FRMD6_HUMAN - dbPTM
FRMD6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FRMD6_HUMAN
UniProt AC Q96NE9
Protein Name FERM domain-containing protein 6
Gene Name FRMD6
Organism Homo sapiens (Human).
Sequence Length 622
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Can colocalize with actin.
Protein Description
Protein Sequence MNKLNFHNNRVMQDRRSVCIFLPNDESLNIIINVKILCHQLLVQVCDLLRLKDCHLFGLSVIQNNEHVYMELSQKLYKYCPKEWKKEASKVRQYEVTWGIDQFGPPMIIHFRVQYYVENGRLISDRAARYYYYWHLRKQVLHSQCVLREEAYFLLAAFALQADLGNFKRNKHYGKYFEPEAYFPSWVVSKRGKDYILKHIPNMHKDQFALTASEAHLKYIKEAVRLDDVAVHYYRLYKDKREIEASLTLGLTMRGIQIFQNLDEEKQLLYDFPWTNVGKLVFVGKKFEILPDGLPSARKLIYYTGCPMRSRHLLQLLSNSHRLYMNLQPVLRHIRKLEENEEKKQYRESYISDNLDLDMDQLEKRSRASGSSAGSMKHKRLSRHSTASHSSSHTSGIEADTKPRDTGPEDSYSSSAIHRKLKTCSSMTSHGSSHTSGVESGGKDRLEEDLQDDEIEMLVDDPRDLEQMNEESLEVSPDMCIYITEDMLMSRKLNGHSGLIVKEIGSSTSSSSETVVKLRGQSTDSLPQTICRKPKTSTDRHSLSLDDIRLYQKDFLRIAGLCQDTAQSYTFGCGHELDEEGLYCNSCLAQQCINIQDAFPVKRTSKYFSLDLTHDEVPEFVV
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
3Ubiquitination-----MNKLNFHNNR
-----CCCCCCCCCC		43.4323000965
159UbiquitinationYFLLAAFALQADLGN
HHHHHHHHHHHHHCC		8.2729967540
167PhosphorylationLQADLGNFKRNKHYG
HHHHHCCCCCCCCCC		8.1533259812
185UbiquitinationEPEAYFPSWVVSKRG
CCHHHCCCEEEECCC		23.7023000965
186PhosphorylationPEAYFPSWVVSKRGK
CHHHCCCEEEECCCH		8.5132645325
190UbiquitinationFPSWVVSKRGKDYIL
CCCEEEECCCHHHHH		54.2623000965
193UbiquitinationWVVSKRGKDYILKHI
EEEECCCHHHHHHHC		51.9323000965
195UbiquitinationVSKRGKDYILKHIPN
EECCCHHHHHHHCCC		16.1923000965
198UbiquitinationRGKDYILKHIPNMHK
CCHHHHHHHCCCCCH		29.9023000965
248PhosphorylationREIEASLTLGLTMRG
HHHHHHHHHCCHHHH		19.1123532336
252PhosphorylationASLTLGLTMRGIQIF
HHHHHCCHHHHHHEE		11.7423532336
302PhosphorylationPSARKLIYYTGCPMR
CCCCHHHHHCCCCCC		12.8628152594
303PhosphorylationSARKLIYYTGCPMRS
CCCHHHHHCCCCCCH		6.9428152594
304PhosphorylationARKLIYYTGCPMRSR
CCHHHHHCCCCCCHH		18.4828152594
324PhosphorylationLSNSHRLYMNLQPVL
HHCCCHHHHHHHHHH		5.5027642862
346PhosphorylationENEEKKQYRESYISD
HHHHHHHHHHHHHHH		25.8123090842
349PhosphorylationEKKQYRESYISDNLD
HHHHHHHHHHHHCCC		20.8322199227
350PhosphorylationKKQYRESYISDNLDL
HHHHHHHHHHHCCCC		10.3318491316
352PhosphorylationQYRESYISDNLDLDM
HHHHHHHHHCCCCCH		16.5322199227
369PhosphorylationLEKRSRASGSSAGSM
HHHHHHHCCCCCHHH		37.7926329039
371PhosphorylationKRSRASGSSAGSMKH
HHHHHCCCCCHHHHH		17.9626329039
372PhosphorylationRSRASGSSAGSMKHK
HHHHCCCCCHHHHHH		39.9326329039
375PhosphorylationASGSSAGSMKHKRLS
HCCCCCHHHHHHHHH		25.1125849741
382PhosphorylationSMKHKRLSRHSTASH
HHHHHHHHCCCCCCC		31.7923927012
385PhosphorylationHKRLSRHSTASHSSS
HHHHHCCCCCCCCCC		25.2630576142
386PhosphorylationKRLSRHSTASHSSSH
HHHHCCCCCCCCCCC		26.5023927012
388PhosphorylationLSRHSTASHSSSHTS
HHCCCCCCCCCCCCC		24.8025849741
390PhosphorylationRHSTASHSSSHTSGI
CCCCCCCCCCCCCCC		30.9223927012
391PhosphorylationHSTASHSSSHTSGIE
CCCCCCCCCCCCCCC		22.2523927012
392PhosphorylationSTASHSSSHTSGIEA
CCCCCCCCCCCCCCC		33.5223927012
394PhosphorylationASHSSSHTSGIEADT
CCCCCCCCCCCCCCC		30.5123927012
395PhosphorylationSHSSSHTSGIEADTK
CCCCCCCCCCCCCCC		32.1430576142
401PhosphorylationTSGIEADTKPRDTGP
CCCCCCCCCCCCCCC		50.42-
406PhosphorylationADTKPRDTGPEDSYS
CCCCCCCCCCCCCCC		56.7826356563
411PhosphorylationRDTGPEDSYSSSAIH
CCCCCCCCCCHHHHH		25.8330266825
412PhosphorylationDTGPEDSYSSSAIHR
CCCCCCCCCHHHHHH		25.5430266825
413PhosphorylationTGPEDSYSSSAIHRK
CCCCCCCCHHHHHHH		23.0525849741
414PhosphorylationGPEDSYSSSAIHRKL
CCCCCCCHHHHHHHH		18.6325849741
415PhosphorylationPEDSYSSSAIHRKLK
CCCCCCHHHHHHHHC		25.8730266825
423PhosphorylationAIHRKLKTCSSMTSH
HHHHHHCCCCCCCCC		28.2330576142
425PhosphorylationHRKLKTCSSMTSHGS
HHHHCCCCCCCCCCC		28.5123312004
426PhosphorylationRKLKTCSSMTSHGSS
HHHCCCCCCCCCCCC		28.3825159151
428PhosphorylationLKTCSSMTSHGSSHT
HCCCCCCCCCCCCCC		21.3723312004
429PhosphorylationKTCSSMTSHGSSHTS
CCCCCCCCCCCCCCC		19.7423312004
432PhosphorylationSSMTSHGSSHTSGVE
CCCCCCCCCCCCCCC		17.3323312004
433PhosphorylationSMTSHGSSHTSGVES
CCCCCCCCCCCCCCC		35.0627794612
435PhosphorylationTSHGSSHTSGVESGG
CCCCCCCCCCCCCCC		29.1725002506
436PhosphorylationSHGSSHTSGVESGGK
CCCCCCCCCCCCCCC		35.1025002506
440PhosphorylationSHTSGVESGGKDRLE
CCCCCCCCCCCCCCC		50.9030576142
497PhosphorylationSRKLNGHSGLIVKEI
HCCCCCCCCEEEEEE		36.3725849741
506PhosphorylationLIVKEIGSSTSSSSE
EEEEEECCCCCCCCC		35.7825849741
507PhosphorylationIVKEIGSSTSSSSET
EEEEECCCCCCCCCE		27.3929255136
508PhosphorylationVKEIGSSTSSSSETV
EEEECCCCCCCCCEE		34.0329255136
509PhosphorylationKEIGSSTSSSSETVV
EEECCCCCCCCCEEE		30.1229255136
509UbiquitinationKEIGSSTSSSSETVV
EEECCCCCCCCCEEE		30.1229967540
510PhosphorylationEIGSSTSSSSETVVK
EECCCCCCCCCEEEE		37.6629255136
511PhosphorylationIGSSTSSSSETVVKL
ECCCCCCCCCEEEEE		31.7729255136
512PhosphorylationGSSTSSSSETVVKLR
CCCCCCCCCEEEEEC		38.9529255136
514PhosphorylationSTSSSSETVVKLRGQ
CCCCCCCEEEEECCC		32.3329255136
517PhosphorylationSSSETVVKLRGQSTD
CCCCEEEEECCCCCC		28.2933259812
517UbiquitinationSSSETVVKLRGQSTD
CCCCEEEEECCCCCC		28.2929967540
522PhosphorylationVVKLRGQSTDSLPQT
EEEECCCCCCCCCHH		36.6930266825
523PhosphorylationVKLRGQSTDSLPQTI
EEECCCCCCCCCHHH		23.0130266825
525PhosphorylationLRGQSTDSLPQTICR
ECCCCCCCCCHHHCC		41.8830266825
529PhosphorylationSTDSLPQTICRKPKT
CCCCCCHHHCCCCCC		21.8030266825
536PhosphorylationTICRKPKTSTDRHSL
HHCCCCCCCCCCCCC		45.4430266825
537PhosphorylationICRKPKTSTDRHSLS
HCCCCCCCCCCCCCC		34.1430266825
538PhosphorylationCRKPKTSTDRHSLSL
CCCCCCCCCCCCCCH		42.1430266825
542PhosphorylationKTSTDRHSLSLDDIR
CCCCCCCCCCHHHHH		22.1330266825
544PhosphorylationSTDRHSLSLDDIRLY
CCCCCCCCHHHHHHH		32.5429255136
545UbiquitinationTDRHSLSLDDIRLYQ
CCCCCCCHHHHHHHH		9.2223000965
551PhosphorylationSLDDIRLYQKDFLRI
CHHHHHHHHHHHHHH		12.0323312004
553UbiquitinationDDIRLYQKDFLRIAG
HHHHHHHHHHHHHHH		36.5723000965
568PhosphorylationLCQDTAQSYTFGCGH
CCHHCHHHCCCCCCC		24.5528348404
570PhosphorylationQDTAQSYTFGCGHEL
HHCHHHCCCCCCCCC		20.8528348404
607PhosphorylationPVKRTSKYFSLDLTH
CCCCCCCCEEEECCC		9.7327732954
609PhosphorylationKRTSKYFSLDLTHDE
CCCCCCEEEECCCCC		20.2028387310
613PhosphorylationKYFSLDLTHDEVPEF
CCEEEECCCCCCCCC		27.2629514088
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 FRMD6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FRMD6_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 FRMD6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUV91_HUMANSUV39H1physical
23455924
CX6B2_HUMANCOX6B2physical
25416956
ASPP2_HUMANTP53BP2physical
26186194
RASF8_HUMANRASSF8physical
26186194
SNX17_HUMANSNX17physical
26186194
RASF7_HUMANRASSF7physical
26186194
1433B_HUMANYWHABphysical
24366813
1433F_HUMANYWHAHphysical
24366813
1433G_HUMANYWHAGphysical
24366813
1433T_HUMANYWHAQphysical
24366813
HTF4_HUMANTCF12physical
21516116
RASF8_HUMANRASSF8physical
28514442
ASPP2_HUMANTP53BP2physical
28514442
RASF7_HUMANRASSF7physical
28514442
SNX17_HUMANSNX17physical
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 FRMD6_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-544, AND MASSSPECTROMETRY.
"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-544, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-412, AND MASSSPECTROMETRY.

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