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NEUR_DROME
ID   NEUR_DROME              Reviewed;         754 AA.
AC   P29503; Q26306; Q27273; Q8INP6; Q8INP7; Q960M1;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 190.
DE   RecName: Full=Protein neuralized;
GN   Name=neur; Synonyms=neu; ORFNames=CG11988;
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] (ISOFORM 2).
RC   STRAIN=Oregon-R;
RX   PubMed=1717258; DOI=10.1002/j.1460-2075.1991.tb07848.x;
RA   Boulianne G.L., de la Concha A., Campos-Ortega J.A., Jan L.Y., Jan Y.N.;
RT   "The Drosophila neurogenic gene neuralized encodes a novel protein and is
RT   expressed in precursors of larval and adult neurons.";
RL   EMBO J. 10:2975-2983(1991).
RN   [2]
RP   ERRATUM OF PUBMED:1717258.
RX   PubMed=8508781; DOI=10.1002/j.1460-2075.1993.tb05914.x;
RA   Boulianne G.L., de la Concha A., Campos-Ortega J.A., Jan L.Y., Jan Y.N.;
RL   EMBO J. 12:2586-2586(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8508767; DOI=10.1002/j.1460-2075.1993.tb05895.x;
RA   Price B.D., Chang Z., Smith R., Bockheim S., Laughon A.;
RT   "The Drosophila neuralized gene encodes a C3HC4 zinc finger.";
RL   EMBO J. 12:2411-2418(1993).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=Berkeley;
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 AND SER-341, 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   STRUCTURE BY NMR OF 106-266.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the neuz (NHR) domain in neuralized from Drosophila
RT   melanogaster.";
RL   Submitted (OCT-2007) to the PDB data bank.
CC   -!- FUNCTION: Involved in neurogenesis. Interacts with other neurogenic
CC       proteins in the specification of the neuroblast versus epidermoblast
CC       cell fate.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P29503-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P29503-2; Sequence=VSP_008046;
CC       Name=3;
CC         IsoId=P29503-3; Sequence=VSP_008045;
CC       Name=4;
CC         IsoId=P29503-4; Sequence=VSP_008045, VSP_008046;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA43806.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X61617; CAA43806.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; S62597; AAB27151.1; -; mRNA.
DR   EMBL; S62583; AAB27147.1; -; mRNA.
DR   EMBL; L12218; AAA28403.1; -; mRNA.
DR   EMBL; AE014297; AAF54330.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF54326.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13406.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13407.1; -; Genomic_DNA.
DR   EMBL; AY051987; AAK93411.1; -; mRNA.
DR   EMBL; BT003772; AAO41451.1; -; mRNA.
DR   PIR; S35371; S35371.
DR   PIR; S35503; S35503.
DR   RefSeq; NP_001163563.1; NM_001170092.3. [P29503-3]
DR   RefSeq; NP_476652.1; NM_057304.5. [P29503-1]
DR   RefSeq; NP_731309.1; NM_169255.3. [P29503-4]
DR   RefSeq; NP_731310.1; NM_169256.3. [P29503-3]
DR   RefSeq; NP_731311.1; NM_169257.3. [P29503-2]
DR   PDB; 2YUE; NMR; -; A=106-266.
DR   PDB; 4KG0; X-ray; 2.10 A; A=105-260.
DR   PDBsum; 2YUE; -.
DR   PDBsum; 4KG0; -.
DR   AlphaFoldDB; P29503; -.
DR   SMR; P29503; -.
DR   BioGRID; 66253; 29.
DR   DIP; DIP-17176N; -.
DR   IntAct; P29503; 4.
DR   MINT; P29503; -.
DR   STRING; 7227.FBpp0081481; -.
DR   iPTMnet; P29503; -.
DR   PaxDb; P29503; -.
DR   DNASU; 41085; -.
DR   EnsemblMetazoa; FBtr0082001; FBpp0081479; FBgn0002932. [P29503-3]
DR   EnsemblMetazoa; FBtr0082002; FBpp0081480; FBgn0002932. [P29503-4]
DR   EnsemblMetazoa; FBtr0082003; FBpp0081481; FBgn0002932. [P29503-1]
DR   EnsemblMetazoa; FBtr0082004; FBpp0081482; FBgn0002932. [P29503-2]
DR   EnsemblMetazoa; FBtr0300414; FBpp0289643; FBgn0002932. [P29503-3]
DR   GeneID; 41085; -.
DR   KEGG; dme:Dmel_CG11988; -.
DR   UCSC; CG11988-RA; d. melanogaster. [P29503-1]
DR   CTD; 41085; -.
DR   FlyBase; FBgn0002932; neur.
DR   VEuPathDB; VectorBase:FBgn0002932; -.
DR   eggNOG; KOG4172; Eukaryota.
DR   eggNOG; KOG4625; Eukaryota.
DR   GeneTree; ENSGT00940000166233; -.
DR   InParanoid; P29503; -.
DR   OMA; AMCPIPQ; -.
DR   PhylomeDB; P29503; -.
DR   SignaLink; P29503; -.
DR   BioGRID-ORCS; 41085; 0 hits in 3 CRISPR screens.
DR   EvolutionaryTrace; P29503; -.
DR   GenomeRNAi; 41085; -.
DR   PRO; PR:P29503; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0002932; Expressed in mesectoderm and 85 other tissues.
DR   ExpressionAtlas; P29503; baseline and differential.
DR   Genevisible; P29503; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:FlyBase.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:Reactome.
DR   GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR   GO; GO:0008356; P:asymmetric cell division; IMP:FlyBase.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR   GO; GO:0007498; P:mesoderm development; IMP:FlyBase.
DR   GO; GO:0035204; P:negative regulation of lamellocyte differentiation; IMP:FlyBase.
DR   GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR   GO; GO:0007400; P:neuroblast fate determination; IMP:FlyBase.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:FlyBase.
DR   GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:FlyBase.
DR   GO; GO:0045314; P:regulation of compound eye photoreceptor development; IMP:FlyBase.
DR   GO; GO:0046532; P:regulation of photoreceptor cell differentiation; IMP:FlyBase.
DR   GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR   GO; GO:0016360; P:sensory organ precursor cell fate determination; IDA:FlyBase.
DR   GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR   Gene3D; 2.60.120.920; -; 2.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR037962; Neuralized.
DR   InterPro; IPR006573; NHR_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12429; PTHR12429; 1.
DR   Pfam; PF07177; Neuralized; 2.
DR   SMART; SM00588; NEUZ; 2.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS51065; NHR; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Developmental protein; Differentiation;
KW   DNA-binding; Metal-binding; Neurogenesis; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..754
FT                   /note="Protein neuralized"
FT                   /id="PRO_0000055975"
FT   DOMAIN          106..260
FT                   /note="NHR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00400"
FT   DOMAIN          368..523
FT                   /note="NHR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00400"
FT   ZN_FING         701..742
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          280..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         338
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         1..90
FT                   /note="MGLSDIPANYMQGSHPHLTLHPQQQHHQNQQHLQHLQQMQQLHNAMPTPAQQ
FT                   AAQVLAMESNELLMSTKDKLSSKKKMHLLKKIKKRFGL -> MGQSAGKI (in
FT                   isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_008045"
FT   VAR_SEQ         672
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12537569,
FT                   ECO:0000303|PubMed:1717258"
FT                   /id="VSP_008046"
FT   CONFLICT        234
FT                   /note="T -> S (in Ref. 1; CAA43806)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="A -> V (in Ref. 3; AAB27151)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        588
FT                   /note="T -> N (in Ref. 3; AAB27151)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        694
FT                   /note="S -> R (in Ref. 3; AAB27151)"
FT                   /evidence="ECO:0000305"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:2YUE"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          130..133
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          136..141
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          149..156
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          158..162
FT                   /evidence="ECO:0007829|PDB:2YUE"
FT   STRAND          165..171
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   HELIX           184..188
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          209..214
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          227..233
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          242..247
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   STRAND          250..257
FT                   /evidence="ECO:0007829|PDB:4KG0"
FT   HELIX           260..263
FT                   /evidence="ECO:0007829|PDB:2YUE"
SQ   SEQUENCE   754 AA;  82325 MW;  A2887404502D70BF CRC64;
     MGLSDIPANY MQGSHPHLTL HPQQQHHQNQ QHLQHLQQMQ QLHNAMPTPA QQAAQVLAME
     SNELLMSTKD KLSSKKKMHL LKKIKKRFGL VRRSPSSCPG PNNLPPLQFH SVHGDNIRIS
     RDGTLARRFE SFCRAITFSA RPVRINERIC VKFAEISNNW NGGIRFGFTS NDPVTLEGTL
     PKYACPDLTN RPGFWAKALH EQYCEKDNIL YYYVNGAGDV IYGINNEEKG VILTGIDTRS
     LLWTVIDIYG NCTGIEFLDS RIYMYQQQPA AIPMATVPAQ QQQMPQPAAN ASSALNSHHP
     HQQSRRSLPG HTAAIEHDLE RHVMPSLQSL HLAGNGGSVA SVEQAAIAHD LANGLPPLRY
     NANGRLIPVP FHNTKGRNVR LSQDRFVASR TESDFCQGYV FTARPIRIGE KLIVQVLKTE
     QMYVGALALG LTSCNPAMLQ PNDLPNDSDF LLDRPEYWVV SKDIAAAPQR GDEIAFFVAP
     NGEVSISKNN GPAVVVMHVD QSLQLWAFLD VYGSTQSLRM FRQQLPNMVA YPSQPQVNVN
     ASSSSACNAA STSRMLPMTE SMSSLNAGAT AKLLHHPSQL SVAQSTSTLA SAGGVNGSRM
     ISMPSNGDIL QIQPNGGGTV LVVNLPPASS SHDINGQLAA RPTATVTSSG VLAGACSSGT
     LISTTSSQYI EQPIANSTNN AANKWKDSLS DQQSTDSSAE CTICYENPID SVLYMCGHMC
     MCYDCAIEQW RGVGGGQCPL CRAVIRDVIR TYTT
 
 
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