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P05213

- TBA1B_MOUSE

UniProt

P05213 - TBA1B_MOUSE

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Protein

Tubulin alpha-1B chain

Gene

Tuba1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei451 – 4511Involved in polymerization

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence Analysis

GO - Molecular functioni

  1. double-stranded RNA binding Source: MGI
  2. GTPase activity Source: InterPro
  3. GTP binding Source: UniProtKB-KW
  4. structural constituent of cytoskeleton Source: MGI

GO - Biological processi

  1. cellular response to interleukin-4 Source: MGI
  2. microtubule cytoskeleton organization Source: MGI
  3. protein folding Source: Reactome
  4. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_199117. Kinesins.
REACT_207679. Separation of Sister Chromatids.
REACT_218773. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_227366. Gap junction assembly.
REACT_246290. Recruitment of NuMA to mitotic centrosomes.
REACT_247933. Post-chaperonin tubulin folding pathway.
REACT_256756. Mitotic Prometaphase.
REACT_257923. Recycling pathway of L1.
REACT_258053. Formation of tubulin folding intermediates by CCT/TriC.
REACT_269412. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1B chain
Alternative name(s):
Alpha-tubulin 2
Alpha-tubulin isotype M-alpha-2
Tubulin alpha-2 chain
Gene namesi
Name:Tuba1b
Synonyms:Tuba2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:107804. Tuba1b.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic microtubule Source: MGI
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: Ensembl
  4. microtubule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Tubulin alpha-1B chainPRO_0000048121Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphoserineBy similarity
Modified residuei83 – 831Nitrated tyrosineBy similarity
Modified residuei232 – 2321PhosphoserineBy similarity
Modified residuei282 – 2821Nitrated tyrosineBy similarity
Cross-linki326 – 326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei339 – 3391Omega-N-methylarginineBy similarity
Cross-linki370 – 370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei432 – 4321PhosphotyrosineBy similarity
Modified residuei439 – 4391PhosphoserineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05213.
PaxDbiP05213.
PRIDEiP05213.

2D gel databases

REPRODUCTION-2DPAGEP05213.

PTM databases

PhosphoSiteiP05213.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP05213.
CleanExiMM_TUBA1B.
ExpressionAtlasiP05213. baseline and differential.
GenevestigatoriP05213.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi204373. 19 interactions.
IntActiP05213. 14 interactions.
MINTiMINT-1869669.

Structurei

3D structure databases

ProteinModelPortaliP05213.
SMRiP05213. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP05213.
KOiK07374.
OMAiCVRARTI.
OrthoDBiEOG7TBC1W.
PhylomeDBiP05213.
TreeFamiTF300314.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. 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]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05213-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE

Y
Length:451
Mass (Da):50,152
Last modified:November 23, 2004 - v2
Checksum:i94355B4EC2086429
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551E → G in BAE30708. (PubMed:16141072)Curated
Sequence conflicti55 – 551E → G in BAE31107. (PubMed:16141072)Curated
Sequence conflicti114 – 1141I → T in BAE34741. (PubMed:16141072)Curated
Sequence conflicti119 – 1191L → P in BAE29999. (PubMed:16141072)Curated
Sequence conflicti119 – 1191L → P in BAE30196. (PubMed:16141072)Curated
Sequence conflicti135 – 1362FL → LF in AAA40507. (PubMed:3839797)Curated
Sequence conflicti340 – 3401S → T(PubMed:3785200)Curated
Sequence conflicti340 – 3401S → T in AAA40507. (PubMed:3839797)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37195.1.
PIRiI77425.
S29013. A61275.
RefSeqiNP_035784.1. NM_011654.2.
UniGeneiMm.392113.
Mm.491454.

Genome annotation databases

EnsembliENSMUST00000077577; ENSMUSP00000076777; ENSMUSG00000023004.
GeneIDi22143.
KEGGimmu:22143.
UCSCiuc007xoj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS37195.1.
PIRi I77425.
S29013. A61275.
RefSeqi NP_035784.1. NM_011654.2.
UniGenei Mm.392113.
Mm.491454.

3D structure databases

ProteinModelPortali P05213.
SMRi P05213. Positions 1-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204373. 19 interactions.
IntActi P05213. 14 interactions.
MINTi MINT-1869669.

PTM databases

PhosphoSitei P05213.

2D gel databases

REPRODUCTION-2DPAGE P05213.

Proteomic databases

MaxQBi P05213.
PaxDbi P05213.
PRIDEi P05213.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000077577 ; ENSMUSP00000076777 ; ENSMUSG00000023004 .
GeneIDi 22143.
KEGGi mmu:22143.
UCSCi uc007xoj.1. mouse.

Organism-specific databases

CTDi 10376.
MGIi MGI:107804. Tuba1b.

Phylogenomic databases

eggNOGi COG5023.
GeneTreei ENSGT00760000119060.
HOGENOMi HOG000165711.
HOVERGENi HBG000089.
InParanoidi P05213.
KOi K07374.
OMAi CVRARTI.
OrthoDBi EOG7TBC1W.
PhylomeDBi P05213.
TreeFami TF300314.

Enzyme and pathway databases

Reactomei REACT_196550. MHC class II antigen presentation.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_199117. Kinesins.
REACT_207679. Separation of Sister Chromatids.
REACT_218773. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_227366. Gap junction assembly.
REACT_246290. Recruitment of NuMA to mitotic centrosomes.
REACT_247933. Post-chaperonin tubulin folding pathway.
REACT_256756. Mitotic Prometaphase.
REACT_257923. Recycling pathway of L1.
REACT_258053. Formation of tubulin folding intermediates by CCT/TriC.
REACT_269412. Hedgehog 'off' state.

Miscellaneous databases

NextBioi 302042.
PROi P05213.
SOURCEi Search...

Gene expression databases

Bgeei P05213.
CleanExi MM_TUBA1B.
ExpressionAtlasi P05213. baseline and differential.
Genevestigatori P05213.

Family and domain databases

Gene3Di 1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProi IPR002452. 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 ]
PANTHERi PTHR11588. PTHR11588. 1 hit.
Pfami PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view ]
PRINTSi PR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTi SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEi PS00227. TUBULIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiTBA1B_MOUSE
AccessioniPrimary (citable) accession number: P05213
Secondary accession number(s): Q3TY23
, Q3U8B1, Q3UAW8, Q4KMW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 23, 2004
Last modified: November 26, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3