TBG2_MOUSE
ID TBG2_MOUSE Reviewed; 451 AA.
AC Q8VCK3;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Tubulin gamma-2 chain;
DE AltName: Full=Gamma-2-tubulin;
GN Name=Tubg2;
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=Retina;
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 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).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:19648910}. Note=Mainly localizes
CC to the centrosome, but a fraction is found outside of the centrosome in
CC the cytoplasm.
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; BC019652; AAH19652.1; -; mRNA.
DR EMBL; BC051439; AAH51439.1; -; mRNA.
DR CCDS; CCDS25452.1; -.
DR RefSeq; NP_598789.1; NM_134028.2.
DR AlphaFoldDB; Q8VCK3; -.
DR SMR; Q8VCK3; -.
DR BioGRID; 222159; 4.
DR IntAct; Q8VCK3; 2.
DR MINT; Q8VCK3; -.
DR STRING; 10090.ENSMUSP00000045901; -.
DR iPTMnet; Q8VCK3; -.
DR PhosphoSitePlus; Q8VCK3; -.
DR REPRODUCTION-2DPAGE; Q8VCK3; -.
DR MaxQB; Q8VCK3; -.
DR PaxDb; Q8VCK3; -.
DR PRIDE; Q8VCK3; -.
DR ProteomicsDB; 262951; -.
DR Antibodypedia; 29321; 78 antibodies from 22 providers.
DR Ensembl; ENSMUST00000043654; ENSMUSP00000045901; ENSMUSG00000045007.
DR GeneID; 103768; -.
DR KEGG; mmu:103768; -.
DR UCSC; uc007lnm.2; mouse.
DR CTD; 27175; -.
DR MGI; MGI:2144208; Tubg2.
DR VEuPathDB; HostDB:ENSMUSG00000045007; -.
DR eggNOG; KOG1374; Eukaryota.
DR GeneTree; ENSGT00940000162499; -.
DR HOGENOM; CLU_015718_1_0_1; -.
DR InParanoid; Q8VCK3; -.
DR OMA; RRESMFK; -.
DR OrthoDB; 687389at2759; -.
DR PhylomeDB; Q8VCK3; -.
DR TreeFam; TF300477; -.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR BioGRID-ORCS; 103768; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Tubg2; mouse.
DR PRO; PR:Q8VCK3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VCK3; protein.
DR Bgee; ENSMUSG00000045007; Expressed in submandibular gland primordium and 133 other tissues.
DR ExpressionAtlas; Q8VCK3; baseline and differential.
DR Genevisible; Q8VCK3; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
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 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 Phosphoprotein; Reference proteome.
FT CHAIN 1..451
FT /note="Tubulin gamma-2 chain"
FT /id="PRO_0000048469"
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; 51122 MW; 1FCC0FF1E04839AA CRC64;
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY
IPRAVLLDLE PRVIHSILNS SYAKLYNPEN IYLSEHGGGA GNNWGRGFSQ GEKIHEDIFD
IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD
VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST
TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP
KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL
SRKSPYLPSA HRVSGLMMAN HTSISSLFES SCQQYDKLWK RGAFLEQFRK EDIFKDNFEE
MHRSREVVQE LIDEYHAATR PDYISWGTQE Q
