GRB10-interacting GYF protein 2 (PERQ amino acid-rich with GYF domain-containing protein 2) (Trinucleotide repeat-containing gene 15 protein)
1_MAAET 6_ QTLNF 11_ GPEWL 16_ RALSS 21_ GGSIT 26_ SPPLS 31_ PALPK 36_ YKLAD 41_ YRYGR 46_ EEMLA 51_ LFLKD 56_ NKIPS 61_ DLLDK 66_ EFLPI 71_ LQEEP 76_ LPPLA 81_ LVPFT 86_ EEEQR 91_ NFSMS 96_ VNSAA 101_ VLRLT 106_ GRGGG 111_ GTVVG 116_ APRGR 121_ SSSRG 126_ RGRGR 131_ GECGF 136_ YQRSF 141_ DEVEG 146_ VFGRG 151_ GGREM 156_ HRSQS 161_ WEERG 166_ DRRFE 171_ KPGRK 176_ DVGRP 181_ NFEEG 186_ GPTSV 191_ GRKHE 196_ FIRSE 201_ SENWR 206_ IFREE 211_ QNGED 216_ EDGGW 221_ RLAGS 226_ RRDGE 231_ RWRPH 236_ SPDGP 241_ RSAGW 246_ REHME 251_ RRRRF 256_ EFDFR 261_ DRDDE 266_ RGYRR 271_ VRSGS 276_ GSIDD 281_ DRDSL 286_ PEWCL 291_ EDAEE 296_ EMGTF 301_ DSSGA 306_ FLSLK 311_ KVQKE 316_ PIPEE 321_ QEMDF 326_ RPVDE 331_ GEECS 336_ DSEGS 341_ HNEEA 346_ KEPDK 351_ TNKKE 356_ GEKTD 361_ RVGVE 366_ ASEET 371_ PQTSS 376_ SSARP 381_ GTPSD 386_ HQSQE 391_ ASQFE 396_ RKDEP 401_ KTEQT 406_ EKAEE 411_ ETRME 416_ NSLPA 421_ KVPSR 426_ GDEMV 431_ ADVQQ 436_ PLSQI 441_ PSDTA 446_ SPLLI 451_ LPPPV 456_ PNPSP 461_ TLRPV 466_ ETPVV 471_ GAPGM 476_ GSVST 481_ EPDDE 486_ EGLKH 491_ LEQQA 496_ EKMVA 501_ YLQDS 506_ ALDDE 511_ RLASK 516_ LQEHR 521_ AKGVS 526_ IPLMH 531_ EAMQK 536_ WYYKD 541_ PQGEI 546_ QGPFN 551_ NQEMA 556_ EWFQA 561_ GYFTM 566_ SLLVK 571_ RACDE 576_ SFQPL 581_ GDIMK 586_ MWGRV 591_ PFSPG 596_ PAPPP 601_ HMGEL 606_ DQERL 611_ TRQQE 616_ LTALY 621_ QMQHL 626_ QYQQF 631_ LIQQQ 636_ YAQVL 641_ AQQQK 646_ AALSS 651_ QQQQQ 656_ LALLL 661_ QQFQT 666_ LKMRI 671_ SDQNI 676_ IPSVT 681_ RSVSV 686_ PDTGS 691_ IWELQ 696_ PTASQ 701_ PTVWE 706_ GGSVW 711_ DLPLD 716_ TTTPG 721_ PALEQ 726_ LQQLE 731_ KAKAA 736_ KLEQE 741_ RREAE 746_ MRAKR 751_ EEEER 756_ KRQEE 761_ LRRQQ 766_ EEILR 771_ RQQEE 776_ ERKRR 781_ EEEEL 786_ ARRKQ 791_ EEALR 796_ RQREQ 801_ EIALR 806_ RQREE 811_ EERQQ 816_ QEEAL 821_ RRLEE 826_ RRREE 831_ EERRK 836_ QEELL 841_ RKQEE 846_ EAAKW 851_ AREEE 856_ EAQRR 861_ LEENR 866_ LRMEE 871_ EAARL 876_ RHEEE 881_ ERKRK 886_ ELEVQ 891_ RQKEL 896_ MRQRQ 901_ QQQEA 906_ LRRLQ 911_ QQQQQ 916_ QQLAQ 921_ MKLPS 926_ SSTWG 931_ QQSNT 936_ TACQS 941_ QATLS 946_ LAEIQ 951_ KLEEE 956_ RERQL 961_ REEQR 966_ RQQRE 971_ LMKAL 976_ QQQQQ 981_ QQQQK 986_ LSGWG 991_ NVSKP 996_ SGTTK 1001_ SLLEI 1006_ QQEEA 1011_ RQMQK 1016_ QQQQQ 1021_ QQHQQ 1026_ PNRAR 1031_ NNTHS 1036_ NLHTS 1041_ IGNSV 1046_ WGSIN 1051_ TGPPN 1056_ QWASD 1061_ LVSSI 1066_ WSNAD 1071_ TKNSN 1076_ MGFWD 1081_ DAVKE 1086_ VGPRN 1091_ STNKN 1096_ KNNAS 1101_ LSKSV 1106_ GVSNR 1111_ QNKKV 1116_ EEEEK 1121_ LLKLF 1126_ QGVNK 1131_ AQDGF 1136_ TQWCE 1141_ QMLHA 1146_ LNTAN 1151_ NLDVP 1156_ TFVSF 1161_ LKEVE 1166_ SPYEV 1171_ HDYIR 1176_ AYLGD 1181_ TSEAK 1186_ EFAKQ 1191_ FLERR 1196_ AKQKA 1201_ NQQRQ 1206_ QQQLP 1211_ QQQQQ 1216_ QPPQQ 1221_ PPQQP 1226_ QQQDS 1231_ VWGMN 1236_ HSTLH 1241_ SVFQT 1246_ NQSNN 1251_ QQSNF 1256_ EAVQS 1261_ GKKKK 1266_ KQKMV 1271_ RADPS 1276_ LLGFS 1281_ VNASS 1286_ ERLNM 1291_GEIET
1: Key component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation (PubMed:22751931, PubMed:31439631, PubMed:35878012). In the 4EHP-GYF2 complex, acts as a factor that bridges EIF4E2 to ZFP36/TTP, linking translation repression with mRNA decay (PubMed:31439631). Also recruits and bridges the association of the 4EHP complex with the decapping effector protein DDX6, which is required for the ZFP36/TTP-mediated down-regulation of AU-rich mRNA (PubMed:31439631). May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors (PubMed:12771153). In association with EIF4E2, assists ribosome-associated quality control (RQC) by sequestering the mRNA cap, blocking ribosome initiation and decreasing the translational load on problematic messages. Part of a pathway that works in parallel to RQC-mediated degradation of the stalled nascent polypeptide (PubMed:32726578). GIGYF2 and EIF4E2 work downstream and independently of ZNF598, which seems to work as a scaffold that can recruit them to faulty mRNA even if alternative recruitment mechanisms may exist (PubMed:32726578)
2: (Microbial infection) Upon SARS coronavirus-2/SARS-CoV-2 infection, the interaction with non-structural protein 2 (nsp2) enhances GIGYF2 binding to EIF4E2 and increases repression of translation initiation of genes involved in antiviral innate immune response such as IFNB1