ROAA_HUMAN
ID ROAA_HUMAN Reviewed; 332 AA.
AC Q99729; B3KNN5; D3DWP7; Q04150; Q8N7U3; Q9BQ99;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A/B;
DE Short=hnRNP A/B;
DE AltName: Full=APOBEC1-binding protein 1;
DE Short=ABBP-1;
GN Name=HNRNPAB; Synonyms=ABBP1, HNRPAB;
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 [MRNA] (ISOFORM 4).
RX PubMed=1717314; DOI=10.1016/0014-5793(91)81249-8;
RA Khan F., Jaiswal A.K., Szer W.;
RT "Cloning and sequence analysis of a human type A/B hnRNP protein.";
RL FEBS Lett. 290:159-161(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8999813; DOI=10.1074/jbc.272.3.1452;
RA Lau P.P., Zhu H.J., Nakamuta M., Chan L.;
RT "Cloning of an Apobec-1-binding protein that also interacts with
RT apolipoprotein B mRNA and evidence for its involvement in RNA editing.";
RL J. Biol. Chem. 272:1452-1455(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis;
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 [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] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta, Skin, and Uterus;
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 PROTEIN SEQUENCE OF 71-101; 111-118; 170-190; 196-203 AND 233-248,
RP METHYLATION AT ARG-245, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-322, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=15782174; DOI=10.1038/nmeth715;
RA Ong S.E., Mittler G., Mann M.;
RT "Identifying and quantifying in vivo methylation sites by heavy methyl
RT SILAC.";
RL Nat. Methods 1:119-126(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-271 (ISOFORM 3), ACETYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-272 (ISOFORM 4), 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-256 (ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-256 (ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-242, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-322, METHYLATION [LARGE SCALE
RP ANALYSIS] AT ARG-250 AND ARG-253 (ISOFORM 3), METHYLATION [LARGE SCALE
RP ANALYSIS] AT ARG-251 AND ARG-254 (ISOFORM 4), AND IDENTIFICATION BY MASS
RP 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).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130 AND LYS-203, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Binds single-stranded RNA. Has a high affinity for G-rich and
CC U-rich regions of hnRNA. Also binds to APOB mRNA transcripts around the
CC RNA editing site.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with APOBEC1.
CC {ECO:0000269|PubMed:17289661}.
CC -!- INTERACTION:
CC Q99729; Q15637: SF1; NbExp=4; IntAct=EBI-1044873, EBI-744603;
CC Q99729; Q9H3D4: TP63; NbExp=3; IntAct=EBI-1044873, EBI-2337775;
CC Q99729; Q9H3D4-1: TP63; NbExp=2; IntAct=EBI-1044873, EBI-2400586;
CC Q99729; Q9H3D4-2: TP63; NbExp=2; IntAct=EBI-1044873, EBI-6481107;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17289661}. Cytoplasm
CC {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q99729-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99729-2; Sequence=VSP_007826, VSP_007828;
CC Name=3;
CC IsoId=Q99729-3; Sequence=VSP_007826, VSP_007828, VSP_007829;
CC Name=4;
CC IsoId=Q99729-4; Sequence=VSP_007826, VSP_007829;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Dimethylation at Arg-322 is probably asymmetric.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50956.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 4]:
CC Sequence=AAA36575.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M65028; AAA36575.1; ALT_FRAME; mRNA.
DR EMBL; U76713; AAC50956.1; ALT_FRAME; mRNA.
DR EMBL; AK054600; BAG51397.1; -; mRNA.
DR EMBL; AK097657; BAC05134.1; -; mRNA.
DR EMBL; CH471165; EAW53843.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53844.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53845.1; -; Genomic_DNA.
DR EMBL; BC001616; AAH01616.1; -; mRNA.
DR EMBL; BC002625; AAH02625.1; -; mRNA.
DR EMBL; BC004561; AAH04561.1; -; mRNA.
DR EMBL; BC009359; AAH09359.1; -; mRNA.
DR EMBL; BC036708; AAH36708.1; -; mRNA.
DR CCDS; CCDS34309.1; -. [Q99729-2]
DR CCDS; CCDS34310.1; -. [Q99729-3]
DR PIR; S17563; S17563.
DR RefSeq; NP_004490.2; NM_004499.3. [Q99729-3]
DR RefSeq; NP_112556.2; NM_031266.2. [Q99729-2]
DR PDB; 3S7R; X-ray; 2.15 A; A/B=59-144.
DR PDBsum; 3S7R; -.
DR AlphaFoldDB; Q99729; -.
DR SMR; Q99729; -.
DR BioGRID; 109423; 252.
DR ComplexPortal; CPX-1097; C-to-U editosome complex.
DR DIP; DIP-50394N; -.
DR IntAct; Q99729; 118.
DR MINT; Q99729; -.
DR STRING; 9606.ENSP00000351108; -.
DR GlyConnect; 1313; 2 N-Linked glycans (1 site). [Q99729-2]
DR GlyGen; Q99729; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99729; -.
DR MetOSite; Q99729; -.
DR PhosphoSitePlus; Q99729; -.
DR SwissPalm; Q99729; -.
DR BioMuta; HNRNPAB; -.
DR DMDM; 158523286; -.
DR SWISS-2DPAGE; Q99729; -.
DR EPD; Q99729; -.
DR jPOST; Q99729; -.
DR MassIVE; Q99729; -.
DR MaxQB; Q99729; -.
DR PaxDb; Q99729; -.
DR PeptideAtlas; Q99729; -.
DR PRIDE; Q99729; -.
DR ProteomicsDB; 78443; -. [Q99729-1]
DR ProteomicsDB; 78444; -. [Q99729-2]
DR ProteomicsDB; 78445; -. [Q99729-3]
DR ProteomicsDB; 78446; -. [Q99729-4]
DR Antibodypedia; 17556; 159 antibodies from 23 providers.
DR DNASU; 3182; -.
DR Ensembl; ENST00000355836.9; ENSP00000348093.5; ENSG00000197451.12. [Q99729-3]
DR Ensembl; ENST00000358344.8; ENSP00000351108.3; ENSG00000197451.12. [Q99729-2]
DR Ensembl; ENST00000504898.5; ENSP00000425031.1; ENSG00000197451.12. [Q99729-2]
DR Ensembl; ENST00000506259.5; ENSP00000427465.1; ENSG00000197451.12. [Q99729-3]
DR GeneID; 3182; -.
DR KEGG; hsa:3182; -.
DR MANE-Select; ENST00000358344.8; ENSP00000351108.3; NM_031266.3; NP_112556.2. [Q99729-2]
DR UCSC; uc003miu.4; human. [Q99729-1]
DR CTD; 3182; -.
DR DisGeNET; 3182; -.
DR GeneCards; HNRNPAB; -.
DR HGNC; HGNC:5034; HNRNPAB.
DR HPA; ENSG00000197451; Low tissue specificity.
DR MIM; 602688; gene.
DR neXtProt; NX_Q99729; -.
DR OpenTargets; ENSG00000197451; -.
DR PharmGKB; PA162391196; -.
DR VEuPathDB; HostDB:ENSG00000197451; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000154735; -.
DR HOGENOM; CLU_012062_1_1_1; -.
DR InParanoid; Q99729; -.
DR OMA; AWYGAWG; -.
DR OrthoDB; 1202220at2759; -.
DR PhylomeDB; Q99729; -.
DR TreeFam; TF314808; -.
DR PathwayCommons; Q99729; -.
DR SignaLink; Q99729; -.
DR BioGRID-ORCS; 3182; 20 hits in 1083 CRISPR screens.
DR ChiTaRS; HNRNPAB; human.
DR EvolutionaryTrace; Q99729; -.
DR GeneWiki; HNRPAB; -.
DR GenomeRNAi; 3182; -.
DR Pharos; Q99729; Tbio.
DR PRO; PR:Q99729; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q99729; protein.
DR Bgee; ENSG00000197451; Expressed in mucosa of sigmoid colon and 206 other tissues.
DR ExpressionAtlas; Q99729; baseline and differential.
DR Genevisible; Q99729; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0045293; C:mRNA editing complex; IC:ComplexPortal.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0003729; F:mRNA binding; TAS:ProtInc.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:HGNC-UCL.
DR GO; GO:0016556; P:mRNA modification; IDA:ComplexPortal.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:ComplexPortal.
DR GO; GO:1901537; P:positive regulation of DNA demethylation; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:HGNC-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:1904580; P:regulation of intracellular mRNA localization; IEA:Ensembl.
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 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..332
FT /note="Heterogeneous nuclear ribonucleoprotein A/B"
FT /id="PRO_0000081492"
FT DOMAIN 69..154
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 153..233
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..332
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 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99020"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 245
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 245
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 250
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q99020"
FT MOD_RES 253
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q99020"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99020"
FT MOD_RES 322
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99020"
FT MOD_RES 322
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0007744|PubMed:15782174"
FT MOD_RES 322
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 26..32
FT /note="ASRGRGW -> GESPAGAG (in isoform 2, isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1717314"
FT /id="VSP_007826"
FT VAR_SEQ 164..165
FT /note="SP -> A (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007828"
FT VAR_SEQ 264..310
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1717314"
FT /id="VSP_007829"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3S7R"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:3S7R"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3S7R"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3S7R"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3S7R"
FT STRAND 109..119
FT /evidence="ECO:0007829|PDB:3S7R"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:3S7R"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3S7R"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:3S7R"
FT MOD_RES Q99729-3:250
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q99729-3:253
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q99729-3:255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q99729-3:271
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES Q99729-4:251
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q99729-4:254
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q99729-4:256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q99729-4:272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ SEQUENCE 332 AA; 36225 MW; F824A7E08D15268A CRC64;
MSEAGEEQPM ETTGATENGH EAVPEASRGR GWTGAAAGAG GATAAPPSGN QNGAEGDQIN
ASKNEEDAGK MFVGGLSWDT SKKDLKDYFT KFGEVVDCTI KMDPNTGRSR GFGFILFKDA
ASVEKVLDQK EHRLDGRVID PKKAMAMKKD PVKKIFVGGL NPESPTEEKI REYFGEFGEI
EAIELPMDPK LNKRRGFVFI TFKEEEPVKK VLEKKFHTVS GSKCEIKVAQ PKEVYQQQQY
GSGGRGNRNR GNRGSGGGGG GGGQSQSWNQ GYGNYWNQGY GYQQGYGPGY GGYDYSPYGY
YGYGPGYDYS QGSTNYGKSQ RRGGHQNNYK PY
