CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015509
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 FYVE, RhoGEF and PH domain-containing protein 5 
Protein Synonyms/Alias
 Zinc finger FYVE domain-containing protein 23 
Gene Name
 FGD5 
Gene Synonyms/Alias
 ZFYVE23 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
729LIFYRDGKRKGVPFSacetylation[1]
975SNWESQQKVADVFLAubiquitination[2]
1033QGGSQTAKHRLLRVVubiquitination[2]
1116QPGREFLKEGTLMKVubiquitination[2]
1122LKEGTLMKVTGKNRRubiquitination[2]
1154KDGKYRLKNTLAVANubiquitination[2]
1301DGCFGELKKRGRAVPubiquitination[2]
1346INPSTFKKQKKVPSAubiquitination[2]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Mediates VEGF-induced CDC42 activation. May regulate proangiogenic action of VEGF in vascular endothelial cells, including network formation, directional movement and proliferation. May play a role in regulating the actin cytoskeleton and cell shape. 
Sequence Annotation
 DOMAIN 892 1084 DH.
 DOMAIN 1113 1207 PH 1.
 DOMAIN 1363 1461 PH 2.
 ZN_FING 1242 1301 FYVE-type.
 MOD_RES 632 632 Phosphoserine (By similarity).
 MOD_RES 635 635 Phosphoserine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Endoplasmic reticulum; Endosome; Golgi apparatus; Guanine-nucleotide releasing factor; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1462 AA 
Protein Sequence
MFRGPKPPIA PKPRLTAPNE WRASVYLNDS LNKCSNGRLP CVDRGLDEGP RSIPKCSESE 60
TDEDYIVVPR VPLREDEPKD EGSVGNKALV SPESSAEEEE EREEGGEACG LEGTGAGEDS 120
VAPAAPGAGA LSREGEEGTD LALEDEGEGC ADEPGTLEQV SRSEEEEKLV QPHRECSLED 180
SGPWAGEGVF QSDLLLPHIH GEDQEPPDTP GEAEEDDEEG CASTDPAGAD EGSGPDRPTE 240
DMGQDAEDTS EEPPEKEELA GVQEAETATD CPEVLEEGCE EATGVTGGEQ VDLSEPPDHE 300
KKTNQEVAAA TLEDHAQDES AEESCQIVPF ENDCMEDFVT SLTGSPYEFF PTESTSFCSE 360
SCSPLSESAK GLESEQAPKL GLRAEENPMV GALCGQCGSL QGGAAEGPAA PDVVVVLEEE 420
ALDDALANPY VMGVGLPGQA APGEGGQAAS DALGGYGSKE ELNCEAEGGL VPADRKNTST 480
RVRPHSGKVA GYVPETVPEE TGPEAGSSAP GIGGAAEEVG KTLLSLEGKP LEASRALPAK 540
PRAFTLYPRS FSVEGREIPV SVYQEPEGSG LDDHRIKRKE DNLSLSCVIG SSGSFSQRNH 600
LPSSGTSTPS SMVDIPPPFD LACITKKPIT KSSPSLLIES DSPDKYKKKK SSFKRFLALT 660
FKKKTENKLH VDVNVSSSRS SSESSYHGPS RILEVDRRSL SNSPQLKSRT GKLRASESPS 720
SLIFYRDGKR KGVPFSRTVS RVESFEDRSR PPFLPLPLTK PRSISFPSAD TSDYENIPAM 780
NSDYENIQIP PRRPARAGAF TKLFEDQSRA LSTANENDGY VDMSSFNAFE SKQQSADQDA 840
ESAYTEPYKV CPISSAAPKE DLTSDEEQRS SEEEDSASRD PSVTHKVEGQ SRALVIAQEL 900
LSSEKAYVEM LQHLNLDFHG AVMRALDDMD HEGRDTLARE ELRQGLSELP AIHDLHQGIL 960
EELEERLSNW ESQQKVADVF LAREQGFDHH ATHILQFDRY LGLLSENCLH SPRLAAAVRE 1020
FEQSVQGGSQ TAKHRLLRVV QRLFQYQVLL TDYLNNLCPD SAEYDNTQGA LSLISKVTDR 1080
ANDSMEQGEN LQKLVHIEHS VRGQGDLLQP GREFLKEGTL MKVTGKNRRP RHLFLMNDVL 1140
LYTYPQKDGK YRLKNTLAVA NMKVSRPVME KVPYALKIET SESCLMLSAS SCAERDEWYG 1200
CLSRALPEDY KAQALAAFHH SVEIRERLGV SLGERPPTLV PVTHVMMCMN CGCDFSLTLR 1260
RHHCHACGKI VCRNCSRNKY PLKYLKDRMA KVCDGCFGEL KKRGRAVPGL MRERPVSMSF 1320
PLSSPRFSGS AFSSVFQSIN PSTFKKQKKV PSALTEVAAS GEGSAISGYL SRCKRGKRHW 1380
KKLWFVIKGK VLYTYMASED KVALESMPLL GFTIAPEKEE GSSEVGPIFH LYHKKTLFYS 1440
FKAEDTNSAQ RWIEAMEDAS VL 1462 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 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:0046847; P:filopodium assembly; ISS:UniProtKB.
 GO:0043088; P:regulation of Cdc42 GTPase activity; ISS:UniProtKB.
 GO:0008360; P:regulation of cell shape; ISS:UniProtKB. 
Interpro
 IPR000219; DH-domain.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR000306; Znf_FYVE.
 IPR017455; Znf_FYVE-rel.
 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