| Tag | Content |
|---|
| CPLM ID | CPLM-004241 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Tubulin alpha chain |
Protein Synonyms/Alias | |
Gene Name | |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Plasmodium falciparum (isolate K1 / Thailand) |
NCBI Taxa ID | 5839 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 40 | DGQMPSDKASRANDD | acetylation | [1] |
|
Reference | [1] Microtubular organization visualized by immunofluorescence microscopy during erythrocytic schizogony in Plasmodium falciparum and investigation of post-translational modifications of parasite tubulin. Read M, Sherwin T, Holloway SP, Gull K, Hyde JE. Parasitology. 1993 Apr;106 ( Pt 3):223-32. [ PMID: 8488059] |
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. |
Sequence Annotation | NP_BIND 142 148 GTP (Potential).
MOD_RES 40 40 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 453 AA |
Protein Sequence | MREVISIHVG QAGIQVGNAC WELFCLEHGI QPDGQMPSDK ASRANDDAFN TFFSETGAGK 60
HVPRCVFVDL EPTVVDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEVIDVCLD 120
RIRKLADNCT GLQGFLMFSA VGGGTGSGFG CLMLERLSVD YGKKSKLNFC CWPSPQVSTA 180
VVEPYNSVLS THSLLEHTDV AIMLDNEAIY DICRRNLDIE RPTYTNLNRL IAQVISSLTA 240
SLRFDGALNV DVTEFQTNLV PYPRIHFMLS SYAPVVSAEK AYHEQLSVSE ITNSAFEPAN 300
MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP 360
TVVPGGDLAK VMRAVCMISN STAIAEVFSR MDQKFDLMYA KRAFVHWYVG EGMEEGEFSE 420
AREDLAALEK DYEEVGIESN EAEGEDEGYE ADY 453 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 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 | |