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 Q10425

Entry ID Method Resolution Chain Position Source
AF-Q10425-F1 Predicted AlphaFoldDB

9 variants for Q10425

Variant ID(s) Position Change Description Diseaes Association Provenance
I_4310629_C_A 17 D>E No Jeffares_SNPs
I_4310819_T_C 81 F>L No Jeffares_SNPs
I_4310886_G_C 103 G>A No Jeffares_SNPs
I_4311096_G_A 173 R>H No Jeffares_SNPs
I_4311293_G_A 239 D>N No Jeffares_SNPs
I_4311923_C_T 449 P>S No Jeffares_SNPs
I_4312118_A_C 514 K>Q No Jeffares_SNPs
I_4312264_G_C 562 Q>H No Jeffares_SNPs
I_4312618_T_G 680 D>E No Jeffares_SNPs

No associated diseases with Q10425

1 regional properties for Q10425

Type Name Position InterPro Accession
domain RecF/RecN/SMC, N-terminal 53 - 1053 IPR003395

Functions

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

8 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.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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, eIF3e An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3e.
eukaryotic translation initiation factor 3 complex, eIF3m An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3m.

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.

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
MSEILIEEIK DQIVVKDEEI DVSELEVKLN VTKPVGYDTV VVIEGAPVVE EAKQQDFFRF
70 80 90 100 110 120
LSSKVLAKIG KVKENGFYMP FEEKNGKKMS LGLVFADFEN VDGADLCVQE LDGKQILKNH
130 140 150 160 170 180
TFVVRKLNQL EKAFSTPDEF SFEEREFKER EHLRSWLTDY YGRDQFISYY GNRVSVNWNR
190 200 210 220 230 240
KSDVPEQIVD RENWTETYVQ WSPMGTYLVS LHLRGIQLWG GESWGMCARF LHPYVKFVDF
250 260 270 280 290 300
SPNEKYLVSW SYEPVRLPPI GHPARETMPF TDDDEGKHCF VWDIASGRIL RSFKIPPQPE
310 320 330 340 350 360
GSKDGKKVIW PIFKWSADDK YLARVTVGQS ISVYETPSLA LVDKKTIKID GVQNFEWCPV
370 380 390 400 410 420
SDALGRDSKE QLLAYWTPEI TNQPARVALI SIPSKSTIRT KNLFNVSDCK LYWQSNGDYL
430 440 450 460 470 480
CVKVDRHTKT KKSTFSNLEI FRIREKNIPV EVVDLKDVVL NFAWEPKSDR FAIISANDQV
490 500 510 520 530 540
LNSTNVKTNL SFYGFEQKKN TPSTFRHIIT FDKKTCNSLF MAPKGRFMVA ATLGSSTQYD
550 560 570 580 590 600
LEFYDLDFDT EKKEPDALAN VQQIGSAEHF GMTELEWDPS GRYVTTSSTI WRHKLENGYR
610 620 630 640 650 660
LCDFRGTLLR EEMIGEFKQF IWRPRPPSPL TKEDMKKIRK KLKDYNRLFD EEDIAEQSSA
670 680 690 700 710 720
NRELAARRRQ LISEWQKYRD EVIARVAEER AITGQPAITV PAEEEEIIQE TVEEVISEEI
EPVED