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Protein

Tubulin alpha-1B chain

Gene

TUBA1B

Organism
Homo sapiens (Human)
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: 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

Keywordsi

LigandGTP-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-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
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 Cilium Assembly
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-8955332 Carboxyterminal post-translational modifications of tubulin
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

EuPathDBiHostDB:ENSG00000123416.15
HGNCiHGNC:18809 TUBA1B
MIMi602530 gene
neXtProtiNX_P68363

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi10376
OpenTargetsiENSG00000123416
PharmGKBiPA162407332

Chemistry databases

ChEMBLiCHEMBL3797010
DrugBankiDB05147 CYT997
DB03010 Epothilone B
DB01873 Epothilone D

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,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei40N6-acetyllysine; alternate1 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
Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.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-2DPAGEiP68363

PTM databases

CarbonylDBiP68363
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

Show more details

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi115651, 143 interactors
CORUMiP68363
IntActiP68363, 48 interactors
MINTiP68363
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[»]
5N5Nelectron microscopy4.00G/H/I/J/K/L1-437[»]
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
OMAiIKMRECI
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
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

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

Similar proteinsi

Entry informationi

Entry nameiTBA1B_HUMAN
AccessioniPrimary (citable) accession number: P68363
Secondary accession number(s): P04687
, P05209, Q27I68, Q8WU19
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 23, 2018
This is version 153 of the entry and version 1 of the sequence. See 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
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