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LIN54_DROME
ID   LIN54_DROME             Reviewed;         950 AA.
AC   A1Z9E2; Q5BIF2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Protein lin-54 homolog;
DE   AltName: Full=Myb complex protein of 120 kDa;
GN   Name=mip120; ORFNames=CG6061;
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] (ISOFORM 2).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP   DREAM COMPLEX.
RX   PubMed=12490953; DOI=10.1038/nature01228;
RA   Beall E.L., Manak J.R., Zhou S., Bell M., Lipsick J.S., Botchan M.R.;
RT   "Role for a Drosophila Myb-containing protein complex in site-specific DNA
RT   replication.";
RL   Nature 420:833-837(2002).
RN   [5]
RP   FUNCTION, AND IDENTIFICATION IN THE DREAM COMPLEX.
RX   PubMed=15479636; DOI=10.1016/j.cell.2004.09.034;
RA   Korenjak M., Taylor-Harding B., Binne U.K., Satterlee J.S., Stevaux O.,
RA   Aasland R., White-Cooper H., Dyson N., Brehm A.;
RT   "Native E2F/RBF complexes contain Myb-interacting proteins and repress
RT   transcription of developmentally controlled E2F target genes.";
RL   Cell 119:181-193(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=15256498; DOI=10.1101/gad.1206604;
RA   Beall E.L., Bell M., Georlette D., Botchan M.R.;
RT   "Dm-myb mutant lethality in Drosophila is dependent upon mip130: positive
RT   and negative regulation of DNA replication.";
RL   Genes Dev. 18:1667-1680(2004).
RN   [7]
RP   IDENTIFICATION IN THE DREAM COMPLEX.
RX   PubMed=15545624; DOI=10.1101/gad.1255204;
RA   Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J.,
RA   Botchan M.R.;
RT   "Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor
RT   complex.";
RL   Genes Dev. 18:2929-2940(2004).
RN   [8]
RP   FUNCTION.
RX   PubMed=18316477; DOI=10.1101/gad.1626308;
RA   Wen H., Andrejka L., Ashton J., Karess R., Lipsick J.S.;
RT   "Epigenetic regulation of gene expression by Drosophila Myb and E2F2-RBF
RT   via the Myb-MuvB/dREAM complex.";
RL   Genes Dev. 22:601-614(2008).
CC   -!- FUNCTION: Component of the DREAM complex, a multiprotein complex that
CC       can both act as a transcription activator or repressor depending on the
CC       context. In follicle cells, the complex plays a central role in the
CC       site-specific DNA replication at the chorion loci. During development,
CC       the complex represses transcription of developmentally controlled E2F
CC       target genes. {ECO:0000269|PubMed:12490953,
CC       ECO:0000269|PubMed:15256498, ECO:0000269|PubMed:15479636,
CC       ECO:0000269|PubMed:18316477}.
CC   -!- SUBUNIT: Component of the DREAM complex at least composed of Myb, Caf1-
CC       55, mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52, HDAC1/Rpd3 and
CC       l(3)mbt. {ECO:0000269|PubMed:12490953, ECO:0000269|PubMed:15479636,
CC       ECO:0000269|PubMed:15545624}.
CC   -!- INTERACTION:
CC       A1Z9E2; Q94517: HDAC1; NbExp=2; IntAct=EBI-75953, EBI-302197;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A1Z9E2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A1Z9E2-2; Sequence=VSP_034282, VSP_034283, VSP_034284;
CC   -!- SIMILARITY: Belongs to the lin-54 family. {ECO:0000305}.
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DR   EMBL; AE013599; AAF58365.1; -; Genomic_DNA.
DR   EMBL; BT021272; AAX33420.1; -; mRNA.
DR   RefSeq; NP_610879.1; NM_137035.2. [A1Z9E2-1]
DR   AlphaFoldDB; A1Z9E2; -.
DR   SMR; A1Z9E2; -.
DR   BioGRID; 62258; 21.
DR   DIP; DIP-61918N; -.
DR   IntAct; A1Z9E2; 20.
DR   STRING; 7227.FBpp0290602; -.
DR   PaxDb; A1Z9E2; -.
DR   PRIDE; A1Z9E2; -.
DR   EnsemblMetazoa; FBtr0087669; FBpp0086789; FBgn0033846. [A1Z9E2-1]
DR   GeneID; 36499; -.
DR   KEGG; dme:Dmel_CG6061; -.
DR   CTD; 36499; -.
DR   FlyBase; FBgn0033846; mip120.
DR   VEuPathDB; VectorBase:FBgn0033846; -.
DR   eggNOG; KOG1171; Eukaryota.
DR   InParanoid; A1Z9E2; -.
DR   OMA; KQMNPQQ; -.
DR   PhylomeDB; A1Z9E2; -.
DR   Reactome; R-DME-1538133; G0 and Early G1.
DR   BioGRID-ORCS; 36499; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; mip120; fly.
DR   GenomeRNAi; 36499; -.
DR   PRO; PR:A1Z9E2; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0033846; Expressed in egg chamber and 22 other tissues.
DR   ExpressionAtlas; A1Z9E2; baseline and differential.
DR   Genevisible; A1Z9E2; DM.
DR   GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR   GO; GO:0031523; C:Myb complex; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR   GO; GO:0007307; P:eggshell chorion gene amplification; IC:FlyBase.
DR   GO; GO:0030317; P:flagellated sperm motility; IMP:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   InterPro; IPR005172; CRC.
DR   InterPro; IPR028307; Lin-54_fam.
DR   InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR   PANTHER; PTHR12446; PTHR12446; 1.
DR   Pfam; PF03638; TCR; 2.
DR   SMART; SM01114; CXC; 2.
DR   PROSITE; PS51634; CRC; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cell cycle; DNA-binding; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..950
FT                   /note="Protein lin-54 homolog"
FT                   /id="PRO_0000341396"
FT   DOMAIN          737..849
FT                   /note="CRC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00971"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..688
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..8
FT                   /note="MDTSGGNL -> MSTYRVDYLT (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_034282"
FT   VAR_SEQ         535..558
FT                   /note="SASVSSEASDSSDAGPEAKKPRYV -> KAALRYYHAARITEGSFPASSETN
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_034283"
FT   VAR_SEQ         559..950
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_034284"
SQ   SEQUENCE   950 AA;  100022 MW;  627C3EA6B44A0A30 CRC64;
     MDTSGGNLDS LDDTEPLPEL SFEDFLEPTS EKSSQHMEIE ALDSEEDNIG GEDLADPAND
     SLNTPQFKKN VVHILEDKRL NSSGLTVLKS HAIKMVTAGG TPPAKAQVTD VKILNKLKPI
     PSSTLKIGST TIATKSTPGS ITKTLGNLTQ IRTKDGQVIF VQKSVPGTQS STAVTGSPSG
     GIRRLVAPSG IQKAVLSKGV TMASTGLVKA AVPAKASTSV PGSAITLKGI QPLAGGTAKA
     STSSTTATTS PSLAQPNKIQ VVRTADGKII KINQAGPSLL VNAKQGTGTT VTPGGSAATS
     VKLSPSTGNV VLNKPVGQVV VRTETPVKTA TGSVASASAT PGKMLVQSGG KQILVSNKNI
     IKLSPNASAT SSTTHTTGGQ TPSTSSGLHA IQLPGKGGIQ YVRVLNNNKS AAGTSATASI
     PKTVQTQKIT VVRPPAATGV PATSTTTSAA AASPAAASKA NLAMGNTNKI VMRSMGGSIV
     PLPSVQTLVS KRALGAISNA SKPASAASSS ATPSASQELP RKHRLTDLNV QLKQSASVSS
     EASDSSDAGP EAKKPRYVIT MQQGSQKAAS QPVQKLINRT ANVQRVVSSS TSPSSNSTKK
     IYNYVQPTGS NGAKYMICNS GVPQSSTSAM RRGYTGYVEN KTRRPPPISP QQHRFKQMGP
     QQQSKHQQLQ AQAKQRIRQQ QLPTEQSTPI KVEPKLPTLP PGVKANVPAK PLFEVLKPPA
     TAAAAGAVDP LGGMTSRRKH CNCSKSQCLK LYCDCFANGE FCQDCTCKDC FNNLDYEVER
     ERAIRSCLDR NPSAFKPKIT APNSGDMRLH NKGCNCKRSG CLKNYCECYE AKIPCSSICK
     CVGCRNMEDR PDVDMDSLDG LMGVEGQKKD KAKNKQLNEN RANIYFTDDV IEATIMCMIS
     RIVMHEKQNV AVEDMEREVM EEMGESLTQI IAFAKEKQET SQIDESKPSS
 
 
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