RBM22_MOUSE
ID RBM22_MOUSE Reviewed; 420 AA.
AC Q8BHS3; Q3TJB0; Q9CXA0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Pre-mRNA-splicing factor RBM22;
DE AltName: Full=RNA-binding motif protein 22;
GN Name=Rbm22;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Heart, Lung, and Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, 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 -!- FUNCTION: Required for pre-mRNA splicing as component of the activated
CC spliceosome. Involved in the first step of pre-mRNA splicing. Binds
CC directly to the internal stem-loop (ISL) domain of the U6 snRNA and to
CC the pre-mRNA intron near the 5' splice site during the activation and
CC catalytic phases of the spliceosome cycle. Involved in both
CC translocations of the nuclear SLU7 to the cytoplasm and the cytosolic
CC calcium-binding protein PDCD6 to the nucleus upon cellular stress
CC responses. {ECO:0000250|UniProtKB:Q9NW64}.
CC -!- SUBUNIT: Component of the pre-catalytic and catalytic spliceosome
CC complexes. Component of the postcatalytic spliceosome P complex.
CC Interacts with PDCD6; the interaction induces translocation of PDCD6 in
CC the cytoplasm. Interacts with PPIL1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NW64}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NW64}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NW64}. Note=Nearly exclusively nuclear.
CC Translocated from the nucleus to the cytoplasm after heat shock cell
CC treatment. May be shuttling between the nucleus and the cytosol.
CC {ECO:0000250|UniProtKB:Q9NW64}.
CC -!- DOMAIN: The C-terminal RRM domain and the zinc finger motif are
CC necessary for RNA-binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLT11 family. {ECO:0000305}.
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DR EMBL; AK018452; BAB31220.1; -; mRNA.
DR EMBL; AK045116; BAC32229.1; -; mRNA.
DR EMBL; AK150271; BAE29427.1; -; mRNA.
DR EMBL; AK151758; BAE30665.1; -; mRNA.
DR EMBL; AK152252; BAE31073.1; -; mRNA.
DR EMBL; AK166600; BAE38885.1; -; mRNA.
DR EMBL; AK167509; BAE39585.1; -; mRNA.
DR EMBL; AK168919; BAE40732.1; -; mRNA.
DR EMBL; BC080205; AAH80205.1; -; mRNA.
DR CCDS; CCDS29272.1; -.
DR RefSeq; NP_080052.1; NM_025776.2.
DR AlphaFoldDB; Q8BHS3; -.
DR SMR; Q8BHS3; -.
DR IntAct; Q8BHS3; 1.
DR STRING; 10090.ENSMUSP00000025506; -.
DR iPTMnet; Q8BHS3; -.
DR PhosphoSitePlus; Q8BHS3; -.
DR EPD; Q8BHS3; -.
DR jPOST; Q8BHS3; -.
DR MaxQB; Q8BHS3; -.
DR PaxDb; Q8BHS3; -.
DR PeptideAtlas; Q8BHS3; -.
DR PRIDE; Q8BHS3; -.
DR ProteomicsDB; 300261; -.
DR Antibodypedia; 1177; 196 antibodies from 28 providers.
DR Ensembl; ENSMUST00000025506; ENSMUSP00000025506; ENSMUSG00000024604.
DR GeneID; 66810; -.
DR KEGG; mmu:66810; -.
DR UCSC; uc008fal.1; mouse.
DR CTD; 55696; -.
DR MGI; MGI:1914060; Rbm22.
DR VEuPathDB; HostDB:ENSMUSG00000024604; -.
DR eggNOG; KOG0153; Eukaryota.
DR GeneTree; ENSGT00390000002792; -.
DR HOGENOM; CLU_027112_3_0_1; -.
DR InParanoid; Q8BHS3; -.
DR OMA; PYFRKGR; -.
DR OrthoDB; 1272857at2759; -.
DR PhylomeDB; Q8BHS3; -.
DR TreeFam; TF314284; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 66810; 29 hits in 75 CRISPR screens.
DR ChiTaRS; Rbm22; mouse.
DR PRO; PR:Q8BHS3; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BHS3; protein.
DR Bgee; ENSMUSG00000024604; Expressed in animal zygote and 263 other tissues.
DR Genevisible; Q8BHS3; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
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:0000974; C:Prp19 complex; IBA:GO_Central.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036002; F:pre-mRNA binding; ISS:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039171; Cwc2/Slt11.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14089; PTHR14089; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Spliceosome; Transport; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT CHAIN 2..420
FT /note="Pre-mRNA-splicing factor RBM22"
FT /id="PRO_0000250548"
FT DOMAIN 232..305
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 159..186
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 303..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NW64"
FT CONFLICT 171
FT /note="G -> R (in Ref. 1; BAE39585)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="P -> L (in Ref. 1; BAB31220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46896 MW; A82549D8CC88C7D0 CRC64;
MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG
VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG LSFKDDMPKS DVNKEYYTQN
MEREISNSDG TRPVGMLGKA TSTSDMLLKL ARTTPYYKRN RPHICSFWVK GECKRGEECP
YRHEKPTDPD DPLADQNIKD RYYGINDPVA DKLLKRASTM PRLDPPEDKT ITTLYVGGLG
DTITETDLRN HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EVAAEKSFNK LIVNGRRLNV
KWGRSQAARG KEKEKDGTTD SGIKLEPVPG LPGALPPPPA AEEEASANYF NLPPSGPPAV
VNIALPPPPG IAPPPPPGFG PHMFHPMGPP PPFMRAPGPI HYPSQDPQRM GAHAGKHSSP
