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Protein

Tubulin beta-1 chain

Gene

Tubb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1467GTPSequence analysis

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • structural constituent of cytoskeleton Source: MGI

GO - Biological processi

  • microtubule-based process Source: MGI
  • spindle assembly Source: MGI
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5610787. Hedgehog 'off' state.
R-MMU-5620924. Intraflagellar transport.
R-MMU-5632684. Hedgehog 'on' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-1 chain
Gene namesi
Name:Tubb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:107814. Tubb1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • microtubule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Tubulin beta-1 chainPRO_0000413097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity
Modified residuei435 – 4351PhosphoserineCombined sources
Modified residuei440 – 44015-glutamyl polyglutamateBy similarity

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: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 similarity1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein

Proteomic databases

EPDiA2AQ07.
MaxQBiA2AQ07.
PaxDbiA2AQ07.
PRIDEiA2AQ07.

PTM databases

iPTMnetiA2AQ07.
PhosphoSiteiA2AQ07.

Expressioni

Gene expression databases

BgeeiA2AQ07.

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

BioGridi244340. 3 interactions.
STRINGi10090.ENSMUSP00000016399.

Structurei

3D structure databases

ProteinModelPortaliA2AQ07.
SMRiA2AQ07. Positions 1-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiA2AQ07.
KOiK07375.
OMAiFDARNIM.
OrthoDBiEOG7ZKS9Z.
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.

A2AQ07-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQIG QCGNQIGAKF WEVIGEEHGI DCAGSYCGTS ALQLERISVY
60 70 80 90 100
YNEAYGKKYV PRAVLVDLEP GTMDSIRSSR LGVLFQPDSF VHGNSGAGNN
110 120 130 140 150
WAKGHYTEGA ELIENVMDVV RRESESCDCL QGFQIVHSLG GGTGSGMGTL
160 170 180 190 200
LMNKIREEYP DRILNSFSVM PSPKVSDTVV EPYNAVLSIH QLIENTDACF
210 220 230 240 250
CIDNEALYDI CFRTLRLTTP TYGDLNHLVS LTMSGITTSL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTAQGSQQ YRALSVAELT QQMFDARNIM
310 320 330 340 350
AACDPRRGRY LTVACIFRGK MSTKEVDQQL LSIQTRNSNC FVEWIPNNVK
360 370 380 390 400
VAVCDIPPRG LNMAATFLGN NTAIQELFTR VSEHFSAMFR RRAFVHWYTS
410 420 430 440 450
EGMDISEFGE AESDIHDLVS EYQQFQDVRA GLEDSEEDVE EAEVEAEDKD

H
Length:451
Mass (Da):50,441
Last modified:February 20, 2007 - v1
Checksum:i9E68D52353E9850F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL844534 Genomic DNA. Translation: CAM26336.1.
CH466551 Genomic DNA. Translation: EDL06679.1.
BC147322 mRNA. Translation: AAI47323.1.
BC147323 mRNA. Translation: AAI47324.1.
BC147687 mRNA. Translation: AAI47688.1.
BC147698 mRNA. Translation: AAI47699.1.
CCDSiCCDS38359.1.
RefSeqiNP_001074440.1. NM_001080971.2.
UniGeneiMm.45285.

Genome annotation databases

EnsembliENSMUST00000016399; ENSMUSP00000016399; ENSMUSG00000016255.
GeneIDi545486.
KEGGimmu:545486.
UCSCiuc008ofe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL844534 Genomic DNA. Translation: CAM26336.1.
CH466551 Genomic DNA. Translation: EDL06679.1.
BC147322 mRNA. Translation: AAI47323.1.
BC147323 mRNA. Translation: AAI47324.1.
BC147687 mRNA. Translation: AAI47688.1.
BC147698 mRNA. Translation: AAI47699.1.
CCDSiCCDS38359.1.
RefSeqiNP_001074440.1. NM_001080971.2.
UniGeneiMm.45285.

3D structure databases

ProteinModelPortaliA2AQ07.
SMRiA2AQ07. Positions 1-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi244340. 3 interactions.
STRINGi10090.ENSMUSP00000016399.

PTM databases

iPTMnetiA2AQ07.
PhosphoSiteiA2AQ07.

Proteomic databases

EPDiA2AQ07.
MaxQBiA2AQ07.
PaxDbiA2AQ07.
PRIDEiA2AQ07.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000016399; ENSMUSP00000016399; ENSMUSG00000016255.
GeneIDi545486.
KEGGimmu:545486.
UCSCiuc008ofe.2. mouse.

Organism-specific databases

CTDi81027.
MGIiMGI:107814. Tubb1.

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiA2AQ07.
KOiK07375.
OMAiFDARNIM.
OrthoDBiEOG7ZKS9Z.
TreeFamiTF300298.

Enzyme and pathway databases

ReactomeiR-MMU-5610787. Hedgehog 'off' state.
R-MMU-5620924. Intraflagellar transport.
R-MMU-5632684. Hedgehog 'on' state.

Miscellaneous databases

NextBioi412643.
PROiA2AQ07.
SOURCEiSearch...

Gene expression databases

BgeeiA2AQ07.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules."
    Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A.
    J. Biol. Chem. 283:14109-14119(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP10.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung and Spleen.
  7. Cited for: GLUTAMYLATION.
  8. "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: GLYCYLATION.

Entry informationi

Entry nameiTBB1_MOUSE
AccessioniPrimary (citable) accession number: A2AQ07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: February 20, 2007
Last modified: May 11, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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.