ID GCP3_HUMAN Reviewed; 907 AA. AC Q96CW5; O43631; O60852; O60853; Q5T8L2; Q7Z4K1; Q96I79; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 27-MAR-2024, entry version 183. DE RecName: Full=Gamma-tubulin complex component 3; DE Short=GCP-3; DE Short=hGCP3; DE AltName: Full=Gamma-ring complex protein 104 kDa; DE Short=h104p; DE Short=hGrip104; DE AltName: Full=Spindle pole body protein Spc98 homolog; DE Short=hSpc98; GN Name=TUBGCP3; Synonyms=GCP3; 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] (ISOFORM 1). RC TISSUE=Cervix carcinoma; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION, AND RP VARIANT SER-208. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Thalamus; 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 GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Eye, Muscle, and Testis; 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 [8] 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 [9] 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation CC at the centrosome. CC -!- SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2, CC TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. Interacts with CDK5RAP2; the CC interaction is leading to centrosomal localization of TUBGCP3 and CC CDK5RAP2. Interacts with NIN (via N-terminus); the interaction may CC promote recruitment of the gamma-tubulin ring complex to the centrosome CC (By similarity). {ECO:0000250|UniProtKB:P58854, CC ECO:0000269|PubMed:17959831}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:14654843}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=Q96CW5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96CW5-2; Sequence=VSP_001620, VSP_001621; CC Name=3; CC IsoId=Q96CW5-3; Sequence=VSP_001622, VSP_001623; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC -!- SIMILARITY: Belongs to the TUBGCP 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; AF042378; AAC39727.1; -; mRNA. DR EMBL; AJ003061; CAA05832.1; -; mRNA. DR EMBL; AJ003062; CAA05833.1; -; mRNA. DR EMBL; BT009772; AAP88774.1; -; mRNA. DR EMBL; AK314785; BAG37319.1; -; mRNA. DR EMBL; AL139384; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL160033; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471085; EAX09164.1; -; Genomic_DNA. DR EMBL; BC007763; AAH07763.1; -; mRNA. DR EMBL; BC013781; AAH13781.1; -; mRNA. DR EMBL; BC046634; AAH46634.1; -; mRNA. DR CCDS; CCDS66584.1; -. [Q96CW5-2] DR CCDS; CCDS9525.1; -. [Q96CW5-1] DR RefSeq; NP_001273206.1; NM_001286277.1. DR RefSeq; NP_001273207.1; NM_001286278.1. [Q96CW5-2] DR RefSeq; NP_001273208.1; NM_001286279.1. DR RefSeq; NP_006313.1; NM_006322.5. [Q96CW5-1] DR PDB; 6V6B; EM; 3.80 A; B=1-907. DR PDB; 6V6S; EM; 4.30 A; B/D/F/H/T=1-907. DR PDB; 6X0U; EM; 3.60 A; B=1-907. DR PDB; 7AS4; EM; 4.13 A; 3/B/D/F/H/N=1-907. DR PDB; 7QJ0; EM; 5.32 A; H/a=1-907. DR PDB; 7QJ1; EM; 7.00 A; H/a=1-907. DR PDB; 7QJ2; EM; 8.60 A; F/H/a/j=1-907. DR PDB; 7QJ3; EM; 7.60 A; H/N/a/n=1-907. DR PDB; 7QJ4; EM; 9.00 A; F/H/N/a/j/n=1-907. DR PDB; 7QJ5; EM; 8.70 A; B/D/F/H/N/a/f/h/j=1-907. DR PDB; 7QJ6; EM; 7.80 A; D/F/H/a/h/j=1-907. DR PDB; 7QJ7; EM; 8.70 A; B/D/F/H/a/f/h/j=1-907. DR PDB; 7QJ8; EM; 8.70 A; D/F/H/N/a/h/j=1-907. DR PDB; 7QJ9; EM; 8.10 A; D/F/H/a/h/j=1-907. DR PDB; 7QJA; EM; 9.20 A; B/D/F/H/a/f/h/j=1-907. DR PDB; 7QJB; EM; 9.20 A; D/F/H/N/a/h/j=1-907. DR PDB; 7QJC; EM; 16.10 A; B/D/F/H/N/a/f/h/j=1-907. DR PDB; 7QJD; EM; 7.10 A; B/D/F/H/N/a/f/h/j/n=1-907. DR PDBsum; 6V6B; -. DR PDBsum; 6V6S; -. DR PDBsum; 6X0U; -. 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 AlphaFoldDB; Q96CW5; -. 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-21067; -. DR EMDB; EMD-21073; -. DR EMDB; EMD-21984; -. DR SMR; Q96CW5; -. DR BioGRID; 115695; 243. DR CORUM; Q96CW5; -. DR IntAct; Q96CW5; 62. DR MINT; Q96CW5; -. DR STRING; 9606.ENSP00000261965; -. DR GlyCosmos; Q96CW5; 3 sites, 1 glycan. DR GlyGen; Q96CW5; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q96CW5; -. DR MetOSite; Q96CW5; -. DR PhosphoSitePlus; Q96CW5; -. DR SwissPalm; Q96CW5; -. DR BioMuta; TUBGCP3; -. DR DMDM; 21362575; -. DR EPD; Q96CW5; -. DR jPOST; Q96CW5; -. DR MassIVE; Q96CW5; -. DR MaxQB; Q96CW5; -. DR PaxDb; 9606-ENSP00000261965; -. DR PeptideAtlas; Q96CW5; -. DR ProteomicsDB; 76231; -. [Q96CW5-1] DR ProteomicsDB; 76232; -. [Q96CW5-2] DR ProteomicsDB; 76233; -. [Q96CW5-3] DR Pumba; Q96CW5; -. DR Antibodypedia; 25680; 250 antibodies from 29 providers. DR DNASU; 10426; -. DR Ensembl; ENST00000261965.8; ENSP00000261965.3; ENSG00000126216.15. [Q96CW5-1] DR Ensembl; ENST00000375669.7; ENSP00000364821.3; ENSG00000126216.15. [Q96CW5-2] DR GeneID; 10426; -. DR KEGG; hsa:10426; -. DR MANE-Select; ENST00000261965.8; ENSP00000261965.3; NM_006322.6; NP_006313.1. DR UCSC; uc001vse.3; human. [Q96CW5-1] DR AGR; HGNC:18598; -. DR CTD; 10426; -. DR DisGeNET; 10426; -. DR GeneCards; TUBGCP3; -. DR HGNC; HGNC:18598; TUBGCP3. DR HPA; ENSG00000126216; Low tissue specificity. DR MIM; 617818; gene. DR neXtProt; NX_Q96CW5; -. DR OpenTargets; ENSG00000126216; -. DR PharmGKB; PA38597; -. DR VEuPathDB; HostDB:ENSG00000126216; -. DR eggNOG; KOG2000; Eukaryota. DR GeneTree; ENSGT00940000157872; -. DR HOGENOM; CLU_003736_5_0_1; -. DR InParanoid; Q96CW5; -. DR OMA; MRMMSVC; -. DR OrthoDB; 197975at2759; -. DR PhylomeDB; Q96CW5; -. DR TreeFam; TF300705; -. DR PathwayCommons; Q96CW5; -. DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes. DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes. DR SignaLink; Q96CW5; -. DR SIGNOR; Q96CW5; -. DR BioGRID-ORCS; 10426; 790 hits in 1179 CRISPR screens. DR ChiTaRS; TUBGCP3; human. DR GeneWiki; TUBGCP3; -. DR GenomeRNAi; 10426; -. DR Pharos; Q96CW5; Tbio. DR PRO; PR:Q96CW5; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q96CW5; Protein. DR Bgee; ENSG00000126216; Expressed in monocyte and 99 other cell types or tissues. DR ExpressionAtlas; Q96CW5; baseline and differential. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central. DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005827; C:polar microtubule; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; NAS:UniProtKB. DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB. DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc. DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central. DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central. DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR GO; GO:0007338; P:single fertilization; NAS:UniProtKB. DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central. DR Gene3D; 1.20.120.1900; Gamma-tubulin complex, C-terminal domain; 1. DR InterPro; IPR007259; GCP. DR InterPro; IPR040457; GCP_C. DR InterPro; IPR042241; GCP_C_sf. DR InterPro; IPR041470; GCP_N. DR PANTHER; PTHR19302; GAMMA TUBULIN COMPLEX PROTEIN; 1. DR PANTHER; PTHR19302:SF14; GAMMA-TUBULIN COMPLEX COMPONENT 3; 1. DR Pfam; PF04130; GCP_C_terminal; 1. DR Pfam; PF17681; GCP_N_terminal; 1. DR Genevisible; Q96CW5; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; KW Microtubule; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..907 FT /note="Gamma-tubulin complex component 3" FT /id="PRO_0000078118" FT REGION 210..241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 210..230 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 391..434 FT /note="RKGGELASAVHAYTKTGDPYMRSLVQHILSLVSHPVLSFLYRWI -> PTRV FT FPTHVFPTRDFPTRDFPMHVFPTRVFPTRVWHSLCFRTRL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_001622" FT VAR_SEQ 435..907 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_001623" FT VAR_SEQ 817..824 FT /note="GQWGVTAA -> VEMCLYCV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9566969, ECO:0000303|Ref.3" FT /id="VSP_001620" FT VAR_SEQ 825..907 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9566969, ECO:0000303|Ref.3" FT /id="VSP_001621" FT VARIANT 208 FT /note="T -> S (in dbSNP:rs1044287)" FT /evidence="ECO:0000269|PubMed:9566969" FT /id="VAR_049251" FT CONFLICT 361 FT /note="S -> I (in Ref. 2; CAA05832/CAA05833)" FT /evidence="ECO:0000305" SQ SEQUENCE 907 AA; 103571 MW; 70FE2FDB7C80344D CRC64; MATPDQKSPN VLLQNLCCRI LGRSEADVAQ QFQYAVRVIG SNFAPTVERD EFLVAEKIKK ELIRQRREAD AALFSELHRK LHSQGVLKNK WSILYLLLSL SEDPRRQPSK VSSYATLFAQ ALPRDAHSTP YYYARPQTLP LSYQDRSAQS AQSSGSVGSS GISSIGLCAL SGPAPAPQSL LPGQSNQAPG VGDCLRQQLG SRLAWTLTAN QPSSQATTSK GVPSAVSRNM TRSRREGDTG GTMEITEAAL VRDILYVFQG IDGKNIKMNN TENCYKVEGK ANLSRSLRDT AVRLSELGWL HNKIRRYTDQ RSLDRSFGLV GQSFCAALHQ ELREYYRLLS VLHSQLQLED DQGVNLGLES SLTLRRLLVW TYDPKIRLKT LAALVDHCQG RKGGELASAV HAYTKTGDPY MRSLVQHILS LVSHPVLSFL YRWIYDGELE DTYHEFFVAS DPTVKTDRLW HDKYTLRKSM IPSFMTMDQS RKVLLIGKSI NFLHQVCHDQ TPTTKMIAVT KSAESPQDAA DLFTDLENAF QGKIDAAYFE TSKYLLDVLN KKYSLLDHMQ AMRRYLLLGQ GDFIRHLMDL LKPELVRPAT TLYQHNLTGI LETAVRATNA QFDSPEILRR LDVRLLEVSP GDTGWDVFSL DYHVDGPIAT VFTRECMSHY LRVFNFLWRA KRMEYILTDI RKGHMCNAKL LRNMPEFSGV LHQCHILASE MVHFIHQMQY YITFEVLECS WDELWNKVQQ AQDLDHIIAA HEVFLDTIIS RCLLDSDSRA LLNQLRAVFD QIIELQNAQD AIYRAALEEL QRRLQFEEKK KQREIEGQWG VTAAEEEEEN KRIGEFKESI PKMCSQLRIL THFYQGIVQQ FLVLLTTSSD ESLRFLSFRL DFNEHYKARE PRLRVSLGTR GRRSSHT //