ID   RBM34_RAT               Reviewed;         428 AA.
AC   Q5M9F1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=RNA-binding protein 34;
DE   AltName: Full=RNA-binding motif protein 34;
GN   Name=Rbm34;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P42696}.
CC   -!- SIMILARITY: Belongs to the RRM RBM34 family. {ECO:0000305}.
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DR   EMBL; BC087155; AAH87155.1; -; mRNA.
DR   RefSeq; NP_001014037.1; NM_001014015.1.
DR   AlphaFoldDB; Q5M9F1; -.
DR   SMR; Q5M9F1; -.
DR   STRING; 10116.ENSRNOP00000027145; -.
DR   iPTMnet; Q5M9F1; -.
DR   PhosphoSitePlus; Q5M9F1; -.
DR   PaxDb; Q5M9F1; -.
DR   PRIDE; Q5M9F1; -.
DR   Ensembl; ENSRNOT00000027145; ENSRNOP00000027145; ENSRNOG00000020004.
DR   GeneID; 307956; -.
DR   KEGG; rno:307956; -.
DR   UCSC; RGD:1310161; rat.
DR   CTD; 23029; -.
DR   RGD; 1310161; Rbm34.
DR   eggNOG; KOG0118; Eukaryota.
DR   GeneTree; ENSGT00390000011249; -.
DR   HOGENOM; CLU_050628_0_0_1; -.
DR   InParanoid; Q5M9F1; -.
DR   OMA; VDHTVVN; -.
DR   OrthoDB; 1176212at2759; -.
DR   PhylomeDB; Q5M9F1; -.
DR   TreeFam; TF313083; -.
DR   PRO; PR:Q5M9F1; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000020004; Expressed in thymus and 20 other tissues.
DR   Genevisible; Q5M9F1; RN.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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..428
FT                   /note="RNA-binding protein 34"
FT                   /id="PRO_0000081792"
FT   DOMAIN          183..278
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          285..362
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..428
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         147
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C5L7"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42696"
FT   CROSSLNK        240
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P42696"
SQ   SEQUENCE   428 AA;  47661 MW;  ACC0C28D36B81042 CRC64;
     MALRGEGRKR KKGQERRQSS EDDVGNAATD YLVGQVADSL RGGARPPGGG TGRLAALFST
     PETLAPPVFV PVPQETSKKR KPDDEEETVA HIKKPALQEP ARKVKVKKLS DADKRLANRE
     SALANADLEE IRQDQGQGRR RSQSRGKVTD GEALDVALSL NEDGRQRTKV PLNPEEERLK
     NERTVFVGNL PVTCNKKKLK SFFKEYGQVE SVRFRSVMPA EGTLSKKLAA IKRKFHPDQK
     SINAYVVFKE ERAAAKALQR NGAQIAEGFR IRVDLASETA SRDKRSVFVG NLPYRVDESA
     LEEHFLDCGS IVAVRIVRNP LTGVGRGFGY VLFENTDAVH LALKLNNSEL MGRKLRVMRS
     VNKEKLKQQN SNPSVKKDGS KSKQRLNFTS KEGKSHSKNA FIGEKAVLMK KKKGQKKKGQ
     TKKPRKQK