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 SWISS-2DPAGE; Q96GQ7; -.
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 Genevisible; Q96GQ7; HS.
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.
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
//
