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Protein

Tubulin alpha-1B chain

Gene

TUBA1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)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: UniProtKB-KW
  • structural constituent of cytoskeleton Source: Ensembl
  • structural molecule activity Source: BHF-UCL
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • cell division Source: BHF-UCL
  • cellular response to interleukin-4 Source: Ensembl
  • cytoskeleton-dependent intracellular transport Source: BHF-UCL
  • microtubule-based process Source: BHF-UCL
  • microtubule cytoskeleton organization Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-190840. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
R-HSA-190861. Gap junction assembly.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-389977. Post-chaperonin tubulin folding pathway.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5610787. Hedgehog 'off' state.
R-HSA-5617833. Assembly of the primary cilium.
R-HSA-5620924. Intraflagellar transport.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-983189. Kinesins.
SIGNORiP68363.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1B chain
Alternative name(s):
Alpha-tubulin ubiquitous
Tubulin K-alpha-1
Tubulin alpha-ubiquitous chain
Cleaved into the following chain:
Gene namesi
Name:TUBA1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18809. TUBA1B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic microtubule Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • microtubule Source: UniProtKB
  • myelin sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

DisGeNETi10376.
OpenTargetsiENSG00000123416.
PharmGKBiPA162407332.

Chemistry databases

ChEMBLiCHEMBL2095182.

Polymorphism and mutation databases

BioMutaiTUBA1B.
DMDMi55977474.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000481081 – 451Tubulin alpha-1B chainAdd BLAST451
ChainiPRO_00004373841 – 450Detyrosinated tubulin alpha-1B chain1 PublicationAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-acetyllysine1 Publication1
Modified residuei48Phosphoserine1 Publication1
Modified residuei232Phosphoserine1 Publication1
Modified residuei282Nitrated tyrosineBy similarity1
Cross-linki326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei339Omega-N-methylarginine1 Publication1
Cross-linki370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei439PhosphoserineBy similarity1
Modified residuei4455-glutamyl polyglutamateBy similarity1
Modified residuei4513'-nitrotyrosine1 Publication1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). 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 (PubMed:26875866).1 Publication
Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).1 Publication
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.1 Publication
Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.1 Publication
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.2 Publications
Tubulin alpha-1B chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules (PubMed:26972003). In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).By similarity1 Publication
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 (PubMed:25908662). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. 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 (By similarity).By similarity1 Publication

Keywords - PTMi

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

Proteomic databases

EPDiP68363.
MaxQBiP68363.
PaxDbiP68363.
PeptideAtlasiP68363.
PRIDEiP68363.
TopDownProteomicsiP68363-1. [P68363-1]

2D gel databases

OGPiP68363.
SWISS-2DPAGEP68363.

PTM databases

iPTMnetiP68363.
PhosphoSitePlusiP68363.
SwissPalmiP68363.

Expressioni

Gene expression databases

BgeeiENSG00000123416.
CleanExiHS_TUBA1B.
ExpressionAtlasiP68363. baseline and differential.
GenevisibleiP68363. HS.

Organism-specific databases

HPAiCAB011513.
HPA039247.
HPA043684.
HPA063394.

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-487083,EBI-741181
EBNA-LPQ8AZK73EBI-487083,EBI-1185167From a different organism.
TUBB3Q135093EBI-487083,EBI-350989

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi115651. 124 interactors.
IntActiP68363. 40 interactors.
MINTiMINT-4998849.
STRINGi9606.ENSP00000336799.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E4HNMR-B416-451[»]
5IJ0electron microscopy3.80A1-437[»]
5IJ9electron microscopy3.70A1-437[»]
ProteinModelPortaliP68363.
SMRiP68363.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68363.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP68363.
KOiK07374.
OMAiWARTRNT.
OrthoDBiEOG091G0736.
PhylomeDBiP68363.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P68363-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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:August 13, 1987 - v1
Checksum:i94355B4EC2086429
GO
Isoform 2 (identifier: P68363-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     108-223: Missing.

Note: No experimental confirmation available.
Show »
Length:335
Mass (Da):37,218
Checksum:iCEC8DAFE68516D27
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti131G → R in AAA91576 (PubMed:6646120).Curated1
Sequence conflicti290E → D in AAA91576 (PubMed:6646120).Curated1
Sequence conflicti308R → G in AAA91576 (PubMed:6646120).Curated1
Sequence conflicti340S → T in AAA91576 (PubMed:6646120).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_055764108 – 223Missing in isoform 2. 1 PublicationAdd BLAST116

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00558 mRNA. Translation: AAA91576.1.
AF081484 mRNA. Translation: AAC31959.1.
DQ400107 mRNA. Translation: ABD60581.1.
BC000696 mRNA. Translation: AAH00696.1.
BC001128 mRNA. Translation: AAH01128.1.
BC006379 mRNA. Translation: AAH06379.1.
BC006481 mRNA. Translation: AAH06481.1.
BC008659 mRNA. Translation: AAH08659.1.
BC009314 mRNA. Translation: AAH09314.1.
BC009509 mRNA. Translation: AAH09509.1.
BC009512 mRNA. Translation: AAH09512.1.
BC009513 mRNA. Translation: AAH09513.1.
BC010494 mRNA. Translation: AAH10494.1.
BC011572 mRNA. Translation: AAH11572.1.
BC015883 mRNA. Translation: AAH15883.1.
BC017004 mRNA. Translation: AAH17004.1.
BC021564 mRNA. Translation: AAH21564.1.
BC030820 mRNA. Translation: AAH30820.1.
BC071904 mRNA. Translation: AAH71904.1.
CCDSiCCDS31792.1. [P68363-1]
PIRiI77403.
RefSeqiNP_006073.2. NM_006082.2. [P68363-1]
UniGeneiHs.524390.

Genome annotation databases

EnsembliENST00000336023; ENSP00000336799; ENSG00000123416. [P68363-1]
GeneIDi10376.
KEGGihsa:10376.
UCSCiuc001rtm.4. human. [P68363-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00558 mRNA. Translation: AAA91576.1.
AF081484 mRNA. Translation: AAC31959.1.
DQ400107 mRNA. Translation: ABD60581.1.
BC000696 mRNA. Translation: AAH00696.1.
BC001128 mRNA. Translation: AAH01128.1.
BC006379 mRNA. Translation: AAH06379.1.
BC006481 mRNA. Translation: AAH06481.1.
BC008659 mRNA. Translation: AAH08659.1.
BC009314 mRNA. Translation: AAH09314.1.
BC009509 mRNA. Translation: AAH09509.1.
BC009512 mRNA. Translation: AAH09512.1.
BC009513 mRNA. Translation: AAH09513.1.
BC010494 mRNA. Translation: AAH10494.1.
BC011572 mRNA. Translation: AAH11572.1.
BC015883 mRNA. Translation: AAH15883.1.
BC017004 mRNA. Translation: AAH17004.1.
BC021564 mRNA. Translation: AAH21564.1.
BC030820 mRNA. Translation: AAH30820.1.
BC071904 mRNA. Translation: AAH71904.1.
CCDSiCCDS31792.1. [P68363-1]
PIRiI77403.
RefSeqiNP_006073.2. NM_006082.2. [P68363-1]
UniGeneiHs.524390.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E4HNMR-B416-451[»]
5IJ0electron microscopy3.80A1-437[»]
5IJ9electron microscopy3.70A1-437[»]
ProteinModelPortaliP68363.
SMRiP68363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115651. 124 interactors.
IntActiP68363. 40 interactors.
MINTiMINT-4998849.
STRINGi9606.ENSP00000336799.

Chemistry databases

ChEMBLiCHEMBL2095182.

PTM databases

iPTMnetiP68363.
PhosphoSitePlusiP68363.
SwissPalmiP68363.

Polymorphism and mutation databases

BioMutaiTUBA1B.
DMDMi55977474.

2D gel databases

OGPiP68363.
SWISS-2DPAGEP68363.

Proteomic databases

EPDiP68363.
MaxQBiP68363.
PaxDbiP68363.
PeptideAtlasiP68363.
PRIDEiP68363.
TopDownProteomicsiP68363-1. [P68363-1]

Protocols and materials databases

DNASUi10376.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336023; ENSP00000336799; ENSG00000123416. [P68363-1]
GeneIDi10376.
KEGGihsa:10376.
UCSCiuc001rtm.4. human. [P68363-1]

Organism-specific databases

CTDi10376.
DisGeNETi10376.
GeneCardsiTUBA1B.
H-InvDBHIX0079488.
HGNCiHGNC:18809. TUBA1B.
HPAiCAB011513.
HPA039247.
HPA043684.
HPA063394.
MIMi602530. gene.
neXtProtiNX_P68363.
OpenTargetsiENSG00000123416.
PharmGKBiPA162407332.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP68363.
KOiK07374.
OMAiWARTRNT.
OrthoDBiEOG091G0736.
PhylomeDBiP68363.
TreeFamiTF300314.

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-190840. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
R-HSA-190861. Gap junction assembly.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-389977. Post-chaperonin tubulin folding pathway.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5610787. Hedgehog 'off' state.
R-HSA-5617833. Assembly of the primary cilium.
R-HSA-5620924. Intraflagellar transport.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-983189. Kinesins.
SIGNORiP68363.

Miscellaneous databases

ChiTaRSiTUBA1B. human.
EvolutionaryTraceiP68363.
GeneWikiiTUBA1B.
GenomeRNAii10376.
PROiP68363.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000123416.
CleanExiHS_TUBA1B.
ExpressionAtlasiP68363. baseline and differential.
GenevisibleiP68363. HS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiTBA1B_HUMAN
AccessioniPrimary (citable) accession number: P68363
Secondary accession number(s): P04687
, P05209, Q27I68, Q8WU19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 30, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.