ID   TBB3_HUMAN              Reviewed;         450 AA.
AC   Q13509; Q9BTZ0; Q9BW10;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   13-OCT-2009, entry version 90.
DE   RecName: Full=Tubulin beta-3 chain;
DE   AltName: Full=Tubulin beta-III;
DE   AltName: Full=Tubulin beta-4;
GN   Name=TUBB3; Synonyms=TUBB4;
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 [MRNA].
RX   MEDLINE=98146276; PubMed=9473684; DOI=10.1016/S0167-4781(97)00168-1;
RA   Ranganathan S., Dexter D.W., Benetatos C.A., Hudes G.R.;
RT   "Cloning and sequencing of human betaIII-tubulin cDNA: induction of
RT   betaIII isotype in human prostate carcinoma cells by acute exposure to
RT   antimicrotubule agents.";
RL   Biochim. Biophys. Acta 1395:237-245(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary cancer;
RA   Banerjee A.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   PROTEIN SEQUENCE OF 63-77; 104-121; 242-251; 163-174 AND 381-390, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [5]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [6]
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   [7]
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., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
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.
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.
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DR   EMBL; U47634; AAC52035.1; -; mRNA.
DR   EMBL; AF427491; AAL28094.1; -; mRNA.
DR   EMBL; BC000748; AAH00748.1; -; mRNA.
DR   EMBL; BC003021; AAH03021.2; -; mRNA.
DR   IPI; IPI00013683; -.
DR   RefSeq; NP_006077.2; -.
DR   UniGene; Hs.511743; -.
DR   HSSP; P02554; 1FFX.
DR   SMR; Q13509; 2-427.
DR   IntAct; Q13509; 4.
DR   STRING; Q13509; -.
DR   PhosphoSite; Q13509; -.
DR   OGP; Q13509; -.
DR   PRIDE; Q13509; -.
DR   Ensembl; ENST00000304984; ENSP00000302777; ENSG00000198211; Homo sapiens.
DR   Ensembl; ENST00000315491; ENSP00000320295; ENSG00000198211; Homo sapiens.
DR   GeneID; 10381; -.
DR   KEGG; hsa:10381; -.
DR   UCSC; uc002fph.1; human.
DR   CTD; 10381; -.
DR   GeneCards; GC16P088514; -.
DR   HGNC; HGNC:20772; TUBB3.
DR   HPA; CAB011512; -.
DR   MIM; 602661; gene.
DR   PharmGKB; PA134953867; -.
DR   HOVERGEN; Q13509; -.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   NextBio; 39327; -.
DR   ArrayExpress; Q13509; -.
DR   Bgee; Q13509; -.
DR   CleanEx; HS_TUBB3; -.
DR   CleanEx; HS_TUBB4; -.
DR   Genevestigator; Q13509; -.
DR   GermOnline; ENSG00000198211; Homo sapiens.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588:SF9; Beta_tubulin; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Direct protein sequencing;
KW   GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN         1    450       Tubulin beta-3 chain.
FT                                /FTId=PRO_0000048250.
FT   NP_BIND     140    146       GTP (Potential).
FT   MOD_RES      58     58       N6-acetyllysine.
FT   CONFLICT    275    275       A -> R (in Ref. 1; AAC52035).
SQ   SEQUENCE   450 AA;  50433 MW;  4B9CDE7DBA102949 CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV
     PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKECENCDCL QGFQLTHSLG GGTGSGMGTL LISKVREEYP DRIMNTFSVV PSPKVSDTVV
     EPYNATLSIH QLVENTDETY CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM
     AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG
     LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEMYEDD EEESEAQGPK
//