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TBG1_DROME
ID   TBG1_DROME              Reviewed;         475 AA.
AC   P23257; Q9VQJ5;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Tubulin gamma-1 chain;
DE   AltName: Full=Gamma-1-tubulin;
GN   Name=gammaTub23C; Synonyms=Tub23C, TubG, TubG1, TubG23C; ORFNames=CG3157;
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 [MRNA].
RX   PubMed=1904010; DOI=10.1016/0092-8674(91)90389-g;
RA   Zheng Y., Jung M.K., Oakley B.R.;
RT   "Gamma-tubulin is present in Drosophila melanogaster and Homo sapiens and
RT   is associated with the centrosome.";
RL   Cell 65:817-823(1991).
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=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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-333.
RC   STRAIN=Canton-S;
RA   Tsoi S.C.M., Huang S.M., Sander M.;
RT   "Genomic organization of the Drosophlia 23C genetic interval:
RT   identification of 3 genes in the 10Kb region surrounding the RRP1 gene.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH OTE.
RX   PubMed=22751930; DOI=10.1128/mcb.00814-12;
RA   Habermann K., Mirgorodskaya E., Gobom J., Lehmann V., Mueller H.,
RA   Bluemlein K., Deery M.J., Czogiel I., Erdmann C., Ralser M.,
RA   von Kries J.P., Lange B.M.;
RT   "Functional analysis of centrosomal kinase substrates in Drosophila
RT   melanogaster reveals a new function of the nuclear envelope component
RT   otefin in cell cycle progression.";
RL   Mol. Cell. Biol. 32:3554-3569(2012).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC       chain is found at microtubule organizing centers (MTOC) such as the
CC       spindle poles or the centrosome, suggesting that it is involved in the
CC       minus-end nucleation of microtubule assembly.
CC   -!- SUBUNIT: Interacts with Ote. {ECO:0000269|PubMed:22751930}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; M61765; AAA28597.1; -; mRNA.
DR   EMBL; AE014134; AAF51174.1; -; Genomic_DNA.
DR   EMBL; AY069633; AAL39778.1; -; mRNA.
DR   EMBL; AF073994; AAC27620.1; -; Genomic_DNA.
DR   PIR; B39527; UBFFG.
DR   RefSeq; NP_476804.1; NM_057456.4.
DR   AlphaFoldDB; P23257; -.
DR   SMR; P23257; -.
DR   BioGRID; 59721; 28.
DR   IntAct; P23257; 4.
DR   STRING; 7227.FBpp0077326; -.
DR   PaxDb; P23257; -.
DR   PRIDE; P23257; -.
DR   DNASU; 33501; -.
DR   EnsemblMetazoa; FBtr0077641; FBpp0077326; FBgn0260639.
DR   GeneID; 33501; -.
DR   KEGG; dme:Dmel_CG3157; -.
DR   CTD; 33501; -.
DR   FlyBase; FBgn0260639; gammaTub23C.
DR   VEuPathDB; VectorBase:FBgn0260639; -.
DR   eggNOG; KOG1374; Eukaryota.
DR   GeneTree; ENSGT00940000156957; -.
DR   HOGENOM; CLU_015718_1_0_1; -.
DR   InParanoid; P23257; -.
DR   OMA; EHGINKE; -.
DR   OrthoDB; 687389at2759; -.
DR   PhylomeDB; P23257; -.
DR   BioGRID-ORCS; 33501; 1 hit in 3 CRISPR screens.
DR   GenomeRNAi; 33501; -.
DR   PRO; PR:P23257; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0260639; Expressed in capitellum (Drosophila) and 25 other tissues.
DR   Genevisible; P23257; DM.
DR   GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0000930; C:gamma-tubulin complex; IPI:FlyBase.
DR   GO; GO:0000931; C:gamma-tubulin large complex; IDA:FlyBase.
DR   GO; GO:0008275; C:gamma-tubulin small complex; IPI:FlyBase.
DR   GO; GO:0005874; C:microtubule; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000242; C:pericentriolar material; IDA:FlyBase.
DR   GO; GO:0005819; C:spindle; IDA:FlyBase.
DR   GO; GO:0005525; F:GTP binding; IDA:FlyBase.
DR   GO; GO:0019001; F:guanyl nucleotide binding; IDA:FlyBase.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0010457; P:centriole-centriole cohesion; IDA:FlyBase.
DR   GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0000212; P:meiotic spindle organization; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007020; P:microtubule nucleation; IDA:FlyBase.
DR   GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0051306; P:mitotic sister chromatid separation; IDA:FlyBase.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:FlyBase.
DR   CDD; cd02188; gamma_tubulin; 1.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR002454; Gamma_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; PTHR11588; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01164; GAMMATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..475
FT                   /note="Tubulin gamma-1 chain"
FT                   /id="PRO_0000048454"
FT   REGION          453..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        402..403
FT                   /note="KL -> NV (in Ref. 1; AAA28597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   475 AA;  53339 MW;  AD35304CA1490262 CRC64;
     MPSEIITLQL GQCGNQIGFE FWKRLCLEHG ISPSGVLEDF ANDGLDRKDV FFYQADDDHY
     IPRAVLLDLE PRVINTIMGS VYSKLYNPEN VYLSKHGGGA GNNWASGYSQ GEKLQEEVFD
     IIDREADGSD SLEGFILCHS IAGGTGSGMG SFIMERLADR YPKKLIQTFS VFPNQDEISD
     VVVQPYNSML TLKRLTTAAD SVVVLDNTAL NRIACDRLHI QNPSFSQINN LVSTIMSVST
     TTLRYPSYMN NNLIGLTAPL IPTPQLHFLM TGYTPLTSDS DIHTQQLVNV RKTTVLDVMR
     RLLQPKNMMV STGPDKSNHH CYISILNIIQ GEVDPTQVHK SLQRIRDRKM AQFIPWGPTS
     IQVALSRSSP YVQSNHRVSG LMLANHTSIC SLFERALNQY DKLRKRGAFL DQFRREDIFK
     DDLNELDESR ETVDCLVQEY EAATREDYMQ FSVKRGNGPV DSKSEDSRSV TSAGS
 
 
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