RMI2_MOUSE
ID RMI2_MOUSE Reviewed; 149 AA.
AC Q3UPE3; Q3V2Y5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=RecQ-mediated genome instability protein 2;
GN Name=Rmi2; Synonyms=Gm929;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Spleen, and Thymus;
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).
CC -!- FUNCTION: Essential component of the RMI complex, a complex that plays
CC an important role in the processing of homologous recombination
CC intermediates. It is required to regulate sister chromatid segregation
CC and to limit DNA crossover. Essential for the stability, localization,
CC and function of BLM, TOP3A, and complexes containing BLM. In the RMI
CC complex, it is required to target BLM to chromatin and stress-induced
CC nuclear foci and mitotic phosphorylation of BLM.
CC {ECO:0000250|UniProtKB:Q96E14}.
CC -!- SUBUNIT: Component of the RMI complex, containing at least TOP3A, RMI1
CC and RMI2. The RMI complex interacts with BLM (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with BLM
CC at nuclear DNA repair foci. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UPE3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UPE3-2; Sequence=VSP_027288;
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RMI2 family. {ECO:0000305}.
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DR EMBL; AK080331; BAE43370.1; -; mRNA.
DR EMBL; AK143588; BAE25452.1; -; mRNA.
DR CCDS; CCDS49761.1; -. [Q3UPE3-1]
DR RefSeq; NP_001156404.1; NM_001162932.1. [Q3UPE3-1]
DR AlphaFoldDB; Q3UPE3; -.
DR SMR; Q3UPE3; -.
DR BioGRID; 230218; 1.
DR ComplexPortal; CPX-3303; BTR double Holliday Junction dissolution complex.
DR STRING; 10090.ENSMUSP00000042676; -.
DR PhosphoSitePlus; Q3UPE3; -.
DR EPD; Q3UPE3; -.
DR MaxQB; Q3UPE3; -.
DR PaxDb; Q3UPE3; -.
DR PeptideAtlas; Q3UPE3; -.
DR PRIDE; Q3UPE3; -.
DR ProteomicsDB; 299836; -. [Q3UPE3-1]
DR ProteomicsDB; 299837; -. [Q3UPE3-2]
DR Antibodypedia; 52376; 40 antibodies from 15 providers.
DR Ensembl; ENSMUST00000037913; ENSMUSP00000042676; ENSMUSG00000037991. [Q3UPE3-1]
DR Ensembl; ENSMUST00000181721; ENSMUSP00000137986; ENSMUSG00000037991. [Q3UPE3-2]
DR GeneID; 223970; -.
DR KEGG; mmu:223970; -.
DR UCSC; uc007yek.2; mouse. [Q3UPE3-1]
DR CTD; 116028; -.
DR MGI; MGI:2685383; Rmi2.
DR VEuPathDB; HostDB:ENSMUSG00000037991; -.
DR eggNOG; ENOG502S4AN; Eukaryota.
DR GeneTree; ENSGT00390000001653; -.
DR HOGENOM; CLU_147474_0_0_1; -.
DR InParanoid; Q3UPE3; -.
DR OMA; RVSLVWM; -.
DR OrthoDB; 1604165at2759; -.
DR PhylomeDB; Q3UPE3; -.
DR TreeFam; TF332971; -.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 223970; 5 hits in 74 CRISPR screens.
DR PRO; PR:Q3UPE3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3UPE3; protein.
DR Bgee; ENSMUSG00000037991; Expressed in yolk sac and 49 other tissues.
DR Genevisible; Q3UPE3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0043007; P:maintenance of rDNA; IBA:GO_Central.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0033045; P:regulation of sister chromatid segregation; ISO:MGI.
DR GO; GO:0071139; P:resolution of recombination intermediates; ISO:MGI.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR032245; RMI2.
DR PANTHER; PTHR33962; PTHR33962; 1.
DR Pfam; PF16100; RMI2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA replication; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..149
FT /note="RecQ-mediated genome instability protein 2"
FT /id="PRO_0000297578"
FT DNA_BIND 46..116
FT /note="OB"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96E14"
FT VAR_SEQ 102..149
FT /note="KYVMVMGVVQACSPEPCLQAVKMTDLSDNPVHESMWELEVEDLHRNIP ->
FT FQNLKETTQLKRTLLPASHNMLDLTLLPASYSMLELTYLHHAAC (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027288"
SQ SEQUENCE 149 AA; 15838 MW; 81CEB953ED137291 CRC64;
MAAAASESLS SGGPGAVRLP RLPPLKVLAG QLRRHAEGGP GAWRLSRAAV GRAPLELVAV
WMQGTVLAAE GGQARLRDSS GAFSVRGLER VPRGRPCLLP GKYVMVMGVV QACSPEPCLQ
AVKMTDLSDN PVHESMWELE VEDLHRNIP
