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Protein

Tubulin alpha-1B chain

Gene

Tuba1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Sitei451Involved in polymerization1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 148GTPSequence analysis7

GO - Molecular functioni

  • double-stranded RNA binding Source: MGI
  • GTPase activity Source: InterPro
  • GTP binding Source: GO_Central
  • structural constituent of cytoskeleton Source: MGI
  • ubiquitin protein ligase binding Source: MGI

GO - Biological processi

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-MMU-2132295 MHC class II antigen presentation
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-437239 Recycling pathway of L1
R-MMU-5610787 Hedgehog 'off' state
R-MMU-5617833 Cilium Assembly
R-MMU-5620924 Intraflagellar transport
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5632684 Hedgehog 'on' state
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6807878 COPI-mediated anterograde transport
R-MMU-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-MMU-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-MMU-68877 Mitotic Prometaphase
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8955332 Carboxyterminal post-translational modifications of tubulin
R-MMU-983189 Kinesins

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
Cleaved into the following chain:
Gene namesi
Name:Tuba1b
Synonyms:Tuba2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:107804 Tuba1b

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000481211 – 451Tubulin alpha-1B chainAdd BLAST451
ChainiPRO_00004373871 – 450Detyrosinated tubulin alpha-1B chain3 PublicationsAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei40N6-acetyllysine; alternateBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei232PhosphoserineBy similarity1
Modified residuei282Nitrated tyrosineBy similarity1
Cross-linki326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei339Omega-N-methylarginineBy similarity1
Cross-linki370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei439PhosphoserineBy similarity1
Modified residuei4455-glutamyl polyglutamate1 Publication1
Modified residuei4513'-nitrotyrosineBy similarity1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglycylated, resulting in 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 polyglycylation is still unclear.1 Publication
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:1967194, PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity).By similarity2 Publications
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly.2 Publications
Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.By similarity
Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.By similarity
Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.5 Publications
Tubulin alpha-1B chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).By similarity2 Publications
Detyrosinated tubulin alpha-1B chain: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle (PubMed:26446751). In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (PubMed:27102488).By similarity2 Publications

Keywords - PTMi

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

Proteomic databases

EPDiP05213
MaxQBiP05213
PaxDbiP05213
PeptideAtlasiP05213
PRIDEiP05213
TopDownProteomicsiP05213

2D gel databases

REPRODUCTION-2DPAGEiP05213

PTM databases

iPTMnetiP05213
PhosphoSitePlusiP05213
SwissPalmiP05213

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000023004 Expressed in 21 organ(s), highest expression level in cerebral cortex
CleanExiMM_TUBA1B
GenevisibleiP05213 MM

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.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204373, 18 interactors
IntActiP05213, 19 interactors
STRINGi10090.ENSMUSP00000076777

Structurei

3D structure databases

ProteinModelPortaliP05213
SMRiP05213
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119060
HOGENOMiHOG000165711
HOVERGENiHBG000089
InParanoidiP05213
KOiK07374
OMAiHLHIGQA
OrthoDBiEOG091G0736
PhylomeDBiP05213
TreeFamiTF300314

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR002452 Alpha_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01162 ALPHATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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)DescriptionActionsGraphical viewLength
Sequence conflicti55E → G in BAE30708 (PubMed:16141072).Curated1
Sequence conflicti55E → G in BAE31107 (PubMed:16141072).Curated1
Sequence conflicti114I → T in BAE34741 (PubMed:16141072).Curated1
Sequence conflicti119L → P in BAE29999 (PubMed:16141072).Curated1
Sequence conflicti119L → P in BAE30196 (PubMed:16141072).Curated1
Sequence conflicti135 – 136FL → LF in AAA40507 (PubMed:3839797).Curated2
Sequence conflicti340S → T (PubMed:3785200).Curated1
Sequence conflicti340S → T in AAA40507 (PubMed:3839797).Curated1

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

Similar proteinsi

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
CCDSiCCDS37195.1
PIRiI77425
S29013 A61275
RefSeqiNP_035784.1, NM_011654.2
UniGeneiMm.392113
Mm.491454

3D structure databases

ProteinModelPortaliP05213
SMRiP05213
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204373, 18 interactors
IntActiP05213, 19 interactors
STRINGi10090.ENSMUSP00000076777

PTM databases

iPTMnetiP05213
PhosphoSitePlusiP05213
SwissPalmiP05213

2D gel databases

REPRODUCTION-2DPAGEiP05213

Proteomic databases

EPDiP05213
MaxQBiP05213
PaxDbiP05213
PeptideAtlasiP05213
PRIDEiP05213
TopDownProteomicsiP05213

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10376
MGIiMGI:107804 Tuba1b

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119060
HOGENOMiHOG000165711
HOVERGENiHBG000089
InParanoidiP05213
KOiK07374
OMAiHLHIGQA
OrthoDBiEOG091G0736
PhylomeDBiP05213
TreeFamiTF300314

Enzyme and pathway databases

ReactomeiR-MMU-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-MMU-2132295 MHC class II antigen presentation
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-437239 Recycling pathway of L1
R-MMU-5610787 Hedgehog 'off' state
R-MMU-5617833 Cilium Assembly
R-MMU-5620924 Intraflagellar transport
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5632684 Hedgehog 'on' state
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6807878 COPI-mediated anterograde transport
R-MMU-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-MMU-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-MMU-68877 Mitotic Prometaphase
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8955332 Carboxyterminal post-translational modifications of tubulin
R-MMU-983189 Kinesins

Miscellaneous databases

PROiPR:P05213
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000023004 Expressed in 21 organ(s), highest expression level in cerebral cortex
CleanExiMM_TUBA1B
GenevisibleiP05213 MM

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR002452 Alpha_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01162 ALPHATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTBA1B_MOUSE
AccessioniPrimary (citable) accession number: P05213
Secondary accession number(s): Q3TY23
, Q3U8B1, Q3UAW8, Q4KMW2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 23, 2004
Last modified: November 7, 2018
This is version 189 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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