UniProt Accession

 CYFP1_HUMAN; Q7L576; A8K6D9; Q14467; Q5IED0; Q6ZSX1; Q9BSD9; Q9BVC7 

Genbank Protein ID

 AY763577; AY763578; AY763579; AY763580; D38549; AK127094; AK291604; CH471258; BC001306; BC005097 

Genbank Nucleotide ID

 AAW51476.1; AAW51477.1; AAW51478.1; AAW51479.1; BAA07552.1; BAC86825.1; BAF84293.1; EAW65555.1; AAH01306.2; AAH05097.1 

Protein Name

 Cytoplasmic FMR1-interacting protein 1 

Protein Synonyms/Alias

 Specifically Rac1-associated protein 1; Sra-1; p140sra-1 

Gene Name

 CYFIP1 

Gene Synonyms/Alias

 KIAA0068 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
110	NRVEIYEKTVEVLEP	ubiquitination	[1]
150	LCHAERRKDFVSEAY	ubiquitination	[2]
294	KKRINLSKIDKYFKQ	ubiquitination	[1, 3]
320	IELARYIKTSAHYEE	ubiquitination	[1]
329	SAHYEENKSRWTCTS	ubiquitination	[1]
422	KLVHPTDKYSNKDCP	ubiquitination	[1, 4]
426	PTDKYSNKDCPDSAE	ubiquitination	[1, 4]
448	YNYTSEEKFALVEVI	ubiquitination	[1]
546	PKSGFDIKVPRRAVG	ubiquitination	[1]
573	LESLIADKSGSKKTL	ubiquitination	[1]
715	DQIFAYYKVMAGSLL	ubiquitination	[1]
725	AGSLLLDKRLRSECK	ubiquitination	[1]
751	NRYETLLKQRHVQLL	ubiquitination	[1, 3]
778	RVSAAMYKSLELAIG	ubiquitination	[1, 4, 5]
879	SQEFQRDKQPNAQPQ	ubiquitination	[1, 3]
892	PQYLHGSKALNLAYS	ubiquitination	[4]
990	IVEYAELKTVCFQNL	ubiquitination	[4]
1053	KMKRLESKYAPLHLV	ubiquitination	[1, 3, 6]
1083	REGDLLTKERLCCGL	ubiquitination	[1]
1197	DGKDEIIKNVPLKKM	acetylation	[7, 8, 9]
1210	KMVERIRKFQILNDE	ubiquitination	[1, 5, 6]
1227	TILDKYLKSGDGEGT	ubiquitination	[1, 5]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

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

  

Keyword

 3D-structure; Actin-binding; Alternative splicing; Cell junction; Cell projection; Cell shape; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Neurogenesis; Polymorphism; Reference proteome; Synapse; Synaptosome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1253 AA 

Protein Sequence

Gene Ontology

 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
 GO:0043005; C:neuron projection; ISS:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 GO:0045202; C:synapse; IEA:UniProtKB-KW.
 GO:0051015; F:actin filament binding; ISS:UniProtKB.
 GO:0048365; F:Rac GTPase binding; ISS:UniProtKB.
 GO:0048675; P:axon extension; IMP:UniProtKB.
 GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
 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.