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

14 structures for P38249

Entry ID Method Resolution Chain Position Source
3JAP EM 490 A o 1-495 PDB
4K51 X-ray 265 A A/B 276-494 PDB
4U1C X-ray 350 A A 225-495 PDB
4U1D X-ray 330 A A/B/C 1-494 PDB
4U1E X-ray 200 A I 1-347 PDB
6FYX EM 305 A o 1-964 PDB
6FYY EM 305 A o 1-964 PDB
6GSM EM 515 A o 5-492 PDB
6GSN EM 575 A o 5-492 PDB
6ZCE EM 530 A o 1-964 PDB
6ZU9 EM 620 A o 1-964 PDB
8CAH EM 300 A o 1-964 PDB
8CAS EM 330 A o 1-964 PDB
AF-P38249-F1 Predicted AlphaFoldDB

20 variants for P38249

Variant ID(s) Position Change Description Diseaes Association Provenance
s02-398144 43 A>V No SGRP
s02-397776 166 L>I No SGRP
s02-397178 365 E>V No SGRP
s02-396966 436 A>T No SGRP
s02-396941 444 S>Y No SGRP
s02-396923 450 K>R No SGRP
s02-396864 470 L>V No SGRP
s02-396773 500 A>V No SGRP
s02-396755 506 E>G No SGRP
s02-396720 518 Q>E No SGRP
s02-396706 522 E>D No SGRP
s02-396699 525 D>N No SGRP
s02-396584 563 V>A No SGRP
s02-396030 748 T>A No SGRP
s02-395922 784 D>N No SGRP
s02-395847 809 A>T No SGRP
s02-395750 841 A>V No SGRP
s02-395600 891 T>I No SGRP
s02-395501 924 G>A No SGRP
s02-395384 963 G>A No SGRP

No associated diseases with P38249

1 regional properties for P38249

Type Name Position InterPro Accession
conserved_site Cytochrome P450, conserved site 494 - 503 IPR017972

Functions

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

9 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.
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.
incipient cellular bud site The portion of the budding yeast plasma membrane where a daughter cell will emerge. The yeast marks this spot with bud-site selection proteins before bud emergence occurs. Actin is polarized to this spot just prior to and during bud emergence.
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.

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.
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.
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.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q14152 EIF3A Eukaryotic translation initiation factor 3 subunit A Homo sapiens (Human) PR
Q9XHR2 TIF3A1 Eukaryotic translation initiation factor 3 subunit A Zea mays (Maize) 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
MAPPPFRPEN AIKRADELIS VGEKQAALQS LHDFITARRI RWATPSTVEP VVFKFLEIGV
70 80 90 100 110 120
ELKKGKLLKD GLHQYKKLIQ GSTEGLVSVG AVARKFIDLV ESKIASEQTR ADELQKQEID
130 140 150 160 170 180
DDLEGGVTPE NLLISVYESD QSVAGFNDEA ITSWLRFTWE SYRAVLDLLR NNALLEITYS
190 200 210 220 230 240
GVVKKTMHFC LKYQRKNEFK RLAEMLRQHL DAANYQQSKS GNNLVDLSDA DTLQRYLDQR
250 260 270 280 290 300
FQQVDVSVKL ELWHEAYRSI EDVFHLMKIS KRAPKPSTLA NYYENLVKVF FVSGDPLLHT
310 320 330 340 350 360
TAWKKFYKLY STNPRATEEE FKTYSSTIFL SAISTQLDEI PSIGYDPHLR MYRLLNLDAK
370 380 390 400 410 420
PTRKEMLQSI IEDESIYGKV DEELKELYDI IEVNFDVDTV KQQLENLLVK LSSKTYFSQY
430 440 450 460 470 480
IAPLRDVIMR RVFVAASQKF TTVSQSELYK LATLPAPLDL SAWDIEKSLL QAAVEDYVSI
490 500 510 520 530 540
TIDHESAKVT FAKDPFDIFA STASKEVSEE ENTEPEVQEE KEETDEALGP QETEDGEEKE
550 560 570 580 590 600
EESDPVIIRN SYIHNKLLEL SNVLHDVDSF NNASYMEKVR IARETLIKKN KDDLEKISKI
610 620 630 640 650 660
VDERVKRSQE QKQKHMEHAA LHAEQDAEVR QQRILEEKAA IEAKLEEEAH RRLIEKKKRE
670 680 690 700 710 720
FEAIKEREIT KMITEVNAKG HVYIDPNEAK SLDLDTIKQV IIAEVSKNKS ELESRMEYAM
730 740 750 760 770 780
KKLDHTERAL RKVELPLLQK EVDKLQETDT ANYEAMKKKI VDAAKAEYEA RMADRKNLVM
790 800 810 820 830 840
VYDDYLKFKE HVSGTKESEL AAIRNQKKAE LEAAKKARIE EVRKRRYEEA IARRKEEIAN
850 860 870 880 890 900
AERQKRAQEL AEATRKQREI EEAAAKKSTP YSFRAGNREP PSTPSTLPKA TVSPDKAKLD
910 920 930 940 950 960
MIAQKQREME EAIEQRLAGR TAGGSSPATP ATPATPATPT PSSGPKKMTM AEKLRAKRLA
KGGR