Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q8QZY1

Entry ID Method Resolution Chain Position Source
AF-Q8QZY1-F1 Predicted AlphaFoldDB

34 variants for Q8QZY1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389374428 3 Y>* No EVA
rs3406188471 31 K>R No EVA
rs3406393039 32 Q>H No EVA
rs3389352862 57 Q>H No EVA
rs3389374405 109 N>I No EVA
rs3389374564 122 V>D No EVA
rs3389388678 127 V>I No EVA
rs3389369613 173 P>H No EVA
rs218487852 210 G>E No EVA
rs245461460 212 M>I No EVA
rs31583179 221 V>I No EVA
rs3389374553 258 G>R No EVA
rs3389374480 259 E>K No EVA
rs3389366506 269 L>F No EVA
rs3389366505 270 G>D No EVA
rs3389369628 317 Y>F No EVA
rs3389382929 326 M>K No EVA
rs3389341803 354 T>I No EVA
rs3389341822 364 N>D No EVA
rs3389341856 380 M>I No EVA
rs3389374522 385 S>N No EVA
rs3389369642 386 I>L No EVA
rs3389366468 389 Q>* No EVA
rs3406021139 407 Q>H No EVA
rs3389382973 423 P>H No EVA
rs3389379146 425 V>M No EVA
rs3389372827 433 P>L No EVA
rs3405775196 438 E>Q No EVA
rs3389377374 493 F>L No EVA
rs3389335549 531 A>T No EVA
rs3389341798 532 D>Y No EVA
rs3389374454 538 R>C No EVA
rs3406276847 545 R>* No EVA
rs13465611 548 H>L No EVA

No associated diseases with Q8QZY1

7 regional properties for Q8QZY1

Type Name Position InterPro Accession
domain FERM domain 17 - 298 IPR000299
domain FERM adjacent 308 - 354 IPR014847
domain FERM, N-terminal 21 - 83 IPR018979
domain FERM, C-terminal PH-like domain 214 - 302 IPR018980
conserved_site FERM conserved site 71 - 100 IPR019747
domain FERM central domain 103 - 210 IPR019748
domain Band 4.1 domain 13 - 210 IPR019749

Functions

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

6 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.
fibrillar center A structure found most metazoan nucleoli, but not usually found in lower eukaryotes; surrounded by the dense fibrillar component; the zone of transcription from multiple copies of the pre-rRNA genes is in the border region between these two structures.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

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.

3 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.
viral translational termination-reinitiation A process which occurs as part of viral mRNA translation which allows expression of a downstream open reading frame (ORF) in a dicistronic mRNA. In this process, ribosomes translate the upstream ORF but following termination, a proportion of 40S subunits remain tethered to the mRNA and go on to re-initiate translation at the start codon of the downstream ORF.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3ZCK1 EIF3L Eukaryotic translation initiation factor 3 subunit L Bos taurus (Bovine) PR
Q5F428 EIF3L Eukaryotic translation initiation factor 3 subunit L Gallus gallus (Chicken) PR
A5A6M4 EIF3L Eukaryotic translation initiation factor 3 subunit L Pan troglodytes (Chimpanzee) PR
Q9Y262 EIF3L Eukaryotic translation initiation factor 3 subunit L Homo sapiens (Human) PR
Q6P878 eif3l Eukaryotic translation initiation factor 3 subunit L Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
Q7T2A5 eif3l Eukaryotic translation initiation factor 3 subunit L Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MSYPADDYES EAAYDPYAYP GDYDMHTGDP KQDLAYERQY EQQTYQVIPE VIKNFIQYFH
70 80 90 100 110 120
KTVSDLIDQK VYELQASRVS SDVIDQKVYE IQDIYENSWT KLTERFFKNT PWPEAEAIAP
130 140 150 160 170 180
QVGNDAVFLI LYKELYYRHI YAKVSGGPSL EQRFESYYNY CNLFNYILNA DGPAPLELPN
190 200 210 220 230 240
QWLWDIIDEF IYQFQSFSQY RCKTAKKSEG EMDFLRSNPK VWNVHSVLNV LHSLVDKSNI
250 260 270 280 290 300
NRQLEVYTSG GDPESVAGEY GRHSLYKMLG YFSLVGLLRL HSLLGDYYQA IKVLENIELN
310 320 330 340 350 360
KKSMYSRVPE CQVTTYYYVG FAYLMMRRYQ DAIRVFANIL LYIQRTKSMF QRTTYKYEMI
370 380 390 400 410 420
NKQNEQMHAL LAIALTMYPM RIDESIHLQL REKYGDKMLR MQKGDPQVYE ELFSYACPKF
430 440 450 460 470 480
LSPVVPNYDN VHPNYHKEPF LQQLKVFSDE VQQQAQLSTI RSFLKLYTTM PVAKLAGFLD
490 500 510 520 530 540
LTEQEFRIQL LVFKHKMKNL VWTSGISALD GEFQSASEVD FYIDKDMIHI ADTKVARRYG
550 560
DFFIRQIHKF EELNRTLKKM GQRP