(data stored in ACNUC10243 zone)

SWISSPROT: 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   30-AUG-2017, entry version 84.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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-
RT   specific 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,
RP   RNA-BINDING, 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
RT   myelin 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.,
RA   Smith L.M., 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.,
RA   Herschman H.R., 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.,
RA   Snee M.J., 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.,
RA   Maggipinto M., Hatfield J.T., Rothnagel J.A., Smith R.;
RT   "Differential subcellular distributions and trafficking functions of
RT   hnRNP A2/B1 spliceoforms.";
RL   Traffic 11:886-898(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-259 AND
RP   SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [10]
RP   ACETYLATION AT MET-1, METHYLATION AT ARG-266, SUBCELLULAR LOCATION
RP   (ISOFORM 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
RT   subcellular 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
CC       particles. The hnRNP particle arrangement on nascent hnRNA is non-
CC       random and sequence-dependent and serves to condense and stabilize
CC       the transcripts and minimize tangling and knotting. Packaging
CC       plays a role in various processes such as transcription, pre-mRNA
CC       processing, RNA nuclear export, subcellular location, mRNA
CC       translation and stability of mature mRNAs. Forms hnRNP particles
CC       with at least 20 other different hnRNP and heterogeneous nuclear
CC       RNA in the nucleus (PubMed:19099192). Involved in transport of
CC       specific mRNAs to the cytoplasm in oligodendrocytes and neurons:
CC       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,
CC       and 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
CC       as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the
CC       N6-methyladenosine (m6A) mark by specifically recognizing and
CC       binding a subset of nuclear m6A-containing pri-miRNAs. Binding to
CC       m6A-containing pri-miRNAs promotes pri-miRNA processing by
CC       enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in
CC       miRNA sorting into exosomes following sumoylation, possibly by
CC       binding (m6A)-containing pre-miRNAs. Acts as a regulator of
CC       efficiency of mRNA splicing, possibly by binding to m6A-containing
CC       pre-mRNAs (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: Identified in the spliceosome C complex. Identified in a
CC       IGF2BP1-dependent mRNP granule complex containing untranslated
CC       mRNAs. Interacts with IGF2BP1. Interacts with C9orf72. Interacts
CC       with DGCR8. Interacts with TARDBP. Interacts with CKAP5.
CC       {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
CC       {ECO:0000269|PubMed:20406423}. Note=Mainly localizes in the
CC       cytoplasm in neural cells. {ECO:0000269|PubMed:20406423}.
CC   -!- SUBCELLULAR LOCATION: Isoform B1b: Cytoplasm
CC       {ECO:0000269|PubMed:20406423}. Nucleus
CC       {ECO:0000269|PubMed:20406423}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:9578590, ECO:0000269|PubMed:9925756}.
CC       Cytoplasm {ECO:0000269|PubMed:9925756}. Cytoplasmic granule
CC       {ECO:0000250|UniProtKB:P22626}. Secreted, exosome
CC       {ECO:0000250|UniProtKB:P22626}. Note=Localized in cytoplasmic mRNP
CC       granules containing untranslated mRNAs. Component of
CC       ribonucleosomes. Not found in the nucleolus. Found in exosomes
CC       follwong sumoylation. {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,
CC       and are less abundant in neighboring glia cells. Isoform A2 is
CC       more abundant than isoform B1 in brain. In testis, isoform A2 and
CC       isoform B1 are present in spermatogonia and spermatocytes, but not
CC       in spermatids or sperm. Isoform A2 is more abundant in the adrenal
CC       medulla than in the cortical cells. Isoform B1 is found in both
CC       adrenal medulla and cortical cells. Isoform A2 is more abundant
CC       than isoform B1 in the adrenal gland. Isoform A2 and isoform B1
CC       are both detected in pancreas and kidney, and at lower levels in
CC       heart and lung. Isoform B1 is more abundant than isoform A2 in
CC       heart, lung and intestine (at protein level). Isoform A2b and
CC       isoform B1b are testis-specific. {ECO:0000269|PubMed:9925756}.
CC   -!- DOMAIN: The low complexity (LC) region is intrinsically
CC       disordered. When incubated at high concentration, it is able to
CC       polymerize into labile, amyloid-like fibers and form cross-beta
CC       polymerization structures, probably driving the formation of
CC       hydrogels. In contrast to irreversible, pathogenic amyloids, the
CC       fibers polymerized from LC regions disassemble upon dilution. A
CC       number of evidences suggest that formation of cross-beta
CC       structures by LC regions mediate the formation of RNA granules,
CC       liquid-like droplets, and hydrogels.
CC       {ECO:0000250|UniProtKB:P22626}.
CC   -!- PTM: Asymmetric dimethylation at Arg-266 constitutes the major
CC       methylation site (PubMed:24098712). According to a report,
CC       methylation affects subcellular location and promotes nuclear
CC       localization (PubMed:10772824). According to another report,
CC       methylation at Arg-266 does not influence nucleocytoplasmic
CC       shuttling (PubMed:24098712). {ECO:0000269|PubMed:10772824,
CC       ECO:0000269|PubMed:24098712}.
CC   -!- PTM: Sumoylated in exosomes, promoting miRNAs-binding.
CC       {ECO:0000250|UniProtKB:P22626}.
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   UniGene; Rn.233238; -.
DR   UniGene; Rn.4057; -.
DR   ProteinModelPortal; A7VJC2; -.
DR   SMR; A7VJC2; -.
DR   BioGrid; 263391; 2.
DR   STRING; 10116.ENSRNOP00000015152; -.
DR   iPTMnet; A7VJC2; -.
DR   SwissPalm; 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   eggNOG; COG0724; LUCA.
DR   HOGENOM; HOG000234442; -.
DR   HOVERGEN; HBG108415; -.
DR   InParanoid; A7VJC2; -.
DR   KO; K13158; -.
DR   PhylomeDB; A7VJC2; -.
DR   PRO; PR:A7VJC2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0015030; C:Cajal body; IDA:BHF-UCL.
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:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
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:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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: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:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
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   InterPro; IPR034489; hnRNP_A2/B1.
DR   InterPro; IPR034486; hnRNPA2B1_RRM1.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR24012:SF539; PTHR24012:SF539; 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;
DR   PRODOM; A7VJC2.
DR   SWISS-2DPAGE; A7VJC2.
KW   Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Isopeptide bond; Methylation;
KW   mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW   RNA-binding; Secreted; Spliceosome; Transport; Ubl conjugation.
FT   CHAIN         1    353       Heterogeneous nuclear ribonucleoproteins
FT                                A2/B1.
FT                                /FTId=PRO_0000365101.
FT   DOMAIN       21    104       RRM 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   DOMAIN      112    191       RRM 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   REGION      193    353       Low complexity (LC) region.
FT                                {ECO:0000269|PubMed:24098712}.
FT   REGION      308    347       Nuclear targeting sequence.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOTIF         9     15       Nuclear localization signal.
FT                                {ECO:0000250|UniProtKB:P22626,
FT                                ECO:0000255}.
FT   COMPBIAS    202    349       Gly-rich. {ECO:0000255}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000269|PubMed:24098712}.
FT   MOD_RES       4      4       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES      29     29       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES      38     38       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:O88569}.
FT   MOD_RES      85     85       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     104    104       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     140    140       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     149    149       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     159    159       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     168    168       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     173    173       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     176    176       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     189    189       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     201    201       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     203    203       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:O88569}.
FT   MOD_RES     203    203       Dimethylated arginine; alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     203    203       Omega-N-methylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     212    212       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     213    213       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:O88569}.
FT   MOD_RES     213    213       Dimethylated arginine; alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     213    213       Omega-N-methylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     225    225       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     228    228       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     231    231       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     236    236       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     238    238       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     259    259       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     266    266       Asymmetric dimethylarginine; alternate.
FT                                {ECO:0000269|PubMed:24098712}.
FT   MOD_RES     266    266       Omega-N-methylarginine; alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     324    324       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     325    325       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     331    331       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     341    341       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     344    344       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     347    347       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   MOD_RES     350    350       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   CROSSLNK     22     22       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   CROSSLNK    104    104       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   CROSSLNK    112    112       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   CROSSLNK    120    120       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   CROSSLNK    137    137       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   CROSSLNK    152    152       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   CROSSLNK    168    168       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   CROSSLNK    173    173       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   CROSSLNK    186    186       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P22626}.
FT   VAR_SEQ       3     14       Missing (in isoform A2 and isoform A2b).
FT                                {ECO:0000303|PubMed:9925756}.
FT                                /FTId=VSP_053031.
FT   VAR_SEQ     254    293       Missing (in isoform A2b and isoform B1b).
FT                                {ECO:0000303|PubMed:9925756}.
FT                                /FTId=VSP_053032.
FT   MUTAGEN     266    266       R->A: Decreased methylation. Does not
FT                                affect subcellular location.
FT                                {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
//

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