ID   DDX27_HUMAN             Reviewed;         796 AA.
AC   Q96GQ7; A0AVB6; B7ZLY1; Q5VXM7; Q8WYG4; Q969N7; Q96F57; Q96L97; Q9BWY9;
AC   Q9BXF0; Q9H990; Q9NWU3; Q9P0C2; Q9UGD6;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 2.
DT   27-MAR-2024, entry version 204.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX27;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 27;
GN   Name=DDX27; Synonyms=cPERP-F {ECO:0000303|PubMed:20813266}, RHLP;
GN   ORFNames=HSPC259, PP3241;
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].
RA   Wang Y., Fan Y.-Z., Han W.-L., Yang T., Gao Y., Ma D.-L.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-766.
RC   TISSUE=Brain, Muscle, and Skin;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-796, AND VARIANT SER-766.
RC   TISSUE=Stomach cancer, and Teratocarcinoma;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-688.
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 600-796.
RC   TISSUE=Umbilical cord blood;
RA   Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA   Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT   "Human partial CDS from CD34+ stem cells.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-166 AND SER-177, AND
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   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA   Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA   Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA   Earnshaw W.C., Rappsilber J.;
RT   "The protein composition of mitotic chromosomes determined using
RT   multiclassifier combinatorial proteomics.";
RL   Cell 142:810-821(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, 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   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP   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   [12]
RP   IDENTIFICATION BY 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   [13]
RP   SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH
RP   BOP1 AND PES1, FUNCTION, AND MUTAGENESIS OF 86-PHE--PHE-88.
RX   PubMed=25825154; DOI=10.1016/j.yexcr.2015.03.017;
RA   Kellner M., Rohrmoser M., Forne I., Voss K., Burger K., Muehl B.,
RA   Gruber-Eber A., Kremmer E., Imhof A., Eick D.;
RT   "DEAD-box helicase DDX27 regulates 3' end formation of ribosomal 47S RNA
RT   and stably associates with the PeBoW-complex.";
RL   Exp. Cell Res. 334:146-159(2015).
CC   -!- FUNCTION: Probable ATP-dependent RNA helicase. Component of the
CC       nucleolar ribosomal RNA (rRNA) processing machinery that regulates 3'
CC       end formation of ribosomal 47S rRNA (PubMed:25825154).
CC       {ECO:0000269|PubMed:25825154}.
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: Associates with PeBoW complex, composed of BOP1, PES1 and
CC       WDR12 (PubMed:25825154). Interacts directly with BOP1 and PES1
CC       (PubMed:25825154). {ECO:0000269|PubMed:25825154}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:25825154}.
CC       Chromosome {ECO:0000269|PubMed:20813266}. Note=Associates with 60S and
CC       90S pre-ribosomal particles (PubMed:25825154).
CC       {ECO:0000269|PubMed:25825154}.
CC   -!- DOMAIN: The C-terminal domain regulates nucleolar localization
CC       (PubMed:25825154). {ECO:0000269|PubMed:25825154}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-32 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF28937.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAF28937.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC       Sequence=AAG22482.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAH16060.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA91284.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB14343.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY044431; AAK95821.1; -; mRNA.
DR   EMBL; AF336851; AAK21271.1; -; mRNA.
DR   EMBL; AL049766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL357560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC009304; AAH09304.2; -; mRNA.
DR   EMBL; BC011927; AAH11927.2; -; mRNA.
DR   EMBL; BC016060; AAH16060.2; ALT_INIT; mRNA.
DR   EMBL; BC126287; AAI26288.1; -; mRNA.
DR   EMBL; BC130275; AAI30276.1; -; mRNA.
DR   EMBL; BC144125; AAI44126.1; -; mRNA.
DR   EMBL; AK022979; BAB14343.1; ALT_INIT; mRNA.
DR   EMBL; AK000603; BAA91284.1; ALT_INIT; mRNA.
DR   EMBL; AF193054; AAG22482.1; ALT_FRAME; mRNA.
DR   EMBL; AF161377; AAF28937.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_060365.7; NM_017895.7.
DR   AlphaFoldDB; Q96GQ7; -.
DR   SMR; Q96GQ7; -.
DR   BioGRID; 120793; 317.
DR   CORUM; Q96GQ7; -.
DR   IntAct; Q96GQ7; 98.
DR   MINT; Q96GQ7; -.
DR   STRING; 9606.ENSP00000483495; -.
DR   GlyGen; Q96GQ7; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q96GQ7; -.
DR   PhosphoSitePlus; Q96GQ7; -.
DR   SwissPalm; Q96GQ7; -.
DR   BioMuta; DDX27; -.
DR   DMDM; 29427946; -.
DR   EPD; Q96GQ7; -.
DR   jPOST; Q96GQ7; -.
DR   MassIVE; Q96GQ7; -.
DR   MaxQB; Q96GQ7; -.
DR   PaxDb; 9606-ENSP00000483495; -.
DR   PeptideAtlas; Q96GQ7; -.
DR   ProteomicsDB; 76655; -.
DR   Pumba; Q96GQ7; -.
DR   DNASU; 55661; -.
DR   GeneID; 55661; -.
DR   KEGG; hsa:55661; -.
DR   UCSC; uc002xuh.4; human.
DR   AGR; HGNC:15837; -.
DR   DisGeNET; 55661; -.
DR   GeneCards; DDX27; -.
DR   HGNC; HGNC:15837; DDX27.
DR   MIM; 616621; gene.
DR   neXtProt; NX_Q96GQ7; -.
DR   PharmGKB; PA27213; -.
DR   VEuPathDB; HostDB:ENSG00000124228; -.
DR   eggNOG; KOG0338; Eukaryota.
DR   InParanoid; Q96GQ7; -.
DR   OrthoDB; 149428at2759; -.
DR   PhylomeDB; Q96GQ7; -.
DR   TreeFam; TF314780; -.
DR   PathwayCommons; Q96GQ7; -.
DR   SignaLink; Q96GQ7; -.
DR   BioGRID-ORCS; 55661; 699 hits in 1170 CRISPR screens.
DR   ChiTaRS; DDX27; human.
DR   GeneWiki; DDX27; -.
DR   GenomeRNAi; 55661; -.
DR   Pharos; Q96GQ7; Tbio.
DR   PRO; PR:Q96GQ7; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q96GQ7; Protein.
DR   GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; 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:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR   CDD; cd17947; DEADc_DDX27; 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; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   PANTHER; PTHR47959:SF14; DEAD-BOX ATP-DEPENDENT RNA HELICASE 28; 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; Q96GQ7; -.
DR   Genevisible; Q96GQ7; HS.
PE   1: Evidence at protein level;
KW   ATP-binding; Chromosome; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..796
FT                   /note="Probable ATP-dependent RNA helicase DDX27"
FT                   /id="PRO_0000055031"
FT   DOMAIN          249..423
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          457..603
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          43..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           86..88
FT                   /note="Required for interaction with the PEBOW complex"
FT                   /evidence="ECO:0000269|PubMed:25825154"
FT   MOTIF           195..200
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           218..246
FT                   /note="Q motif"
FT   MOTIF           371..374
FT                   /note="DEAD box"
FT   COMPBIAS        46..61
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..175
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..757
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..778
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         262..269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         54
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921N6"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921N6"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VARIANT         766
FT                   /note="G -> S (in dbSNP:rs1130146)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_022849"
FT   MUTAGEN         86..88
FT                   /note="Missing: No interaction with PEBOW complex."
FT                   /evidence="ECO:0000269|PubMed:25825154"
FT   CONFLICT        482
FT                   /note="L -> F (in Ref. 1; AAK21271)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        542
FT                   /note="N -> S (in Ref. 4; BAA91284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        548
FT                   /note="V -> D (in Ref. 1; AAK95821 and 4; BAB14343)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        674
FT                   /note="A -> T (in Ref. 1; AAK21271)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   796 AA;  89835 MW;  9282C712B8F8B84A CRC64;
     MVLAQRRRGG CEKLRAGPQA VLASGSGFCD NMLADLGLIG TIGEDDEVPV EPESDSGDEE
     EEGPIVLGRR QKALGKNRSA DFNPDFVFTE KEGTYDGSWA LADVMSQLKK KRAATTLDEK
     IEKVRKKRKT EDKEAKSGKL EKEKEAKEGS EPKEQEDLQE NDEEGSEDEA SETDYSSADE
     NILTKADTLK VKDRKKKKKK GQEAGGFFED ASQYDENLSF QDMNLSRPLL KAITAMGFKQ
     PTPIQKACIP VGLLGKDICA CAATGTGKTA AFALPVLERL IYKPRQAPVT RVLVLVPTRE
     LGIQVHSVTR QLAQFCNITT CLAVGGLDVK SQEAALRAAP DILIATPGRL IDHLHNCPSF
     HLSSIEVLIL DEADRMLDEY FEEQMKEIIR MCSHHRQTML FSATMTDEVK DLASVSLKNP
     VRIFVNSNTD VAPFLRQEFI RIRPNREGDR EAIVAALLTR TFTDHVMLFT QTKKQAHRMH
     ILLGLMGLQV GELHGNLSQT QRLEALRRFK DEQIDILVAT DVAARGLDIE GVKTVINFTM
     PNTIKHYVHR VGRTARAGRA GRSVSLVGED ERKMLKEIVK AAKAPVKARI LPQDVILKFR
     DKIEKMEKDV YAVLQLEAEE KEMQQSEAQI NTAKRLLEKG KEAVVQEPER SWFQTKEERK
     KEKIAKALQE FDLALRGKKK RKKFMKDAKK KGEMTAEERS QFEILKAQMF AERLAKRNRR
     AKRARAMPEE EPVRGPAKKQ KQGKKSVFDE ELTNTSKKAL KQYRAGPSFE ERKQLGLPHQ
     RRGGNFKSKS RYKRRK
//