Full text data of DDX27
DDX27
(RHLP)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Probable ATP-dependent RNA helicase DDX27; 3.6.4.13 (DEAD box protein 27)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Probable ATP-dependent RNA helicase DDX27; 3.6.4.13 (DEAD box protein 27)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00293078
IPI00293078 Splice Isoform 1 Of Probable ATP-dependent RNA helicase no information available soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic GQEAGGFFEDASQYDENLSFQDMNLSRPLLK found at its expected molecular weight found at molecular weight
IPI00293078 Splice Isoform 1 Of Probable ATP-dependent RNA helicase no information available soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic GQEAGGFFEDASQYDENLSFQDMNLSRPLLK found at its expected molecular weight found at molecular weight
UniProt
Q96GQ7
ID DDX27_HUMAN Reviewed; 796 AA.
AC Q96GQ7; A0AVB6; B7ZLY1; Q5VXM7; Q8WYG4; Q969N7; Q96F57; Q96L97;
read moreAC Q9BWY9; Q9BXF0; Q9H990; Q9NWU3; Q9P0C2; Q9UGD6;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 22-JAN-2014, entry version 122.
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=RHLP; ORFNames=HSPC259, PP3241;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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
RT project: 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA 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,
RP AND MASS SPECTROMETRY.
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-79, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-32 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28937.1; Type=Frameshift; Positions=Several;
CC Sequence=AAF28937.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
CC Sequence=AAG22482.1; Type=Frameshift; Positions=208, 427, 434, 532;
CC Sequence=AAH16060.2; Type=Erroneous initiation;
CC Sequence=BAA91284.1; Type=Erroneous initiation;
CC Sequence=BAB14343.1; Type=Erroneous initiation;
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DR EMBL; AY044431; AAK95821.1; -; mRNA.
DR EMBL; AF336851; AAK21271.1; -; mRNA.
DR EMBL; AL049766; CAI22427.1; -; Genomic_DNA.
DR EMBL; AL357560; CAI22427.1; JOINED; Genomic_DNA.
DR EMBL; AL357560; CAH70236.1; -; Genomic_DNA.
DR EMBL; AL049766; CAH70236.1; JOINED; 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 UniGene; Hs.129261; -.
DR UniGene; Hs.65234; -.
DR ProteinModelPortal; Q96GQ7; -.
DR SMR; Q96GQ7; 219-622.
DR IntAct; Q96GQ7; 6.
DR MINT; MINT-1420816; -.
DR PhosphoSite; Q96GQ7; -.
DR DMDM; 29427946; -.
DR SWISS-2DPAGE; Q96GQ7; -.
DR PaxDb; Q96GQ7; -.
DR PeptideAtlas; Q96GQ7; -.
DR PRIDE; Q96GQ7; -.
DR DNASU; 55661; -.
DR Ensembl; ENST00000371764; ENSP00000360828; ENSG00000124228.
DR GeneID; 55661; -.
DR KEGG; hsa:55661; -.
DR UCSC; uc002xuh.3; human.
DR CTD; 55661; -.
DR GeneCards; GC20P047835; -.
DR HGNC; HGNC:15837; DDX27.
DR HPA; HPA047087; -.
DR neXtProt; NX_Q96GQ7; -.
DR PharmGKB; PA27213; -.
DR eggNOG; COG0513; -.
DR HOVERGEN; HBG106162; -.
DR InParanoid; Q96GQ7; -.
DR KO; K13181; -.
DR OMA; QFCNITT; -.
DR OrthoDB; EOG7G1V5Q; -.
DR PhylomeDB; Q96GQ7; -.
DR ChiTaRS; DDX27; human.
DR GeneWiki; DDX27; -.
DR GenomeRNAi; 55661; -.
DR NextBio; 60399; -.
DR PRO; PR:Q96GQ7; -.
DR ArrayExpress; Q96GQ7; -.
DR Bgee; Q96GQ7; -.
DR CleanEx; HS_DDX27; -.
DR Genevestigator; Q96GQ7; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 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 ATP-binding; Complete proteome; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 796 Probable ATP-dependent RNA helicase
FT DDX27.
FT /FTId=PRO_0000055031.
FT DOMAIN 249 423 Helicase ATP-binding.
FT DOMAIN 457 603 Helicase C-terminal.
FT NP_BIND 262 269 ATP (By similarity).
FT MOTIF 195 200 Nuclear localization signal (Potential).
FT MOTIF 218 246 Q motif.
FT MOTIF 371 374 DEAD box.
FT COMPBIAS 44 200 Asp/Glu/Lys-rich.
FT MOD_RES 54 54 Phosphoserine (By similarity).
FT MOD_RES 56 56 Phosphoserine (By similarity).
FT MOD_RES 79 79 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 177 177 Phosphoserine.
FT VARIANT 766 766 G -> S (in dbSNP:rs1130146).
FT /FTId=VAR_022849.
FT CONFLICT 482 482 L -> F (in Ref. 1; AAK21271).
FT CONFLICT 542 542 N -> S (in Ref. 4; BAA91284).
FT CONFLICT 548 548 V -> D (in Ref. 1; AAK95821 and 4;
FT BAB14343).
FT CONFLICT 674 674 A -> T (in Ref. 1; AAK21271).
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
//
ID DDX27_HUMAN Reviewed; 796 AA.
AC Q96GQ7; A0AVB6; B7ZLY1; Q5VXM7; Q8WYG4; Q969N7; Q96F57; Q96L97;
read moreAC Q9BWY9; Q9BXF0; Q9H990; Q9NWU3; Q9P0C2; Q9UGD6;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 22-JAN-2014, entry version 122.
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=RHLP; ORFNames=HSPC259, PP3241;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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
RT project: 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA 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,
RP AND MASS SPECTROMETRY.
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-79, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-32 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28937.1; Type=Frameshift; Positions=Several;
CC Sequence=AAF28937.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
CC Sequence=AAG22482.1; Type=Frameshift; Positions=208, 427, 434, 532;
CC Sequence=AAH16060.2; Type=Erroneous initiation;
CC Sequence=BAA91284.1; Type=Erroneous initiation;
CC Sequence=BAB14343.1; Type=Erroneous initiation;
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DR EMBL; AY044431; AAK95821.1; -; mRNA.
DR EMBL; AF336851; AAK21271.1; -; mRNA.
DR EMBL; AL049766; CAI22427.1; -; Genomic_DNA.
DR EMBL; AL357560; CAI22427.1; JOINED; Genomic_DNA.
DR EMBL; AL357560; CAH70236.1; -; Genomic_DNA.
DR EMBL; AL049766; CAH70236.1; JOINED; 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 UniGene; Hs.129261; -.
DR UniGene; Hs.65234; -.
DR ProteinModelPortal; Q96GQ7; -.
DR SMR; Q96GQ7; 219-622.
DR IntAct; Q96GQ7; 6.
DR MINT; MINT-1420816; -.
DR PhosphoSite; Q96GQ7; -.
DR DMDM; 29427946; -.
DR SWISS-2DPAGE; Q96GQ7; -.
DR PaxDb; Q96GQ7; -.
DR PeptideAtlas; Q96GQ7; -.
DR PRIDE; Q96GQ7; -.
DR DNASU; 55661; -.
DR Ensembl; ENST00000371764; ENSP00000360828; ENSG00000124228.
DR GeneID; 55661; -.
DR KEGG; hsa:55661; -.
DR UCSC; uc002xuh.3; human.
DR CTD; 55661; -.
DR GeneCards; GC20P047835; -.
DR HGNC; HGNC:15837; DDX27.
DR HPA; HPA047087; -.
DR neXtProt; NX_Q96GQ7; -.
DR PharmGKB; PA27213; -.
DR eggNOG; COG0513; -.
DR HOVERGEN; HBG106162; -.
DR InParanoid; Q96GQ7; -.
DR KO; K13181; -.
DR OMA; QFCNITT; -.
DR OrthoDB; EOG7G1V5Q; -.
DR PhylomeDB; Q96GQ7; -.
DR ChiTaRS; DDX27; human.
DR GeneWiki; DDX27; -.
DR GenomeRNAi; 55661; -.
DR NextBio; 60399; -.
DR PRO; PR:Q96GQ7; -.
DR ArrayExpress; Q96GQ7; -.
DR Bgee; Q96GQ7; -.
DR CleanEx; HS_DDX27; -.
DR Genevestigator; Q96GQ7; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 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 ATP-binding; Complete proteome; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 796 Probable ATP-dependent RNA helicase
FT DDX27.
FT /FTId=PRO_0000055031.
FT DOMAIN 249 423 Helicase ATP-binding.
FT DOMAIN 457 603 Helicase C-terminal.
FT NP_BIND 262 269 ATP (By similarity).
FT MOTIF 195 200 Nuclear localization signal (Potential).
FT MOTIF 218 246 Q motif.
FT MOTIF 371 374 DEAD box.
FT COMPBIAS 44 200 Asp/Glu/Lys-rich.
FT MOD_RES 54 54 Phosphoserine (By similarity).
FT MOD_RES 56 56 Phosphoserine (By similarity).
FT MOD_RES 79 79 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 177 177 Phosphoserine.
FT VARIANT 766 766 G -> S (in dbSNP:rs1130146).
FT /FTId=VAR_022849.
FT CONFLICT 482 482 L -> F (in Ref. 1; AAK21271).
FT CONFLICT 542 542 N -> S (in Ref. 4; BAA91284).
FT CONFLICT 548 548 V -> D (in Ref. 1; AAK95821 and 4;
FT BAB14343).
FT CONFLICT 674 674 A -> T (in Ref. 1; AAK21271).
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
//