ID   ELAV1_MOUSE             Reviewed;         326 AA.
AC   P70372; Q60745; Q78QY3;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   02-SEP-2026, entry version 194.
DE   RecName: Full=ELAV-like protein 1;
DE   AltName: Full=Elav-like generic protein;
DE   AltName: Full=Hu-antigen R;
DE            Short=HuR;
DE   AltName: Full=MelG;
GN   Name=Elavl1; Synonyms=Elra, Hua;
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], AND SUBCELLULAR LOCATION.
RC   TISSUE=Brain, and Spleen;
RX   PubMed=9763509; DOI=10.1242/jcs.111.21.3145;
RA   Atasoy U., Watson J., Patel D., Keene J.D.;
RT   "ELAV protein HuA (HuR) can redistribute between nucleus and cytoplasm and
RT   is upregulated during serum stimulation and T cell activation.";
RL   J. Cell Sci. 111:3145-3156(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 119-292.
RC   TISSUE=Brain;
RX   PubMed=7753842; DOI=10.1073/pnas.92.10.4557;
RA   Good P.J.;
RT   "A conserved family of elav-like genes in vertebrates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:4557-4561(1995).
RN   [5]
RP   METHYLATION AT ARG-217.
RX   PubMed=12237300; DOI=10.1074/jbc.m206187200;
RA   Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W.,
RA   Stallcup M.R., Laird-Offringa I.A.;
RT   "Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing
RT   protein, by CARM1. Coactivator-associated arginine methyltransferase.";
RL   J. Biol. Chem. 277:44623-44630(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [7]
RP   FUNCTION IN MRNA LOCALIZATION, INTERACTION WITH ZNF385A, AND RNA-BINDING.
RX   PubMed=21402775; DOI=10.1128/mcb.01424-10;
RA   Nakamura H., Kawagishi H., Watanabe A., Sugimoto K., Maruyama M.,
RA   Sugimoto M.;
RT   "Cooperative role of the RNA-binding proteins Hzf and HuR in p53
RT   activation.";
RL   Mol. Cell. Biol. 31:1997-2009(2011).
RN   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-206 AND ARG-217, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [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).
RN   [9]
RP   FUNCTION, AND RNA-BINDING.
RX   PubMed=24394384; DOI=10.1038/ncb2902;
RA   Wang Y., Li Y., Toth J.I., Petroski M.D., Zhang Z., Zhao J.C.;
RT   "N-methyladenosine modification destabilizes developmental regulators in
RT   embryonic stem cells.";
RL   Nat. Cell Biol. 16:191-198(2014).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=27616329; DOI=10.1016/j.bbalip.2016.09.006;
RA   Nishino T., Matsunaga R., Jikihara H., Uchida M., Maeda A., Qi G., Abe T.,
RA   Kiyonari H., Tashiro S., Inagaki-Ohara K., Shimamoto F., Konishi H.;
RT   "Antagonizing effect of CLPABP on the function of HuR as a regulator of
RT   ARE-containing leptin mRNA stability and the effect of its depletion on
RT   obesity in old male mouse.";
RL   Biochim. Biophys. Acta 1861:1816-1827(2016).
CC   -!- FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs
CC       and increases their stability. Involved in embryonic stem cell (ESC)
CC       differentiation: preferentially binds mRNAs that are not methylated by
CC       N6-methyladenosine (m6A), stabilizing them, promoting ESC
CC       differentiation (PubMed:24394384). Has also been shown to be capable of
CC       binding to m6A-containing mRNAs and contributes to MYC stability by
CC       binding to m6A-containing MYC mRNAs (By similarity). Binds to poly-U
CC       elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs.
CC       Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs.
CC       In the case of the FOS AU-rich element, binds to a core element of 27
CC       nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds
CC       preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro (By similarity).
CC       With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their
CC       nuclear export induced by CDKN2A. Hence, may regulate p53/TP53
CC       expression and mediate in part the CDKN2A anti-proliferative activity.
CC       May also bind with ZNF385A the CCNB1 mRNA (PubMed:21402775). Increases
CC       the stability of the leptin mRNA harboring an AU-rich element (ARE) in
CC       its 3' UTR (PubMed:27616329). {ECO:0000250|UniProtKB:Q15717,
CC       ECO:0000269|PubMed:21402775, ECO:0000269|PubMed:24394384,
CC       ECO:0000269|PubMed:27616329}.
CC   -!- SUBUNIT: Monomer and homodimer (in vitro). Interacts with ANP32A (By
CC       similarity). Interacts with ZNF385A; the interaction is indirect and
CC       mRNA-dependent and may regulate p53/TP53 expression (PubMed:21402775).
CC       Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1,
CC       HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
CC       YBX1. Interacts with AGO1 and AGO2. Interacts with IGF2BP1. Interacts
CC       with IGF2BP2 and IGF2BP3. Interacts with HNRNPL (By similarity).
CC       Interacts with DHX36; this interaction occurs in a RNA-dependent
CC       manner. Interacts with ILF3; this interaction occurs in a RNA-dependent
CC       manner (By similarity). Interacts with PLEKHN1 (By similarity).
CC       Interacts with SHFL; the interaction increases in presence of RNA (By
CC       similarity). Interacts with YBX1; interaction recruits ELAVL1 on C5-
CC       methylcytosine (m5C)-containing mRNAs, thereby promoting mRNA stability
CC       (By similarity). Interacts with FXR1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q15717, ECO:0000269|PubMed:21402775}.
CC   -!- INTERACTION:
CC       P70372; Q03160: Grb7; NbExp=7; IntAct=EBI-6877056, EBI-7100053;
CC       P70372; Q80ZW7: Tia1; NbExp=2; IntAct=EBI-6877056, EBI-7809240;
CC       P70372; P62960: Ybx1; NbExp=5; IntAct=EBI-6877056, EBI-529779;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9763509}. Nucleus
CC       {ECO:0000269|PubMed:9763509}. Cytoplasm, Stress granule
CC       {ECO:0000269|PubMed:27616329}. Cytoplasm, P-body
CC       {ECO:0000250|UniProtKB:Q15717}. Note=Translocates into the cytoplasm
CC       following phosphorylation by MAPKAPK2. Likewise, phosphorylation by
CC       PRKCD promotes translocation from the nucleus into the cytoplasm, where
CC       it is associated with free and cytoskeleton-bound polysomes (By
CC       similarity). Localizes to the stress granules in the presence of
CC       PLEKHN1. {ECO:0000250|UniProtKB:Q15717, ECO:0000269|PubMed:27616329}.
CC   -!- DOMAIN: The first RRM (RNA recognition motif) domain is essential for
CC       binding to AU-rich elements. {ECO:0000250|UniProtKB:Q15717}.
CC   -!- PTM: Phosphorylated by MAPKAPK2. Phosphorylated by PRKCD.
CC       {ECO:0000250|UniProtKB:Q15717}.
CC   -!- PTM: Methylated at Arg-217 by CARM1 in T-cells in response to LPS
CC       challenge. {ECO:0000269|PubMed:12237300}.
CC   -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000305}.
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DR   EMBL; U65735; AAB17967.1; -; mRNA.
DR   EMBL; AK080365; BAC37892.1; -; mRNA.
DR   EMBL; CH466566; EDL21996.1; -; Genomic_DNA.
DR   EMBL; CH466566; EDL21997.1; -; Genomic_DNA.
DR   EMBL; U17595; AAA96941.1; -; mRNA.
DR   CCDS; CCDS22084.1; -.
DR   PIR; I49144; I49144.
DR   RefSeq; NP_034615.2; NM_010485.3.
DR   RefSeq; XP_006508761.1; XM_006508698.5.
DR   RefSeq; XP_030099161.1; XM_030243301.2.
DR   RefSeq; XP_030099162.1; XM_030243302.2.
DR   AlphaFoldDB; P70372; -.
DR   SMR; P70372; -.
DR   BioGRID; 200482; 47.
DR   CORUM; P70372; -.
DR   DIP; DIP-46480N; -.
DR   FunCoup; P70372; 4222.
DR   IntAct; P70372; 38.
DR   MINT; P70372; -.
DR   STRING; 10090.ENSMUSP00000096549; -.
DR   GlyGen; P70372; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P70372; -.
DR   PhosphoSitePlus; P70372; -.
DR   SwissPalm; P70372; -.
DR   jPOST; P70372; -.
DR   PaxDb; 10090-ENSMUSP00000096549; -.
DR   PeptideAtlas; P70372; -.
DR   ProteomicsDB; 275522; -.
DR   Pumba; P70372; -.
DR   TopDownProteomics; P70372; -.
DR   Antibodypedia; 3933; 503 antibodies from 40 providers.
DR   DNASU; 15568; -.
DR   Ensembl; ENSMUST00000098950.6; ENSMUSP00000096549.5; ENSMUSG00000040028.11.
DR   Ensembl; ENSMUST00000209010.2; ENSMUSP00000146866.2; ENSMUSG00000040028.11.
DR   GeneID; 15568; -.
DR   KEGG; mmu:15568; -.
DR   UCSC; uc009kts.1; mouse.
DR   AGR; MGI:1100851; -.
DR   CTD; 1994; -.
DR   MGI; MGI:1100851; Elavl1.
DR   VEuPathDB; HostDB:ENSMUSG00000040028; -.
DR   eggNOG; KOG0145; Eukaryota.
DR   GeneTree; ENSGT00940000155528; -.
DR   HOGENOM; CLU_026186_2_2_1; -.
DR   InParanoid; P70372; -.
DR   OMA; NQMRYNN; -.
DR   OrthoDB; 266020at2759; -.
DR   PhylomeDB; P70372; -.
DR   Reactome; R-MMU-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR   BioGRID-ORCS; 15568; 21 hits in 83 CRISPR screens.
DR   PRO; PR:P70372; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P70372; protein.
DR   Bgee; ENSMUSG00000040028; Expressed in endocardial cushion and 286 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IPI:MGI.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005730; C:nucleolus; ISO:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR   GO; GO:0106222; F:lncRNA binding; IDA:MGI.
DR   GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; ISO:GO_Central.
DR   GO; GO:0140517; F:protein-RNA adaptor activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; ISO:GO_Central.
DR   GO; GO:0000512; P:lncRNA-mediated post-transcriptional gene silencing; IMP:FlyBase.
DR   GO; GO:0061157; P:mRNA destabilization; ISO:GO_Central.
DR   GO; GO:0048255; P:mRNA stabilization; IDA:CACAO.
DR   GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR   GO; GO:0045772; P:positive regulation of autophagosome size; ISO:GO_Central.
DR   GO; GO:0010508; P:positive regulation of autophagy; ISO:GO_Central.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:GO_Central.
DR   GO; GO:0045727; P:positive regulation of translation; IDA:MGI.
DR   GO; GO:0016441; P:post-transcriptional gene silencing; IDA:ARUK-UCL.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:CACAO.
DR   GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB.
DR   GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR   CDD; cd12769; RRM1_HuR; 1.
DR   CDD; cd12773; RRM2_HuR; 1.
DR   CDD; cd12653; RRM3_HuR; 1.
DR   FunFam; 3.30.70.330:FF:000006; ELAV-like 3; 1.
DR   FunFam; 3.30.70.330:FF:000005; ELAV-like protein; 1.
DR   FunFam; 3.30.70.330:FF:000215; ELAV-like protein; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR006548; ELAD_HU_SF.
DR   InterPro; IPR002343; Hud_Sxl_RNA.
DR   InterPro; IPR034996; HuR_RRM2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   NCBIfam; TIGR01661; ELAV_HUD_SF; 1.
DR   PANTHER; PTHR10352; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT G; 1.
DR   Pfam; PF00076; RRM_1; 3.
DR   PRINTS; PR00961; HUDSXLRNA.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q15717"
FT   CHAIN           2..326
FT                   /note="ELAV-like protein 1"
FT                   /id="PRO_0000081578"
FT   DOMAIN          20..98
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          106..186
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          244..322
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15717"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15717"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15717"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15717"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15717"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         206
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         217
FT                   /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT                   /evidence="ECO:0000269|PubMed:12237300"
FT   MOD_RES         217
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15717"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15717"
FT   CROSSLNK        191
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15717"
FT   CONFLICT        3
FT                   /note="N -> G (in Ref. 1; AAB17967)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="D -> G (in Ref. 1; AAB17967)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="N -> I (in Ref. 1; AAB17967 and 4; AAA96941)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="A -> S (in Ref. 1; AAB17967)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   326 AA;  36169 MW;  74A98DEE5B921AF6 CRC64;
     MSNGYEDHMA EDCRDDIGRT NLIVNYLPQN MTQEELRSLF SSIGEVESAK LIRDKVAGHS
     LGYGFVNYVT AKDAERAIST LNGLRLQSKT IKVSYARPSS EVIKDANLYI SGLPRTMTQK
     DVEDMFSRFG RIINSRVLVD QTTGLSRGVA FIRFDKRSEA EEAITSFNGH KPPGSSEPIT
     VKFAANPNQN KNMALLSQLY HSPARRFGGP VHHQAQRFRF SPMGVDHMSG ISGVNVPGNA
     SSGWCIFIYN LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM
     AIASLNGYRL GDKILQVSFK TNKSHK
//