ID TBB2_ANEPH Reviewed; 411 AA. AC P33631; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 29-MAY-2024, entry version 90. DE RecName: Full=Tubulin beta-2 chain; DE AltName: Full=Beta-2-tubulin; DE Flags: Fragment; GN Name=TUBB2; OS Anemia phyllitidis (Fern) (Osmunda phyllitidis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Polypodiopsida; Polypodiidae; Schizaeales; Anemiaceae; Anemia. OX NCBI_TaxID=12940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Moepps B., Maucher H.P., Bogenberger J.M., Schraudolf H.; RT "Characterization of the alpha and beta tubulin gene families from Anemia RT phyllitidis L.Sw."; RL Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder CC consisting of laterally associated linear protofilaments composed of CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to CC GTPase activity of alpha-tubulin. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a CC hollow water-filled tube with an outer diameter of 25 nm and an inner CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to CC form protofilaments running lengthwise along the microtubule wall with CC the beta-tubulin subunit facing the microtubule plus end conferring a CC structural polarity. Microtubules usually have 13 protofilaments but CC different protofilament numbers can be found in some organisms and CC specialized cells. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}. 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; X69186; CAA48930.1; -; mRNA. DR PIR; S32669; S32669. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:TreeGrafter. DR GO; GO:0000278; P:mitotic cell cycle; IEA:TreeGrafter. DR CDD; cd02187; beta_tubulin; 1. DR Gene3D; 1.10.287.600; Helix hairpin bin; 1. DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1. DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1. DR InterPro; IPR002453; Beta_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR037103; Tubulin/FtsZ-like_C. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf. DR InterPro; IPR023123; Tubulin_C. DR InterPro; IPR017975; Tubulin_CS. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR PANTHER; PTHR11588; TUBULIN; 1. DR PANTHER; PTHR11588:SF429; TUBULIN BETA-1 CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1. DR PROSITE; PS00227; TUBULIN; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Cytoskeleton; GTP-binding; Magnesium; Metal-binding; KW Microtubule; Nucleotide-binding. FT CHAIN <1..411 FT /note="Tubulin beta-2 chain" FT /id="PRO_0000048330" FT REGION 390..411 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 37 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 37 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 106 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 110 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 111 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 112 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 172 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 194 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT NON_TER 1 SQ SEQUENCE 411 AA; 46218 MW; C66DC6A067F3A9A3 CRC64; TGTYRGDSET QLERVNVYYN EASCGRYVPR AVLMDLEPGT MDSVRSGPYG QIFRPDNFVF GQSGAGNNWA KGHYTEGAEL IDSVLDVVRK EAENCDCLQG FQVCHSLGGG TGSGMGTLLI SKIREEYPDR MMXTFSVFPS PKVSDTVVEP YNATLSVHQL VENADECMVL DNEALYDICF RTLKLVTPTF GDLNHLISAT MSGVTCCLRF PGQLNSDLRK LAVNLIPFPR LHFFMVGFAP LTSRGSQQYR ALTVPELTQQ MRDAKNMMCA ADPRHGRYLT ASAMFRGKMS TKEVDEQMIN VQNKNSSYFV EWIPNNVKSS VCDIPPVGLK MACTFIGNST SIQEMFRRVR DQFTAMFRXK AFLHWYTGEG MDEMEFTEAE SNMNDLVSEY QQYQDATAEP EGXYEEDYDE A //