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Protein

Tubulin gamma-1 chain

Gene

TUBG1

Organism
Homo sapiens (Human)
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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 148GTPSequence analysis7

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000131462-MONOMER.
ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-8854518. AURKA Activation by TPX2.
SIGNORiP23258.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:12417. TUBG1.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • cell leading edge Source: Ensembl
  • centriole Source: Ensembl
  • centrosome Source: UniProtKB
  • ciliary basal body Source: Ensembl
  • condensed nuclear chromosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic microtubule Source: Ensembl
  • cytosol Source: Reactome
  • gamma-tubulin complex Source: UniProtKB
  • pericentriolar material Source: Ensembl
  • polar microtubule Source: UniProtKB
  • recycling endosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Cortical dysplasia, complex, with other brain malformations 4 (CDCBM4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include early-onset seizures, microcephaly, spastic tetraplegia, and various malformations of cortical development, such as agyria, posterior or frontal pachygyria, thick cortex, and subcortical band heterotopia and thin corpus callosum in some patients.
See also OMIM:615412
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07057792Y → C in CDCBM4. 1 PublicationCorresponds to variant rs398123046dbSNPEnsembl.1
Natural variantiVAR_070578331T → P in CDCBM4. 1 PublicationCorresponds to variant rs398123047dbSNPEnsembl.1
Natural variantiVAR_070579387L → P in CDCBM4; the chaperonin-dependent folding and hence the yield of monomeric gamma-tubulin is compromised. 1 PublicationCorresponds to variant rs398123045dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi7283.
MalaCardsiTUBG1.
MIMi615412. phenotype.
OpenTargetsiENSG00000131462.
PharmGKBiPA37079.

Chemistry databases

DrugBankiDB00570. Vinblastine.

Polymorphism and mutation databases

BioMutaiTUBG1.
DMDMi20455518.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000484651 – 451Tubulin gamma-1 chainAdd BLAST451

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei131Phosphoserine; by BRSK1By similarity1

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.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP23258.
MaxQBiP23258.
PaxDbiP23258.
PeptideAtlasiP23258.
PRIDEiP23258.

2D gel databases

REPRODUCTION-2DPAGEIPI00295081.

PTM databases

iPTMnetiP23258.
PhosphoSitePlusiP23258.

Miscellaneous databases

PMAP-CutDBP23258.

Expressioni

Gene expression databases

BgeeiENSG00000131462.
CleanExiHS_TUBG1.
ExpressionAtlasiP23258. baseline and differential.
GenevisibleiP23258. HS.

Organism-specific databases

HPAiCAB004608.
HPA043012.
HPA046040.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
AXIN1O151694EBI-302589,EBI-710484
MARK4Q96L344EBI-302589,EBI-302319
MZT1Q08AG73EBI-302589,EBI-2637198
MZT2BQ6NZ672EBI-302589,EBI-1052566

Protein-protein interaction databases

BioGridi113134. 240 interactors.
DIPiDIP-29890N.
IntActiP23258. 99 interactors.
MINTiMINT-4051249.
STRINGi9606.ENSP00000251413.

Structurei

Secondary structure

1451
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Helixi11 – 28Combined sources18
Beta strandi33 – 35Combined sources3
Helixi48 – 50Combined sources3
Beta strandi52 – 54Combined sources3
Beta strandi60 – 62Combined sources3
Beta strandi64 – 71Combined sources8
Helixi72 – 79Combined sources8
Turni81 – 85Combined sources5
Helixi88 – 90Combined sources3
Beta strandi91 – 93Combined sources3
Helixi104 – 127Combined sources24
Beta strandi134 – 144Combined sources11
Helixi145 – 160Combined sources16
Beta strandi164 – 172Combined sources9
Helixi184 – 197Combined sources14
Beta strandi200 – 206Combined sources7
Helixi207 – 216Combined sources10
Helixi225 – 239Combined sources15
Turni240 – 243Combined sources4
Beta strandi244 – 247Combined sources4
Beta strandi248 – 250Combined sources3
Helixi253 – 260Combined sources8
Beta strandi262 – 265Combined sources4
Beta strandi268 – 274Combined sources7
Helixi290 – 296Combined sources7
Helixi300 – 302Combined sources3
Beta strandi303 – 305Combined sources3
Beta strandi317 – 327Combined sources11
Helixi330 – 342Combined sources13
Beta strandi350 – 352Combined sources3
Beta strandi356 – 361Combined sources6
Beta strandi374 – 381Combined sources8
Helixi382 – 384Combined sources3
Helixi385 – 400Combined sources16
Helixi406 – 409Combined sources4
Helixi412 – 414Combined sources3
Helixi419 – 437Combined sources19
Helixi441 – 443Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z5VX-ray2.71A1-449[»]
1Z5WX-ray3.00A1-449[»]
3CB2X-ray2.30A/B1-451[»]
ProteinModelPortaliP23258.
SMRiP23258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23258.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1374. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00530000063251.
HOGENOMiHOG000165714.
HOVERGENiHBG098558.
InParanoidiP23258.
KOiK10389.
OMAiEHGINKE.
OrthoDBiEOG091G08A9.
PhylomeDBiP23258.
TreeFamiTF300477.

Family and domain databases

CDDicd02188. gamma_tubulin. 1 hit.
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.

P23258-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV
60 70 80 90 100
FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPEN 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 NRIATDRLHI 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 TCRQYDKLRK
410 420 430 440 450
REAFLEQFRK EDMFKDNFDE MDTSREIVQQ LIDEYHAATR PDYISWGTQE

Q
Length:451
Mass (Da):51,170
Last modified:May 2, 2002 - v2
Checksum:iE2A4C0179ED0CFE8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti35G → A in AAA52620 (PubMed:1904010).Curated1
Sequence conflicti202V → L in AAA52620 (PubMed:1904010).Curated1

Mass spectrometryi

Molecular mass is 51197.98 Da from positions 1 - 451. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07057792Y → C in CDCBM4. 1 PublicationCorresponds to variant rs398123046dbSNPEnsembl.1
Natural variantiVAR_070578331T → P in CDCBM4. 1 PublicationCorresponds to variant rs398123047dbSNPEnsembl.1
Natural variantiVAR_070579387L → P in CDCBM4; the chaperonin-dependent folding and hence the yield of monomeric gamma-tubulin is compromised. 1 PublicationCorresponds to variant rs398123045dbSNPEnsembl.1
Natural variantiVAR_052674413M → V.Corresponds to variant rs13663dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61764 mRNA. Translation: AAA52620.1.
BT019931 mRNA. Translation: AAV38734.1.
CR407642 mRNA. Translation: CAG28570.1.
AK313339 mRNA. Translation: BAG36143.1.
BC000619 mRNA. Translation: AAH00619.1.
CCDSiCCDS11433.1.
PIRiA39527. UBHUG.
RefSeqiNP_001061.2. NM_001070.4.
UniGeneiHs.279669.

Genome annotation databases

EnsembliENST00000251413; ENSP00000251413; ENSG00000131462.
GeneIDi7283.
KEGGihsa:7283.
UCSCiuc002ian.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61764 mRNA. Translation: AAA52620.1.
BT019931 mRNA. Translation: AAV38734.1.
CR407642 mRNA. Translation: CAG28570.1.
AK313339 mRNA. Translation: BAG36143.1.
BC000619 mRNA. Translation: AAH00619.1.
CCDSiCCDS11433.1.
PIRiA39527. UBHUG.
RefSeqiNP_001061.2. NM_001070.4.
UniGeneiHs.279669.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z5VX-ray2.71A1-449[»]
1Z5WX-ray3.00A1-449[»]
3CB2X-ray2.30A/B1-451[»]
ProteinModelPortaliP23258.
SMRiP23258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113134. 240 interactors.
DIPiDIP-29890N.
IntActiP23258. 99 interactors.
MINTiMINT-4051249.
STRINGi9606.ENSP00000251413.

Chemistry databases

DrugBankiDB00570. Vinblastine.

PTM databases

iPTMnetiP23258.
PhosphoSitePlusiP23258.

Polymorphism and mutation databases

BioMutaiTUBG1.
DMDMi20455518.

2D gel databases

REPRODUCTION-2DPAGEIPI00295081.

Proteomic databases

EPDiP23258.
MaxQBiP23258.
PaxDbiP23258.
PeptideAtlasiP23258.
PRIDEiP23258.

Protocols and materials databases

DNASUi7283.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251413; ENSP00000251413; ENSG00000131462.
GeneIDi7283.
KEGGihsa:7283.
UCSCiuc002ian.4. human.

Organism-specific databases

CTDi7283.
DisGeNETi7283.
GeneCardsiTUBG1.
HGNCiHGNC:12417. TUBG1.
HPAiCAB004608.
HPA043012.
HPA046040.
MalaCardsiTUBG1.
MIMi191135. gene.
615412. phenotype.
neXtProtiNX_P23258.
OpenTargetsiENSG00000131462.
PharmGKBiPA37079.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1374. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00530000063251.
HOGENOMiHOG000165714.
HOVERGENiHBG098558.
InParanoidiP23258.
KOiK10389.
OMAiEHGINKE.
OrthoDBiEOG091G08A9.
PhylomeDBiP23258.
TreeFamiTF300477.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000131462-MONOMER.
ReactomeiR-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-8854518. AURKA Activation by TPX2.
SIGNORiP23258.

Miscellaneous databases

ChiTaRSiTUBG1. human.
EvolutionaryTraceiP23258.
GeneWikiiTUBG1.
GenomeRNAii7283.
PMAP-CutDBP23258.
PROiP23258.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000131462.
CleanExiHS_TUBG1.
ExpressionAtlasiP23258. baseline and differential.
GenevisibleiP23258. HS.

Family and domain databases

CDDicd02188. gamma_tubulin. 1 hit.
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...

Entry informationi

Entry nameiTBG1_HUMAN
AccessioniPrimary (citable) accession number: P23258
Secondary accession number(s): Q53X79, Q9BW59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 2, 2002
Last modified: November 30, 2016
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.