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 Q9XHR2

Entry ID Method Resolution Chain Position Source
AF-Q9XHR2-F1 Predicted AlphaFoldDB

No variants for Q9XHR2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9XHR2

No associated diseases with Q9XHR2

1 regional properties for Q9XHR2

Type Name Position InterPro Accession
domain Proteasome component (PCI) domain 316 - 523 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, 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.
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.

2 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.

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.
translation reinitiation A gene-specific translational control mechanism where the small ribosomal subunit remains attached to the mRNA following termination of translation, then resumes scanning on the same mRNA molecule and initiates again at a downstream start site. Reinitiation depends on de novo recruitment of the ternary complex that is required to recognize the next AUG codon.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P38249 RPG1 Eukaryotic translation initiation factor 3 subunit A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q14152 EIF3A Eukaryotic translation initiation factor 3 subunit A Homo sapiens (Human) PR
P23116 Eif3a Eukaryotic translation initiation factor 3 subunit A Mus musculus (Mouse) PR
Q9LD55 TIF3A1 Eukaryotic translation initiation factor 3 subunit A Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MATFAKPENA LKRAEELIHV GQKQSALQAL HDLITSKRYR SWQKPLEKIM MKYVELCVDL
70 80 90 100 110 120
RKGRFAKDGL IQYRIVCQQV NVSSLEDVIK HFMQLSNEKA EQAKSQVEAL EDALDVEDLE
130 140 150 160 170 180
ADKRPEDLML SFVSGEKGKD RSDKEVVTPW FKFLWETYRT VLEILRNNSK LEALYAMTAH
190 200 210 220 230 240
RAFQFCKQYK RTTEFRSCVR SIRNHLANLN KYRDQRDRPD LTAPESLQLY LDTRVEQLKV
250 260 270 280 290 300
ATELSLWQEA FRSVEDIHGL MTMVKKMPKP SILVVYYAKL TEIFWISDSH LYHAYAWLKL
310 320 330 340 350 360
FNLQKSYNKN LSQKDLQLIA SSVLLAALSV SPYDKKYGAF ETENEKERNM RLSNLVNFSL
370 380 390 400 410 420
DNKRENREMP SRPYLLSELA SKGVLSCASQ EVRDLYNLLE HRFLPLDLAS KVQPLLLKIS
430 440 450 460 470 480
KIGGKLSSAS SVPEVKLSQY ISALEKLTTL RVLQQASCIF KSIKIDMLSR MIPFFDFSVV
490 500 510 520 530 540
EKISVDAAKQ NFVAIKVDHL SGVVQFGTVD IESDGLSDHL SVLADSLNKA RIHICPPVKK
550 560 570 580 590 600
PSKLGESLIS LAAIVENEHK RLLARKSIIE KRKEELERQI LEKEKEEEKK RMSSQKKTVD
610 620 630 640 650 660
EERVRLLNEQ RQREQDRIRR EIEEKNKAEA KKMLEDLNKA GKKHVVVEGE LTKEAYMELA
670 680 690 700 710 720
RNEQLKERHE MEKKLQKFAK TMDYLERAKR QEEAPLIEQA FQKRLEEEKI LHEQEQLREI
730 740 750 760 770 780
ELSKQHHASD LQEKNRLSRM LEHKNALQER IIQERAAEFG RLKKERDERM NRLISSRKHE
790 800 810 820 830 840
RETVRKLMFY LNLEEQRIEM LREEEEARKR EAEERRKREE AERKAKLDAI AEKQRLREIE
850 860 870 880 890 900
LEEKAKATRE KLLKGSEAVR APDSAPVAQP PRESAAAAAA AAAAAPAPSK YIPKFKRGGD
910 920 930 940 950 960
SSSIPSGSRD EDRWGSRGPL RQDGPPARLD APSSRQDTDR WRGSRFPSNS TSSSSTWSRS
RN