RBM4B_HUMAN
ID RBM4B_HUMAN Reviewed; 359 AA.
AC Q9BQ04; B3KT83;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=RNA-binding protein 4B;
DE AltName: Full=RNA-binding motif protein 30;
DE AltName: Full=RNA-binding motif protein 4B;
DE AltName: Full=RNA-binding protein 30;
GN Name=RBM4B; Synonyms=RBM30;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Substantia nigra;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 PROTEIN SEQUENCE OF 4-11; 80-95; 98-111; 130-139; 183-198 AND 309-336, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP INTERACTION WITH TNPO3, AND TISSUE SPECIFICITY.
RX PubMed=12628928; DOI=10.1093/emboj/cdg126;
RA Lai M.-C., Kuo H.-W., Chang W.-C., Tarn W.-Y.;
RT "A novel splicing regulator shares a nuclear import pathway with SR
RT proteins.";
RL EMBO J. 22:1359-1369(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18708123; DOI=10.1016/j.neulet.2008.08.017;
RA Pfuhl T., Mamiani A., Durr M., Welter S., Stieber J., Ankara J., Liss M.,
RA Dobner T., Schmitt A., Falkai P., Kremmer E., Jung V., Barth S.,
RA Grasser F.A.;
RT "The LARK/RBM4a protein is highly expressed in cerebellum as compared to
RT cerebrum.";
RL Neurosci. Lett. 444:11-15(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP STRUCTURE BY NMR OF 69-155.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second RNA binding domain in RNA-binding protein
RT 30.";
RL Submitted (SEP-2006) to the PDB data bank.
RN [10]
RP VARIANT VAL-93.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Required for the translational activation of PER1 mRNA in
CC response to circadian clock. Binds directly to the 3'-UTR of the PER1
CC mRNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TNPO3, which may mediate nuclear import of the
CC protein. {ECO:0000269|PubMed:12628928}.
CC -!- INTERACTION:
CC Q9BQ04; Q86V38: ATN1; NbExp=3; IntAct=EBI-715531, EBI-11954292;
CC Q9BQ04; Q86Y13: DZIP3; NbExp=4; IntAct=EBI-715531, EBI-948630;
CC Q9BQ04; Q9BUJ2: HNRNPUL1; NbExp=3; IntAct=EBI-715531, EBI-1018153;
CC Q9BQ04; Q13351: KLF1; NbExp=3; IntAct=EBI-715531, EBI-8284732;
CC Q9BQ04; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-715531, EBI-10271199;
CC Q9BQ04; Q8NB12: SMYD1; NbExp=2; IntAct=EBI-715531, EBI-8463848;
CC Q9BQ04; P09012: SNRPA; NbExp=3; IntAct=EBI-715531, EBI-607085;
CC Q9BQ04; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-715531, EBI-10241197;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus.
CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney (at protein level).
CC Ubiquitously expressed. {ECO:0000269|PubMed:12628928,
CC ECO:0000269|PubMed:18708123}.
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DR EMBL; AK095158; BAG52995.1; -; mRNA.
DR EMBL; CH471076; EAW74558.1; -; Genomic_DNA.
DR EMBL; BC003503; AAH03503.1; -; mRNA.
DR EMBL; BC004951; AAH04951.1; -; mRNA.
DR CCDS; CCDS8149.1; -.
DR RefSeq; NP_001273064.1; NM_001286135.1.
DR RefSeq; NP_113680.1; NM_031492.3.
DR RefSeq; XP_011543599.1; XM_011545297.2.
DR RefSeq; XP_016873891.1; XM_017018402.1.
DR PDB; 2DGT; NMR; -; A=75-153.
DR PDBsum; 2DGT; -.
DR AlphaFoldDB; Q9BQ04; -.
DR SMR; Q9BQ04; -.
DR BioGRID; 123760; 240.
DR IntAct; Q9BQ04; 47.
DR MINT; Q9BQ04; -.
DR STRING; 9606.ENSP00000433071; -.
DR iPTMnet; Q9BQ04; -.
DR PhosphoSitePlus; Q9BQ04; -.
DR BioMuta; RBM4B; -.
DR DMDM; 62511129; -.
DR SWISS-2DPAGE; Q9BQ04; -.
DR EPD; Q9BQ04; -.
DR jPOST; Q9BQ04; -.
DR MassIVE; Q9BQ04; -.
DR MaxQB; Q9BQ04; -.
DR PaxDb; Q9BQ04; -.
DR PeptideAtlas; Q9BQ04; -.
DR PRIDE; Q9BQ04; -.
DR ProteomicsDB; 78606; -.
DR Antibodypedia; 16362; 70 antibodies from 21 providers.
DR DNASU; 83759; -.
DR Ensembl; ENST00000310046.9; ENSP00000310471.4; ENSG00000173914.12.
DR Ensembl; ENST00000525754.5; ENSP00000433071.1; ENSG00000173914.12.
DR GeneID; 83759; -.
DR KEGG; hsa:83759; -.
DR MANE-Select; ENST00000310046.9; ENSP00000310471.4; NM_031492.4; NP_113680.1.
DR UCSC; uc001oja.5; human.
DR CTD; 83759; -.
DR GeneCards; RBM4B; -.
DR HGNC; HGNC:28842; RBM4B.
DR HPA; ENSG00000173914; Low tissue specificity.
DR neXtProt; NX_Q9BQ04; -.
DR OpenTargets; ENSG00000173914; -.
DR PharmGKB; PA134977404; -.
DR VEuPathDB; HostDB:ENSG00000173914; -.
DR eggNOG; KOG0109; Eukaryota.
DR GeneTree; ENSGT00940000154421; -.
DR HOGENOM; CLU_045263_0_0_1; -.
DR InParanoid; Q9BQ04; -.
DR OMA; RYEREPY; -.
DR OrthoDB; 1563362at2759; -.
DR PhylomeDB; Q9BQ04; -.
DR TreeFam; TF320661; -.
DR PathwayCommons; Q9BQ04; -.
DR SignaLink; Q9BQ04; -.
DR BioGRID-ORCS; 83759; 20 hits in 1086 CRISPR screens.
DR ChiTaRS; RBM4B; human.
DR EvolutionaryTrace; Q9BQ04; -.
DR GenomeRNAi; 83759; -.
DR Pharos; Q9BQ04; Tdark.
DR PRO; PR:Q9BQ04; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BQ04; protein.
DR Bgee; ENSG00000173914; Expressed in cortical plate and 158 other tissues.
DR ExpressionAtlas; Q9BQ04; baseline and differential.
DR Genevisible; Q9BQ04; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR CDD; cd12606; RRM1_RBM4; 1.
DR CDD; cd12607; RRM2_RBM4; 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; IPR034897; RBM4_RRM1.
DR InterPro; IPR034898; RBM4_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Direct protein sequencing; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..359
FT /note="RNA-binding protein 4B"
FT /id="PRO_0000081787"
FT DOMAIN 2..72
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 78..148
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 160..177
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 196..359
FT /note="Interaction with TNPO3"
FT /evidence="ECO:0000250"
FT VARIANT 93
FT /note="E -> V"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064766"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:2DGT"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:2DGT"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2DGT"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:2DGT"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:2DGT"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2DGT"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:2DGT"
SQ SEQUENCE 359 AA; 40150 MW; C336DF80460BD474 CRC64;
MVKLFIGNLP REATEQEIRS LFEQYGKVLE CDIIKNYGFV HIEDKTAAED AIRNLHHYKL
HGVNINVEAS KNKSKASTKL HVGNISPTCT NQELRAKFEE YGPVIECDIV KDYAFVHMER
AEDAVEAIRG LDNTEFQGKR MHVQLSTSRL RTAPGMGDQS GCYRCGKEGH WSKECPVDRT
GRVADFTEQY NEQYGAVRTP YTMGYGESMY YNDAYGALDY YKRYRVRSYE AVAAAAAASA
YNYAEQTMSH LPQVQSTTVT SHLNSTSVDP YDRHLLPNSG AAATSAAMAA AAATTSSYYG
RDRSPLRRAA AMLPTVGEGY GYGPESELSQ ASAATRNSLY DMARYEREQY VDRARYSAF
