CYFP1_HUMAN
ID CYFP1_HUMAN Reviewed; 1253 AA.
AC Q7L576; A8K6D9; Q14467; Q5IED0; Q6ZSX1; Q9BSD9; Q9BVC7;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cytoplasmic FMR1-interacting protein 1;
DE AltName: Full=Specifically Rac1-associated protein 1;
DE Short=Sra-1;
DE AltName: Full=p140sra-1;
GN Name=CYFIP1 {ECO:0000312|HGNC:HGNC:13759};
GN Synonyms=KIAA0068 {ECO:0000312|EMBL:BAA07552.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAW51476.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT SER-820.
RA Jiang Y.-H., Beaudet A.L.;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA07552.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow {ECO:0000269|PubMed:7584044};
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC86825.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-820.
RC TISSUE=Brain {ECO:0000312|EMBL:BAC86825.1}, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAW51476.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH05097.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH05097.1}, and
RC Placenta {ECO:0000312|EMBL:AAH01306.2};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAW51476.1}
RP PROTEIN SEQUENCE OF 50-58; 111-130; 151-163; 366-377; 441-448; 505-515;
RP 564-573; 754-760; 815-826; 867-877; 1054-1076; 1211-1224 AND 1228-1240, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Hepatoma;
RA Bienvenut W.V., Claeys D., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=9417078; DOI=10.1074/jbc.273.1.291;
RA Kobayashi K., Kuroda S., Fukata M., Nakamura T., Nagase T., Nomura N.,
RA Matsuura Y., Yoshida-Kubomura N., Iwamatsu A., Kaibuchi K.;
RT "p140Sra-1 (specifically Rac1-associated protein) is a novel specific
RT target for Rac1 small GTPase.";
RL J. Biol. Chem. 273:291-295(1998).
RN [8] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH DPYSL2.
RX PubMed=16260607; DOI=10.1128/mcb.25.22.9920-9935.2005;
RA Kawano Y., Yoshimura T., Tsuboi D., Kawabata S., Kaneko-Kawano T.,
RA Shirataki H., Takenawa T., Kaibuchi K.;
RT "CRMP-2 is involved in kinesin-1-dependent transport of the Sra-1/WAVE1
RT complex and axon formation.";
RL Mol. Cell. Biol. 25:9920-9935(2005).
RN [9]
RP IDENTIFICATION IN THE WAVE2 COMPLEX.
RX PubMed=16417406; DOI=10.1371/journal.pbio.0040038;
RA Weiner O.D., Rentel M.C., Ott A., Brown G.E., Jedrychowski M., Yaffe M.B.,
RA Gygi S.P., Cantley L.C., Bourne H.R., Kirschner M.W.;
RT "Hem-1 complexes are essential for Rac activation, actin polymerization,
RT and myosin regulation during neutrophil chemotaxis.";
RL PLoS Biol. 4:E38-E38(2006).
RN [10]
RP FUNCTION.
RX PubMed=19524508; DOI=10.1016/j.cell.2009.04.013;
RA Silva J.M., Ezhkova E., Silva J., Heart S., Castillo M., Campos Y.,
RA Castro V., Bonilla F., Cordon-Cardo C., Muthuswamy S.K., Powers S.,
RA Fuchs E., Hannon G.J.;
RT "Cyfip1 is a putative invasion suppressor in epithelial cancers.";
RL Cell 137:1047-1061(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583 AND THR-1234, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF WAVE1 COMPLEX, FUNCTION,
RP INTERACTION WITH RAC1, MUTAGENESIS OF CYS-179; ARG-190; GLU-434; PHE-626;
RP MET-632; LEU-697; TYR-704; LEU-841 AND 844-PHE-TRP-845, AND SUBUNIT.
RX PubMed=21107423; DOI=10.1038/nature09623;
RA Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M.,
RA Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.;
RT "Structure and control of the actin regulatory WAVE complex.";
RL Nature 468:533-538(2010).
CC -!- FUNCTION: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the
CC mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-
CC FMR1 complex this subunit is an adapter between EIF4E and FMR1.
CC Promotes the translation repression activity of FMR1 in brain probably
CC by mediating its association with EIF4E and mRNA (By similarity).
CC Regulates formation of membrane ruffles and lamellipodia. Plays a role
CC in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE
CC complex that regulates actin filament reorganization via its
CC interaction with the Arp2/3 complex. Actin remodeling activity is
CC regulated by RAC1. Regulator of epithelial morphogenesis. As component
CC of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and
CC signaling from early endosomes (By similarity). May act as an invasion
CC suppressor in cancers. {ECO:0000250|UniProtKB:Q7TMB8,
CC ECO:0000269|PubMed:16260607, ECO:0000269|PubMed:19524508,
CC ECO:0000269|PubMed:21107423, ECO:0000269|PubMed:9417078}.
CC -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 or
CC CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer
CC containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by
CC WAVE1, ABI2 and BRK1. Component of the CYFIP1-EIF4E-FMR1 complex which
CC is composed of CYFIP, EIF4E and FMR1. Interacts with FMR1 but does not
CC bind to related proteins FXR1 or FXR2. Interaction with EIF4E
CC stimulates FMR1 binding. Component of the WAVE2 complex composed of
CC ABI1, CYFIP1/SRA1, NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells)
CC and WASF2/WAVE2 (PubMed:16417406). Interacts with the active GTP-bound
CC form of RAC1. Interacts through its C-terminus with the C-terminus of
CC DPYSL2/CRMP2 which is necessary for DPYSL2-induced axon outgrowth.
CC Interacts with NYAP1, NYAP2 and MYO16. Interacts with TMEM108 (via N-
CC terminus); the interaction associates TMEM108 with the WAVE1 complex
CC (By similarity). {ECO:0000250|UniProtKB:Q7TMB8,
CC ECO:0000269|PubMed:16260607, ECO:0000269|PubMed:16417406,
CC ECO:0000269|PubMed:21107423}.
CC -!- INTERACTION:
CC Q7L576; P01023: A2M; NbExp=3; IntAct=EBI-1048143, EBI-640741;
CC Q7L576; Q06787: FMR1; NbExp=4; IntAct=EBI-1048143, EBI-366305;
CC Q7L576; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1048143, EBI-10975473;
CC Q7L576; O14901: KLF11; NbExp=3; IntAct=EBI-1048143, EBI-948266;
CC Q7L576; P51608: MECP2; NbExp=3; IntAct=EBI-1048143, EBI-1189067;
CC Q7L576; Q9Y2A7: NCKAP1; NbExp=5; IntAct=EBI-1048143, EBI-389845;
CC Q7L576; P07196: NEFL; NbExp=3; IntAct=EBI-1048143, EBI-475646;
CC Q7L576; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1048143, EBI-5235340;
CC Q7L576; O76024: WFS1; NbExp=3; IntAct=EBI-1048143, EBI-720609;
CC Q7L576; P63073: Eif4e; Xeno; NbExp=2; IntAct=EBI-1048143, EBI-2000006;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7TMB8}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TMB8}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:Q7TMB8}. Cell
CC projection, ruffle {ECO:0000250|UniProtKB:Q7TMB8}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q7TMB8}. Note=Highly expressed in the
CC perinuclear region (By similarity). Enriched in synaptosomes (By
CC similarity). Also enriched in membrane ruffles and at the tips of
CC lamellipodia (By similarity). {ECO:0000250|UniProtKB:Q7TMB8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=3;
CC IsoId=Q7L576-1; Sequence=Displayed;
CC Name=2; Synonyms=4;
CC IsoId=Q7L576-2; Sequence=VSP_052346, VSP_052347;
CC Name=3; Synonyms=5;
CC IsoId=Q7L576-3; Sequence=VSP_052345;
CC -!- MISCELLANEOUS: Breakpoint hotspot for the Prader-Willi/Angelman
CC syndromes and may be implicated in autism. Commonly altered in tumors.
CC -!- SIMILARITY: Belongs to the CYFIP family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07552.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY763577; AAW51476.1; -; mRNA.
DR EMBL; AY763578; AAW51477.1; -; mRNA.
DR EMBL; AY763579; AAW51478.1; -; mRNA.
DR EMBL; AY763580; AAW51479.1; -; mRNA.
DR EMBL; D38549; BAA07552.1; ALT_INIT; mRNA.
DR EMBL; AK127094; BAC86825.1; -; mRNA.
DR EMBL; AK291604; BAF84293.1; -; mRNA.
DR EMBL; CH471258; EAW65555.1; -; Genomic_DNA.
DR EMBL; BC001306; AAH01306.2; -; mRNA.
DR EMBL; BC005097; AAH05097.1; -; mRNA.
DR CCDS; CCDS73695.1; -. [Q7L576-2]
DR CCDS; CCDS73696.1; -. [Q7L576-1]
DR RefSeq; NP_001028200.1; NM_001033028.1. [Q7L576-2]
DR RefSeq; NP_001274739.1; NM_001287810.2. [Q7L576-1]
DR RefSeq; NP_001311049.1; NM_001324120.1. [Q7L576-1]
DR RefSeq; NP_001311052.1; NM_001324123.1. [Q7L576-1]
DR RefSeq; NP_055423.1; NM_014608.4. [Q7L576-1]
DR PDB; 3P8C; X-ray; 2.29 A; A=1-1253.
DR PDB; 4N78; X-ray; 2.43 A; A=1-1253.
DR PDBsum; 3P8C; -.
DR PDBsum; 4N78; -.
DR AlphaFoldDB; Q7L576; -.
DR SMR; Q7L576; -.
DR BioGRID; 116800; 137.
DR CORUM; Q7L576; -.
DR DIP; DIP-38873N; -.
DR IntAct; Q7L576; 76.
DR MINT; Q7L576; -.
DR STRING; 9606.ENSP00000481038; -.
DR GlyConnect; 1168; 1 N-Linked glycan (1 site).
DR GlyGen; Q7L576; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q7L576; -.
DR MetOSite; Q7L576; -.
DR PhosphoSitePlus; Q7L576; -.
DR SwissPalm; Q7L576; -.
DR BioMuta; CYFIP1; -.
DR DMDM; 74738589; -.
DR EPD; Q7L576; -.
DR jPOST; Q7L576; -.
DR MassIVE; Q7L576; -.
DR MaxQB; Q7L576; -.
DR PaxDb; Q7L576; -.
DR PeptideAtlas; Q7L576; -.
DR PRIDE; Q7L576; -.
DR ProteomicsDB; 68792; -. [Q7L576-1]
DR ProteomicsDB; 68793; -. [Q7L576-2]
DR ProteomicsDB; 68794; -. [Q7L576-3]
DR Antibodypedia; 72407; 117 antibodies from 26 providers.
DR DNASU; 23191; -.
DR Ensembl; ENST00000610365.4; ENSP00000478779.1; ENSG00000273749.5. [Q7L576-1]
DR Ensembl; ENST00000617556.4; ENSP00000480525.1; ENSG00000273749.5. [Q7L576-2]
DR Ensembl; ENST00000617928.5; ENSP00000481038.1; ENSG00000273749.5. [Q7L576-1]
DR Ensembl; ENST00000671714.1; ENSP00000500331.1; ENSG00000288461.1. [Q7L576-1]
DR Ensembl; ENST00000672091.1; ENSP00000499947.1; ENSG00000288461.1. [Q7L576-1]
DR GeneID; 23191; -.
DR KEGG; hsa:23191; -.
DR MANE-Select; ENST00000617928.5; ENSP00000481038.1; NM_014608.6; NP_055423.1.
DR UCSC; uc001yus.5; human. [Q7L576-1]
DR CTD; 23191; -.
DR DisGeNET; 23191; -.
DR GeneCards; CYFIP1; -.
DR HGNC; HGNC:13759; CYFIP1.
DR HPA; ENSG00000273749; Low tissue specificity.
DR MIM; 606322; gene.
DR neXtProt; NX_Q7L576; -.
DR OpenTargets; ENSG00000273749; -.
DR PharmGKB; PA38367; -.
DR VEuPathDB; HostDB:ENSG00000273749; -.
DR eggNOG; KOG3534; Eukaryota.
DR GeneTree; ENSGT00500000044831; -.
DR HOGENOM; CLU_002688_2_1_1; -.
DR InParanoid; Q7L576; -.
DR OMA; HKESFFY; -.
DR OrthoDB; 108507at2759; -.
DR PhylomeDB; Q7L576; -.
DR TreeFam; TF312925; -.
DR PathwayCommons; Q7L576; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q7L576; -.
DR SIGNOR; Q7L576; -.
DR BioGRID-ORCS; 23191; 269 hits in 1078 CRISPR screens.
DR ChiTaRS; CYFIP1; human.
DR EvolutionaryTrace; Q7L576; -.
DR GeneWiki; CYFIP1; -.
DR GenomeRNAi; 23191; -.
DR Pharos; Q7L576; Tbio.
DR PRO; PR:Q7L576; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q7L576; protein.
DR Bgee; ENSG00000273749; Expressed in esophagus squamous epithelium and 209 other tissues.
DR ExpressionAtlas; Q7L576; baseline and differential.
DR Genevisible; Q7L576; HS.
DR GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
DR GO; GO:0090724; C:central region of growth cone; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0044294; C:dendritic growth cone; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0090725; C:peripheral region of growth cone; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0031209; C:SCAR complex; IMP:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IEA:Ensembl.
DR GO; GO:0048675; P:axon extension; IMP:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0097484; P:dendrite extension; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0099563; P:modification of synaptic structure; IBA:GO_Central.
DR GO; GO:1903422; P:negative regulation of synaptic vesicle recycling; IEA:Ensembl.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IMP:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:1900006; P:positive regulation of dendrite development; IEA:Ensembl.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IDA:ARUK-UCL.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; IEA:Ensembl.
DR GO; GO:0016601; P:Rac protein signal transduction; IMP:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
DR GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR GO; GO:0099578; P:regulation of translation at postsynapse, modulating synaptic transmission; IEA:Ensembl.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0031529; P:ruffle organization; ISS:UniProtKB.
DR InterPro; IPR009828; CYRIA/CYRIB_Rac1-bd.
DR InterPro; IPR008081; Cytoplasmic_FMR1-int.
DR PANTHER; PTHR12195; PTHR12195; 1.
DR Pfam; PF07159; DUF1394; 1.
DR Pfam; PF05994; FragX_IP; 1.
DR PIRSF; PIRSF008153; FMR1_interacting; 1.
DR PRINTS; PR01698; CYTOFMRPINTP.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell projection;
KW Cell shape; Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Neurogenesis; Phosphoprotein;
KW Reference proteome; Synapse; Synaptosome.
FT CHAIN 1..1253
FT /note="Cytoplasmic FMR1-interacting protein 1"
FT /id="PRO_0000279706"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..806
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_052345"
FT VAR_SEQ 1..431
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_052346"
FT VAR_SEQ 432..557
FT /note="AEEYERATRYNYTSEEKFALVEVIAMIKGLQVLMGRMESVFNHAIRHTVYAA
FT LQDFSQVTLREPLRQAIKKKKNVIQSVLQAIRKTVCDWETGHEPFNDPALRGEKDPKSG
FT FDIKVPRRAVGPSST -> MAESLGSAELLRQLKSLGMERLLHAVNTFLRQSCTYLPLL
FT TFGGKTSFVSLDVYGTEANCSATSCSFPKAAATWPRRQAPGPLGELVRGPPDQGVAEQS
FT FSHGLFEFGITNVPCIFSPPQMFPWII (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_052347"
FT VARIANT 532
FT /note="A -> P (in dbSNP:rs34683919)"
FT /id="VAR_053849"
FT VARIANT 820
FT /note="G -> D (in dbSNP:rs17137190)"
FT /id="VAR_053850"
FT VARIANT 820
FT /note="G -> S (in dbSNP:rs7170637)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1"
FT /id="VAR_053851"
FT MUTAGEN 179
FT /note="C->R: Reduced interaction with RAC1."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 190
FT /note="R->D: Reduced interaction with RAC1."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 434
FT /note="E->K: Reduced interaction with RAC1; when associated
FT with A-626."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 626
FT /note="F->A: Reduced interaction with RAC1; when associated
FT with K-434."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 632
FT /note="M->D: Reduced interaction with RAC1."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 697
FT /note="L->D: Constitutive induction of the formation of
FT actin filaments; when associated with D-704."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 704
FT /note="Y->D: Constitutive induction of the formation of
FT actin filaments; when associated with D-697."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 841
FT /note="L->A: Constitutive induction of the formation of
FT actin filaments; when associated with 844-A-A-845."
FT /evidence="ECO:0000269|PubMed:21107423"
FT MUTAGEN 844..845
FT /note="FW->AA: Constitutive induction of the formation of
FT actin filaments; when associated with A-841."
FT /evidence="ECO:0000269|PubMed:21107423"
FT CONFLICT 583
FT /note="S -> N (in Ref. 1; AAW51478 and 3; BAC86825)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="Y -> H (in Ref. 1; AAW51478 and 3; BAC86825)"
FT /evidence="ECO:0000305"
FT CONFLICT 930
FT /note="M -> R (in Ref. 1; AAW51478 and 3; BAC86825)"
FT /evidence="ECO:0000305"
FT CONFLICT 1176
FT /note="V -> A (in Ref. 1; AAW51479)"
FT /evidence="ECO:0000305"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 59..84
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 104..143
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 155..177
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 179..193
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 234..250
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 257..274
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 346..365
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 384..417
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 445..467
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 469..489
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 493..501
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 505..518
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 531..534
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 556..570
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 580..583
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 586..598
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 599..601
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 602..606
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 608..615
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 625..630
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 631..633
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 640..642
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 644..655
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 661..663
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 664..668
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 670..680
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 685..721
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 725..733
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 747..750
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 760..762
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 764..788
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 792..794
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 795..813
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 821..828
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 832..836
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 838..849
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 851..854
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 855..858
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 859..862
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 885..887
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 892..901
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 902..906
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 911..942
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 944..955
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 965..967
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 969..979
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 981..984
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 987..992
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 993..1025
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1026..1029
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1043..1053
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1055..1057
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1059..1066
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1069..1083
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1086..1088
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 1090..1092
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1093..1101
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 1107..1110
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 1121..1123
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1127..1139
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1149..1153
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1156..1167
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1171..1177
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1179..1190
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1201..1225
FT /evidence="ECO:0007829|PDB:3P8C"
SQ SEQUENCE 1253 AA; 145182 MW; D8F45E13207BEF16 CRC64;
MAAQVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSLLYQP NFNTNFEDRN AFVTGIARYI
EQATVHSSMN EMLEEGQEYA VMLYTWRSCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVT
KLMNFMYFQR NAIERFCGEV RRLCHAERRK DFVSEAYLIT LGKFINMFAV LDELKNMKCS
VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNKI TQSLQQQLEV ISGYEELLAD
IVNLCVDYYE NRMYLTPSEK HMLLKVMGFG LYLMDGSVSN IYKLDAKKRI NLSKIDKYFK
QLQVVPLFGD MQIELARYIK TSAHYEENKS RWTCTSSGSS PQYNICEQMI QIREDHMRFI
SELARYSNSE VVTGSGRQEA QKTDAEYRKL FDLALQGLQL LSQWSAHVME VYSWKLVHPT
DKYSNKDCPD SAEEYERATR YNYTSEEKFA LVEVIAMIKG LQVLMGRMES VFNHAIRHTV
YAALQDFSQV TLREPLRQAI KKKKNVIQSV LQAIRKTVCD WETGHEPFND PALRGEKDPK
SGFDIKVPRR AVGPSSTQLY MVRTMLESLI ADKSGSKKTL RSSLEGPTIL DIEKFHRESF
FYTHLINFSE TLQQCCDLSQ LWFREFFLEL TMGRRIQFPI EMSMPWILTD HILETKEASM
MEYVLYSLDL YNDSAHYALT RFNKQFLYDE IEAEVNLCFD QFVYKLADQI FAYYKVMAGS
LLLDKRLRSE CKNQGATIHL PPSNRYETLL KQRHVQLLGR SIDLNRLITQ RVSAAMYKSL
ELAIGRFESE DLTSIVELDG LLEINRMTHK LLSRYLTLDG FDAMFREANH NVSAPYGRIT
LHVFWELNYD FLPNYCYNGS TNRFVRTVLP FSQEFQRDKQ PNAQPQYLHG SKALNLAYSS
IYGSYRNFVG PPHFQVICRL LGYQGIAVVM EELLKVVKSL LQGTILQYVK TLMEVMPKIC
RLPRHEYGSP GILEFFHHQL KDIVEYAELK TVCFQNLREV GNAILFCLLI EQSLSLEEVC
DLLHAAPFQN ILPRVHVKEG ERLDAKMKRL ESKYAPLHLV PLIERLGTPQ QIAIAREGDL
LTKERLCCGL SMFEVILTRI RSFLDDPIWR GPLPSNGVMH VDECVEFHRL WSAMQFVYCI
PVGTHEFTVE QCFGDGLHWA GCMIIVLLGQ QRRFAVLDFC YHLLKVQKHD GKDEIIKNVP
LKKMVERIRK FQILNDEIIT ILDKYLKSGD GEGTPVEHVR CFQPPIHQSL ASS
