Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23258 (TBG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin gamma-1 chain
Alternative name(s):
Gamma-1-tubulin
Gamma-tubulin complex component 1
Short name=GCP-1
Gene names
Name:TUBG1
Synonyms:TUBG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.8 Ref.9

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome Ref.7.

Post-translational modification

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.

Involvement in disease

Cortical dysplasia, complex, with other brain malformations 4 (CDCBM4) [MIM:615412]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Belongs to the tubulin family.

Mass spectrometry

Molecular mass is 51197.98 Da from positions 1 - 451. Determined by MALDI. Ref.6

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandGTP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cytoplasmic microtubule organization

Inferred from electronic annotation. Source: InterPro

meiotic spindle organization

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule cytoskeleton organization

Traceable author statement Ref.1. Source: ProtInc

microtubule nucleation

Inferred from electronic annotation. Source: InterPro

mitotic cell cycle

Traceable author statement. Source: Reactome

protein polymerization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentapical part of cell

Inferred from electronic annotation. Source: Ensembl

cell leading edge

Inferred from electronic annotation. Source: Ensembl

centriole

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from direct assay PubMed 17286961PubMed 21399614. Source: UniProtKB

ciliary basal body

Inferred from electronic annotation. Source: Ensembl

condensed nuclear chromosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

cytoplasmic microtubule

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

gamma-tubulin complex

Traceable author statement Ref.7. Source: UniProtKB

nonmotile primary cilium

Inferred from electronic annotation. Source: Ensembl

pericentriolar material

Inferred from electronic annotation. Source: Ensembl

polar microtubule

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

structural constituent of cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Tubulin gamma-1 chain
PRO_0000048465

Regions

Nucleotide binding142 – 1487GTP Potential

Amino acid modifications

Modified residue1311Phosphoserine; by BRSK1 By similarity

Natural variations

Natural variant921Y → C in CDCBM4. Ref.11
VAR_070577
Natural variant3311T → P in CDCBM4. Ref.11
VAR_070578
Natural variant3871L → P in CDCBM4; the chaperonin-dependent folding and hence the yield of monomeric gamma-tubulin is compromised. Ref.11
VAR_070579
Natural variant4131M → V.
Corresponds to variant rs13663 [ dbSNP | Ensembl ].
VAR_052674

Experimental info

Sequence conflict351G → A in AAA52620. Ref.1
Sequence conflict2021V → L in AAA52620. Ref.1

Secondary structure

.................................................................... 451
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23258 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: E2A4C0179ED0CFE8

FASTA45151,170
        10         20         30         40         50         60 
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY 

        70         80         90        100        110        120 
IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD 

       130        140        150        160        170        180 
IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD 

       190        200        210        220        230        240 
VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST 

       250        260        270        280        290        300 
TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP 

       310        320        330        340        350        360 
KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL 

       370        380        390        400        410        420 
SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK REAFLEQFRK EDMFKDNFDE 

       430        440        450 
MDTSREIVQQ LIDEYHAATR PDYISWGTQE Q 

« Hide

References

« Hide 'large scale' references
[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]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]"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: Skin.
[6]"Cluster analysis of an extensive human breast cancer cell line protein expression map database."
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Tissue: Mammary cancer.
[7]"Characterization of the human homologue of the yeast spc98p and its association with gamma-tubulin."
Tassin A.-M., Celati C., Moudjou M., Bornens M.
J. Cell Biol. 141:689-701(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"CDK5RAP2 is a pericentriolar protein that functions in centrosomal attachment of the gamma-tubulin ring complex."
Fong K.W., Choi Y.K., Rattner J.B., Qi R.Z.
Mol. Biol. Cell 19:115-125(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK5RAP2.
[9]"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIFO.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of cortical development and microcephaly."
Poirier K., Lebrun N., Broix L., Tian G., Saillour Y., Boscheron C., Parrini E., Valence S., Pierre B.S., Oger M., Lacombe D., Genevieve D., Fontana E., Darra F., Cances C., Barth M., Bonneau D., Bernadina B.D. expand/collapse author list , N'guyen S., Gitiaux C., Parent P., des Portes V., Pedespan J.M., Legrez V., Castelnau-Ptakine L., Nitschke P., Hieu T., Masson C., Zelenika D., Andrieux A., Francis F., Guerrini R., Cowan N.J., Bahi-Buisson N., Chelly J.
Nat. Genet. 45:639-647(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDCBM4 CYS-92; PRO-331 AND PRO-387, CHARACTERIZATION OF VARIANT CDCBM4 PRO-387.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRUBHUG. A39527.
RefSeqNP_001061.2. NM_001070.4.
UniGeneHs.279669.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z5VX-ray2.71A1-449[»]
1Z5WX-ray3.00A1-449[»]
3CB2X-ray2.30A/B1-451[»]
ProteinModelPortalP23258.
SMRP23258. Positions 2-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113134. 60 interactions.
DIPDIP-29890N.
IntActP23258. 30 interactions.
MINTMINT-4051249.
STRING9606.ENSP00000251413.

PTM databases

PhosphoSiteP23258.

Polymorphism databases

DMDM20455518.

2D gel databases

REPRODUCTION-2DPAGEIPI00295081.

Proteomic databases

PaxDbP23258.
PRIDEP23258.

Protocols and materials databases

DNASU7283.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251413; ENSP00000251413; ENSG00000131462.
GeneID7283.
KEGGhsa:7283.
UCSCuc002ian.3. human.

Organism-specific databases

CTD7283.
GeneCardsGC17P040761.
HGNCHGNC:12417. TUBG1.
HPACAB004608.
MIM191135. gene.
615412. phenotype.
neXtProtNX_P23258.
PharmGKBPA37079.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5023.
HOGENOMHOG000165714.
HOVERGENHBG098558.
InParanoidP23258.
KOK10389.
OMAEGFMLMH.
OrthoDBEOG70S755.
PhylomeDBP23258.
TreeFamTF300477.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressP23258.
BgeeP23258.
CleanExHS_TUBG1.
GenevestigatorP23258.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR002454. 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]
PANTHERPTHR11588. PTHR11588. 1 hit.
PTHR11588:SF7. PTHR11588:SF7. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01164. GAMMATUBULIN.
PR01161. TUBULIN.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23258.
GeneWikiTUBG1.
GenomeRNAi7283.
NextBio28475.
PMAP-CutDBP23258.
PROP23258.
SOURCESearch...

Entry information

Entry nameTBG1_HUMAN
AccessionPrimary (citable) accession number: P23258
Secondary accession number(s): Q53X79, Q9BW59
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 2, 2002
Last modified: April 16, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM