RBM45_MOUSE
ID RBM45_MOUSE Reviewed; 476 AA.
AC Q8BHN5; Q8C1Z5;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=RNA-binding protein 45;
DE AltName: Full=Developmentally-regulated RNA-binding protein 1;
DE Short=RB-1;
DE AltName: Full=RNA-binding motif protein 45;
GN Name=Rbm45; Synonyms=Drb1 {ECO:0000312|EMBL:BAC16208.1}, Drbp1;
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|EMBL:BAC16208.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:BAC16208.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAC16208.1};
RX PubMed=12220514; DOI=10.1016/s0006-291x(02)02132-0;
RA Tamada H., Sakashita E., Shimazaki K., Ueno E., Hamamoto T., Kagawa Y.,
RA Endo H.;
RT "cDNA cloning and characterization of Drb1, a new member of RRM-type neural
RT RNA-binding protein.";
RL Biochem. Biophys. Res. Commun. 297:96-104(2002).
RN [2] {ECO:0000312|EMBL:AAN41644.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAN41644.1};
RC TISSUE=Embryonic heart {ECO:0000312|EMBL:AAN41644.1};
RA Chen X.G., Li Y.;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ; TISSUE=Blood;
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:0000305, ECO:0000312|EMBL:AAH57890.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI {ECO:0000312|EMBL:AAH57890.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH57890.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
CC -!- FUNCTION: RNA-binding protein with binding specificity for poly(C). May
CC play an important role in neural development (By similarity).
CC {ECO:0000250|UniProtKB:Q8CFD1, ECO:0000250|UniProtKB:Q8IUH3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly cytoplasmic. May shuttle between cytoplasm and
CC nucleus. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41024.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB036992; BAC16208.1; -; mRNA.
DR EMBL; AY152391; AAN41644.1; -; mRNA.
DR EMBL; AK089975; BAC41024.1; ALT_FRAME; mRNA.
DR EMBL; BC057890; AAH57890.1; -; mRNA.
DR CCDS; CCDS16157.1; -.
DR RefSeq; NP_700454.1; NM_153405.2.
DR AlphaFoldDB; Q8BHN5; -.
DR SMR; Q8BHN5; -.
DR STRING; 10090.ENSMUSP00000040420; -.
DR iPTMnet; Q8BHN5; -.
DR PhosphoSitePlus; Q8BHN5; -.
DR EPD; Q8BHN5; -.
DR MaxQB; Q8BHN5; -.
DR PaxDb; Q8BHN5; -.
DR PeptideAtlas; Q8BHN5; -.
DR PRIDE; Q8BHN5; -.
DR ProteomicsDB; 255002; -.
DR Antibodypedia; 19584; 138 antibodies from 23 providers.
DR Ensembl; ENSMUST00000046389; ENSMUSP00000040420; ENSMUSG00000042369.
DR GeneID; 241490; -.
DR KEGG; mmu:241490; -.
DR UCSC; uc008kez.1; mouse.
DR CTD; 129831; -.
DR MGI; MGI:2387367; Rbm45.
DR VEuPathDB; HostDB:ENSMUSG00000042369; -.
DR eggNOG; ENOG502QTJ8; Eukaryota.
DR GeneTree; ENSGT00680000100059; -.
DR HOGENOM; CLU_035274_1_0_1; -.
DR InParanoid; Q8BHN5; -.
DR OMA; ILFHPHP; -.
DR OrthoDB; 673895at2759; -.
DR PhylomeDB; Q8BHN5; -.
DR TreeFam; TF324216; -.
DR BioGRID-ORCS; 241490; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Rbm45; mouse.
DR PRO; PR:Q8BHN5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BHN5; protein.
DR Bgee; ENSMUSG00000042369; Expressed in pineal body and 217 other tissues.
DR Genevisible; Q8BHN5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR CDD; cd12366; RRM1_RBM45; 1.
DR CDD; cd12367; RRM2_RBM45; 1.
DR CDD; cd12368; RRM3_RBM45; 1.
DR CDD; cd12369; RRM4_RBM45; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR033101; RBM45.
DR InterPro; IPR034203; RBM45_RRM1.
DR InterPro; IPR034206; RBM45_RRM2.
DR InterPro; IPR034207; RBM45_RRM3.
DR InterPro; IPR034208; RBM45_RRM4.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10352:SF18; PTHR10352:SF18; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Isopeptide bond;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..476
FT /note="RNA-binding protein 45"
FT /id="PRO_0000081573"
FT DOMAIN 26..106
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 121..192
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 392..464
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH3"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH3"
FT CONFLICT 121
FT /note="T -> S (in Ref. 3; BAC41024)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="E -> K (in Ref. 3; BAC41024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53324 MW; 00A7E233C221653F CRC64;
MDDAGGLGGS GGFRPGVDSL DEPPNSRIFL VISKHTSELV LRERFSPFGD IQDIWVVRDK
HTKESKGVAF VKFARSSQAC RAMEEMHGQC LGPSDTKPIK VFIAQSRSSG SHRDVEDEEL
TRIFVMIPKS YTEEDLREKF KVYGDIEYCS IIKNKVTGES KGLGYVRYLK PSQAAQAIEN
CDRSFRALLA EPKNKVSGSP EQDDYSSGRQ EALGQEPRAN LFPFVGEQQS EFSTFDKNDS
RGQEAVSKRL SVVSRVPFTE EQLFSIFDIV PGLEYCEVPR DPYSNYGHGV VQYFNVASAI
YAKYKLHGFQ YPPGNRIVVS FLDDGSNMTE LIRKMATQMV AAQLASMVWS TTSQQQFLQY
GGNAASQAPQ IQTDVVLPSC KKKAPPETPV KERLFVVFNP HPLPLDVLED IFCRFGNLIE
VYLVSGKNVG YVKYADRKSA NEAITTLHGK ILNGVRLKVM LADSPREESK KRQRTY
