RB15B_MOUSE
ID RB15B_MOUSE Reviewed; 887 AA.
AC Q6PHZ5; Q8C6G2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Putative RNA-binding protein 15B;
DE AltName: Full=RNA-binding motif protein 15B;
GN Name=Rbm15b;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-887.
RC TISSUE=Embryo;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 343-887.
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-111 AND SER-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Pancreas, 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).
RN [5]
RP STRUCTURE BY NMR OF 404-487.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA recognition motif from hypothetical RNA
RT binding protein BC052180.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein that acts as a key regulator of N6-
CC methyladenosine (m6A) methylation of RNAs, thereby regulating different
CC processes, such as alternative splicing of mRNAs and X chromosome
CC inactivation mediated by Xist RNA. Associated component of the WMM
CC complex, a complex that mediates N6-methyladenosine (m6A) methylation
CC of RNAs, a modification that plays a role in the efficiency of mRNA
CC splicing and RNA processing. Plays a key role in m6A methylation,
CC possibly by binding target RNAs and recruiting the WMM complex.
CC Involved in random X inactivation mediated by Xist RNA: acts by binding
CC Xist RNA and recruiting the WMM complex, which mediates m6A
CC methylation, leading to target YTHDC1 reader on Xist RNA and promoting
CC transcription repression activity of Xist. Functions in the regulation
CC of alternative or illicit splicing, possibly by regulating m6A
CC methylation. Inhibits pre-mRNA splicing. Also functions as a mRNA
CC export factor by acting as a cofactor for the nuclear export receptor
CC NXF1. {ECO:0000250|UniProtKB:Q8NDT2}.
CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex
CC composed of a catalytic subcomplex, named MAC, and of an associated
CC subcomplex, named MACOM. The MAC subcomplex is composed of METTL3 and
CC METTL14. The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI,
CC VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B). May interact with
CC NCOR2. Interacts with NXF1, the interaction is required to promote mRNA
CC export. {ECO:0000250|UniProtKB:Q8NDT2}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q8NDT2}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q8NDT2}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q8NDT2}. Note=Colocalizes with BMLF1 in the
CC nucleus. Localized in the nucleoplasm with a granular staining pattern
CC and excluded from the nucleoli. {ECO:0000250|UniProtKB:Q8NDT2}.
CC -!- SIMILARITY: Belongs to the RRM Spen family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52180.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAC35951.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC147636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052180; AAH52180.1; ALT_SEQ; mRNA.
DR EMBL; AK075777; BAC35951.1; ALT_INIT; mRNA.
DR CCDS; CCDS52915.1; -.
DR RefSeq; NP_780611.3; NM_175402.4.
DR PDB; 1WHY; NMR; -; A=404-487.
DR PDBsum; 1WHY; -.
DR AlphaFoldDB; Q6PHZ5; -.
DR SMR; Q6PHZ5; -.
DR BioGRID; 224554; 3.
DR STRING; 10090.ENSMUSP00000059330; -.
DR iPTMnet; Q6PHZ5; -.
DR PhosphoSitePlus; Q6PHZ5; -.
DR EPD; Q6PHZ5; -.
DR jPOST; Q6PHZ5; -.
DR MaxQB; Q6PHZ5; -.
DR PaxDb; Q6PHZ5; -.
DR PeptideAtlas; Q6PHZ5; -.
DR PRIDE; Q6PHZ5; -.
DR ProteomicsDB; 300309; -.
DR Antibodypedia; 59712; 58 antibodies from 18 providers.
DR DNASU; 109095; -.
DR Ensembl; ENSMUST00000055843; ENSMUSP00000059330; ENSMUSG00000074102.
DR GeneID; 109095; -.
DR KEGG; mmu:109095; -.
DR UCSC; uc012gzz.1; mouse.
DR CTD; 29890; -.
DR MGI; MGI:1923598; Rbm15b.
DR VEuPathDB; HostDB:ENSMUSG00000074102; -.
DR eggNOG; KOG0112; Eukaryota.
DR GeneTree; ENSGT00940000160561; -.
DR HOGENOM; CLU_012724_1_0_1; -.
DR InParanoid; Q6PHZ5; -.
DR OMA; NFAYIQY; -.
DR OrthoDB; 367857at2759; -.
DR PhylomeDB; Q6PHZ5; -.
DR TreeFam; TF354224; -.
DR BioGRID-ORCS; 109095; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Rbm15b; mouse.
DR EvolutionaryTrace; Q6PHZ5; -.
DR PRO; PR:Q6PHZ5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6PHZ5; protein.
DR Bgee; ENSMUSG00000074102; Expressed in ventricular zone and 235 other tissues.
DR ExpressionAtlas; Q6PHZ5; baseline and differential.
DR Genevisible; Q6PHZ5; MM.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12554; RRM1_RBM15B; 1.
DR CDD; cd12556; RRM2_RBM15B; 1.
DR CDD; cd12558; RRM3_RBM15B; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034475; RBM15B_RRM1.
DR InterPro; IPR034535; RBM15B_RRM2.
DR InterPro; IPR034536; RBM15B_RRM3.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR010912; SPOC_met.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF07744; SPOC; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
DR PROSITE; PS50917; SPOC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..887
FT /note="Putative RNA-binding protein 15B"
FT /id="PRO_0000081779"
FT DOMAIN 136..216
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 333..410
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 414..488
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 708..886
FT /note="SPOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00249"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..887
FT /note="Interaction with Epstein-Barr virus BMLF1"
FT /evidence="ECO:0000250"
FT MOTIF 590..594
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 19..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDT2"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDT2"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDT2"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDT2"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDT2"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NDT2"
FT CROSSLNK 699
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NDT2"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:1WHY"
FT HELIX 427..435
FT /evidence="ECO:0007829|PDB:1WHY"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:1WHY"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:1WHY"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:1WHY"
FT HELIX 459..469
FT /evidence="ECO:0007829|PDB:1WHY"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:1WHY"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:1WHY"
SQ SEQUENCE 887 AA; 97076 MW; F9DFCA06595C5DCC CRC64;
MKRQSERDSS PSGRGSSSSA KRPREREREA EAGGRRAAHK ASGGTKHPVP ARARDKPRGS
GGGGGHRDGR AAGDANHRAS GGRSSGAPGG GGRTGKASGD PGAGGASPRA SPLPPPPPPP
GAEPAGPGST AAPEYKTLLI SSLSPALPAE HLEDRLFHQF KRFGEISLRL SHTPELGRVA
YVNFRHPQDA REARQHALAR QLLLYDRPLK VEPVYLRGGG SSRRSSSSSA AASTPPPGPP
APADPLGYLP LHGGYQYKQR SLSPVAAPPL REPRARHAAA AFALDAAAAA AVGLSRERAL
DYYGLYDDRG RPYGYQAVCE EDLMPEDDQR ATRNLFIGNL DHSVSEVELR RAFEKYGIIE
EVVIKRPARG QGGAYAFLKF QNLDMAHRAK VAMSGRVIGR NPIKIGYGKA NPTTRLWVGG
LGPNTSLAAL AREFDRFGSI RTIDHVKGDS FAYIQYESLD AAQAACAKMR GFPLGGPDRR
LRVDFAKAEE TRYPQQYQPS PLPVHYELLT DGYTRHRNLD ADLRVRDRTP PHLLYSDRDR
TFLEGDWTSL SKSSDRRNSL EGYSRSVRSR SGERWGGDGD RSIAKPWEER RKRRSLSSDR
GRTTHSPYEE RSRTKGGGQQ SERGSDRTPE RSRKENHSSE GTKESGSNSL SNSRHGAEER
SHHHHHHEAP DSSHGKKTRE SERNHRTTEA EPKTLEEPKH ETKKLKTLSE YAQTLQLGWN
GLLVLKNSCF PTSMHILEGD QGVISGLLKD HPSGSKLTQL KIAQRLRLDQ PKLDEVTRRI
KQGSPNGYAV LLAIQSTPSG PGAEGMPVVE PGLQRRLLRN LVSYLKQKQA AGVISLPVGG
SKGRDNTGML YAFPPCDFSQ QYLQSALRTL GKLEEEHMVI VIVRDTA
