SEPT8_HUMAN - dbPTM
SEPT8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEPT8_HUMAN
UniProt AC Q92599
Protein Name Septin-8
Gene Name 8-Sep
Organism Homo sapiens (Human).
Sequence Length 483
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. In platelets, found in areas surrounding alpha-granules.
Protein Description Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion..
Protein Sequence MAATDLERFSNAEPEPRSLSLGGHVGFDSLPDQLVSKSVTQGFSFNILCVGETGIGKSTLMNTLFNTTFETEEASHHEACVRLRPQTYDLQESNVQLKLTIVDAVGFGDQINKDESYRPIVDYIDAQFENYLQEELKIRRSLFDYHDTRIHVCLYFITPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTISKSELHKFKIKIMGELVSNGVQIYQFPTDDEAVAEINAVMNAHLPFAVVGSTEEVKVGNKLVRARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHSRHYELYRRCKLEEMGFQDSDGDSQPFSLQETYEAKRKEFLSELQRKEEEMRQMFVNKVKETELELKEKERELHEKFEHLKRVHQEEKRKVEEKRRELEEETNAFNRRKAAVEALQSQALHATSQQPLRKDKDKKNRSDIGAHQPGMSLSSSKVMMTKASVEPLNCSSWWPAIQCCSCLVRDATWREGFL
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
2Acetylation------MAATDLERF
------CCCCHHHHH
21.0422814378
4Phosphorylation----MAATDLERFSN
----CCCCHHHHHHC
31.4228857561
10PhosphorylationATDLERFSNAEPEPR
CCHHHHHHCCCCCCC
41.1528355574
17MethylationSNAEPEPRSLSLGGH
HCCCCCCCCCCCCCC
48.87115916457
18PhosphorylationNAEPEPRSLSLGGHV
CCCCCCCCCCCCCCC
32.7822617229
20PhosphorylationEPEPRSLSLGGHVGF
CCCCCCCCCCCCCCC
26.6422617229
29PhosphorylationGGHVGFDSLPDQLVS
CCCCCCCCCCHHHCC
39.2720068231
36PhosphorylationSLPDQLVSKSVTQGF
CCCHHHCCCCCCCCC
28.0127362937
53PhosphorylationNILCVGETGIGKSTL
EEEEECCCCCCHHHH
28.33-
100PhosphorylationSNVQLKLTIVDAVGF
CCCEEEEEEEEHHCC
19.84-
141PhosphorylationEELKIRRSLFDYHDT
HHHHHCHHHHHHHCC
24.4430108239
163PhosphorylationFITPTGHSLKSLDLV
EECCCCCCCCCCCEE
38.55-
166PhosphorylationPTGHSLKSLDLVTMK
CCCCCCCCCCEEEHH
32.2021964256
171PhosphorylationLKSLDLVTMKKLDSK
CCCCCEEEHHHCCCC
30.4820068231
173UbiquitinationSLDLVTMKKLDSKVN
CCCEEEHHHCCCCCC
40.60-
178UbiquitinationTMKKLDSKVNIIPII
EHHHCCCCCCEEEEE
38.68-
192PhosphorylationIAKADTISKSELHKF
EEECCCCCHHHHHHH
32.02-
193AcetylationAKADTISKSELHKFK
EECCCCCHHHHHHHE
44.0612430123
193UbiquitinationAKADTISKSELHKFK
EECCCCCHHHHHHHE
44.06-
194PhosphorylationKADTISKSELHKFKI
ECCCCCHHHHHHHEE
38.3028348404
198AcetylationISKSELHKFKIKIMG
CCHHHHHHHEEEEEH
62.0612430135
198UbiquitinationISKSELHKFKIKIMG
CCHHHHHHHEEEEEH
62.06-
200AcetylationKSELHKFKIKIMGEL
HHHHHHHEEEEEHHH
48.1412430147
202UbiquitinationELHKFKIKIMGELVS
HHHHHEEEEEHHHHH
27.51-
251UbiquitinationEEVKVGNKLVRARQY
CEEEECCEEEECCCC
42.29-
275AcetylationENHCDFVKLREMLIR
CCCCCHHHHHHHHHH
41.6526051181
297PhosphorylationEQTHSRHYELYRRCK
HHHHHHHHHHHHHHC
13.40-
300PhosphorylationHSRHYELYRRCKLEE
HHHHHHHHHHHCHHH
5.53-
304UbiquitinationYELYRRCKLEEMGFQ
HHHHHHHCHHHCCCC
58.06-
313PhosphorylationEEMGFQDSDGDSQPF
HHCCCCCCCCCCCCC
32.4829802988
317PhosphorylationFQDSDGDSQPFSLQE
CCCCCCCCCCCCHHH
45.3326471730
321PhosphorylationDGDSQPFSLQETYEA
CCCCCCCCHHHHHHH
35.5128555341
326PhosphorylationPFSLQETYEAKRKEF
CCCHHHHHHHHHHHH
17.09-
329UbiquitinationLQETYEAKRKEFLSE
HHHHHHHHHHHHHHH
52.65-
331UbiquitinationETYEAKRKEFLSELQ
HHHHHHHHHHHHHHH
52.70-
340UbiquitinationFLSELQRKEEEMRQM
HHHHHHHHHHHHHHH
57.42-
351UbiquitinationMRQMFVNKVKETELE
HHHHHHHHHHHHHHH
49.75-
353UbiquitinationQMFVNKVKETELELK
HHHHHHHHHHHHHHH
61.60-
360UbiquitinationKETELELKEKERELH
HHHHHHHHHHHHHHH
58.32-
3692-HydroxyisobutyrylationKERELHEKFEHLKRV
HHHHHHHHHHHHHHH
45.35-
369UbiquitinationKERELHEKFEHLKRV
HHHHHHHHHHHHHHH
45.35-
381AcetylationKRVHQEEKRKVEEKR
HHHHHHHHHHHHHHH
57.687708507
387AcetylationEKRKVEEKRRELEEE
HHHHHHHHHHHHHHH
43.1620167786
402UbiquitinationTNAFNRRKAAVEALQ
HHHHHHHHHHHHHHH
37.14-
410PhosphorylationAAVEALQSQALHATS
HHHHHHHHHHHHHHC
20.4724719451
416PhosphorylationQSQALHATSQQPLRK
HHHHHHHHCCCCCCC
19.1329514088
417PhosphorylationSQALHATSQQPLRKD
HHHHHHHCCCCCCCC
27.8329514088
435 (in isoform 4)Phosphorylation-9.85-
438 (in isoform 4)Phosphorylation-30.50-
440 (in isoform 4)Phosphorylation-4.66-

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
163SPhosphorylationKinaseMAPKAPK5Q8IW41
PSP
192SPhosphorylationKinaseMAPKAPK5Q8IW41
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEPT8_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 SEPT8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEPT5_HUMANSEPT5physical
12023038
PPHLN_HUMANPPHLN1physical
21900206
KMT2B_HUMANKMT2Bphysical
21900206
JADE1_HUMANJADE1physical
21900206
SH3G3_HUMANSH3GL3physical
21900206
A2MG_HUMANA2Mphysical
21900206
SH3G1_HUMANSH3GL1physical
21900206
RNF8_HUMANRNF8physical
23442799
SEP10_HUMANSEPT10physical
26344197
SEP11_HUMANSEPT11physical
26344197
SEPT5_HUMANSEPT5physical
26344197
ZWILC_HUMANZWILCHphysical
26344197

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 SEPT8_HUMAN

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Related Literatures of Post-Translational Modification

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