Search Results

Overview

Uniprot ID	Q7L576
Protein Name	Cytoplasmic FMR1-interacting protein 1
Gene Name	CYFIP1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
1053	KMKRLESKYAPLHLV
540	LRGEKDPKSGFDIKV

Function

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. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). May act as an invasion suppressor in cancers

Protein Sequence

10 MAAQVTLEDA 20 LSNVDLLEEL 30 PLPDQQPCIE 40 PPPSSLLYQP 50 NFNTNFEDRN 60 AFVTGIARYI 70 EQATVHSSMN 80 EMLEEGQEYA 90 VMLYTWRSCS 100 RAIPQVKCNE 110 QPNRVEIYEK 120 TVEVLEPEVT 130 KLMNFMYFQR 140 NAIERFCGEV 150 RRLCHAERRK 160 DFVSEAYLIT 170 LGKFINMFAV 180 LDELKNMKCS 190 VKNDHSAYKR 200 AAQFLRKMAD 210 PQSIQESQNL 220 SMFLANHNKI 230 TQSLQQQLEV 240 ISGYEELLAD 250 IVNLCVDYYE 260 NRMYLTPSEK 270 HMLLKVMGFG 280 LYLMDGSVSN 290 IYKLDAKKRI 300 NLSKIDKYFK 310 QLQVVPLFGD 320 MQIELARYIK 330 TSAHYEENKS 340 RWTCTSSGSS 350 PQYNICEQMI 360 QIREDHMRFI 370 SELARYSNSE 380 VVTGSGRQEA 390 QKTDAEYRKL 400 FDLALQGLQL 410 LSQWSAHVME 420 VYSWKLVHPT 430 DKYSNKDCPD 440 SAEEYERATR 450 YNYTSEEKFA 460 LVEVIAMIKG 470 LQVLMGRMES 480 VFNHAIRHTV 490 YAALQDFSQV 500 TLREPLRQAI 510 KKKKNVIQSV 520 LQAIRKTVCD 530 WETGHEPFND 540 PALRGEKDPK 550 SGFDIKVPRR 560 AVGPSSTQLY 570 MVRTMLESLI 580 ADKSGSKKTL 590 RSSLEGPTIL 600 DIEKFHRESF 610 FYTHLINFSE 620 TLQQCCDLSQ 630 LWFREFFLEL 640 TMGRRIQFPI 650 EMSMPWILTD 660 HILETKEASM 670 MEYVLYSLDL 680 YNDSAHYALT 690 RFNKQFLYDE 700 IEAEVNLCFD 710 QFVYKLADQI 720 FAYYKVMAGS 730 LLLDKRLRSE 740 CKNQGATIHL 750 PPSNRYETLL 760 KQRHVQLLGR 770 SIDLNRLITQ 780 RVSAAMYKSL 790 ELAIGRFESE 800 DLTSIVELDG 810 LLEINRMTHK 820 LLSRYLTLDG 830 FDAMFREANH 840 NVSAPYGRIT 850 LHVFWELNYD 860 FLPNYCYNGS 870 TNRFVRTVLP 880 FSQEFQRDKQ 890 PNAQPQYLHG 900 SKALNLAYSS 910 IYGSYRNFVG 920 PPHFQVICRL 930 LGYQGIAVVM 940 EELLKVVKSL 950 LQGTILQYVK 960 TLMEVMPKIC 970 RLPRHEYGSP 980 GILEFFHHQL 990 KDIVEYAELK 1000 TVCFQNLREV 1010 GNAILFCLLI 1020 EQSLSLEEVC 1030 DLLHAAPFQN 1040 ILPRVHVKEG 1050 ERLDAKMKRL 1060 ESKYAPLHLV 1070 PLIERLGTPQ 1080 QIAIAREGDL 1090 LTKERLCCGL 1100 SMFEVILTRI 1110 RSFLDDPIWR 1120 GPLPSNGVMH 1130 VDECVEFHRL 1140 WSAMQFVYCI 1150 PVGTHEFTVE 1160 QCFGDGLHWA 1170 GCMIIVLLGQ 1180 QRRFAVLDFC 1190 YHLLKVQKHD 1200 GKDEIIKNVP 1210 LKKMVERIRK 1220 FQILNDEIIT 1230 ILDKYLKSGD 1240 GEGTPVEHVR 1250 CFQPPIHQSL ASS

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0060076	excitatory synapse
Cellular Component	GO:0070062	extracellular exosome
Cellular Component	GO:0005576	extracellular region
Cellular Component	GO:0005925	focal adhesion
Cellular Component	GO:0030027	lamellipodium
Cellular Component	GO:0043005	neuron projection
Cellular Component	GO:0048471	perinuclear region of cytoplasm
Cellular Component	GO:0098794	postsynapse
Cellular Component	GO:0001726	ruffle
Cellular Component	GO:0031209	SCAR complex
Cellular Component	GO:0034774	secretory granule lumen
Cellular Component	GO:0035580	specific granule lumen
Cellular Component	GO:0045202	synapse
Cellular Component	GO:1904724	tertiary granule lumen
Molecular Function	GO:0051015	actin filament binding
Molecular Function	GO:0000340	RNA 7-methylguanosine cap binding
Molecular Function	GO:0031267	small GTPase binding
Molecular Function	GO:0030371	translation repressor activity
Biological Process	GO:0048675	axon extension
Biological Process	GO:0007411	axon guidance
Biological Process	GO:0000902	cell morphogenesis
Biological Process	GO:0050890	cognition
Biological Process	GO:0097484	dendrite extension
Biological Process	GO:0030032	lamellipodium assembly
Biological Process	GO:0017148	negative regulation of translation
Biological Process	GO:2000601	positive regulation of Arp2/3 complex-mediated actin nucleation
Biological Process	GO:0010592	positive regulation of lamellipodium assembly
Biological Process	GO:0051388	positive regulation of neurotrophin TRK receptor signaling pathway
Biological Process	GO:0016601	Rac protein signal transduction
Biological Process	GO:0030833	regulation of actin filament polymerization
Biological Process	GO:0008360	regulation of cell shape
Biological Process	GO:1905274	regulation of modification of postsynaptic actin cytoskeleton
Biological Process	GO:0006417	regulation of translation
Biological Process	GO:0099578	regulation of translation at postsynapse, modulating synaptic transmission
Biological Process	GO:0031529	ruffle organization

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.