CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015822
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytoplasmic FMR1-interacting protein 1 
Protein Synonyms/Alias
 Specifically Rac1-associated protein 1; Sra-1 
Gene Name
 Cyfip1 
Gene Synonyms/Alias
 Kiaa0068; Shyc; Sra1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
197RAAQFLRKMADPQSIubiquitination[1]
426PTDKYSNKDCPDNAEubiquitination[1]
1051KMKRLESKYAPLHLVubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA (By similarity). Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis. May act as an invasion suppressor in cancers. 
Sequence Annotation
 REGION 724 732 EIF4E-binding.  
Keyword
 Actin-binding; Alternative splicing; Cell junction; Cell projection; Cell shape; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Neurogenesis; Reference proteome; Synapse; Synaptosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1253 AA 
Protein Sequence
MAAQVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSLLYQP NFNTNFEDRN AFVTGIARYI 60
EQATVHSSMN EMLEEGQEYA VMLYTWRSCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVT 120
KLMNFMYFQR NAIERFCGEV RRLCHAERRK DFVSEAYLIT LGKFINMFAV LDELKNMKCS 180
VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNKI TQSLQQQLEV ISGYEELLAD 240
IVNLCVDYYE NRMYLTPSEK HMLLKVMGFG LYLMDGSVSN IYKLDAKKRI NLSKIDKYFK 300
QLQVVPLFGD MQIELARYIK TSAHYEENKS RWTCASSSSS PQYNICEQMI QIREDHMRFI 360
SELARYSNSE VVTGSGRQEA QKTDAEYRKL FDLALQGLQL LSQWSAHVME VYSWKLVHPT 420
DKYSNKDCPD NAEEYERATR YNYTTEEKFA LVEVIAMIKG LQVLMGRMES VFNHAIRHTV 480
YAALQDFSQV TLREPLRQAI KKKKNVIQSV LQAIRKTVCD WETGHEPFND PALRGEKDPK 540
SGFDIKVPRR AVGPSSTQLY MVRTMLESLS SAELLRQLKS LGMERLLHVV NAFLRQSYTY 600
PPLLTFGETL QQCCDLSQLW FREFFLELTM GRRIQFPIEM SMPWILTDHI LETKEASMME 660
YVLYSLDLYN DSAHYALTKF NKQFLYDEIE AEVNLCFDQF VYKLADQIFA YYKVMAGSLL 720
LDKRLRSECK NQGATIHLPP SNRYETLLKQ RHVQLLGRSI DLNRLITQRV SAAMYKSLEL 780
AIGRFESEDL TSVVELDGLL EINRMTHKLL SRYLTLDSFD AMFREANHNV SAPYGRITLH 840
VFWELNYDFL PNYCYNGSTN RFVRTVLPFS QEFQRDKQPN AQPQYLHGSK ALNLAYSSIY 900
GSYRNFVGPP HFQVICRLLG YQGIAVVMEE LLKVVKSLLQ GTILQYVKTL MEVMPKICRL 960
PRHEYGSPGI LEFFHHQLKD IVEYAELKTV CFQNLREVGN AVLFCLLIEQ SLSLEEVCDL 1020
LHAAPFQNIL PRIHVKEGER VDAKMKRLES KYAPLHLVPL IERLGTPQQI AIAREGDLLT 1080
KERLCCGLSM FEVILTRIRT FLDDPIWRGP LPSNGVMHVD ECVEFHRLWS AMQFVYCIPV 1140
GTHEFTVEQC FGDGLHWAGC MIIVLLGQQR RFAVLDFCYH LLKVQKHDGK DEIIKNVPLK 1200
KMVERIRKFQ ILNDEIITIL DKYLKSGDGE STPVEHVRCF QPPIHQSLAS S 1251 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0030027; C:lamellipodium; IDA:MGI.
 GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
 GO:0043005; C:neuron projection; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 GO:0045202; C:synapse; IEA:UniProtKB-KW.
 GO:0051015; F:actin filament binding; ISS:UniProtKB.
 GO:0005522; F:profilin binding; TAS:MGI.
 GO:0048365; F:Rac GTPase binding; ISS:UniProtKB.
 GO:0048675; P:axon extension; ISS:UniProtKB.
 GO:0030032; P:lamellipodium assembly; IDA:MGI.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
 GO:0031529; P:ruffle organization; ISS:UniProtKB. 
Interpro
 IPR008081; Cytoplasmic_FMR1-int.
 IPR016536; Cytoplasmic_FMR1-int_sub. 
Pfam
 PF05994; FragX_IP 
SMART
  
PROSITE
  
PRINTS
 PR01698; CYTOFMRPINTP.