FGD3_HUMAN - dbPTM
FGD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FGD3_HUMAN
UniProt AC Q5JSP0
Protein Name FYVE, RhoGEF and PH domain-containing protein 3
Gene Name FGD3
Organism Homo sapiens (Human).
Sequence Length 725
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton .
Protein Description Promotes the formation of filopodia. May activate CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape (By similarity)..
Protein Sequence MESGRGSSTPPGPIAALGMPDTGPGSSSLGKLQALPVGPRAHCGDPVSLAAAGDGSPDIGPTGELSGSLKIPNRDSGIDSPSSSVAGENFPCEEGLEAGPSPTVLGAHAEMALDSQVPKVTPQEEADSDVGEEPDSENTPQKADKDAGLAQHSGPQKLLHIAQELLHTEETYVKRLHLLDQVFCTRLTDAGIPPEVIMGIFSNISSIHRFHGQFLLPELKTRITEEWDTNPRLGDILQKLAPFLKMYGEYVKNFDRAVGLVSTWTQRSPLFKDVVHSIQKQEVCGNLTLQHHMLEPVQRVPRYELLLKDYLKRLPQDAPDRKDAERSLELISTAANHSNAAIRKVEKMHKLLEVYEQLGGEEDIVNPANELIKEGQIQKLSAKNGTPQDRHLFLFNSMILYCVPKLRLMGQKFSVREKMDISGLQVQDIVKPNTAHTFIITGRKRSLELQTRTEEEKKEWIQIIQATIEKHKQNSETFKAFGGAFSQDEDPSLSPDMPITSTSPVEPVVTTEGSSGAAGLEPRKLSSKTRRDKEKQSCKSCGETFNSITKRRHHCKLCGAVICGKCSEFKAENSRQSRVCRDCFLTQPVAPESTEKTPTADPQPSLLCGPLRLSESGETWSEVWAAIPMSDPQVLHLQGGSQDGRLPRTIPLPSCKLSVPDPEERLDSGHVWKLQWAKQSWYLSASSAELQQQWLETLSTAAHGDTAQDSPGALQLQVPMGAAAP
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
3Phosphorylation-----MESGRGSSTP
-----CCCCCCCCCC		32.2726074081
7Phosphorylation-MESGRGSSTPPGPI
-CCCCCCCCCCCCCC		29.6723401153
8PhosphorylationMESGRGSSTPPGPIA
CCCCCCCCCCCCCCC		48.0030576142
9PhosphorylationESGRGSSTPPGPIAA
CCCCCCCCCCCCCCC		34.8928348404
22PhosphorylationAALGMPDTGPGSSSL
CCCCCCCCCCCCCCC		39.1326074081
26PhosphorylationMPDTGPGSSSLGKLQ
CCCCCCCCCCCCCEE		21.6426074081
27PhosphorylationPDTGPGSSSLGKLQA
CCCCCCCCCCCCEEE		35.1826074081
28PhosphorylationDTGPGSSSLGKLQAL
CCCCCCCCCCCEEEC		42.7226074081
48PhosphorylationAHCGDPVSLAAAGDG
CCCCCCCHHHCCCCC		20.0626552605
56PhosphorylationLAAAGDGSPDIGPTG
HHCCCCCCCCCCCCC		24.9223401153
62PhosphorylationGSPDIGPTGELSGSL
CCCCCCCCCCCCCCE		37.7730108239
66PhosphorylationIGPTGELSGSLKIPN
CCCCCCCCCCEECCC		23.2526552605
68PhosphorylationPTGELSGSLKIPNRD
CCCCCCCCEECCCCC		24.1026552605
76PhosphorylationLKIPNRDSGIDSPSS
EECCCCCCCCCCCCC		34.1226074081
80PhosphorylationNRDSGIDSPSSSVAG
CCCCCCCCCCCCCCC		25.4326074081
82PhosphorylationDSGIDSPSSSVAGEN
CCCCCCCCCCCCCCC		38.9226074081
83PhosphorylationSGIDSPSSSVAGENF
CCCCCCCCCCCCCCC		32.0126074081
84PhosphorylationGIDSPSSSVAGENFP
CCCCCCCCCCCCCCC		21.9630576142
101PhosphorylationEGLEAGPSPTVLGAH
CCCCCCCCCCCCCHH		32.0826074081
103PhosphorylationLEAGPSPTVLGAHAE
CCCCCCCCCCCHHHH		32.4726074081
115PhosphorylationHAEMALDSQVPKVTP
HHHHHHHCCCCCCCC		33.6522468782
121PhosphorylationDSQVPKVTPQEEADS
HCCCCCCCCHHHHCC		25.9430278072
128PhosphorylationTPQEEADSDVGEEPD
CCHHHHCCCCCCCCC		41.0423401153
136PhosphorylationDVGEEPDSENTPQKA
CCCCCCCCCCCCCHH		43.3830576142
139PhosphorylationEEPDSENTPQKADKD
CCCCCCCCCCHHHHH		24.0528450419
145UbiquitinationNTPQKADKDAGLAQH
CCCCHHHHHCCHHHH		55.10-
157UbiquitinationAQHSGPQKLLHIAQE
HHHCHHHHHHHHHHH		57.03-
174UbiquitinationHTEETYVKRLHLLDQ
CCCCHHHHHHHHHHH		38.54-
220UbiquitinationQFLLPELKTRITEEW
CCCCHHHHHHCCCCC		33.81-
220UbiquitinationQFLLPELKTRITEEW
CCCCHHHHHHCCCCC		33.81-
239UbiquitinationRLGDILQKLAPFLKM
CHHHHHHHHHHHHHH		43.07-
239UbiquitinationRLGDILQKLAPFLKM
CHHHHHHHHHHHHHH		43.07-
308UbiquitinationPRYELLLKDYLKRLP
CHHHHHHHHHHHCCC		44.27-
308UbiquitinationPRYELLLKDYLKRLP
CHHHHHHHHHHHCCC		44.27-
327PhosphorylationDRKDAERSLELISTA
CHHHHHHHHHHHHHH		20.0824247654
355PhosphorylationMHKLLEVYEQLGGEE
HHHHHHHHHHHCCCC		6.6523879269
379UbiquitinationIKEGQIQKLSAKNGT
HHHCCHHHHHHCCCC		46.14-
379UbiquitinationIKEGQIQKLSAKNGT
HHHCCHHHHHHCCCC		46.14-
397PhosphorylationRHLFLFNSMILYCVP
CHHHHHHHHHHHHHH		10.4019835603
401PhosphorylationLFNSMILYCVPKLRL
HHHHHHHHHHHHHHH		4.7719835603
412UbiquitinationKLRLMGQKFSVREKM
HHHHCCCCCCCHHCC		33.60-
414PhosphorylationRLMGQKFSVREKMDI
HHCCCCCCCHHCCCC		27.57-
446PhosphorylationIITGRKRSLELQTRT
EEECCCCEEECCCCC		29.2728857561
486PhosphorylationKAFGGAFSQDEDPSL
HHHCCCCCCCCCCCC		35.8729802988
492PhosphorylationFSQDEDPSLSPDMPI
CCCCCCCCCCCCCCC		54.5228348404
494PhosphorylationQDEDPSLSPDMPITS
CCCCCCCCCCCCCCC		24.1628348404
500PhosphorylationLSPDMPITSTSPVEP
CCCCCCCCCCCCCCC		21.7826074081
501PhosphorylationSPDMPITSTSPVEPV
CCCCCCCCCCCCCCE		27.8426074081
502PhosphorylationPDMPITSTSPVEPVV
CCCCCCCCCCCCCEE		28.5326074081
503PhosphorylationDMPITSTSPVEPVVT
CCCCCCCCCCCCEEE		27.0726074081
510PhosphorylationSPVEPVVTTEGSSGA
CCCCCEEECCCCCCC		21.2626074081
511PhosphorylationPVEPVVTTEGSSGAA
CCCCEEECCCCCCCC		27.0926074081
514PhosphorylationPVVTTEGSSGAAGLE
CEEECCCCCCCCCCC		21.2626074081
515PhosphorylationVVTTEGSSGAAGLEP
EEECCCCCCCCCCCH		43.2226074081
526PhosphorylationGLEPRKLSSKTRRDK
CCCHHCCCCCCCCHH		32.5926074081
527PhosphorylationLEPRKLSSKTRRDKE
CCHHCCCCCCCCHHH		48.7826074081
529PhosphorylationPRKLSSKTRRDKEKQ
HHCCCCCCCCHHHHH		32.6526074081
533AcetylationSSKTRRDKEKQSCKS
CCCCCCHHHHHHHHH		66.0720167786
540PhosphorylationKEKQSCKSCGETFNS
HHHHHHHHHHHHHHH		31.5126552605
544PhosphorylationSCKSCGETFNSITKR
HHHHHHHHHHHHHHC		17.2530108239
547PhosphorylationSCGETFNSITKRRHH
HHHHHHHHHHHCHHH		27.6930576142
549PhosphorylationGETFNSITKRRHHCK
HHHHHHHHHCHHHHC		20.5127794612
550AcetylationETFNSITKRRHHCKL
HHHHHHHHCHHHHCC		45.8520167786
586PhosphorylationVCRDCFLTQPVAPES
CCHHHCCCCCCCCCC		15.5824114839
593PhosphorylationTQPVAPESTEKTPTA
CCCCCCCCCCCCCCC		40.5823312004
594PhosphorylationQPVAPESTEKTPTAD
CCCCCCCCCCCCCCC		39.5823312004
597PhosphorylationAPESTEKTPTADPQP
CCCCCCCCCCCCCCC		21.4626552605
599PhosphorylationESTEKTPTADPQPSL
CCCCCCCCCCCCCCE		49.2623312004
605PhosphorylationPTADPQPSLLCGPLR
CCCCCCCCEEEEEEE		28.8223312004
656UbiquitinationTIPLPSCKLSVPDPE
CCCCCCCEEECCCHH		48.40-
658PhosphorylationPLPSCKLSVPDPEER
CCCCCEEECCCHHHH		19.6622617229
673UbiquitinationLDSGHVWKLQWAKQS
CCCCCEEEEHHHHHH		29.70-
710PhosphorylationHGDTAQDSPGALQLQ
CCCCCCCCCCCEEEE		17.1026074081
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
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:24658274
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FGD3_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 FGD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FGD3_HUMAN !!
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 FGD3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9 AND SER-128, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND MASSSPECTROMETRY.

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