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Protein

Tubulin gamma-1 chain

Gene

Tubg1

Organism
Mus musculus (Mouse)
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. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation (By similarity).By similarity

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  • cytoplasmic microtubule organization Source: InterPro
  • meiotic spindle organization Source: UniProtKB
  • microtubule nucleation Source: UniProtKB
  • mitotic spindle organization Source: UniProtKB
  • regulation of mitotic nuclear division Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-380320. Recruitment of NuMA to mitotic centrosomes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin gamma-1 chain
Alternative name(s):
Gamma-1-tubulin
Gamma-tubulin complex component 1
Short name:
GCP-1
Gene namesi
Name:Tubg1
Synonyms:Tubg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:101834. Tubg1.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: MGI
  • cell leading edge Source: MGI
  • centriole Source: MGI
  • centrosome Source: UniProtKB
  • ciliary basal body Source: MGI
  • cilium Source: MGI
  • condensed nuclear chromosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic microtubule Source: MGI
  • gamma-tubulin complex Source: Ensembl
  • microtubule organizing center Source: UniProtKB
  • nonmotile primary cilium Source: MGI
  • pericentriolar material Source: MGI
  • polar microtubule Source: UniProtKB
  • recycling endosome Source: MGI
  • spindle microtubule Source: MGI
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311S → A: Weak effect possibly due to low expression of this mutant. 1 Publication
Mutagenesisi131 – 1311S → D: Phosphomimetic mutant that lead to increased centrosome number. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Tubulin gamma-1 chainPRO_0000048466Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311Phosphoserine; by BRSK11 Publication

Post-translational modificationi

Phosphorylation at Ser-131 by BRSK1 regulates centrosome duplication, possibly by mediating relocation of gamma-tubulin and its associated proteins from the cytoplasm to the centrosome.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP83887.
PaxDbiP83887.
PeptideAtlasiP83887.
PRIDEiP83887.

PTM databases

iPTMnetiP83887.
PhosphoSiteiP83887.

Expressioni

Gene expression databases

BgeeiP83887.
CleanExiMM_TUBG1.
ExpressionAtlasiP83887. baseline and differential.
GenevisibleiP83887. MM.

Interactioni

Subunit structurei

Interacts with TUBGCP2 and TUBGCP3 (By similarity). Interacts with B9D2. Interacts with CDK5RAP2; the interaction is leading to centrosomal localization of TUBG1 and CDK5RAP2 (By similarity). Interacts with PIFO.By similarity2 Publications

Protein-protein interaction databases

BioGridi222149. 106 interactions.
IntActiP83887. 105 interactions.
MINTiMINT-4137131.
STRINGi10090.ENSMUSP00000048036.

Structurei

3D structure databases

ProteinModelPortaliP83887.
SMRiP83887. Positions 2-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1374. Eukaryota.
COG5023. LUCA.
HOGENOMiHOG000165714.
HOVERGENiHBG098558.
InParanoidiP83887.
KOiK10389.
OMAiEHGINKE.
OrthoDBiEOG70S755.
PhylomeDBiP83887.
TreeFamiTF300477.

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.

P83887-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV
60 70 80 90 100
FFYQADDEHY IPRAVLLDLE PRVIHSILNS SYAKLYNPEN IYLSEHGGGA
110 120 130 140 150
GNNWASGFSQ GEKIHEDIFD IIDREADGSD SLEGFVLCHS IAGGTGSGLG
160 170 180 190 200
SYLLERLNDR YPKKLVQTYS VFPNQDEMSD VVVQPYNSLL TLKRLTQNAD
210 220 230 240 250
CVVVLDNTAL NLIATDRLHI QNPSFSQINQ LVSTIMSAST TTLRYPGYMN
260 270 280 290 300
NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP
310 320 330 340 350
KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP
360 370 380 390 400
WGPASIQVAL SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQFDKLRK
410 420 430 440 450
REAFMEQFRK EDIFKDNFDE MDTSREIVQQ LIDEYHAATR PDYISWGTQE

Q
Length:451
Mass (Da):51,101
Last modified:May 10, 2004 - v1
Checksum:iA8F1068D12D0C88A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC006581 mRNA. Translation: AAH06581.1.
CCDSiCCDS25451.1.
RefSeqiNP_598785.1. NM_134024.2.
UniGeneiMm.479145.

Genome annotation databases

EnsembliENSMUST00000043680; ENSMUSP00000048036; ENSMUSG00000035198.
GeneIDi103733.
KEGGimmu:103733.
UCSCiuc007lnk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC006581 mRNA. Translation: AAH06581.1.
CCDSiCCDS25451.1.
RefSeqiNP_598785.1. NM_134024.2.
UniGeneiMm.479145.

3D structure databases

ProteinModelPortaliP83887.
SMRiP83887. Positions 2-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222149. 106 interactions.
IntActiP83887. 105 interactions.
MINTiMINT-4137131.
STRINGi10090.ENSMUSP00000048036.

PTM databases

iPTMnetiP83887.
PhosphoSiteiP83887.

Proteomic databases

EPDiP83887.
PaxDbiP83887.
PeptideAtlasiP83887.
PRIDEiP83887.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043680; ENSMUSP00000048036; ENSMUSG00000035198.
GeneIDi103733.
KEGGimmu:103733.
UCSCiuc007lnk.1. mouse.

Organism-specific databases

CTDi7283.
MGIiMGI:101834. Tubg1.

Phylogenomic databases

eggNOGiKOG1374. Eukaryota.
COG5023. LUCA.
HOGENOMiHOG000165714.
HOVERGENiHBG098558.
InParanoidiP83887.
KOiK10389.
OMAiEHGINKE.
OrthoDBiEOG70S755.
PhylomeDBiP83887.
TreeFamiTF300477.

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-380320. Recruitment of NuMA to mitotic centrosomes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-8854518. AURKA Activation by TPX2.

Miscellaneous databases

ChiTaRSiTubg1. mouse.
PROiP83887.
SOURCEiSearch...

Gene expression databases

BgeeiP83887.
CleanExiMM_TUBG1.
ExpressionAtlasiP83887. baseline and differential.
GenevisibleiP83887. MM.

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. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  2. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 49-84; 195-217 AND 416-425, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  3. Cited for: INTERACTION WITH B9D2.
  4. "SADB phosphorylation of gamma-tubulin regulates centrosome duplication."
    Alvarado-Kristensson M., Rodriguez M.J., Silio V., Valpuesta J.M., Carrera A.C.
    Nat. Cell Biol. 11:1081-1092(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-131, MUTAGENESIS OF SER-131.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Lung, Spleen and Testis.
  6. Cited for: INTERACTION WITH PIFO.

Entry informationi

Entry nameiTBG1_MOUSE
AccessioniPrimary (citable) accession number: P83887
Secondary accession number(s): Q9Z310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 6, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.