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ELP2_DROME
ID   ELP2_DROME              Reviewed;         794 AA.
AC   Q7K4B3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Elongator complex protein 2;
DE            Short=ELP2;
DE   AltName: Full=Stat3-interacting protein homolog;
GN   Name=Elp2; Synonyms=StIP; ORFNames=CG11887;
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=Embryo;
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   FUNCTION IN THE STAT PATHWAY.
RA   Han L., Harrison D.;
RT   "The function of StIP in the JAK/STAT pathway.";
RL   (In) Abstracts of the 47th Annual Drosophila Research Conference, pp.25-25,
RL   Houston (2006).
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) (By similarity). The elongator complex
CC       catalyzes the formation of carboxymethyluridine in the wobble base at
CC       position 34 in tRNAs (By similarity). Involved in the regulation of the
CC       STAT pathway (Ref.4). {ECO:0000250|UniProtKB:Q6IA86,
CC       ECO:0000269|Ref.4}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000250|UniProtKB:Q6IA86}.
CC   -!- SUBUNIT: Component of the elongator complex.
CC       {ECO:0000250|UniProtKB:Q6IA86}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6IA86}. Nucleus
CC       {ECO:0000250|UniProtKB:Q6IA86}.
CC   -!- DOMAIN: Folds into a two seven-bladed beta-propeller structure which is
CC       required for elongator complex assembly.
CC       {ECO:0000250|UniProtKB:P42935}.
CC   -!- SIMILARITY: Belongs to the WD repeat ELP2 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:Q6IA86}.
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DR   EMBL; AE013599; AAF58765.2; -; Genomic_DNA.
DR   EMBL; AY052019; AAK93443.1; -; mRNA.
DR   RefSeq; NP_610600.1; NM_136756.4.
DR   AlphaFoldDB; Q7K4B3; -.
DR   SMR; Q7K4B3; -.
DR   BioGRID; 61932; 2.
DR   IntAct; Q7K4B3; 2.
DR   STRING; 7227.FBpp0087307; -.
DR   PaxDb; Q7K4B3; -.
DR   PRIDE; Q7K4B3; -.
DR   EnsemblMetazoa; FBtr0088212; FBpp0087307; FBgn0033540.
DR   GeneID; 36123; -.
DR   KEGG; dme:Dmel_CG11887; -.
DR   CTD; 55250; -.
DR   FlyBase; FBgn0033540; Elp2.
DR   VEuPathDB; VectorBase:FBgn0033540; -.
DR   eggNOG; KOG0645; Eukaryota.
DR   eggNOG; KOG1063; Eukaryota.
DR   GeneTree; ENSGT00390000000916; -.
DR   HOGENOM; CLU_006430_1_0_1; -.
DR   InParanoid; Q7K4B3; -.
DR   OMA; EHTKRVN; -.
DR   OrthoDB; 461632at2759; -.
DR   PhylomeDB; Q7K4B3; -.
DR   UniPathway; UPA00988; -.
DR   BioGRID-ORCS; 36123; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 36123; -.
DR   PRO; PR:Q7K4B3; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0033540; Expressed in wing disc and 35 other tissues.
DR   Genevisible; Q7K4B3; DM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033588; C:elongator holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 2.130.10.10; -; 5.
DR   InterPro; IPR037289; Elp2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR44111; PTHR44111; 1.
DR   Pfam; PF00400; WD40; 7.
DR   SMART; SM00320; WD40; 11.
DR   SUPFAM; SSF50978; SSF50978; 3.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 7.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Reference proteome; Repeat; tRNA processing; WD repeat.
FT   CHAIN           1..794
FT                   /note="Elongator complex protein 2"
FT                   /id="PRO_0000284002"
FT   REPEAT          55..93
FT                   /note="WD 1"
FT   REPEAT          98..140
FT                   /note="WD 2"
FT   REPEAT          147..188
FT                   /note="WD 3"
FT   REPEAT          203..244
FT                   /note="WD 4"
FT   REPEAT          286..328
FT                   /note="WD 5"
FT   REPEAT          337..376
FT                   /note="WD 6"
FT   REPEAT          384..423
FT                   /note="WD 7"
FT   REPEAT          433..472
FT                   /note="WD 8"
FT   REPEAT          557..601
FT                   /note="WD 9"
FT   REPEAT          604..643
FT                   /note="WD 10"
FT   REPEAT          654..693
FT                   /note="WD 11"
FT   REPEAT          705..751
FT                   /note="WD 12"
FT   REPEAT          759..794
FT                   /note="WD 13"
SQ   SEQUENCE   794 AA;  88974 MW;  F13A7F063716F9D0 CRC64;
     MQVENLHTSV ACNRCTECAD WGPNGWIAYG ACNAIAIMDP KFQGNSAKVL FTLVEHTKRV
     NTVRWLDCDK LLSGGDDAIA ILWELDETGT TKSFTLKGHT SGVNTVDGIR QQDGSWLLAT
     AAADTTIKLW TFQDNNYVCF QTISLSDGFC FCLRLQLLPK SNQVLLAFSG DDETVSLWSE
     QVETAGEGDS LGRQFQRKHK LTGHEDWVRG LDFVVDGEDL LLASGSQDNF IRLWRIAPRS
     KEQMQENRVD LHQLSHNDDE IKVEEKILQL GKEAWYAVSL ESVLYGHEGW IYGVHWHKTP
     DQELRLLSAS IDKTVIIWAP TEEGIWLEEV RVGEVGGNSV GFYGGKFSGD GHSIMAHSYQ
     GGFHIWSQDP DRPQLWTPGV IVGGHYGEVR DLAWEHSGAY LMTASADQTT RLHAPWLQDG
     ANPTWHELAR PQIHGYDMQA LALLSRYKFA SGAEEKIVRT FQAPANFIEN FRHISGIEND
     DAGDVLLDSL PKGASVPSLG LSNKAVYKVD SEVESTSKTS KDEYPDNYFV PIALETPPQE
     ETLMQNTLWP ELQKLYGHGY EIFALAATAD GSLLASTCKA SNAEHAQIIL WNPSNWKQIQ
     KLSGHQLTVT QLSFSPDSRY LLSVSRDRRW CLYERQDSSV SYQLVASTDK SNGVHTRIIW
     SCDWSHDGQF FVTSSRDGKV VVWKKEEDCK ESSLNGWQAN GVLELKNESI TAVAFSNSYL
     SGTDDTYILA LGTETGLIKI YQFVRGAWKL LSDLNKSQAH HLTVRRLQFR PGKQLQLASC
     GEDHLVRIYD IKLT
 
 
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