FGD6_MOUSE - dbPTM
FGD6_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FGD6_MOUSE
UniProt AC Q69ZL1
Protein Name FYVE, RhoGEF and PH domain-containing protein 6
Gene Name Fgd6
Organism Mus musculus (Mouse).
Sequence Length 1399
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton .
Protein Description May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a role in regulating the actin cytoskeleton and cell shape (By similarity)..
Protein Sequence MTSAAELKKPPLAPKPKLVGTNNKPPPPPIAPKPDIGSASVPRLTKKTKPAIAPKPKVPTNSVVQDIKHPPSKKPTLNLEEREPELPESTGKSNCKDVRDPHSDYILPTCSCSSGCIHEPRTRETQCVEQLVLEPLGMKENLENSKNGESSKRGSSWDSSSEKCRGQSGVVLKASILEEKLKEVLTQQRSPCGSPGRHRAPKKPEMNGDHSCTRQIRIEFADVSSSLTGFEKVPAHHNCHPQLPRDESQTLKTCQDGSAESRGHTDSCEPENKRVASDGISQKTEVKGLGPLEIHLLPYTSKFPTPKPRKTHAAARLRRQKHVDTPGESTEEPGNSNNGSSCLLEDYCLKNNKVSVLRQNALYNQGPVDEVRPANQRALTGDSNSGGQDSVGSQKAVQQQTPSLDTDSSLTSDSSGSGVSPAVDKETTYTQCSTQPLSLPKQVTSACTDQPPATCNPEVSAPPIQKESSSSRIIPKKPQRHSLPAAGVLKKAASEELVEKSSSGKETNVEKGLHRNYLHHPGPPNHGASASPFDMPNPTSEKPVWKLPHPILPFSGSPEALKRVTLSLNNEPSVSLTKPRAKSLSAVDADRCNKPCKDPPKKTSFKKLINVKLSIGFIKSDFQKIRSKSCQHGDVSAGHPLAREPKGLESDWQGLATGEEKRSKPTKAHSAENCSLESQKVKSWGQSSAVNGQRAESLDDRILSRHTSCTGDFGPEYENVRHYEEIPEYENLPFVMAGRNTPDLGWQNSSSVEDTDASLYEVEEPYNAPDGQLQLDPRHQPCSSGTSQEGKDALHLGLSDLPSDEEVINSSDEDDVSSESSKGEPDPLEDKQDEDAGMKSKVHHIAKEIMSSEKVFVDVLKLLHIDFRGAVAHASRQLGKPVIEDRILNQILYYLPQLYELNRDLLKELEERMLTWTEQQRIADIFVKKGPYLKMYSTYIKEFDKNVALLDEQCKKNPGFAAVVREFEMSPRCANLALKHYLLKPVQRIPQYRLLLTDYLKNLLEDSVDHRDTQDALAVVIEVANHANDTMKQGDNFQKLMQIQYSLSGHHEIVQPGRVFLKEGTLMKLSRKVMQPRMFFLFNDALLYTTPMQSGMYKLNNMLSLAGMKVRKPTQEAYQNELKIESVERSFILSASSAAERDDWLEAISSSIEEYAKKRITFCPSRSLDEDSERKEEVSPLGAKAPIWIPDTRATMCMICTSEFTLTWRRHHCRACGKIVCQACSSNKYGLDYLKGQLARVCEHCFQELQKLDHQLSPRVGSPGNHKSPSSALSSVLHSIPSGRKQKKIPAALKEVSANTEDSTMSGYLYRSKGSKKPWKHLWFVIKNKVLYTYAASEDVAALESQPLLGFTVTLVKDENSESKVFQLLHKGMVFYVFKADDAHSTQRWIDAFQEGTVL
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------MTSAAELKK
------CCCHHHHCC		38.0827149854
3Phosphorylation-----MTSAAELKKP
-----CCCHHHHCCC		37.0227149854
156PhosphorylationESSKRGSSWDSSSEK
CCCCCCCCCCCCCCC		37.41-
159PhosphorylationKRGSSWDSSSEKCRG
CCCCCCCCCCCCCCC		29.52-
160PhosphorylationRGSSWDSSSEKCRGQ
CCCCCCCCCCCCCCC		39.79-
190PhosphorylationEVLTQQRSPCGSPGR
HHHHCCCCCCCCCCC		21.8723970565
194PhosphorylationQQRSPCGSPGRHRAP
CCCCCCCCCCCCCCC		30.7923384938
311PhosphorylationPTPKPRKTHAAARLR
CCCCCCCCHHHHHHH		20.3022817900
380PhosphorylationPANQRALTGDSNSGG
CCCCCCCCCCCCCCC		37.6527149854
403PhosphorylationAVQQQTPSLDTDSSL
HHHHCCCCCCCCCCC		42.1227841257
482PhosphorylationPKKPQRHSLPAAGVL
CCCCCCCCCCHHHHH		37.9329899451
494PhosphorylationGVLKKAASEELVEKS
HHHHHHHCHHHHHHH		36.1425521595
531PhosphorylationPNHGASASPFDMPNP
CCCCCCCCCCCCCCC		24.49-
555PhosphorylationPHPILPFSGSPEALK
CCCCCCCCCCHHHHH		36.1026824392
557PhosphorylationPILPFSGSPEALKRV
CCCCCCCCHHHHHHE		20.5425521595
567PhosphorylationALKRVTLSLNNEPSV
HHHHEEEECCCCCCC		21.4927841257
583PhosphorylationLTKPRAKSLSAVDAD
CCCCCCCCCCCCCHH		26.9425521595
585PhosphorylationKPRAKSLSAVDADRC
CCCCCCCCCCCHHHC		33.0823737553
604PhosphorylationKDPPKKTSFKKLINV
CCCCCCCCHHHHHCC		43.9028059163
607AcetylationPKKTSFKKLINVKLS
CCCCCHHHHHCCEEE		53.2224062335
629PhosphorylationFQKIRSKSCQHGDVS
HHHHHCCCCCCCCCC		21.9125266776
636PhosphorylationSCQHGDVSAGHPLAR
CCCCCCCCCCCCCCC		33.0229550500
670PhosphorylationSKPTKAHSAENCSLE
CCCCCCCCCCCCCCC		41.9825521595
697PhosphorylationVNGQRAESLDDRILS
HCCCCCCCHHHHHHH		35.7923984901
707PhosphorylationDRILSRHTSCTGDFG
HHHHHHCCCCCCCCC		25.1225367039
708PhosphorylationRILSRHTSCTGDFGP
HHHHHCCCCCCCCCC		11.9827149854
717PhosphorylationTGDFGPEYENVRHYE
CCCCCCCCCCCCCHH		18.8825367039
729PhosphorylationHYEEIPEYENLPFVM
CHHCCCCCCCCCEEE		12.5525367039
787PhosphorylationQPCSSGTSQEGKDAL
CCCCCCCCCCHHCCE		29.7529899451
1090PhosphorylationNDALLYTTPMQSGMY
CCEEECCCCCCCCCH		11.8222817900
1094PhosphorylationLYTTPMQSGMYKLNN
ECCCCCCCCCHHHHH		21.1921183079
1109UbiquitinationMLSLAGMKVRKPTQE
HHHHCCCCCCCCCHH		37.6622790023
1161PhosphorylationEYAKKRITFCPSRSL
HHHHHHCCCCCCCCC		24.1830635358
1165PhosphorylationKRITFCPSRSLDEDS
HHCCCCCCCCCCCCH		35.3620469934
1167PhosphorylationITFCPSRSLDEDSER
CCCCCCCCCCCCHHC		44.5027818261
1172PhosphorylationSRSLDEDSERKEEVS
CCCCCCCHHCHHHCC		36.9320531401
1179PhosphorylationSERKEEVSPLGAKAP
HHCHHHCCCCCCCCC		20.0728066266
1257PhosphorylationQKLDHQLSPRVGSPG
HHCCCCCCCCCCCCC		12.2327841257
1262PhosphorylationQLSPRVGSPGNHKSP
CCCCCCCCCCCCCCH		27.1227841257
1268PhosphorylationGSPGNHKSPSSALSS
CCCCCCCCHHHHHHH		23.5921454597
1270PhosphorylationPGNHKSPSSALSSVL
CCCCCCHHHHHHHHH		35.0221454597
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 FGD6_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FGD6_MOUSE !!
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 FGD6_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FGD6_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FGD6_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, AND MASSSPECTROMETRY.

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