CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013678
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 FYVE, RhoGEF and PH domain-containing protein 3 
Protein Synonyms/Alias
 Zinc finger FYVE domain-containing protein 5 
Gene Name
 FGD3 
Gene Synonyms/Alias
 ZFYVE5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
220QFLLPELKTRITEEWubiquitination[1]
239RLGDILQKLAPFLKMubiquitination[1]
308PRYELLLKDYLKRLPubiquitination[1]
379IKEGQIQKLSAKNGTubiquitination[1]
412KLRLMGQKFSVREKMubiquitination[1]
533SSKTRRDKEKQSCKSacetylation[2]
550ETFNSITKRRHHCKLacetylation[2]
656TIPLPSCKLSVPDPEubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional 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). 
Sequence Annotation
 DOMAIN 157 341 DH.
 DOMAIN 370 469 PH 1.
 DOMAIN 604 703 PH 2.
 ZN_FING 532 588 FYVE-type.
 MOD_RES 128 128 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 725 AA 
Protein Sequence
MESGRGSSTP PGPIAALGMP DTGPGSSSLG KLQALPVGPR AHCGDPVSLA AAGDGSPDIG 60
PTGELSGSLK IPNRDSGIDS PSSSVAGENF PCEEGLEAGP SPTVLGAHAE MALDSQVPKV 120
TPQEEADSDV GEEPDSENTP QKADKDAGLA QHSGPQKLLH IAQELLHTEE TYVKRLHLLD 180
QVFCTRLTDA GIPPEVIMGI FSNISSIHRF HGQFLLPELK TRITEEWDTN PRLGDILQKL 240
APFLKMYGEY VKNFDRAVGL VSTWTQRSPL FKDVVHSIQK QEVCGNLTLQ HHMLEPVQRV 300
PRYELLLKDY LKRLPQDAPD RKDAERSLEL ISTAANHSNA AIRKVEKMHK LLEVYEQLGG 360
EEDIVNPANE LIKEGQIQKL SAKNGTPQDR HLFLFNSMIL YCVPKLRLMG QKFSVREKMD 420
ISGLQVQDIV KPNTAHTFII TGRKRSLELQ TRTEEEKKEW IQIIQATIEK HKQNSETFKA 480
FGGAFSQDED PSLSPDMPIT STSPVEPVVT TEGSSGAAGL EPRKLSSKTR RDKEKQSCKS 540
CGETFNSITK RRHHCKLCGA VICGKCSEFK AENSRQSRVC RDCFLTQPVA PESTEKTPTA 600
DPQPSLLCGP LRLSESGETW SEVWAAIPMS DPQVLHLQGG SQDGRLPRTI PLPSCKLSVP 660
DPEERLDSGH VWKLQWAKQS WYLSASSAEL QQQWLETLST AAHGDTAQDS PGALQLQVPM 720
GAAAP 725 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
 GO:0031267; F:small GTPase binding; ISS:UniProtKB.
 GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
 GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
 GO:0046847; P:filopodium assembly; ISS:UniProtKB.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0043088; P:regulation of Cdc42 GTPase activity; ISS:UniProtKB.
 GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. 
Interpro
 IPR000219; DH-domain.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR000306; Znf_FYVE.
 IPR017455; Znf_FYVE-rel.
 IPR011011; Znf_FYVE_PHD.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF01363; FYVE
 PF00169; PH
 PF00621; RhoGEF 
SMART
 SM00064; FYVE
 SM00233; PH
 SM00325; RhoGEF 
PROSITE
 PS50010; DH_2
 PS50003; PH_DOMAIN
 PS50178; ZF_FYVE 
PRINTS