Tag | Content |
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CPLM ID | CPLM-028392 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Beta-Tubulin at 56D, isoform A |
Protein Synonyms/Alias | FI19422p1 |
Gene Name | betaTub56D |
Gene Synonyms/Alias | betaTub56D-RA; CG9277; Dmel_CG9277 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
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67 | YNEASGGKYVPRAVL | acetylation | [1] |
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Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). |
Sequence Annotation | |
Keyword | Complete proteome; GTP-binding; Microtubule; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 456 AA |
Protein Sequence | MLIGARPIHR VYDGVHGWPK PRSRAQTCFW EIISDEHGID ATGAYHGDSD LQLERINVYY 60 NEASGGKYVP RAVLVDLEPG TMDSVRSGPF GQIFRPDNFV FGQSGAGNNW AKGHYTEGAE 120 LVDSVLDVVR KEAESCDCLQ GFQLTHSLGG GTGSGMGTLL ISKIREEYPD RIMNTYSVVP 180 SPKVSDTVVE PYNATLSVHQ LVENTDETYC IDNEALYDIC FRTLKLTTPT YGDLNHLVSL 240 TMSGVTTCLR FPGQLNADLR KLAVNMVPFP RLHFFMPGFA PLTSRGSQQY RALTVPELTQ 300 QMFDAKNMMA ACDPRHGRYL TVAAIFRGRM SMKEVDEQML NIQNKNSSYF VEWIPNNVKT 360 AVCDIPPRGL KMSATFIGNS TAIQELFKRI SEQFTAMFRR KAFLHWYTGE GMDEMEFTEA 420 ESNMNDLVSE YQQYQEATAD EDAEFEEEQE AEVDEN 456 |
Gene Ontology | GO:0005874; C:microtubule; IEA:UniProtKB-KW. GO:0005525; F:GTP binding; IEA:UniProtKB-KW. GO:0003924; F:GTPase activity; IEA:InterPro. GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro. GO:0007017; P:microtubule-based process; IEA:InterPro. GO:0051258; P:protein polymerization; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |