MRNIP_MOUSE
ID MRNIP_MOUSE Reviewed; 335 AA.
AC Q9D1F5; Q9CX85;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=MRN complex-interacting protein {ECO:0000312|MGI:MGI:1915317};
DE AltName: Full=MRN-interacting protein {ECO:0000250|UniProtKB:Q6NTE8};
GN Name=Mrnip {ECO:0000312|MGI:MGI:1915317};
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 STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
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=Mammary gland;
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).
CC -!- FUNCTION: Plays a role in the cellular response to DNA damage and the
CC maintenance of genome stability through its association with the MRN
CC damage-sensing complex. Promotes chromatin loading and activity of the
CC MRN complex to facilitate subsequent ATM-mediated DNA damage response
CC signaling and DNA repair. {ECO:0000250|UniProtKB:Q6NTE8}.
CC -!- SUBUNIT: Associates with the MRE11-RAD50-NBN (MRN) damage-sensing
CC complex; this association is constitutive. Interacts with MRE11.
CC Interacts with NBN. Interacts with RAD50.
CC {ECO:0000250|UniProtKB:Q6NTE8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6NTE8}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q6NTE8}. Note=Recruited to sites of
CC DNA damage. Phosphorylation induces its nuclear localization and
CC promotes genome stability. {ECO:0000250|UniProtKB:Q6NTE8}.
CC -!- PTM: Phosphorylated; phosphorylation is constitutive and occurs in the
CC absence of any DNA-damaging stimulus. Phosphorylation is necessary for
CC its nuclear retention. {ECO:0000250|UniProtKB:Q6NTE8}.
CC -!- SIMILARITY: Belongs to the MRNIP family. {ECO:0000305}.
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DR EMBL; AK003636; BAB22904.1; -; mRNA.
DR EMBL; AK019392; BAB31698.1; -; mRNA.
DR EMBL; AL627187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028428; AAH28428.1; -; mRNA.
DR CCDS; CCDS48784.1; -.
DR RefSeq; NP_080819.2; NM_026543.3.
DR AlphaFoldDB; Q9D1F5; -.
DR STRING; 10090.ENSMUSP00000020647; -.
DR iPTMnet; Q9D1F5; -.
DR PhosphoSitePlus; Q9D1F5; -.
DR EPD; Q9D1F5; -.
DR jPOST; Q9D1F5; -.
DR MaxQB; Q9D1F5; -.
DR PaxDb; Q9D1F5; -.
DR PeptideAtlas; Q9D1F5; -.
DR PRIDE; Q9D1F5; -.
DR ProteomicsDB; 290319; -.
DR Antibodypedia; 62814; 108 antibodies from 13 providers.
DR Ensembl; ENSMUST00000020647; ENSMUSP00000020647; ENSMUSG00000020381.
DR GeneID; 68067; -.
DR KEGG; mmu:68067; -.
DR UCSC; uc007irv.2; mouse.
DR CTD; 51149; -.
DR MGI; MGI:1915317; Mrnip.
DR VEuPathDB; HostDB:ENSMUSG00000020381; -.
DR eggNOG; ENOG502S8YD; Eukaryota.
DR GeneTree; ENSGT00390000006124; -.
DR HOGENOM; CLU_068693_0_0_1; -.
DR InParanoid; Q9D1F5; -.
DR OMA; FPRWKLP; -.
DR OrthoDB; 1146272at2759; -.
DR PhylomeDB; Q9D1F5; -.
DR TreeFam; TF333430; -.
DR BioGRID-ORCS; 68067; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Mrnip; mouse.
DR PRO; PR:Q9D1F5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D1F5; protein.
DR Bgee; ENSMUSG00000020381; Expressed in animal zygote and 143 other tissues.
DR ExpressionAtlas; Q9D1F5; baseline and differential.
DR Genevisible; Q9D1F5; MM.
DR GO; GO:0030870; C:Mre11 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR InterPro; IPR032739; MRNIP.
DR PANTHER; PTHR15863; PTHR15863; 1.
DR Pfam; PF15749; MRNIP; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..335
FT /note="MRN complex-interacting protein"
FT /id="PRO_0000326120"
FT REGION 75..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..230
FT /note="Necessary for the association with the MRN complex"
FT /evidence="ECO:0000250|UniProtKB:Q6NTE8"
FT REGION 273..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 145..148
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000250|UniProtKB:Q6NTE8"
FT COMPBIAS 127..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NTE8"
FT CONFLICT 294
FT /note="E -> G (in Ref. 2; BAB31698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 36897 MW; 4F24FDA35BEB6070 CRC64;
MAPAQQSRVL RCCSCHIFQA HQVKKSLKWT CKACGEKQSF VRAYGEGSGA DCRRHVQKLN
LLQGQVSELS LRSVEEAVNG SEEENAGPLQ AEAGSQQAPS KPLESRWLKY LDKGCEDQEL
DRGRPALKTQ LSTSAERPSS PAQPRKRKWN QRTGQPAHSL HGQGVDSVED NFEHQDSTGL
FGTEQQGTSP ALSTANHTRE LGFPRWKLPS PVTQVNAPSS KWARFLLAPG NSPQVDEKPS
PLQEATMLAD LAQGTVENKT PVEGHFSRAP AIRPPQAIHT TTPQLDRPDR KTREQPRDMG
TPRADGRPLA QGTQKAPPLQ LHNLFTTGED FDDDL
