ROA1_MOUSE
ID ROA1_MOUSE Reviewed; 320 AA.
AC P49312; P97312; Q3V269;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A1;
DE Short=hnRNP A1;
DE AltName: Full=HDP-1;
DE AltName: Full=Helix-destabilizing protein;
DE AltName: Full=Single-strand-binding protein;
DE AltName: Full=Topoisomerase-inhibitor suppressed;
DE AltName: Full=hnRNP core protein A1;
DE Contains:
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed;
GN Name=Hnrnpa1; Synonyms=Fli-2, Hnrpa1, Tis;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1406633; DOI=10.1128/mcb.12.10.4449-4455.1992;
RA Ben-David Y., Bani M.R., Chabot B., de Koven A., Bernstein A.;
RT "Retroviral insertions downstream of the heterogeneous nuclear
RT ribonucleoprotein A1 gene in erythroleukemia cells: evidence that A1 is not
RT essential for cell growth.";
RL Mol. Cell. Biol. 12:4449-4455(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RX PubMed=8912629; DOI=10.1006/bbrc.1996.1609;
RA Onishi Y., Kizaki H.;
RT "Molecular cloning of the genes suppressed in RVC lymphoma cells by
RT topoisomerase inhibitors.";
RL Biochem. Biophys. Res. Commun. 228:7-13(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Amnion, Liver, Muellerian duct, Pancreas, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Limb, and Olfactory epithelium;
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 107-113 AND 285-300.
RC STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-22, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-194; ARG-206; ARG-218; ARG-225;
RP ARG-232; ARG-284 AND ARG-300, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
CC -!- FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles,
CC transport of poly(A) mRNA from the nucleus to the cytoplasm and
CC modulation of splice site selection. Plays a role in the splicing of
CC pyruvate kinase PKM by binding repressively to sequences flanking PKM
CC exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion
CC and production of the PKM M2 isoform. Binds to the IRES and thereby
CC inhibits the translation of the apoptosis protease activating factor
CC APAF1. May bind to specific miRNA hairpins.
CC {ECO:0000250|UniProtKB:P09651}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Identified in a
CC IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.
CC Interacts with SEPT6. Interacts with C9orf72. Interacts with KHDRBS1.
CC Interacts with UBQLN2 (By similarity). Interacts with PPIA/CYPA (By
CC similarity). {ECO:0000250|UniProtKB:P09651}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09651}. Cytoplasm
CC {ECO:0000250|UniProtKB:P09651}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. Shuttles continuously between
CC the nucleus and the cytoplasm along with mRNA. Component of
CC ribonucleosomes. {ECO:0000250|UniProtKB:P09651}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P49312-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P49312-2; Sequence=VSP_005825;
CC -!- PTM: Sumoylated. {ECO:0000250}.
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DR EMBL; M99167; AAA37633.1; -; mRNA.
DR EMBL; D86729; BAA13162.1; -; mRNA.
DR EMBL; D86728; BAA13161.1; -; mRNA.
DR EMBL; AK007802; BAB25267.1; -; mRNA.
DR EMBL; AK088308; BAC40273.1; -; mRNA.
DR EMBL; AK131999; BAE20929.1; -; mRNA.
DR EMBL; AK135391; BAE22518.1; -; mRNA.
DR EMBL; AK161730; BAE36552.1; -; mRNA.
DR EMBL; AK166901; BAE39104.1; -; mRNA.
DR EMBL; AK167161; BAE39302.1; -; mRNA.
DR EMBL; AK167810; BAE39837.1; -; mRNA.
DR EMBL; AK167913; BAE39920.1; -; mRNA.
DR EMBL; AK168420; BAE40333.1; -; mRNA.
DR EMBL; AK168531; BAE40409.1; -; mRNA.
DR EMBL; BC080675; AAH80675.1; -; mRNA.
DR EMBL; BC083136; AAH83136.1; -; mRNA.
DR CCDS; CCDS37233.1; -. [P49312-1]
DR PIR; A44485; A44485.
DR RefSeq; NP_034577.1; NM_010447.5. [P49312-1]
DR AlphaFoldDB; P49312; -.
DR BMRB; P49312; -.
DR SMR; P49312; -.
DR BioGRID; 200357; 21.
DR IntAct; P49312; 13.
DR MINT; P49312; -.
DR STRING; 10090.ENSMUSP00000042658; -.
DR iPTMnet; P49312; -.
DR PhosphoSitePlus; P49312; -.
DR SwissPalm; P49312; -.
DR EPD; P49312; -.
DR jPOST; P49312; -.
DR MaxQB; P49312; -.
DR PaxDb; P49312; -.
DR PeptideAtlas; P49312; -.
DR PRIDE; P49312; -.
DR ProteomicsDB; 301633; -. [P49312-1]
DR ProteomicsDB; 301634; -. [P49312-2]
DR TopDownProteomics; P49312-1; -. [P49312-1]
DR Antibodypedia; 7969; 514 antibodies from 39 providers.
DR DNASU; 15382; -.
DR Ensembl; ENSMUST00000087351; ENSMUSP00000084609; ENSMUSG00000046434. [P49312-1]
DR Ensembl; ENSMUST00000230171; ENSMUSP00000155833; ENSMUSG00000046434. [P49312-1]
DR Ensembl; ENSMUST00000231141; ENSMUSP00000155311; ENSMUSG00000046434. [P49312-2]
DR GeneID; 15382; -.
DR KEGG; mmu:15382; -.
DR UCSC; uc007xxp.2; mouse. [P49312-1]
DR UCSC; uc011zrp.1; mouse. [P49312-2]
DR CTD; 3178; -.
DR MGI; MGI:104820; Hnrnpa1.
DR VEuPathDB; HostDB:ENSMUSG00000046434; -.
DR GeneTree; ENSGT00950000183123; -.
DR HOGENOM; CLU_012062_1_0_1; -.
DR InParanoid; P49312; -.
DR Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 15382; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Hnrnpa1; mouse.
DR PRO; PR:P49312; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P49312; protein.
DR Bgee; ENSMUSG00000046434; Expressed in cortical plate and 263 other tissues.
DR ExpressionAtlas; P49312; baseline and differential.
DR Genevisible; P49312; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:HGNC-UCL.
DR GO; GO:1990826; C:nucleoplasmic periphery of the nuclear pore complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISS:HGNC-UCL.
DR GO; GO:1990814; F:DNA/DNA annealing activity; ISO:MGI.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0033592; F:RNA strand annealing activity; ISO:MGI.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:HGNC-UCL.
DR GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
DR GO; GO:0061752; F:telomeric repeat-containing RNA binding; ISO:MGI.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IDA:MGI.
DR GO; GO:0035865; P:cellular response to potassium ion; ISO:MGI.
DR GO; GO:1903936; P:cellular response to sodium arsenite; ISS:UniProtKB.
DR GO; GO:1904577; P:cellular response to tunicamycin; ISO:MGI.
DR GO; GO:0051170; P:import into nucleus; ISS:HGNC-UCL.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051168; P:nuclear export; ISS:HGNC-UCL.
DR GO; GO:0045760; P:positive regulation of action potential; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0008380; P:RNA splicing; IDA:MGI.
DR CDD; cd12761; RRM1_hnRNPA1; 1.
DR CDD; cd12580; RRM2_hnRNPA1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR021662; HnRNPA1_C.
DR InterPro; IPR034845; hnRNPA1_RRM1.
DR InterPro; IPR034803; hnRNPA1_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF11627; HnRNPA1; 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; Spliceosome; Transport; Ubl conjugation.
FT CHAIN 1..320
FT /note="Heterogeneous nuclear ribonucleoprotein A1"
FT /id="PRO_0000424511"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CHAIN 2..320
FT /note="Heterogeneous nuclear ribonucleoprotein A1, N-
FT terminally processed"
FT /id="PRO_0000081830"
FT DOMAIN 14..97
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 105..184
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 4..94
FT /note="Globular A domain"
FT REGION 95..185
FT /note="Globular B domain"
FT REGION 182..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..240
FT /note="RNA-binding RGG-box"
FT REGION 268..305
FT /note="Nuclear targeting sequence"
FT /evidence="ECO:0000250"
FT REGION 274..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 2
FT /note="N-acetylserine; in Heterogeneous nuclear
FT ribonucleoprotein A1, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 3
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 194
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09867"
FT MOD_RES 194
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 194
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 206
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 206
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 206
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 218
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 218
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 225
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 225
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 225
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 232
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04256"
FT MOD_RES 232
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 284
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 298
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 300
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 310
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 311
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 312
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT MOD_RES 318
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09651"
FT VAR_SEQ 252..303
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_005825"
SQ SEQUENCE 320 AA; 34196 MW; 59485C9FA1FF8AE1 CRC64;
MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN TKRSRGFGFV
TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA HLTVKKIFVG GIKEDTEEHH
LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA
LSKQEMASAS SSQRGRSGSG NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS
GDGYNGFGND GSNFGGGGSY NDFGNYNNQS SNFGPMKGGN FGGRSSGPYG GGGQYFAKPR
NQGGYGGSSS SSSYGSGRRF
