RBM42_HUMAN
ID RBM42_HUMAN Reviewed; 480 AA.
AC Q9BTD8; O00320; Q8N5R7; Q9BU66;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=RNA-binding protein 42;
DE AltName: Full=RNA-binding motif protein 42;
GN Name=RBM42;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Lung, and Muscle;
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 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 [4]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 4).
RX PubMed=19170760; DOI=10.1111/j.1365-2443.2008.01256.x;
RA Fukuda T., Naiki T., Saito M., Irie K.;
RT "hnRNP K interacts with RNA binding motif protein 42 and functions in the
RT maintenance of cellular ATP level during stress conditions.";
RL Genes Cells 14:113-128(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION BY
RP 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 [6]
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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-153; ARG-158; ARG-168 AND
RP ARG-181, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Binds (via the RRM domain) to the 3'-untranslated region
CC (UTR) of CDKN1A mRNA. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HNRNPK. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BTD8; P61978: HNRNPK; NbExp=3; IntAct=EBI-746862, EBI-304185;
CC Q9BTD8; P86480: PRR20D; NbExp=3; IntAct=EBI-746862, EBI-12754095;
CC Q9BTD8; P25788: PSMA3; NbExp=3; IntAct=EBI-746862, EBI-348380;
CC Q9BTD8; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-746862, EBI-11987469;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Upon stress response, localizes with HNRNPK in cytoplasmic
CC aggregates of stalled translational preinitiation complexes called
CC stress granules. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BTD8-1; Sequence=Displayed;
CC Name=2; Synonyms=RBM42a;
CC IsoId=Q9BTD8-2; Sequence=VSP_028817;
CC Name=3;
CC IsoId=Q9BTD8-3; Sequence=VSP_028818;
CC Name=4; Synonyms=RBM42b;
CC IsoId=Q9BTD8-4; Sequence=VSP_037256;
CC -!- SIMILARITY: Belongs to the RRM RBM42 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB57629.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC002115; AAB57629.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC002868; AAH02868.1; -; mRNA.
DR EMBL; BC004204; AAH04204.1; -; mRNA.
DR EMBL; BC031682; AAH31682.1; -; mRNA.
DR CCDS; CCDS12468.1; -. [Q9BTD8-1]
DR RefSeq; NP_001306042.1; NM_001319113.1. [Q9BTD8-3]
DR RefSeq; NP_077297.2; NM_024321.4. [Q9BTD8-1]
DR PDB; 6QW6; EM; 2.92 A; R=1-480.
DR PDB; 6QX9; EM; 3.28 A; R=1-480.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; Q9BTD8; -.
DR SMR; Q9BTD8; -.
DR BioGRID; 122588; 174.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR IntAct; Q9BTD8; 61.
DR MINT; Q9BTD8; -.
DR STRING; 9606.ENSP00000262633; -.
DR GlyGen; Q9BTD8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BTD8; -.
DR PhosphoSitePlus; Q9BTD8; -.
DR BioMuta; RBM42; -.
DR DMDM; 74761247; -.
DR EPD; Q9BTD8; -.
DR jPOST; Q9BTD8; -.
DR MassIVE; Q9BTD8; -.
DR MaxQB; Q9BTD8; -.
DR PaxDb; Q9BTD8; -.
DR PeptideAtlas; Q9BTD8; -.
DR PRIDE; Q9BTD8; -.
DR ProteomicsDB; 78975; -. [Q9BTD8-1]
DR ProteomicsDB; 78976; -. [Q9BTD8-2]
DR ProteomicsDB; 78977; -. [Q9BTD8-3]
DR ProteomicsDB; 78978; -. [Q9BTD8-4]
DR TopDownProteomics; Q9BTD8-2; -. [Q9BTD8-2]
DR Antibodypedia; 29473; 145 antibodies from 24 providers.
DR DNASU; 79171; -.
DR Ensembl; ENST00000262633.9; ENSP00000262633.3; ENSG00000126254.12. [Q9BTD8-1]
DR Ensembl; ENST00000588161.5; ENSP00000466044.1; ENSG00000126254.12. [Q9BTD8-2]
DR GeneID; 79171; -.
DR KEGG; hsa:79171; -.
DR MANE-Select; ENST00000262633.9; ENSP00000262633.3; NM_024321.5; NP_077297.2.
DR UCSC; uc002oan.4; human. [Q9BTD8-1]
DR CTD; 79171; -.
DR GeneCards; RBM42; -.
DR HGNC; HGNC:28117; RBM42.
DR HPA; ENSG00000126254; Low tissue specificity.
DR MIM; 613232; gene.
DR neXtProt; NX_Q9BTD8; -.
DR OpenTargets; ENSG00000126254; -.
DR PharmGKB; PA162400760; -.
DR VEuPathDB; HostDB:ENSG00000126254; -.
DR eggNOG; KOG0226; Eukaryota.
DR GeneTree; ENSGT00930000151055; -.
DR InParanoid; Q9BTD8; -.
DR OMA; RMPMMRG; -.
DR OrthoDB; 1249623at2759; -.
DR PhylomeDB; Q9BTD8; -.
DR TreeFam; TF313946; -.
DR PathwayCommons; Q9BTD8; -.
DR SignaLink; Q9BTD8; -.
DR BioGRID-ORCS; 79171; 548 hits in 1088 CRISPR screens.
DR ChiTaRS; RBM42; human.
DR GenomeRNAi; 79171; -.
DR Pharos; Q9BTD8; Tdark.
DR PRO; PR:Q9BTD8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BTD8; protein.
DR Bgee; ENSG00000126254; Expressed in mucosa of transverse colon and 198 other tissues.
DR ExpressionAtlas; Q9BTD8; baseline and differential.
DR Genevisible; Q9BTD8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR CDD; cd12383; RRM_RBM42; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034215; RBM42_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..480
FT /note="RNA-binding protein 42"
FT /id="PRO_0000307750"
FT DOMAIN 381..459
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..480
FT /note="Necessary for interaction with HNRNPK"
FT /evidence="ECO:0000250"
FT REGION 319..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Basic and acidic 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:22814378"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 153
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 158
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 168
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 181
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 147..180
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_037256"
FT VAR_SEQ 147..176
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028817"
FT VAR_SEQ 147..175
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028818"
SQ SEQUENCE 480 AA; 50414 MW; 865780E6D7615DBE CRC64;
MAGAGPAPGL PGAGGPVVPG PGAGIPGKSG EERLKEMEAE MALFEQEVLG APVPGIPTAV
PAVPTVPTVP TVEAMQVPAA PVIRPIIATN TYQQVQQTLE ARAAAAATVV PPMVGGPPFV
GPVGFGPGDR SHLDSPEARE AMFLRRAAVA PQRAPILRPA FVPHVLQRAD SALSSAAAGP
RPMALRPPHQ ALVGPPLPGP PGPPMMLPPM ARAPGPPLGS MAALRPPLEE PAAPRELGLG
LGLGLKEKEE AVVAAAAGLE EASAAVAVGA GGAPAGPAVI GPSLPLALAM PLPEPEPLPL
PLEVVRGLLP PLRIPELLSL RPRPRPPRPE PPPGLMALEV PEPLGEDKKK GKPEKLKRCI
RTAAGSSWED PSLLEWDADD FRIFCGDLGN EVNDDILARA FSRFPSFLKA KVIRDKRTGK
TKGYGFVSFK DPSDYVRAMR EMNGKYVGSR PIKLRKSMWK DRNLDVVRKK QKEKKKLGLR
