsumi K.,Muto M.
Dynamic changes in subnuclear NP95 location during the cell cycle and its spatial relationship with DNA replication foci.
Exp. Cell Res.
263
202-208
2001
247224
Bonapace I.M.,Latella L.,Papait R.,Nicassio F.,Sacco A.,Muto M.,Crescenzi M.,Di Fiore P.P.
Np95 is regulated by E1A during mitotic reactivation of terminally differentiated cells and is essential for S phase entry.
J. Cell Biol.
157
909-914
2002
247225
Citterio E.,Papait R.,Nicassio F.,Vecchi M.,Gomiero P.,Mantovani R.,Di Fiore P.P.,Bonapace I.M.
Np95 is a histone-binding protein endowed with ubiquitin ligase activity.
Mol. Cell. Biol.
24
2526-2535
2004
247226
Unoki M.,Nishidate T.,Nakamura Y.
ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain.
Oncogene
23
7601-7610
2004
247227
Sharif J.,Muto M.,Takebayashi S.,Suetake I.,Iwamatsu A.,Endo T.A.,Shinga J.,Mizutani-Koseki Y.,Toyoda T.,Okamura K.,Tajima S.,Mitsuya K.,Okano M.,Koseki H.
The SRA protein Np95 mediates epigenetic inheritance by recruiting Dnmt1 to methylated DNA.
Nature
450
908-912
2007
247228
Bostick M.,Kim J.K.,Esteve P.O.,Clark A.,Pradhan S.,Jacobsen S.E.
UHRF1 plays a role in maintaining DNA methylation in mammalian cells.
Science
317
1760-1764
2007
247229
Meilinger D.,Fellinger K.,Bultmann S.,Rothbauer U.,Bonapace I.M.,Klinkert W.E.,Spada F.,Leonhardt H.
Np95 interacts with de novo DNA methyltransferases, Dnmt3a and Dnmt3b, and mediates epigenetic silencing of the viral CMV promoter in embryonic stem cells.
EMBO Rep.
10
1259-1264
2009
247230
Trost M.,English L.,Lemieux S.,Courcelles M.,Desjardins M.,Thibault P.
The phagosomal proteome in interferon-gamma-activated macrophages.
Immunity
30
143-154
2009
247231
Kim J.K.,Esteve P.O.,Jacobsen S.E.,Pradhan S.
UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells.
Nucleic Acids Res.
37
493-505
2009
247232
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
247233
Rottach A.,Frauer C.,Pichler G.,Bonapace I.M.,Spada F.,Leonhardt H.
The multi-domain protein Np95 connects DNA methylation and histone modification.
Nucleic Acids Res.
38
1796-1804
2010
247234
Nady N.,Lemak A.,Walker J.R.,Avvakumov G.V.,Kareta M.S.,Achour M.,Xue S.,Duan S.,Allali-Hassani A.,Zuo X.,Wang Y.X.,Bronner C.,Chedin F.,Arrowsmith C.H.,Dhe-Paganon S.
Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein.
J. Biol. Chem.
286
24300-24311
2011
247235
Qin W.,Leonhardt H.,Spada F.
Usp7 and Uhrf1 control ubiquitination and stability of the maintenance DNA methyltransferase Dnmt1.
J. Cell. Biochem.
112
439-444
2011
247236
Graf U.,Casanova E.A.,Wyck S.,Dalcher D.,Gatti M.,Vollenweider E.,Okoniewski M.J.,Weber F.A.,Patel S.S.,Schmid M.W.,Li J.,Sharif J.,Wanner G.A.,Koseki H.,Wong J.,Pelczar P.,Penengo L.,Santoro R.,Cinelli P.
Pramel7 mediates ground-state pluripotency through proteasomal-epigenetic combined pathways.
Nat. Cell Biol.
19
763-773
2017
247237
Arita K.,Ariyoshi M.,Tochio H.,Nakamura Y.,Shirakawa M.
Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism.
Nature
455
818-821
2008
247238
Hashimoto H.,Horton J.R.,Zhang X.,Bostick M.,Jacobsen S.E.,Cheng X.
The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix.
Nature
455
826-829
2008
247239
Hashimoto H.,Horton J.R.,Zhang X.,Cheng X.
UHRF1, a modular multi-domain protein, regulates replication-coupled crosstalk between DNA methylation and histone modifications.
Epigenetics
4
8-14
2009