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Q9D6F9

- TBB4A_MOUSE

UniProt

Q9D6F9 - TBB4A_MOUSE

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Protein
Tubulin beta-4A chain
Gene
Tubb4a, Tubb4
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 – 1467GTP Reviewed prediction

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTPase activity Source: InterPro
  3. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. cell projection organization Source: UniProtKB-KW
  2. microtubule-based process Source: InterPro
  3. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_199117. Kinesins.
REACT_207679. Separation of Sister Chromatids.
REACT_218773. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_227366. Gap junction assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-4A chain
Alternative name(s):
Tubulin beta-4 chain
Gene namesi
Name:Tubb4a
Synonyms:Tubb4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:107848. Tubb4a.

Subcellular locationi

GO - Cellular componenti

  1. cell projection Source: MGI
  2. cilium Source: MGI
  3. cytoplasm Source: MGI
  4. internode region of axon Source: MGI
  5. microtubule Source: UniProtKB-KW
  6. myelin sheath Source: MGI
  7. neuronal cell body Source: MGI
  8. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Tubulin beta-4A chain
PRO_0000048254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine; by CDK1 By 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

Phosphoprotein

Proteomic databases

MaxQBiQ9D6F9.
PRIDEiQ9D6F9.

2D gel databases

REPRODUCTION-2DPAGEIPI00109073.
Q9D6F9.

PTM databases

PhosphoSiteiQ9D6F9.

Expressioni

Gene expression databases

BgeeiQ9D6F9.
CleanExiMM_TUBB4.
GenevestigatoriQ9D6F9.

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

BioGridi204380. 6 interactions.
IntActiQ9D6F9. 8 interactions.
MINTiMINT-4137071.

Structurei

3D structure databases

ProteinModelPortaliQ9D6F9.
SMRiQ9D6F9. Positions 2-427.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the tubulin family.

Phylogenomic databases

GeneTreeiENSGT00750000117394.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ9D6F9.
KOiK07375.
OMAiMQLERIN.
OrthoDBiEOG71ZP1H.
PhylomeDBiQ9D6F9.
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.

Q9D6F9-1 [UniParc]FASTAAdd to Basket

« Hide

MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY    50
YNEATGGNYV PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 100
WAKGHYTEGA ELVDAVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL 150
LISKIREEFP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY 200
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 250
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM 300
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LSVQSKNSSY FVEWIPNNVK 350
TAVCDIPPRG LKMAATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 400
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEGEFEEEAE EEVA 444
Length:444
Mass (Da):49,586
Last modified:May 1, 2007 - v3
Checksum:iF7429D057C11A3F5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731M → I in AAA40509. 1 Publication
Sequence conflicti111 – 1111E → Q in AAA40509. 1 Publication
Sequence conflicti270 – 2701F → L in AAA40509. 1 Publication
Sequence conflicti293 – 2931M → V in AAA40509. 1 Publication
Sequence conflicti303 – 3031C → S in AAA40509. 1 Publication
Sequence conflicti351 – 3511T → A in AAA40509. 1 Publication
Sequence conflicti400 – 4001G → A in AAA40509. 1 Publication
Sequence conflicti427 – 4271D → G in BAB28967. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK013717 mRNA. Translation: BAB28967.1.
BC049112 mRNA. Translation: AAH49112.1.
BC054831 mRNA. Translation: AAH54831.1.
M28730 mRNA. Translation: AAA40509.1.
CCDSiCCDS28925.1.
RefSeqiNP_033477.2. NM_009451.3.
UniGeneiMm.7420.

Genome annotation databases

EnsembliENSMUST00000071135; ENSMUSP00000071135; ENSMUSG00000062591.
GeneIDi22153.
KEGGimmu:22153.
UCSCiuc008dea.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK013717 mRNA. Translation: BAB28967.1 .
BC049112 mRNA. Translation: AAH49112.1 .
BC054831 mRNA. Translation: AAH54831.1 .
M28730 mRNA. Translation: AAA40509.1 .
CCDSi CCDS28925.1.
RefSeqi NP_033477.2. NM_009451.3.
UniGenei Mm.7420.

3D structure databases

ProteinModelPortali Q9D6F9.
SMRi Q9D6F9. Positions 2-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204380. 6 interactions.
IntActi Q9D6F9. 8 interactions.
MINTi MINT-4137071.

Chemistry

BindingDBi Q9D6F9.

PTM databases

PhosphoSitei Q9D6F9.

2D gel databases

REPRODUCTION-2DPAGE IPI00109073.
Q9D6F9.

Proteomic databases

MaxQBi Q9D6F9.
PRIDEi Q9D6F9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000071135 ; ENSMUSP00000071135 ; ENSMUSG00000062591 .
GeneIDi 22153.
KEGGi mmu:22153.
UCSCi uc008dea.1. mouse.

Organism-specific databases

CTDi 10382.
MGIi MGI:107848. Tubb4a.

Phylogenomic databases

GeneTreei ENSGT00750000117394.
HOGENOMi HOG000165710.
HOVERGENi HBG000089.
InParanoidi Q9D6F9.
KOi K07375.
OMAi MQLERIN.
OrthoDBi EOG71ZP1H.
PhylomeDBi Q9D6F9.
TreeFami TF300298.

Enzyme and pathway databases

Reactomei REACT_196550. MHC class II antigen presentation.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_199117. Kinesins.
REACT_207679. Separation of Sister Chromatids.
REACT_218773. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_227366. Gap junction assembly.

Miscellaneous databases

NextBioi 302070.
PROi Q9D6F9.
SOURCEi Search...

Gene expression databases

Bgeei Q9D6F9.
CleanExi MM_TUBB4.
Genevestigatori Q9D6F9.

Family and domain databases

Gene3Di 1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProi IPR013838. 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 ]
PANTHERi PTHR11588. PTHR11588. 1 hit.
Pfami PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view ]
PRINTSi PR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTi SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEi PS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hippocampus.
  2. "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].
    Strain: C57BL/6.
    Tissue: Brain and Olfactory epithelium.
  3. Lubec G., Klug S., Kang S.U.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 3-19; 47-77; 104-121; 163-174; 242-276; 283-297; 310-318; 321-359; 363-379 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  4. "Five mouse tubulin isotypes and their regulated expression during development."
    Lewis S.A., Lee M.G.-S., Cowan N.J.
    J. Cell Biol. 101:852-861(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-444.
  5. Cited for: POLYGLUTAMYLATION.
  6. "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: POLYGLYCYLATION.

Entry informationi

Entry nameiTBB4A_MOUSE
AccessioniPrimary (citable) accession number: Q9D6F9
Secondary accession number(s): Q62364, Q80Y54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 1, 2007
Last modified: September 3, 2014
This is version 115 of the entry and version 3 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