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SAYP_DROME
ID   SAYP_DROME              Reviewed;        2006 AA.
AC   Q9VWF2; C7LAD9; Q7JW70;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 3.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Supporter of activation of yellow protein;
DE   AltName: Full=Protein enhancer of yellow 3;
GN   Name=e(y)3; Synonyms=l(1)G0084, SAYP; ORFNames=CG12238;
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;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-2006.
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   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND DOMAIN.
RX   PubMed=15616585; DOI=10.1038/sj.emboj.7600508;
RA   Shidlovskii Y.V., Krasnov A.N., Nikolenko J.V., Lebedeva L.A.,
RA   Kopantseva M., Ermolaeva M.A., Ilyin Y.V., Nabirochkina E.N.,
RA   Georgiev P.G., Georgieva S.G.;
RT   "A novel multidomain transcription coactivator SAYP can also repress
RT   transcription in heterochromatin.";
RL   EMBO J. 24:97-107(2005).
CC   -!- FUNCTION: Essential transcription regulator during early development.
CC       Coactivates transcription of some euchromatin genes and repress
CC       transcription in of euchromatin genes translocated to heterochromatin.
CC       {ECO:0000269|PubMed:15616585}.
CC   -!- INTERACTION:
CC       Q9VWF2; A1Z6M0: Bap170; NbExp=5; IntAct=EBI-131186, EBI-126851;
CC       Q9VWF2; P49846: Taf5; NbExp=5; IntAct=EBI-131186, EBI-15595394;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15616585}. Cytoplasm
CC       {ECO:0000269|PubMed:15616585}. Chromosome
CC       {ECO:0000269|PubMed:15616585}. Note=On polytene chromosomes, it mainly
CC       localizes to transcriptionally active euchromatin sites but also
CC       localizes to heterochromatic regions such as the chromocenter and the
CC       chromosome 4. Cytoplasmic in nursing cells and growing oocytes.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in ovary.
CC       Expressed in nursing cells and growing oocytes at all stages of
CC       development and accumulates in mature oocytes. Expressed in the nuclei
CC       of syncytium blastoderm of early embryos and in the nuclei of different
CC       tissues of late embryos, larvae, and adults.
CC       {ECO:0000269|PubMed:15616585}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout all stages of development.
CC       Expressed at higher level in adult females.
CC       {ECO:0000269|PubMed:15616585}.
CC   -!- DOMAIN: The PHD fingers mediate the transcription repression in
CC       heterochromatin. {ECO:0000269|PubMed:15616585}.
CC   -!- DOMAIN: The SAY domain is essential for fly viability and transcription
CC       activation. {ECO:0000269|PubMed:15616585}.
CC   -!- SIMILARITY: Belongs to the SAYP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM48352.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014298; AAF48990.3; -; Genomic_DNA.
DR   EMBL; BT099689; ACV44475.1; -; mRNA.
DR   EMBL; AY118323; AAM48352.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001259718.1; NM_001272789.1.
DR   RefSeq; NP_001259721.1; NM_001272792.1.
DR   RefSeq; NP_608334.3; NM_134490.3.
DR   AlphaFoldDB; Q9VWF2; -.
DR   SMR; Q9VWF2; -.
DR   BioGRID; 59261; 28.
DR   DIP; DIP-48904N; -.
DR   IntAct; Q9VWF2; 26.
DR   MINT; Q9VWF2; -.
DR   STRING; 7227.FBpp0074531; -.
DR   PaxDb; Q9VWF2; -.
DR   PRIDE; Q9VWF2; -.
DR   DNASU; 32965; -.
DR   EnsemblMetazoa; FBtr0074762; FBpp0074531; FBgn0087008.
DR   EnsemblMetazoa; FBtr0334278; FBpp0306393; FBgn0087008.
DR   EnsemblMetazoa; FBtr0334281; FBpp0306396; FBgn0087008.
DR   GeneID; 32965; -.
DR   KEGG; dme:Dmel_CG12238; -.
DR   CTD; 32965; -.
DR   FlyBase; FBgn0087008; e(y)3.
DR   VEuPathDB; VectorBase:FBgn0087008; -.
DR   eggNOG; KOG1512; Eukaryota.
DR   GeneTree; ENSGT00940000155172; -.
DR   InParanoid; Q9VWF2; -.
DR   OrthoDB; 708781at2759; -.
DR   PhylomeDB; Q9VWF2; -.
DR   SignaLink; Q9VWF2; -.
DR   BioGRID-ORCS; 32965; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 32965; -.
DR   PRO; PR:Q9VWF2; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0087008; Expressed in second segment of antenna (Drosophila) and 47 other tissues.
DR   ExpressionAtlas; Q9VWF2; baseline and differential.
DR   Genevisible; Q9VWF2; DM.
DR   GO; GO:0035060; C:brahma complex; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR   GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR   GO; GO:0005701; C:polytene chromosome chromocenter; IDA:UniProtKB.
DR   GO; GO:0031213; C:RSF complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IGI:FlyBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   Activator; Chromosome; Cytoplasm; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..2006
FT                   /note="Supporter of activation of yellow protein"
FT                   /id="PRO_0000059340"
FT   ZN_FING         1694..1751
FT                   /note="PHD-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         1753..1796
FT                   /note="PHD-type 2; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          1..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          929..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1082
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1099..1196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1340..1573
FT                   /note="SAY"
FT   REGION          1579..1685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1887..1911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..535
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..758
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..844
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..976
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        977..1029
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1167..1184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1599..1615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1623..1685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1887..1910
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2006 AA;  212726 MW;  B1567640FB4E5084 CRC64;
     MNDLRQQQMV AATSSSGSES GTAVESAAAT STAGSAGAAG RPQSNCSANS NAKSVAASST
     SEEEQRVSST SSPAQRDQQL NADRDREQEP EPQQQQQREE ALQHQHNQPG HITSTTASPP
     PTLPPPTTPC DDAPSTTGAS ASASSASGEA PSAASAAGAA GGPMAATALE VESEERDGHK
     IILKLSKHAN PNSNANESQP GGDERRVEPL RIQLPCGGAE GGLVAKQQDA FDADASSCSS
     SCAEDEVATT LGQQLRNTPH IVPKLTIRAA NERRVGSVVP KLTIKLPENP AASGSNSNSG
     SCSAAVSGAQ SAMPAKNDAH LSSLSPASAS SSSASSSSSS SSSSSLAEMQ TVPKLMIKTT
     LAGSSCISSS EELPQQQQQI PKLTIKTGGG GQEHVHTVIM THDLNNAQSI PKLTIKTKSI
     EMIEDEQAAK LEQQLQPLPK LTIKNLCSPK HKVRAVLEEK PPTAASKLAI PKPTPNPTPA
     PMTNGGESNS SSQEFCGFSD PDADIAAPAS DDVRRNSDDM VIDDSLSKEH DPKIFHNLPP
     MPASNGIASG GSKASKASKS AQSQHNVVDM VDLTSSPSPG SSPTHVPNNF TGRISPKGLL
     IDCLRMQTAI GCYVPEEADS RVRPAASPNS NILLSQLTAP AKSFTTTTPK SKSSKYPQLT
     ERLMANGSGT GGGSVIAAES EAVVGPLPAA NPAQSIIESI EILDTPDGSP RVAYMDEDSN
     PMLNKHLQTI HKLAMDHGVE QRMDTQDNNN ENHLKRTNSE GNESPSSRLP PSKQRRLDND
     ENDQQTQNCH DPARKCSESL QALPPSHRSR KQKHERILNT DLEGSLFPPT QQQSISTPDQ
     NGALSSEVEG EDAKAQDPLE PATPQPPPVA TPAGTGKKRG RPKRIQNQSS PDGGGAVTPK
     PGTPQEEANS AVKSRRVQLL RKRLAIDMVS VGQEQADMKA KEKESSVGVP NARVEDGLAE
     TLESPKTRDH RPLRATRRTT TSTNTNLQPT PKSTRKRQSK ASVQQSQLPP PTMAQFGSSE
     SESNNNNNSS ISFALSAQID LTMCSSSSST SSGAAANQQV IGGSGSSSML PPTTILSSSD
     PLPDVIFQPN DFSSIMATQQ LRSSRPSSIS CGSTGGSQPD CHDEDNYTSA LDNSGDETAL
     PMPPTRGRGR GRRSRGGRGR GSSSVDRAVS VGGTASTTPA TQPRAPRMSR GASAVAKAIA
     MSRPRCVGGL KHQPDPERLK GLFSPSPQVF EEDTRMSADL SNSNQSMASL MEPPLTPQKQ
     PDFLNNEESQ SSMVSNVSMM DSNQGQSADA ILGSALKRPK KKKMETCVAE DTDYSASSIA
     EYDWPPPKGC CPSKNRDTFM IQEQVALYLG ITSFKRKYPD LPRRSVDMEE RNWLQEKGLV
     SEKLCDLGIT AVWASDILDI MYADFFDKYE EYKEYIRRKH LREIEAKQKA LGLTVGAGRG
     LQARDRAMLS ATKWNAYFNK SRKDERQSCM DLQTFTINQP QPRTAPTCTR LERSTSDLIR
     AVAEEANIPA PPNLLPPRDY DEAFRNSDYA YPLTVVPDQF SMAYRQFEPA ELRAYPLDTA
     LDKPPTDLMA QLLQAKSEAV GSDEIKTSAP APKDLGQEQS AIKSVTVTAP VRRSRRSTRQ
     QTDKVRTASS SSTSSAQSVS SASSGNGSSS DTESGDESDF SSTSSCSSST GASSGAGSED
     EDGNECSSSV RLSTCGVCLR SQHRNARDMP EAFIRCYTCR KRVHPSCVDM PPRMVGRVRN
     YNWQCAGCKC CIKCRSSQRP GKMLYCEQCD RGYHIYCLGL RTVPDGRWSC ERCCFCMRCG
     ATKPEGLPQV AALSQASGGP SANGDRSKAA RNKRLKWVHE YRIDHVTKIR EHAAMFCVPC
     ARNKPAKRQS AAGAAGAAAV TPVLEATSAQ TDDSPMPSPG LTTNGGRALS PTAALSPKAA
     VPVASLPPVL EATTVTTNIA GTIGRRQAGN AVNITTMQCS SSSSSNFSGN GVTEDAANVT
     ATGTATAAAG APAATPIGIA PPPVVA
 
 
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