Q8AVJ0

PR
Gene name
eif3l (eif3eip, eif3s6ip)
Protein name
Eukaryotic translation initiation factor 3 subunit L
Names
eIF3l, Eukaryotic translation initiation factor 3 subunit 6-interacting protein, Eukaryotic translation initiation factor 3 subunit E-interacting protein
Species
Xenopus laevis (African clawed frog)
KEGG Pathway
xla:380037
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-65 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8AVJ0

Entry ID Method Resolution Chain Position Source
AF-Q8AVJ0-F1 Predicted AlphaFoldDB

No variants for Q8AVJ0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8AVJ0

No associated diseases with Q8AVJ0

12 regional properties for Q8AVJ0

Type Name Position InterPro Accession
domain Protein kinase domain 620 - 883 IPR000719
domain Ephrin receptor ligand binding domain 21 - 203 IPR001090
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 621 - 879 IPR001245
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 242 - 262 IPR001426
domain Sterile alpha motif domain 909 - 976 IPR001660
domain Fibronectin type III 324 - 532 IPR003961
active_site Tyrosine-protein kinase, active site 741 - 753 IPR008266
binding_site Protein kinase, ATP binding site 626 - 652 IPR017441
domain Tyrosine-protein kinase, catalytic domain 620 - 879 IPR020635
domain Ephrin receptor, transmembrane domain 544 - 617 IPR027936
domain Ephrin type-B receptor 1, ligand binding domain 22 - 197 IPR034231
domain EphB1, SAM domain 909 - 976 IPR042819

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
eukaryotic 43S preinitiation complex A protein complex composed of the 40S ribosomal subunit plus eIF1A, eIF3, and eIF2-GTP-bound methionyl-initiator methionine tRNA.
eukaryotic 48S preinitiation complex A protein complex composed of the small ribosomal subunit, eIF3, eIF1A, methionyl-initiatior methionine and a capped mRNA. The complex is initially positioned at the 5'-end of the capped mRNA.
eukaryotic translation initiation factor 3 complex A complex of several polypeptides that plays at least two important roles in protein synthesis: First, eIF3 binds to the 40S ribosome and facilitates loading of the Met-tRNA/eIF2.GTP ternary complex to form the 43S preinitiation complex. Subsequently, eIF3 apparently assists eIF4 in recruiting mRNAs to the 43S complex. The eIF3 complex contains five conserved core subunits, and may contain several additional proteins; the non-core subunits are thought to mediate association of the complex with specific sets of mRNAs.

1 GO annotations of molecular function

Name Definition
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.

2 GO annotations of biological process

Name Definition
formation of cytoplasmic translation initiation complex Joining of the large subunit, with release of IF2/eIF2 and IF3/eIF3. This leaves the functional ribosome at the AUG, with the methionyl/formyl-methionyl-tRNA positioned at the P site.
translational initiation The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSHAKEDYDS SYDPYSYQAD YDGHTGDPKQ DLAYERQYEQ QTYQVIPEVI KNFIQYFHKT
70 80 90 100 110 120
VSDLIDQKVY ELQASRVSSD LIDQKVYEIQ DIYENSWAKL TERFFKNAPW PEAEAIAPQV
130 140 150 160 170 180
GNDAVFLILY KELYYRHIYA KVTGGPTLEQ RFESYYNYCN LFNYILNADG PAPLELPNQW
190 200 210 220 230 240
LWDIIDEFIY QFQSFSQYRC KTAKKSEEEI EFLRSNPKIW NVHSVLNVLH SLVDKSNINR
250 260 270 280 290 300
QLEVYTSGGD PESVAGEYGR HSLYKMLGYF SLVGLLRLHS LLGDYYQAIK VLENIELNKK
310 320 330 340 350 360
SMYSRVPECQ VTTYYYVGFA YLMMRRYQDS IRVFANILLY IQRTKSMFQR TTYKYEMINK
370 380 390 400 410 420
QNEQMHALLS IALTMYPMRI DESIHTQLRE KYGDKMLRMQ KGDAQIYEEL FNYACPKFLS
430 440 450 460 470 480
PVVPNYDNVN PNYHKEPYLQ QLKVFLDEVQ QQAQLSTIRS FLKLYTTMPV AKLAGFLDLP
490 500 510 520 530 540
EQEFRIQLLV FKHKMKNLVW TSGISALEGE FQSASEVDFY IDKDMIHIAD TKVARRYGDF
550 560
FIRQIHKFEE LNKTLKKMSQ KP