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ELP4_DROME
ID   ELP4_DROME              Reviewed;         437 AA.
AC   Q9VMQ7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Elongator complex protein 4;
DE            Short=ELP4;
GN   ORFNames=CG6907;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Testis;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-242, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Component of the elongator complex which is required for
CC       multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC       uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC       (5-carbamoylmethyl uridine). The elongator complex catalyzes the
CC       formation of carboxymethyluridine in the wobble base at position 34 in
CC       tRNAs. {ECO:0000250|UniProtKB:Q96EB1}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000250|UniProtKB:Q96EB1}.
CC   -!- SUBUNIT: Component of the elongator complex.
CC       {ECO:0000250|UniProtKB:Q96EB1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96EB1}. Nucleus
CC       {ECO:0000250|UniProtKB:Q96EB1}.
CC   -!- SIMILARITY: Belongs to the ELP4 family. {ECO:0000305}.
CC   -!- CAUTION: The elongator complex was originally thought to play a role in
CC       transcription elongation. However, it is no longer thought to play a
CC       direct role in this process and its primary function is thought to be
CC       in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}.
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DR   EMBL; AE014134; AAF52255.1; -; Genomic_DNA.
DR   EMBL; AY075211; AAL68078.1; -; mRNA.
DR   RefSeq; NP_001285628.1; NM_001298699.1.
DR   RefSeq; NP_608932.1; NM_135088.2.
DR   AlphaFoldDB; Q9VMQ7; -.
DR   SMR; Q9VMQ7; -.
DR   BioGRID; 59943; 5.
DR   IntAct; Q9VMQ7; 1.
DR   STRING; 7227.FBpp0078729; -.
DR   iPTMnet; Q9VMQ7; -.
DR   PaxDb; Q9VMQ7; -.
DR   PRIDE; Q9VMQ7; -.
DR   DNASU; 33775; -.
DR   EnsemblMetazoa; FBtr0079096; FBpp0078729; FBgn0031711.
DR   EnsemblMetazoa; FBtr0343257; FBpp0309927; FBgn0031711.
DR   GeneID; 33775; -.
DR   KEGG; dme:Dmel_CG6907; -.
DR   UCSC; CG6907-RA; d. melanogaster.
DR   FlyBase; FBgn0031711; CG6907.
DR   VEuPathDB; VectorBase:FBgn0031711; -.
DR   eggNOG; KOG3949; Eukaryota.
DR   HOGENOM; CLU_031345_3_1_1; -.
DR   InParanoid; Q9VMQ7; -.
DR   OMA; NTTMWDD; -.
DR   OrthoDB; 973442at2759; -.
DR   PhylomeDB; Q9VMQ7; -.
DR   UniPathway; UPA00988; -.
DR   BioGRID-ORCS; 33775; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 33775; -.
DR   PRO; PR:Q9VMQ7; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0031711; Expressed in secondary oocyte and 36 other tissues.
DR   ExpressionAtlas; Q9VMQ7; baseline and differential.
DR   Genevisible; Q9VMQ7; DM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0033588; C:elongator holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR   GO; GO:0008607; F:phosphorylase kinase regulator activity; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR008728; Elongator_complex_protein_4.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12896; PTHR12896; 1.
DR   Pfam; PF05625; PAXNEB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT   CHAIN           1..437
FT                   /note="Elongator complex protein 4"
FT                   /id="PRO_0000284010"
FT   REGION          179..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   437 AA;  48712 MW;  638DAE60A4827247 CRC64;
     MTSFRKRTVQ KPIRGTRTSP HTAQVITSSG NPYLDVVIGG GLPMGSICLI EEDRFMTHAK
     VLAKYFLAEG VISKQEIFLG SLDDIPAEML RRLPRPLTDQ ESMEQSEVQA LGDAGAENGL
     RIAWRYNDLP LVNSEHATAK IGHHFNLMEQ MDSMMLYNVK TTLWDDSPKH LDIVIDEEFS
     KSSSPTTPSL EQQPVEDAPP IPGTETAPQE KMPAQEEENS ANNNNNNNNN SSSVTSSTKT
     GSQDSPLQVF HNPRYKGLLN DIQQLLRNES FVAGTKNNLC RVCLTSLGSP LWYDEHFGED
     LIKFLTLLMA SVRNCNSVCL ITMPMHLIAK YDASLVPKIR QLVDYAIELE SFAGSERETH
     PAFKEYSGLL HLHKMSAINT LAVHMPETPD LAFKLRRKKF IIEKFHLPPE LQESSAKPDN
     CISGLLSNSN ATASLDF
 
 
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