FGD1_HUMAN - dbPTM
FGD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FGD1_HUMAN
UniProt AC P98174
Protein Name FYVE, RhoGEF and PH domain-containing protein 1
Gene Name FGD1
Organism Homo sapiens (Human).
Sequence Length 961
Subcellular Localization Cytoplasm. Cell projection, lamellipodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Associated with membrane ruffles and lamellipodia..
Protein Description Activates 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..
Protein Sequence MHGHRAPGGAGPSEPEHPATNPPGAAPPACADSDPGASEPGLLARRGSGSALGGPLDPQFVGPSDTSLGAAPGHRVLPCGPSPQHHRALRFSYHLEGSQPRPGLHQGNRILVKSLSLDPGQSLEPHPEGPQRLRSDPGPPTETPSQRPSPLKRAPGPKPQVPPKPSYLQMPRMPPPLEPIPPPPSRPLPADPRVAKGLAPRAEASPSSAAVSSLIEKFEREPVIVASDRPVPGPSPGPPEPVMLPQPTSQPPVPQLPEGEASRCLFLLAPGPRDGEKVPNRDSGIDSISSPSNSEETCFVSDDGPPSHSLCPGPPALASVPVALADPHRPGSQEVDSDLEEEDDEEEEEEKDREIPVPLMERQESVELTVQQKVFHIANELLQTEKAYVSRLHLLDQVFCARLLEEARNRSSFPADVVHGIFSNICSIYCFHQQFLLPELEKRMEEWDRYPRIGDILQKLAPFLKMYGEYVKNFDRAVELVNTWTERSTQFKVIIHEVQKEEACGNLTLQHHMLEPVQRIPRYELLLKDYLLKLPHGSPDSKDAQKSLELIATAAEHSNAAIRKMERMHKLLKVYELLGGEEDIVSPTKELIKEGHILKLSAKNGTTQDRYLILFNDRLLYCVPRLRLLGQKFSVRARIDVDGMELKESSNLNLPRTFLVSGKQRSLELQARTEEEKKDWVQAINSTLLKHEQTLETFKLLNSTNREDEDTPPNSPNVDLGKRAPTPIREKEVTMCMRCQEPFNSITKRRHHCKACGHVVCGKCSEFRARLVYDNNRSNRVCTDCYVALHGVPGSSPACSQHTPQRRRSILEKQASVAAENSVICSFLHYMEKGGKGWHKAWFVVPENEPLVLYIYGAPQDVKAQRSLPLIGFEVGPPEAGERPDRRHVFKITQSHLSWYFSPETEELQRRWMAVLGRAGRGDTFCPGPTLSEDREMEEAPVAALGATAEPPESPQTRDKT
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
46MethylationEPGLLARRGSGSALG
CCCCCCCCCCCCCCC		37.71-
48PhosphorylationGLLARRGSGSALGGP
CCCCCCCCCCCCCCC		27.9729255136
50PhosphorylationLARRGSGSALGGPLD
CCCCCCCCCCCCCCC		23.2429255136
64PhosphorylationDPQFVGPSDTSLGAA
CHHHCCCCCCCCCCC		47.8223927012
66PhosphorylationQFVGPSDTSLGAAPG
HHCCCCCCCCCCCCC		30.1327251275
67PhosphorylationFVGPSDTSLGAAPGH
HCCCCCCCCCCCCCC		29.7827251275
82PhosphorylationRVLPCGPSPQHHRAL
CEECCCCCHHHHCHH		23.6030266825
90MethylationPQHHRALRFSYHLEG
HHHHCHHHEEEECCC		19.92-
92PhosphorylationHHRALRFSYHLEGSQ
HHCHHHEEEECCCCC		12.7629978859
93PhosphorylationHRALRFSYHLEGSQP
HCHHHEEEECCCCCC		14.0129978859
98PhosphorylationFSYHLEGSQPRPGLH
EEEECCCCCCCCCCC		27.8629978859
101MethylationHLEGSQPRPGLHQGN
ECCCCCCCCCCCCCC		30.22-
109MethylationPGLHQGNRILVKSLS
CCCCCCCEEEEEEEE		30.37-
114PhosphorylationGNRILVKSLSLDPGQ
CCEEEEEEEECCCCC		18.7330266825
116PhosphorylationRILVKSLSLDPGQSL
EEEEEEEECCCCCCC		37.5129255136
122PhosphorylationLSLDPGQSLEPHPEG
EECCCCCCCCCCCCC		40.3823403867
135PhosphorylationEGPQRLRSDPGPPTE
CCCCCCCCCCCCCCC		53.3930266825
141PhosphorylationRSDPGPPTETPSQRP
CCCCCCCCCCCCCCC		56.4727732954
143PhosphorylationDPGPPTETPSQRPSP
CCCCCCCCCCCCCCC		30.6227732954
145PhosphorylationGPPTETPSQRPSPLK
CCCCCCCCCCCCCCC		46.3629978859
149PhosphorylationETPSQRPSPLKRAPG
CCCCCCCCCCCCCCC		45.0821712546
205PhosphorylationLAPRAEASPSSAAVS
CCCCCCCCCCHHHHH		19.4721712546
207PhosphorylationPRAEASPSSAAVSSL
CCCCCCCCHHHHHHH		30.0721815630
208PhosphorylationRAEASPSSAAVSSLI
CCCCCCCHHHHHHHH		24.5129396449
212PhosphorylationSPSSAAVSSLIEKFE
CCCHHHHHHHHHHHH		18.0720393185
213PhosphorylationPSSAAVSSLIEKFER
CCHHHHHHHHHHHHC		27.1124719451
235PhosphorylationDRPVPGPSPGPPEPV
CCCCCCCCCCCCCCC		48.6925850435
365PhosphorylationPLMERQESVELTVQQ
CHHCCHHHEEEEHHH		16.7422617229
369PhosphorylationRQESVELTVQQKVFH
CHHHEEEEHHHHHHH		11.6328102081
459UbiquitinationRIGDILQKLAPFLKM
CHHHHHHHHHHHHHH		43.07-
528UbiquitinationPRYELLLKDYLLKLP
CHHHHHHHHHHHHCC		44.27-
542UbiquitinationPHGSPDSKDAQKSLE
CCCCCCCHHHHHHHH		65.54-
547PhosphorylationDSKDAQKSLELIATA
CCHHHHHHHHHHHHH		18.2624719451
553PhosphorylationKSLELIATAAEHSNA
HHHHHHHHHHHHHHH		21.29-
558PhosphorylationIATAAEHSNAAIRKM
HHHHHHHHHHHHHHH		21.4824719451
575PhosphorylationMHKLLKVYELLGGEE
HHHHHHHHHHHCCCC		10.1627642862
586PhosphorylationGGEEDIVSPTKELIK
CCCCCCCCCCHHHHH		27.4722199227
588PhosphorylationEEDIVSPTKELIKEG
CCCCCCCCHHHHHHC		29.6420068231
589UbiquitinationEDIVSPTKELIKEGH
CCCCCCCHHHHHHCC		54.64-
593UbiquitinationSPTKELIKEGHILKL
CCCHHHHHHCCEEEE		70.98-
599UbiquitinationIKEGHILKLSAKNGT
HHHCCEEEEEECCCC		39.53-
621PhosphorylationLFNDRLLYCVPRLRL
EECCHHHHHHHHHHH		8.9421945579
649PhosphorylationDGMELKESSNLNLPR
CCCEECCCCCCCCCC		23.9620068231
650PhosphorylationGMELKESSNLNLPRT
CCEECCCCCCCCCCE		46.5626471730
663UbiquitinationRTFLVSGKQRSLELQ
CEEEECCCHHHHHHH		34.72-
699UbiquitinationEQTLETFKLLNSTNR
HHHHHHHHHHHCCCC		60.53-
703PhosphorylationETFKLLNSTNREDED
HHHHHHHCCCCCCCC		27.3330266825
704PhosphorylationTFKLLNSTNREDEDT
HHHHHHCCCCCCCCC		36.9030266825
711PhosphorylationTNREDEDTPPNSPNV
CCCCCCCCCCCCCCC		38.3030266825
715PhosphorylationDEDTPPNSPNVDLGK
CCCCCCCCCCCCCCC		24.5130278072
726PhosphorylationDLGKRAPTPIREKEV
CCCCCCCCCCCHHHE		30.2929514088
745PhosphorylationRCQEPFNSITKRRHH
CCCCCCCHHHCCCHH		31.8225850435
747PhosphorylationQEPFNSITKRRHHCK
CCCCCHHHCCCHHCC		20.5125850435
795PhosphorylationALHGVPGSSPACSQH
ECCCCCCCCHHHHCC		27.3821712546
796PhosphorylationLHGVPGSSPACSQHT
CCCCCCCCHHHHCCC		23.5621712546
800PhosphorylationPGSSPACSQHTPQRR
CCCCHHHHCCCHHHH		27.4021712546
803PhosphorylationSPACSQHTPQRRRSI
CHHHHCCCHHHHHHH		17.3021712546
809PhosphorylationHTPQRRRSILEKQAS
CCHHHHHHHHHHHHH		29.7024719451
816PhosphorylationSILEKQASVAAENSV
HHHHHHHHHHHHHHH		15.1422199227
822PhosphorylationASVAAENSVICSFLH
HHHHHHHHHHHHHHH		12.3629083192
948PhosphorylationPVAALGATAEPPESP
CCHHCCCCCCCCCCC		29.7429978859
954PhosphorylationATAEPPESPQTRDKT
CCCCCCCCCCCCCCC		28.2530576142
957PhosphorylationEPPESPQTRDKT---
CCCCCCCCCCCC---		44.1925850435
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
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FGD1_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 FGD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VKGC_HUMANGGCXphysical
26496610
STX3_HUMANSTX3physical
26496610
TAP2_HUMANTAP2physical
26496610
PITM1_HUMANPITPNM1physical
26496610
SPD2A_HUMANSH3PXD2Aphysical
26496610
INT7_HUMANINTS7physical
26496610
RM18_HUMANMRPL18physical
26496610
FXL19_HUMANFBXL19physical
26496610
ESYT2_HUMANESYT2physical
26496610
MILK2_HUMANMICALL2physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
305400Aarskog-Scott syndrome (AAS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FGD1_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-48; SER-205; THR-704;THR-711 AND SER-715, AND MASS SPECTROMETRY.

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