UniProt Accession

 SEPT2_HUMAN; Q15019; B4DGE8; Q14132; Q53QU3; Q8IUK9; Q96CB0 

Genbank Protein ID

 D63878; D28540; AF038404; AK294563; AC005104; AC104841; BC014455; BC033559 

Genbank Nucleotide ID

 BAA09928.2; BAA05893.1; AAB92377.1; BAG57759.1; AAY14718.1; AAH14455.1; AAH33559.1 

Protein Name

 Septin-2 

Protein Synonyms/Alias

 Neural precursor cell expressed developmentally down-regulated protein 5; NEDD-5 

Gene Name

 SEPT2 

Gene Synonyms/Alias

 DIFF6; KIAA0158; NEDD5 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
38	EASQKMSKQQPTQFI	ubiquitination	[1, 2]
109	VIPGAAEKIERTVQI	ubiquitination	[1]
218	NIVPVIAKADTLTLK	ubiquitination	[1, 3]
225	KADTLTLKERERLKK	ubiquitination	[1]
267	KEQTRLLKASIPFSV	ubiquitination	[1, 2, 3]
284	SNQLIEAKGKKVRGR	ubiquitination	[1, 2]
286	QLIEAKGKKVRGRLY	ubiquitination	[1]
287	LIEAKGKKVRGRLYP	ubiquitination	[1]
310	PEHNDFLKLRTMLIT	ubiquitination	[1, 2]
345	RLKRGGRKVENEDMN	ubiquitination	[1, 3]
353	VENEDMNKDQILLEK	ubiquitination	[1, 3]
360	KDQILLEKEAELRRM	ubiquitination	[2, 4]

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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] 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] 

Functional Description

 Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements. In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri. 

Sequence Annotation

 NP_BIND 44 51 GTP.
 NP_BIND 183 191 GTP.
 REGION 260 270 Important for dimerization.
 BINDING 78 78 GTP (By similarity).
 BINDING 104 104 GTP; via amide nitrogen (By similarity).
 BINDING 241 241 GTP; via amide nitrogen and carbonyl
 BINDING 256 256 GTP.
 MOD_RES 190 190 N6-acetyllysine.
 MOD_RES 218 218 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division; Cell membrane; Cell projection; Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; Kinetochore; Membrane; Mitosis; Nucleotide-binding; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 361 AA 

Protein Sequence

Gene Ontology

 GO:0015629; C:actin cytoskeleton; IDA:HPA.
 GO:0009986; C:cell surface; IEA:Compara.
 GO:0060170; C:cilium membrane; ISS:UniProtKB.
 GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0000145; C:exocyst; IEA:Compara.
 GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0031105; C:septin complex; IEA:InterPro.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0045202; C:synapse; IEA:Compara.
 GO:0030234; F:enzyme regulator activity; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0042384; P:cilium assembly; ISS:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0031175; P:neuron projection development; IEA:Compara.
 GO:0002036; P:regulation of L-glutamate transport; IEA:Compara.
 GO:0032880; P:regulation of protein localization; IEA:Compara.
 GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB. 

Interpro

 IPR000038; Cell_div_GTP-bd.
 IPR027417; P-loop_NTPase.
 IPR016491; Septin.
 IPR008113; Septin2. 

Pfam

 PF00735; Septin 

SMART

  

PROSITE

  

PRINTS

 PR01740; SEPTIN2.