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P05213 (TBA1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin alpha-1B chain
Alternative name(s):
Alpha-tubulin 2
Alpha-tubulin isotype M-alpha-2
Tubulin alpha-2 chain
Gene names
Name:Tuba1b
Synonyms:Tuba2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence 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. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Ubiquitously expressed with highest levels in spleen, thymus and immature brain.

Post-translational modification

Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively By similarity.

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.

Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling By similarity.

Sequence similarities

Belongs to the tubulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Tubulin alpha-1B chain
PRO_0000048121

Regions

Nucleotide binding142 – 1487GTP Potential

Sites

Site4511Involved in polymerization

Amino acid modifications

Modified residue481Phosphoserine By similarity
Modified residue831Nitrated tyrosine By similarity
Modified residue2321Phosphoserine By similarity
Modified residue2821Nitrated tyrosine By similarity
Modified residue3391Omega-N-methylarginine By similarity
Modified residue4321Phosphotyrosine By similarity
Modified residue4391Phosphoserine By similarity
Cross-link326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict551E → G in BAE30708. Ref.2
Sequence conflict551E → G in BAE31107. Ref.2
Sequence conflict1141I → T in BAE34741. Ref.2
Sequence conflict1191L → P in BAE29999. Ref.2
Sequence conflict1191L → P in BAE30196. Ref.2
Sequence conflict135 – 1362FL → LF in AAA40507. Ref.5
Sequence conflict3401S → T Ref.1
Sequence conflict3401S → T in AAA40507. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P05213 [UniParc].

Last modified November 23, 2004. Version 2.
Checksum: 94355B4EC2086429

FASTA45150,152
        10         20         30         40         50         60 
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK 

        70         80         90        100        110        120 
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD 

       130        140        150        160        170        180 
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA 

       190        200        210        220        230        240 
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA 

       250        260        270        280        290        300 
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 

       310        320        330        340        350        360 
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP 

       370        380        390        400        410        420 
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 

       430        440        450 
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y 

« Hide

References

« Hide 'large scale' references
[1]"Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-specific expression of two sister genes."
Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.
Mol. Cell. Biol. 6:2409-2419(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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 and NOD.
Tissue: Amnion, Bone marrow, Eye, Kidney, Liver, Thymus and Visual cortex.
[3]"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/6J, Czech II and FVB/N.
Tissue: Limb, Mammary tumor, Olfactory epithelium and Salivary gland.
[4]Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-304; 312-320; 327-336; 340-370; 374-390; 395-401 AND 403-432, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[5]"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 100-451.
[6]"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.
[7]"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
M13446 mRNA. Translation: AAA40500.1.
AK075955 mRNA. Translation: BAC36080.1.
AK137885 mRNA. Translation: BAE23512.1.
AK150128 mRNA. Translation: BAE29327.1.
AK150179 mRNA. Translation: BAE29362.1.
AK150968 mRNA. Translation: BAE29999.1.
AK151199 mRNA. Translation: BAE30196.1.
AK151809 mRNA. Translation: BAE30708.1.
AK152298 mRNA. Translation: BAE31107.1.
AK153064 mRNA. Translation: BAE31690.1.
AK153254 mRNA. Translation: BAE31845.1.
AK158958 mRNA. Translation: BAE34741.1.
AK164428 mRNA. Translation: BAE37783.1.
AK168770 mRNA. Translation: BAE40606.1.
AK169075 mRNA. Translation: BAE40860.1.
AK169092 mRNA. Translation: BAE40875.1.
AK169130 mRNA. Translation: BAE40909.1.
AK169665 mRNA. Translation: BAE41287.1.
BC002219 mRNA. Translation: AAH02219.1.
BC008117 mRNA. Translation: AAH08117.1.
BC063777 mRNA. Translation: AAH63777.1.
BC083120 mRNA. Translation: AAH83120.1.
BC098321 mRNA. Translation: AAH98321.1.
BC108337 mRNA. Translation: AAI08338.1.
BC108394 mRNA. Translation: AAI08395.1.
M28727 mRNA. Translation: AAA40507.1.
CCDSCCDS37195.1.
PIRI77425.
A61275. S29013.
RefSeqNP_035784.1. NM_011654.2.
UniGeneMm.392113.
Mm.491454.

3D structure databases

ProteinModelPortalP05213.
SMRP05213. Positions 1-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204373. 18 interactions.
IntActP05213. 14 interactions.
MINTMINT-1869669.

PTM databases

PhosphoSiteP05213.

2D gel databases

REPRODUCTION-2DPAGEP05213.

Proteomic databases

MaxQBP05213.
PaxDbP05213.
PRIDEP05213.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077577; ENSMUSP00000076777; ENSMUSG00000023004.
GeneID22143.
KEGGmmu:22143.
UCSCuc007xoj.1. mouse.

Organism-specific databases

CTD10376.
MGIMGI:107804. Tuba1b.

Phylogenomic databases

eggNOGCOG5023.
GeneTreeENSGT00750000117333.
HOGENOMHOG000165711.
HOVERGENHBG000089.
InParanoidP05213.
KOK07374.
OMACVRARTI.
OrthoDBEOG7TBC1W.
PhylomeDBP05213.
TreeFamTF300314.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_17056. Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding.
REACT_209837. Membrane Trafficking.

Gene expression databases

BgeeP05213.
CleanExMM_TUBA1B.
GenevestigatorP05213.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR002452. Alpha_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.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01162. ALPHATUBULIN.
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

NextBio302042.
PROP05213.
SOURCESearch...

Entry information

Entry nameTBA1B_MOUSE
AccessionPrimary (citable) accession number: P05213
Secondary accession number(s): Q3TY23 expand/collapse secondary AC list , Q3U8B1, Q3UAW8, Q4KMW2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 23, 2004
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot