EXOC7_HUMAN - dbPTM
EXOC7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXOC7_HUMAN
UniProt AC Q9UPT5
Protein Name Exocyst complex component 7
Gene Name EXOC7
Organism Homo sapiens (Human).
Sequence Length 735
Subcellular Localization Cytoplasm, cytosol . Cell membrane
Peripheral membrane protein . Midbody, Midbody ring . Translocates, as a preformed complex with EXOC3/SEC6 and EXOC4/SEC8, to the plasma membrane in response to insulin through the activation of ARHQ (By similarit
Protein Description Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion (By similarity)..
Protein Sequence MIPPQEASARRREIEDKLKQEEETLSFIRDSLEKSDQLTKNMVSILSSFESRLMKLENSIIPVHKQTENLQRLQENVEKTLSCLDHVISYYHVASDTEKIIREGPTGRLEEYLGSMAKIQKAVEYFQDNSPDSPELNKVKLLFERGKEALESEFRSLMTRHSKVVSPVLILDLISGDDDLEAQEDVTLEHLPESVLQDVIRISRWLVEYGRNQDFMNVYYQIRSSQLDRSIKGLKEHFHKSSSSSGVPYSPAIPNKRKDTPTKKPVKRPGTIRKAQNLLKQYSQHGLDGKKGGSNLIPLEGLLPCTPRGGLPGPWINAACVCAADISPGHEHDFRVKHLSEALNDKHGPLAGRDDMLDVETDAYIHCVSAFVKLAQSEYQLLADIIPEHHQKKTFDSLIQDALDGLMLEGENIVSAARKAIVRHDFSTVLTVFPILRHLKQTKPEFDQVLQGTAASTKNKLPGLITSMETIGAKALEDFADNIKNDPDKEYNMPKDGTVHELTSNAILFLQQLLDFQETAGAMLASQETSSSATSYSSEFSKRLLSTYICKVLGNLQLNLLSKSKVYEDPALSAIFLHNNYNYILKSLEKSELIQLVAVTQKTAERSYREHIEQQIQTYQRSWLKVTDYIAEKNLPVFQPGVKLRDKERQIIKERFKGFNDGLEELCKIQKAWAIPDTEQRDRIRQAQKTIVKETYGAFLQKFGSVPFTKNPEKYIKYGVEQVGDMIDRLFDTSA
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
342-HydroxyisobutyrylationFIRDSLEKSDQLTKN
HHHHHHHHCHHHHHH		65.70-
40UbiquitinationEKSDQLTKNMVSILS
HHCHHHHHHHHHHHH		52.1921890473
40UbiquitinationEKSDQLTKNMVSILS
HHCHHHHHHHHHHHH		52.1921890473
40 (in isoform 1)Ubiquitination-52.1921890473
40UbiquitinationEKSDQLTKNMVSILS
HHCHHHHHHHHHHHH		52.1921890473
40 (in isoform 4)Ubiquitination-52.1921890473
40 (in isoform 2)Ubiquitination-52.1921890473
40 (in isoform 3)Ubiquitination-52.1921890473
44PhosphorylationQLTKNMVSILSSFES
HHHHHHHHHHHHHHH		13.6728985074
48PhosphorylationNMVSILSSFESRLMK
HHHHHHHHHHHHHHH		29.5928270605
51PhosphorylationSILSSFESRLMKLEN
HHHHHHHHHHHHHHH		28.8028270605
55UbiquitinationSFESRLMKLENSIIP
HHHHHHHHHHHCCCC		58.19-
65 (in isoform 3)Ubiquitination-60.1821890473
65 (in isoform 2)Ubiquitination-60.1821890473
65 (in isoform 4)Ubiquitination-60.1821890473
65 (in isoform 1)Ubiquitination-60.1821890473
65UbiquitinationNSIIPVHKQTENLQR
HCCCCHHHHCHHHHH		60.1821890473
65UbiquitinationNSIIPVHKQTENLQR
HCCCCHHHHCHHHHH		60.1821890473
65UbiquitinationNSIIPVHKQTENLQR
HCCCCHHHHCHHHHH		60.1821890473
80PhosphorylationLQENVEKTLSCLDHV
HHHHHHHHHHHHHHH		15.4820071362
82PhosphorylationENVEKTLSCLDHVIS
HHHHHHHHHHHHHHH		20.1920071362
90PhosphorylationCLDHVISYYHVASDT
HHHHHHHHHHHHCCH		6.1022817900
115PhosphorylationRLEEYLGSMAKIQKA
HHHHHHHHHHHHHHH		16.9926546556
118UbiquitinationEYLGSMAKIQKAVEY
HHHHHHHHHHHHHHH		36.71-
121UbiquitinationGSMAKIQKAVEYFQD
HHHHHHHHHHHHHHH		58.85-
125PhosphorylationKIQKAVEYFQDNSPD
HHHHHHHHHHHCCCC		10.43-
130PhosphorylationVEYFQDNSPDSPELN
HHHHHHCCCCCHHHH		38.07-
133PhosphorylationFQDNSPDSPELNKVK
HHHCCCCCHHHHHHH		24.53-
138 (in isoform 1)Ubiquitination-54.0621890473
138 (in isoform 2)Ubiquitination-54.0621890473
138 (in isoform 3)Ubiquitination-54.0621890473
138 (in isoform 4)Ubiquitination-54.0621890473
138AcetylationPDSPELNKVKLLFER
CCCHHHHHHHHHHHH		54.0611922939
138UbiquitinationPDSPELNKVKLLFER
CCCHHHHHHHHHHHH		54.062190698
140AcetylationSPELNKVKLLFERGK
CHHHHHHHHHHHHHH		40.8711922949
140UbiquitinationSPELNKVKLLFERGK
CHHHHHHHHHHHHHH		40.87-
147AcetylationKLLFERGKEALESEF
HHHHHHHHHHHHHHH		46.1411922959
147UbiquitinationKLLFERGKEALESEF
HHHHHHHHHHHHHHH		46.14-
224PhosphorylationNVYYQIRSSQLDRSI
HHHHHHHHHHHHHHH		24.86-
225PhosphorylationVYYQIRSSQLDRSIK
HHHHHHHHHHHHHHH		25.55-
230PhosphorylationRSSQLDRSIKGLKEH
HHHHHHHHHHHHHHH		28.4628857561
241PhosphorylationLKEHFHKSSSSSGVP
HHHHHHHCCCCCCCC		27.2121945579
242PhosphorylationKEHFHKSSSSSGVPY
HHHHHHCCCCCCCCC		38.7621945579
243PhosphorylationEHFHKSSSSSGVPYS
HHHHHCCCCCCCCCC		35.3023401153
244PhosphorylationHFHKSSSSSGVPYSP
HHHHCCCCCCCCCCC		32.8121945579
245PhosphorylationFHKSSSSSGVPYSPA
HHHCCCCCCCCCCCC		45.8421945579
249PhosphorylationSSSSGVPYSPAIPNK
CCCCCCCCCCCCCCC		25.5321945579
250PhosphorylationSSSGVPYSPAIPNKR
CCCCCCCCCCCCCCC		11.2019664994
250 (in isoform 1)Phosphorylation-11.20-
250 (in isoform 2)Phosphorylation-11.20-
260PhosphorylationIPNKRKDTPTKKPVK
CCCCCCCCCCCCCCC		35.5729083192
262PhosphorylationNKRKDTPTKKPVKRP
CCCCCCCCCCCCCCC		54.5129083192
271PhosphorylationKPVKRPGTIRKAQNL
CCCCCCHHHHHHHHH		21.9421406692
282PhosphorylationAQNLLKQYSQHGLDG
HHHHHHHHHHCCCCC		14.5430266825
283PhosphorylationQNLLKQYSQHGLDGK
HHHHHHHHHCCCCCC		17.1323401153
294 (in isoform 1)Phosphorylation-36.8128122231
312 (in isoform 6)Phosphorylation-50.5025849741
340PhosphorylationDFRVKHLSEALNDKH
HHHHHHHHHHHHCCC		22.1225849741
384 (in isoform 2)Phosphorylation-39.04-
385 (in isoform 2)Phosphorylation-4.75-
415 (in isoform 1)Phosphorylation-16.65-
416 (in isoform 1)Phosphorylation-10.61-
466PhosphorylationNKLPGLITSMETIGA
CCCCCCHHCHHHHCH		27.3618452278
467PhosphorylationKLPGLITSMETIGAK
CCCCCHHCHHHHCHH		13.9718452278
470PhosphorylationGLITSMETIGAKALE
CCHHCHHHHCHHHHH		18.9720071362
643MalonylationPVFQPGVKLRDKERQ
CCCCCCCCCCHHHHH		43.6632601280
653UbiquitinationDKERQIIKERFKGFN
HHHHHHHHHHHCCCC		44.45-
657MalonylationQIIKERFKGFNDGLE
HHHHHHHCCCCHHHH		69.6726320211
705PhosphorylationAFLQKFGSVPFTKNP
HHHHHHCCCCCCCCH		29.7428857561
714AcetylationPFTKNPEKYIKYGVE
CCCCCHHHHHHHCHH		54.2469835
717AcetylationKNPEKYIKYGVEQVG
CCHHHHHHHCHHHHH		32.6361135
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
250SPhosphorylationKinaseMAPK1P28482
GPS
250SPhosphorylationKinaseMAPK3P27361
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXOC7_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 EXOC7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZC3HE_HUMANZC3H14physical
16189514
KXDL1_HUMANKXD1physical
16189514
IFT20_HUMANIFT20physical
16189514
RT4I1_HUMANRTN4IP1physical
16189514
USBP1_HUMANUSHBP1physical
16189514
PRP19_HUMANPRPF19physical
16189514
DLG3_HUMANDLG3physical
12738960
NMDE2_HUMANGRIN2Bphysical
12738960
EXOC4_HUMANEXOC4physical
12738960
RHOQ_HUMANRHOQphysical
12687004
PRP19_HUMANPRPF19physical
21639856
KINH_HUMANKIF5Bphysical
22939629
IFT20_HUMANIFT20physical
25416956
SRCRL_HUMANSSC5Dphysical
25416956
EXOC6_HUMANEXOC6physical
26344197
EXC6B_HUMANEXOC6Bphysical
26344197
EXOC8_HUMANEXOC8physical
26344197
EXOC5_HUMANEXOC5physical
27173435
EXOC4_HUMANEXOC4physical
27173435
EXOC8_HUMANEXOC8physical
27173435
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 EXOC7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-250, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.

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