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Protein

Tubulin beta chain

Gene

TUBB

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.

Regions

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

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. MHC class I protein binding Source: UniProtKB
  4. structural constituent of cytoskeleton Source: Ensembl
  5. structural molecule activity Source: BHF-UCL
  6. ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. cell division Source: BHF-UCL
  2. cellular process Source: DFLAT
  3. cytoskeleton-dependent intracellular transport Source: BHF-UCL
  4. G2/M transition of mitotic cell cycle Source: Reactome
  5. GTP catabolic process Source: InterPro
  6. microtubule-based process Source: BHF-UCL
  7. mitotic cell cycle Source: Reactome
  8. movement of cell or subcellular component Source: UniProtKB
  9. natural killer cell mediated cytotoxicity Source: UniProtKB
  10. organelle organization Source: Reactome
  11. protein polymerization Source: InterPro
  12. spindle assembly Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta chain
Alternative name(s):
Tubulin beta-5 chain
Gene namesi
Name:TUBB
Synonyms:TUBB5
ORF Names:OK/SW-cl.56
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:20778. TUBB.

Subcellular locationi

GO - Cellular componenti

  1. cell body Source: DFLAT
  2. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  3. cytoskeleton Source: UniProtKB
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: UniProtKB
  6. microtubule Source: UniProtKB
  7. nuclear envelope lumen Source: DFLAT
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Cortical dysplasia, complex, with other brain malformations 61 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder of aberrant neuronal migration and disturbed axonal guidance. Affected individuals have microcephaly, ataxia, and severe delayed psychomotor development. Brain imaging shows variable malformations of cortical development, including white matter streaks, dysmorphic basal ganglia, corpus callosum abnormalities, brainstem and cerebellar hypoplasia, cortical dysplasia, polymicrogyria.

See also OMIM:615771
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti299 – 2991M → V in CDCBM6; decreases the ability of the protein to assemble into tubulin heterodimers. 1 Publication
VAR_071763
Natural varianti353 – 3531V → I in CDCBM6; does not affect the ability of the mutant polypeptides to assemble into heterodimers and incorporate into microtubules. 1 Publication
VAR_071764
Natural varianti401 – 4011E → K in CDCBM6; arrests the assembly pathway of alpha/beta-tubulin; the mutant protein is unable to coassemble into a tubulin heterodimer but is instead distributed throughout the cytoplasm. 1 Publication
VAR_071765

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615771. phenotype.
PharmGKBiPA358.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Tubulin beta chainPRO_0000048243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581N6-acetyllysine; alternate1 Publication
Modified residuei58 – 581N6-succinyllysine; alternateBy similarity
Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity
Modified residuei318 – 3181Omega-N-methylarginine1 Publication
Cross-linki324 – 324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also 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) 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 glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable).Curated

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP07437.
PaxDbiP07437.
PRIDEiP07437.

2D gel databases

OGPiP07437.
REPRODUCTION-2DPAGEP07437.
SWISS-2DPAGEP07437.
UCD-2DPAGEP07437.

PTM databases

PhosphoSiteiP07437.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest levels in spleen, thymus and immature brain.1 Publication

Gene expression databases

BgeeiP07437.
CleanExiHS_TUBB.
ExpressionAtlasiP07437. baseline and differential.
GenevestigatoriP07437.

Organism-specific databases

HPAiCAB005417.
CAB012406.
HPA043640.
HPA046280.

Interactioni

Subunit structurei

May interact with RNABP10 (By similarity). Interacts with MX1 (By similarity). 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 PIFO.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EBNA-LPQ8AZK73EBI-350864,EBI-1185167From a different organism.
LRRK2Q5S0074EBI-350864,EBI-5323863

Protein-protein interaction databases

BioGridi128444. 183 interactions.
DIPiDIP-32772N.
IntActiP07437. 78 interactions.
MINTiMINT-1146393.
STRINGi9606.ENSP00000410071.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QNZX-ray2.20C429-438[»]
3QO0X-ray2.30C422-441[»]
ProteinModelPortaliP07437.
SMRiP07437. 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.
HOVERGENiHBG000089.
InParanoidiP07437.
KOiK07375.
OMAiWPIPSIV.
PhylomeDBiP07437.
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.

P07437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY
60 70 80 90 100
YNEATGGKYV PRAILVDLEP 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 QQVFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDFGEEA EEEA
Length:444
Mass (Da):49,671
Last modified:December 21, 2004 - v2
Checksum:i1E6CD0A36773A103
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161K → R no nucleotide entry (PubMed:6688039).Curated
Sequence conflicti216 – 2161K → R in AAB59507 (PubMed:6865944).Curated
Sequence conflicti231 – 2311A → G no nucleotide entry (PubMed:6688039).Curated
Sequence conflicti231 – 2311A → G in AAB59507 (PubMed:6865944).Curated
Sequence conflicti234 – 2352SG → EC no nucleotide entry (PubMed:6688039).Curated
Sequence conflicti234 – 2352SG → EC in AAB59507 (PubMed:6865944).Curated
Sequence conflicti288 – 2881E → D no nucleotide entry (PubMed:6688039).Curated
Sequence conflicti288 – 2881E → D in AAB59507 (PubMed:6865944).Curated
Sequence conflicti298 – 2981N → D in AAH20946 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti299 – 2991M → V in CDCBM6; decreases the ability of the protein to assemble into tubulin heterodimers. 1 Publication
VAR_071763
Natural varianti353 – 3531V → I in CDCBM6; does not affect the ability of the mutant polypeptides to assemble into heterodimers and incorporate into microtubules. 1 Publication
VAR_071764
Natural varianti401 – 4011E → K in CDCBM6; arrests the assembly pathway of alpha/beta-tubulin; the mutant protein is unable to coassemble into a tubulin heterodimer but is instead distributed throughout the cytoplasm. 1 Publication
VAR_071765

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00314 Genomic DNA. Translation: AAB59507.1.
AF141349 mRNA. Translation: AAD33873.1.
AF070561 mRNA. Translation: AAC28642.1.
AF070593 mRNA. Translation: AAC28650.1.
AF070600 mRNA. Translation: AAC28654.1.
BA000025 Genomic DNA. Translation: BAB63321.1.
AB088100 Genomic DNA. Translation: BAC54932.1.
AB062393 mRNA. Translation: BAB93480.1.
BC001938 mRNA. Translation: AAH01938.1.
BC002347 mRNA. Translation: AAH02347.1.
BC005838 mRNA. Translation: AAH05838.1.
BC007605 mRNA. Translation: AAH07605.1.
BC013374 mRNA. Translation: AAH13374.1.
BC019924 mRNA. Translation: AAH19924.1.
BC020946 mRNA. Translation: AAH20946.1.
BC021909 mRNA. Translation: AAH21909.1.
BC070326 mRNA. Translation: AAH70326.1.
CCDSiCCDS4687.1.
PIRiA26561.
RefSeqiNP_001280141.1. NM_001293212.1.
NP_001280142.1. NM_001293213.1.
NP_001280143.1. NM_001293214.1.
NP_001280144.1. NM_001293215.1.
NP_001280145.1. NM_001293216.1.
NP_821133.1. NM_178014.3.
UniGeneiHs.636480.

Genome annotation databases

EnsembliENST00000327892; ENSP00000339001; ENSG00000196230.
ENST00000383564; ENSP00000373058; ENSG00000183311.
ENST00000419792; ENSP00000401317; ENSG00000235067.
ENST00000421473; ENSP00000399155; ENSG00000224156.
ENST00000422650; ENSP00000400663; ENSG00000229684.
ENST00000422674; ENSP00000406811; ENSG00000227739.
ENST00000432462; ENSP00000410829; ENSG00000232421.
ENST00000436628; ENSP00000410071; ENSG00000232575.
GeneIDi203068.
KEGGihsa:203068.
UCSCiuc003nrl.3. human.

Polymorphism databases

DMDMi56757569.

Cross-referencesi

Web resourcesi

Wikipedia

Tubulin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00314 Genomic DNA. Translation: AAB59507.1.
AF141349 mRNA. Translation: AAD33873.1.
AF070561 mRNA. Translation: AAC28642.1.
AF070593 mRNA. Translation: AAC28650.1.
AF070600 mRNA. Translation: AAC28654.1.
BA000025 Genomic DNA. Translation: BAB63321.1.
AB088100 Genomic DNA. Translation: BAC54932.1.
AB062393 mRNA. Translation: BAB93480.1.
BC001938 mRNA. Translation: AAH01938.1.
BC002347 mRNA. Translation: AAH02347.1.
BC005838 mRNA. Translation: AAH05838.1.
BC007605 mRNA. Translation: AAH07605.1.
BC013374 mRNA. Translation: AAH13374.1.
BC019924 mRNA. Translation: AAH19924.1.
BC020946 mRNA. Translation: AAH20946.1.
BC021909 mRNA. Translation: AAH21909.1.
BC070326 mRNA. Translation: AAH70326.1.
CCDSiCCDS4687.1.
PIRiA26561.
RefSeqiNP_001280141.1. NM_001293212.1.
NP_001280142.1. NM_001293213.1.
NP_001280143.1. NM_001293214.1.
NP_001280144.1. NM_001293215.1.
NP_001280145.1. NM_001293216.1.
NP_821133.1. NM_178014.3.
UniGeneiHs.636480.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QNZX-ray2.20C429-438[»]
3QO0X-ray2.30C422-441[»]
ProteinModelPortaliP07437.
SMRiP07437. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128444. 183 interactions.
DIPiDIP-32772N.
IntActiP07437. 78 interactions.
MINTiMINT-1146393.
STRINGi9606.ENSP00000410071.

Chemistry

ChEMBLiCHEMBL2095182.
DrugBankiDB01394. Colchicine.
DB01179. Podofilox.
DB00570. Vinblastine.
DB00541. Vincristine.
DB00361. Vinorelbine.
GuidetoPHARMACOLOGYi2640.

PTM databases

PhosphoSiteiP07437.

Polymorphism databases

DMDMi56757569.

2D gel databases

OGPiP07437.
REPRODUCTION-2DPAGEP07437.
SWISS-2DPAGEP07437.
UCD-2DPAGEP07437.

Proteomic databases

MaxQBiP07437.
PaxDbiP07437.
PRIDEiP07437.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327892; ENSP00000339001; ENSG00000196230.
ENST00000383564; ENSP00000373058; ENSG00000183311.
ENST00000419792; ENSP00000401317; ENSG00000235067.
ENST00000421473; ENSP00000399155; ENSG00000224156.
ENST00000422650; ENSP00000400663; ENSG00000229684.
ENST00000422674; ENSP00000406811; ENSG00000227739.
ENST00000432462; ENSP00000410829; ENSG00000232421.
ENST00000436628; ENSP00000410071; ENSG00000232575.
GeneIDi203068.
KEGGihsa:203068.
UCSCiuc003nrl.3. human.

Organism-specific databases

CTDi203068.
GeneCardsiGC06P030687.
GC06Pi30696.
GC06Pj30677.
GC06Pk30678.
GC06Pl30732.
GC06Pm30766.
GC06Pn30677.
GC06Po30679.
HGNCiHGNC:20778. TUBB.
HPAiCAB005417.
CAB012406.
HPA043640.
HPA046280.
MIMi191130. gene.
615771. phenotype.
neXtProtiNX_P07437.
PharmGKBiPA358.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5023.
HOVERGENiHBG000089.
InParanoidiP07437.
KOiK07375.
OMAiWPIPSIV.
PhylomeDBiP07437.
TreeFamiTF300298.

Enzyme and pathway databases

ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

ChiTaRSiTUBB. human.
GeneWikiiTUBB.
GenomeRNAii203068.
NextBioi90324.
PROiP07437.
SOURCEiSearch...

Gene expression databases

BgeeiP07437.
CleanExiHS_TUBB.
ExpressionAtlasiP07437. baseline and differential.
GenevestigatoriP07437.

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. "Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes."
    Lee M.G.-S., Lewis S.A., Wilde C.D., Cowan N.J.
    Cell 33:477-487(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of two human beta-tubulin isotypes."
    Hall J.L., Dudley L., Dobner P.R., Lewis S.A., Cowan N.J.
    Mol. Cell. Biol. 3:854-862(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site."
    Crabtree D.V., Ojima I., Geng X., Adler A.J.
    Bioorg. Med. Chem. 9:1967-1976(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  4. Yu W., Gibbs R.A.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
    Shiina S., Tamiya G., Oka A., Inoko H.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Genome diversity in HLA: a new strategy for detection of genetic polymorphisms in expressed genes within the HLA class III and class I regions."
    Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon adenocarcinoma.
  8. "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, Eye, Lung, Muscle and Placenta.
  9. Bienvenut W.V., Campbell A., Ozanne B.W., Lourenco F., Olson M.F.
    Submitted (DEC-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-19; 47-77; 104-174; 242-276; 283-297; 310-359 AND 363-390, METHYLATION AT ARG-318, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Foreskin fibroblast and Mammary carcinoma.
  10. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 3-19; 47-58; 63-77; 104-121; 163-174; 242-251; 253-276; 283-297; 310-318; 325-336 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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.
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: TISSUE SPECIFICITY.
  15. Cited for: INTERACTION WITH PIFO.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. Cited for: VARIANTS CDCBM6 VAL-299; ILE-353 AND LYS-401, CHARACTERIZATION OF VARIANTS CDCBM6 VAL-299 AND LYS-401.

Entry informationi

Entry nameiTBB5_HUMAN
AccessioniPrimary (citable) accession number: P07437
Secondary accession number(s): P05218, Q8WUC1, Q9CY33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 21, 2004
Last modified: March 4, 2015
This is version 178 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.