ROAA_MOUSE
ID ROAA_MOUSE Reviewed; 285 AA.
AC Q99020; Q8BPE0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A/B;
DE Short=hnRNP A/B;
DE AltName: Full=CArG-binding factor-A;
DE Short=CBF-A;
GN Name=Hnrnpab; Synonyms=Cbf-a, Cgbfa, Hnrpab;
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 [MRNA].
RC TISSUE=Muscle;
RX PubMed=1398104; DOI=10.1016/0378-1119(92)90276-u;
RA Kamada S., Miwa T.;
RT "A protein binding to CArG box motifs and to single-stranded DNA functions
RT as a transcriptional repressor.";
RL Gene 119:229-236(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP PROTEIN SEQUENCE OF 117-124; 161-174; 177-195 AND 201-208, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220 AND LYS-271, AND
RP IDENTIFICATION BY MASS 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).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-250; ARG-255; ARG-258 AND
RP ARG-275, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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: Transcriptional repressor. Binds to CArG box motifs, single-
CC stranded and double-stranded DNA, and RNA. It may be that repression by
CC CBF-A is a result of competitive binding of CBF, a putative positive
CC factor, and CBF-A to the same or overlapping motifs around the CArG
CC boxes.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with APOBEC1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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DR EMBL; D90151; BAA14181.1; -; mRNA.
DR EMBL; L36663; AAA92146.1; -; mRNA.
DR EMBL; AK076132; BAC36208.1; -; mRNA.
DR CCDS; CCDS24654.1; -.
DR PIR; JQ0448; JQ0448.
DR RefSeq; NP_034578.1; NM_010448.3.
DR AlphaFoldDB; Q99020; -.
DR SMR; Q99020; -.
DR BioGRID; 200358; 48.
DR ComplexPortal; CPX-1098; C-to-U editosome complex.
DR DIP; DIP-31415N; -.
DR IntAct; Q99020; 9.
DR MINT; Q99020; -.
DR iPTMnet; Q99020; -.
DR PhosphoSitePlus; Q99020; -.
DR SwissPalm; Q99020; -.
DR EPD; Q99020; -.
DR jPOST; Q99020; -.
DR MaxQB; Q99020; -.
DR PRIDE; Q99020; -.
DR ProteomicsDB; 300432; -.
DR Antibodypedia; 17556; 159 antibodies from 23 providers.
DR DNASU; 15384; -.
DR Ensembl; ENSMUST00000074669; ENSMUSP00000074238; ENSMUSG00000020358.
DR GeneID; 15384; -.
DR KEGG; mmu:15384; -.
DR UCSC; uc007iua.1; mouse.
DR CTD; 3182; -.
DR MGI; MGI:1330294; Hnrnpab.
DR VEuPathDB; HostDB:ENSMUSG00000020358; -.
DR GeneTree; ENSGT00940000154735; -.
DR InParanoid; Q99020; -.
DR BioGRID-ORCS; 15384; 15 hits in 78 CRISPR screens.
DR ChiTaRS; Hnrnpab; mouse.
DR PRO; PR:Q99020; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99020; protein.
DR Bgee; ENSMUSG00000020358; Expressed in primitive streak and 260 other tissues.
DR ExpressionAtlas; Q99020; baseline and differential.
DR Genevisible; Q99020; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0045293; C:mRNA editing complex; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IPI:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:HGNC-UCL.
DR GO; GO:0016556; P:mRNA modification; ISO:MGI.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:1901537; P:positive regulation of DNA demethylation; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd12757; RRM1_hnRNPAB; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012956; CARG-binding_factor_N.
DR InterPro; IPR034846; hnRNPAB_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08143; CBFNT; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..285
FT /note="Heterogeneous nuclear ribonucleoprotein A/B"
FT /id="PRO_0000081493"
FT DOMAIN 75..158
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 159..238
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99729"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99729"
FT MOD_RES 250
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99729"
FT MOD_RES 250
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 255
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 258
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 271
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 275
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 275
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99729"
FT MOD_RES 275
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99729"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99729"
FT CONFLICT 26
FT /note="G -> S (in Ref. 2; BAC36208)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="A -> R (in Ref. 2; BAC36208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 30831 MW; 7881F34131160E0C CRC64;
MSDAAEEQPM ETTGATENGH EAAPEGEAPV EPSAAAAAPA ASAGSGGGTT TAPSGNQNGA
EGDQINASKN EEDAGKMFVG GLSWDTSKKD LKDYFTKFGE VVDCTIKMDP NTGRSRGFGF
ILFKDSSSVE KVLDQKEHRL DGRVIDPKKA MAMKKDPVKK IFVGGLNPEA TEEKIREYFG
QFGEIEAIEL PIDPKLNKRR GFVFITFKEE DPVKKVLEKK FHTVSGSKCE IKVAQPKEVY
QQQQYGSGGR GNRNRGNRGS GGGQGSTNYG KSQRRGGHQN NYKPY
