RBM42_MOUSE
ID RBM42_MOUSE Reviewed; 478 AA.
AC Q91V81; Q3UBE0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=RNA-binding protein 42;
DE AltName: Full=RNA-binding motif protein 42;
GN Name=Rbm42;
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=Bone marrow;
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 MRNA].
RC STRAIN=129, and FVB/N; TISSUE=Mammary tumor;
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 [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19170760; DOI=10.1111/j.1365-2443.2008.01256.x;
RA Fukuda T., Naiki T., Saito M., Irie K.;
RT "hnRNP K interacts with RNA binding motif protein 42 and functions in the
RT maintenance of cellular ATP level during stress conditions.";
RL Genes Cells 14:113-128(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Binds (via the RRM domain) to the 3'-untranslated region
CC (UTR) of CDKN1A mRNA. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HNRNPK. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19170760}. Cytoplasm
CC {ECO:0000269|PubMed:19170760}. Note=Upon stress response, localizes
CC with HNRNPK in cytoplasmic aggregates of stalled translational
CC preinitiation complexes called stress granules.
CC -!- TISSUE SPECIFICITY: Expressed in cell lines (at protein level).
CC Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney
CC and testis. {ECO:0000269|PubMed:19170760}.
CC -!- SIMILARITY: Belongs to the RRM RBM42 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09148.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH11286.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH27372.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH57928.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK151000; BAE30024.1; -; mRNA.
DR EMBL; BC009148; AAH09148.1; ALT_INIT; mRNA.
DR EMBL; BC011286; AAH11286.1; ALT_INIT; mRNA.
DR EMBL; BC027372; AAH27372.1; ALT_INIT; mRNA.
DR EMBL; BC057928; AAH57928.1; ALT_INIT; mRNA.
DR CCDS; CCDS52179.1; -.
DR RefSeq; NP_598454.2; NM_133693.2.
DR AlphaFoldDB; Q91V81; -.
DR SMR; Q91V81; -.
DR STRING; 10090.ENSMUSP00000040005; -.
DR iPTMnet; Q91V81; -.
DR PhosphoSitePlus; Q91V81; -.
DR EPD; Q91V81; -.
DR MaxQB; Q91V81; -.
DR PaxDb; Q91V81; -.
DR PeptideAtlas; Q91V81; -.
DR PRIDE; Q91V81; -.
DR ProteomicsDB; 255000; -.
DR Antibodypedia; 29473; 145 antibodies from 24 providers.
DR Ensembl; ENSMUST00000042726; ENSMUSP00000040005; ENSMUSG00000036733.
DR GeneID; 68035; -.
DR KEGG; mmu:68035; -.
DR UCSC; uc009gfp.1; mouse.
DR CTD; 79171; -.
DR MGI; MGI:1915285; Rbm42.
DR VEuPathDB; HostDB:ENSMUSG00000036733; -.
DR eggNOG; KOG0226; Eukaryota.
DR GeneTree; ENSGT00930000151055; -.
DR InParanoid; Q91V81; -.
DR OMA; RMPMMRG; -.
DR OrthoDB; 1249623at2759; -.
DR TreeFam; TF313946; -.
DR BioGRID-ORCS; 68035; 15 hits in 71 CRISPR screens.
DR ChiTaRS; Rbm42; mouse.
DR PRO; PR:Q91V81; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q91V81; protein.
DR Bgee; ENSMUSG00000036733; Expressed in granulocyte and 63 other tissues.
DR ExpressionAtlas; Q91V81; baseline and differential.
DR Genevisible; Q91V81; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR CDD; cd12383; RRM_RBM42; 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; IPR034215; RBM42_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; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..478
FT /note="RNA-binding protein 42"
FT /id="PRO_0000307751"
FT DOMAIN 379..457
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..478
FT /note="Necessary for interaction with HNRNPK"
FT /evidence="ECO:0000250"
FT REGION 317..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 151
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT MOD_RES 156
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT MOD_RES 166
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT MOD_RES 179
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT CONFLICT 310
FT /note="L -> M (in Ref. 1; BAE30024)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="K -> E (in Ref. 1; BAE30024)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="D -> N (in Ref. 1; BAE30024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 50236 MW; 717C54B0CF47F51F CRC64;
MASAMAGAGP APGLPVAGGP VVPGPGVGIP GKSGEERLKE MEAEMALFEQ EVLGAPVTGI
PTAVPAVPTV EAMQVPPAPV IRPIIATNTY QQVQQTLEAR AAAAATVVPP MVGGPPFVGP
VGFGPADRGH LDSPEAREAM FLRRAAVAPQ RAPILRPAFV PHVLQRADSA LSSAAGGPRP
MALRPPHQAL VGPPLPGPPG PPMMLPPMAR APGPPLGSMA ALRPPLEEPA APRELGLGLG
LGLKDKEEAV VAAAAGLEEA SAAVAVGAGG APAGPAVIGP SLPLALAMPL PEPEPLPLPL
EVVRGLLPPL RIPELLSLRP RPRPPRPEPP PGLMALEVPE PLGEDKKKGK PEKLKRCIRT
AAGSSWEDPS LLEWDADDFR IFCGDLGNEV NDDILARAFS RFPSFLKAKV IRDKRTGKTK
GYGFVSFKDP SDYVRAMREM NGKYVGSRPI KLRKSMWKDR NLDVVRKKQK EKKKLGLR
