SEPT7_HUMAN - dbPTM
SEPT7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEPT7_HUMAN
UniProt AC Q16181
Protein Name Septin-7
Gene Name 7-Sep
Organism Homo sapiens (Human).
Sequence Length 437
Subcellular Localization Cytoplasm . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle . Cleavage furrow . Midbody . Cytoplasm, cytoskeleton, cilium axoneme. Cell projection, cilium, flagellum . Distributed throughout the cytoplasm in prometaphase cells.
Protein Description Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. 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]
Protein Sequence MSVSARSAAAEERSVNSSTMVAQQKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKANWEAQQRILEQQNSSRTLEKNKKKGKIF
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 Orthologous
Protein Cluster
2Phosphorylation------MSVSARSAA
------CCHHHHHHH		25.4420068231
2O-linked_Glycosylation------MSVSARSAA
------CCHHHHHHH		25.4430379171
2Acetylation------MSVSARSAA
------CCHHHHHHH		25.4419413330
2 (in isoform 2)Phosphorylation-25.4420068231
4 (in isoform 2)Phosphorylation-15.6220068231
7Phosphorylation-MSVSARSAAAEERS
-CCHHHHHHHHHHHC		23.2120068231
7 (in isoform 2)Phosphorylation-23.2120068231
14PhosphorylationSAAAEERSVNSSTMV
HHHHHHHCCCHHHHH		29.0030622161
14 (in isoform 2)Phosphorylation-29.0020068231
17PhosphorylationAEERSVNSSTMVAQQ
HHHHCCCHHHHHHHH		25.6530622161
17 (in isoform 2)Phosphorylation-25.6520068231
18 (in isoform 2)Phosphorylation-18.4720068231
18PhosphorylationEERSVNSSTMVAQQK
HHHCCCHHHHHHHHC		18.4720068231
19PhosphorylationERSVNSSTMVAQQKN
HHCCCHHHHHHHHCC		18.5830622161
19 (in isoform 2)Phosphorylation-18.5820068231
29 (in isoform 2)Phosphorylation-26.1225159151
30PhosphorylationQQKNLEGYVGFANLP
HHCCCCCCCEECCCC		6.5025159151
41PhosphorylationANLPNQVYRKSVKRG
CCCCCHHHHHHHHCC		11.5428152594
44PhosphorylationPNQVYRKSVKRGFEF
CCHHHHHHHHCCCEE		24.71-
69PhosphorylationGKSTLINSLFLTDLY
CHHHHHHHHHCCCCC		17.3224076635
73PhosphorylationLINSLFLTDLYSPEY
HHHHHHCCCCCCCCC		19.3428450419
76PhosphorylationSLFLTDLYSPEYPGP
HHHCCCCCCCCCCCC		25.6228450419
77PhosphorylationLFLTDLYSPEYPGPS
HHCCCCCCCCCCCCC		20.6725849741
80PhosphorylationTDLYSPEYPGPSHRI
CCCCCCCCCCCCCCC		19.5128450419
84PhosphorylationSPEYPGPSHRIKKTV
CCCCCCCCCCCEEEE		31.1728102081
88UbiquitinationPGPSHRIKKTVQVEQ
CCCCCCCEEEEEEEC		42.20-
89UbiquitinationGPSHRIKKTVQVEQS
CCCCCCEEEEEEECC		52.11-
96PhosphorylationKTVQVEQSKVLIKEG
EEEEEECCEEEEEEC		15.9525056879
97UbiquitinationTVQVEQSKVLIKEGG
EEEEECCEEEEEECC		40.53-
97AcetylationTVQVEQSKVLIKEGG
EEEEECCEEEEEECC		40.5326051181
124O-linked_GlycosylationFGDAVDNSNCWQPVI
CCCCCCCCCCCHHHH		28.9730379171
141PhosphorylationIDSKFEDYLNAESRV
HHHHHHHHHCHHHHC		8.4824927040
173UbiquitinationAPSGHGLKPLDIEFM
CCCCCCCCCCCHHHH		48.39-
173AcetylationAPSGHGLKPLDIEFM
CCCCCCCCCCCHHHH		48.3926051181
180 (in isoform 2)Acetylation-1.28-
181UbiquitinationPLDIEFMKRLHEKVN
CCCHHHHHHHHHHHC		58.07-
181AcetylationPLDIEFMKRLHEKVN
CCCHHHHHHHHHHHC		58.0719608861
185 (in isoform 2)Acetylation-64.39-
186AcetylationFMKRLHEKVNIIPLI
HHHHHHHHHCCHHHH		29.8119608861
186UbiquitinationFMKRLHEKVNIIPLI
HHHHHHHHHCCHHHH		29.81-
186MalonylationFMKRLHEKVNIIPLI
HHHHHHHHHCCHHHH		29.8126320211
195UbiquitinationNIIPLIAKADTLTPE
CCHHHHHCCCCCCHH		39.54-
198PhosphorylationPLIAKADTLTPEECQ
HHHHCCCCCCHHHHH		37.0729514088
208AcetylationPEECQQFKKQIMKEI
HHHHHHHHHHHHHHH		39.1623954790
208UbiquitinationPEECQQFKKQIMKEI
HHHHHHHHHHHHHHH		39.16-
209UbiquitinationEECQQFKKQIMKEIQ
HHHHHHHHHHHHHHH		46.47-
212 (in isoform 2)Acetylation-2.70-
213UbiquitinationQFKKQIMKEIQEHKI
HHHHHHHHHHHHCCC		53.98-
213AcetylationQFKKQIMKEIQEHKI
HHHHHHHHHHHHCCC		53.9819608861
219AcetylationMKEIQEHKIKIYEFP
HHHHHHCCCEEEECC		44.9625953088
221AcetylationEIQEHKIKIYEFPET
HHHHCCCEEEECCCC		44.0026051181
223PhosphorylationQEHKIKIYEFPETDD
HHCCCEEEECCCCCC		13.4024732914
228PhosphorylationKIYEFPETDDEEENK
EEEECCCCCCHHHHH		49.3322167270
234 (in isoform 2)Ubiquitination-46.3621906983
235AcetylationTDDEEENKLVKKIKD
CCCHHHHHHHHHHHH		58.9223236377
235UbiquitinationTDDEEENKLVKKIKD
CCCHHHHHHHHHHHH		58.92-
236 (in isoform 1)Ubiquitination-11.7121906983
238AcetylationEEENKLVKKIKDRLP
HHHHHHHHHHHHHCC		60.2525953088
238UbiquitinationEEENKLVKKIKDRLP
HHHHHHHHHHHHHCC		60.25-
239UbiquitinationEENKLVKKIKDRLPL
HHHHHHHHHHHHCCE		47.73-
251PhosphorylationLPLAVVGSNTIIEVN
CCEEEECCCEEEEEC		21.1325693802
253PhosphorylationLAVVGSNTIIEVNGK
EEEECCCEEEEECCE		25.6525693802
260AcetylationTIIEVNGKRVRGRQY
EEEEECCEEECCCCC		42.3826051181
260UbiquitinationTIIEVNGKRVRGRQY
EEEEECCEEECCCCC		42.38-
294SulfoxidationNMLIRTHMQDLKDVT
HHHHHHHHHHHHHHC		3.0730846556
297 (in isoform 2)Ubiquitination-2.62-
298AcetylationRTHMQDLKDVTNNVH
HHHHHHHHHHCCCCC		59.4426051181
298UbiquitinationRTHMQDLKDVTNNVH
HHHHHHHHHHCCCCC		59.44-
306PhosphorylationDVTNNVHYENYRSRK
HHCCCCCCCCHHHCC		11.11-
309PhosphorylationNNVHYENYRSRKLAA
CCCCCCCHHHCCEEE		9.6829496907
311PhosphorylationVHYENYRSRKLAAVT
CCCCCHHHCCEEEEE		24.3329496907
313UbiquitinationYENYRSRKLAAVTYN
CCCHHHCCEEEEEEC		43.66-
318 (in isoform 2)Phosphorylation-13.42-
318PhosphorylationSRKLAAVTYNGVDNN
HCCEEEEEECCCCCC		13.4221945579
319PhosphorylationRKLAAVTYNGVDNNK
CCEEEEEECCCCCCC		11.8821945579
326MalonylationYNGVDNNKNKGQLTK
ECCCCCCCCCCCCCC		67.3126320211
328UbiquitinationGVDNNKNKGQLTKSP
CCCCCCCCCCCCCCH		50.04-
332PhosphorylationNKNKGQLTKSPLAQM
CCCCCCCCCCHHHHC		22.9123927012
333 (in isoform 2)Phosphorylation-59.68-
333UbiquitinationKNKGQLTKSPLAQME
CCCCCCCCCHHHHCH		59.68-
334PhosphorylationNKGQLTKSPLAQMEE
CCCCCCCCHHHHCHH		21.6519664994
339SulfoxidationTKSPLAQMEEERREH
CCCHHHHCHHHHHHH		6.1021406390
364AcetylationMEQVFEMKVKEKVQK
HHHHHHHHHHHHHHH		42.8525953088
368AcetylationFEMKVKEKVQKLKDS
HHHHHHHHHHHHCHH		44.227822297
371AcetylationKVKEKVQKLKDSEAE
HHHHHHHHHCHHHHH		61.5626051181
373AcetylationKEKVQKLKDSEAELQ
HHHHHHHCHHHHHHH		67.26-
373UbiquitinationKEKVQKLKDSEAELQ
HHHHHHHCHHHHHHH		67.26-
373MalonylationKEKVQKLKDSEAELQ
HHHHHHHCHHHHHHH		67.2626320211
387AcetylationQRRHEQMKKNLEAQH
HHHHHHHHHHHHHHH		37.907708301
394 (in isoform 2)Ubiquitination-32.38-
395AcetylationKNLEAQHKELEEKRR
HHHHHHHHHHHHHHH		52.4923749302
408AcetylationRRQFEDEKANWEAQQ
HHHHHHHHHHHHHHH		60.3826051181
422 (in isoform 2)Phosphorylation-41.46-
423 (in isoform 2)Phosphorylation-19.50-
423PhosphorylationRILEQQNSSRTLEKN
HHHHHHHHHHHHHHH		19.5029255136
424PhosphorylationILEQQNSSRTLEKNK
HHHHHHHHHHHHHHH		36.5129255136
425 (in isoform 2)Phosphorylation-43.05-
425MethylationLEQQNSSRTLEKNKK
HHHHHHHHHHHHHHH		43.0530758601
426PhosphorylationEQQNSSRTLEKNKKK
HHHHHHHHHHHHHHC		41.0129255136
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
228TPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEPT7_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 SEPT7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEPT9_HUMANSEPT9physical
22939629
TOP2B_HUMANTOP2Bphysical
22939629
TRI55_HUMANTRIM55physical
22939629
SRSF5_HUMANSRSF5physical
22939629
ZN326_HUMANZNF326physical
22939629
VTNC_HUMANVTNphysical
22939629
UT14A_HUMANUTP14Aphysical
22939629
SRSF7_HUMANSRSF7physical
22939629
TF3C1_HUMANGTF3C1physical
22939629
TPBG_HUMANTPBGphysical
22939629
TRA2B_HUMANTRA2Bphysical
22939629
SMCA5_HUMANSMARCA5physical
22939629
VASN_HUMANVASNphysical
22939629
SRP14_HUMANSRP14physical
22939629
SURF4_HUMANSURF4physical
22939629
U2AF1_HUMANU2AF1physical
22939629
U2AF2_HUMANU2AF2physical
22939629
UBC9_HUMANUBE2Iphysical
22939629
TRA2A_HUMANTRA2Aphysical
22939629
SSRG_HUMANSSR3physical
22939629
SON_HUMANSONphysical
22939629
RNF8_HUMANRNF8physical
23442799
REL_HUMANRELphysical
25416956
SEP10_HUMANSEPT10physical
25416956
AP3B1_HUMANAP3B1physical
25380047
SEP10_HUMANSEPT10physical
26344197
SEP11_HUMANSEPT11physical
26344197
SEPT5_HUMANSEPT5physical
26344197
SEPT6_HUMANSEPT6physical
26344197
SEPT8_HUMANSEPT8physical
26344197
SEPT9_HUMANSEPT9physical
26344197
YTHD2_HUMANYTHDF2physical
26344197
ZWILC_HUMANZWILCHphysical
26344197
SEP10_HUMANSEPT10physical
28514442
SEPT6_HUMANSEPT6physical
28514442
SEPT5_HUMANSEPT5physical
28514442
SEPT8_HUMANSEPT8physical
28514442
SEPT4_HUMANSEPT4physical
28514442
SEP11_HUMANSEPT11physical
28514442
SEPT9_HUMANSEPT9physical
28514442
SEP14_HUMANSEPT14physical
28514442
PRCC_HUMANPRCCphysical
27173435
CHRD1_HUMANCHORDC1physical
27173435
SEP11_HUMANSEPT11physical
27173435
GORS2_HUMANGORASP2physical
27173435
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEPT7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-186 AND LYS-213, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-334; SER-424 ANDTHR-426, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASSSPECTROMETRY.
"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-423 AND THR-426, ANDMASS SPECTROMETRY.
"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-334, AND MASSSPECTROMETRY.
"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 THR-426, AND MASSSPECTROMETRY.
"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-30, AND MASSSPECTROMETRY.
"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-319, AND MASSSPECTROMETRY.

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