DDX54_HUMAN
ID DDX54_HUMAN Reviewed; 881 AA.
AC Q8TDD1; Q86YT8; Q9BRZ1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=ATP-dependent RNA helicase DDX54;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase DP97;
DE AltName: Full=DEAD box RNA helicase 97 kDa;
DE AltName: Full=DEAD box protein 54;
GN Name=DDX54;
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).
RC TISSUE=Placenta;
RA Perelygin A.A.;
RT "Positional cloning of the Flv gene.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-881 (ISOFORM 1), AND FUNCTION.
RX PubMed=12466272; DOI=10.1074/jbc.m210066200;
RA Rajendran R.R., Nye A.C., Frasor J., Balsara R.D., Martini P.G.,
RA Katzenellenbogen B.S.;
RT "Regulation of nuclear receptor transcriptional activity by a novel DEAD
RT box RNA helicase (DP97).";
RL J. Biol. Chem. 278:4628-4638(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-881 (ISOFORM 1).
RC TISSUE=Kidney;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-75; SER-644; SER-782
RP AND SER-788, 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 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-39; SER-41 AND
RP SER-782, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-698 AND SER-782, 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 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-41 AND SER-782, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-75 AND SER-782, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, 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 [15]
RP VARIANTS ARG-20; SER-216; MET-286; PHE-298 AND GLN-611, AND TISSUE
RP SPECIFICITY.
RX PubMed=31256877; DOI=10.1016/j.ajhg.2019.06.001;
RG University of Washington Center for Mendelian Genomics, Baylor-Hopkins Center for Mendelian Genomics, Telethon Undiagnosed Diseases Program;
RA Paine I., Posey J.E., Grochowski C.M., Jhangiani S.N., Rosenheck S.,
RA Kleyner R., Marmorale T., Yoon M., Wang K., Robison R., Cappuccio G.,
RA Pinelli M., Magli A., Coban Akdemir Z., Hui J., Yeung W.L., Wong B.K.Y.,
RA Ortega L., Bekheirnia M.R., Bierhals T., Hempel M., Johannsen J.,
RA Santer R., Aktas D., Alikasifoglu M., Bozdogan S., Aydin H., Karaca E.,
RA Bayram Y., Ityel H., Dorschner M., White J.J., Wilichowski E.,
RA Wortmann S.B., Casella E.B., Kitajima J.P., Kok F., Monteiro F.,
RA Muzny D.M., Bamshad M., Gibbs R.A., Sutton V.R., Van Esch H.,
RA Brunetti-Pierri N., Hildebrandt F., Brautbar A., Van den Veyver I.B.,
RA Glass I., Lessel D., Lyon G.J., Lupski J.R.;
RT "Paralog studies augment gene discovery: DDX and DHX genes.";
RL Am. J. Hum. Genet. 105:302-316(2019).
CC -!- FUNCTION: Has RNA-dependent ATPase activity. Represses the
CC transcriptional activity of nuclear receptors.
CC {ECO:0000269|PubMed:12466272}.
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 -!- SUBUNIT: Interacts in a hormone-dependent manner with nuclear
CC receptors.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TDD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDD1-2; Sequence=VSP_040135;
CC -!- TISSUE SPECIFICITY: Expressed in the fallopian tube, cervix and uterus.
CC Also expressed in the brain. {ECO:0000269|PubMed:31256877}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN59978.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AF478457; AAL85336.1; -; mRNA.
DR EMBL; AC089999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY148094; AAN59978.1; ALT_SEQ; mRNA.
DR EMBL; BC005848; AAH05848.2; -; mRNA.
DR CCDS; CCDS31907.1; -. [Q8TDD1-1]
DR CCDS; CCDS44984.1; -. [Q8TDD1-2]
DR RefSeq; NP_001104792.1; NM_001111322.1. [Q8TDD1-2]
DR RefSeq; NP_076977.3; NM_024072.3. [Q8TDD1-1]
DR AlphaFoldDB; Q8TDD1; -.
DR SMR; Q8TDD1; -.
DR BioGRID; 122503; 331.
DR IntAct; Q8TDD1; 98.
DR MINT; Q8TDD1; -.
DR STRING; 9606.ENSP00000323858; -.
DR iPTMnet; Q8TDD1; -.
DR PhosphoSitePlus; Q8TDD1; -.
DR SwissPalm; Q8TDD1; -.
DR BioMuta; DDX54; -.
DR DMDM; 46576615; -.
DR SWISS-2DPAGE; Q8TDD1; -.
DR EPD; Q8TDD1; -.
DR jPOST; Q8TDD1; -.
DR MassIVE; Q8TDD1; -.
DR MaxQB; Q8TDD1; -.
DR PaxDb; Q8TDD1; -.
DR PeptideAtlas; Q8TDD1; -.
DR PRIDE; Q8TDD1; -.
DR ProteomicsDB; 74267; -. [Q8TDD1-1]
DR ProteomicsDB; 74268; -. [Q8TDD1-2]
DR Antibodypedia; 18719; 169 antibodies from 28 providers.
DR DNASU; 79039; -.
DR Ensembl; ENST00000306014.10; ENSP00000304072.5; ENSG00000123064.13. [Q8TDD1-1]
DR Ensembl; ENST00000314045.11; ENSP00000323858.7; ENSG00000123064.13. [Q8TDD1-2]
DR GeneID; 79039; -.
DR KEGG; hsa:79039; -.
DR MANE-Select; ENST00000306014.10; ENSP00000304072.5; NM_024072.4; NP_076977.3.
DR UCSC; uc001tup.4; human. [Q8TDD1-1]
DR CTD; 79039; -.
DR DisGeNET; 79039; -.
DR GeneCards; DDX54; -.
DR HGNC; HGNC:20084; DDX54.
DR HPA; ENSG00000123064; Low tissue specificity.
DR MIM; 611665; gene.
DR neXtProt; NX_Q8TDD1; -.
DR OpenTargets; ENSG00000123064; -.
DR PharmGKB; PA134992026; -.
DR VEuPathDB; HostDB:ENSG00000123064; -.
DR eggNOG; KOG0337; Eukaryota.
DR GeneTree; ENSGT00550000075100; -.
DR HOGENOM; CLU_003041_5_2_1; -.
DR InParanoid; Q8TDD1; -.
DR OMA; MRWDKKS; -.
DR OrthoDB; 268859at2759; -.
DR PhylomeDB; Q8TDD1; -.
DR TreeFam; TF105707; -.
DR PathwayCommons; Q8TDD1; -.
DR SignaLink; Q8TDD1; -.
DR BioGRID-ORCS; 79039; 760 hits in 1088 CRISPR screens.
DR ChiTaRS; DDX54; human.
DR GenomeRNAi; 79039; -.
DR Pharos; Q8TDD1; Tbio.
DR PRO; PR:Q8TDD1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8TDD1; protein.
DR Bgee; ENSG00000123064; Expressed in sural nerve and 183 other tissues.
DR ExpressionAtlas; Q8TDD1; baseline and differential.
DR Genevisible; Q8TDD1; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0016070; P:RNA metabolic process; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10.
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:SF292; PTHR24031:SF292; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..881
FT /note="ATP-dependent RNA helicase DDX54"
FT /id="PRO_0000055056"
FT DOMAIN 127..299
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 326..473
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..647
FT /note="Interaction with nuclear receptors"
FT REGION 725..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 96..124
FT /note="Q motif"
FT MOTIF 247..250
FT /note="DEAD box"
FT COMPBIAS 17..31
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 804
FT /note="Q -> QA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040135"
FT VARIANT 20
FT /note="W -> R (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance;
FT dbSNP:rs774035439)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083615"
FT VARIANT 216
FT /note="N -> S (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance;
FT dbSNP:rs764707570)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083616"
FT VARIANT 286
FT /note="V -> M (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance;
FT dbSNP:rs148961522)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083617"
FT VARIANT 298
FT /note="L -> F (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance;
FT dbSNP:rs1593005589)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083618"
FT VARIANT 570
FT /note="R -> H (in dbSNP:rs35519289)"
FT /id="VAR_052171"
FT VARIANT 611
FT /note="R -> Q (found in a patient with a neurodevelopmental
FT disorder; unknown pathological significance;
FT dbSNP:rs777276705)"
FT /evidence="ECO:0000269|PubMed:31256877"
FT /id="VAR_083619"
FT VARIANT 693
FT /note="R -> Q (in dbSNP:rs11564)"
FT /id="VAR_052172"
FT VARIANT 712
FT /note="V -> A (in dbSNP:rs10354)"
FT /id="VAR_052173"
FT VARIANT 821
FT /note="P -> L (in dbSNP:rs1048889)"
FT /id="VAR_033860"
SQ SEQUENCE 881 AA; 98595 MW; 9823C75156D998C4 CRC64;
MAADKGPAAG PRSRAAMAQW RKKKGLRKRR GAASQARGSD SEDGEFEIQA EDDARARKLG
PGRPLPTFPT SECTSDVEPD TREMVRAQNK KKKKSGGFQS MGLSYPVFKG IMKKGYKVPT
PIQRKTIPVI LDGKDVVAMA RTGSGKTACF LLPMFERLKT HSAQTGARAL ILSPTRELAL
QTLKFTKELG KFTGLKTALI LGGDRMEDQF AALHENPDII IATPGRLVHV AVEMSLKLQS
VEYVVFDEAD RLFEMGFAEQ LQEIIARLPG GHQTVLFSAT LPKLLVEFAR AGLTEPVLIR
LDVDTKLNEQ LKTSFFLVRE DTKAAVLLHL LHNVVRPQDQ TVVFVATKHH AEYLTELLTT
QRVSCAHIYS ALDPTARKIN LAKFTLGKCS TLIVTDLAAR GLDIPLLDNV INYSFPAKGK
LFLHRVGRVA RAGRSGTAYS LVAPDEIPYL LDLHLFLGRS LTLARPLKEP SGVAGVDGML
GRVPQSVVDE EDSGLQSTLE ASLELRGLAR VADNAQQQYV RSRPAPSPES IKRAKEMDLV
GLGLHPLFSS RFEEEELQRL RLVDSIKNYR SRATIFEINA SSRDLCSQVM RAKRQKDRKA
IARFQQGQQG RQEQQEGPVG PAPSRPALQE KQPEKEEEEE AGESVEDIFS EVVGRKRQRS
GPNRGAKRRR EEARQRDQEF YIPYRPKDFD SERGLSISGE GGAFEQQAAG AVLDLMGDEA
QNLTRGRQQL KWDRKKKRFV GQSGQEDKKK IKTESGRYIS SSYKRDLYQK WKQKQKIDDR
DSDEEGASDR RGPERRGGKR DRGQGASRPH APGTPAGRVR PELKTKQQIL KQRRRAQKLH
FLQRGGLKQL SARNRRRVQE LQQGAFGRGA RSKKGKMRKR M
