SEPT2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SEPT2_RAT
• UniProt AC: Q91Y81
• Protein Name: Septin-2
• Gene Name: 2-Sep
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 361
• Subcellular Localization: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Cleavage furrow. Midbody. Cytoplasm, cell cortex. Cell projection, cilium membrane. Cell projection, cilium, flagellum . In metaphase cells, localized within the microtubule spindl
• 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. 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 (By similarity)..
• Protein Sequence: MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERIIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINSRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHSIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDTDSSTLGHHV

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	TQFINPETPGYVGFA CCCCCCCCCCCCCCC	24.22	22108457
17	Phosphorylation	INPETPGYVGFANLP CCCCCCCCCCCCCCC	9.90	22276854
190	Acetylation	KADTLTLKERERLKK ECCCCCHHHHHHHHH	49.87	22902405
207	Phosphorylation	LDEIEEHSIKIYHLP HHHHHHCCEEEEECC	28.93	25575281
211	Phosphorylation	EEHSIKIYHLPDAES HHCCEEEEECCCCCC	7.72	25403869
218	Phosphorylation	YHLPDAESDEDEDFK EECCCCCCCCCCCHH	48.28	19700791
228	Phosphorylation	DEDFKEQTRLLKASI CCCHHHHHHHHHHCC	25.11	16641100
232	Acetylation	KEQTRLLKASIPFSV HHHHHHHHHCCCEEE	44.68	22902405

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

Oops, there are no upstream regulatory protein records of SEPT2_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SEPT2_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SEPT2_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of SEPT2_RAT !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites.";
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND THR-228, ANDMASS SPECTROMETRY.
PubMed: 16641100