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TWIST_DROME
ID   TWIST_DROME             Reviewed;         490 AA.
AC   P10627; Q1LZ34; Q8MT07; Q8T8Y9; Q9W1W1;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   03-AUG-2022, entry version 199.
DE   RecName: Full=Protein twist;
GN   Name=twi; ORFNames=CG2956;
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 [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=Oregon-R;
RX   PubMed=3416836; DOI=10.1002/j.1460-2075.1988.tb03056.x;
RA   Thisse B., Stoetzel C., Gorostiza-Thisse C., Perrin-Schmitt F.;
RT   "Sequence of the twist gene and nuclear localization of its protein in
RT   endomesodermal cells of early Drosophila embryos.";
RL   EMBO J. 7:2175-2183(1988).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA   Celniker S.E.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=1765010; DOI=10.1242/dev.113.1.79;
RA   Bate M., Rushton E., Currie D.A.;
RT   "Cells with persistent twist expression are the embryonic precursors of
RT   adult muscles in Drosophila.";
RL   Development 113:79-89(1991).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 AND SER-328, 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).
RN   [8]
RP   INTERACTION WITH AKIRIN.
RX   PubMed=22396663; DOI=10.1371/journal.pgen.1002547;
RA   Nowak S.J., Aihara H., Gonzalez K., Nibu Y., Baylies M.K.;
RT   "Akirin links twist-regulated transcription with the Brahma chromatin
RT   remodeling complex during embryogenesis.";
RL   PLoS Genet. 8:e1002547-e1002547(2012).
CC   -!- FUNCTION: Involved in the establishment and dorsoventral patterning of
CC       germ layers in the embryo. {ECO:0000269|PubMed:3416836}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Homodimer. Interacts with akirin (PubMed:22396663).
CC       {ECO:0000269|PubMed:22396663}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC       ECO:0000269|PubMed:3416836}.
CC   -!- TISSUE SPECIFICITY: Expressed in embryonic abdomen; a single cell
CC       ventrally, pairs of cells laterally and three cells dorsally in each
CC       hemisegment. In the thorax, there are patches of cells associated with
CC       the imaginal disks. During larval development, cells proliferate and,
CC       in the abdomen, they form ventral, lateral and dorsal clusters, which
CC       are the precursors of the adult abdominal muscles. In the thorax, they
CC       form populations of cells in the imaginal disks that correspond to the
CC       adepithelial cells. {ECO:0000269|PubMed:1765010}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC   -!- DISRUPTION PHENOTYPE: Embryos fail to form the ventral furrow at
CC       gastrulation and lack mesoderm and all internal organs.
CC       {ECO:0000269|PubMed:3416836}.
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DR   EMBL; X12506; CAA31024.1; -; Genomic_DNA.
DR   EMBL; X14569; CAA32707.1; -; mRNA.
DR   EMBL; AE013599; AAF46941.1; -; Genomic_DNA.
DR   EMBL; AE013599; ABC66041.1; -; Genomic_DNA.
DR   EMBL; AY075213; AAL68080.1; -; mRNA.
DR   EMBL; AY118454; AAM49823.1; -; mRNA.
DR   EMBL; BT025192; ABF17883.1; -; mRNA.
DR   PIR; S00995; S00995.
DR   RefSeq; NP_001033967.1; NM_001038878.2.
DR   RefSeq; NP_001286752.1; NM_001299823.1.
DR   RefSeq; NP_523816.2; NM_079092.3.
DR   AlphaFoldDB; P10627; -.
DR   SMR; P10627; -.
DR   BioGRID; 63264; 16.
DR   IntAct; P10627; 1.
DR   STRING; 7227.FBpp0071864; -.
DR   iPTMnet; P10627; -.
DR   PaxDb; P10627; -.
DR   EnsemblMetazoa; FBtr0071953; FBpp0071864; FBgn0003900.
DR   EnsemblMetazoa; FBtr0100130; FBpp0099476; FBgn0003900.
DR   EnsemblMetazoa; FBtr0345653; FBpp0311714; FBgn0003900.
DR   GeneID; 37655; -.
DR   KEGG; dme:Dmel_CG2956; -.
DR   UCSC; CG2956-RA; d. melanogaster.
DR   UCSC; CG2956-RB; d. melanogaster.
DR   CTD; 37655; -.
DR   FlyBase; FBgn0003900; twi.
DR   VEuPathDB; VectorBase:FBgn0003900; -.
DR   eggNOG; KOG4447; Eukaryota.
DR   GeneTree; ENSGT00940000172846; -.
DR   HOGENOM; CLU_529215_0_0_1; -.
DR   InParanoid; P10627; -.
DR   OMA; MQPEHKK; -.
DR   OrthoDB; 897131at2759; -.
DR   PhylomeDB; P10627; -.
DR   SignaLink; P10627; -.
DR   BioGRID-ORCS; 37655; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 37655; -.
DR   PRO; PR:P10627; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0003900; Expressed in mesoderm anlage and 31 other tissues.
DR   ExpressionAtlas; P10627; baseline and differential.
DR   Genevisible; P10627; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0031032; P:actomyosin structure organization; IMP:FlyBase.
DR   GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR   GO; GO:0007499; P:ectoderm and mesoderm interaction; NAS:FlyBase.
DR   GO; GO:0007369; P:gastrulation; IMP:UniProtKB.
DR   GO; GO:0010004; P:gastrulation involving germ band extension; TAS:FlyBase.
DR   GO; GO:0007507; P:heart development; TAS:FlyBase.
DR   GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
DR   GO; GO:0007498; P:mesoderm development; IEP:FlyBase.
DR   GO; GO:0001710; P:mesodermal cell fate commitment; IMP:UniProtKB.
DR   GO; GO:0007501; P:mesodermal cell fate specification; TAS:FlyBase.
DR   GO; GO:0055001; P:muscle cell development; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR   GO; GO:0016202; P:regulation of striated muscle tissue development; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR   GO; GO:0007370; P:ventral furrow formation; IMP:UniProtKB.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR015789; Twist-related.
DR   PANTHER; PTHR23349:SF50; PTHR23349:SF50; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..490
FT                   /note="Protein twist"
FT                   /id="PRO_0000127478"
FT   DOMAIN          362..413
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          48..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CONFLICT        44
FT                   /note="Q -> H (in Ref. 1; CAA31024/CAA32707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="T -> A (in Ref. 1; CAA31024/CAA32707 and 4;
FT                   AAL68080)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251
FT                   /note="L -> Q (in Ref. 1; CAA31024/CAA32707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251
FT                   /note="Missing (in Ref. 4; AAL68080/AAM49823)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        453
FT                   /note="A -> G (in Ref. 1; CAA31024)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   490 AA;  54422 MW;  AEB0D4D4EEE97DB7 CRC64;
     MMSARSVSPK VLLDISYKPT LPNIMELQNN VIKLIQVEQQ AYMQSGYQLQ HQQQHLHSHQ
     HHQQHHQQQH AQYAPLPSEY AAYGITELED TDYNIPSNEV LSTSSNQSAQ STSLELNNNN
     TSSNTNSSGN NPSGFDGQAS SGSSWNEHGK RARSSGDYDC QTGGSLVMQP EHKKLIHQQQ
     QQQQQHQQQI YVDYLPTTVD EVASAQSCPG VQSTCTSPQS HFDFPDEELP EHKAQVFLPL
     YNNQQQQSQQ LQQQQPHQQS HAQMHFQNAY RQSFEGYEPA NSLNGSAYSS SDRDDMEYAR
     HNALSSVSDL NGGVMSPACL ADDGSAGSLL DGSDAGGKAF RKPRRRLKRK PSKTEETDEF
     SNQRVMANVR ERQRTQSLND AFKSLQQIIP TLPSDKLSKI QTLKLATRYI DFLCRMLSSS
     DISLLKALEA QGSPSAYGSA SSLLSAAANG AEADLKCLRK ANGAPIIPPE KLSYLFGVWR
     MEGDAQHQKA
 
 
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