Full text data of TUBB4B
TUBB4B
(TUBB2C)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Tubulin beta-4B chain (Tubulin beta-2 chain; Tubulin beta-2C chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tubulin beta-4B chain (Tubulin beta-2 chain; Tubulin beta-2C chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P68371
ID TBB4B_HUMAN Reviewed; 445 AA.
AC P68371; A2BFA2; P05217;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-1987, sequence version 1.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Tubulin beta-4B chain;
DE AltName: Full=Tubulin beta-2 chain;
DE AltName: Full=Tubulin beta-2C chain;
GN Name=TUBB4B; Synonyms=TUBB2C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3999141; DOI=10.1016/0022-2836(85)90023-3;
RA Lewis S.A., Gilmartin M.E., Hall J.L., Cowan N.J.;
RT "Three expressed sequences within the human beta-tubulin multigene
RT family each define a distinct isotype.";
RL J. Mol. Biol. 182:11-20(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Cervix, Lung, Lymph, Muscle, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=20191564; DOI=10.1002/cm.20436;
RA Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C.,
RA Lopez-Jimenez E., Leton R., Cascon A., Robledo M.,
RA Rodriguez-Antona C.;
RT "Tumoral and tissue-specific expression of the major human beta-
RT tubulin isotypes.";
RL Cytoskeleton 67:214-223(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC binds two moles of GTP, one at an exchangeable site on the beta
CC chain and one at a non-exchangeable site on the alpha chain.
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is
CC a hollow water-filled tube with an outer diameter of 25 nm and an
CC inner diameter of 15 nM. Alpha-beta heterodimers associate head-
CC to-tail to form protofilaments running lengthwise along the
CC microtubule wall with the beta-tubulin subunit facing the
CC microtubule plus end conferring a structural polarity.
CC Microtubules usually have 13 protofilaments but different
CC protofilament numbers can be found in some organisms and
CC specialized cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The highly acidic C-terminal region may bind cations such
CC as calcium.
CC -!- PTM: Some glutamate residues at the C-terminus are
CC polyglutamylated. This modification occurs exclusively on
CC glutamate residues and results in polyglutamate chains on the
CC gamma-carboxyl group. Also monoglycylated but not polyglycylated
CC due to the absence of functional TTLL10 in human. Monoglycylation
CC is mainly limited to tubulin incorporated into axonemes (cilia and
CC flagella) whereas glutamylation is prevalent in neuronal cells,
CC centrioles, axonemes, and the mitotic spindle. Both modifications
CC can coexist on the same protein on adjacent residues, and lowering
CC glycylation levels increases polyglutamylation, and reciprocally.
CC The precise function of such modifications is still unclear but
CC they regulate the assembly and dynamics of axonemal microtubules
CC (Probable).
CC -!- SIMILARITY: Belongs to the tubulin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X02344; CAA26203.1; -; Genomic_DNA.
DR EMBL; BX255925; CAM24148.1; -; Genomic_DNA.
DR EMBL; BC001911; AAH01911.1; -; mRNA.
DR EMBL; BC002783; AAH02783.1; -; mRNA.
DR EMBL; BC002885; AAH02885.1; -; mRNA.
DR EMBL; BC004188; AAH04188.1; -; mRNA.
DR EMBL; BC007889; AAH07889.1; -; mRNA.
DR EMBL; BC012835; AAH12835.1; -; mRNA.
DR EMBL; BC019359; AAH19359.1; -; mRNA.
DR EMBL; BC019829; AAH19829.1; -; mRNA.
DR EMBL; BC039175; AAH39175.1; -; mRNA.
DR EMBL; BC071889; AAH71889.1; -; mRNA.
DR PIR; I38370; I38370.
DR RefSeq; NP_006079.1; NM_006088.5.
DR UniGene; Hs.433615; -.
DR ProteinModelPortal; P68371; -.
DR SMR; P68371; 2-427.
DR IntAct; P68371; 37.
DR MINT; MINT-1390314; -.
DR STRING; 9606.ENSP00000341289; -.
DR BindingDB; P68371; -.
DR ChEMBL; CHEMBL2095182; -.
DR PhosphoSite; P68371; -.
DR DMDM; 55977480; -.
DR OGP; P05217; -.
DR REPRODUCTION-2DPAGE; IPI00007752; -.
DR SWISS-2DPAGE; P68371; -.
DR PeptideAtlas; P68371; -.
DR PRIDE; P68371; -.
DR DNASU; 10383; -.
DR Ensembl; ENST00000340384; ENSP00000341289; ENSG00000188229.
DR GeneID; 10383; -.
DR KEGG; hsa:10383; -.
DR UCSC; uc004cmg.1; human.
DR CTD; 10383; -.
DR GeneCards; GC09P140136; -.
DR HGNC; HGNC:20771; TUBB4B.
DR HPA; CAB010880; -.
DR HPA; HPA043640; -.
DR HPA; HPA046280; -.
DR MIM; 602660; gene.
DR neXtProt; NX_P68371; -.
DR PharmGKB; PA142670672; -.
DR HOGENOM; HOG000165710; -.
DR HOVERGEN; HBG000089; -.
DR InParanoid; P68371; -.
DR KO; K07375; -.
DR OMA; DQAYCID; -.
DR OrthoDB; EOG71ZP1H; -.
DR PhylomeDB; P68371; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; TUBB4B; human.
DR GeneWiki; TUBB2C; -.
DR GenomeRNAi; 10383; -.
DR NextBio; 39335; -.
DR PRO; PR:P68371; -.
DR ArrayExpress; P68371; -.
DR Bgee; P68371; -.
DR CleanEx; HS_TUBB2C; -.
DR Genevestigator; P68371; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042288; F:MHC class I protein binding; TAS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0006928; P:cellular component movement; TAS:ProtInc.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; NAS:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR GO; GO:0051225; P:spindle assembly; IEA:Ensembl.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding;
KW Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1 445 Tubulin beta-4B chain.
FT /FTId=PRO_0000048248.
FT NP_BIND 140 146 GTP (Potential).
FT MOD_RES 58 58 N6-acetyllysine.
FT MOD_RES 172 172 Phosphoserine; by CDK1 (Probable).
SQ SEQUENCE 445 AA; 49831 MW; A552C52822AFA072 CRC64;
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGKYV
PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEFEEEA EEEVA
//
ID TBB4B_HUMAN Reviewed; 445 AA.
AC P68371; A2BFA2; P05217;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-1987, sequence version 1.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Tubulin beta-4B chain;
DE AltName: Full=Tubulin beta-2 chain;
DE AltName: Full=Tubulin beta-2C chain;
GN Name=TUBB4B; Synonyms=TUBB2C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3999141; DOI=10.1016/0022-2836(85)90023-3;
RA Lewis S.A., Gilmartin M.E., Hall J.L., Cowan N.J.;
RT "Three expressed sequences within the human beta-tubulin multigene
RT family each define a distinct isotype.";
RL J. Mol. Biol. 182:11-20(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Cervix, Lung, Lymph, Muscle, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=20191564; DOI=10.1002/cm.20436;
RA Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C.,
RA Lopez-Jimenez E., Leton R., Cascon A., Robledo M.,
RA Rodriguez-Antona C.;
RT "Tumoral and tissue-specific expression of the major human beta-
RT tubulin isotypes.";
RL Cytoskeleton 67:214-223(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC binds two moles of GTP, one at an exchangeable site on the beta
CC chain and one at a non-exchangeable site on the alpha chain.
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is
CC a hollow water-filled tube with an outer diameter of 25 nm and an
CC inner diameter of 15 nM. Alpha-beta heterodimers associate head-
CC to-tail to form protofilaments running lengthwise along the
CC microtubule wall with the beta-tubulin subunit facing the
CC microtubule plus end conferring a structural polarity.
CC Microtubules usually have 13 protofilaments but different
CC protofilament numbers can be found in some organisms and
CC specialized cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The highly acidic C-terminal region may bind cations such
CC as calcium.
CC -!- PTM: Some glutamate residues at the C-terminus are
CC polyglutamylated. This modification occurs exclusively on
CC glutamate residues and results in polyglutamate chains on the
CC gamma-carboxyl group. Also monoglycylated but not polyglycylated
CC due to the absence of functional TTLL10 in human. Monoglycylation
CC is mainly limited to tubulin incorporated into axonemes (cilia and
CC flagella) whereas glutamylation is prevalent in neuronal cells,
CC centrioles, axonemes, and the mitotic spindle. Both modifications
CC can coexist on the same protein on adjacent residues, and lowering
CC glycylation levels increases polyglutamylation, and reciprocally.
CC The precise function of such modifications is still unclear but
CC they regulate the assembly and dynamics of axonemal microtubules
CC (Probable).
CC -!- SIMILARITY: Belongs to the tubulin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X02344; CAA26203.1; -; Genomic_DNA.
DR EMBL; BX255925; CAM24148.1; -; Genomic_DNA.
DR EMBL; BC001911; AAH01911.1; -; mRNA.
DR EMBL; BC002783; AAH02783.1; -; mRNA.
DR EMBL; BC002885; AAH02885.1; -; mRNA.
DR EMBL; BC004188; AAH04188.1; -; mRNA.
DR EMBL; BC007889; AAH07889.1; -; mRNA.
DR EMBL; BC012835; AAH12835.1; -; mRNA.
DR EMBL; BC019359; AAH19359.1; -; mRNA.
DR EMBL; BC019829; AAH19829.1; -; mRNA.
DR EMBL; BC039175; AAH39175.1; -; mRNA.
DR EMBL; BC071889; AAH71889.1; -; mRNA.
DR PIR; I38370; I38370.
DR RefSeq; NP_006079.1; NM_006088.5.
DR UniGene; Hs.433615; -.
DR ProteinModelPortal; P68371; -.
DR SMR; P68371; 2-427.
DR IntAct; P68371; 37.
DR MINT; MINT-1390314; -.
DR STRING; 9606.ENSP00000341289; -.
DR BindingDB; P68371; -.
DR ChEMBL; CHEMBL2095182; -.
DR PhosphoSite; P68371; -.
DR DMDM; 55977480; -.
DR OGP; P05217; -.
DR REPRODUCTION-2DPAGE; IPI00007752; -.
DR SWISS-2DPAGE; P68371; -.
DR PeptideAtlas; P68371; -.
DR PRIDE; P68371; -.
DR DNASU; 10383; -.
DR Ensembl; ENST00000340384; ENSP00000341289; ENSG00000188229.
DR GeneID; 10383; -.
DR KEGG; hsa:10383; -.
DR UCSC; uc004cmg.1; human.
DR CTD; 10383; -.
DR GeneCards; GC09P140136; -.
DR HGNC; HGNC:20771; TUBB4B.
DR HPA; CAB010880; -.
DR HPA; HPA043640; -.
DR HPA; HPA046280; -.
DR MIM; 602660; gene.
DR neXtProt; NX_P68371; -.
DR PharmGKB; PA142670672; -.
DR HOGENOM; HOG000165710; -.
DR HOVERGEN; HBG000089; -.
DR InParanoid; P68371; -.
DR KO; K07375; -.
DR OMA; DQAYCID; -.
DR OrthoDB; EOG71ZP1H; -.
DR PhylomeDB; P68371; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; TUBB4B; human.
DR GeneWiki; TUBB2C; -.
DR GenomeRNAi; 10383; -.
DR NextBio; 39335; -.
DR PRO; PR:P68371; -.
DR ArrayExpress; P68371; -.
DR Bgee; P68371; -.
DR CleanEx; HS_TUBB2C; -.
DR Genevestigator; P68371; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042288; F:MHC class I protein binding; TAS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0006928; P:cellular component movement; TAS:ProtInc.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; NAS:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR GO; GO:0051225; P:spindle assembly; IEA:Ensembl.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding;
KW Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1 445 Tubulin beta-4B chain.
FT /FTId=PRO_0000048248.
FT NP_BIND 140 146 GTP (Potential).
FT MOD_RES 58 58 N6-acetyllysine.
FT MOD_RES 172 172 Phosphoserine; by CDK1 (Probable).
SQ SEQUENCE 445 AA; 49831 MW; A552C52822AFA072 CRC64;
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGKYV
PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEFEEEA EEEVA
//
MIM
602660
*RECORD*
*FIELD* NO
602660
*FIELD* TI
*602660 TUBULIN, BETA-4B; TUBB4B
;;TUBULIN, BETA-2C; TUBB2C;;
TUBULIN, BETA-2;;
TUBULIN, BETA, CLASS IVB
read more*FIELD* TX
DESCRIPTION
Microtubules are dynamic polymeric structures consisting of heterodimers
of alpha-tubulins (see 602529) and beta-tubulins, such as TUBB4B, that
are continuously incorporated and released. Microtubules function in
mitosis, intracellular transport, neuron morphology, and ciliary and
flagellar motility (Leandro-Garcia et al., 2010).
CLONING
Lewis et al. (1985) cloned the tubulin beta-2 isoform gene. The beta-2
gene is expressed as a 1.8-kb mRNA, and the sequence encodes a predicted
445-amino acid protein. Lewis and Cowan (1990) stated that the mouse
homolog of beta-2, M-beta-3, is expressed abundantly in testis and at
lower levels in many other tissues.
Using database analysis, Leandro-Garcia et al. (2010) identified 8 major
beta-tubulins, including TUBB4B, which they called TUBB2C. Quantitative
RT-PCR showed variable TUBB2C expression in all 21 normal human tissues
examined, with highest expression in heart and testis, and lowest
expression in prostate. TUBB2C was the predominant beta-tubulin isotype
in testis, kidney, heart, skeletal muscle, and lung. Abnormal TUBB2C
expression was detected in several tumors compared with their normal
counterparts.
GENE FAMILY
Lewis and Cowan (1990) reviewed the beta-tubulin gene family. In humans,
this family consists of 15 to 20 dispersed genes, many of which are
processed pseudogenes. The positions of the first 2 introns are
identical among members of the human and chicken gene families. Within a
vertebrate species, the genes are distinguished by their C-terminal
region. The amino acid sequence differences show varying degrees of
conservation across species, depending on the isotype.
MAPPING
Hartz (2013) mapped the TUBB4B gene to chromosome 9q34.3 based on an
alignment of the TUBB4B sequence (GenBank GENBANK BC001911) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 2/28/2013.
2. Leandro-Garcia, L. J.; Leskela, S.; Landa, I.; Montero-Conde, C.;
Lopez-Jimenez, E.; Leton, R.; Cascon, A.; Robledo, M.; Rodriguez-Antona,
C.: Tumoral and tissue-specific expression of the major human beta-tubulin
isotypes. Cytoskeleton 67: 214-223, 2010.
3. Lewis, S. A.; Cowan, N. J.: Tubulin genes: structure, expression,
and regulation.In: Avila, J. (ed.): Microtubule proteins. Boca
Raton: CRC Press, Inc. 1990. Pp. 37-66.
4. Lewis, S. A.; Gilmartin, M. E.; Hall, J. L.; Cowan, N. J.: Three
expressed sequences within the human beta-tubulin multigene family
each define a distinct isotype. J. Molec. Biol. 182: 11-20, 1985.
*FIELD* CN
Patricia A. Hartz - updated: 02/28/2013
*FIELD* CD
Rebekah S. Rasooly: 5/27/1998
*FIELD* ED
mgross: 02/28/2013
alopez: 6/11/2009
psherman: 6/15/1999
alopez: 5/27/1998
*RECORD*
*FIELD* NO
602660
*FIELD* TI
*602660 TUBULIN, BETA-4B; TUBB4B
;;TUBULIN, BETA-2C; TUBB2C;;
TUBULIN, BETA-2;;
TUBULIN, BETA, CLASS IVB
read more*FIELD* TX
DESCRIPTION
Microtubules are dynamic polymeric structures consisting of heterodimers
of alpha-tubulins (see 602529) and beta-tubulins, such as TUBB4B, that
are continuously incorporated and released. Microtubules function in
mitosis, intracellular transport, neuron morphology, and ciliary and
flagellar motility (Leandro-Garcia et al., 2010).
CLONING
Lewis et al. (1985) cloned the tubulin beta-2 isoform gene. The beta-2
gene is expressed as a 1.8-kb mRNA, and the sequence encodes a predicted
445-amino acid protein. Lewis and Cowan (1990) stated that the mouse
homolog of beta-2, M-beta-3, is expressed abundantly in testis and at
lower levels in many other tissues.
Using database analysis, Leandro-Garcia et al. (2010) identified 8 major
beta-tubulins, including TUBB4B, which they called TUBB2C. Quantitative
RT-PCR showed variable TUBB2C expression in all 21 normal human tissues
examined, with highest expression in heart and testis, and lowest
expression in prostate. TUBB2C was the predominant beta-tubulin isotype
in testis, kidney, heart, skeletal muscle, and lung. Abnormal TUBB2C
expression was detected in several tumors compared with their normal
counterparts.
GENE FAMILY
Lewis and Cowan (1990) reviewed the beta-tubulin gene family. In humans,
this family consists of 15 to 20 dispersed genes, many of which are
processed pseudogenes. The positions of the first 2 introns are
identical among members of the human and chicken gene families. Within a
vertebrate species, the genes are distinguished by their C-terminal
region. The amino acid sequence differences show varying degrees of
conservation across species, depending on the isotype.
MAPPING
Hartz (2013) mapped the TUBB4B gene to chromosome 9q34.3 based on an
alignment of the TUBB4B sequence (GenBank GENBANK BC001911) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 2/28/2013.
2. Leandro-Garcia, L. J.; Leskela, S.; Landa, I.; Montero-Conde, C.;
Lopez-Jimenez, E.; Leton, R.; Cascon, A.; Robledo, M.; Rodriguez-Antona,
C.: Tumoral and tissue-specific expression of the major human beta-tubulin
isotypes. Cytoskeleton 67: 214-223, 2010.
3. Lewis, S. A.; Cowan, N. J.: Tubulin genes: structure, expression,
and regulation.In: Avila, J. (ed.): Microtubule proteins. Boca
Raton: CRC Press, Inc. 1990. Pp. 37-66.
4. Lewis, S. A.; Gilmartin, M. E.; Hall, J. L.; Cowan, N. J.: Three
expressed sequences within the human beta-tubulin multigene family
each define a distinct isotype. J. Molec. Biol. 182: 11-20, 1985.
*FIELD* CN
Patricia A. Hartz - updated: 02/28/2013
*FIELD* CD
Rebekah S. Rasooly: 5/27/1998
*FIELD* ED
mgross: 02/28/2013
alopez: 6/11/2009
psherman: 6/15/1999
alopez: 5/27/1998