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 Q5E9B4

Entry ID Method Resolution Chain Position Source
AF-Q5E9B4-F1 Predicted AlphaFoldDB

78 variants for Q5E9B4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs472342547 2 P>A No EVA
rs134313873 2 P>Q No EVA
rs474567504 4 A>G No EVA
rs460951385 4 A>P No EVA
rs463423287 5 A>S No EVA
rs480196113 9 S>* No EVA
rs480196113 9 S>L No EVA
rs459928311 9 S>P No EVA
rs480196113 9 S>W No EVA
rs448635975 10 E>G No EVA
rs468613840 12 S>F No EVA
rs437150705 14 R>G No EVA
rs433238215 16 E>D No EVA
rs464526488 16 E>G No EVA
rs464526488 16 E>V No EVA
rs472331074 17 S>R No EVA
rs452236383 17 S>R No EVA
rs454713503 19 V>G No EVA
rs434685208 19 V>M No EVA
rs474646937 23 K>T No EVA
rs443228817 24 R>P No EVA
rs470724538 27 G>W No EVA
rs439325430 28 R>G No EVA
rs1118243418 28 R>K No EVA
rs459938899 28 R>S No EVA
rs480029166 29 R>G No EVA
rs442328984 29 R>H No EVA
rs462450345 30 S>R No EVA
rs482555374 32 E>A No EVA
rs482555374 32 E>V No EVA
rs450838395 33 D>A No EVA
rs464387676 36 R>P No EVA
rs446856283 37 E>G No EVA
rs465993007 38 T>A No EVA
rs434554213 42 L>V No EVA
rs454693792 45 I>L No EVA
rs468481239 46 I>L No EVA
rs437087636 47 T>P No EVA
rs456976017 48 D>H No EVA
rs470536205 49 H>L No EVA
rs439337611 50 R>L No EVA
rs473112690 52 S>I No EVA
rs442225299 52 S>R No EVA
rs451779579 65 G>A No EVA
rs471947678 70 A>D No EVA
rs471947678 70 A>G No EVA
rs460505579 71 A>G No EVA
rs442912241 76 T>A No EVA
rs483103154 82 V>A No EVA
rs483103154 82 V>E No EVA
rs450759682 85 V>E No EVA
rs457926588 90 R>P No EVA
rs446690739 95 R>G No EVA
rs453897917 102 E>D No EVA
rs473969937 103 S>C No EVA
rs442694554 103 S>T No EVA
rs462657239 105 Q>H No EVA
rs449300670 107 E>D No EVA
rs476294069 107 E>G No EVA
rs466063546 154 Q>H No EVA
rs452264466 154 Q>P No EVA
rs434673043 155 A>G No EVA
rs454528759 159 I>T No EVA
rs474559500 160 H>D No EVA
rs443363421 164 V>G No EVA
rs457002569 165 I>T No EVA
rs470661159 174 V>G No EVA
rs1118265716 179 R>K No EVA
rs799947572 180 E>G No EVA
rs442432069 187 F>I No EVA
rs439825816 194 C>G No EVA
rs434273912 232 V>G No EVA
rs454106117 233 I>V No EVA
rs446981558 237 K>N No EVA
rs462383307 278 F>I No EVA
rs472822231 289 V>E No EVA
rs439919778 290 A>V No EVA
rs132854745 352 L>Y No EVA

No associated diseases with Q5E9B4

No regional properties for Q5E9B4

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q5E9B4

Functions

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

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
eukaryotic translation initiation factor 2B complex A multisubunit guanine nucleotide exchange factor which catalyzes the exchange of GDP bound to initiation factor eIF2 for GTP, generating active eIF2-GTP. In humans, it is composed of five subunits, alpha, beta, delta, gamma and epsilon.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GTP binding Binding to GTP, guanosine triphosphate.
guanyl-nucleotide exchange factor activity Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.

6 GO annotations of biological process

Name Definition
central nervous system development The process whose specific outcome is the progression of the central nervous system over time, from its formation to the mature structure. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain and spinal cord. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
myelination The process in which myelin sheaths are formed and maintained around neurons. Oligodendrocytes in the brain and spinal cord and Schwann cells in the peripheral nervous system wrap axons with compact layers of their plasma membrane. Adjacent myelin segments are separated by a non-myelinated stretch of axon called a node of Ranvier.
oligodendrocyte development The process aimed at the progression of an oligodendrocyte over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell. An oligodendrocyte is a type of glial cell involved in myelinating the axons in the central nervous system.
ovarian follicle development The process whose specific outcome is the progression of the ovarian follicle over time, from its formation to the mature structure.
T cell receptor signaling pathway The series of molecular signals initiated by the cross-linking of an antigen receptor on a T cell.
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.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P32502 GCD7 Translation initiation factor eIF-2B subunit beta Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MPGAAAKGSE LSERIESFVE ALKRGGGRRS SEDMARETLG LLRRIITDHR WSNAGELMEL
70 80 90 100 110 120
IRREGRRMTA AQPSETTVGN MVRRVLRIIR EEYGRLHGRS DESDQQESLH KLLTSGGLSE
130 140 150 160 170 180
DFRSHYAQLQ SNIIEAINEL LVELEGTTEN IAAQALEHIH SNEVIMTIGF SRTVEAFLRE
190 200 210 220 230 240
AARKRKFHVI VAECAPFCQG HEMAVNLSKA GIETTVMTDA AIFAVMSRVN KVIIGTKTIL
250 260 270 280 290 300
ANGALRAVAG THTLALAAKH HSTPLIVCAP MFKLSPQFPN EEDSFHKFVA PEEVLPFTEG
310 320 330 340 350
DILEKVSVHC PVFDYVPPEL ITLFISNIGG NAPSYIYRLM SELYHPDDHV L