NCBP3_HUMAN
ID NCBP3_HUMAN Reviewed; 620 AA.
AC Q53F19; B3KWG7; Q7L406; Q96FK1; Q9NXZ4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Nuclear cap-binding protein subunit 3 {ECO:0000312|HGNC:HGNC:24612};
DE AltName: Full=Protein ELG;
GN Name=NCBP3 {ECO:0000312|HGNC:HGNC:24612}; Synonyms=C17orf85;
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 [MRNA] (ISOFORM 2).
RA Robinson P., Green S., Carter C., Coadwell J., Kilshaw P.;
RT "Transcriptional regulation of the alpha E integrin gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 267-620 (ISOFORM 1).
RC TISSUE=Gastric mucosa;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-620.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-209; SER-210; THR-413
RP AND SER-415, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-209 AND SER-210, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-209 AND SER-210, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-73 AND SER-415, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NCBP1; SRRT; KPNA3; THOC5
RP AND EIF4A3, RNA-BINDING, MUTAGENESIS OF ASP-134 AND 155-TRP--ASP-158, WLDD
RP MOTIF, RRM REGION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26382858; DOI=10.1038/ncomms9192;
RA Gebhardt A., Habjan M., Benda C., Meiler A., Haas D.A., Hein M.Y., Mann A.,
RA Mann M., Habermann B., Pichlmair A.;
RT "mRNA export through an additional cap-binding complex consisting of NCBP1
RT and NCBP3.";
RL Nat. Commun. 6:8192-8192(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12; LYS-70; LYS-186 AND LYS-541,
RP AND 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).
CC -!- FUNCTION: Associates with NCBP1/CBP80 to form an alternative cap-
CC binding complex (CBC) which plays a key role in mRNA export. NCBP3
CC serves as adapter protein linking the capped RNAs (m7GpppG-capped RNA)
CC to NCBP1/CBP80. Unlike the conventional CBC with NCBP2 which binds both
CC small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their
CC export from the nucleus, the alternative CBC with NCBP3 does not bind
CC snRNA and associates only with mRNA thereby playing a role in only mRNA
CC export. The alternative CBC is particularly important in cellular
CC stress situations such as virus infections and the NCBP3 activity is
CC critical to inhibit virus growth (PubMed:26382858).
CC {ECO:0000269|PubMed:26382858}.
CC -!- SUBUNIT: Component of an alternative cap-binding complex (CBC) composed
CC of NCBP1/CBP80 and NCBP3. Interacts with SRRT, KPNA3, THOC5 and EIF4A3.
CC {ECO:0000269|PubMed:26382858}.
CC -!- INTERACTION:
CC Q53F19; O00629: KPNA4; NbExp=5; IntAct=EBI-6657994, EBI-396343;
CC Q53F19; Q96PV6: LENG8; NbExp=7; IntAct=EBI-6657994, EBI-739546;
CC Q53F19; Q09161: NCBP1; NbExp=11; IntAct=EBI-6657994, EBI-464743;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26382858}. Cytoplasm
CC {ECO:0000269|PubMed:26382858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q53F19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53F19-2; Sequence=VSP_028999;
CC -!- SIMILARITY: Belongs to the NCBP3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD97190.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ277841; CAB91001.1; -; mRNA.
DR EMBL; AC005940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK125048; BAG54129.1; -; mRNA.
DR EMBL; AK223470; BAD97190.1; ALT_INIT; mRNA.
DR EMBL; CH471108; EAW90479.1; -; Genomic_DNA.
DR EMBL; BC010707; AAH10707.1; -; mRNA.
DR CCDS; CCDS45578.1; -. [Q53F19-1]
DR RefSeq; NP_001107590.1; NM_001114118.2. [Q53F19-1]
DR RefSeq; XP_016880318.1; XM_017024829.1. [Q53F19-2]
DR AlphaFoldDB; Q53F19; -.
DR SMR; Q53F19; -.
DR BioGRID; 120662; 182.
DR ComplexPortal; CPX-3624; Alternative nuclear cap-binding complex.
DR IntAct; Q53F19; 299.
DR MINT; Q53F19; -.
DR STRING; 9606.ENSP00000373657; -.
DR iPTMnet; Q53F19; -.
DR PhosphoSitePlus; Q53F19; -.
DR BioMuta; NCBP3; -.
DR DMDM; 160017360; -.
DR EPD; Q53F19; -.
DR jPOST; Q53F19; -.
DR MassIVE; Q53F19; -.
DR MaxQB; Q53F19; -.
DR PaxDb; Q53F19; -.
DR PeptideAtlas; Q53F19; -.
DR PRIDE; Q53F19; -.
DR ProteomicsDB; 62454; -. [Q53F19-1]
DR ProteomicsDB; 62455; -. [Q53F19-2]
DR Antibodypedia; 64617; 43 antibodies from 13 providers.
DR DNASU; 55421; -.
DR Ensembl; ENST00000389005.6; ENSP00000373657.4; ENSG00000074356.17. [Q53F19-1]
DR GeneID; 55421; -.
DR KEGG; hsa:55421; -.
DR MANE-Select; ENST00000389005.6; ENSP00000373657.4; NM_001114118.3; NP_001107590.1.
DR UCSC; uc010ckl.3; human. [Q53F19-1]
DR CTD; 55421; -.
DR GeneCards; NCBP3; -.
DR HGNC; HGNC:24612; NCBP3.
DR HPA; ENSG00000074356; Low tissue specificity.
DR MIM; 616624; gene.
DR neXtProt; NX_Q53F19; -.
DR OpenTargets; ENSG00000074356; -.
DR PharmGKB; PA145149545; -.
DR VEuPathDB; HostDB:ENSG00000074356; -.
DR eggNOG; ENOG502QRX4; Eukaryota.
DR GeneTree; ENSGT00390000005712; -.
DR HOGENOM; CLU_488838_0_0_1; -.
DR InParanoid; Q53F19; -.
DR OMA; DANEDKS; -.
DR OrthoDB; 535499at2759; -.
DR PhylomeDB; Q53F19; -.
DR TreeFam; TF331339; -.
DR PathwayCommons; Q53F19; -.
DR SignaLink; Q53F19; -.
DR SIGNOR; Q53F19; -.
DR BioGRID-ORCS; 55421; 37 hits in 1067 CRISPR screens.
DR ChiTaRS; NCBP3; human.
DR GenomeRNAi; 55421; -.
DR Pharos; Q53F19; Tbio.
DR PRO; PR:Q53F19; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q53F19; protein.
DR Bgee; ENSG00000074356; Expressed in right uterine tube and 176 other tissues.
DR ExpressionAtlas; Q53F19; baseline and differential.
DR Genevisible; Q53F19; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005845; C:mRNA cap binding complex; IPI:ComplexPortal.
DR GO; GO:0005846; C:nuclear cap binding complex; IPI:ComplexPortal.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034518; C:RNA cap binding complex; TAS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:ComplexPortal.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0006408; P:snRNA export from nucleus; IMP:ComplexPortal.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR019416; NCBP3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR PANTHER; PTHR16291; PTHR16291; 1.
DR Pfam; PF10309; NCBP3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Cytoplasm; Isopeptide bond;
KW mRNA capping; mRNA processing; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transport; Ubl conjugation.
FT CHAIN 1..620
FT /note="Nuclear cap-binding protein subunit 3"
FT /id="PRO_0000308582"
FT REGION 15..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..187
FT /note="RNA recognition motif (RRM) domain"
FT /evidence="ECO:0000303|PubMed:26382858"
FT REGION 185..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..158
FT /note="WLDD motif; essential for 7-methylguanosine-
FT containing mRNA cap binding"
FT /evidence="ECO:0000269|PubMed:26382858"
FT COMPBIAS 187..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..366
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 413
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..280
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_028999"
FT MUTAGEN 134
FT /note="D->A: Minor loss of 7-methylguanosine-containing
FT mRNA cap binding."
FT /evidence="ECO:0000269|PubMed:26382858"
FT MUTAGEN 155..158
FT /note="WLDD->ALAA: Complete loss of 7-methylguanosine-
FT containing mRNA cap binding."
FT /evidence="ECO:0000269|PubMed:26382858"
FT CONFLICT 465
FT /note="D -> N (in Ref. 5; BAD97190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 620 AA; 70593 MW; 78ABD2F3E0BE4760 CRC64;
MAAVRGLRVS VKAEAPAGPA LGLPSPEAES GVDRGEPEPM EVEEGELEIV PVRRSLKELI
PDTSRRYENK AGSFITGIDV TSKEAIEKKE QRAKRFHFRS EVNLAQRNVA LDRDMMKKAI
PKVRLETIYI CGVDEMSTQD VFSYFKEYPP AHIEWLDDTS CNVVWLDEMT ATRALINMSS
LPAQDKIRSR DASEDKSAEK RKKDKQEDSS DDDEAEEGEV EDENSSDVEL DTLSQVEEES
LLRNDLRPAN KLAKGNRLFM RFATKDDKKE LGAARRSQYY MKYGNPNYGG MKGILSNSWK
RRYHSRRIQR DVIKKRALIG DDVGLTSYKH RHSGLVNVPE EPIEEEEEEE EEEEEEEEED
QDMDADDRVV VEYHEELPAL KQPRERSASR RSSASSSDSD EMDYDLELKM ISTPSPKKSM
KMTMYADEVE SQLKNIRNSM RADSVSSSNI KNRIGNKLPP EKFADVRHLL DEKRQHSRPR
PPVSSTKSDI RQRLGKRPHS PEKAFSSNPV VRREPSSDVH SRLGVPRQDS KGLYADTREK
KSGNLWTRLG SAPKTKEKNT KKVDHRAPGA EEDDSELQRA WGALIKEKEQ SRQKKSRLDN
LPSLQIEVSR ESSSGSEAES
