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Protein

Tubulin beta-1 chain

Gene

TUBB1

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 (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 146GTPSequence analysis7

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101162-MONOMER.
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-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
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.
SIGNORiQ9H4B7.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-1 chain
Gene namesi
Name:TUBB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16257. TUBB1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Macrothrombocytopenia, autosomal dominant, TUBB1-related (MAD-TUBB1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA congenital blood disorder characterized by increased platelet size and decreased number of circulating platelets.
See also OMIM:613112
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063411318R → W in MAD-TUBB1. 1 PublicationCorresponds to variant rs121918555dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi81027.
MalaCardsiTUBB1.
MIMi613112. phenotype.
OpenTargetsiENSG00000101162.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
PharmGKBiPA38100.

Chemistry databases

ChEMBLiCHEMBL1915.
DrugBankiDB06772. Cabazitaxel.
DB01394. Colchicine.
DB01248. Docetaxel.
DB01229. Paclitaxel.
DB00309. Vindesine.

Polymorphism and mutation databases

BioMutaiTUBB1.
DMDMi62903515.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000482421 – 451Tubulin beta-1 chainAdd BLAST451

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei172Phosphoserine; by CDK11 Publication1
Modified residuei4405-glutamyl polyglutamateBy similarity1

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
Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein

Proteomic databases

EPDiQ9H4B7.
MaxQBiQ9H4B7.
PaxDbiQ9H4B7.
PeptideAtlasiQ9H4B7.
PRIDEiQ9H4B7.
TopDownProteomicsiQ9H4B7.

2D gel databases

OGPiQ9H4B7.

PTM databases

iPTMnetiQ9H4B7.
PhosphoSitePlusiQ9H4B7.

Expressioni

Tissue specificityi

Hematopoietic cell-specific. Major isotype in leukocytes, where it represents 50% of all beta-tubulins.1 Publication

Gene expression databases

BgeeiENSG00000101162.
CleanExiHS_TUBB1.
GenevisibleiQ9H4B7. HS.

Organism-specific databases

HPAiCAB004286.
HPA043640.
HPA046280.

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. Interacts with RANBP10.1 Publication

Protein-protein interaction databases

BioGridi123347. 68 interactors.
DIPiDIP-42487N.
IntActiQ9H4B7. 28 interactors.
MINTiMINT-1891365.
STRINGi9606.ENSP00000217133.

Chemistry databases

BindingDBiQ9H4B7.

Structurei

3D structure databases

ProteinModelPortaliQ9H4B7.
SMRiQ9H4B7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ9H4B7.
KOiK07375.
OMAiFDARNIM.
OrthoDBiEOG091G06U2.
PhylomeDBiQ9H4B7.
TreeFamiTF300298.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_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]
PRINTSiPR01163. BETATUBULIN.
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.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H4B7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQIG QCGNQIGAKF WEMIGEEHGI DLAGSDRGAS ALQLERISVY
60 70 80 90 100
YNEAYGRKYV PRAVLVDLEP GTMDSIRSSK LGALFQPDSF VHGNSGAGNN
110 120 130 140 150
WAKGHYTEGA ELIENVLEVV RHESESCDCL QGFQIVHSLG GGTGSGMGTL
160 170 180 190 200
LMNKIREEYP DRIMNSFSVM PSPKVSDTVV EPYNAVLSIH QLIENADACF
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS LTMSGITTSL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTAQGSQQ YRALSVAELT QQMFDARNTM
310 320 330 340 350
AACDLRRGRY LTVACIFRGK MSTKEVDQQL LSVQTRNSSC FVEWIPNNVK
360 370 380 390 400
VAVCDIPPRG LSMAATFIGN NTAIQEIFNR VSEHFSAMFK RKAFVHWYTS
410 420 430 440 450
EGMDINEFGE AENNIHDLVS EYQQFQDAKA VLEEDEEVTE EAEMEPEDKG

H
Length:451
Mass (Da):50,327
Last modified:March 1, 2001 - v1
Checksum:i6A3E5208C1C89AE4
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03454243Q → H.Corresponds to variant rs415064dbSNPEnsembl.1
Natural variantiVAR_03454343Q → P.2 PublicationsCorresponds to variant rs463312dbSNPEnsembl.1
Natural variantiVAR_052671274T → M.Corresponds to variant rs35565630dbSNPEnsembl.1
Natural variantiVAR_052672307R → H.1 PublicationCorresponds to variant rs6070697dbSNPEnsembl.1
Natural variantiVAR_063411318R → W in MAD-TUBB1. 1 PublicationCorresponds to variant rs121918555dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ292757 mRNA. Translation: CAC16605.1.
AL109840 Genomic DNA. Translation: CAC09371.2.
BC033679 mRNA. Translation: AAH33679.1.
CCDSiCCDS13475.1.
RefSeqiNP_110400.1. NM_030773.3.
UniGeneiHs.303023.

Genome annotation databases

EnsembliENST00000217133; ENSP00000217133; ENSG00000101162.
GeneIDi81027.
KEGGihsa:81027.
UCSCiuc002yak.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ292757 mRNA. Translation: CAC16605.1.
AL109840 Genomic DNA. Translation: CAC09371.2.
BC033679 mRNA. Translation: AAH33679.1.
CCDSiCCDS13475.1.
RefSeqiNP_110400.1. NM_030773.3.
UniGeneiHs.303023.

3D structure databases

ProteinModelPortaliQ9H4B7.
SMRiQ9H4B7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123347. 68 interactors.
DIPiDIP-42487N.
IntActiQ9H4B7. 28 interactors.
MINTiMINT-1891365.
STRINGi9606.ENSP00000217133.

Chemistry databases

BindingDBiQ9H4B7.
ChEMBLiCHEMBL1915.
DrugBankiDB06772. Cabazitaxel.
DB01394. Colchicine.
DB01248. Docetaxel.
DB01229. Paclitaxel.
DB00309. Vindesine.

PTM databases

iPTMnetiQ9H4B7.
PhosphoSitePlusiQ9H4B7.

Polymorphism and mutation databases

BioMutaiTUBB1.
DMDMi62903515.

2D gel databases

OGPiQ9H4B7.

Proteomic databases

EPDiQ9H4B7.
MaxQBiQ9H4B7.
PaxDbiQ9H4B7.
PeptideAtlasiQ9H4B7.
PRIDEiQ9H4B7.
TopDownProteomicsiQ9H4B7.

Protocols and materials databases

DNASUi81027.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217133; ENSP00000217133; ENSG00000101162.
GeneIDi81027.
KEGGihsa:81027.
UCSCiuc002yak.3. human.

Organism-specific databases

CTDi81027.
DisGeNETi81027.
GeneCardsiTUBB1.
HGNCiHGNC:16257. TUBB1.
HPAiCAB004286.
HPA043640.
HPA046280.
MalaCardsiTUBB1.
MIMi612901. gene.
613112. phenotype.
neXtProtiNX_Q9H4B7.
OpenTargetsiENSG00000101162.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
PharmGKBiPA38100.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ9H4B7.
KOiK07375.
OMAiFDARNIM.
OrthoDBiEOG091G06U2.
PhylomeDBiQ9H4B7.
TreeFamiTF300298.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101162-MONOMER.
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-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
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.
SIGNORiQ9H4B7.

Miscellaneous databases

GeneWikiiTUBB1.
GenomeRNAii81027.
PROiQ9H4B7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101162.
CleanExiHS_TUBB1.
GenevisibleiQ9H4B7. HS.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_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]
PRINTSiPR01163. BETATUBULIN.
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.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTBB1_HUMAN
AccessioniPrimary (citable) accession number: Q9H4B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 135 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.