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DDX60_HUMAN
ID   DDX60_HUMAN             Reviewed;        1712 AA.
AC   Q8IY21; Q6PK35; Q9NVE3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX60;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 60;
GN   Name=DDX60;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1174.
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   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, AND
RP   INTERACTION WITH EXOSC1; EXOSC4; DDX58/RIG-I; IFIH1/MDA5; DHX58/LGP2.
RX   PubMed=21791617; DOI=10.1128/mcb.01368-10;
RA   Miyashita M., Oshiumi H., Matsumoto M., Seya T.;
RT   "DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-
RT   like receptor-mediated signaling.";
RL   Mol. Cell. Biol. 31:3802-3819(2011).
RN   [5]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=21478870; DOI=10.1038/nature09907;
RA   Schoggins J.W., Wilson S.J., Panis M., Murphy M.Y., Jones C.T.,
RA   Bieniasz P., Rice C.M.;
RT   "A diverse range of gene products are effectors of the type I interferon
RT   antiviral response.";
RL   Nature 472:481-485(2011).
CC   -!- FUNCTION: Positively regulates DDX58/RIG-I- and IFIH1/MDA5-dependent
CC       type I interferon and interferon inducible gene expression in response
CC       to viral infection. Binds ssRNA, dsRNA and dsDNA and can promote the
CC       binding of DDX58/RIG-I to dsRNA. Exhibits antiviral activity against
CC       hepatitis C virus and vesicular stomatitis virus (VSV).
CC       {ECO:0000269|PubMed:21478870, ECO:0000269|PubMed:21791617}.
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 with EXOSC1, EXOSC4, DDX58/RIG-I, IFIH1/MDA5 and
CC       DHX58/LGP2. {ECO:0000269|PubMed:21791617}.
CC   -!- INTERACTION:
CC       Q8IY21; P60228: EIF3E; NbExp=2; IntAct=EBI-2807346, EBI-347740;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21791617}.
CC   -!- TISSUE SPECIFICITY: Brain, lymph node, prostate, stomach, thyroid,
CC       tongue, trachea, uterus, skeletal muscle, spleen, kidney, liver and
CC       small intestine. {ECO:0000269|PubMed:21791617}.
CC   -!- INDUCTION: By interferon (IFN). Up-regulated during vesicular
CC       stomatitis virus (VSV), or poliovirus (PV) infection.
CC       {ECO:0000269|PubMed:21478870, ECO:0000269|PubMed:21791617}.
CC   -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR   EMBL; AC068989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC007820; AAH07820.1; -; mRNA.
DR   EMBL; BC038115; AAH38115.1; -; mRNA.
DR   EMBL; AK001649; BAA91809.1; -; mRNA.
DR   CCDS; CCDS34097.1; -.
DR   RefSeq; NP_060101.3; NM_017631.5.
DR   AlphaFoldDB; Q8IY21; -.
DR   BioGRID; 120742; 84.
DR   IntAct; Q8IY21; 76.
DR   STRING; 9606.ENSP00000377344; -.
DR   iPTMnet; Q8IY21; -.
DR   PhosphoSitePlus; Q8IY21; -.
DR   BioMuta; DDX60; -.
DR   DMDM; 296439377; -.
DR   EPD; Q8IY21; -.
DR   jPOST; Q8IY21; -.
DR   MassIVE; Q8IY21; -.
DR   MaxQB; Q8IY21; -.
DR   PaxDb; Q8IY21; -.
DR   PeptideAtlas; Q8IY21; -.
DR   PRIDE; Q8IY21; -.
DR   ProteomicsDB; 71088; -.
DR   Antibodypedia; 49250; 41 antibodies from 19 providers.
DR   DNASU; 55601; -.
DR   Ensembl; ENST00000393743.8; ENSP00000377344.3; ENSG00000137628.18.
DR   GeneID; 55601; -.
DR   KEGG; hsa:55601; -.
DR   MANE-Select; ENST00000393743.8; ENSP00000377344.3; NM_017631.6; NP_060101.3.
DR   UCSC; uc003irp.4; human.
DR   CTD; 55601; -.
DR   DisGeNET; 55601; -.
DR   GeneCards; DDX60; -.
DR   HGNC; HGNC:25942; DDX60.
DR   HPA; ENSG00000137628; Tissue enhanced (stomach).
DR   MIM; 613974; gene.
DR   neXtProt; NX_Q8IY21; -.
DR   OpenTargets; ENSG00000137628; -.
DR   PharmGKB; PA162383444; -.
DR   VEuPathDB; HostDB:ENSG00000137628; -.
DR   eggNOG; KOG0949; Eukaryota.
DR   eggNOG; KOG0950; Eukaryota.
DR   GeneTree; ENSGT00940000157188; -.
DR   HOGENOM; CLU_002305_0_0_1; -.
DR   InParanoid; Q8IY21; -.
DR   OMA; FEFYQSK; -.
DR   OrthoDB; 546283at2759; -.
DR   PhylomeDB; Q8IY21; -.
DR   TreeFam; TF314846; -.
DR   PathwayCommons; Q8IY21; -.
DR   SignaLink; Q8IY21; -.
DR   BioGRID-ORCS; 55601; 11 hits in 1080 CRISPR screens.
DR   ChiTaRS; DDX60; human.
DR   GenomeRNAi; 55601; -.
DR   Pharos; Q8IY21; Tbio.
DR   PRO; PR:Q8IY21; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q8IY21; protein.
DR   Bgee; ENSG00000137628; Expressed in jejunal mucosa and 178 other tissues.
DR   ExpressionAtlas; Q8IY21; baseline and differential.
DR   Genevisible; Q8IY21; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:1900245; P:positive regulation of MDA-5 signaling pathway; IMP:UniProtKB.
DR   GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IMP:UniProtKB.
DR   GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; ATP-binding; Cytoplasm; Helicase; Hydrolase; Immunity;
KW   Innate immunity; Nucleotide-binding; Reference proteome; RNA-binding.
FT   CHAIN           1..1712
FT                   /note="Probable ATP-dependent RNA helicase DDX60"
FT                   /id="PRO_0000318154"
FT   DOMAIN          772..939
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1226..1370
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           889..892
FT                   /note="DEVH box"
FT   BINDING         785..792
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   VARIANT         672
FT                   /note="V -> M (in dbSNP:rs550625)"
FT                   /id="VAR_055895"
FT   VARIANT         998
FT                   /note="I -> V (in dbSNP:rs576619)"
FT                   /id="VAR_055896"
FT   CONFLICT        415
FT                   /note="V -> I (in Ref. 3; BAA91809)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="E -> G (in Ref. 2; AAH38115)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        731
FT                   /note="V -> I (in Ref. 2; AAH38115)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1385
FT                   /note="A -> T (in Ref. 2; AAH38115)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1712 AA;  197853 MW;  4F71D8E5A06D3EB9 CRC64;
     MERNVLTTFS QEMSQLILNE MPKAEYSSLF NDFVESEFFL IDGDSLLITC ICEISFKPGQ
     NLHFFYLVER YLVDLISKGG QFTIVFFKDA EYAYFNFPEL LSLRTALILH LQKNTTIDVR
     TTFSRCLSKE WGSFLEESYP YFLIVADEGL NDLQTQLFNF LIIHSWARKV NVVLSSGQES
     DVLCLYAYLL PSMYRHQIFS WKNKQNIKDA YTTLLNQLER FKLSALAPLF GSLKWNNITE
     EAHKTVSLLT QVWPEGSDIR RVFCVTSCSL SLRMYHRFLG NREPSSGQET EIQQVNSNCL
     TLQEMEDLCK LHCLTVVFLL HLPLSQRACA RVITSHWAED MKPLLQMKKW CEYFILRNIH
     TFEFWNLNLI HLSDLNDELL LKNIAFYYEN ENVKGLHLNL GDTIMKDYEY LWNTVSKLVR
     DFEVGQPFPL RTTKVCFLEK KPSPIKDSSN EMVPNLGFIP TSSFVVDKFA GDILKDLPFL
     KSDDPIVTSL VKQKEFDELV HWHSHKPLSD DYDRSRCQFD EKSRDPRVLR SVQKYHVFQR
     FYGNSLETVS SKIIVTQTIK SKKDFSGPKS KKAHETKAEI IARENKKRLF AREEQKEEQK
     WNALSFSIEE QLKENLHSGI KSLEDFLKSC KSSCVKLQVE MVGLTACLKA WKEHCRSEEG
     KTTKDLSIAV QVMKRIHSLM EKYSELLQED DRQLIARCLK YLGFDELASS LHPAQDAEND
     VKVKKRNKYS VGIGPARFQL QYMGHYLIRD ERKDPDPRVQ DFIPDTWQRE LLDVVDKNES
     AVIVAPTSSG KTYASYYCME KVLKESDDGV VVYVAPTKAL VNQVAATVQN RFTKNLPSGE
     VLCGVFTREY RHDALNCQVL ITVPACFEIL LLAPHRQNWV KKIRYVIFDE VHCLGGEIGA
     EIWEHLLVMI RCPFLALSAT ISNPEHLTEW LQSVKWYWKQ EDKIIENNTA SKRHVGRQAG
     FPKDYLQVKQ SYKVRLVLYG ERYNDLEKHV CSIKHGDIHF DHFHPCAALT TDHIERYGFP
     PDLTLSPRES IQLYDAMFQI WKSWPRAQEL CPENFIHFNN KLVIKKMDAR KYEESLKAEL
     TSWIKNGNVE QARMVLQNLS PEADLSPENM ITMFPLLVEK LRKMEKLPAL FFLFKLGAVE
     NAAESVSTFL KKKQETKRPP KADKEAHVMA NKLRKVKKSI EKQKIIDEKS QKKTRNVDQS
     LIHEAEHDNL VKCLEKNLEI PQDCTYADQK AVDTETLQKV FGRVKFERKG EELKALAERG
     IGYHHSAMSF KEKQLVEILF RKGYLRVVTA TGTLALGVNM PCKSVVFAQN SVYLDALNYR
     QMSGRAGRRG QDLMGDVYFF DIPFPKIGKL IKSNVPELRG HFPLSITLVL RLMLLASKGD
     DPEDAKAKVL SVLKHSLLSF KQPRVMDMLK LYFLFSLQFL VKEGYLDQEG NPMGFAGLVS
     HLHYHEPSNL VFVSFLVNGL FHDLCQPTRK GSKHFSQDVM EKLVLVLAHL FGRRYFPPKF
     QDAHFEFYQS KVFLDDLPED FSDALDEYNM KIMEDFTTFL RIVSKLADMN QEYQLPLSKI
     KFTGKECEDS QLVSHLMSCK EGRVAISPFV CLSGNFDDDL LRLETPNHVT LGTIGVNRSQ
     APVLLSQKFD NRGRKMSLNA YALDFYKHGS LIGLVQDNRM NEGDAYYLLK DFALTIKSIS
     VSLRELCENE DDNVVLAFEQ LSTTFWEKLN KV
 
 
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