HNRPR_HUMAN
ID HNRPR_HUMAN Reviewed; 633 AA.
AC O43390; Q2L7G6; Q5TEH1; Q9BV64; S4R3J4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein R;
DE Short=hnRNP R;
GN Name=HNRNPR; Synonyms=HNRPR;
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 1).
RX PubMed=9421497; DOI=10.1093/nar/26.2.439;
RA Hassfeld W., Chan E.K.L., Mathison D.A., Portman D., Dreyfuss G.,
RA Steiner G., Tan E.M.;
RT "Molecular definition of heterogeneous nuclear ribonucleoprotein R (hnRNP
RT R) using autoimmune antibody: immunological relationship with hnRNP P.";
RL Nucleic Acids Res. 26:439-445(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=15858414; DOI=10.1097/00001756-200505120-00014;
RA Huang J., Chen X.H., Wu K., Xu P.;
RT "Cloning and expression of a novel isoform of heterogeneous nuclear
RT ribonucleoprotein-R.";
RL NeuroReport 16:727-730(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP PROTEIN SEQUENCE OF 2-13; 32-41; 70-84; 95-103; 134-145; 175-216; 225-255;
RP 258-285; 290-300; 347-366; 373-384; 398-414 AND 428-441, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP 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 [6]
RP PROTEIN SEQUENCE OF 32-41 AND 347-359, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
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 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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, 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 [11]
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 [12]
RP INTERACTION WITH GTPBP1.
RX PubMed=21515746; DOI=10.1096/fj.10-178715;
RA Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J.,
RA Chung S.J., Senju S., Nishimura Y., Kim K.T.;
RT "Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding
RT protein 1 (GTPBP1) with its target mRNAs.";
RL FASEB J. 25:2757-2769(2011).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [15]
RP IDENTIFICATION BY 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY MASS
RP 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-171 AND LYS-359, 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).
RN [20]
RP STRUCTURE BY NMR OF 333-416.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in heterogeneous nuclear
RT ribonucleoprotein R (HNRNP R).";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Component of ribonucleosomes, which are complexes of at least
CC 20 other different heterogeneous nuclear ribonucleoproteins (hnRNP).
CC hnRNP play an important role in processing of precursor mRNA in the
CC nucleus.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.
CC Interacts with GTPBP1. {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:21515746}.
CC -!- INTERACTION:
CC O43390; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-713419, EBI-742808;
CC O43390; P16333: NCK1; NbExp=2; IntAct=EBI-713419, EBI-389883;
CC O43390; Q99873: PRMT1; NbExp=5; IntAct=EBI-713419, EBI-78738;
CC O43390-2; Q9Y5E9: PCDHB14; NbExp=3; IntAct=EBI-12236340, EBI-10329013;
CC O43390-2; Q9Y272: RASD1; NbExp=3; IntAct=EBI-12236340, EBI-740818;
CC O43390-2; Q13148: TARDBP; NbExp=3; IntAct=EBI-12236340, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7TMK9}. Microsome
CC {ECO:0000250|UniProtKB:Q7TMK9}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:17289661}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. The tyrosine phosphorylated form bound to RNA is found in
CC microsomes (By similarity). {ECO:0000250|UniProtKB:Q7TMK9,
CC ECO:0000269|PubMed:17289661}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O43390-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43390-2; Sequence=VSP_038360;
CC Name=3; Synonyms=hnRNP-R2;
CC IsoId=O43390-3; Sequence=VSP_047647;
CC Name=4;
CC IsoId=O43390-4; Sequence=VSP_054703, VSP_038360;
CC -!- MISCELLANEOUS: [Isoform 3]: Expression is low and neural-specific.
CC {ECO:0000305}.
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DR EMBL; AF000364; AAC39540.1; -; mRNA.
DR EMBL; DQ351905; ABC73063.1; -; mRNA.
DR EMBL; AL109936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001449; AAH01449.1; -; mRNA.
DR CCDS; CCDS232.1; -. [O43390-1]
DR CCDS; CCDS44085.1; -. [O43390-2]
DR CCDS; CCDS60020.1; -. [O43390-4]
DR CCDS; CCDS72727.1; -. [O43390-3]
DR PIR; T02673; T02673.
DR RefSeq; NP_001095868.1; NM_001102398.2. [O43390-2]
DR RefSeq; NP_001284549.1; NM_001297620.1. [O43390-3]
DR RefSeq; NP_005817.1; NM_005826.4. [O43390-1]
DR RefSeq; XP_005245768.1; XM_005245711.4. [O43390-1]
DR RefSeq; XP_011538773.1; XM_011540471.2. [O43390-2]
DR RefSeq; XP_016855497.1; XM_017000008.1. [O43390-3]
DR PDB; 2DK2; NMR; -; A=333-416.
DR PDBsum; 2DK2; -.
DR AlphaFoldDB; O43390; -.
DR SMR; O43390; -.
DR BioGRID; 115530; 451.
DR CORUM; O43390; -.
DR IntAct; O43390; 117.
DR MINT; O43390; -.
DR STRING; 9606.ENSP00000363745; -.
DR GlyGen; O43390; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43390; -.
DR MetOSite; O43390; -.
DR PhosphoSitePlus; O43390; -.
DR SwissPalm; O43390; -.
DR BioMuta; HNRNPR; -.
DR EPD; O43390; -.
DR jPOST; O43390; -.
DR MassIVE; O43390; -.
DR MaxQB; O43390; -.
DR PaxDb; O43390; -.
DR PeptideAtlas; O43390; -.
DR PRIDE; O43390; -.
DR ProteomicsDB; 48919; -. [O43390-1]
DR ProteomicsDB; 48920; -. [O43390-2]
DR ProteomicsDB; 61330; -.
DR TopDownProteomics; O43390-1; -. [O43390-1]
DR Antibodypedia; 3187; 177 antibodies from 28 providers.
DR DNASU; 10236; -.
DR Ensembl; ENST00000302271.11; ENSP00000304405.6; ENSG00000125944.21. [O43390-1]
DR Ensembl; ENST00000374612.5; ENSP00000363741.1; ENSG00000125944.21. [O43390-1]
DR Ensembl; ENST00000374616.7; ENSP00000363745.3; ENSG00000125944.21. [O43390-2]
DR Ensembl; ENST00000427764.3; ENSP00000392799.2; ENSG00000125944.21. [O43390-3]
DR Ensembl; ENST00000478691.5; ENSP00000474437.1; ENSG00000125944.21. [O43390-4]
DR Ensembl; ENST00000634263.1; ENSP00000489371.1; ENSG00000282958.5. [O43390-1]
DR Ensembl; ENST00000634634.1; ENSP00000488941.1; ENSG00000282958.5. [O43390-3]
DR Ensembl; ENST00000634713.1; ENSP00000488945.1; ENSG00000282958.5. [O43390-2]
DR Ensembl; ENST00000634766.2; ENSP00000489252.1; ENSG00000282958.5. [O43390-1]
DR Ensembl; ENST00000635150.1; ENSP00000489275.1; ENSG00000282958.5. [O43390-4]
DR GeneID; 10236; -.
DR KEGG; hsa:10236; -.
DR MANE-Select; ENST00000302271.11; ENSP00000304405.6; NM_005826.5; NP_005817.1.
DR UCSC; uc001bgp.5; human. [O43390-1]
DR CTD; 10236; -.
DR DisGeNET; 10236; -.
DR GeneCards; HNRNPR; -.
DR HGNC; HGNC:5047; HNRNPR.
DR HPA; ENSG00000125944; Low tissue specificity.
DR MIM; 607201; gene.
DR neXtProt; NX_O43390; -.
DR OpenTargets; ENSG00000125944; -.
DR PharmGKB; PA162391459; -.
DR VEuPathDB; HostDB:ENSG00000125944; -.
DR eggNOG; KOG0117; Eukaryota.
DR GeneTree; ENSGT00940000153511; -.
DR HOGENOM; CLU_022960_2_1_1; -.
DR InParanoid; O43390; -.
DR OMA; GRANNMY; -.
DR OrthoDB; 1384330at2759; -.
DR PhylomeDB; O43390; -.
DR TreeFam; TF314932; -.
DR PathwayCommons; O43390; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR SignaLink; O43390; -.
DR BioGRID-ORCS; 10236; 146 hits in 1081 CRISPR screens.
DR ChiTaRS; HNRNPR; human.
DR EvolutionaryTrace; O43390; -.
DR GeneWiki; HNRNPR; -.
DR GenomeRNAi; 10236; -.
DR Pharos; O43390; Tbio.
DR PRO; PR:O43390; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43390; protein.
DR Bgee; ENSG00000125944; Expressed in ventricular zone and 113 other tissues.
DR ExpressionAtlas; O43390; baseline and differential.
DR Genevisible; O43390; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; NAS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; NAS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR CDD; cd12488; RRM2_hnRNPR; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR041337; hnRNP_Q_AcD.
DR InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR InterPro; IPR034411; hnRNPR_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF18360; hnRNP_Q_AcD; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Isopeptide bond;
KW Microsome; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..633
FT /note="Heterogeneous nuclear ribonucleoprotein R"
FT /id="PRO_0000081870"
FT DOMAIN 165..244
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 246..328
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 341..411
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 462..471
FT /note="1; approximate"
FT REPEAT 472..482
FT /note="2"
FT REPEAT 488..497
FT /note="3; approximate"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..567
FT /note="RNA-binding RGG-box"
FT REGION 462..497
FT /note="3 X 11 AA approximate repeats of D-D-Y-Y-G-Y-D-Y-H-
FT D-Y"
FT REGION 501..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 412..418
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 582..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 366
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_054703"
FT VAR_SEQ 129..166
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15858414"
FT /id="VSP_047647"
FT VAR_SEQ 269
FT /note="V -> VTGL (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038360"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:2DK2"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:2DK2"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:2DK2"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:2DK2"
FT STRAND 376..383
FT /evidence="ECO:0007829|PDB:2DK2"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:2DK2"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:2DK2"
SQ SEQUENCE 633 AA; 70943 MW; 088341F6465ED46F CRC64;
MANQVNGNAV QLKEEEEPMD TSSVTHTEHY KTLIEAGLPQ KVAERLDEIF QTGLVAYVDL
DERAIDALRE FNEEGALSVL QQFKESDLSH VQNKSAFLCG VMKTYRQREK QGSKVQESTK
GPDEAKIKAL LERTGYTLDV TTGQRKYGGP PPDSVYSGVQ PGIGTEVFVG KIPRDLYEDE
LVPLFEKAGP IWDLRLMMDP LSGQNRGYAF ITFCGKEAAQ EAVKLCDSYE IRPGKHLGVC
ISVANNRLFV GSIPKNKTKE NILEEFSKVT EGLVDVILYH QPDDKKKNRG FCFLEYEDHK
SAAQARRRLM SGKVKVWGNV VTVEWADPVE EPDPEVMAKV KVLFVRNLAT TVTEEILEKS
FSEFGKLERV KKLKDYAFVH FEDRGAAVKA MDEMNGKEIE GEEIEIVLAK PPDKKRKERQ
AARQASRSTA YEDYYYHPPP RMPPPIRGRG RGGGRGGYGY PPDYYGYEDY YDDYYGYDYH
DYRGGYEDPY YGYDDGYAVR GRGGGRGGRG APPPPRGRGA PPPRGRAGYS QRGAPLGPPR
GSRGGRGGPA QQQRGRGSRG SRGNRGGNVG GKRKADGYNQ PDSKRRQTNN QQNWGSQPIA
QQPLQQGGDY SGNYGYNNDN QEFYQDTYGQ QWK
