dbPTM

SEPT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SEPT2_HUMAN
UniProt AC	Q15019
Protein Name	Septin-2
Gene Name	2-Sep
Organism	Homo sapiens (Human).
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 ce
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. [PubMed: 25588830 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.]
Protein Sequence	MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDGDGGALGHHV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSKQQPTQF ------CCCCCCCCC	38.89	28857561
3	Ubiquitination	-----MSKQQPTQFI -----CCCCCCCCCC	52.21	-
3	Acetylation	-----MSKQQPTQFI -----CCCCCCCCCC	52.21	25953088
7	Phosphorylation	-MSKQQPTQFINPET -CCCCCCCCCCCCCC	31.60	21945579
14	Phosphorylation	TQFINPETPGYVGFA CCCCCCCCCCCCCCC	24.22	21945579
17	Phosphorylation	INPETPGYVGFANLP CCCCCCCCCCCCCCC	9.90	21945579
31	Phosphorylation	PNQVHRKSVKKGFEF CCCHHHHHCCCCCEE	38.84	24719451
38 (in isoform 2)	Ubiquitination	-	6.25	21890473
52 (in isoform 2)	Phosphorylation	-	34.83	27642862
74	Ubiquitination	VIPGAAEKIERTVQI CCCCHHHHHEEEEEE	45.18	-
74	Acetylation	VIPGAAEKIERTVQI CCCCHHHHHEEEEEE	45.18	25953088
78	Phosphorylation	AAEKIERTVQIEAST HHHHHEEEEEEEEEE	12.17	-
96	Methylation	EERGVKLRLTVVDTP HHCCEEEEEEEECCC	23.69	115916449
102	Phosphorylation	LRLTVVDTPGYGDAI EEEEEECCCCCCCCC	13.65	28152594
105	Phosphorylation	TVVDTPGYGDAINCR EEECCCCCCCCCCCH	17.03	28152594
109 (in isoform 2)	Ubiquitination	-	6.26	-
111	S-nitrosylation	GYGDAINCRDCFKTI CCCCCCCCHHHHHHH	2.95	2212679
116	Ubiquitination	INCRDCFKTIISYID CCCHHHHHHHHHHHH	45.18	-
120	Phosphorylation	DCFKTIISYIDEQFE HHHHHHHHHHHHHHH	16.52	22199227
129	Phosphorylation	IDEQFERYLHDESGL HHHHHHHHHHCCCCC	10.94	28152594
129	Nitration	IDEQFERYLHDESGL HHHHHHHHHHCCCCC	10.94	-
134	Phosphorylation	ERYLHDESGLNRRHI HHHHHCCCCCCHHHH	55.42	20044836
161	Acetylation	SPFGHGLKPLDVAFM CCCCCCCCHHHHHHH	48.39	26051181
174	Ubiquitination	FMKAIHNKVNIVPVI HHHHHHCCCCCHHEE	23.61	-
174	Malonylation	FMKAIHNKVNIVPVI HHHHHHCCCCCHHEE	23.61	26320211
183	Ubiquitination	NIVPVIAKADTLTLK CCHHEEEECCCCCHH	35.35	21906983
190	Ubiquitination	KADTLTLKERERLKK ECCCCCHHHHHHHHH	49.87	19608861
190	Acetylation	KADTLTLKERERLKK ECCCCCHHHHHHHHH	49.87	19608861
190	Malonylation	KADTLTLKERERLKK ECCCCCHHHHHHHHH	49.87	26320211
200	Ubiquitination	ERLKKRILDEIEEHN HHHHHHHHHHHHHCC	5.85	19608861
200	Acetylation	ERLKKRILDEIEEHN HHHHHHHHHHHHHCC	5.85	19608861
209	Ubiquitination	EIEEHNIKIYHLPDA HHHHCCCEEEECCCC	42.39	-
211	Phosphorylation	EEHNIKIYHLPDAES HHCCCEEEECCCCCC	7.72	22167270
218 (in isoform 2)	Ubiquitination	-	48.28	-
218	Phosphorylation	YHLPDAESDEDEDFK EECCCCCCCCCCCHH	48.28	29255136
225 (in isoform 2)	Ubiquitination	-	62.32	-
225	Acetylation	SDEDEDFKEQTRLLK CCCCCCHHHHHHHHH	62.32	19608861
225	Ubiquitination	SDEDEDFKEQTRLLK CCCCCCHHHHHHHHH	62.32	19608861
228	Phosphorylation	DEDFKEQTRLLKASI CCCHHHHHHHHHHCC	25.11	22167270
232 (in isoform 1)	Ubiquitination	-	44.68	21890473
232	Ubiquitination	KEQTRLLKASIPFSV HHHHHHHHHCCCEEE	44.68	21906983
232	Acetylation	KEQTRLLKASIPFSV HHHHHHHHHCCCEEE	44.68	25953088
234	Phosphorylation	QTRLLKASIPFSVVG HHHHHHHCCCEEEEC	29.25	27251275
238	Phosphorylation	LKASIPFSVVGSNQL HHHCCCEEEECCCHH	15.56	27251275
249 (in isoform 1)	Ubiquitination	-	59.48	21890473
249	Malonylation	SNQLIEAKGKKVRGR CCHHEEECCCEECCE	59.48	26320211
249	Acetylation	SNQLIEAKGKKVRGR CCHHEEECCCEECCE	59.48	25953088
249	Ubiquitination	SNQLIEAKGKKVRGR CCHHEEECCCEECCE	59.48	-
267 (in isoform 2)	Ubiquitination	-	53.05	21890473
275 (in isoform 1)	Ubiquitination	-	35.60	21890473
275	Ubiquitination	PEHNDFLKLRTMLIT CCCCCHHHHHHHHHH	35.60	-
284 (in isoform 2)	Ubiquitination	-	2.19	21890473
286 (in isoform 2)	Ubiquitination	-	42.62	-
287 (in isoform 2)	Ubiquitination	-	2.35	-
291	Phosphorylation	MQDLQEVTQDLHYEN HHHHHHHHHHHCHHH	18.66	27251275
296	Phosphorylation	EVTQDLHYENFRSER HHHHHHCHHHHHHHH	21.62	18083107
310	Acetylation	RLKRGGRKVENEDMN HHHHCCCCCCCCCCC	58.12	26051181
310 (in isoform 2)	Ubiquitination	-	58.12	21890473
310	Ubiquitination	RLKRGGRKVENEDMN HHHHCCCCCCCCCCC	58.12	21906983
318	Malonylation	VENEDMNKDQILLEK CCCCCCCHHHHHHHH	44.35	26320211
318	Acetylation	VENEDMNKDQILLEK CCCCCCCHHHHHHHH	44.35	26051181
318	Ubiquitination	VENEDMNKDQILLEK CCCCCCCHHHHHHHH	44.35	-
325 (in isoform 1)	Ubiquitination	-	63.29	21890473
325	Acetylation	KDQILLEKEAELRRM HHHHHHHHHHHHHHH	63.29	26051181
325	Ubiquitination	KDQILLEKEAELRRM HHHHHHHHHHHHHHH	63.29	21906983
331 (in isoform 2)	Phosphorylation	-	43.70	27642862
339	Sulfoxidation	MQEMIARMQAQMQMQ HHHHHHHHHHHHHHH	2.60	30846556
343	Sulfoxidation	IARMQAQMQMQMQGG HHHHHHHHHHHHCCC	3.92	30846556
345	Sulfoxidation	RMQAQMQMQMQGGDG HHHHHHHHHHCCCCC	2.77	30846556
345 (in isoform 2)	Ubiquitination	-	2.77	-
347	Sulfoxidation	QAQMQMQMQGGDGDG HHHHHHHHCCCCCCC	3.16	30846556
353 (in isoform 2)	Ubiquitination	-	58.03	-
360 (in isoform 2)	Ubiquitination	-	25.78	21890473

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
218	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
218	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SEPT2_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DAZP2_HUMAN	DAZAP2	physical	16189514
SEPT6_HUMAN	SEPT6	physical	16189514
SEPT7_HUMAN	SEPT7	physical	17353931
SYUA_HUMAN	SNCA	physical	12695511
SEPT9_HUMAN	SEPT9	physical	12388755
SEPT6_HUMAN	SEPT6	physical	12388755
SEPT7_HUMAN	SEPT7	physical	12388755
ISG15_HUMAN	ISG15	physical	18305167
COG4_HUMAN	COG4	physical	21900206
JUPI2_HUMAN	HN1L	physical	21900206
MTOR_HUMAN	MTOR	physical	21900206
STMN1_HUMAN	STMN1	physical	21900206
SRRM2_HUMAN	SRRM2	physical	22939629
SMCA5_HUMAN	SMARCA5	physical	22939629
TRA2A_HUMAN	TRA2A	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
SRS10_HUMAN	SRSF10	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
SRSF7_HUMAN	SRSF7	physical	22939629
TRI55_HUMAN	TRIM55	physical	22939629
TRA2B_HUMAN	TRA2B	physical	22939629
UT14A_HUMAN	UTP14A	physical	22939629
ZN326_HUMAN	ZNF326	physical	22939629
SON_HUMAN	SON	physical	22939629
ZCH18_HUMAN	ZC3H18	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
TF3C1_HUMAN	GTF3C1	physical	22939629
VASN_HUMAN	VASN	physical	22939629
TPBG_HUMAN	TPBG	physical	22939629
SURF4_HUMAN	SURF4	physical	22939629
TPR_HUMAN	TPR	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
SEPT7_HUMAN	SEPT7	physical	22863883
SEP11_HUMAN	SEPT11	physical	22863883
COPA_HUMAN	COPA	physical	22863883
DDB2_HUMAN	DDB2	physical	22863883
SEPT5_HUMAN	SEPT5	physical	25416956
SEPT6_HUMAN	SEPT6	physical	25416956
PKHF2_HUMAN	PLEKHF2	physical	25416956
BRE1B_HUMAN	RNF40	physical	26344197
SEP10_HUMAN	SEPT10	physical	26344197
SEP11_HUMAN	SEPT11	physical	26344197
SEPT5_HUMAN	SEPT5	physical	26344197
SEPT6_HUMAN	SEPT6	physical	26344197
SEPT7_HUMAN	SEPT7	physical	26344197
SEPT8_HUMAN	SEPT8	physical	26344197
SEPT9_HUMAN	SEPT9	physical	26344197
SEPT3_HUMAN	SEPT3	physical	28514442
SEPT6_HUMAN	SEPT6	physical	28514442
SEPT7_HUMAN	SEPT7	physical	28514442
SEP10_HUMAN	SEPT10	physical	28514442
SEPT5_HUMAN	SEPT5	physical	28514442
SEPT8_HUMAN	SEPT8	physical	28514442
SEPT9_HUMAN	SEPT9	physical	28514442
SEP11_HUMAN	SEPT11	physical	28514442
SEPT4_HUMAN	SEPT4	physical	28514442
TPM2_HUMAN	TPM2	physical	28514442

Drug and Disease Associations

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

Regulatory Network of SEPT2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-190, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	19369195 [Abstract]
"The phosphorylation of SEPT2 on Ser218 by casein kinase 2 isimportant to hepatoma carcinoma cell proliferation."; Yu W., Ding X., Chen F., Liu M., Shen S., Gu X., Yu L.; Mol. Cell. Biochem. 325:61-67(2009). Cited for: PHOSPHORYLATION AT SER-218, MUTAGENESIS OF SER-218, AND TISSUESPECIFICITY.	19165576 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	18318008 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	17487921 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	16565220 [Abstract]
"Phosphoproteomic analysis of the human pituitary."; Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; Pituitary 9:109-120(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	16807684 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Septin 2 phosphorylation: theoretical and mass spectrometric evidencefor the existence of a single phosphorylation site in vivo."; She Y.M., Huang Y.W., Zhang L., Trimble W.S.; Rapid Commun. Mass Spectrom. 18:1123-1130(2004). Cited for: PHOSPHORYLATION AT SER-218.	15150837 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17, AND MASSSPECTROMETRY.	15592455 [Abstract]