TBG1_HUMAN
ID TBG1_HUMAN Reviewed; 451 AA.
AC P23258; Q53X79; Q9BW59;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Tubulin gamma-1 chain;
DE AltName: Full=Gamma-1-tubulin;
DE AltName: Full=Gamma-tubulin complex component 1;
DE Short=GCP-1;
GN Name=TUBG1; Synonyms=TUBG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
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 MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [6]
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=11840567;
RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA Zvelebil M.J.;
RT "Cluster analysis of an extensive human breast cancer cell line protein
RT expression map database.";
RL Proteomics 2:212-223(2002).
RN [7]
RP INTERACTION WITH TUBGCP2 AND TUBGCP3, AND SUBCELLULAR LOCATION.
RX PubMed=9566967; DOI=10.1083/jcb.141.3.663;
RA Murphy S.M., Urbani L., Stearns T.;
RT "The mammalian gamma-tubulin complex contains homologues of the yeast
RT spindle pole body components spc97p and spc98p.";
RL J. Cell Biol. 141:663-674(1998).
RN [8]
RP INTERACTION WITH TUBGCP2, AND SUBCELLULAR LOCATION.
RX PubMed=9566969; DOI=10.1083/jcb.141.3.689;
RA Tassin A.-M., Celati C., Moudjou M., Bornens M.;
RT "Characterization of the human homologue of the yeast spc98p and its
RT association with gamma-tubulin.";
RL J. Cell Biol. 141:689-701(1998).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP INTERACTION WITH CDK5RAP2.
RX PubMed=17959831; DOI=10.1091/mbc.e07-04-0371;
RA Fong K.W., Choi Y.K., Rattner J.B., Qi R.Z.;
RT "CDK5RAP2 is a pericentriolar protein that functions in centrosomal
RT attachment of the gamma-tubulin ring complex.";
RL Mol. Biol. Cell 19:115-125(2008).
RN [11]
RP INTERACTION WITH PIFO.
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).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH SAS6 AND NUP62, AND SUBCELLULAR LOCATION.
RX PubMed=24107630; DOI=10.4161/cc.26671;
RA Hashizume C., Moyori A., Kobayashi A., Yamakoshi N., Endo A., Wong R.W.;
RT "Nucleoporin Nup62 maintains centrosome homeostasis.";
RL Cell Cycle 12:3804-3816(2013).
RN [14]
RP INTERACTION WITH EML3 AND HAUS8, AND SUBCELLULAR LOCATION.
RX PubMed=30723163; DOI=10.1074/jbc.ra118.007164;
RA Luo J., Yang B., Xin G., Sun M., Zhang B., Guo X., Jiang Q., Zhang C.;
RT "The microtubule-associated protein EML3 regulates mitotic spindle assembly
RT by recruiting the Augmin complex to spindle microtubules.";
RL J. Biol. Chem. 294:5643-5656(2019).
RN [15]
RP VARIANTS CDCBM4 CYS-92; PRO-331 AND PRO-387, AND CHARACTERIZATION OF
RP VARIANT CDCBM4 PRO-387.
RX PubMed=23603762; DOI=10.1038/ng.2613;
RA Poirier K., Lebrun N., Broix L., Tian G., Saillour Y., Boscheron C.,
RA Parrini E., Valence S., Pierre B.S., Oger M., Lacombe D., Genevieve D.,
RA Fontana E., Darra F., Cances C., Barth M., Bonneau D., Bernadina B.D.,
RA N'guyen S., Gitiaux C., Parent P., des Portes V., Pedespan J.M., Legrez V.,
RA Castelnau-Ptakine L., Nitschke P., Hieu T., Masson C., Zelenika D.,
RA Andrieux A., Francis F., Guerrini R., Cowan N.J., Bahi-Buisson N.,
RA Chelly J.;
RT "Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of
RT cortical development and microcephaly.";
RL Nat. Genet. 45:639-647(2013).
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.
CC -!- SUBUNIT: Interacts with TUBGCP2 and TUBGCP3 (PubMed:9566969,
CC PubMed:9566969). Interacts with B9D2 (By similarity). Interacts with
CC CDK5RAP2; the interaction is leading to centrosomal localization of
CC TUBG1 and CDK5RAP2 (PubMed:17959831). Interacts with PIFO
CC (PubMed:20643351). Interacts with SAS6 and NUP62 at the centrosome
CC (PubMed:24107630). Interacts with EML3 (phosphorylated at 'Thr-881')
CC and HAUS8 (PubMed:30723163). {ECO:0000250|UniProtKB:P83887,
CC ECO:0000269|PubMed:17959831, ECO:0000269|PubMed:20643351,
CC ECO:0000269|PubMed:24107630, ECO:0000269|PubMed:30723163,
CC ECO:0000269|PubMed:9566967, ECO:0000269|PubMed:9566969}.
CC -!- INTERACTION:
CC P23258; O15169: AXIN1; NbExp=4; IntAct=EBI-302589, EBI-710484;
CC P23258; Q96L34: MARK4; NbExp=4; IntAct=EBI-302589, EBI-302319;
CC P23258; Q08AG7: MZT1; NbExp=4; IntAct=EBI-302589, EBI-2637198;
CC P23258; Q6NZ67: MZT2B; NbExp=4; IntAct=EBI-302589, EBI-1052566;
CC P23258; P23258: TUBG1; NbExp=6; IntAct=EBI-302589, EBI-302589;
CC P23258; Q9UGJ1-2: TUBGCP4; NbExp=2; IntAct=EBI-302589, EBI-10964469;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:24107630, ECO:0000269|PubMed:9566967,
CC ECO:0000269|PubMed:9566969}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:30723163}. Note=Localizes to mitotic spindle
CC microtubules. {ECO:0000269|PubMed:30723163}.
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:0000250}.
CC -!- MASS SPECTROMETRY: Mass=51197.98; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11840567};
CC -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 4
CC (CDCBM4) [MIM:615412]: A disorder of aberrant neuronal migration and
CC disturbed axonal guidance. Clinical features include early-onset
CC seizures, microcephaly, spastic tetraplegia, and various malformations
CC of cortical development, such as agyria, posterior or frontal
CC pachygyria, thick cortex, and subcortical band heterotopia and thin
CC corpus callosum in some patients. {ECO:0000269|PubMed:23603762}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M61764; AAA52620.1; -; mRNA.
DR EMBL; BT019931; AAV38734.1; -; mRNA.
DR EMBL; CR407642; CAG28570.1; -; mRNA.
DR EMBL; AK313339; BAG36143.1; -; mRNA.
DR EMBL; BC000619; AAH00619.1; -; mRNA.
DR CCDS; CCDS11433.1; -.
DR PIR; A39527; UBHUG.
DR RefSeq; NP_001061.2; NM_001070.4.
DR PDB; 1Z5V; X-ray; 2.71 A; A=1-449.
DR PDB; 1Z5W; X-ray; 3.00 A; A=1-449.
DR PDB; 3CB2; X-ray; 2.30 A; A/B=1-451.
DR PDB; 6V5V; EM; 3.80 A; g=1-451.
DR PDB; 6V6S; EM; 4.30 A; a/b/c/d/e/f/g/h/i/j/k/l/m/t=1-451.
DR PDB; 7AS4; EM; 4.13 A; 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-447.
DR PDB; 7QJ0; EM; 5.32 A; U/V/W/X/Y/Z=1-451.
DR PDB; 7QJ1; EM; 7.00 A; U/V/W/X/Y/Z=1-451.
DR PDB; 7QJ2; EM; 8.60 A; S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJ3; EM; 7.60 A; 1/2/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJ4; EM; 9.00 A; 1/2/S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJ5; EM; 8.70 A; 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJ6; EM; 7.80 A; Q/R/S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJ7; EM; 8.70 A; O/P/Q/R/S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJ8; EM; 8.70 A; 1/2/Q/R/S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJ9; EM; 8.10 A; Q/R/S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJA; EM; 9.20 A; O/P/Q/R/S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJB; EM; 9.20 A; 1/2/Q/R/S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJC; EM; 16.10 A; 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJD; EM; 7.10 A; 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-451.
DR PDB; 7QJE; EM; 7.80 A; W/X/Y/Z=1-451.
DR PDBsum; 1Z5V; -.
DR PDBsum; 1Z5W; -.
DR PDBsum; 3CB2; -.
DR PDBsum; 6V5V; -.
DR PDBsum; 6V6S; -.
DR PDBsum; 7AS4; -.
DR PDBsum; 7QJ0; -.
DR PDBsum; 7QJ1; -.
DR PDBsum; 7QJ2; -.
DR PDBsum; 7QJ3; -.
DR PDBsum; 7QJ4; -.
DR PDBsum; 7QJ5; -.
DR PDBsum; 7QJ6; -.
DR PDBsum; 7QJ7; -.
DR PDBsum; 7QJ8; -.
DR PDBsum; 7QJ9; -.
DR PDBsum; 7QJA; -.
DR PDBsum; 7QJB; -.
DR PDBsum; 7QJC; -.
DR PDBsum; 7QJD; -.
DR PDBsum; 7QJE; -.
DR AlphaFoldDB; P23258; -.
DR SMR; P23258; -.
DR BioGRID; 113134; 347.
DR CORUM; P23258; -.
DR DIP; DIP-29890N; -.
DR IntAct; P23258; 157.
DR MINT; P23258; -.
DR STRING; 9606.ENSP00000251413; -.
DR DrugBank; DB00570; Vinblastine.
DR iPTMnet; P23258; -.
DR MetOSite; P23258; -.
DR PhosphoSitePlus; P23258; -.
DR BioMuta; TUBG1; -.
DR DMDM; 20455518; -.
DR REPRODUCTION-2DPAGE; IPI00295081; -.
DR EPD; P23258; -.
DR jPOST; P23258; -.
DR MassIVE; P23258; -.
DR MaxQB; P23258; -.
DR PaxDb; P23258; -.
DR PeptideAtlas; P23258; -.
DR PRIDE; P23258; -.
DR ProteomicsDB; 54075; -.
DR ABCD; P23258; 6 sequenced antibodies.
DR Antibodypedia; 3898; 611 antibodies from 43 providers.
DR DNASU; 7283; -.
DR Ensembl; ENST00000251413.8; ENSP00000251413.2; ENSG00000131462.9.
DR GeneID; 7283; -.
DR KEGG; hsa:7283; -.
DR MANE-Select; ENST00000251413.8; ENSP00000251413.2; NM_001070.5; NP_001061.2.
DR UCSC; uc002ian.4; human.
DR CTD; 7283; -.
DR DisGeNET; 7283; -.
DR GeneCards; TUBG1; -.
DR HGNC; HGNC:12417; TUBG1.
DR HPA; ENSG00000131462; Tissue enhanced (testis).
DR MalaCards; TUBG1; -.
DR MIM; 191135; gene.
DR MIM; 615412; phenotype.
DR neXtProt; NX_P23258; -.
DR OpenTargets; ENSG00000131462; -.
DR Orphanet; 261183; 15q11.2 microdeletion syndrome.
DR PharmGKB; PA37079; -.
DR VEuPathDB; HostDB:ENSG00000131462; -.
DR eggNOG; KOG1374; Eukaryota.
DR GeneTree; ENSGT00940000156957; -.
DR InParanoid; P23258; -.
DR OMA; EHGINKE; -.
DR OrthoDB; 687389at2759; -.
DR PhylomeDB; P23258; -.
DR TreeFam; TF300477; -.
DR BRENDA; 3.6.5.6; 2681.
DR PathwayCommons; P23258; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; P23258; -.
DR SIGNOR; P23258; -.
DR BioGRID-ORCS; 7283; 783 hits in 1081 CRISPR screens.
DR ChiTaRS; TUBG1; human.
DR EvolutionaryTrace; P23258; -.
DR GeneWiki; TUBG1; -.
DR GenomeRNAi; 7283; -.
DR Pharos; P23258; Tbio.
DR PRO; PR:P23258; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P23258; protein.
DR Bgee; ENSG00000131462; Expressed in right testis and 206 other tissues.
DR ExpressionAtlas; P23258; baseline and differential.
DR Genevisible; P23258; HS.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0097730; C:non-motile cilium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000242; C:pericentriolar material; IEA:Ensembl.
DR GO; GO:0005827; C:polar microtubule; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; ISS:UniProtKB.
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 3D-structure; Cytoplasm; Cytoskeleton; Disease variant; GTP-binding;
KW Lissencephaly; Microtubule; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..451
FT /note="Tubulin gamma-1 chain"
FT /id="PRO_0000048465"
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:0000250|UniProtKB:P83887"
FT VARIANT 92
FT /note="Y -> C (in CDCBM4; dbSNP:rs398123046)"
FT /evidence="ECO:0000269|PubMed:23603762"
FT /id="VAR_070577"
FT VARIANT 331
FT /note="T -> P (in CDCBM4; dbSNP:rs398123047)"
FT /evidence="ECO:0000269|PubMed:23603762"
FT /id="VAR_070578"
FT VARIANT 387
FT /note="L -> P (in CDCBM4; the chaperonin-dependent folding
FT and hence the yield of monomeric gamma-tubulin is
FT compromised; dbSNP:rs398123045)"
FT /evidence="ECO:0000269|PubMed:23603762"
FT /id="VAR_070579"
FT VARIANT 413
FT /note="M -> V (in dbSNP:rs13663)"
FT /id="VAR_052674"
FT CONFLICT 35
FT /note="G -> A (in Ref. 1; AAA52620)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="V -> L (in Ref. 1; AAA52620)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 11..28
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1Z5V"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:3CB2"
FT TURN 81..85
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 104..127
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 145..160
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 225..239
FT /evidence="ECO:0007829|PDB:3CB2"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1Z5V"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1Z5V"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 290..296
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 317..327
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:1Z5V"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:3CB2"
FT STRAND 374..381
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 385..400
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 419..437
FT /evidence="ECO:0007829|PDB:3CB2"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:3CB2"
SQ SEQUENCE 451 AA; 51170 MW; E2A4C0179ED0CFE8 CRC64;
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY
IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA GNNWASGFSQ 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 HTSISSLFER TCRQYDKLRK REAFLEQFRK EDMFKDNFDE
MDTSREIVQQ LIDEYHAATR PDYISWGTQE Q
