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Protein

Tubulin gamma-2 chain

Gene

gammaTub37C

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. Required for oocyte activation and consequently for organization of the female meiotic spindle. Essential for centrosome organization and assembly of biastral mitotic spindles in embryos.2 Publications

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  • attachment of spindle microtubules to kinetochore involved in meiotic chromosome segregation Source: FlyBase
  • cell division Source: UniProtKB-KW
  • cytoplasmic microtubule organization Source: InterPro
  • microtubule-based process Source: FlyBase
  • microtubule nucleation Source: InterPro
  • mitotic nuclear division Source: UniProtKB-KW
  • oocyte nucleus localization involved in oocyte dorsal/ventral axis specification Source: FlyBase
  • spindle assembly involved in female meiosis I Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Meiosis, Mitosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin gamma-2 chain
Alternative name(s):
Gamma-2-tubulin
Gene namesi
Name:gammaTub37C
Synonyms:Tub37CD, TubG2, TubG37C
ORF Names:CG17566
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0010097. gammaTub37C.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: FlyBase
  • cytoplasm Source: FlyBase
  • gamma-tubulin complex Source: InterPro
  • meiotic spindle Source: FlyBase
  • microtubule Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • microtubule organizing center 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 – 457457Tubulin gamma-2 chainPRO_0000048455Add
BLAST

Proteomic databases

PaxDbiP42271.
PRIDEiP42271.

Expressioni

Tissue specificityi

Expressed in nurse cells and oocytes of developing egg chambers.2 Publications

Developmental stagei

Expressed both maternally and zygotically. Zygotic expression is restricted to adult females.2 Publications

Gene expression databases

BgeeiP42271.
ExpressionAtlasiP42271. differential.
GenevisibleiP42271. DM.

Interactioni

Protein-protein interaction databases

BioGridi61183. 12 interactions.
DIPiDIP-60707N.
IntActiP42271. 3 interactions.
MINTiMINT-953464.
STRINGi7227.FBpp0304827.

Structurei

3D structure databases

ProteinModelPortaliP42271.
SMRiP42271. Positions 2-447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1374. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00530000063251.
InParanoidiP42271.
KOiK10389.
OMAiILRQYDG.
OrthoDBiEOG70S755.
PhylomeDBiP42271.

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.

P42271-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSEIITLQL GQCGNQIGFE FWKRLCLEHG ISPDGVLEDF ATDGQDRKDV
60 70 80 90 100
FFYQADDNHY IPRAVLIDLE PRVINNIMTS PYSKLYNQEN VFLSKHGGGA
110 120 130 140 150
GNNWASGFSQ GEKVQEEVFD ILDREADGSD SLEGFVLCHS IAGGTGSGMG
160 170 180 190 200
SYVLERLSER FPKKLIQTYS VFPNQDEISD VVVQPYNSIL TLKRLTKCAD
210 220 230 240 250
SVVVLDNTAL NRIATERLHI QTPTFTQINN LVSTIMSLST TTLRYPSYMN
260 270 280 290 300
NNLIGLTASL IPTPQLHFLM TGYTPLMSDC ETKTSVRKTT VLDVMRRLLQ
310 320 330 340 350
PKNMMVSALT DKQSRQCFVS ILNIIQGEVD PSQVHKSLQR IRERKLANFI
360 370 380 390 400
PWGPASIQVA LPRSSPYVQS AHKVSGLMMA NHTGISSLFK RALAQYDKLR
410 420 430 440 450
KRNAFLDNFR RESMFQDDLT ELDIARDTVD CLVQEYEAAT QIDYPQWSPA

VEASKAG
Length:457
Mass (Da):51,296
Last modified:March 15, 2004 - v3
Checksum:i00C326DC5744618A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2821T → A in AAB52553 (PubMed:9133431).Curated
Sequence conflicti343 – 3431E → K in AAC35843 (PubMed:9155007).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081252 Genomic DNA. Translation: AAC35843.1.
AJ010552 Genomic DNA. Translation: CAA09233.1.
M76765 mRNA. Translation: AAB52553.1.
AF091265 Genomic DNA. Translation: AAC64117.1.
AE014134 Genomic DNA. Translation: AAF53774.1.
AY070558 mRNA. Translation: AAL48029.1.
PIRiT08419.
RefSeqiNP_001260565.1. NM_001273636.1.
NP_476922.1. NM_057574.5.
UniGeneiDm.469.

Genome annotation databases

EnsemblMetazoaiFBtr0081228; FBpp0080769; FBgn0010097.
FBtr0332572; FBpp0304827; FBgn0010097.
GeneIDi35199.
KEGGidme:Dmel_CG17566.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081252 Genomic DNA. Translation: AAC35843.1.
AJ010552 Genomic DNA. Translation: CAA09233.1.
M76765 mRNA. Translation: AAB52553.1.
AF091265 Genomic DNA. Translation: AAC64117.1.
AE014134 Genomic DNA. Translation: AAF53774.1.
AY070558 mRNA. Translation: AAL48029.1.
PIRiT08419.
RefSeqiNP_001260565.1. NM_001273636.1.
NP_476922.1. NM_057574.5.
UniGeneiDm.469.

3D structure databases

ProteinModelPortaliP42271.
SMRiP42271. Positions 2-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61183. 12 interactions.
DIPiDIP-60707N.
IntActiP42271. 3 interactions.
MINTiMINT-953464.
STRINGi7227.FBpp0304827.

Proteomic databases

PaxDbiP42271.
PRIDEiP42271.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081228; FBpp0080769; FBgn0010097.
FBtr0332572; FBpp0304827; FBgn0010097.
GeneIDi35199.
KEGGidme:Dmel_CG17566.

Organism-specific databases

CTDi35199.
FlyBaseiFBgn0010097. gammaTub37C.

Phylogenomic databases

eggNOGiKOG1374. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00530000063251.
InParanoidiP42271.
KOiK10389.
OMAiILRQYDG.
OrthoDBiEOG70S755.
PhylomeDBiP42271.

Miscellaneous databases

ChiTaRSigammaTub37C. fly.
GenomeRNAii35199.
PROiP42271.

Gene expression databases

BgeeiP42271.
ExpressionAtlasiP42271. differential.
GenevisibleiP42271. 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. "Essential role for gamma-tubulin in the acentriolar female meiotic spindle of Drosophila."
    Tavosanis G., Llamazares S., Goulielmos G., Gonzalez C.
    EMBO J. 16:1809-1819(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  2. "Differential expression of two gamma-tubulin isoforms during gametogenesis and development in Drosophila."
    Wilson P.G., Zheng Y., Oakley C.E., Oakley B.R., Borisy G.G., Fuller M.T.
    Dev. Biol. 184:207-221(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Ovary.
  3. "Maternally expressed gamma Tub37CD in Drosophila is differentially required for female meiosis and embryonic mitosis."
    Wilson P.G., Borisy G.G.
    Dev. Biol. 199:273-290(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. "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.

Entry informationi

Entry nameiTBG2_DROME
AccessioniPrimary (citable) accession number: P42271
Secondary accession number(s): O77160, Q9V476
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 15, 2004
Last modified: June 8, 2016
This is version 136 of the entry and version 3 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.