RBM7_MOUSE
ID RBM7_MOUSE Reviewed; 265 AA.
AC Q9CQT2; Q3UB91; Q7TQE3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=RNA-binding protein 7 {ECO:0000305};
DE AltName: Full=RNA-binding motif protein 7 {ECO:0000312|MGI:MGI:1914260};
GN Name=Rbm7 {ECO:0000312|MGI:MGI:1914260};
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Guo T.B., Kato M.V., Boros L.G., Chan K.C., Sinha Hikim A.P., Hudson A.P.,
RA Swerdloff R.S., Mitchell A.P., Lin R.-J., Salameh W.A.;
RT "RNA binding motif protein 7, a novel ubiquitous protein involved in pre-
RT mRNA processing during male meiosis.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, Stomach, and Testis;
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-136,
RP MUTAGENESIS OF SER-136, SUBCELLULAR LOCATION, AND INTERACTION WITH ZCCHC8.
RX PubMed=25525152; DOI=10.1261/rna.048090.114;
RA Tiedje C., Lubas M., Tehrani M., Menon M.B., Ronkina N., Rousseau S.,
RA Cohen P., Kotlyarov A., Gaestel M.;
RT "p38MAPK/MK2-mediated phosphorylation of RBM7 regulates the human nuclear
RT exosome targeting complex.";
RL RNA 21:262-278(2015).
CC -!- FUNCTION: RNA-binding subunit of the trimeric nuclear exosome targeting
CC (NEXT) complex, a complex that functions as an RNA exosome cofactor
CC that directs a subset of non-coding short-lived RNAs for exosomal
CC degradation. NEXT is involved in surveillance and turnover of aberrant
CC transcripts and non-coding RNAs. Binds preferentially polyuridine
CC sequences and associates with newly synthesized RNAs, including pre-
CC mRNAs and short-lived exosome substrates such as promoter upstream
CC transcripts (PROMPTs), enhancer RNAs (eRNAs), and 3'-extended products
CC from small nuclear RNAs (snRNAs). Participates in several biological
CC processes including DNA damage response (DDR) and stress response.
CC During stress response, activation of the p38MAPK-MK2 pathway decreases
CC RBM7-RNA-binding and subsequently the RNA exosome degradation
CC activities, thereby modulating the turnover of non-coding
CC transcriptome. Participates in DNA damage response (DDR), through its
CC interaction with MEPCE and LARP7, the core subunits of 7SK snRNP
CC complex, that release the positive transcription elongation factor b
CC (P-TEFb) complex from the 7SK snRNP. In turn, activation of P-TEFb
CC complex induces the transcription of P-TEFb-dependent DDR genes to
CC promote cell viability. {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- SUBUNIT: Component of the nuclear exosome targeting (NEXT) complex
CC composed of MTREX, ZCCHC8, and RBM7 that directs a subset of non-coding
CC short-lived RNAs for exosomal degradation (PubMed:25525152). Interacts
CC with ZCCHC8 and SF3B2/SAP145. Binds to MTREX through ZCCHC8. Interacts
CC with YWHAE and YWHAZ; these interactions are stress-dependent and RBM7
CC phosphorylation dependent; release RNA from the NEXT complex and may
CC affect RNA targeting to the nuclear RNA exosomome for degradation.
CC Interacts with MEPCE and LARP7, the core subunits of 7SK snRNP; upon
CC genotoxic stress this interaction is enhanced, triggering the release
CC of inactive P-TEFb complex from the core and P-TEFb complex activation
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y580,
CC ECO:0000269|PubMed:25525152}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9Y580}. Nucleus {ECO:0000269|PubMed:25525152}.
CC Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- DOMAIN: The RRM domain mediates RNA binding; the RNA must have four
CC nucleotides for efficient binding. Mediates the interaction of NEXT
CC complex with promoter upstream transcripts (PROMPTs) and potentially
CC aberrant forms of other non coding RNAs, such as snRNAs. The RRM domain
CC exhibits specificity for polyuridine sequences.
CC {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- PTM: Phosphorylated at Ser-136 by MAPK14/p38-alpha-activated
CC MAPKAPK2/MK2; this phosphorylation is stress-dependent; this
CC phosphorylation decreases its RNA-binding capacity therefore affecting
CC RNA nuclear exosome-mediated degradation (PubMed:25525152). This
CC phosphorylation mediates YWHAE and YWHAZ interactions (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y580, ECO:0000269|PubMed:25525152}.
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DR EMBL; AF458961; AAL60585.1; -; mRNA.
DR EMBL; AK005200; BAB23878.1; -; mRNA.
DR EMBL; AK006755; BAB24729.1; -; mRNA.
DR EMBL; AK008645; BAB25804.1; -; mRNA.
DR EMBL; AK151056; BAE30073.1; -; mRNA.
DR EMBL; BC054774; AAH54774.1; -; mRNA.
DR CCDS; CCDS23155.1; -.
DR RefSeq; NP_659197.2; NM_144948.5.
DR AlphaFoldDB; Q9CQT2; -.
DR BioGRID; 211873; 1.
DR IntAct; Q9CQT2; 1.
DR STRING; 10090.ENSMUSP00000126374; -.
DR iPTMnet; Q9CQT2; -.
DR PhosphoSitePlus; Q9CQT2; -.
DR EPD; Q9CQT2; -.
DR jPOST; Q9CQT2; -.
DR MaxQB; Q9CQT2; -.
DR PaxDb; Q9CQT2; -.
DR PRIDE; Q9CQT2; -.
DR ProteomicsDB; 253182; -.
DR DNASU; 67010; -.
DR Ensembl; ENSMUST00000170000; ENSMUSP00000126374; ENSMUSG00000042396.
DR GeneID; 67010; -.
DR KEGG; mmu:67010; -.
DR UCSC; uc009pic.2; mouse.
DR CTD; 10179; -.
DR MGI; MGI:1914260; Rbm7.
DR VEuPathDB; HostDB:ENSMUSG00000042396; -.
DR eggNOG; KOG4454; Eukaryota.
DR GeneTree; ENSGT00870000136493; -.
DR HOGENOM; CLU_087967_0_0_1; -.
DR InParanoid; Q9CQT2; -.
DR OMA; SHDYDSR; -.
DR OrthoDB; 1298240at2759; -.
DR PhylomeDB; Q9CQT2; -.
DR TreeFam; TF323596; -.
DR BioGRID-ORCS; 67010; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Rbm7; mouse.
DR PRO; PR:Q9CQT2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CQT2; protein.
DR Bgee; ENSMUSG00000042396; Expressed in humerus cartilage element and 250 other tissues.
DR ExpressionAtlas; Q9CQT2; baseline and differential.
DR Genevisible; Q9CQT2; MM.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0017069; F:snRNA binding; ISO:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0016076; P:snRNA catabolic process; ISO:MGI.
DR CDD; cd12592; RRM_RBM7; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034500; RBM7_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Meiosis; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT CHAIN 2..265
FT /note="RNA-binding protein 7"
FT /id="PRO_0000081762"
FT DOMAIN 10..87
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 25..35
FT /note="ZCCHC8 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT REGION 59..76
FT /note="ZCCHC8 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT REGION 91..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT MOD_RES 136
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000269|PubMed:25525152"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 152
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT MUTAGEN 136
FT /note="S->A: Does not phosphorylated by MAPK14/p38-alpha-
FT activated MAPKAPK2/MK2. Does not affect localization. Does
FT not affect interaction with ZCCHC8."
FT /evidence="ECO:0000269|PubMed:25525152"
FT CONFLICT 240
FT /note="N -> D (in Ref. 3; AAH54774)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 265 AA; 30148 MW; 5D99650FD1FBF0C8 CRC64;
MGAAAAEADR TLFVGNLETK VTEELLFELF HQAGPVIKVK IPKDKDGKLK QFAFVNFKHE
VSVPYAMNLL NGIKLFGRPI KIQFRSGSSH ASQDASVSYP QHHVGNLSPT STSPNSYERT
VGNVSPTAQM VQRSFSSPED YQRQAVMNSV FRQMSYAGKF GSPHADQLGF SPSAQPHGHT
FNQSSSSQWR QDALSSQRKR QNSHPYLADR HYSREQRYSD HGSDYHYRGS REDFYYDDRN
HDGWSHDYDN RRDSSRGGKW PSSRH
