RBM34_MOUSE
ID RBM34_MOUSE Reviewed; 442 AA.
AC Q8C5L7; B2RUP0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=RNA-binding protein 34;
DE AltName: Full=RNA-binding motif protein 34;
GN Name=Rbm34; Synonyms=D8Ertd233e;
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] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [2] {ECO:0000312|EMBL:EDL11822.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAI41279.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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 [4] {ECO:0000312|EMBL:AAI41279.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI41279.1};
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-153, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P42696}.
CC -!- SIMILARITY: Belongs to the RRM RBM34 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37124.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC119874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11822.1; -; Genomic_DNA.
DR EMBL; AK078099; BAC37124.1; ALT_FRAME; mRNA.
DR EMBL; BC141278; AAI41279.1; -; mRNA.
DR CCDS; CCDS22787.1; -.
DR RefSeq; NP_766350.2; NM_172762.2.
DR AlphaFoldDB; Q8C5L7; -.
DR SMR; Q8C5L7; -.
DR BioGRID; 206450; 2.
DR STRING; 10090.ENSMUSP00000048450; -.
DR iPTMnet; Q8C5L7; -.
DR PhosphoSitePlus; Q8C5L7; -.
DR EPD; Q8C5L7; -.
DR jPOST; Q8C5L7; -.
DR MaxQB; Q8C5L7; -.
DR PaxDb; Q8C5L7; -.
DR PeptideAtlas; Q8C5L7; -.
DR PRIDE; Q8C5L7; -.
DR ProteomicsDB; 300266; -.
DR ProteomicsDB; 335327; -.
DR Antibodypedia; 34694; 126 antibodies from 22 providers.
DR DNASU; 52202; -.
DR Ensembl; ENSMUST00000045994; ENSMUSP00000048450; ENSMUSG00000033931.
DR GeneID; 52202; -.
DR KEGG; mmu:52202; -.
DR UCSC; uc009nzb.1; mouse.
DR CTD; 23029; -.
DR MGI; MGI:1098653; Rbm34.
DR VEuPathDB; HostDB:ENSMUSG00000033931; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00390000011249; -.
DR HOGENOM; CLU_050628_0_0_1; -.
DR InParanoid; Q8C5L7; -.
DR OMA; VDHTVVN; -.
DR OrthoDB; 1176212at2759; -.
DR TreeFam; TF313083; -.
DR BioGRID-ORCS; 52202; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q8C5L7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8C5L7; protein.
DR Bgee; ENSMUSG00000033931; Expressed in ear vesicle and 226 other tissues.
DR ExpressionAtlas; Q8C5L7; baseline and differential.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR CDD; cd12394; RRM1_RBM34; 1.
DR CDD; cd12395; RRM2_RBM34; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034220; RBM34_RRM1.
DR InterPro; IPR034221; RBM34_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..442
FT /note="RNA-binding protein 34"
FT /id="PRO_0000081791"
FT DOMAIN 189..284
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 291..368
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..442
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 153
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42696"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P42696"
SQ SEQUENCE 442 AA; 49116 MW; F3EB5612B3A0B520 CRC64;
MALGGEERKR RKGSERRQSS GDGVSCAASD YLVGQVADSL RGGPRPPGGG TGRLAALFST
AEPSAPPVFV PVPQETSKKR KLDDDDDDEE ESVSQTKKPV LQEPSRKVKV KKLSDADKRL
ANRESALASA DLEEELHQDQ GQGRRRRSQS RGKVADGEAL DVALSLAKDG GQRTKIPVNP
EEERLKNERT VFVGNLPVTC NKKKLKSFFK EYGQVESVRF RSVMPAEGTL TKKLAAIKRK
FHPDQKSINA YVVFKDESAA AKALQRNGAQ IAEGFRIRVD LASETASRDK RSVFVGNLPY
KIEDSALEEH FLDCGSIVAV RIVRNPLTGV GRGFGYVLFE NTDAVHLALK LNNSELMGRK
LRVMRSVNKE KLKQQNSNPS LKKDVIKPKQ RLNFTSKEGK FHSKEGKFHS KNAFIGEKAV
LMKKKKKGQK KKVQMKKPRK QQ
