Q9D6F9 (TBB4A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin beta-4A chain

Alternative name(s):
Tubulin beta-4 chain

Gene names

Name:	Tubb4a
Synonyms:	Tubb4

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	444 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.
Subunit structure	Dimer of alpha and beta chains.
Subcellular location	Cytoplasm › cytoskeleton.
Domain	The highly acidic C-terminal region may bind cations such as calcium.
Post-translational modification	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
Biological process	Cilium biogenesis/degradation
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	cell projection organization Inferred from electronic annotation. Source: UniProtKB-KW microtubule-based process Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular_component	cilium Inferred from direct assay PubMed 11724907PubMed 14625387. Source: MGI cytoplasm Inferred from direct assay PubMed 16574095. Source: MGI internode region of axon Inferred from direct assay PubMed 16421295. Source: MGI microtubule Inferred from electronic annotation. Source: UniProtKB-KW myelin sheath Inferred from direct assay PubMed 16421295. Source: MGI neuronal cell body Inferred from direct assay PubMed 16421295. Source: MGI plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro structural constituent of cytoskeleton 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 – 444	444	Tubulin beta-4A chain		PRO_0000048254
Regions
	Nucleotide binding	140 – 146	7	GTP Potential
Amino acid modifications
	Modified residue	36	1	Phosphotyrosine Ref.6
	Modified residue	172	1	Phosphoserine; by CDK1 By similarity
	Modified residue	366	1	Phosphothreonine Ref.7
Experimental info
	Sequence conflict	73	1	M → I in AAA40509. Ref.4
	Sequence conflict	111	1	E → Q in AAA40509. Ref.4
	Sequence conflict	270	1	F → L in AAA40509. Ref.4
	Sequence conflict	293	1	M → V in AAA40509. Ref.4
	Sequence conflict	303	1	C → S in AAA40509. Ref.4
	Sequence conflict	351	1	T → A in AAA40509. Ref.4
	Sequence conflict	400	1	G → A in AAA40509. Ref.4
	Sequence conflict	427	1	D → G in BAB28967. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9D6F9 [UniParc]. Last modified May 1, 2007. Version 3. Checksum: F7429D057C11A3F5	FASTA	444	49,586
	10 20 30 40 50 60 MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGNYV 70 80 90 100 110 120 PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDAVLDVV 130 140 150 160 170 180 RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEFP DRIMNTFSVV PSPKVSDTVV 190 200 210 220 230 240 EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL 250 260 270 280 290 300 RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM 310 320 330 340 350 360 AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LSVQSKNSSY FVEWIPNNVK TAVCDIPPRG 370 380 390 400 410 420 LKMAATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 430 440 EYQQYQDATA EEGEFEEEAE EEVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Hippocampus.
[2]	"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]. Strain: C57BL/6. Tissue: Brain and Olfactory epithelium.
[3]	Lubec G., Klug S., Kang S.U. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 3-19; 47-77; 104-121; 163-174; 242-276; 283-297; 310-318; 321-359; 363-379 AND 381-390, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[4]	"Five mouse tubulin isotypes and their regulated expression during development." Lewis S.A., Lee M.G.-S., Cowan N.J. J. Cell Biol. 101:852-861(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-444.
[5]	"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] [Europe PMC] [Abstract] Cited for: POLYGLUTAMYLATION.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, MASS SPECTROMETRY. Tissue: Brain.
[7]	Lubec G., Kang S. Submitted (APR-2007) to UniProtKB Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366, MASS SPECTROMETRY. Tissue: Brain.
[8]	"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] [Europe PMC] [Abstract] Cited for: POLYGLYCYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK013717 mRNA. Translation: BAB28967.1. BC049112 mRNA. Translation: AAH49112.1. BC054831 mRNA. Translation: AAH54831.1. M28730 mRNA. Translation: AAA40509.1.
IPI	IPI00109073.
RefSeq	NP_033477.2. NM_009451.3.
UniGene	Mm.7420.
3D structure databases
ProteinModelPortal	Q9D6F9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9D6F9. 6 interactions.
PTM databases
PhosphoSite	Q9D6F9.
2D gel databases
REPRODUCTION-2DPAGE	IPI00109073. Q9D6F9.
Proteomic databases
PRIDE	Q9D6F9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000071135; ENSMUSP00000071135; ENSMUSG00000062591.
GeneID	22153.
KEGG	mmu:22153.
UCSC	uc007qbb.2. mouse.
Organism-specific databases
CTD	10382.
MGI	MGI:107848. Tubb4a.
Phylogenomic databases
GeneTree	ENSGT00700000104169.
HOGENOM	HOG000165710.
HOVERGEN	HBG000089.
InParanoid	Q9D6F9.
KO	K07375.
OMA	EAENSDC.
OrthoDB	EOG4DFPNJ.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane. REACT_88307. Membrane Trafficking.
Gene expression databases
Bgee	Q9D6F9.
CleanEx	MM_TUBB4.
Genevestigator	Q9D6F9.
GermOnline	ENSMUSG00000062591. Mus musculus.
Family and domain databases
Gene3D	1.10.287.600. 1 hit. 3.30.1330.20. 1 hit. 3.40.50.1440. 1 hit.
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]
PANTHER	PTHR11588. PTHR11588. 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
BindingDB	Q9D6F9.
NextBio	302070.
SOURCE	Search...

Entry information

Entry name

TBB4A_MOUSE

Accession

Primary (citable) accession number: Q9D6F9
Secondary accession number(s): Q62364, Q80Y54

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program