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Protein

Tubulin gamma chain

Gene

TUB4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. TUB4 is an important spindle pole body component that organizes both cytoplasmic and nuclear microtubule arrays.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi143 – 1497GTPSequence analysis

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • structural constituent of cytoskeleton Source: SGD

GO - Biological processi

  • cytoplasmic microtubule organization Source: InterPro
  • microtubule nucleation Source: SGD
  • mitotic spindle organization in nucleus Source: SGD
  • positive regulation of cytoplasmic translation Source: SGD
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32329-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin gamma chain
Alternative name(s):
Gamma-tubulin
Gene namesi
Name:TUB4
Ordered Locus Names:YLR212C
ORF Names:L8167.21
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR212C.
SGDiS000004202. TUB4.

Subcellular locationi

GO - Cellular componenti

  • gamma-tubulin small complex, spindle pole body Source: SGD
  • inner plaque of spindle pole body Source: SGD
  • microtubule Source: UniProtKB-KW
  • nucleus Source: GOC
  • outer plaque of spindle pole body Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Tubulin gamma chainPRO_0000048481Add
BLAST

Proteomic databases

MaxQBiP53378.
PeptideAtlasiP53378.

PTM databases

iPTMnetiP53378.

Interactioni

Subunit structurei

Interacts with SPC72, SPC97 and SPC98.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SPC97P388634EBI-19013,EBI-17786
SPC98P535405EBI-19013,EBI-17794

Protein-protein interaction databases

BioGridi31480. 42 interactions.
DIPiDIP-821N.
IntActiP53378. 8 interactions.
MINTiMINT-631633.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5FLZelectron microscopy6.90C/D1-473[»]
5FM1electron microscopy8.00C/D1-473[»]
ProteinModelPortaliP53378.
SMRiP53378. Positions 4-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063251.
HOGENOMiHOG000165714.
InParanoidiP53378.
KOiK10389.
OMAiKEDPDIM.
OrthoDBiEOG7NKKVN.

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.
PTHR11588:SF7. PTHR11588:SF7. 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.

P53378-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGEIITLQA GQCGNHVGKF LWSQLAKEHA IGTDGLSQLP DSSTERDDDT
60 70 80 90 100
KPFFRENSRN KFTPRAIMMD SEPSVIADVE NTFRGFFDPR NTWVASDGAS
110 120 130 140 150
AGNSWANGYD IGTRNQDDIL NKIDKEIDST DNFEGFQLLH SVAGGTGSGL
160 170 180 190 200
GSNLLEALCD RYPKKILTTY SVFPARSSEV VVQSYNTILA LRRLIEDSDA
210 220 230 240 250
TVVFDNASLL NISGKVFRNP NIDLQHTNQL ISTIISSVTN SIRFPSYMYS
260 270 280 290 300
SMSSIYSTLI PSPELHFLSP SFTPFTSDYI HDDIAHKGHS SYDVMLDLLD
310 320 330 340 350
PSNSLVSTAM NNPTYFNVYN TIIGNVEPRQ ISRAMTKLQQ RIKFPSWSSS
360 370 380 390 400
AMHVNIGRRS PYLPLQPNEN EVSGMMLSNM STVVNVFENA CNTFDKVFAK
410 420 430 440 450
GAFLNNYNVG DLFQSMQNVQ DEFAESREVV QSLMEDYVAA EQDSYLDDVL
460 470
VDDENMVGEL EEDLDADGDH KLV
Length:473
Mass (Da):52,627
Last modified:October 1, 1996 - v1
Checksum:i3EA6F89E4A9A12F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14913 Genomic DNA. Translation: AAB67442.1.
BK006945 Genomic DNA. Translation: DAA09529.1.
PIRiS48563.
RefSeqiNP_013313.1. NM_001182099.1.

Genome annotation databases

EnsemblFungiiYLR212C; YLR212C; YLR212C.
GeneIDi850909.
KEGGisce:YLR212C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14913 Genomic DNA. Translation: AAB67442.1.
BK006945 Genomic DNA. Translation: DAA09529.1.
PIRiS48563.
RefSeqiNP_013313.1. NM_001182099.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5FLZelectron microscopy6.90C/D1-473[»]
5FM1electron microscopy8.00C/D1-473[»]
ProteinModelPortaliP53378.
SMRiP53378. Positions 4-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31480. 42 interactions.
DIPiDIP-821N.
IntActiP53378. 8 interactions.
MINTiMINT-631633.

PTM databases

iPTMnetiP53378.

Proteomic databases

MaxQBiP53378.
PeptideAtlasiP53378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR212C; YLR212C; YLR212C.
GeneIDi850909.
KEGGisce:YLR212C.

Organism-specific databases

EuPathDBiFungiDB:YLR212C.
SGDiS000004202. TUB4.

Phylogenomic databases

GeneTreeiENSGT00530000063251.
HOGENOMiHOG000165714.
InParanoidiP53378.
KOiK10389.
OMAiKEDPDIM.
OrthoDBiEOG7NKKVN.

Enzyme and pathway databases

BioCyciYEAST:G3O-32329-MONOMER.

Miscellaneous databases

PROiP53378.

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.
PTHR11588:SF7. PTHR11588:SF7. 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. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "A highly divergent gamma-tubulin gene is essential for cell growth and proper microtubule organization in Saccharomyces cerevisiae."
    Sobel S.G., Snyder M.
    J. Cell Biol. 131:1775-1788(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: Y270.
  4. "Gamma-tubulin-like Tub4p of Saccharomyces cerevisiae is associated with the spindle pole body substructures that organize microtubules and is required for mitotic spindle formation."
    Spang A., Geissler S., Grain K., Schiebel E.
    J. Cell Biol. 134:429-441(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Receptors determine the cellular localization of a gamma-tubulin complex and thereby the site of microtubule formation."
    Knop M., Schiebel E.
    EMBO J. 17:3952-3967(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPC72.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTBG_YEAST
AccessioniPrimary (citable) accession number: P53378
Secondary accession number(s): D6VYL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7200 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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.