ID RBM22_HUMAN Reviewed; 420 AA.
AC Q9NW64; A6NDM5; B4DLI9; O95607;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 194.
DE RecName: Full=Pre-mRNA-splicing factor RBM22;
DE AltName: Full=RNA-binding motif protein 22;
DE AltName: Full=Zinc finger CCCH domain-containing protein 16;
GN Name=RBM22; Synonyms=ZC3H16; ORFNames=199G4;
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] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland, and Umbilical cord blood;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 126-420.
RC TISSUE=Brain;
RX PubMed=8681136; DOI=10.1101/gr.6.1.26;
RA Loftus S.K., Dixon J., Koprivnikar K., Dixon M.J., Wasmuth J.J.;
RT "Transcriptional map of the Treacher Collins candidate gene region.";
RL Genome Res. 6:26-34(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PDCD6.
RX PubMed=17045351; DOI=10.1016/j.bbamcr.2006.09.003;
RA Montaville P., Dai Y., Cheung C.Y., Giller K., Becker S., Michalak M.,
RA Webb S.E., Miller A.L., Krebs J.;
RT "Nuclear translocation of the calcium-binding protein ALG-2 induced by the
RT RNA-binding protein RBM22.";
RL Biochim. Biophys. Acta 1763:1335-1343(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-170 AND LYS-324.
RX PubMed=19133299; DOI=10.1016/j.bbamcr.2008.12.006;
RA Krebs J.;
RT "The influence of calcium signaling on the regulation of alternative
RT splicing.";
RL Biochim. Biophys. Acta 1793:979-984(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21122810; DOI=10.1016/j.bbamcr.2010.11.010;
RA Janowicz A., Michalak M., Krebs J.;
RT "Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7.";
RL Biochim. Biophys. Acta 1813:1045-1049(2011).
RN [14]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=22246180; DOI=10.1038/emboj.2011.502;
RA Rasche N., Dybkov O., Schmitzova J., Akyildiz B., Fabrizio P., Luhrmann R.;
RT "Cwc2 and its human homologue RBM22 promote an active conformation of the
RT spliceosome catalytic centre.";
RL EMBO J. 31:1591-1604(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-102, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-149 AND LYS-290, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-139, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP INTERACTION WITH PPIL1.
RX PubMed=33220177; DOI=10.1016/j.neuron.2020.10.035;
RA Chai G., Webb A., Li C., Antaki D., Lee S., Breuss M.W., Lang N.,
RA Stanley V., Anzenberg P., Yang X., Marshall T., Gaffney P., Wierenga K.J.,
RA Chung B.H., Tsang M.H., Pais L.S., Lovgren A.K., VanNoy G.E., Rehm H.L.,
RA Mirzaa G., Leon E., Diaz J., Neumann A., Kalverda A.P., Manfield I.W.,
RA Parry D.A., Logan C.V., Johnson C.A., Bonthron D.T., Valleley E.M.A.,
RA Issa M.Y., Abdel-Ghafar S.F., Abdel-Hamid M.S., Jennings P., Zaki M.S.,
RA Sheridan E., Gleeson J.G.;
RT "Mutations in Spliceosomal Genes PPIL1 and PRP17 Cause Neurodegenerative
RT Pontocerebellar Hypoplasia with Microcephaly.";
RL Neuron 109:241-256(2021).
RN [21]
RP STRUCTURE BY NMR OF 227-304.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in pre-mRNA-splicing factor
RT RBM22.";
RL Submitted (OCT-2007) to the PDB data bank.
RN [22] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [23] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=28076346; DOI=10.1038/nature21079;
RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT "Cryo-EM structure of a human spliceosome activated for step 2 of
RT splicing.";
RL Nature 542:318-323(2017).
RN [24] {ECO:0007744|PDB:6FF4}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29361316; DOI=10.1016/j.cell.2018.01.010;
RA Haselbach D., Komarov I., Agafonov D.E., Hartmuth K., Graf B., Dybkov O.,
RA Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Structure and Conformational Dynamics of the Human Spliceosomal Bact
RT Complex.";
RL Cell 172:454-464(2018).
RN [25] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.10 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29360106; DOI=10.1038/cr.2018.14;
RA Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.;
RT "Structure of the human activated spliceosome in three conformational
RT states.";
RL Cell Res. 28:307-322(2018).
RN [26] {ECO:0007744|PDB:5YZG}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29301961; DOI=10.1126/science.aar6401;
RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.;
RT "Structure of a human catalytic step I spliceosome.";
RL Science 359:537-545(2018).
RN [27] {ECO:0007744|PDB:6QDV}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 18-306, FUNCTION,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=30705154; DOI=10.1126/science.aaw5569;
RA Fica S.M., Oubridge C., Wilkinson M.E., Newman A.J., Nagai K.;
RT "A human postcatalytic spliceosome structure reveals essential roles of
RT metazoan factors for exon ligation.";
RL Science 363:710-714(2019).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the activated
CC spliceosome (PubMed:28502770, PubMed:28076346, PubMed:29361316,
CC PubMed:29360106, PubMed:29301961, PubMed:30705154). Involved in the
CC first step of pre-mRNA splicing. Binds directly to the internal stem-
CC loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the
CC 5' splice site during the activation and catalytic phases of the
CC spliceosome cycle. Involved in both translocations of the nuclear SLU7
CC to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the
CC nucleus upon cellular stress responses. {ECO:0000269|PubMed:17045351,
CC ECO:0000269|PubMed:21122810, ECO:0000269|PubMed:22246180,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106,
CC ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30705154}.
CC -!- SUBUNIT: Component of the pre-catalytic and catalytic spliceosome
CC complexes (PubMed:11991638, PubMed:28502770, PubMed:28076346,
CC PubMed:29361316, PubMed:29360106, PubMed:29301961). Component of the
CC postcatalytic spliceosome P complex (PubMed:30705154). Interacts with
CC PDCD6; the interaction induces translocation of PDCD6 in the cytoplasm.
CC Interacts with PPIL1 (PubMed:33220177). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:17045351, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316,
CC ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:33220177}.
CC -!- INTERACTION:
CC Q9NW64; Q53EZ4: CEP55; NbExp=6; IntAct=EBI-2602260, EBI-747776;
CC Q9NW64; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2602260, EBI-3867333;
CC Q9NW64; O75420: GIGYF1; NbExp=3; IntAct=EBI-2602260, EBI-947774;
CC Q9NW64; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2602260, EBI-618309;
CC Q9NW64; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-2602260, EBI-748420;
CC Q9NW64; Q9NZQ3-3: NCKIPSD; NbExp=5; IntAct=EBI-2602260, EBI-10963850;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17045351,
CC ECO:0000269|PubMed:21122810, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316,
CC ECO:0000269|PubMed:30705154}. Cytoplasm {ECO:0000269|PubMed:21122810}.
CC Note=Nearly exclusively nuclear. Translocated from the nucleus to the
CC cytoplasm after heat shock cell treatment. May be shuttling between the
CC nucleus and the cytosol. {ECO:0000269|PubMed:21122810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NW64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NW64-2; Sequence=VSP_036832;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC99998.1; Type=Miscellaneous discrepancy; Note=Chimera.; Evidence={ECO:0000305};
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DR EMBL; AL136933; CAB66867.1; -; mRNA.
DR EMBL; AK001152; BAA91521.1; -; mRNA.
DR EMBL; AK297019; BAG59551.1; -; mRNA.
DR EMBL; AC008453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61711.1; -; Genomic_DNA.
DR EMBL; BC003402; AAH03402.1; -; mRNA.
DR EMBL; U39402; AAC99998.1; ALT_SEQ; mRNA.
DR CCDS; CCDS34278.1; -. [Q9NW64-1]
DR RefSeq; NP_060517.1; NM_018047.2. [Q9NW64-1]
DR PDB; 2YTC; NMR; -; A=227-304.
DR PDB; 5MQF; EM; 5.90 A; P=1-420.
DR PDB; 5XJC; EM; 3.60 A; O=1-420.
DR PDB; 5YZG; EM; 4.10 A; O=1-420.
DR PDB; 5Z56; EM; 5.10 A; O=1-420.
DR PDB; 5Z57; EM; 6.50 A; O=1-420.
DR PDB; 6FF4; EM; 16.00 A; P=1-420.
DR PDB; 6FF7; EM; 4.50 A; P=1-420.
DR PDB; 6ICZ; EM; 3.00 A; O=1-420.
DR PDB; 6ID0; EM; 2.90 A; O=1-420.
DR PDB; 6ID1; EM; 2.86 A; O=1-420.
DR PDB; 6QDV; EM; 3.30 A; M=18-306.
DR PDB; 6ZYM; EM; 3.40 A; P=1-218.
DR PDB; 7A5P; EM; 5.00 A; P=1-420.
DR PDB; 7AAV; EM; 4.20 A; P=1-420.
DR PDB; 7ABG; EM; 7.80 A; P=1-420.
DR PDB; 7ABI; EM; 8.00 A; P=1-420.
DR PDB; 7QTT; EM; 3.10 A; U=1-420.
DR PDB; 7W59; EM; 3.60 A; O=1-420.
DR PDB; 7W5A; EM; 3.60 A; O=1-420.
DR PDB; 7W5B; EM; 4.30 A; O=1-420.
DR PDB; 8C6J; EM; 2.80 A; M=1-420.
DR PDB; 8CH6; EM; 5.90 A; U=1-420.
DR PDBsum; 2YTC; -.
DR PDBsum; 5MQF; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 6FF4; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6ID0; -.
DR PDBsum; 6ID1; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 6ZYM; -.
DR PDBsum; 7A5P; -.
DR PDBsum; 7AAV; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7QTT; -.
DR PDBsum; 7W59; -.
DR PDBsum; 7W5A; -.
DR PDBsum; 7W5B; -.
DR PDBsum; 8C6J; -.
DR PDBsum; 8CH6; -.
DR AlphaFoldDB; Q9NW64; -.
DR EMDB; EMD-11569; -.
DR EMDB; EMD-11693; -.
DR EMDB; EMD-11695; -.
DR EMDB; EMD-11697; -.
DR EMDB; EMD-14146; -.
DR EMDB; EMD-16452; -.
DR EMDB; EMD-16658; -.
DR EMDB; EMD-32317; -.
DR EMDB; EMD-32319; -.
DR EMDB; EMD-32321; -.
DR EMDB; EMD-3545; -.
DR EMDB; EMD-4255; -.
DR EMDB; EMD-4525; -.
DR EMDB; EMD-6721; -.
DR EMDB; EMD-6864; -.
DR EMDB; EMD-6889; -.
DR EMDB; EMD-6890; -.
DR EMDB; EMD-9645; -.
DR EMDB; EMD-9646; -.
DR EMDB; EMD-9647; -.
DR SMR; Q9NW64; -.
DR BioGRID; 120821; 194.
DR CORUM; Q9NW64; -.
DR IntAct; Q9NW64; 55.
DR MINT; Q9NW64; -.
DR STRING; 9606.ENSP00000199814; -.
DR GlyGen; Q9NW64; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9NW64; -.
DR MetOSite; Q9NW64; -.
DR PhosphoSitePlus; Q9NW64; -.
DR SwissPalm; Q9NW64; -.
DR BioMuta; RBM22; -.
DR DMDM; 74762758; -.
DR EPD; Q9NW64; -.
DR jPOST; Q9NW64; -.
DR MassIVE; Q9NW64; -.
DR MaxQB; Q9NW64; -.
DR PaxDb; 9606-ENSP00000199814; -.
DR PeptideAtlas; Q9NW64; -.
DR ProteomicsDB; 82897; -. [Q9NW64-1]
DR ProteomicsDB; 82898; -. [Q9NW64-2]
DR Pumba; Q9NW64; -.
DR Antibodypedia; 1177; 220 antibodies from 28 providers.
DR DNASU; 55696; -.
DR Ensembl; ENST00000199814.9; ENSP00000199814.4; ENSG00000086589.12. [Q9NW64-1]
DR Ensembl; ENST00000447771.6; ENSP00000412118.2; ENSG00000086589.12. [Q9NW64-2]
DR GeneID; 55696; -.
DR KEGG; hsa:55696; -.
DR MANE-Select; ENST00000199814.9; ENSP00000199814.4; NM_018047.3; NP_060517.1.
DR UCSC; uc003lst.4; human. [Q9NW64-1]
DR AGR; HGNC:25503; -.
DR CTD; 55696; -.
DR GeneCards; RBM22; -.
DR HGNC; HGNC:25503; RBM22.
DR HPA; ENSG00000086589; Low tissue specificity.
DR MIM; 612430; gene.
DR neXtProt; NX_Q9NW64; -.
DR OpenTargets; ENSG00000086589; -.
DR PharmGKB; PA134982384; -.
DR VEuPathDB; HostDB:ENSG00000086589; -.
DR eggNOG; KOG0153; Eukaryota.
DR GeneTree; ENSGT00390000002792; -.
DR HOGENOM; CLU_027112_3_0_1; -.
DR InParanoid; Q9NW64; -.
DR OMA; CPLRVQW; -.
DR OrthoDB; 929875at2759; -.
DR PhylomeDB; Q9NW64; -.
DR TreeFam; TF314284; -.
DR PathwayCommons; Q9NW64; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9NW64; -.
DR BioGRID-ORCS; 55696; 737 hits in 1165 CRISPR screens.
DR EvolutionaryTrace; Q9NW64; -.
DR GeneWiki; RBM22; -.
DR GenomeRNAi; 55696; -.
DR Pharos; Q9NW64; Tbio.
DR PRO; PR:Q9NW64; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NW64; Protein.
DR Bgee; ENSG00000086589; Expressed in tibia and 202 other cell types or tissues.
DR ExpressionAtlas; Q9NW64; baseline and differential.
DR Genevisible; Q9NW64; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA: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; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IDA:UniProtKB.
DR CDD; cd12224; RRM_RBM22; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 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; IPR048995; STL11/RBM22-like_N.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14089; PRE-MRNA-SPLICING FACTOR RBM22; 1.
DR PANTHER; PTHR14089:SF18; PRE-MRNA-SPLICING FACTOR RBM22; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF21369; STL11_N; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Spliceosome; Transport;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..420
FT /note="Pre-mRNA-splicing factor RBM22"
FT /id="PRO_0000250546"
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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 43..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036832"
FT MUTAGEN 170
FT /note="K->R: Accumulates in speckle-like structures."
FT /evidence="ECO:0000269|PubMed:19133299"
FT MUTAGEN 324
FT /note="K->R: Accumulates in speckle-like structures."
FT /evidence="ECO:0000269|PubMed:19133299"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6ID0"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 166..171
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6ID0"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:7QTT"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6ID0"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:6ID0"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:6ID1"
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
//
