CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012252
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Septin-6 
Protein Synonyms/Alias
  
Gene Name
 SEPT6 
Gene Synonyms/Alias
 KIAA0128; SEP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
66MDTLFNTKFEGEPATubiquitination[1]
185NIIPIIAKADAISKSubiquitination[1]
191AKADAISKSELTKFKubiquitination[1]
196ISKSELTKFKIKITSacetylation[2]
196ISKSELTKFKIKITSubiquitination[1]
249EELKIGNKMMRARQYubiquitination[1]
273EAHCDFVKLREMLIRubiquitination[1]
316KDTDPDSKPFSLQETubiquitination[3]
327LQETYEAKRNEFLGEubiquitination[3, 4]
362AELKEAEKELHEKFDubiquitination[1]
367AEKELHEKFDRLKKLacetylation[2]
367AEKELHEKFDRLKKLubiquitination[1]
386KKKLEDKKKSLDDEVubiquitination[1]
387KKLEDKKKSLDDEVNubiquitination[1]
397DDEVNAFKQRKTAAEubiquitination[1]
400VNAFKQRKTAAELLQubiquitination[1]
420AGGSQTLKRDKEKKNubiquitination[1, 3, 5]
426LKRDKEKKNNPWLCTubiquitination[3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis. May play a role in HCV RNA replication. 
Sequence Annotation
 NP_BIND 49 56 GTP.
 NP_BIND 185 193 GTP.
 BINDING 104 104 GTP; via amide nitrogen (By similarity).
 BINDING 239 239 GTP; via amide nitrogen and carbonyl
 BINDING 254 254 GTP (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 367 367 N6-acetyllysine.
 MOD_RES 416 416 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; Host-virus interaction; Kinetochore; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 434 AA 
Protein Sequence
MAATDIARQV GEGCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE TGLGKSTLMD 60
TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVRLKLTIV STVGFGDQIN KEDSYKPIVE 120
FIDAQFEAYL QEELKIRRVL HTYHDSRIHV CLYFIAPTGH SLKSLDLVTM KKLDSKVNII 180
PIIAKADAIS KSELTKFKIK ITSELVSNGV QIYQFPTDDE SVAEINGTMN AHLPFAVIGS 240
TEELKIGNKM MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HTRHYELYRR 300
CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV KEKEAELKEA 360
EKELHEKFDR LKKLHQDEKK KLEDKKKSLD DEVNAFKQRK TAAELLQSQG SQAGGSQTLK 420
RDKEKKNNPW LCTE 434 
Gene Ontology
 GO:0043679; C:axon terminus; IEA:Compara.
 GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
 GO:0031105; C:septin complex; IEA:InterPro.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0008021; C:synaptic vesicle; IEA:Compara.
 GO:0005525; F:GTP binding; TAS:UniProtKB.
 GO:0000910; P:cytokinesis; TAS:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR000038; Cell_div_GTP-bd.
 IPR027417; P-loop_NTPase.
 IPR016491; Septin. 
Pfam
 PF00735; Septin 
SMART
  
PROSITE
  
PRINTS