GCP3_HUMAN
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 03-AUG-2022, entry version 174.
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}.
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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 SMR; Q96CW5; -.
DR BioGRID; 115695; 221.
DR CORUM; Q96CW5; -.
DR IntAct; Q96CW5; 59.
DR MINT; Q96CW5; -.
DR STRING; 9606.ENSP00000261965; -.
DR GlyGen; Q96CW5; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q96CW5; -.
DR MetOSite; Q96CW5; -.
DR PhosphoSitePlus; Q96CW5; -.
DR BioMuta; TUBGCP3; -.
DR DMDM; 21362575; -.
DR EPD; Q96CW5; -.
DR jPOST; Q96CW5; -.
DR MassIVE; Q96CW5; -.
DR MaxQB; Q96CW5; -.
DR PaxDb; Q96CW5; -.
DR PeptideAtlas; Q96CW5; -.
DR PRIDE; Q96CW5; -.
DR ProteomicsDB; 76231; -. [Q96CW5-1]
DR ProteomicsDB; 76232; -. [Q96CW5-2]
DR ProteomicsDB; 76233; -. [Q96CW5-3]
DR Antibodypedia; 25680; 218 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 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; 480444at2759; -.
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; 755 hits in 1100 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 97 other tissues.
DR ExpressionAtlas; Q96CW5; baseline and differential.
DR Genevisible; Q96CW5; HS.
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:0008275; C:gamma-tubulin small 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; -; 1.
DR InterPro; IPR007259; GCP.
DR InterPro; IPR040457; GCP_C.
DR InterPro; IPR042241; GCP_C_sf.
DR InterPro; IPR041470; GCP_N.
DR PANTHER; PTHR19302; PTHR19302; 1.
DR Pfam; PF04130; GCP_C_terminal; 1.
DR Pfam; PF17681; GCP_N_terminal; 1.
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
