ID   DDX24_HUMAN             Reviewed;         859 AA.
AC   Q9GZR7; E7EMJ4; Q4V9L5;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 208.
DE   RecName: Full=ATP-dependent RNA helicase DDX24;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 24;
GN   Name=DDX24;
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 1).
RX   PubMed=10936056; DOI=10.1006/geno.2000.6255;
RA   Zhao Y., Yu L., Fu Q., Chen W., Jiang J., Gao J., Zhao S.;
RT   "Cloning and characterization of human DDX24 and mouse Ddx24, two novel
RT   putative DEAD-box proteins, and mapping DDX24 to human chromosome 14q32.";
RL   Genomics 67:351-355(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Chondrosarcoma, and Uterus;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-94; SER-287; SER-295
RP   AND THR-302, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT   and fractionation of phosphopeptides with strong anion exchange
RT   chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-94; SER-287 AND
RP   SER-295, AND IDENTIFICATION BY 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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-71, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-94, 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, 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   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-370; LYS-624; LYS-808 AND
RP   LYS-825, 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: ATP-dependent RNA helicase. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- INTERACTION:
CC       Q9GZR7; P68400: CSNK2A1; NbExp=2; IntAct=EBI-713081, EBI-347804;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9GZR7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9GZR7-2; Sequence=VSP_053881;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in heart and brain, but
CC       with lowest levels in thymus and small intestine.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF214731; AAG02169.1; -; mRNA.
DR   EMBL; AL136886; CAB66820.1; -; mRNA.
DR   EMBL; AK025162; BAB15079.1; -; mRNA.
DR   EMBL; BC008847; AAH08847.1; -; mRNA.
DR   EMBL; BC009406; AAH09406.1; -; mRNA.
DR   EMBL; BC096826; AAH96826.1; -; mRNA.
DR   CCDS; CCDS9918.1; -. [Q9GZR7-1]
DR   RefSeq; NP_065147.1; NM_020414.3. [Q9GZR7-1]
DR   AlphaFoldDB; Q9GZR7; -.
DR   BioGRID; 121353; 584.
DR   DIP; DIP-47301N; -.
DR   IntAct; Q9GZR7; 134.
DR   MINT; Q9GZR7; -.
DR   STRING; 9606.ENSP00000481495; -.
DR   GlyGen; Q9GZR7; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9GZR7; -.
DR   MetOSite; Q9GZR7; -.
DR   PhosphoSitePlus; Q9GZR7; -.
DR   SwissPalm; Q9GZR7; -.
DR   BioMuta; DDX24; -.
DR   DMDM; 18202929; -.
DR   EPD; Q9GZR7; -.
DR   jPOST; Q9GZR7; -.
DR   MassIVE; Q9GZR7; -.
DR   MaxQB; Q9GZR7; -.
DR   PaxDb; 9606-ENSP00000481495; -.
DR   PeptideAtlas; Q9GZR7; -.
DR   ProteomicsDB; 62284; -.
DR   ProteomicsDB; 80121; -. [Q9GZR7-1]
DR   Pumba; Q9GZR7; -.
DR   Antibodypedia; 108; 234 antibodies from 26 providers.
DR   DNASU; 57062; -.
DR   Ensembl; ENST00000613280.4; ENSP00000482106.1; ENSG00000273761.5. [Q9GZR7-1]
DR   Ensembl; ENST00000618456.2; ENSP00000478630.1; ENSG00000273761.5. [Q9GZR7-2]
DR   Ensembl; ENST00000621632.5; ENSP00000481495.1; ENSG00000089737.19. [Q9GZR7-1]
DR   GeneID; 57062; -.
DR   KEGG; hsa:57062; -.
DR   MANE-Select; ENST00000621632.5; ENSP00000481495.1; NM_020414.4; NP_065147.1.
DR   UCSC; uc001ycj.4; human. [Q9GZR7-1]
DR   AGR; HGNC:13266; -.
DR   CTD; 57062; -.
DR   DisGeNET; 57062; -.
DR   GeneCards; DDX24; -.
DR   HGNC; HGNC:13266; DDX24.
DR   HPA; ENSG00000089737; Low tissue specificity.
DR   MIM; 606181; gene.
DR   neXtProt; NX_Q9GZR7; -.
DR   OpenTargets; ENSG00000089737; -.
DR   PharmGKB; PA27211; -.
DR   VEuPathDB; HostDB:ENSG00000089737; -.
DR   eggNOG; KOG0347; Eukaryota.
DR   GeneTree; ENSGT00550000074847; -.
DR   InParanoid; Q9GZR7; -.
DR   OMA; QMIQKAR; -.
DR   OrthoDB; 56712at2759; -.
DR   PhylomeDB; Q9GZR7; -.
DR   TreeFam; TF105837; -.
DR   PathwayCommons; Q9GZR7; -.
DR   SignaLink; Q9GZR7; -.
DR   SIGNOR; Q9GZR7; -.
DR   BioGRID-ORCS; 57062; 686 hits in 1166 CRISPR screens.
DR   ChiTaRS; DDX24; human.
DR   GeneWiki; DDX24; -.
DR   GenomeRNAi; 57062; -.
DR   Pharos; Q9GZR7; Tbio.
DR   PRO; PR:Q9GZR7; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9GZR7; Protein.
DR   Bgee; ENSG00000089737; Expressed in right testis and 100 other cell types or tissues.
DR   ExpressionAtlas; Q9GZR7; baseline and differential.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:LIFEdb.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; NAS:UniProtKB.
DR   GO; GO:0016070; P:RNA metabolic process; NAS:UniProtKB.
DR   CDD; cd17946; DEADc_DDX24; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR24031:SF91; ATP-DEPENDENT RNA HELICASE DDX24; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
DR   SWISS-2DPAGE; Q9GZR7; -.
DR   Genevisible; Q9GZR7; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Helicase; Hydrolase;
KW   Isopeptide bond; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   RNA-binding; Ubl conjugation.
FT   CHAIN           1..859
FT                   /note="ATP-dependent RNA helicase DDX24"
FT                   /id="PRO_0000055029"
FT   DOMAIN          224..528
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          578..723
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          61..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           192..220
FT                   /note="Q motif"
FT   MOTIF           471..474
FT                   /note="DEAD box"
FT   COMPBIAS        76..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..376
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..831
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         237..244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         71
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         287
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         302
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CROSSLNK        370
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        624
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        808
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        825
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         171..225
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_053881"
FT   VARIANT         316
FT                   /note="E -> K (in dbSNP:rs35413935)"
FT                   /id="VAR_052162"
SQ   SEQUENCE   859 AA;  96332 MW;  B01B1170B2CFA0F7 CRC64;
     MKLKDTKSRP KQSSCGKFQT KGIKVVGKWK EVKIDPNMFA DGQMDDLVCF EELTDYQLVS
     PAKNPSSLFS KEAPKRKAQA VSEEEEEEEG KSSSPKKKIK LKKSKNVATE GTSTQKEFEV
     KDPELEAQGD DMVCDDPEAG EMTSENLVQT APKKKKNKGK KGLEPSQSTA AKVPKKAKTW
     IPEVHDQKAD VSAWKDLFVP RPVLRALSFL GFSAPTPIQA LTLAPAIRDK LDILGAAETG
     SGKTLAFAIP MIHAVLQWQK RNAAPPPSNT EAPPGETRTE AGAETRSPGK AEAESDALPD
     DTVIESEALP SDIAAEARAK TGGTVSDQAL LFGDDDAGEG PSSLIREKPV PKQNENEEEN
     LDKEQTGNLK QELDDKSATC KAYPKRPLLG LVLTPTRELA VQVKQHIDAV ARFTGIKTAI
     LVGGMSTQKQ QRMLNRRPEI VVATPGRLWE LIKEKHYHLR NLRQLRCLVV DEADRMVEKG
     HFAELSQLLE MLNDSQYNPK RQTLVFSATL TLVHQAPARI LHKKHTKKMD KTAKLDLLMQ
     KIGMRGKPKV IDLTRNEATV ETLTETKIHC ETDEKDFYLY YFLMQYPGRS LVFANSISCI
     KRLSGLLKVL DIMPLTLHAC MHQKQRLRNL EQFARLEDCV LLATDVAARG LDIPKVQHVI
     HYQVPRTSEI YVHRSGRTAR ATNEGLSLML IGPEDVINFK KIYKTLKKDE DIPLFPVQTK
     YMDVVKERIR LARQIEKSEY RNFQACLHNS WIEQAAAALE IELEEDMYKG GKADQQEERR
     RQKQMKVLKK ELRHLLSQPL FTESQKTKYP TQSGKPPLLV SAPSKSESAL SCLSKQKKKK
     TKKPKEPQPE QPQPSTSAN
//