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 27-MAR-2024, entry version 227. 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|HGNC:HGNC:12417}; 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 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). 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 CIMAP3 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). Interacts with DNM2; this interaction may CC participate in centrosome cohesion (By similarity). CC {ECO:0000250|UniProtKB:P83887, ECO:0000250|UniProtKB:P83888, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-11888; -. DR EMDB; EMD-14005; -. DR EMDB; EMD-14006; -. DR EMDB; EMD-14007; -. DR EMDB; EMD-14008; -. DR EMDB; EMD-14009; -. DR EMDB; EMD-14010; -. DR EMDB; EMD-14011; -. DR EMDB; EMD-14012; -. DR EMDB; EMD-14013; -. DR EMDB; EMD-14014; -. DR EMDB; EMD-14015; -. DR EMDB; EMD-14016; -. DR EMDB; EMD-14017; -. DR EMDB; EMD-14018; -. DR EMDB; EMD-14019; -. DR EMDB; EMD-21054; -. DR EMDB; EMD-21073; -. DR SMR; P23258; -. DR BioGRID; 113134; 377. DR CORUM; P23258; -. DR DIP; DIP-29890N; -. DR IntAct; P23258; 162. DR MINT; P23258; -. DR STRING; 9606.ENSP00000251413; -. DR DrugBank; DB00570; Vinblastine. DR GlyGen; P23258; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000251413; -. DR PeptideAtlas; P23258; -. DR ProteomicsDB; 54075; -. DR Pumba; P23258; -. DR ABCD; P23258; 6 sequenced antibodies. DR Antibodypedia; 3898; 699 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 AGR; HGNC:12417; -. 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; HRYISIL; -. DR OrthoDB; 5476567at2759; -. 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; 818 hits in 1174 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 208 other cell types or tissues. DR ExpressionAtlas; P23258; baseline and differential. 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; TAS:ProtInc. 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 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. DR Genevisible; P23258; HS. 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 //