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DCTN2_DROME
ID   DCTN2_DROME             Reviewed;         380 AA.
AC   Q7K2D2;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Dynactin subunit 2;
DE            Short=Dynamitin;
DE   AltName: Full=Dynactin 2 p50 subunit {ECO:0000312|FlyBase:FBgn0021825};
GN   Name=DCTN2-p50 {ECO:0000312|FlyBase:FBgn0021825};
GN   Synonyms=Dmn {ECO:0000312|FlyBase:FBgn0021825};
GN   ORFNames=CG8269 {ECO:0000312|FlyBase:FBgn0021825};
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-58 AND SER-86, 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).
CC   -!- FUNCTION: Modulates cytoplasmic dynein binding to an organelle, and
CC       plays a role in prometaphase chromosome alignment and spindle
CC       organization during mitosis. May play a role in synapse formation
CC       during brain development (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Subunit of dynactin, a multiprotein complex associated with
CC       dynein. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dynactin subunit 2 family. {ECO:0000305}.
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DR   EMBL; AE013599; AAF59034.1; -; Genomic_DNA.
DR   EMBL; AY061092; AAL28640.1; -; mRNA.
DR   RefSeq; NP_524690.1; NM_079951.3.
DR   AlphaFoldDB; Q7K2D2; -.
DR   SMR; Q7K2D2; -.
DR   BioGRID; 68822; 34.
DR   IntAct; Q7K2D2; 2.
DR   STRING; 7227.FBpp0087722; -.
DR   iPTMnet; Q7K2D2; -.
DR   PaxDb; Q7K2D2; -.
DR   PRIDE; Q7K2D2; -.
DR   DNASU; 44086; -.
DR   EnsemblMetazoa; FBtr0088641; FBpp0087722; FBgn0021825.
DR   GeneID; 44086; -.
DR   KEGG; dme:Dmel_CG8269; -.
DR   CTD; 44086; -.
DR   FlyBase; FBgn0021825; DCTN2-p50.
DR   VEuPathDB; VectorBase:FBgn0021825; -.
DR   eggNOG; KOG3958; Eukaryota.
DR   GeneTree; ENSGT00390000003427; -.
DR   HOGENOM; CLU_049964_1_0_1; -.
DR   InParanoid; Q7K2D2; -.
DR   OMA; RGYDMRG; -.
DR   OrthoDB; 951183at2759; -.
DR   PhylomeDB; Q7K2D2; -.
DR   Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   BioGRID-ORCS; 44086; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 44086; -.
DR   PRO; PR:Q7K2D2; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0021825; Expressed in oviduct (Drosophila) and 32 other tissues.
DR   Genevisible; Q7K2D2; DM.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005869; C:dynactin complex; ISS:UniProtKB.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR   GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR   GO; GO:0061883; P:clathrin-dependent endocytosis involved in vitellogenesis; IDA:FlyBase.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR   GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR   GO; GO:0051028; P:mRNA transport; IDA:FlyBase.
DR   GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IDA:FlyBase.
DR   GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR   GO; GO:0045451; P:pole plasm oskar mRNA localization; IDA:FlyBase.
DR   GO; GO:2001019; P:positive regulation of retrograde axon cargo transport; IMP:FlyBase.
DR   GO; GO:0008090; P:retrograde axonal transport; IMP:FlyBase.
DR   GO; GO:0007051; P:spindle organization; IMP:FlyBase.
DR   InterPro; IPR028133; Dynamitin.
DR   PANTHER; PTHR15346; PTHR15346; 1.
DR   Pfam; PF04912; Dynamitin; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Membrane; Microtubule;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..380
FT                   /note="Dynactin subunit 2"
FT                   /id="PRO_0000288772"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          100..135
FT                   /evidence="ECO:0000255"
FT   COILED          353..377
FT                   /evidence="ECO:0000255"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   380 AA;  41998 MW;  CF7E1D3BFF5989C5 CRC64;
     MADPKFQNLP GIAYDQPDVY ETPDDPELDT SDYYEEEPEN EAIERLHISP SVAHKRFSGA
     TVEGSVDFTD RIGRRMCRGY DTRGSSDYEL VGQGEKETPV QKCQRLQIEM NELLNEVAAL
     QVDRKVADEE KQSYDAVATV ISTARKVLES LKLEQVLGKE QTPGSKQVKA LISQVEEFKQ
     SGVLTAIPTP GTDLAATARV ASLEQRISQL EKVLGAQPDK LSRLTAATNT TNVLEAVRHL
     STKAALIQPD KLDTIEQRLT SLAGKMDAIA EKSSGSAQDA KRDQKITELY DIAKRTEPVV
     EILPHVIERM QALEALHKYA NNFAKIIAEI EQKQGTITTS LVNNKELLHS VQETFAQNLE
     TINSKVAKVE QRVAAISSAK
 
 
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