Search Results

Overview

Uniprot IDQ04637
Protein NameEukaryotic translation initiation factor 4 gamma 1
Gene NameEIF4G1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1007 KTIDQIHKEAEMEEH
1019 EEHREHIKVQQLMAK
1026 KVQQLMAKGSDKRRG
1059 WNTVPISKGSRPIDT
1071 IDTSRLTKITKPGSI
1074 SRLTKITKPGSIDSN
1095 GGRLSWGKGSSGGSG
1153 LSRERGEKAGDRGDR
1188 ATKRSFSKEVEERSR
1206 SQPEGLRKAASLTED
190 RDPNQGGKDITEEIM
524 KIKELNKKEAVGDLL
593 NIQPGEQKYEYKSDQ
714 GPRKEPRKIIATVLM
950 GKDLDFEKAKPRMDQ
952 DLDFEKAKPRMDQYF

Function

Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:29987188). Exists in two complexes, either with EIF1 or with EIF4E (mutually exclusive) (PubMed:29987188). Together with EIF1, is required for leaky scanning, in particular for avoiding cap-proximal start codon (PubMed:29987188). Together with EIF4E, antagonizes the scanning promoted by EIF1-EIF4G1 and locates the start codon (through a TISU element) without scanning (PubMed:29987188). As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139)

Protein Sequence

10 MNKAPQSTGP 20 PPAPSPGLPQ 30 PAFPPGQTAP 40 VVFSTPQATQ 50 MNTPSQPRQH 60 FYPSRAQPPS 70 SAASRVQSAA 80 PARPGPAAHV 90 YPAGSQVMMI 100 PSQISYPASQ 110 GAYYIPGQGR 120 STYVVPTQQY 130 PVQPGAPGFY 140 PGASPTEFGT 150 YAGAYYPAQG 160 VQQFPTGVAP 170 TPVLMNQPPQ 180 IAPKRERKTI 190 RIRDPNQGGK 200 DITEEIMSGA 210 RTASTPTPPQ 220 TGGGLEPQAN 230 GETPQVAVIV 240 RPDDRSQGAI 250 IADRPGLPGP 260 EHSPSESQPS 270 SPSPTPSPSP 280 VLEPGSEPNL 290 AVLSIPGDTM 300 TTIQMSVEES 310 TPISRETGEP 320 YRLSPEPTPL 330 AEPILEVEVT 340 LSKPVPESEF 350 SSSPLQAPTP 360 LASHTVEIHE 370 PNGMVPSEDL 380 EPEVESSPEL 390 APPPACPSES 400 PVPIAPTAQP 410 EELLNGAPSP 420 PAVDLSPVSE 430 PEEQAKEVTA 440 SMAPPTIPSA 450 TPATAPSATS 460 PAQEEEMEEE 470 EEEEEGEAGE 480 AGEAESEKGG 490 EELLPPESTP 500 IPANLSQNLE 510 AAAATQVAVS 520 VPKRRRKIKE 530 LNKKEAVGDL 540 LDAFKEANPA 550 VPEVENQPPA 560 GSNPGPESEG 570 SGVPPRPEEA 580 DETWDSKEDK 590 IHNAENIQPG 600 EQKYEYKSDQ 610 WKPLNLEEKK 620 RYDREFLLGF 630 QFIFASMQKP 640 EGLPHISDVV 650 LDKANKTPLR 660 PLDPTRLQGI 670 NCGPDFTPSF 680 ANLGRTTLST 690 RGPPRGGPGG 700 ELPRGPAGLG 710 PRRSQQGPRK 720 EPRKIIATVL 730 MTEDIKLNKA 740 EKAWKPSSKR 750 TAADKDRGEE 760 DADGSKTQDL 770 FRRVRSILNK 780 LTPQMFQQLM 790 KQVTQLAIDT 800 EERLKGVIDL 810 IFEKAISEPN 820 FSVAYANMCR 830 CLMALKVPTT 840 EKPTVTVNFR 850 KLLLNRCQKE 860 FEKDKDDDEV 870 FEKKQKEMDE 880 AATAEERGRL 890 KEELEEARDI 900 ARRRSLGNIK 910 FIGELFKLKM 920 LTEAIMHDCV 930 VKLLKNHDEE 940 SLECLCRLLT 950 TIGKDLDFEK 960 AKPRMDQYFN 970 QMEKIIKEKK 980 TSSRIRFMLQ 990 DVLDLRGSNW 1000 VPRRGDQGPK 1010 TIDQIHKEAE 1020 MEEHREHIKV 1030 QQLMAKGSDK 1040 RRGGPPGPPI 1050 SRGLPLVDDG 1060 GWNTVPISKG 1070 SRPIDTSRLT 1080 KITKPGSIDS 1090 NNQLFAPGGR 1100 LSWGKGSSGG 1110 SGAKPSDAAS 1120 EAARPATSTL 1130 NRFSALQQAV 1140 PTESTDNRRV 1150 VQRSSLSRER 1160 GEKAGDRGDR 1170 LERSERGGDR 1180 GDRLDRARTP 1190 ATKRSFSKEV 1200 EERSRERPSQ 1210 PEGLRKAASL 1220 TEDRDRGRDA 1230 VKREAALPPV 1240 SPLKAALSEE 1250 ELEKKSKAII 1260 EEYLHLNDMK 1270 EAVQCVQELA 1280 SPSLLFIFVR 1290 HGVESTLERS 1300 AIAREHMGQL 1310 LHQLLCAGHL 1320 STAQYYQGLY 1330 EILELAEDME 1340 IDIPHVWLYL 1350 AELVTPILQE 1360 GGVPMGELFR 1370 EITKPLRPLG 1380 KAASLLLEIL 1390 GLLCKSMGPK 1400 KVGTLWREAG 1410 LSWKEFLPEG 1420 QDIGAFVAEQ 1430 KVEYTLGEES 1440 EAPGQRALPS 1450 EELNRQLEKL 1460 LKEGSSNQRV 1470 FDWIEANLSE 1480 QQIVSNTLVR 1490 ALMTAVCYSA 1500 IIFETPLRVD 1510 VAVLKARAKL 1520 LQKYLCDEQK 1530 ELQALYALQA 1540 LVVTLEQPPN 1550 LLRMFFDALY 1560 DEDVVKEDAF 1570 YSWESSKDPA 1580 EQQGKGVALK 1590 SVTAFFKWLR EAEEESDHN

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0010494 cytoplasmic stress granule
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016281 eukaryotic translation initiation factor 4F complex
Cellular Component GO:0016020 membrane
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005840 ribosome
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0008190 eukaryotic initiation factor 4E binding
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008135 translation factor activity, RNA binding
Molecular Function GO:0003743 translation initiation factor activity
Molecular Function GO:0031369 translation initiation factor binding
Biological Process GO:0002191 cap-dependent translational initiation
Biological Process GO:0031669 cellular response to nutrient levels
Biological Process GO:0097009 energy homeostasis
Biological Process GO:0035278 miRNA-mediated gene silencing by inhibition of translation
Biological Process GO:0010507 negative regulation of autophagy
Biological Process GO:0030307 positive regulation of cell growth
Biological Process GO:1905537 positive regulation of eukaryotic translation initiation factor 4F complex assembly
Biological Process GO:1900087 positive regulation of G1/S transition of mitotic cell cycle
Biological Process GO:1904377 positive regulation of protein localization to cell periphery
Biological Process GO:0051247 positive regulation of protein metabolic process
Biological Process GO:0036493 positive regulation of translation in response to endoplasmic reticulum stress
Biological Process GO:0080135 regulation of cellular response to stress
Biological Process GO:1905606 regulation of presynapse assembly
Biological Process GO:0006446 regulation of translational initiation
Biological Process GO:0006412 translation
Biological Process GO:0006413 translational initiation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] 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.

[6] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[7] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[8] 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.

[9] 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.