ID TBB4$CHICK STANDARD; PRT; 449 AA. AC P09652; DT 01-MAR-1989 (REL. 10, CREATED) DT 01-MAR-1989 (REL. 10, LAST SEQUENCE UPDATE) DT 01-FEB-1991 (REL. 17, LAST ANNOTATION UPDATE) DE TUBULIN BETA-4 CHAIN (CLASS-III). OS GALLUS GALLUS (CHICKEN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; AVES; NEOGNATHAE; OC GALLIFORMES. RN [1] RP SEQUENCE FROM N.A. RC MEDLINE=85030582; RA SULLIVAN K.F., CLEVELAND D.W.; RL J. CELL BIOL. 99:1754-1760(1984). RN [2] RP PHOSPHORYLATION. RC MEDLINE=88167174; RA LUDUENA R.F., ZIMMERMANN H.-P., LITTLE M.; RL FEBS LETT. 230:142-146(1988). 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 NONEXCHANGEABLE SITE ON THE ALPHA-CHAIN. CC -!- SUBUNIT: DIMER OF ALPHA AND BETA CHAINS. CC -!- TISSUE SPECIFICITY: NEURON-SPECIFIC. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M15052; GGTUB4B. DR PIR; A29161; A29161. DR PROSITE; PS00227; TUBULIN. DR PROSITE; PS00228; TUBULIN_B_AUTOREG. KW MICROTUBULES; GTP-BINDING; MULTIGENE FAMILY; PHOSPHORYLATION. FT NP_BIND 140 146 GTP (PUTATIVE). FT MOD_RES 444 444 PHOSPHORYLATION. SQ SEQUENCE 449 AA; 50420 MW; 1029538 CN; 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 APLTRRGSQQ YRALTVPELT QQMFDAKNMM AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEMYEDD EEESEQGAK //