dbPTM

SEPT2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SEPT2_MOUSE
UniProt AC	P42208
Protein Name	Septin-2
Gene Name	2-Sep
Organism	Mus musculus (Mouse).
Sequence Length	361
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Cleavage furrow. Midbody. Cytoplasm, cell cortex. Cell projection, cilium membrane. Cell projection, cilium, flagellum . In metaphase cells, lo
Protein Description	Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity). 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 (By similarity). 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..
Protein Sequence	MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERIIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHSIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDSDSGALGQHV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSKQQPTQF ------CCCCCCCCC	38.89	29514104
3	Ubiquitination	-----MSKQQPTQFI -----CCCCCCCCCC	52.21	22790023
7	Phosphorylation	-MSKQQPTQFINPET -CCCCCCCCCCCCCC	31.60	22499769
14	Phosphorylation	TQFINPETPGYVGFA CCCCCCCCCCCCCCC	24.22	22499769
17	Phosphorylation	INPETPGYVGFANLP CCCCCCCCCCCCCCC	9.90	25338131
31	Phosphorylation	PNQVHRKSVKKGFEF CCCHHHHHCCCCCEE	38.84	-
74	Ubiquitination	IIPGAAEKIERTVQI CCCCHHHHHEEEEEE	45.18	22790023
120	Phosphorylation	DCFKTIISYIDEQFE HHHHHHHHHHHHHHH	16.52	-
183	Acetylation	NIVPVIAKADTLTLK CCHHEEEECCCCCHH	35.35	22826441
183	Ubiquitination	NIVPVIAKADTLTLK CCHHEEEECCCCCHH	35.35	22790023
190	Acetylation	KADTLTLKERERLKK ECCCCCHHHHHHHHH	49.87	-
207	Phosphorylation	LDEIEEHSIKIYHLP HHHHHHCCEEEEECC	28.93	28638064
211	Phosphorylation	EEHSIKIYHLPDAES HHCCEEEEECCCCCC	7.72	25619855
218	Phosphorylation	YHLPDAESDEDEDFK EECCCCCCCCCCCHH	48.28	24925903
225	Ubiquitination	SDEDEDFKEQTRLLK CCCCCCHHHHHHHHH	62.32	22790023
228	Phosphorylation	DEDFKEQTRLLKASI CCCHHHHHHHHHHCC	25.11	25619855
232	Ubiquitination	KEQTRLLKASIPFSV HHHHHHHHHCCCEEE	44.68	22790023
249	Ubiquitination	SNQLIEAKGKKVRGR CCHHEEECCCEECCE	59.48	22790023
318	Ubiquitination	VENEDMNKDQILLEK CCCCCCCHHHHHHHH	44.35	22790023
325	Ubiquitination	KDQILLEKEAELRRM HHHHHHHHHHHHHHH	63.29	22790023
352	Phosphorylation	MQMQGGDSDSGALGQ HHHCCCCCCCCCCCC	36.63	24899341
354	Phosphorylation	MQGGDSDSGALGQHV HCCCCCCCCCCCCCC	29.89	26643407

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of SEPT2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SEPT2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SEPT2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SEPT7_MOUSE	Sept7	physical	11739749
SEPT5_MOUSE	Sept5	physical	11739749
SEPT4_MOUSE	Sept4	physical	14723703
SEPT7_HUMAN	SEPT7	physical	26496610
METK2_HUMAN	MAT2A	physical	26496610
SEPT9_HUMAN	SEPT9	physical	26496610
SEPT6_HUMAN	SEPT6	physical	26496610
SEPT8_HUMAN	SEPT8	physical	26496610
BORG4_HUMAN	CDC42EP4	physical	26496610
SDF2L_HUMAN	SDF2L1	physical	26496610
DJB11_HUMAN	DNAJB11	physical	26496610
SEP11_HUMAN	SEPT11	physical	26496610
EVI5L_HUMAN	EVI5L	physical	26496610
SEP10_HUMAN	SEPT10	physical	26496610

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SEPT2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	17203969 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	16452087 [Abstract]