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

12 structures for P32497

Entry ID Method Resolution Chain Position Source
3JAP EM 490 A p 193-812 PDB
4U1C X-ray 350 A C 247-812 PDB
5H7U NMR - A 36-163 PDB
6FYX EM 305 A q 251-812 PDB
6FYY EM 305 A q 251-812 PDB
6GSM EM 515 A q 96-794 PDB
6GSN EM 575 A q 96-794 PDB
6ZCE EM 530 A q 1-812 PDB
6ZU9 EM 620 A q 1-812 PDB
8CAH EM 300 A q 1-812 PDB
8CAS EM 330 A q 1-812 PDB
AF-P32497-F1 Predicted AlphaFoldDB

5 variants for P32497

Variant ID(s) Position Change Description Diseaes Association Provenance
s13-895055 124 Q>P No SGRP
s13-894038 463 F>Y No SGRP
s13-893658 590 L>I No SGRP
s13-893247 727 F>V No SGRP
s13-893177 750 N>S No SGRP

No associated diseases with P32497

2 regional properties for P32497

Type Name Position InterPro Accession
domain Proteasome component (PCI) domain 608 - 797 IPR000717
domain Eukaryotic translation initiation factor 3 subunit C, N-terminal domain 243 - 639 IPR008905

Functions

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

6 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.
multi-eIF complex A multifactor complex composed of multiple translation initiation factors and the initiatior tRNAiMet, which is ready to bind to the small (40S) ribosome to form the 43S preinitiation complex. In S. cerevisiae, this complex is composed of eIF1, eIF2, eIF3, and eIF5.

3 GO annotations of molecular function

Name Definition
mRNA binding Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.
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.

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
MSRFFSSNYE YDVASSSSEE DLLSSSEEDL LSSSSSESEL DQESDDSFFN ESESESEADV
70 80 90 100 110 120
DSDDSDAKPY GPDWFKKSEF RKQGGGSNKF LKSSNYDSSD EESDEEDGKK VVKSAKEKLL
130 140 150 160 170 180
DEMQDVYNKI SQAENSDDWL TISNEFDLIS RLLVRAQQQN WGTPNIFIKV VAQVEDAVNN
190 200 210 220 230 240
TQQADLKNKA VARAYNTTKQ RVKKVSRENE DSMAKFRNDP ESFDKEPTAD LDISANGFTI
250 260 270 280 290 300
SSSQGNDQAV QEDFFTRLQT IIDSRGKKTV NQQSLISTLE ELLTVAEKPY EFIMAYLTLI
310 320 330 340 350 360
PSRFDASANL SYQPIDQWKS SFNDISKLLS ILDQTIDTYQ VNEFADPIDF IEDEPKEDSD
370 380 390 400 410 420
GVKRILGSIF SFVERLDDEF MKSLLNIDPH SSDYLIRLRD EQSIYNLILR TQLYFEATLK
430 440 450 460 470 480
DEHDLERALT RPFVKRLDHI YYKSENLIKI METAAWNIIP AQFKSKFTSK DQLDSADYVD
490 500 510 520 530 540
NLIDGLSTIL SKQNNIAVQK RAILYNIYYT ALNKDFQTAK DMLLTSQVQT NINQFDSSLQ
550 560 570 580 590 600
ILFNRVVVQL GLSAFKLCLI EECHQILNDL LSSSHLREIL GQQSLHRISL NSSNNASADE
610 620 630 640 650 660
RARQCLPYHQ HINLDLIDVV FLTCSLLIEI PRMTAFYSGI KVKRIPYSPK SIRRSLEHYD
670 680 690 700 710 720
KLSFQGPPET LRDYVLFAAK SMQKGNWRDS VKYLREIKSW ALLPNMETVL NSLTERVQVE
730 740 750 760 770 780
SLKTYFFSFK RFYSSFSVAK LAELFDLPEN KVVEVLQSVI AELEIPAKLN DEKTIFVVEK
790 800 810
GDEITKLEEA MVKLNKEYKI AKERLNPPSN RR