Q922F4 (TBB6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin beta-6 chain

Gene names

Name:

Tubb6

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain By similarity.
Subunit structure	Dimer of alpha and beta chains By similarity.
Subcellular location	Cytoplasm › cytoskeleton By similarity.
Domain	The highly acidic C-terminal region may bind cations such as calcium.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. Ref.4 Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules.
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 447	447	Tubulin beta-6 chain		PRO_0000048256
Regions
	Nucleotide binding	140 – 146	7	GTP Potential
Amino acid modifications
	Modified residue	56	1	Phosphoserine By similarity
	Modified residue	106	1	Phosphotyrosine Ref.4
	Modified residue	172	1	Phosphoserine; by CDK1 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q922F4 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: B02883BCF61CB514	FASTA	447	50,090
	10 20 30 40 50 60 MREIVHIQAG QCGNQIGTKF WEVISDEHGI DQAGGYVGDS ALQLERISVY YNESSSKKYV 70 80 90 100 110 120 PRAALVDLEP GTMDSVRSGP FGQLFRPDNF IFGQTGAGNN WAKGHYTEGA ELVDSVLDVV 130 140 150 160 170 180 RKECEHCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV 190 200 210 220 230 240 EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTSL 250 260 270 280 290 300 RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM 310 320 330 340 350 360 AACDPRHGRY LTVATVFRGP MSMKEVDEQM LAIQNKNSSY FVEWIPNNVK VAVCDIPPRG 370 380 390 400 410 420 LKMASTFIGN STAIQELFKR ISEQFSAMFR RKAFLHWFTG EGMDEMEFTE AESNMNDLVS 430 440 EYQQYQDATV NDGEEAFEDE DEEEINE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[2]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 104-121; 242-251; 253-262; 283-297; 310-318; 337-350 AND 363-379, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[3]	"Tubulin polyglutamylase enzymes are members of the TTL domain protein family." Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M., Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S., Gaertig J., Edde B. Science 308:1758-1762(2005) [PubMed: 15890843] [Abstract] Cited for: POLYGLUTAMYLATION.
[4]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-106, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation." Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C. Cell 137:1076-1087(2009) [PubMed: 19524510] [Abstract] Cited for: POLYGLYCYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC008225 mRNA. Translation: AAH08225.1.
IPI	IPI00122928.
RefSeq	NP_080749.2. NM_026473.2.
UniGene	Mm.181860.
3D structure databases
ProteinModelPortal	Q922F4.
SMR	Q922F4. Positions 2-427.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q922F4. 4 interactions.
STRING	Q922F4.
PTM databases
PhosphoSite	Q922F4.
Proteomic databases
PRIDE	Q922F4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000001513; ENSMUSP00000001513; ENSMUSG00000001473.
GeneID	67951.
KEGG	mmu:67951.
Organism-specific databases
CTD	84617.
MGI	MGI:1915201. Tubb6.
Phylogenomic databases
HOGENOM	HBG750007.
HOVERGEN	HBG000089.
InParanoid	Q922F4.
OMA	VYYNQAS.
OrthoDB	EOG4W6NW0.
PhylomeDB	Q922F4.
Gene expression databases
ArrayExpress	Q922F4.
Bgee	Q922F4.
CleanEx	MM_TUBB6.
Genevestigator	Q922F4.
GermOnline	ENSMUSG00000001473. Mus musculus.
Family and domain databases
InterPro	IPR013838. Beta-tubulin_BS. IPR002453. Beta_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]
Gene3D	G3DSA:3.30.1330.20. Tubulin/FtsZ_2-layer-sand-dom. 1 hit. G3DSA:1.10.287.600. Tubulin_C. 1 hit. G3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit.
KO	K07375.
PANTHER	PTHR11588. Tubulin. 1 hit.
Pfam	PF00091. Tubulin. 1 hit. PF03953. Tubulin_C. 1 hit. [Graphical view]
PRINTS	PR01163. BETATUBULIN. 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. PS00228. TUBULIN_B_AUTOREG. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	326054.
SOURCE	Search...

Entry information

Entry name

TBB6_MOUSE

Accession

Primary (citable) accession number: Q922F4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	December 1, 2001
Last modified:	November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program