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 Q3ZCK1

Entry ID Method Resolution Chain Position Source
AF-Q3ZCK1-F1 Predicted AlphaFoldDB

72 variants for Q3ZCK1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs479336571 5 A>T No EVA
rs468202463 10 S>P No EVA
rs435218879 11 E>G No EVA
rs462047964 21 G>S No EVA
rs470519413 57 Q>* No EVA
rs439291416 58 Y>F No EVA
rs3423208581 88 V>L No EVA
rs441805670 89 Y>* No EVA
rs459956816 102 L>F No EVA
rs476303777 124 N>T No EVA
rs137752854 125 D>N No EVA
rs438373953 148 P>S No EVA
rs478927192 149 S>Y No EVA
rs459205612 215 L>F No EVA
rs477721611 215 L>P No EVA
rs461709570 259 E>G No EVA
rs450778165 260 Y>* No EVA
rs480516198 260 Y>D No EVA
rs462842305 263 H>L No EVA
rs462842305 263 H>P No EVA
rs478095434 264 S>Y No EVA
rs444972630 268 M>V No EVA
rs464699389 273 S>G No EVA
rs479930474 288 Y>C No EVA
rs471731160 341 L>V No EVA
rs471897265 362 K>N No EVA
rs438799258 364 N>I No EVA
rs460508334 365 E>D No EVA
rs479311556 366 Q>H No EVA
rs443103852 371 L>V No EVA
rs450245156 382 I>T No EVA
rs465061386 389 Q>R No EVA
rs447203172 392 E>V No EVA
rs435939012 393 K>N No EVA
rs454723597 395 G>E No EVA
rs469886653 397 K>N No EVA
rs437014535 405 D>A No EVA
rs452248189 408 V>G No EVA
rs471899626 414 S>I No EVA
rs472629089 428 Y>N No EVA
rs461672506 431 V>A No EVA
rs483305782 432 H>P No EVA
rs443812736 434 N>K No EVA
rs459096584 443 Q>K No EVA
rs477152613 446 V>G No EVA
rs447338629 447 F>V No EVA
rs480849147 463 F>L No EVA
rs720855515 464 L>V No EVA
rs447976903 468 T>P No EVA
rs470084211 470 M>V No EVA
rs452216612 472 V>L No EVA
rs454271043 480 D>A No EVA
rs434570712 480 D>H No EVA
rs472667525 482 T>P No EVA
rs442882990 483 E>G No EVA
rs476942097 486 F>I No EVA
rs459170516 489 Q>K No EVA
rs441345298 492 V>F No EVA
rs459315996 495 H>N No EVA
rs480888084 497 M>L No EVA
rs463319346 502 W>S No EVA
rs482187474 506 I>V No EVA
rs466284047 513 F>L No EVA
rs436428743 514 Q>L No EVA
rs454849361 515 S>A No EVA
rs437174995 519 V>G No EVA
rs452800897 521 F>I No EVA
rs441382424 522 Y>* No EVA
rs471254904 522 Y>C No EVA
rs459751294 524 D>H No EVA
rs474513343 525 K>R No EVA
rs445461092 546 Q>P No EVA

No associated diseases with Q3ZCK1

1 regional properties for Q3ZCK1

Type Name Position InterPro Accession
domain Proteasome component (PCI) domain 331 - 537 IPR000717

Functions

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

5 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.
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
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
Q8QZY1 Eif3l Eukaryotic translation initiation factor 3 subunit L Mus musculus (Mouse) 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 PWPEAETIAP
130 140 150 160 170 180
QVGNDAVFLI LYKELYYRHI YAKVSGGPSL EQRFESYYNY CNLFNYILNA DGPAPLELPN
190 200 210 220 230 240
QWLWDIIDEF IYQFQSFSQY RCKTAKKSEE EIDFLRSNPK IWNVHSVLNV 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 ELFSYSCPKF
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