ID RB15B_HUMAN Reviewed; 890 AA. AC Q8NDT2; A4QPG7; Q6QE19; Q9BV96; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 3. DT 27-MAR-2024, entry version 183. DE RecName: Full=Putative RNA-binding protein 15B {ECO:0000305}; DE AltName: Full=One-twenty two protein 3 {ECO:0000303|PubMed:16129689, ECO:0000303|PubMed:19586903}; DE Short=HsOTT3 {ECO:0000303|PubMed:19586903}; DE Short=HuOTT3 {ECO:0000303|PubMed:16129689}; DE AltName: Full=RNA-binding motif protein 15B {ECO:0000303|PubMed:19586903}; GN Name=RBM15B {ECO:0000303|PubMed:16129689, ECO:0000303|PubMed:19586903, GN ECO:0000312|HGNC:HGNC:24303}; GN Synonyms=OTT3 {ECO:0000303|PubMed:16129689, GN ECO:0000303|PubMed:19586903}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Colon; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-890 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 633-780. RC TISSUE=Head; RA Sales M.M., Ferrasi A.C., Pereira A.A., Pardini M.I.M.C., Camargo A.A.; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION, INTERACTION WITH EPSTEIN-BARR VIRUS BMLF1 (MICROBIAL INFECTION) RP AND NCOR2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16129689; DOI=10.1074/jbc.m501725200; RA Hiriart E., Gruffat H., Buisson M., Mikaelian I., Keppler S., Meresse P., RA Mercher T., Bernard O.A., Sergeant A., Manet E.; RT "Interaction of the Epstein-Barr virus mRNA export factor EB2 with human RT Spen proteins SHARP, OTT1, and a novel member of the family, OTT3, links RT Spen proteins with splicing regulation and mRNA export."; RL J. Biol. Chem. 280:36935-36945(2005). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ALYREF AND NXF1. RX PubMed=19586903; DOI=10.1074/jbc.m109.040113; RA Uranishi H., Zolotukhin A.S., Lindtner S., Warming S., Zhang G.M., Bear J., RA Copeland N.G., Jenkins N.A., Pavlakis G.N., Felber B.K.; RT "The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the RT nuclear export receptor NXF1."; RL J. Biol. Chem. 284:26106-26116(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-552, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP FUNCTION. RX PubMed=21044963; DOI=10.1074/jbc.m110.192518; RA Loyer P., Busson A., Trembley J.H., Hyle J., Grenet J., Zhao W., RA Ribault C., Montier T., Kidd V.J., Lahti J.M.; RT "The RNA binding motif protein 15B (RBM15B/OTT3) is a functional competitor RT of serine-arginine (SR) proteins and antagonizes the positive effect of the RT CDK11p110-cyclin L2alpha complex on splicing."; RL J. Biol. Chem. 286:147-159(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-552 AND SER-562, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532; SER-556 AND SER-562, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-213 AND LYS-702, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [18] RP FUNCTION, RNA-BINDING, AND IDENTIFICATION IN THE WMM COMPLEX. RX PubMed=27602518; DOI=10.1038/nature19342; RA Patil D.P., Chen C.K., Pickering B.F., Chow A., Jackson C., Guttman M., RA Jaffrey S.R.; RT "m(6)A RNA methylation promotes XIST-mediated transcriptional repression."; RL Nature 537:369-373(2016). CC -!- FUNCTION: RNA-binding protein that acts as a key regulator of N6- CC methyladenosine (m6A) methylation of RNAs, thereby regulating different CC processes, such as alternative splicing of mRNAs and X chromosome CC inactivation mediated by Xist RNA (PubMed:16129689, PubMed:27602518). CC Associated component of the WMM complex, a complex that mediates N6- CC methyladenosine (m6A) methylation of RNAs, a modification that plays a CC role in the efficiency of mRNA splicing and RNA processing CC (PubMed:27602518). Plays a key role in m6A methylation, possibly by CC binding target RNAs and recruiting the WMM complex (PubMed:27602518). CC Involved in random X inactivation mediated by Xist RNA: acts by binding CC Xist RNA and recruiting the WMM complex, which mediates m6A CC methylation, leading to target YTHDC1 reader on Xist RNA and promoting CC transcription repression activity of Xist (PubMed:27602518). Functions CC in the regulation of alternative or illicit splicing, possibly by CC regulating m6A methylation (PubMed:16129689). Inhibits pre-mRNA CC splicing (PubMed:21044963). Also functions as a mRNA export factor by CC acting as a cofactor for the nuclear export receptor NXF1 CC (PubMed:19586903). {ECO:0000269|PubMed:19586903, CC ECO:0000269|PubMed:21044963, ECO:0000269|PubMed:27602518, CC ECO:0000305|PubMed:16129689}. CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex CC composed of a catalytic subcomplex, named MAC, and of an associated CC subcomplex, named MACOM (PubMed:27602518). The MAC subcomplex is CC composed of METTL3 and METTL14 (PubMed:27602518). The MACOM subcomplex CC is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of CC RBM15 (RBM15 or RBM15B) (PubMed:27602518). May interact with NCOR2 CC (PubMed:16129689). Interacts with NXF1, the interaction is required to CC promote mRNA export (PubMed:19586903). {ECO:0000269|PubMed:16129689, CC ECO:0000269|PubMed:19586903, ECO:0000269|PubMed:27602518}. CC -!- SUBUNIT: (Microbial infection) Interacts (via the SPOC domain) with CC Epstein-Barr virus BMLF1 (via the N-terminus); the interaction is CC direct. {ECO:0000269|PubMed:16129689}. CC -!- INTERACTION: CC Q8NDT2; Q8IVL1: NAV2; NbExp=3; IntAct=EBI-726721, EBI-741200; CC Q8NDT2-2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-10269922, EBI-396137; CC Q8NDT2-2; Q92997: DVL3; NbExp=3; IntAct=EBI-10269922, EBI-739789; CC Q8NDT2-2; Q8IVL1: NAV2; NbExp=3; IntAct=EBI-10269922, EBI-741200; CC Q8NDT2-2; O76024: WFS1; NbExp=3; IntAct=EBI-10269922, EBI-720609; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm CC {ECO:0000269|PubMed:16129689}. Nucleus speckle CC {ECO:0000269|PubMed:19586903}. Nucleus envelope CC {ECO:0000269|PubMed:19586903}. Note=Colocalizes with BMLF1 in the CC nucleus. Localized in the nucleoplasm with a granular staining pattern CC and excluded from the nucleoli. {ECO:0000269|PubMed:16129689}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8NDT2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NDT2-2; Sequence=VSP_053878; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:16129689}. CC -!- SIMILARITY: Belongs to the RRM Spen family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH01367.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAS50153.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305}; CC Sequence=CAD38547.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC092037; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001367; AAH01367.2; ALT_INIT; mRNA. DR EMBL; BC139836; AAI39837.1; -; mRNA. DR EMBL; AL831838; CAD38547.2; ALT_INIT; mRNA. DR EMBL; AY545557; AAS50153.1; ALT_SEQ; mRNA. DR CCDS; CCDS33764.1; -. [Q8NDT2-1] DR RefSeq; NP_037418.3; NM_013286.4. [Q8NDT2-1] DR AlphaFoldDB; Q8NDT2; -. DR SMR; Q8NDT2; -. DR BioGRID; 118943; 95. DR IntAct; Q8NDT2; 41. DR MINT; Q8NDT2; -. DR STRING; 9606.ENSP00000454545; -. DR GlyGen; Q8NDT2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8NDT2; -. DR PhosphoSitePlus; Q8NDT2; -. DR BioMuta; RBM15B; -. DR DMDM; 229463030; -. DR EPD; Q8NDT2; -. DR jPOST; Q8NDT2; -. DR MassIVE; Q8NDT2; -. DR MaxQB; Q8NDT2; -. DR PaxDb; 9606-ENSP00000454545; -. DR PeptideAtlas; Q8NDT2; -. DR ProteomicsDB; 73053; -. [Q8NDT2-1] DR Pumba; Q8NDT2; -. DR Antibodypedia; 59712; 75 antibodies from 18 providers. DR DNASU; 29890; -. DR Ensembl; ENST00000563281.2; ENSP00000454545.1; ENSG00000259956.2. [Q8NDT2-1] DR GeneID; 29890; -. DR KEGG; hsa:29890; -. DR MANE-Select; ENST00000563281.2; ENSP00000454545.1; NM_013286.5; NP_037418.3. DR UCSC; uc003dbd.4; human. [Q8NDT2-1] DR AGR; HGNC:24303; -. DR CTD; 29890; -. DR DisGeNET; 29890; -. DR GeneCards; RBM15B; -. DR HGNC; HGNC:24303; RBM15B. DR HPA; ENSG00000259956; Low tissue specificity. DR MIM; 612602; gene. DR neXtProt; NX_Q8NDT2; -. DR OpenTargets; ENSG00000259956; -. DR PharmGKB; PA134870079; -. DR VEuPathDB; HostDB:ENSG00000259956; -. DR eggNOG; KOG0112; Eukaryota. DR GeneTree; ENSGT00940000160561; -. DR HOGENOM; CLU_012724_1_0_1; -. DR InParanoid; Q8NDT2; -. DR OMA; PGSCEYK; -. DR OrthoDB; 2873387at2759; -. DR PhylomeDB; Q8NDT2; -. DR TreeFam; TF354224; -. DR PathwayCommons; Q8NDT2; -. DR SignaLink; Q8NDT2; -. DR BioGRID-ORCS; 29890; 12 hits in 1153 CRISPR screens. DR ChiTaRS; RBM15B; human. DR GenomeRNAi; 29890; -. DR Pharos; Q8NDT2; Tbio. DR PRO; PR:Q8NDT2; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q8NDT2; Protein. DR Bgee; ENSG00000259956; Expressed in ganglionic eminence and 190 other cell types or tissues. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IDA:UniProtKB. DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0001510; P:RNA methylation; IDA:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR CDD; cd12554; RRM1_RBM15B; 1. DR CDD; cd12556; RRM2_RBM15B; 1. DR CDD; cd12558; RRM3_RBM15B; 1. DR CDD; cd21550; SPOC_RBM15B; 1. DR Gene3D; 2.40.290.10; -; 1. DR Gene3D; 3.30.70.330; -; 3. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR034475; RBM15B_RRM1. DR InterPro; IPR034535; RBM15B_RRM2. DR InterPro; IPR034536; RBM15B_RRM3. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR016194; SPOC-like_C_dom_sf. DR InterPro; IPR012921; SPOC_C. DR InterPro; IPR010912; SPOC_met. DR PANTHER; PTHR23189; RNA RECOGNITION MOTIF-CONTAINING; 1. DR PANTHER; PTHR23189:SF40; RNA-BINDING PROTEIN 15B-RELATED; 1. DR Pfam; PF00076; RRM_1; 2. DR Pfam; PF07744; SPOC; 1. DR SMART; SM00360; RRM; 3. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR SUPFAM; SSF100939; SPOC domain-like; 1. DR PROSITE; PS50102; RRM; 3. DR PROSITE; PS50917; SPOC; 1. DR Genevisible; Q8NDT2; HS. PE 1: Evidence at protein level; KW Alternative splicing; Host-virus interaction; Isopeptide bond; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..890 FT /note="Putative RNA-binding protein 15B" FT /id="PRO_0000081778" FT DOMAIN 139..219 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 337..414 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 418..492 FT /note="RRM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 711..889 FT /note="SPOC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00249" FT REGION 1..133 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 219..253 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 547..705 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 722..890 FT /note="Interaction with Epstein-Barr virus BMLF1" FT MOTIF 593..597 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 19..36 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 110..127 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 561..620 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 627..644 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 658..705 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 109 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PHZ5" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PHZ5" FT MOD_RES 267 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 532 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 552 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 556 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 562 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 213 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 702 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..327 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_053878" FT CONFLICT 593 FT /note="R -> K (in Ref. 2; AAI39837)" FT /evidence="ECO:0000305" SQ SEQUENCE 890 AA; 97205 MW; 276C94252F036C83 CRC64; MKRQSERDSS PSGRGSSSSA KRPREREREA EAGGRRAAHK ASGGAKHPVP ARARDKPRGS GSGGGGHRDG RGTGDANHRA SSGRSSGSGA GGGGRGGKAS GDPGASGMSP RASPLPPPPP PPGAEPACPG SSAAAPEYKT LLISSLSPAL PAEHLEDRLF HQFKRFGEIS LRLSHTPELG RVAYVNFRHP QDAREARQHA LARQLLLYDR PLKVEPVYLR GGGGSSRRSS SSSAAASTPP PGPPAPADPL GYLPLHGGYQ YKQRSLSPVA APPLREPRAR HAAAAFALDA AAAAAVGLSR ERALDYYGLY DDRGRPYGYP AVCEEDLMPE DDQRATRNLF IGNLDHSVSE VELRRAFEKY GIIEEVVIKR PARGQGGAYA FLKFQNLDMA HRAKVAMSGR VIGRNPIKIG YGKANPTTRL WVGGLGPNTS LAALAREFDR FGSIRTIDHV KGDSFAYIQY ESLDAAQAAC AKMRGFPLGG PDRRLRVDFA KAEETRYPQQ YQPSPLPVHY ELLTDGYTRH RNLDADLVRD RTPPHLLYSD RDRTFLEGDW TSPSKSSDRR NSLEGYSRSV RSRSGERWGA DGDRGLPKPW EERRKRRSLS SDRGRTTHSP YEERSRTKGS GQQSERGSDR TPERSRKENH SSEGTKESSS NSLSNSRHGA EERGHHHHHH EAADSSHGKK ARDSERNHRT TEAEPKPLEE PKHETKKLKN LSEYAQTLQL GWNGLLVLKN SCFPTSMHIL EGDQGVISSL LKDHTSGSKL TQLKIAQRLR LDQPKLDEVT RRIKQGSPNG YAVLLATQAT PSGLGTEGMP TVEPGLQRRL LRNLVSYLKQ KQAAGVISLP VGGSKGRDGT GMLYAFPPCD FSQQYLQSAL RTLGKLEEEH MVIVIVRDTA //