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 27-MAR-2024, entry version 208. 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=AAA36575.1; Type=Frameshift; 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; 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; 321. DR ComplexPortal; CPX-1097; C-to-U editosome complex. DR DIP; DIP-50394N; -. DR IntAct; Q99729; 122. DR MINT; Q99729; -. DR STRING; 9606.ENSP00000425031; -. 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 EPD; Q99729; -. DR jPOST; Q99729; -. DR MassIVE; Q99729; -. DR MaxQB; Q99729; -. DR PaxDb; 9606-ENSP00000351108; -. DR PeptideAtlas; Q99729; -. DR ProteomicsDB; 78443; -. [Q99729-1] DR ProteomicsDB; 78444; -. [Q99729-2] DR ProteomicsDB; 78445; -. [Q99729-3] DR ProteomicsDB; 78446; -. [Q99729-4] DR Pumba; Q99729; -. DR Antibodypedia; 17556; 183 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 AGR; HGNC:5034; -. 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; RSFNDGF; -. DR OrthoDB; 3127428at2759; -. DR PhylomeDB; Q99729; -. DR TreeFam; TF314808; -. DR PathwayCommons; Q99729; -. DR SignaLink; Q99729; -. DR BioGRID-ORCS; 3182; 22 hits in 1161 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 208 other cell types or tissues. DR ExpressionAtlas; Q99729; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL. DR GO; GO:0045293; C:mRNA editing complex; NAS:ComplexPortal. 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:0003723; F:RNA binding; HDA:UniProtKB. 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; NAS:ComplexPortal. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS: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 PANTHER; PTHR48033:SF1; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A_B; 1. DR PANTHER; PTHR48033; RNA-BINDING (RRM/RBD/RNP MOTIFS) FAMILY PROTEIN; 1. DR Pfam; PF08143; CBFNT; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 2. DR SWISS-2DPAGE; Q99729; -. DR Genevisible; Q99729; HS. 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 //