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Database: UniProt
Entry: Q9NW64
LinkDB: Q9NW64
Original site: Q9NW64 
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   29-SEP-2021, entry version 182.
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   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   [21] {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   [22] {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   [23] {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   [24] {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   [25] {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   [26] {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       {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17045351,
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   -!- 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   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   SMR; Q9NW64; -.
DR   BioGRID; 120821; 83.
DR   CORUM; Q9NW64; -.
DR   IntAct; Q9NW64; 53.
DR   STRING; 9606.ENSP00000199814; -.
DR   GlyGen; Q9NW64; 1 site, 1 O-linked glycan (1 site).
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; Q9NW64; -.
DR   PeptideAtlas; Q9NW64; -.
DR   PRIDE; Q9NW64; -.
DR   ProteomicsDB; 82897; -. [Q9NW64-1]
DR   ProteomicsDB; 82898; -. [Q9NW64-2]
DR   Antibodypedia; 1177; 185 antibodies.
DR   DNASU; 55696; -.
DR   Ensembl; ENST00000199814; ENSP00000199814; ENSG00000086589. [Q9NW64-1]
DR   Ensembl; ENST00000447771; ENSP00000412118; ENSG00000086589. [Q9NW64-2]
DR   GeneID; 55696; -.
DR   KEGG; hsa:55696; -.
DR   UCSC; uc003lst.4; human. [Q9NW64-1]
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; PYFRKGR; -.
DR   OrthoDB; 1272857at2759; -.
DR   PhylomeDB; Q9NW64; -.
DR   TreeFam; TF314284; -.
DR   PathwayCommons; Q9NW64; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 55696; 698 hits in 1024 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 endometrium and 236 other 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:0035690; P:cellular response to drug; 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   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   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          226..229
FT                   /evidence="ECO:0007829|PDB:6FF4"
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
//
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