CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024676
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Septin-11 
Protein Synonyms/Alias
  
Gene Name
 Sept11 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
175TMKKLDSKVNIIPIIubiquitination[1]
190AKADTIAKNELHKFKacetylation[2]
195IAKNELHKFKSKIMSacetylation[2]
315KDTDPDSKPFSLQETacetylation[2]
315KDTDPDSKPFSLQETubiquitination[1]
336EFLGELQKKEEEMRQubiquitination[1]
357KEKEAELKEAEKELHacetylation[2]
361AELKEAEKELHEKFDacetylation[2]
366AEKELHEKFDLLKRTacetylation[2]
371HEKFDLLKRTHQEEKacetylation[2]
386KKVEDKKKELEEEVSubiquitination[1]
397EEVSNFQKKKAAAQLacetylation[2]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity. 
Sequence Annotation
 NP_BIND 48 55 GTP (By similarity).
 NP_BIND 184 192 GTP (By similarity).
 BINDING 103 103 GTP; via amide nitrogen (By similarity).
 BINDING 238 238 GTP; via amide nitrogen and carbonyl
 BINDING 253 253 GTP (By similarity).
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 Acetylation; Alternative splicing; Cell cycle; Cell division; Cell junction; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; Nucleotide-binding; Reference proteome; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 431 AA 
Protein Sequence
MAVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET GIGKSTLMDT 60
LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD TVGFGDQINK DDSYKPIVEY 120
IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP 180
IIAKADTIAK NELHKFKSKI MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST 240
EEVKIGNKMA KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC 300
KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK EKEAELKEAE 360
KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVSNFQKKKA AAQLLQSQAQ QSGAQQTKKD 420
KDKKNPWLCT E 431 
Gene Ontology
 GO:0030424; C:axon; IEA:UniProtKB-SubCell.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
 GO:0031105; C:septin complex; IEA:InterPro.
 GO:0001725; C:stress fiber; IEA:Compara.
 GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0051291; P:protein heterooligomerization; IEA:Compara. 
Interpro
 IPR000038; Cell_div_GTP-bd.
 IPR027417; P-loop_NTPase.
 IPR016491; Septin. 
Pfam
 PF00735; Septin 
SMART
  
PROSITE
  
PRINTS