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 A7MB16

Entry ID Method Resolution Chain Position Source
AF-A7MB16-F1 Predicted AlphaFoldDB

78 variants for A7MB16

Variant ID(s) Position Change Description Diseaes Association Provenance
rs109547901 48 A>V No EVA
rs723929995 68 A>T No EVA
rs453369396 74 A>T No EVA
rs470585031 143 D>G No EVA
rs453830548 145 L>V No EVA
rs526686975 146 K>E No EVA
rs474721825 147 D>E No EVA
rs440256503 147 D>N No EVA
rs454812608 148 R>P No EVA
rs438003027 149 P>A No EVA
rs452555654 150 Q>H No EVA
rs469388293 150 Q>P No EVA
rs467157079 152 A>G No EVA
rs432492892 152 A>T No EVA
rs447073958 153 D>G No EVA
rs481670165 155 I>M No EVA
rs468116700 158 V>G No EVA
rs447953570 159 I>V No EVA
rs475747536 164 V>L No EVA
rs137801532 167 V>G No EVA
rs462554535 173 E>D No EVA
rs466393080 237 L>I No EVA
rs463800365 273 E>G No EVA
rs443744605 274 C>G No EVA
rs471802108 274 C>W No EVA
rs441427022 278 Y>* No EVA
rs451830641 278 Y>H No EVA
rs472711150 279 S>R No EVA
rs452763021 280 V>G No EVA
rs436001920 286 D>G No EVA
rs467425999 288 T>A No EVA
rs436935615 289 S>Y No EVA
rs445066601 299 V>G No EVA
rs466318732 332 W>S No EVA
rs719149490 437 S>P No EVA
rs440322236 444 W>* No EVA
rs481476608 445 S>C No EVA
rs461351503 446 P>L No EVA
rs444507045 454 W>R No EVA
rs475916806 466 T>I No EVA
rs452701665 468 M>L No EVA
rs473663462 491 W>* No EVA
rs438962705 491 W>R No EVA
rs453529462 497 Y>* No EVA
rs467958573 498 L>F No EVA
rs436735121 498 L>M No EVA
rs437621260 499 C>* No EVA
rs454386011 499 C>G No EVA
rs468925366 505 T>S No EVA
rs445748673 506 P>T No EVA
rs477226219 509 T>P No EVA
rs481449434 540 F>C No EVA
rs461437302 543 E>A No EVA
rs454563440 566 V>M No EVA
rs444595100 574 L>I No EVA
rs449414203 593 Q>P No EVA
rs480647512 595 V>G No EVA
rs464045236 601 R>L No EVA
rs469286259 605 G>D No EVA
rs446003127 610 V>F No EVA
rs477395621 613 S>* No EVA
rs466970706 618 M>I No EVA
rs446920728 619 N>T No EVA
rs461436118 622 E>A No EVA
rs481589549 622 E>Q No EVA
rs447635200 623 H>L No EVA
rs447635200 623 H>R No EVA
rs482521405 640 T>P No EVA
rs459243887 645 W>G No EVA
rs470405344 651 N>H No EVA
rs456737348 651 N>K No EVA
rs476940058 656 W>G No EVA
rs476940058 656 W>R No EVA
rs444825976 667 S>N No EVA
rs479442633 667 S>R No EVA
rs465813708 669 D>H No EVA
rs459081742 760 D>E No EVA
rs382547002 763 V>I No EVA

No associated diseases with A7MB16

3 regional properties for A7MB16

Type Name Position InterPro Accession
domain RNA recognition motif domain 157 - 240 IPR000504
domain Translation initiation factor, beta propellor-like domain 479 - 674 IPR013979
domain eIF3B, RNA recognition motif 156 - 236 IPR034363

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, Stress granule
  • Localizes to stress granules following cellular stress
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytoplasmic stress granule A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress.
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.
eukaryotic translation initiation factor 3 complex, eIF3m An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3m.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.

3 GO annotations of molecular function

Name Definition
RNA binding Binding to an RNA molecule or a portion thereof.
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.
translation initiation factor binding Binding to a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation.

5 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.
IRES-dependent viral translational initiation Process by which viral mRNA translation is initiated, where a domain in the 5' untranslated region (UTR) of the viral mRNA called an internal ribosome entry site (IRES) binds the host 43S preinitiation complex, circumventing regular cap-dependent translation initiation.
regulation of translational initiation Any process that modulates the frequency, rate or extent of translational initiation.
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.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P55884 EIF3B Eukaryotic translation initiation factor 3 subunit B Homo sapiens (Human) PR
Q8JZQ9 Eif3b Eukaryotic translation initiation factor 3 subunit B Mus musculus (Mouse) PR
Q4G061 Eif3b Eukaryotic translation initiation factor 3 subunit B Rattus norvegicus (Rat) PR
Q9XWI6 eif-3.B Eukaryotic translation initiation factor 3 subunit B Caenorhabditis elegans PR
10 20 30 40 50 60
MQDAENVAAP EAAEQRAEPG PEQAAAEPSP GAEVARPGVQ EAAGGEDAEA GPGPEGPAEP
70 80 90 100 110 120
AADGEGKADA TPGATPPPPE ESSAQLAGEA PAEQAQDAAA EAGSEGAGGD PDGAAEDGGA
130 140 150 160 170 180
DEPSFSDPED FVDDVSEEEL LADVLKDRPQ EADGIDSVIV VDNVPQVGPD RLEKLKNVIH
190 200 210 220 230 240
KIFSKFGKIT NDFYPEEDGR TKGYIFLEYA SPAHALDAVK NADGYKLDKQ HTFRVNLFTD
250 260 270 280 290 300
FDKYMTISDE WDIPEKQPFK DLGNLRYWLE EAECRDQYSV IFESGDRTSI FWNDVKDPVS
310 320 330 340 350 360
IEERARWTET YVRWSPKGTY LATFHQRGIA LWGGEKFKQI QRFSHQGVQL IDFSPCERYL
370 380 390 400 410 420
VTFSPLMDTQ DDPQAIIIWD ILTGQKKRGF HCESSAHWPI FKWSHDGKFF ARMTLDTLSI
430 440 450 460 470 480
YETPSMGLLD KKSLKISGIK DFSWSPGGNI IAFWVPEDKD IPARVTLMQL PTRQEIRVRN
490 500 510 520 530 540
LFNVVDCKLH WQKNGDYLCV KVDRTPKGTQ GVVTNFEIFR MREKQVPVDV VEMKETIIAF
550 560 570 580 590 600
AWEPNGSKFA VLHGEAPRIS VSFYHVKNNG KIELIKMFDK QQANTIFWSP QGQFVVLAGL
610 620 630 640 650 660
RSMNGALAFV DTSDCTVMNI AEHYMASDVE WDPTGRYVVT SVSWWSHKVD NAYWLWTFQG
670 680 690 700 710 720
RLLQKNSKDR FCQLLWRPRP PTLLSQDQIK QIKKDLKKYS KIFEQKDRLS QSKASKELVE
730 740 750 760 770 780
RRRTMMEDFR KYRKMAQELY MEQKNARLEL RGGVDTDELD SNVDDWEEET IEFFVTEEII
PLGNQE