EME1_MOUSE
ID EME1_MOUSE Reviewed; 570 AA.
AC Q8BJW7;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Crossover junction endonuclease EME1;
DE EC=3.1.22.-;
GN Name=Eme1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, INTERACTION WITH MUS81, AND TISSUE SPECIFICITY.
RX PubMed=14609959; DOI=10.1093/emboj/cdg580;
RA Abraham J., Lemmers B., Hande M.P., Moynahan M.E., Chahwan C., Ciccia A.,
RA Essers J., Hanada K., Chahwan R., Khaw A.K., McPherson P., Shehabeldin A.,
RA Laister R., Arrowsmith C., Kanaar R., West S.C., Jasin M., Hakem R.;
RT "Eme1 is involved in DNA damage processing and maintenance of genomic
RT stability in mammalian cells.";
RL EMBO J. 22:6137-6147(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=27010503; DOI=10.1371/journal.pone.0152278;
RA Braun J., Meixner A., Brachner A., Foisner R.;
RT "The GIY-YIG type endonuclease ankyrin repeat and LEM domain-containing
RT protein 1 (ANKLE1) is dispensable for mouse hematopoiesis.";
RL PLoS ONE 11:E0152278-E0152278(2016).
CC -!- FUNCTION: Interacts with MUS81 to form a DNA structure-specific
CC endonuclease with substrate preference for branched DNA structures with
CC a 5'-end at the branch nick. Typical substrates include 3'-flap
CC structures, replication forks and nicked Holliday junctions. May be
CC required in mitosis for the processing of stalled or collapsed
CC replication forks. {ECO:0000269|PubMed:14609959}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: May self-associate (By similarity). Interacts with MUS81.
CC {ECO:0000250, ECO:0000269|PubMed:14609959}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Recruited to regions of
CC DNA damage in S-phase cells. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in brain, heart, kidney, liver,
CC lung, muscle, skin, small intestine, spleen, stomach, testis and thymus
CC (PubMed:14609959, PubMed:27010503). Expressed in bone marrow
CC (PubMed:27010503). Also expressed in embryonic stem cells (ES cells)
CC (PubMed:14609959). {ECO:0000269|PubMed:14609959,
CC ECO:0000269|PubMed:27010503}.
CC -!- SIMILARITY: Belongs to the EME1/MMS4 family. {ECO:0000305}.
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DR EMBL; AK078516; BAC37318.1; -; mRNA.
DR EMBL; AL645764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089459; AAH89459.1; -; mRNA.
DR CCDS; CCDS25262.1; -.
DR RefSeq; NP_808420.1; NM_177752.4.
DR AlphaFoldDB; Q8BJW7; -.
DR SMR; Q8BJW7; -.
DR BioGRID; 234502; 5.
DR ComplexPortal; CPX-585; Deoxyribonuclease complex MUS81-EME1.
DR STRING; 10090.ENSMUSP00000036361; -.
DR iPTMnet; Q8BJW7; -.
DR PhosphoSitePlus; Q8BJW7; -.
DR EPD; Q8BJW7; -.
DR jPOST; Q8BJW7; -.
DR MaxQB; Q8BJW7; -.
DR PaxDb; Q8BJW7; -.
DR PeptideAtlas; Q8BJW7; -.
DR PRIDE; Q8BJW7; -.
DR ProteomicsDB; 277585; -.
DR Antibodypedia; 4245; 231 antibodies from 31 providers.
DR DNASU; 268465; -.
DR Ensembl; ENSMUST00000039949; ENSMUSP00000036361; ENSMUSG00000039055.
DR GeneID; 268465; -.
DR KEGG; mmu:268465; -.
DR UCSC; uc007kzf.1; mouse.
DR CTD; 146956; -.
DR MGI; MGI:3576783; Eme1.
DR VEuPathDB; HostDB:ENSMUSG00000039055; -.
DR eggNOG; ENOG502R8ER; Eukaryota.
DR GeneTree; ENSGT00530000063937; -.
DR HOGENOM; CLU_034099_2_0_1; -.
DR InParanoid; Q8BJW7; -.
DR OMA; FCVESDW; -.
DR OrthoDB; 1595761at2759; -.
DR PhylomeDB; Q8BJW7; -.
DR TreeFam; TF325310; -.
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 268465; 21 hits in 110 CRISPR screens.
DR ChiTaRS; Eme1; mouse.
DR PRO; PR:Q8BJW7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BJW7; protein.
DR Bgee; ENSMUSG00000039055; Expressed in exoccipital bone and 148 other tissues.
DR Genevisible; Q8BJW7; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:1905347; C:endodeoxyribonuclease complex; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR GO; GO:0043596; C:nuclear replication fork; IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; ISO:MGI.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0031297; P:replication fork processing; ISO:MGI.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; ISO:MGI.
DR Gene3D; 1.10.150.670; -; 1.
DR Gene3D; 3.40.1620.30; -; 1.
DR Gene3D; 4.10.800.30; -; 1.
DR InterPro; IPR042530; EME1/EME2_C.
DR InterPro; IPR043086; EME1_nucdom_sub1.
DR InterPro; IPR043087; Eme1_nucdom_sub2.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR033310; Mms4/EME1/EME2.
DR PANTHER; PTHR21077; PTHR21077; 1.
DR Pfam; PF02732; ERCC4; 1.
DR SMART; SM00891; ERCC4; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Isopeptide bond; Magnesium; Metal-binding; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..570
FT /note="Crossover junction endonuclease EME1"
FT /id="PRO_0000223631"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT CROSSLNK 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
SQ SEQUENCE 570 AA; 63481 MW; F1FC9B68AD1A76A0 CRC64;
MALRRLSLSR LSTESDSEDL PTFAFLKKEP SSTNRKPPQR AKNIVVVTSD SEASCPPSPG
LKGPPCVPSA AGAPPQAGPV RVLSSSSEDE DVFVPLAERI TCKLLTSKQL CPELSSSSLK
TGLDGQNNAS APCDWKRQPW PKIPDVPLHG ALEKSAANDE DSLLDDQCRQ LPTYQATCRE
LAVSKTNSDR PLPKKRTKHI QTVQSGGSQG CWRPGQASRK ENTPRQHERK KKAEMIKRLK
AQRPEECLKH IVVVLDPVLL QMEGGGQLLG ALQAMECSCV IEVQAIPRSI TWRRRRTELV
EDGDDWMEEP TILVLVLAEV FMSMAYNLKQ ASPSSTEKGK ETLRSFVTDV TAKTGKALSL
VIVDQEKCFR PQNPPRRRKS GMANKQAKAK HQQRQESSTG LMVSRADMEK ALVDLQLYTE
AQAWMVQSWK ELADFTCAFT KAVAEAPFKK LRDQVTFSFF LEKDWAGGMK VDQSGRGLAL
IWRRQIQQLN RVSSEMASAI VDAYPSPQLL VQAYQRCFSE QERQNLLADI QVRRGEGVTA
TSRRVGPELS RRIYLQMTTA QPDLILDSVD
