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; ARCHOSAURIA; AVES; OC NEOGNATHAE; GALLIFORMES; PHASIANIDAE; PHASIANINAE; GALLUS. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 85030582. RA SULLIVAN K.F., CLEVELAND D.W.; RT "Sequence of a highly divergent beta tubulin gene reveals regional RT heterogeneity in the beta tubulin polypeptide."; RL J. CELL BIOL. 99:1754-1760(1984). RN [2] RP PHOSPHORYLATION. RX MEDLINE; 88167174. RA LUDUENA R.F., ZIMMERMANN H.-P., LITTLE M.; RT "Identification of the phosphorylated beta-tubulin isotype in RT differentiated neuroblastoma cells."; 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 This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; G212832; -. DR PIR; A29161; A29161. DR PROSITE; PS00227; TUBULIN; 1. DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1. DR PFAM; PF00091; tubulin; 1. KW MICROTUBULES; GTP-BINDING; MULTIGENE FAMILY; PHOSPHORYLATION. FT NP_BIND 140 146 GTP (POTENTIAL). FT MOD_RES 444 444 PHOSPHORYLATION. SQ SEQUENCE 449 AA; 50420 MW; 916A918E CRC32; 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 //