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Protein

Tubulin gamma-1 chain

Gene

gammaTub23C

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence analysis

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: FlyBase
  • guanyl nucleotide binding Source: FlyBase
  • structural constituent of cytoskeleton Source: FlyBase

GO - Biological processi

  • centriole-centriole cohesion Source: FlyBase
  • centrosome duplication Source: FlyBase
  • centrosome organization Source: FlyBase
  • cytoplasmic microtubule organization Source: InterPro
  • microtubule-based process Source: FlyBase
  • microtubule nucleation Source: FlyBase
  • mitotic nuclear division Source: FlyBase
  • mitotic sister chromatid separation Source: FlyBase
  • mitotic spindle assembly Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • regulation of cell cycle Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin gamma-1 chain
Alternative name(s):
Gamma-1-tubulin
Gene namesi
Name:gammaTub23C
Synonyms:Tub23C, TubG, TubG1, TubG23C
ORF Names:CG3157
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0260639. gammaTub23C.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • gamma-tubulin complex Source: FlyBase
  • gamma-tubulin large complex Source: FlyBase
  • gamma-tubulin ring complex Source: FlyBase
  • gamma-tubulin small complex Source: FlyBase
  • microtubule Source: FlyBase
  • microtubule organizing center Source: FlyBase
  • pericentriolar material Source: FlyBase
  • spindle Source: FlyBase
  • tubulin complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475Tubulin gamma-1 chainPRO_0000048454Add
BLAST

Proteomic databases

PaxDbiP23257.
PRIDEiP23257.

Expressioni

Gene expression databases

BgeeiP23257.
GenevisibleiP23257. DM.

Interactioni

Protein-protein interaction databases

BioGridi59721. 4 interactions.
IntActiP23257. 2 interactions.
MINTiMINT-942410.
STRINGi7227.FBpp0077326.

Structurei

3D structure databases

ProteinModelPortaliP23257.
SMRiP23257. Positions 2-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1374. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00530000063251.
InParanoidiP23257.
KOiK10389.
OMAiEHGINKE.
OrthoDBiEOG70S755.
PhylomeDBiP23257.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002454. Gamma_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01164. GAMMATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23257-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSEIITLQL GQCGNQIGFE FWKRLCLEHG ISPSGVLEDF ANDGLDRKDV
60 70 80 90 100
FFYQADDDHY IPRAVLLDLE PRVINTIMGS VYSKLYNPEN VYLSKHGGGA
110 120 130 140 150
GNNWASGYSQ GEKLQEEVFD IIDREADGSD SLEGFILCHS IAGGTGSGMG
160 170 180 190 200
SFIMERLADR YPKKLIQTFS VFPNQDEISD VVVQPYNSML TLKRLTTAAD
210 220 230 240 250
SVVVLDNTAL NRIACDRLHI QNPSFSQINN LVSTIMSVST TTLRYPSYMN
260 270 280 290 300
NNLIGLTAPL IPTPQLHFLM TGYTPLTSDS DIHTQQLVNV RKTTVLDVMR
310 320 330 340 350
RLLQPKNMMV STGPDKSNHH CYISILNIIQ GEVDPTQVHK SLQRIRDRKM
360 370 380 390 400
AQFIPWGPTS IQVALSRSSP YVQSNHRVSG LMLANHTSIC SLFERALNQY
410 420 430 440 450
DKLRKRGAFL DQFRREDIFK DDLNELDESR ETVDCLVQEY EAATREDYMQ
460 470
FSVKRGNGPV DSKSEDSRSV TSAGS
Length:475
Mass (Da):53,339
Last modified:March 15, 2004 - v2
Checksum:iAD35304CA1490262
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti402 – 4032KL → NV in AAA28597 (PubMed:1904010).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61765 mRNA. Translation: AAA28597.1.
AE014134 Genomic DNA. Translation: AAF51174.1.
AY069633 mRNA. Translation: AAL39778.1.
AF073994 Genomic DNA. Translation: AAC27620.1.
PIRiB39527. UBFFG.
RefSeqiNP_476804.1. NM_057456.4.
UniGeneiDm.2033.

Genome annotation databases

EnsemblMetazoaiFBtr0077641; FBpp0077326; FBgn0260639.
GeneIDi33501.
KEGGidme:Dmel_CG3157.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61765 mRNA. Translation: AAA28597.1.
AE014134 Genomic DNA. Translation: AAF51174.1.
AY069633 mRNA. Translation: AAL39778.1.
AF073994 Genomic DNA. Translation: AAC27620.1.
PIRiB39527. UBFFG.
RefSeqiNP_476804.1. NM_057456.4.
UniGeneiDm.2033.

3D structure databases

ProteinModelPortaliP23257.
SMRiP23257. Positions 2-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59721. 4 interactions.
IntActiP23257. 2 interactions.
MINTiMINT-942410.
STRINGi7227.FBpp0077326.

Proteomic databases

PaxDbiP23257.
PRIDEiP23257.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077641; FBpp0077326; FBgn0260639.
GeneIDi33501.
KEGGidme:Dmel_CG3157.

Organism-specific databases

CTDi33501.
FlyBaseiFBgn0260639. gammaTub23C.

Phylogenomic databases

eggNOGiKOG1374. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00530000063251.
InParanoidiP23257.
KOiK10389.
OMAiEHGINKE.
OrthoDBiEOG70S755.
PhylomeDBiP23257.

Miscellaneous databases

GenomeRNAii33501.
PROiP23257.

Gene expression databases

BgeeiP23257.
GenevisibleiP23257. DM.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002454. Gamma_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01164. GAMMATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gamma-tubulin is present in Drosophila melanogaster and Homo sapiens and is associated with the centrosome."
    Zheng Y., Jung M.K., Oakley B.R.
    Cell 65:817-823(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Genomic organization of the Drosophlia 23C genetic interval: identification of 3 genes in the 10Kb region surrounding the RRP1 gene."
    Tsoi S.C.M., Huang S.M., Sander M.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-333.
    Strain: Canton-S.

Entry informationi

Entry nameiTBG1_DROME
AccessioniPrimary (citable) accession number: P23257
Secondary accession number(s): Q9VQJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: March 15, 2004
Last modified: June 8, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.