ID TBG1_MOUSE Reviewed; 451 AA.
AC P83887; Q9Z310;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Tubulin gamma-1 chain {ECO:0000305};
DE AltName: Full=Gamma-1-tubulin;
DE AltName: Full=Gamma-tubulin complex component 1;
DE Short=GCP-1;
GN Name=Tubg1 {ECO:0000312|MGI:MGI:101834}; Synonyms=Tubg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 49-84; 195-217 AND 416-425, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP INTERACTION WITH B9D2.
RX PubMed=18287022; DOI=10.1073/pnas.0712385105;
RA Town T., Breunig J.J., Sarkisian M.R., Spilianakis C., Ayoub A.E., Liu X.,
RA Ferrandino A.F., Gallagher A.R., Li M.O., Rakic P., Flavell R.A.;
RT "The stumpy gene is required for mammalian ciliogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2853-2858(2008).
RN [4]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-131, AND MUTAGENESIS OF
RP SER-131.
RX PubMed=19648910; DOI=10.1038/ncb1921;
RA Alvarado-Kristensson M., Rodriguez M.J., Silio V., Valpuesta J.M.,
RA Carrera A.C.;
RT "SADB phosphorylation of gamma-tubulin regulates centrosome duplication.";
RL Nat. Cell Biol. 11:1081-1092(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH CIMAP3.
RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL Dev. Cell 19:66-77(2010).
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. Pericentriolar matrix component that
CC regulates alpha/beta chain minus-end nucleation, centrosome duplication
CC and spindle formation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TUBGCP2 and TUBGCP3 (By similarity). Interacts
CC with B9D2 (PubMed:18287022). Interacts with CDK5RAP2; the interaction
CC is leading to centrosomal localization of TUBG1 and CDK5RAP2 (By
CC similarity). Interacts with CIMAP3 (PubMed:20643351). Interacts with
CC SAS6 and NUP62 at the centrosome (By similarity). Interacts with EML3
CC (phosphorylated at 'Thr-882') and HAUS8 (By similarity). Interacts with
CC DNM2; this interaction may participate in centrosome cohesion (By
CC similarity). {ECO:0000250|UniProtKB:P23258,
CC ECO:0000250|UniProtKB:P83888, ECO:0000269|PubMed:18287022,
CC ECO:0000269|PubMed:20643351}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:19648910}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:P23258}. Note=Mainly
CC localizes to the centrosome, but a fraction is found outside of the
CC centrosome in the cytoplasm (PubMed:19648910). Localizes to mitotic
CC spindle microtubules (By similarity). {ECO:0000250|UniProtKB:P23258,
CC ECO:0000269|PubMed:19648910}.
CC -!- PTM: Phosphorylation at Ser-131 by BRSK1 regulates centrosome
CC duplication, possibly by mediating relocation of gamma-tubulin and its
CC associated proteins from the cytoplasm to the centrosome.
CC {ECO:0000269|PubMed:19648910}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; BC006581; AAH06581.1; -; mRNA.
DR CCDS; CCDS25451.1; -.
DR RefSeq; NP_598785.1; NM_134024.2.
DR AlphaFoldDB; P83887; -.
DR SMR; P83887; -.
DR BioGRID; 222149; 114.
DR IntAct; P83887; 106.
DR MINT; P83887; -.
DR STRING; 10090.ENSMUSP00000048036; -.
DR iPTMnet; P83887; -.
DR PhosphoSitePlus; P83887; -.
DR SwissPalm; P83887; -.
DR EPD; P83887; -.
DR PaxDb; 10090-ENSMUSP00000048036; -.
DR PeptideAtlas; P83887; -.
DR ProteomicsDB; 263083; -.
DR Pumba; P83887; -.
DR Antibodypedia; 3898; 699 antibodies from 43 providers.
DR DNASU; 103733; -.
DR Ensembl; ENSMUST00000043680.9; ENSMUSP00000048036.9; ENSMUSG00000035198.10.
DR GeneID; 103733; -.
DR KEGG; mmu:103733; -.
DR UCSC; uc007lnk.1; mouse.
DR AGR; MGI:101834; -.
DR CTD; 7283; -.
DR MGI; MGI:101834; Tubg1.
DR VEuPathDB; HostDB:ENSMUSG00000035198; -.
DR eggNOG; KOG1374; Eukaryota.
DR GeneTree; ENSGT00940000156957; -.
DR HOGENOM; CLU_015718_1_0_1; -.
DR InParanoid; P83887; -.
DR OMA; HRYISIL; -.
DR OrthoDB; 5476567at2759; -.
DR PhylomeDB; P83887; -.
DR TreeFam; TF300477; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 103733; 27 hits in 78 CRISPR screens.
DR ChiTaRS; Tubg1; mouse.
DR PRO; PR:P83887; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P83887; Protein.
DR Bgee; ENSMUSG00000035198; Expressed in embryonic post-anal tail and 258 other cell types or tissues.
DR ExpressionAtlas; P83887; baseline and differential.
DR Genevisible; P83887; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR GO; GO:0000930; C:gamma-tubulin complex; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; TAS:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0097730; C:non-motile cilium; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR GO; GO:0005827; C:polar microtubule; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IDA:MGI.
DR GO; GO:0000922; C:spindle pole; TAS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0000212; P:meiotic spindle organization; IEP:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; TAS:UniProtKB.
DR CDD; cd02188; gamma_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 1.
DR PANTHER; PTHR11588:SF62; TUBULIN GAMMA-1 CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..451
FT /note="Tubulin gamma-1 chain"
FT /id="PRO_0000048466"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 131
FT /note="Phosphoserine; by BRSK1"
FT /evidence="ECO:0000269|PubMed:19648910"
FT MUTAGEN 131
FT /note="S->A: Weak effect possibly due to low expression of
FT this mutant."
FT /evidence="ECO:0000269|PubMed:19648910"
FT MUTAGEN 131
FT /note="S->D: Phosphomimetic mutant that lead to increased
FT centrosome number."
FT /evidence="ECO:0000269|PubMed:19648910"
SQ SEQUENCE 451 AA; 51101 MW; A8F1068D12D0C88A CRC64;
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY
IPRAVLLDLE PRVIHSILNS SYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD
IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD
VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NLIATDRLHI QNPSFSQINQ LVSTIMSAST
TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP
KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL
SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQFDKLRK REAFMEQFRK EDIFKDNFDE
MDTSREIVQQ LIDEYHAATR PDYISWGTQE Q
//
