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Protein

Tubulin beta-4B chain

Gene

Tubb4b

Organism
Mus musculus (Mouse)
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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1467GTPSequence Analysis

GO - Molecular functioni

  1. double-stranded RNA binding Source: MGI
  2. GTPase activity Source: InterPro
  3. GTP binding Source: UniProtKB
  4. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. microtubule-based process Source: UniProtKB
  2. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_272448. Recruitment of mitotic centrosome proteins and complexes.
REACT_276302. Loss of Nlp from mitotic centrosomes.
REACT_278699. Hedgehog 'off' state.
REACT_286537. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_295993. Gap junction assembly.
REACT_297274. Orphan transporters.
REACT_298063. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_306375. Mitotic Prometaphase.
REACT_307151. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_316383. MHC class II antigen presentation.
REACT_319119. Post-chaperonin tubulin folding pathway.
REACT_319807. Assembly of the primary cilium.
REACT_321346. Separation of Sister Chromatids.
REACT_328862. Anchoring of the basal body to the plasma membrane.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_330163. Formation of tubulin folding intermediates by CCT/TriC.
REACT_332968. Recruitment of NuMA to mitotic centrosomes.
REACT_341960. Intraflagellar transport.
REACT_342780. Kinesins.
REACT_345278. Regulation of PLK1 Activity at G2/M Transition.
REACT_351311. Hedgehog 'on' state.
REACT_353475. Recycling pathway of L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-4B chain
Alternative name(s):
Tubulin beta-2C chain
Gene namesi
Name:Tubb4b
Synonyms:Tubb2c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1915472. Tubb4b.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: MGI
  3. microtubule Source: MGI
  4. myelin sheath Source: UniProtKB
  5. nucleus Source: MGI
  6. tubulin complex Source: UniProtKB
  7. vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Tubulin beta-4B chainPRO_0000048249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581N6-acetyllysine1 Publication
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity

Post-translational modificationi

Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or 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 such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP68372.
PaxDbiP68372.
PRIDEiP68372.

2D gel databases

REPRODUCTION-2DPAGEIPI00169463.
P68372.
UCD-2DPAGEP05217.
P68372.

PTM databases

PhosphoSiteiP68372.

Expressioni

Gene expression databases

BgeeiP68372.
CleanExiMM_TUBB2C.
ExpressionAtlasiP68372. baseline and differential.
GenevestigatoriP68372.

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.

Protein-protein interaction databases

BioGridi230642. 28 interactions.
IntActiP68372. 39 interactions.
MINTiMINT-4137100.

Structurei

3D structure databases

SMRiP68372. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The highly acidic C-terminal region may bind cations such as calcium.

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiP68372.
KOiK07375.
OMAiENTDQAY.
OrthoDBiEOG71ZP1H.
PhylomeDBiP68372.
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.

P68372-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY
60 70 80 90 100
YNEATGGKYV PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEFEEEA EEEVA
Length:445
Mass (Da):49,831
Last modified:August 13, 1987 - v1
Checksum:iA552C52822AFA072
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071L → P in AAH05547 (PubMed:15489334).Curated
Sequence conflicti342 – 3421V → A in BAE27282 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146587 mRNA. Translation: BAE27282.1.
AK167022 mRNA. Translation: BAE39195.1.
AL732309 Genomic DNA. Translation: CAM14671.1.
BC005547 mRNA. Translation: AAH05547.1.
BC022919 mRNA. Translation: AAH22919.1.
BC083319 mRNA. Translation: AAH83319.1.
CCDSiCCDS15753.1.
PIRiC25437.
RefSeqiNP_666228.1. NM_146116.2.
UniGeneiMm.227260.
Mm.491119.

Genome annotation databases

EnsembliENSMUST00000043584; ENSMUSP00000042342; ENSMUSG00000036752.
GeneIDi227613.
KEGGimmu:227613.
UCSCiuc008iqs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK146587 mRNA. Translation: BAE27282.1.
AK167022 mRNA. Translation: BAE39195.1.
AL732309 Genomic DNA. Translation: CAM14671.1.
BC005547 mRNA. Translation: AAH05547.1.
BC022919 mRNA. Translation: AAH22919.1.
BC083319 mRNA. Translation: AAH83319.1.
CCDSiCCDS15753.1.
PIRiC25437.
RefSeqiNP_666228.1. NM_146116.2.
UniGeneiMm.227260.
Mm.491119.

3D structure databases

SMRiP68372. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230642. 28 interactions.
IntActiP68372. 39 interactions.
MINTiMINT-4137100.

PTM databases

PhosphoSiteiP68372.

2D gel databases

REPRODUCTION-2DPAGEIPI00169463.
P68372.
UCD-2DPAGEP05217.
P68372.

Proteomic databases

MaxQBiP68372.
PaxDbiP68372.
PRIDEiP68372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043584; ENSMUSP00000042342; ENSMUSG00000036752.
GeneIDi227613.
KEGGimmu:227613.
UCSCiuc008iqs.2. mouse.

Organism-specific databases

CTDi10383.
MGIiMGI:1915472. Tubb4b.

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiP68372.
KOiK07375.
OMAiENTDQAY.
OrthoDBiEOG71ZP1H.
PhylomeDBiP68372.
TreeFamiTF300298.

Enzyme and pathway databases

ReactomeiREACT_272448. Recruitment of mitotic centrosome proteins and complexes.
REACT_276302. Loss of Nlp from mitotic centrosomes.
REACT_278699. Hedgehog 'off' state.
REACT_286537. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_295993. Gap junction assembly.
REACT_297274. Orphan transporters.
REACT_298063. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_306375. Mitotic Prometaphase.
REACT_307151. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_316383. MHC class II antigen presentation.
REACT_319119. Post-chaperonin tubulin folding pathway.
REACT_319807. Assembly of the primary cilium.
REACT_321346. Separation of Sister Chromatids.
REACT_328862. Anchoring of the basal body to the plasma membrane.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_330163. Formation of tubulin folding intermediates by CCT/TriC.
REACT_332968. Recruitment of NuMA to mitotic centrosomes.
REACT_341960. Intraflagellar transport.
REACT_342780. Kinesins.
REACT_345278. Regulation of PLK1 Activity at G2/M Transition.
REACT_351311. Hedgehog 'on' state.
REACT_353475. Recycling pathway of L1.

Miscellaneous databases

NextBioi378658.
PROiP68372.
SOURCEiSearch...

Gene expression databases

BgeeiP68372.
CleanExiMM_TUBB2C.
ExpressionAtlasiP68372. baseline and differential.
GenevestigatoriP68372.

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. "The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype."
    Wang D., Villasante A., Lewis S.A., Cowan N.J.
    J. Cell Biol. 103:1903-1910(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain, Kidney and Mammary tumor.
  5. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 3-19; 47-58; 63-121; 163-174; 217-276; 283-297; 310-318; 321-359; 363-379 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  6. Cited for: POLYGLUTAMYLATION.
  7. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYGLYCYLATION.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTBB4B_MOUSE
AccessioniPrimary (citable) accession number: P68372
Secondary accession number(s): P05217
, Q3TKF0, Q3UJ73, Q99JZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 1, 2015
This is version 111 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, Direct protein sequencing, 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

External Data

Dasty 3

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 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.