Sequence of RN169_HUMAN
EC Number:2.3.2.27
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
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
0 MAAAGPSTRA SSAAAAAALS RRGRRGRCDE TAAAKTGAPG PASGPSLLVL SPPLLQPPLP
60 PRPEESGCAG CLEPPGEAAA LPCGHSLCRG CAQRAADAAG PGCPRCRARG PGWARRRARD
120 DGQADSEVLG ECARRSQPER CRPRRDGGAA AAGPRPEQEP RAAPAEPDFI FRAPIKLSKP
180 GELREEYESL RKLREEKLQE EKPSEDQIHK LLPEDTETGK RKMDEQKKRD EPLVLKTNLE
240 RCPARLSDSE NEEPSRGQMT QTHRSAFVSK NNSYSLAFLA GKLNSKVERS QSCSDTAQER
300 AKSRVRAVPG NKAKVTTMTP ASNPIIGVLL STQNNRCVSA PDLTIEKRLP FSSLSSLASL
360 HKPERSVSPE SNDSISEELN HFKPIVCSPC TPPKRLPDGR VLSPLIIKST PRNLNRSLQK
420 QTSYEASPRI LKKWEQIFQE RQIKKTLSKA TLTSLAPEMG EELLGSEGIH SSKEKPLVAV
480 NTRLSGGQVL SEYTGPTSAD LDHFPSVSQT KAEQDSDNKS STEIPLETCC SSELKGGGSG
540 TSLEREQFEG LGSTPDAKLD KTCISRAMKI TTVNSVLPQN SVLGGVLKTK QQLKTLNHFD
600 LTNGVLVESL SEEPLPSLRR GRKRHCKTKH LEQNGSLKKL RQTSGEVGLA PTDPVLREME
660 QKLQQEEEDR QLALQLQRMF DNERRTVSRR KGSVDQYLLR SSNMAGAK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
349983
Ohara O.,Nagase T.,Mitsui G.,Kohga H.,Kikuno R.,Hiraoka S.,Takahashi Y.,Kitajima S.,Saga Y.,Koseki H.
Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method.
DNA Res.
9
47-57
2002
349984
Bechtel S.,Rosenfelder H.,Duda A.,Schmidt C.P.,Ernst U.,Wellenreuther R.,Mehrle A.,Schuster C.,Bahr A.,Bloecker H.,Heubner D.,Hoerlein A.,Michel G.,Wedler H.,Koehrer K.,Ottenwaelder B.,Poustka A.,Wiemann S.,Schupp I.
The full-ORF clone resource of the German cDNA consortium.
BMC Genomics
8
399-399
2007
349985
Daub H.,Olsen J.V.,Bairlein M.,Gnad F.,Oppermann F.S.,Korner R.,Greff Z.,Keri G.,Stemmann O.,Mann M.
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
Mol. Cell
31
438-448
2008
349986
Dephoure N.,Zhou C.,Villen J.,Beausoleil S.A.,Bakalarski C.E.,Elledge S.J.,Gygi S.P.
A quantitative atlas of mitotic phosphorylation.
Proc. Natl. Acad. Sci. U.S.A.
105
10762-10767
2008
349987
Gauci S.,Helbig A.O.,Slijper M.,Krijgsveld J.,Heck A.J.,Mohammed S.
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Anal. Chem.
81
4493-4501
2009
349988
Mayya V.,Lundgren D.H.,Hwang S.-I.,Rezaul K.,Wu L.,Eng J.K.,Rodionov V.,Han D.K.
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
Sci. Signal.
2
0-0
2009
349989
Olsen J.V.,Vermeulen M.,Santamaria A.,Kumar C.,Miller M.L.,Jensen L.J.,Gnad F.,Cox J.,Jensen T.S.,Nigg E.A.,Brunak S.,Mann M.
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
Sci. Signal.
3
0-0
2010
349990
Chen J.,Feng W.,Jiang J.,Deng Y.,Huen M.S.
Ring finger protein RNF169 antagonises the ubiquitin-dependent signaling cascade at sites of DNA Damage.
J. Biol. Chem.
287
27715-27722
2012
349991
Poulsen M.,Lukas C.,Lukas J.,Bekker-Jensen S.,Mailand N.
Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks.
J. Cell Biol.
197
189-199
2012
349992
Panier S.,Ichijima Y.,Fradet-Turcotte A.,Leung C.C.,Kaustov L.,Arrowsmith C.H.,Durocher D.
Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks.
Mol. Cell
47
383-395
2012
349993
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
349994
Bian Y.,Song C.,Cheng K.,Dong M.,Wang F.,Huang J.,Sun D.,Wang L.,Ye M.,Zou H.
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
J. Proteomics
96
253-262
2014
349995
Hendriks I.A.,Lyon D.,Young C.,Jensen L.J.,Vertegaal A.C.,Nielsen M.L.
Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
Nat. Struct. Mol. Biol.
24
325-336
2017
349996
An L.,Dong C.,Li J.,Chen J.,Yuan J.,Huang J.,Chan K.M.,Yu C.H.,Huen M.S.Y.
RNF169 limits 53BP1 deposition at DSBs to stimulate single-strand annealing repair.
Proc. Natl. Acad. Sci. U.S.A.
115
0-0
2018
349997
Menon V.R.,Ananthapadmanabhan V.,Swanson S.,Saini S.,Sesay F.,Yakovlev V.,Florens L.,DeCaprio J.A.,Washburn M.P.,Dozmorov M.,Litovchick L.
DYRK1A regulates the recruitment of 53BP1 to the sites of DNA damage in part through interaction with RNF169.
Cell Cycle
18
531-551
2019
349998
Dong C.,An L.,Yu C.H.,Huen M.S.Y.
A DYRK1B-dependent pathway suppresses rDNA transcription in response to DNA damage.
Nucleic Acids Res.
49
1485-1496
2021
