ROA2_RAT
ID ROA2_RAT Reviewed; 353 AA.
AC A7VJC2; A7VJC1; A7VJC3; A7VJC4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Heterogeneous nuclear ribonucleoproteins A2/B1 {ECO:0000312|EMBL:BAF79676.1};
DE Short=hnRNP A2/B1;
GN Name=Hnrnpa2b1 {ECO:0000250|UniProtKB:P22626};
GN Synonyms=Hnrnp {ECO:0000312|EMBL:BAF79676.1},
GN Hnrpa2b1 {ECO:0000250|UniProtKB:P22626};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A2; B1; A2B AND B1B), SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9925756; DOI=10.1006/excr.1998.4323;
RA Kamma H., Horiguchi H., Wan L., Matsui M., Fuiwara M., Fujimoto M.,
RA Yazawa T., Dreyfuss G.;
RT "Molecular characterization of the hnRNP A2/B1 proteins: tissue-specific
RT expression and novel isoforms.";
RL Exp. Cell Res. 246:399-411(1999).
RN [2]
RP PROTEIN SEQUENCE OF 100-113; 116-137 AND 2014-226, FUNCTION, RNA-BINDING,
RP AND SUBCELLULAR LOCATION.
RX PubMed=9578590; DOI=10.1021/bi9800247;
RA Hoek K.S., Kidd G.J., Carson J.H., Smith R.;
RT "hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin
RT basic protein mRNA.";
RL Biochemistry 37:7021-7029(1998).
RN [3]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=10567417; DOI=10.1074/jbc.274.48.34389;
RA Munro T.P., Magee R.J., Kidd G.J., Carson J.H., Barbarese E., Smith L.M.,
RA Smith R.;
RT "Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2
RT response element for RNA trafficking.";
RL J. Biol. Chem. 274:34389-34395(1999).
RN [4]
RP METHYLATION.
RX PubMed=10772824; DOI=10.1006/excr.2000.4827;
RA Nichols R.C., Wang X.W., Tang J., Hamilton B.J., High F.A., Herschman H.R.,
RA Rigby W.F.;
RT "The RGG domain in hnRNP A2 affects subcellular localization.";
RL Exp. Cell Res. 256:522-532(2000).
RN [5]
RP FUNCTION.
RX PubMed=15659580; DOI=10.1093/nar/gki203;
RA Moran-Jones K., Wayman L., Kennedy D.D., Reddel R.R., Sara S., Snee M.J.,
RA Smith R.;
RT "hnRNP A2, a potential ssDNA/RNA molecular adapter at the telomere.";
RL Nucleic Acids Res. 33:486-496(2005).
RN [6]
RP REVIEW.
RX PubMed=19099192; DOI=10.1007/s00018-008-8532-1;
RA He Y., Smith R.;
RT "Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B.";
RL Cell. Mol. Life Sci. 66:1239-1256(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
RN [8]
RP SUBCELLULAR LOCATION (ISOFORMS B1; A2; A2B AND B1B).
RX PubMed=20406423; DOI=10.1111/j.1600-0854.2010.01072.x;
RA Han S.P., Friend L.R., Carson J.H., Korza G., Barbarese E., Maggipinto M.,
RA Hatfield J.T., Rothnagel J.A., Smith R.;
RT "Differential subcellular distributions and trafficking functions of hnRNP
RT A2/B1 spliceoforms.";
RL Traffic 11:886-898(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-259 AND SER-344, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP ACETYLATION AT MET-1, METHYLATION AT ARG-266, SUBCELLULAR LOCATION (ISOFORM
RP A2), AND MUTAGENESIS OF ARG-266.
RX PubMed=24098712; DOI=10.1371/journal.pone.0075669;
RA Friend L.R., Landsberg M.J., Nouwens A.S., Wei Y., Rothnagel J.A.,
RA Smith R.;
RT "Arginine methylation of hnRNP A2 does not directly govern its subcellular
RT localization.";
RL PLoS ONE 8:E75669-E75669(2013).
CC -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that
CC associates with nascent pre-mRNAs, packaging them into hnRNP particles.
CC The hnRNP particle arrangement on nascent hnRNA is non-random and
CC sequence-dependent and serves to condense and stabilize the transcripts
CC and minimize tangling and knotting. Packaging plays a role in various
CC processes such as transcription, pre-mRNA processing, RNA nuclear
CC export, subcellular location, mRNA translation and stability of mature
CC mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and
CC heterogeneous nuclear RNA in the nucleus (PubMed:19099192). Involved in
CC transport of specific mRNAs to the cytoplasm in oligodendrocytes and
CC neurons: acts by specifically recognizing and binding the A2RE (21
CC nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11
CC nucleotide oligonucleotide) sequence motifs present on some mRNAs, and
CC promotes their transport to the cytoplasm (PubMed:9578590,
CC PubMed:10567417). Specifically binds single-stranded telomeric DNA
CC sequences, protecting telomeric DNA repeat against endonuclease
CC digestion (PubMed:15659580). Also binds other RNA molecules, such as
CC primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-
CC methyladenosine (m6A) mark by specifically recognizing and binding a
CC subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing
CC pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8
CC to pri-miRNA transcripts. Involved in miRNA sorting into exosomes
CC following sumoylation, possibly by binding (m6A)-containing pre-miRNAs.
CC Acts as a regulator of efficiency of mRNA splicing, possibly by binding
CC to m6A-containing pre-mRNAs. Plays a role in the splicing of pyruvate
CC kinase PKM by binding repressively to sequences flanking PKM exon 9,
CC inhibiting exon 9 inclusion and resulting in exon 10 inclusion and
CC production of the PKM M2 isoform (By similarity). Also plays a role in
CC the activation of the innate immune response. Mechanistically, senses
CC the presence of viral DNA in the nucleus, homodimerizes and is
CC demethylated by JMJD6. In turn, translocates to the cytoplasm where it
CC activates the TBK1-IRF3 pathway, leading to interferon alpha/beta
CC production (By similarity). {ECO:0000250|UniProtKB:P22626,
CC ECO:0000269|PubMed:10567417, ECO:0000269|PubMed:15659580,
CC ECO:0000269|PubMed:9578590, ECO:0000303|PubMed:19099192}.
CC -!- SUBUNIT: Homodimer; dimerization is required for nucleocytoplasmic
CC translocation. Identified in the spliceosome C complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.
CC Interacts with IGF2BP1. Interacts with C9orf72. Interacts with DGCR8.
CC Interacts with TARDBP. Interacts with CKAP5. Interacts with TBK1.
CC Interacts with STING1. Interacts with SRC (By similarity). Interacts
CC with PPIA/CYPA (By similarity). {ECO:0000250|UniProtKB:P22626}.
CC -!- SUBCELLULAR LOCATION: [Isoform B1]: Nucleus
CC {ECO:0000269|PubMed:20406423}.
CC -!- SUBCELLULAR LOCATION: [Isoform A2]: Nucleus
CC {ECO:0000269|PubMed:20406423, ECO:0000269|PubMed:24098712}.
CC -!- SUBCELLULAR LOCATION: [Isoform A2b]: Cytoplasm
CC {ECO:0000269|PubMed:20406423}. Nucleus {ECO:0000269|PubMed:20406423}.
CC Note=Mainly localizes in the cytoplasm in neural cells.
CC {ECO:0000269|PubMed:20406423}.
CC -!- SUBCELLULAR LOCATION: [Isoform B1b]: Cytoplasm
CC {ECO:0000269|PubMed:20406423}. Nucleus {ECO:0000269|PubMed:20406423}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22626}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:9578590, ECO:0000269|PubMed:9925756}.
CC Cytoplasm {ECO:0000269|PubMed:9925756}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:P22626}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P22626}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. Component of ribonucleosomes.
CC Not found in the nucleolus. Found in exosomes following sumoylation.
CC {ECO:0000250|UniProtKB:P22626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000269|PubMed:9925756};
CC Name=B1 {ECO:0000303|PubMed:9925756};
CC IsoId=A7VJC2-1; Sequence=Displayed;
CC Name=A2 {ECO:0000303|PubMed:9925756};
CC IsoId=A7VJC2-2; Sequence=VSP_053031;
CC Name=A2b; Synonyms=B0a {ECO:0000303|PubMed:9925756};
CC IsoId=A7VJC2-3; Sequence=VSP_053031, VSP_053032;
CC Name=B1b; Synonyms=B0b {ECO:0000303|PubMed:9925756};
CC IsoId=A7VJC2-4; Sequence=VSP_053032;
CC -!- TISSUE SPECIFICITY: In the brain, isoform A2 and isoform B1 are
CC abundant in large ganglion-type neurons, such as Purkinje cells, and
CC are less abundant in neighboring glia cells. Isoform A2 is more
CC abundant than isoform B1 in brain. In testis, isoform A2 and isoform B1
CC are present in spermatogonia and spermatocytes, but not in spermatids
CC or sperm. Isoform A2 is more abundant in the adrenal medulla than in
CC the cortical cells. Isoform B1 is found in both adrenal medulla and
CC cortical cells. Isoform A2 is more abundant than isoform B1 in the
CC adrenal gland. Isoform A2 and isoform B1 are both detected in pancreas
CC and kidney, and at lower levels in heart and lung. Isoform B1 is more
CC abundant than isoform A2 in heart, lung and intestine (at protein
CC level). Isoform A2b and isoform B1b are testis-specific.
CC {ECO:0000269|PubMed:9925756}.
CC -!- DOMAIN: The disordered region, when incubated at high concentration, is
CC able to polymerize into labile, amyloid-like fibers and form cross-beta
CC polymerization structures, probably driving the formation of hydrogels.
CC In contrast to irreversible, pathogenic amyloids, the fibers
CC polymerized from LC regions disassemble upon dilution. A number of
CC evidence suggests that formation of cross-beta structures by LC regions
CC mediate the formation of RNA granules, liquid-like droplets, and
CC hydrogels. {ECO:0000250|UniProtKB:P22626}.
CC -!- PTM: Asymmetric dimethylation at Arg-266 constitutes the major
CC methylation site (PubMed:24098712). According to a report, methylation
CC affects subcellular location and promotes nuclear localization
CC (PubMed:10772824). According to another report, methylation at Arg-266
CC does not influence nucleocytoplasmic shuttling (PubMed:24098712).
CC {ECO:0000269|PubMed:10772824, ECO:0000269|PubMed:24098712}.
CC -!- PTM: Sumoylated in exosomes, promoting miRNAs-binding.
CC {ECO:0000250|UniProtKB:P22626}.
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DR EMBL; AB006815; BAF79675.1; -; mRNA.
DR EMBL; AB006816; BAF79676.1; -; mRNA.
DR EMBL; AB006817; BAF79677.1; -; mRNA.
DR EMBL; AB006818; BAF79678.1; -; mRNA.
DR RefSeq; NP_001098083.1; NM_001104613.1. [A7VJC2-1]
DR AlphaFoldDB; A7VJC2; -.
DR SMR; A7VJC2; -.
DR BioGRID; 263391; 6.
DR IntAct; A7VJC2; 7.
DR MINT; A7VJC2; -.
DR STRING; 10116.ENSRNOP00000015152; -.
DR iPTMnet; A7VJC2; -.
DR SwissPalm; A7VJC2; -.
DR jPOST; A7VJC2; -.
DR PaxDb; A7VJC2; -.
DR PeptideAtlas; A7VJC2; -.
DR PRIDE; A7VJC2; -.
DR GeneID; 362361; -.
DR KEGG; rno:362361; -.
DR UCSC; RGD:1310403; rat. [A7VJC2-1]
DR CTD; 3181; -.
DR RGD; 1310403; Hnrnpa2b1.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; A7VJC2; -.
DR OrthoDB; 1202220at2759; -.
DR PhylomeDB; A7VJC2; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:A7VJC2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015030; C:Cajal body; IDA:BHF-UCL.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0000785; C:chromatin; IDA:RGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:RGD.
DR GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:1990715; F:mRNA CDS binding; IDA:RGD.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; ISO:RGD.
DR GO; GO:0001069; F:regulatory region RNA binding; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; IDA:RGD.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA:BHF-UCL.
DR GO; GO:0030324; P:lung development; IEP:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:1990428; P:miRNA transport; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; ISO:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
DR GO; GO:1905663; P:positive regulation of telomerase RNA reverse transcriptase activity; IDA:BHF-UCL.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; IDA:BHF-UCL.
DR GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
DR GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD.
DR GO; GO:0050658; P:RNA transport; IMP:RGD.
DR GO; GO:0016233; P:telomere capping; IDA:UniProtKB.
DR CDD; cd12762; RRM1_hnRNPA2B1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034489; hnRNP_A2/B1.
DR InterPro; IPR034486; hnRNPA2B1_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR48026:SF13; PTHR48026:SF13; 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; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding; Secreted; Spliceosome; Transport;
KW Ubl conjugation.
FT CHAIN 1..353
FT /note="Heterogeneous nuclear ribonucleoproteins A2/B1"
FT /id="PRO_0000365101"
FT DOMAIN 21..104
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 112..191
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 193..353
FT /note="Disordered"
FT /evidence="ECO:0000269|PubMed:24098712"
FT REGION 308..347
FT /note="Nuclear targeting sequence"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOTIF 9..15
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P22626, ECO:0000255"
FT COMPBIAS 191..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:24098712"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 38
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88569"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 104
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 168
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 173
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 203
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88569"
FT MOD_RES 203
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 203
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 213
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88569"
FT MOD_RES 213
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 213
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 228
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 238
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 266
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:24098712"
FT MOD_RES 266
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 325
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 331
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 347
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT MOD_RES 350
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P22626"
FT VAR_SEQ 3..14
FT /note="Missing (in isoform A2 and isoform A2b)"
FT /evidence="ECO:0000303|PubMed:9925756"
FT /id="VSP_053031"
FT VAR_SEQ 254..293
FT /note="Missing (in isoform A2b and isoform B1b)"
FT /evidence="ECO:0000303|PubMed:9925756"
FT /id="VSP_053032"
FT MUTAGEN 266
FT /note="R->A: Decreased methylation. Does not affect
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:24098712"
SQ SEQUENCE 353 AA; 37478 MW; 1C2E7BA8C8E98D6E CRC64;
MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC VVMRDPASKR
SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE ESGKPGAHVT VKKLFVGGIK
EDTEEHHLRD YFEEYGKIDT IEIITDRQSG KKRGFGFVTF DDHDPVDKIF LQKYHTINGH
NAEVRKALSR QEMQEVQSSR SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF
GDGYNGYGGG PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGNY
NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR SRY
