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Q9BVA1

- TBB2B_HUMAN

UniProt

Q9BVA1 - TBB2B_HUMAN

Protein

Tubulin beta-2B chain

Gene

TUBB2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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. TUBB2B is implicated in neuronal migration.By similarity1 Publication

    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. protein binding Source: IntAct
    4. structural constituent of cytoskeleton Source: InterPro

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. microtubule-based process Source: InterPro
    4. neuron migration Source: UniProtKB
    5. protein folding Source: Reactome
    6. protein polymerization Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
    REACT_121399. MHC class II antigen presentation.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
    REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
    REACT_16967. Post-chaperonin tubulin folding pathway.
    REACT_22365. Recycling pathway of L1.
    REACT_25201. Kinesins.
    REACT_682. Mitotic Prometaphase.
    REACT_9509. Gap junction assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin beta-2B chain
    Gene namesi
    Name:TUBB2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:30829. TUBB2B.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule Source: UniProtKB
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Polymicrogyria, symmetric or asymmetric (PMGYSA) [MIM:610031]: A malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti172 – 1721S → P in PMGYSA; affects microtubules assembly. 1 Publication
    VAR_063389
    Natural varianti210 – 2101I → T in PMGYSA. 1 Publication
    VAR_063391
    Natural varianti228 – 2281L → P in PMGYSA. 1 Publication
    VAR_063392
    Natural varianti265 – 2651F → L in PMGYSA; affects microtubules assembly. 1 Publication
    VAR_063393
    Natural varianti312 – 3121T → M in PMGYSA. 1 Publication
    VAR_063394

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi610031. phenotype.
    Orphaneti45358. Congenital fibrosis of extraocular muscles.
    300573. Polymicrogyria due to TUBB2B mutation.
    PharmGKBiPA142670671.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Tubulin beta-2B chainPRO_0000262651Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei172 – 1721Phosphoserine; by CDK1By similarity

    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

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BVA1.
    PaxDbiQ9BVA1.
    PRIDEiQ9BVA1.

    PTM databases

    PhosphoSiteiQ9BVA1.

    Expressioni

    Tissue specificityi

    High expression in brain.1 Publication

    Gene expression databases

    ArrayExpressiQ9BVA1.
    BgeeiQ9BVA1.
    CleanExiHS_TUBB2B.
    GenevestigatoriQ9BVA1.

    Organism-specific databases

    HPAiHPA043640.
    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CACNA1AO005552EBI-355665,EBI-766279

    Protein-protein interaction databases

    BioGridi131483. 27 interactions.
    IntActiQ9BVA1. 17 interactions.
    MINTiMINT-1152234.
    STRINGi9606.ENSP00000259818.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BVA1.
    SMRiQ9BVA1. Positions 1-431.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    HOGENOMiHOG000165710.
    HOVERGENiHBG000089.
    InParanoidiQ9BVA1.
    KOiK07375.
    OMAiYQQEEEY.
    OrthoDBiEOG71ZP1H.
    PhylomeDBiQ9BVA1.
    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.

    Q9BVA1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY    50
    YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 100
    WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL 150
    LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY 200
    CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 250
    RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM 300
    AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 350
    TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 400
    EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA 445
    Length:445
    Mass (Da):49,953
    Last modified:June 1, 2001 - v1
    Checksum:i4DC3956EFF880746
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti172 – 1721S → P in PMGYSA; affects microtubules assembly. 1 Publication
    VAR_063389
    Natural varianti201 – 2011C → S.1 Publication
    Corresponds to variant rs1054331 [ dbSNP | Ensembl ].
    VAR_063390
    Natural varianti210 – 2101I → T in PMGYSA. 1 Publication
    VAR_063391
    Natural varianti228 – 2281L → P in PMGYSA. 1 Publication
    VAR_063392
    Natural varianti265 – 2651F → L in PMGYSA; affects microtubules assembly. 1 Publication
    VAR_063393
    Natural varianti312 – 3121T → M in PMGYSA. 1 Publication
    VAR_063394

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT019930 mRNA. Translation: AAV38733.1.
    CR456788 mRNA. Translation: CAG33069.1.
    AK289433 mRNA. Translation: BAF82122.1.
    AL445309 Genomic DNA. Translation: CAI40952.1.
    CH471087 Genomic DNA. Translation: EAW55125.1.
    BC001352 mRNA. Translation: AAH01352.1.
    BC063610 mRNA. Translation: AAH63610.1.
    CCDSiCCDS4485.1.
    RefSeqiNP_821080.1. NM_178012.4.
    UniGeneiHs.300701.

    Genome annotation databases

    EnsembliENST00000259818; ENSP00000259818; ENSG00000137285.
    GeneIDi347733.
    KEGGihsa:347733.
    UCSCiuc003mvg.3. human.

    Polymorphism databases

    DMDMi74761283.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT019930 mRNA. Translation: AAV38733.1 .
    CR456788 mRNA. Translation: CAG33069.1 .
    AK289433 mRNA. Translation: BAF82122.1 .
    AL445309 Genomic DNA. Translation: CAI40952.1 .
    CH471087 Genomic DNA. Translation: EAW55125.1 .
    BC001352 mRNA. Translation: AAH01352.1 .
    BC063610 mRNA. Translation: AAH63610.1 .
    CCDSi CCDS4485.1.
    RefSeqi NP_821080.1. NM_178012.4.
    UniGenei Hs.300701.

    3D structure databases

    ProteinModelPortali Q9BVA1.
    SMRi Q9BVA1. Positions 1-431.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 131483. 27 interactions.
    IntActi Q9BVA1. 17 interactions.
    MINTi MINT-1152234.
    STRINGi 9606.ENSP00000259818.

    Chemistry

    BindingDBi Q9BVA1.
    ChEMBLi CHEMBL2095182.

    PTM databases

    PhosphoSitei Q9BVA1.

    Polymorphism databases

    DMDMi 74761283.

    Proteomic databases

    MaxQBi Q9BVA1.
    PaxDbi Q9BVA1.
    PRIDEi Q9BVA1.

    Protocols and materials databases

    DNASUi 347733.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259818 ; ENSP00000259818 ; ENSG00000137285 .
    GeneIDi 347733.
    KEGGi hsa:347733.
    UCSCi uc003mvg.3. human.

    Organism-specific databases

    CTDi 347733.
    GeneCardsi GC06M003224.
    HGNCi HGNC:30829. TUBB2B.
    HPAi HPA043640.
    HPA046280.
    MIMi 610031. phenotype.
    612850. gene.
    neXtProti NX_Q9BVA1.
    Orphaneti 45358. Congenital fibrosis of extraocular muscles.
    300573. Polymicrogyria due to TUBB2B mutation.
    PharmGKBi PA142670671.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5023.
    HOGENOMi HOG000165710.
    HOVERGENi HBG000089.
    InParanoidi Q9BVA1.
    KOi K07375.
    OMAi YQQEEEY.
    OrthoDBi EOG71ZP1H.
    PhylomeDBi Q9BVA1.
    TreeFami TF300298.

    Enzyme and pathway databases

    Reactomei REACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
    REACT_121399. MHC class II antigen presentation.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
    REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
    REACT_16967. Post-chaperonin tubulin folding pathway.
    REACT_22365. Recycling pathway of L1.
    REACT_25201. Kinesins.
    REACT_682. Mitotic Prometaphase.
    REACT_9509. Gap junction assembly.

    Miscellaneous databases

    ChiTaRSi TUBB2B. human.
    GenomeRNAii 347733.
    NextBioi 99262.
    PROi Q9BVA1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BVA1.
    Bgeei Q9BVA1.
    CleanExi HS_TUBB2B.
    Genevestigatori Q9BVA1.

    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

    1. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 and Muscle.
    7. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 47-58; 63-121; 163-174; 217-276; 283-297; 310-318; 325-359; 363-379 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    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.
    9. Cited for: FUNCTION, VARIANTS PMGYSA PRO-172; THR-210; PRO-228; LEU-265 AND MET-312, VARIANT SER-201, CHARACTERIZATION OF VARIANTS PMGYSA PRO-172 AND LEU-265.
    10. Cited for: TISSUE SPECIFICITY.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTBB2B_HUMAN
    AccessioniPrimary (citable) accession number: Q9BVA1
    Secondary accession number(s): A8K068
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 128 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 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3