ILF3_MOUSE
ID ILF3_MOUSE Reviewed; 898 AA.
AC Q9Z1X4; Q80VD5; Q812A1; Q8BP80; Q8C2H8; Q8K588;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Interleukin enhancer-binding factor 3;
GN Name=Ilf3;
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 [GENOMIC DNA] (ISOFORM 1).
RX PubMed=7519613; DOI=10.1016/s0021-9258(17)32048-3;
RA Kao P.N., Chen L., Brock G., Ng J., Kenny J., Smith A.J., Corthesy B.;
RT "Cloning and expression of cyclosporin A- and FK506-sensitive nuclear
RT factor of activated T-cells: NF45 and NF90.";
RL J. Biol. Chem. 269:20691-20699(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHARACTERIZATION.
RC TISSUE=Testis;
RX PubMed=10337617; DOI=10.1007/s003359901022;
RA Buaas F.W., Lee K., Edelhoff S., Disteche C., Braun R.E.;
RT "Cloning and characterization of the mouse interleukin enhancer binding
RT factor 3 (Ilf3) homolog in a screen for RNA binding proteins.";
RL Mamm. Genome 10:451-456(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RA Gasmi L., Viranaicken W., Denoulet P., Larcher J.-C.;
RT "Alternative splicing generates two mRNA transcripts of mouse interleukin
RT enhancer binding factor 3 (Ilf3).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-516 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 549-898.
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [6]
RP PROTEIN SEQUENCE OF 163-176; 421-434; 614-628 AND 853-867.
RX PubMed=15364895; DOI=10.1096/fj.04-1763fje;
RA Larcher J.-C., Gasmi L., Viranaicken W., Edde B., Bernard R., Ginzburg I.,
RA Denoulet P.;
RT "Ilf3 and NF90 associate with the axonal targeting element of Tau mRNA.";
RL FASEB J. 18:1761-1763(2004).
RN [7]
RP IDENTIFICATION BY MASS 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-67; SER-190; SER-482 AND
RP SER-486, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-188 AND THR-315.
RX PubMed=21123651; DOI=10.1101/gad.1965010;
RA Harashima A., Guettouche T., Barber G.N.;
RT "Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase
RT PKR constitutes a novel mechanism of translational regulation and cellular
RT defense.";
RL Genes Dev. 24:2640-2653(2010).
CC -!- FUNCTION: RNA-binding protein that plays an essential role in the
CC biogenesis of circular RNAs (circRNAs) which are produced by back-
CC splicing circularization of pre-mRNAs. Within the nucleus, promotes
CC circRNAs processing by stabilizing the regulatory elements residing in
CC the flanking introns of the circularized exons. Plays thereby a role in
CC the back-splicing of a subset of circRNAs. As a consequence,
CC participates in a wide range of transcriptional and post-
CC transcriptional processes. Binds to poly-U elements and AU-rich
CC elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Upon
CC viral infection, ILF3 accumulates in the cytoplasm and participates in
CC the innate antiviral response. Mechanistically, ILF3 becomes
CC phosphorylated and activated by the double-stranded RNA-activated
CC protein kinase/PKR which releases ILF3 from cellular mature circRNAs.
CC In turn, unbound ILF3 molecules are able to interact with and thus
CC inhibit viral mRNAs. {ECO:0000250|UniProtKB:Q12906,
CC ECO:0000269|PubMed:21123651}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with FUS and SMN. Interacts
CC (via C-terminus) with PRMT1. Forms a complex with ILF2. Can also bind
CC to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and
CC the heterodimeric complex of XRCC6/KU70 and XRCC5/KU80. Forms a
CC heteromeric complex with ZNF346 and ILF3. Found in a nuclear export
CC complex with XPO5, ILF3, Ran and double-stranded RNA or double-stranded
CC minihelix VA1 RNA. Found in a nuclear export complex with XPO5, RAN,
CC ILF3, ZNF346 and double-stranded RNA. Interacts with XPO5 and ZNF346.
CC Forms a complex with ILF2, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA.
CC Interacts with AGO1 and AGO2. Interacts with DHX36; this interaction
CC occurs in a RNA-dependent manner. Interacts with ELAVL1; this
CC interaction occurs in a RNA-dependent manner. Interacts with HAVCR2;
CC this interaction promotes ILF3 ubiquitination and subsequent
CC degradation (By similarity). {ECO:0000250|UniProtKB:Q12906}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q12906}. Cytoplasm
CC {ECO:0000269|PubMed:21123651}. Nucleus {ECO:0000269|PubMed:21123651}.
CC Note=Localizes in the cytoplasm in response to viral infection. The
CC unphosphorylated form is retained in the nucleus by ILF2.
CC Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2
CC from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of
CC ILF3. Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000269|PubMed:21123651}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Z1X4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z1X4-2; Sequence=VSP_013406, VSP_013407, VSP_013408;
CC Name=3;
CC IsoId=Q9Z1X4-3; Sequence=VSP_013406;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the thymus,
CC testis, ovary and at lower levelss in the spleen.
CC -!- PTM: Phosphorylated at Thr-188 and Thr-315 by PKR in response to RNA
CC viruses. This phosphorylation results in the dissociation of ILF2 from
CC the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3
CC where it can bind to viral RNAs and impede viral replication.
CC {ECO:0000269|PubMed:21123651}.
CC -!- PTM: Methylated by protein arginine N-methyltransferase 1.
CC {ECO:0000250|UniProtKB:Q12906}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC71052.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC36863.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF506968; AAM34210.1; -; Genomic_DNA.
DR EMBL; AF098967; AAC71052.1; ALT_FRAME; mRNA.
DR EMBL; AF497751; AAO23054.1; -; mRNA.
DR EMBL; AF497752; AAO23055.1; -; mRNA.
DR EMBL; AK048096; BAC33239.1; -; mRNA.
DR EMBL; AK077560; BAC36863.1; ALT_FRAME; mRNA.
DR EMBL; AK088604; BAC40448.1; -; mRNA.
DR EMBL; BC047272; AAH47272.1; -; mRNA.
DR CCDS; CCDS40552.1; -. [Q9Z1X4-1]
DR CCDS; CCDS90512.1; -. [Q9Z1X4-2]
DR CCDS; CCDS90514.1; -. [Q9Z1X4-3]
DR RefSeq; NP_001036172.1; NM_001042707.2. [Q9Z1X4-1]
DR RefSeq; NP_001036173.1; NM_001042708.2. [Q9Z1X4-2]
DR RefSeq; NP_001264250.1; NM_001277321.1.
DR RefSeq; NP_001264251.1; NM_001277322.1. [Q9Z1X4-3]
DR RefSeq; NP_034691.2; NM_010561.3. [Q9Z1X4-3]
DR RefSeq; XP_006510094.1; XM_006510031.2. [Q9Z1X4-1]
DR PDB; 4AT7; X-ray; 1.90 A; B=1-381.
DR PDB; 4AT8; X-ray; 2.69 A; B/D=1-381.
DR PDB; 4AT9; X-ray; 2.80 A; B=1-381.
DR PDB; 4ATB; X-ray; 3.10 A; B/D=1-381.
DR PDB; 5DV7; X-ray; 3.50 A; C=4-701.
DR PDBsum; 4AT7; -.
DR PDBsum; 4AT8; -.
DR PDBsum; 4AT9; -.
DR PDBsum; 4ATB; -.
DR PDBsum; 5DV7; -.
DR AlphaFoldDB; Q9Z1X4; -.
DR SMR; Q9Z1X4; -.
DR BioGRID; 200648; 67.
DR IntAct; Q9Z1X4; 6.
DR MINT; Q9Z1X4; -.
DR STRING; 10090.ENSMUSP00000065770; -.
DR iPTMnet; Q9Z1X4; -.
DR PhosphoSitePlus; Q9Z1X4; -.
DR EPD; Q9Z1X4; -.
DR jPOST; Q9Z1X4; -.
DR MaxQB; Q9Z1X4; -.
DR PaxDb; Q9Z1X4; -.
DR PeptideAtlas; Q9Z1X4; -.
DR PRIDE; Q9Z1X4; -.
DR ProteomicsDB; 267328; -. [Q9Z1X4-1]
DR ProteomicsDB; 267329; -. [Q9Z1X4-2]
DR ProteomicsDB; 267330; -. [Q9Z1X4-3]
DR Antibodypedia; 1051; 360 antibodies from 37 providers.
DR DNASU; 16201; -.
DR Ensembl; ENSMUST00000067646; ENSMUSP00000065770; ENSMUSG00000032178. [Q9Z1X4-1]
DR Ensembl; ENSMUST00000213603; ENSMUSP00000149483; ENSMUSG00000032178. [Q9Z1X4-3]
DR Ensembl; ENSMUST00000214758; ENSMUSP00000151032; ENSMUSG00000032178. [Q9Z1X4-3]
DR Ensembl; ENSMUST00000216892; ENSMUSP00000149786; ENSMUSG00000032178. [Q9Z1X4-2]
DR GeneID; 16201; -.
DR KEGG; mmu:16201; -.
DR UCSC; uc009old.2; mouse. [Q9Z1X4-3]
DR UCSC; uc009ole.2; mouse. [Q9Z1X4-1]
DR CTD; 3609; -.
DR MGI; MGI:1339973; Ilf3.
DR VEuPathDB; HostDB:ENSMUSG00000032178; -.
DR eggNOG; KOG3792; Eukaryota.
DR GeneTree; ENSGT00940000156719; -.
DR InParanoid; Q9Z1X4; -.
DR OMA; YYQGGDN; -.
DR OrthoDB; 612611at2759; -.
DR PhylomeDB; Q9Z1X4; -.
DR TreeFam; TF320194; -.
DR BioGRID-ORCS; 16201; 12 hits in 75 CRISPR screens.
DR ChiTaRS; Ilf3; mouse.
DR PRO; PR:Q9Z1X4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9Z1X4; protein.
DR Bgee; ENSMUSG00000032178; Expressed in embryonic post-anal tail and 295 other tissues.
DR ExpressionAtlas; Q9Z1X4; baseline and differential.
DR Genevisible; Q9Z1X4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; IMP:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006479; P:protein methylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR DisProt; DP01562; -.
DR Gene3D; 3.30.460.10; -; 2.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR006561; DZF_dom.
DR InterPro; IPR033099; ILF3/NF90.
DR InterPro; IPR043519; NT_sf.
DR PANTHER; PTHR45762:SF4; PTHR45762:SF4; 3.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF07528; DZF; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00572; DZF; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51703; DZF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antiviral defense;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..898
FT /note="Interleukin enhancer-binding factor 3"
FT /id="PRO_0000126071"
FT DOMAIN 5..378
FT /note="DZF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT DOMAIN 398..467
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 524..590
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 52..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..898
FT /note="Interaction with PRMT1"
FT /evidence="ECO:0000250"
FT REGION 631..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 371..389
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 67..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT MOD_RES 188
FT /note="Phosphothreonine; by PKR"
FT /evidence="ECO:0000269|PubMed:21123651"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 315
FT /note="Phosphothreonine; by PKR"
FT /evidence="ECO:0000269|PubMed:21123651"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT MOD_RES 460
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 592
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT CROSSLNK 348
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT CROSSLNK 489
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12906"
FT VAR_SEQ 1
FT /note="M -> MALYHHHFITRRRR (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10337617,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|Ref.3"
FT /id="VSP_013406"
FT VAR_SEQ 689..703
FT /note="QFYSNGGHSGNAGGG -> DFFTDCYGYHDFGAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013407"
FT VAR_SEQ 704..898
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013408"
FT CONFLICT 796
FT /note="G -> C (in Ref. 2; AAC71052)"
FT /evidence="ECO:0000305"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 25..53
FT /evidence="ECO:0007829|PDB:4AT7"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:4AT7"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:4AT7"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4AT7"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:4AT7"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:4AT7"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4AT7"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:4AT7"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 200..219
FT /evidence="ECO:0007829|PDB:4AT7"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:4AT7"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:4AT7"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:4AT7"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:4AT9"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 308..326
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:4AT7"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:4AT7"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:5DV7"
FT STRAND 419..425
FT /evidence="ECO:0007829|PDB:5DV7"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:5DV7"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:5DV7"
FT STRAND 441..449
FT /evidence="ECO:0007829|PDB:5DV7"
FT HELIX 450..465
FT /evidence="ECO:0007829|PDB:5DV7"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:5DV7"
FT HELIX 528..535
FT /evidence="ECO:0007829|PDB:5DV7"
FT STRAND 542..547
FT /evidence="ECO:0007829|PDB:5DV7"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:5DV7"
FT STRAND 554..561
FT /evidence="ECO:0007829|PDB:5DV7"
FT STRAND 564..572
FT /evidence="ECO:0007829|PDB:5DV7"
FT HELIX 573..588
FT /evidence="ECO:0007829|PDB:5DV7"
SQ SEQUENCE 898 AA; 96021 MW; 171B31100D1181F7 CRC64;
MRPMRIFVND DRHVMAKHSS VYPTQEELEA VQNMVSHTER ALKAVSDWID EQEKGNSELS
EAENMDTPPD DESKEGAGEQ KAEHMTRTLR GVMRVGLVAK GLLLKGDLDL ELVLLCKEKP
TTALLDKVAD NLAIQLTTVT EDKYEILQSV DDAAIVIKNT KEPPLSLTIH LTSPVVREEM
EKVLAGETLS VNDPPDVLDR QKCLAALASL RHAKWFQARA NGLKSCVIVI RVLRDLCTRV
PTWGPLRGWP LELLCEKSIG TANRPMGAGE ALRRVLECLA SGIVMPDGSG IYDPCEKEAT
DAIGHLDRQQ REDITQSAQH ALRLAAFGQL HKVLGMDPLP SKMPKKPKNE NPVDYTVQIP
PSTTYAITPM KRPMEEDGEE KSPSKKKKKI QKKEEKADPP QAMNALMRLN QLKPGLQYKL
ISQTGPVHAP IFTMSVEVDG SNFEASGPSK KTAKLHVAVK VLQDMGLPTG AEGRDSSKGE
DSAEESDGKP AIVAPPPVVE AVSNPSSVFP SDATTEQGPI LTKHGKNPVM ELNEKRRGLK
YELISETGGS HDKRFVMEVE VDGQKFQGAG SNKKVAKAYA ALAALEKLFP DTPLALEANK
KKRTPVPVRG GPKFAAKPHN PGFGMGGPMH NEVPPPPNIR GRGRGGNIRG RGRGRGFGGA
NHGGGYMNAG AGYGSYGYSS NSATAGYSQF YSNGGHSGNA GGGGSGGGGG SSSYSSYYQG
DSYNSPVPPK HAGKKPLHGG QQKASYSSGY QSHQGQQQPY NQSQYSSYGT PQGKQKGYGH
GQGSYSSYSN SYNSPGGGGG SDYSYDSKFN YSGSGGRSGG NSYGSSGSSS YNTGSHGGYG
TGSGGSSSYQ GKQGGYSSQS NYSSPGSSQS YSGPASSYQS SQGGYSRNTE HSMNYQYR
