P23258 (TBG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton › centrosome 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.
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 component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome meiotic spindle organization Inferred from sequence or structural similarity. Source: UniProtKB protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular_component	centrosome Inferred from direct assay PubMed 17286961PubMed 21399614. Source: UniProtKB condensed nuclear chromosome Inferred from sequence or structural similarity. Source: UniProtKB cytosol Traceable author statement. Source: Reactome gamma-tubulin complex Traceable author statement Ref.7. Source: UniProtKB polar microtubule Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	GTP 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MARK4	Q96L34	4	EBI-302589,EBI-302319
MZT1	Q08AG7	2	EBI-302589,EBI-2637198
MZT2B	Q6NZ67	2	EBI-302589,EBI-1052566

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 451

451

Tubulin gamma-1 chain

PRO_0000048465

Regions

Nucleotide binding

142 – 148

7

GTP Potential

Amino acid modifications

Modified residue

131

1

Phosphoserine; by BRSK1 By similarity

Natural variations

Natural variant

413

1

M → V.
Corresponds to variant rs13663 [ dbSNP | Ensembl ].

VAR_052674

Experimental info

Sequence conflict

35

1

G → A in AAA52620. Ref.1

Sequence conflict

202

1

V → L in AAA52620. Ref.1

Secondary structure

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451

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Helix

11 – 28

18

Beta strand

33 – 35

3

Helix

48 – 50

3

Beta strand

52 – 54

3

Beta strand

60 – 62

3

Beta strand

64 – 71

8

Helix

72 – 79

8

Turn

81 – 85

5

Helix

88 – 90

3

Beta strand

91 – 93

3

Helix

104 – 127

24

Beta strand

134 – 144

11

Helix

145 – 160

16

Beta strand

164 – 172

9

Helix

184 – 197

14

Beta strand

200 – 206

7

Helix

207 – 216

10

Helix

225 – 239

15

Turn

240 – 243

4

Beta strand

244 – 247

4

Beta strand

248 – 250

3

Helix

253 – 260

8

Beta strand

262 – 265

4

Beta strand

268 – 274

7

Helix

290 – 296

7

Helix

300 – 302

3

Beta strand

303 – 305

3

Beta strand

317 – 327

11

Helix

330 – 342

13

Beta strand

350 – 352

3

Beta strand

356 – 361

6

Beta strand

374 – 381

8

Helix

382 – 384

3

Helix

385 – 400

16

Helix

406 – 409

4

Helix

412 – 414

3

Helix

419 – 437

19

Helix

441 – 443

3

Sequences

	Sequence		Length	Mass (Da)
	P23258 [UniParc]. Last modified May 2, 2002. Version 2. Checksum: E2A4C0179ED0CFE8	FASTA	451	51,170
	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

References

	« Hide 'large scale' referencesShow '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. , 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].
+	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.

IPI

IPI00295081.

PIR

UBHUG. A39527.

RefSeq

NP_001061.2. NM_001070.4.

UniGene

Hs.279669.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z5V	X-ray	2.71	A	1-449	[»]
1Z5W	X-ray	3.00	A	1-449	[»]
3CB2	X-ray	2.30	A/B	1-451	[»]

ProteinModelPortal

P23258.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29890N.

IntAct

P23258. 20 interactions.

MINT

MINT-4051249.

STRING

9606.ENSP00000251413.

PTM databases

PhosphoSite

P23258.

Polymorphism databases

DMDM

20455518.

2D gel databases

REPRODUCTION-2DPAGE

IPI00295081.

Proteomic databases

PaxDb

P23258.

PRIDE

P23258.

Protocols and materials databases

DNASU

7283.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000251413; ENSP00000251413; ENSG00000131462.

GeneID

7283.

KEGG

hsa:7283.

UCSC

uc002ian.3. human.

Organism-specific databases

CTD

7283.

GeneCards

GC17P040761.

HGNC

HGNC:12417. TUBG1.

HPA

CAB004608.

MIM

191135. gene.

neXtProt

NX_P23258.

PharmGKB

PA37079.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5023.

HOGENOM

HOG000165714.

HOVERGEN

HBG098558.

InParanoid

P23258.

KO

K10389.

OMA

AGNNWAA.

OrthoDB

EOG444KK7.

PhylomeDB

P23258.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

Bgee

P23258.

CleanEx

HS_TUBG1.

Genevestigator

P23258.

GermOnline

ENSG00000131462. Homo sapiens.

Family and domain databases

Gene3D

1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.

InterPro

IPR002454. 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]

PANTHER

PTHR11588. PTHR11588. 1 hit.

Pfam

PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]

PRINTS

PR01164. GAMMATUBULIN.
PR01161. TUBULIN.

SMART

SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]

SUPFAM

SSF55307. Tub_FtsZ_C. 1 hit.
SSF52490. Tubulin_FtsZ. 1 hit.

PROSITE

PS00227. TUBULIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23258.

GenomeRNAi

7283.

NextBio

28475.

PMAP-CutDB

P23258.

SOURCE

Search...

Entry information

Entry name

TBG1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.