FRMD8_HUMAN - dbPTM
FRMD8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FRMD8_HUMAN
UniProt AC Q9BZ67
Protein Name FERM domain-containing protein 8
Gene Name FRMD8
Organism Homo sapiens (Human).
Sequence Length 464
Subcellular Localization
Protein Description
Protein Sequence MDGTEGSAGQPGPAERSHRSSVSSVGARAADVLVYLADDTVVPLAVENLPSLSAHELHRAVREVLQLPDIALDVFALWLVSPLLEVQLKPKHQPYKLGRQWPELLLRFTSAPDDDVAMDEPFLQFRRNVFFPKRRELQIHDEEVLRLLYEEAKGNVLAARYPCDVEDCEALGALVCRVQLGPYQPGRPAACDLREKLDSFLPAHLCKRGQSLFAALRGRGARAGPGEQGLLNAYRQVQEVSSDGGCEAALGTHYRAYLLKCHELPFYGCAFFHGEVDKPAQGFLHRGGRKPVSVAISLEGVHVIDSREKHVLLGLRFQELSWDHTSPEEEEPILWLEFDGDSEGTPVNKLLKIYSKQAELMSSLIEYCIELSQAAEPAGPQDSATGSPSDPSSSLAPVQRPKLRRQGSVVSSRIQHLSTIDYVEDGKGIRRVKPKRTTSFFSRQLSLGQGSYTVVQPGDSLEQG
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
1Acetylation-------MDGTEGSA
-------CCCCCCCC		10.9322814378
17PhosphorylationQPGPAERSHRSSVSS
CCCCCCCCCCCCCHH		18.1123663014
20PhosphorylationPAERSHRSSVSSVGA
CCCCCCCCCCHHHHH		29.6630278072
21PhosphorylationAERSHRSSVSSVGAR
CCCCCCCCCHHHHHH		26.4428355574
21 (in isoform 2)Phosphorylation-26.4425849741
23 (in isoform 2)Phosphorylation-22.6625849741
23PhosphorylationRSHRSSVSSVGARAA
CCCCCCCHHHHHHHH		22.6628355574
24 (in isoform 2)Phosphorylation-23.5525849741
24PhosphorylationSHRSSVSSVGARAAD
CCCCCCHHHHHHHHH		23.5528355574
97 (in isoform 2)Ubiquitination-5.8821906983
99UbiquitinationHQPYKLGRQWPELLL
CCCCCCCCCCCHHHH		45.91-
119UbiquitinationPDDDVAMDEPFLQFR
CCCCCCCCCHHHHHH		51.1621906983
133UbiquitinationRRNVFFPKRRELQIH
HHHHCCCCCCCCCCC		59.95-
1332-HydroxyisobutyrylationRRNVFFPKRRELQIH
HHHHCCCCCCCCCCC		59.95-
153 (in isoform 1)Ubiquitination-55.0621906983
153UbiquitinationRLLYEEAKGNVLAAR
HHHHHHHCCCEEEEE		55.0621906983
162UbiquitinationNVLAARYPCDVEDCE
CEEEEECCCCHHHHH		11.41-
173UbiquitinationEDCEALGALVCRVQL
HHHHHHCCEEEEEEC		9.55-
196UbiquitinationAACDLREKLDSFLPA
CCCCHHHHHHHHHHH		51.68-
199PhosphorylationDLREKLDSFLPAHLC
CHHHHHHHHHHHHHH		38.84-
207UbiquitinationFLPAHLCKRGQSLFA
HHHHHHHHHCHHHHH		66.96-
211PhosphorylationHLCKRGQSLFAALRG
HHHHHCHHHHHHHCC		28.4228857561
217MethylationQSLFAALRGRGARAG
HHHHHHHCCCCCCCC		28.21-
222MethylationALRGRGARAGPGEQG
HHCCCCCCCCCCHHH		42.79-
226UbiquitinationRGARAGPGEQGLLNA
CCCCCCCCHHHHHHH		38.65-
241PhosphorylationYRQVQEVSSDGGCEA
HHHHEECCCCCCCHH		23.2028348404
242PhosphorylationRQVQEVSSDGGCEAA
HHHEECCCCCCCHHH		45.5128348404
260UbiquitinationHYRAYLLKCHELPFY
HHHHHHHHHCCCCCC		30.83-
275UbiquitinationGCAFFHGEVDKPAQG
EEEEEECCCCCCCCC		38.69-
309UbiquitinationHVIDSREKHVLLGLR
EEECCCCCEEEEEEE		37.59-
318UbiquitinationVLLGLRFQELSWDHT
EEEEEEEEECCCCCC		44.26-
349UbiquitinationSEGTPVNKLLKIYSK
CCCCCHHHHHHHHHH		56.27-
352UbiquitinationTPVNKLLKIYSKQAE
CCHHHHHHHHHHHHH		50.46-
371 (in isoform 2)Ubiquitination-2.0321906983
372PhosphorylationIEYCIELSQAAEPAG
HHHHHHHHHHCCCCC		12.6528348404
383PhosphorylationEPAGPQDSATGSPSD
CCCCCCCCCCCCCCC		23.6027251275
385PhosphorylationAGPQDSATGSPSDPS
CCCCCCCCCCCCCCC		41.9928348404
387PhosphorylationPQDSATGSPSDPSSS
CCCCCCCCCCCCCCC		19.5127251275
393UbiquitinationGSPSDPSSSLAPVQR
CCCCCCCCCCCCCCC		34.4621906983
408PhosphorylationPKLRRQGSVVSSRIQ
CHHHHCCCCHHHHHE		15.8227794612
411PhosphorylationRRQGSVVSSRIQHLS
HHCCCCHHHHHEEHH		16.2528102081
412PhosphorylationRQGSVVSSRIQHLST
HCCCCHHHHHEEHHC		23.0728102081
418PhosphorylationSSRIQHLSTIDYVED
HHHHEEHHCCEEEEC		22.6129978859
419PhosphorylationSRIQHLSTIDYVEDG
HHHEEHHCCEEEECC		24.9929978859
422PhosphorylationQHLSTIDYVEDGKGI
EEHHCCEEEECCCCC		11.2429978859
427UbiquitinationIDYVEDGKGIRRVKP
CEEEECCCCCCCCCC		64.582190698
427 (in isoform 1)Ubiquitination-64.5821906983
437PhosphorylationRRVKPKRTTSFFSRQ
CCCCCCCCCCCHHCE		32.6830266825
438PhosphorylationRVKPKRTTSFFSRQL
CCCCCCCCCCHHCEE		27.8030266825
439PhosphorylationVKPKRTTSFFSRQLS
CCCCCCCCCHHCEEE		24.5530266825
442PhosphorylationKRTTSFFSRQLSLGQ
CCCCCCHHCEEECCC		19.6720068231
446PhosphorylationSFFSRQLSLGQGSYT
CCHHCEEECCCCCEE		23.3230266825
451PhosphorylationQLSLGQGSYTVVQPG
EEECCCCCEEEECCC		15.1130266825
452PhosphorylationLSLGQGSYTVVQPGD
EECCCCCEEEECCCC		15.4623403867
453PhosphorylationSLGQGSYTVVQPGDS
ECCCCCEEEECCCCC		18.8530266825
460PhosphorylationTVVQPGDSLEQG---
EEECCCCCCCCC---		39.4623403867
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

Oops, there are no upstream regulatory protein records of FRMD8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FRMD8_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 FRMD8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 FRMD8_HUMAN

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Related Literatures of Post-Translational Modification
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-439, AND MASSSPECTROMETRY.

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