Qki
entrez
19317
canonical
uniprot
Q9QYS9
canonical
ensembl
ENSMUSG00000062078
resolver
ensp
ENSMUSP00000046740
resolver
ensp
ENSMUSP00000156511
resolver
ensp
ENSMUSP00000156665
resolver
ensp
ENSMUSP00000258103
resolver
ensp
ENSMUSP00000258112
resolver
genesymbol
Qki
resolver
genesymbol_syn
Qk
resolver
genesymbol_syn
Qk1
resolver
uniprot
O88972
resolver
uniprot
Q61110
resolver
uniprot
Q78ZE4
resolver
uniprot
Q78ZE5
resolver
uniprot
Q8K4X9
resolver
uniprot
Q8K4Y0
resolver
uniprot
Q9CW34
resolver
uniprot
Q9QUH4
resolver
uniprot
Q9R2A8
resolver
uniprot
Q9Z246
resolver
uniprot_entry
QKI_MOUSE
resolver
uniprot_sec
O88972
resolver
uniprot_sec
Q61110
resolver
uniprot_sec
Q78ZE4
resolver
uniprot_sec
Q78ZE5
resolver
uniprot_sec
Q8K4X9
resolver
uniprot_sec
Q8K4Y0
resolver
uniprot_sec
Q9CW34
resolver
uniprot_sec
Q9QUH4
resolver
uniprot_sec
Q9R2A8
resolver
uniprot_sec
Q9Z246
resolver
amino_acid_sequence
MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Qki are the cause of quakingviable (qkv). Qkv is a spontaneous mutation resulting in hypomyelinization of the central and peripheral nervous systems. Mutant mice develop normally until postnatal day 10 when they display rapid tremors or 'quaking' that is especially pronounced in hindlimbs and experience convulsive tonic-clonic seizures as they mature (PubMed:8589716). Mice with qkv specifically lack isoform 3 and isoform 4 in myelin-forming cells, while isoform 1 is lacking in oligodendrocytes of severely affected tracts (PubMed:12888522). Mice with qkv also lack the PRKN gene product, suggesting that the absence of PRKN may also affect the phenotype (PubMed:15014970). {ECO:0000269|PubMed:12888522, ECO:0000269|PubMed:15014970, ECO:0000269|PubMed:8589716}.
uniprot
proteins
function
FUNCTION: RNA reader protein, which recognizes and binds specific RNAs, thereby regulating RNA metabolic processes, such as pre-mRNA splicing, circular RNA (circRNA) formation, mRNA export, mRNA stability and/or translation (PubMed:10535969, PubMed:11297509, PubMed:11917126, PubMed:12467586, PubMed:15568022, PubMed:31868295, PubMed:36088389). Involved in various cellular processes, such as mRNA storage into stress granules, apoptosis, lipid deposition, interferon response, glial cell fate and development (PubMed:10535969, PubMed:11297509, PubMed:11917126, PubMed:12467586, PubMed:15568022, PubMed:31868295). Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence (PubMed:16041388). Acts as a mRNA modification reader that specifically recognizes and binds mRNA transcripts modified by internal N(7)-methylguanine (m7G) (By similarity). Promotes the formation of circular RNAs (circRNAs) during the epithelial to mesenchymal transition and in cardiomyocytes: acts by binding to sites flanking circRNA-forming exons (PubMed:37272356). CircRNAs are produced by back-splicing circularization of pre-mRNAs (PubMed:37272356). Plays a central role in myelinization via 3 distinct mechanisms (PubMed:10864952, PubMed:11917126, PubMed:12467586, PubMed:15568022, PubMed:20956316, PubMed:21253564). First, acts by protecting and promoting stability of target mRNAs such as MBP, SIRT2 and CDKN1B, which promotes oligodendrocyte differentiation (PubMed:10864952, PubMed:15568022, PubMed:28188285). Second, participates in mRNA transport by regulating the nuclear export of MBP mRNA (PubMed:12467586). Finally, indirectly regulates mRNA splicing of MAG pre-mRNA during oligodendrocyte differentiation by acting as a negative regulator of MAG exon 12 alternative splicing: acts by binding to HNRNPA1 mRNA splicing factor, preventing its translation (PubMed:11917126, PubMed:20956316, PubMed:21253564). Involved in microglia differentiation and remyelination by regulating microexon alternative splicing of the Rho GTPase pathway (PubMed:33045062, PubMed:33378678). Involved in macrophage differentiation: promotes monocyte differentiation by regulating pre-mRNA splicing in naive peripheral blood monocytes (PubMed:36088389). Acts as an important regulator of muscle development: required for the contractile function of cardiomyocytes by regulating alternative splicing of cardiomyocyte transcripts (PubMed:33397958, PubMed:36627242). Acts as a negative regulator of thermogenesis by decreasing stability, nuclear export and translation of mRNAs encoding PPARGC1A and UCP1 (PubMed:31868295). Also required for visceral endoderm function and blood vessel development (PubMed:11892011, PubMed:16470614). May also play a role in smooth muscle development (PubMed:14706070). In addition to its RNA-binding activity, also acts as a nuclear transcription coactivator for SREBF2/SREBP2 (PubMed:33942715, PubMed:34021134). {ECO:0000250|UniProtKB:Q96PU8, ECO:0000269|PubMed:10535969, ECO:0000269|PubMed:10864952, ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:11892011, ECO:0000269|PubMed:11917126, ECO:0000269|PubMed:12467586, ECO:0000269|PubMed:14706070, ECO:0000269|PubMed:15568022, ECO:0000269|PubMed:16041388, ECO:0000269|PubMed:16470614, ECO:0000269|PubMed:20956316, ECO:0000269|PubMed:21253564, ECO:0000269|PubMed:28188285, ECO:0000269|PubMed:31868295, ECO:0000269|PubMed:33045062, ECO:0000269|PubMed:33378678, ECO:0000269|PubMed:33397958, ECO:0000269|PubMed:33942715, ECO:0000269|PubMed:34021134, ECO:0000269|PubMed:36088389, ECO:0000269|PubMed:36627242, ECO:0000269|PubMed:37272356}.; FUNCTION: [Isoform QKI5]: Nuclear isoform that acts as an indirect regulator of mRNA splicing (PubMed:11917126, PubMed:29021242). Regulates mRNA splicing of MAG pre-mRNA by inhibiting translation of HNRNPA1 mRNA, thereby preventing MAG exon 12 alternative splicing (PubMed:11917126, PubMed:21253564). Involved in oligodendrocyte differentiation by promoting stabilization of SIRT2 mRNA (PubMed:28188285). Acts as a negative regulator of the interferon response by binding to MAVS mRNA, down-regulating its expression (By similarity). Also inhibits the interferon response by binding to fibrinectin FN1 pre-mRNA, repressing EDA exon inclusion in FN1 (By similarity). Delays macrophage differentiation by binding to CSF1R mRNA, promoting its degradation (By similarity). In addition to its RNA-binding activity, also acts as a nuclear transcription coactivator for SREBF2/SREBP2, promoting SREBF2/SREBP2-dependent cholesterol biosynthesis (PubMed:33942715, PubMed:34021134). SREBF2/SREBP2-dependent cholesterol biosynthesis participates to myelinization and is required for eye lens transparency (PubMed:33942715, PubMed:34021134). {ECO:0000250|UniProtKB:Q96PU8, ECO:0000269|PubMed:11917126, ECO:0000269|PubMed:21253564, ECO:0000269|PubMed:28188285, ECO:0000269|PubMed:29021242, ECO:0000269|PubMed:33942715, ECO:0000269|PubMed:34021134}.; FUNCTION: [Isoform QKI6]: Cytosolic isoform that specifically recognizes and binds mRNA transcripts modified by internal N(7)-methylguanine (m7G) (By similarity). Interaction with G3BP1 promotes localization of m7G-containing mRNAs into stress granules in response to stress, thereby suppressing their translation (By similarity). Acts as a translational repressor for HNRNPA1 and GLI1 (PubMed:10535969, PubMed:16198329, PubMed:20956316, PubMed:29021242). Translation inhibition of HNRNPA1 during oligodendrocyte differentiation prevents inclusion of exon 12 in MAG pre-mRNA splicing (PubMed:20956316). Involved in astrocyte differentiation by regulating translation of target mRNAs (PubMed:33750804). {ECO:0000250|UniProtKB:Q96PU8, ECO:0000269|PubMed:10535969, ECO:0000269|PubMed:16198329, ECO:0000269|PubMed:20956316, ECO:0000269|PubMed:29021242, ECO:0000269|PubMed:33750804}.; FUNCTION: [Isoform QKI7]: Cytosolic isoform that specifically recognizes and binds mRNA transcripts modified by internal N(7)-methylguanine (m7G) (By similarity). Interaction with G3BP1 promotes localization of m7G-containing mRNAs into stress granules in response to stress, thereby suppressing their translation (By similarity). Acts as a negative regulator of angiogenesis by binding to mRNAs encoding CDH5, NLGN1 and TNFAIP6, promoting their degradation (PubMed:32732889). Can also induce apoptosis in the cytoplasm (PubMed:11297509). Heterodimerization with other isoforms results in nuclear translocation of isoform QKI7 and suppression of apoptosis (PubMed:11297509). Also binds some microRNAs: promotes stabilitation of miR-122 by mediating recruitment of poly(A) RNA polymerase TENT2, leading to 3' adenylation and stabilization of miR-122 (By similarity). {ECO:0000250|UniProtKB:Q96PU8, ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:32732889}.
uniprot
proteins
mass_dalton
37671
uniprot
proteins
mutagenesis
MUTAGEN 17; /note="Y->F: Impaired homodimerization."; /evidence="ECO:0000269|PubMed:22982292"; MUTAGEN 21; /note="L->A: Impaired homodimerization."; /evidence="ECO:0000269|PubMed:22982292"; MUTAGEN 48; /note="E->A: Impaired homodimerization."; /evidence="ECO:0000269|PubMed:22982292"; MUTAGEN 48; /note="E->G: In qk-Kt4; induces embryonic lethality possibly due to its inability to homodimerize."; /evidence="ECO:0000269|PubMed:10506177, ECO:0000269|PubMed:22982292, ECO:0000269|PubMed:8589716, ECO:0000269|PubMed:9671495"; MUTAGEN 157; /note="V->E: In qk-k24; induces embryonic lethality possibly due to blood vessel defects; prevents RNA-binding but not homodimerization."; /evidence="ECO:0000269|PubMed:10328999, ECO:0000269|PubMed:11892011, ECO:0000269|PubMed:12467586"; MUTAGEN 276..279; /note="PPGP->AAGA: Strongly impairs phosphorylation."; /evidence="ECO:0000269|PubMed:12682013"; MUTAGEN 285; /note="Y->F: Abolishes phosphorylation and RNA-binding; when associated with F-288; F-290; F-292 and F-303."; /evidence="ECO:0000269|PubMed:12682013"; MUTAGEN 288; /note="Y->F: Abolishes phosphorylation and RNA-binding; when associated with F-285; F-290; F-292 and F-303."; /evidence="ECO:0000269|PubMed:12682013"; MUTAGEN 290; /note="Y->F: Abolishes phosphorylation and RNA-binding; when associated with F-285; F-288; F-292 and F-303."; /evidence="ECO:0000269|PubMed:12682013"; MUTAGEN 292; /note="Y->F: Abolishes phosphorylation and RNA-binding; when associated with F-285; F-288; F-290 and F-303."; /evidence="ECO:0000269|PubMed:12682013"; MUTAGEN 303; /note="Y->F: Abolishes phosphorylation and RNA-binding; when associated with F-285; F-288; F-290 and F-292."; /evidence="ECO:0000269|PubMed:12682013"; MUTAGEN 324; /note="R->A: Abolishes nuclear localization; when associated with A-330."; /evidence="ECO:0000269|PubMed:10506177"; MUTAGEN 328; /note="Y->F: Does not affect nuclear localization."; /evidence="ECO:0000269|PubMed:10506177"; MUTAGEN 330; /note="R->A: Abolishes nuclear localization; when associated with A-324."; /evidence="ECO:0000269|PubMed:10506177
uniprot
proteins
post_translational_modification
PTM: Methylated by PRMT1. {ECO:0000269|PubMed:12529443}.; PTM: Tyrosine phosphorylated at its C-terminus, probably by FYN. Phosphorylation leads to decreased mRNA-binding affinity, affecting transport and/or stabilization of MBP mRNA. The level of Tyr phosphorylation in the developing myelin is highest in the first postnatal week (P7). During the vigorous accumulation of MBP mRNA between P7 and P20, phosphorylation in the developing myelin drastically declines. By the end of the fourth postnatal week (P28), phosphorylation is reduced approximately 90%. {ECO:0000269|PubMed:12682013, ECO:0000269|PubMed:15528192}.; PTM: Ubiquitinated by RNF6 in macrophages, leading to its degradation. {ECO:0000269|PubMed:36088389}.
uniprot
proteins
protein_family
Quaking family
uniprot
proteins
pubmed
10328999
uniprot
proteins
pubmed
10384037
uniprot
proteins
pubmed
10506177
uniprot
proteins
pubmed
10535969
uniprot
proteins
pubmed
10864952
uniprot
proteins
pubmed
11297509
uniprot
proteins
pubmed
11892011
uniprot
proteins
pubmed
11917126
uniprot
proteins
pubmed
12467586
uniprot
proteins
pubmed
12529443
uniprot
proteins
pubmed
12682013
uniprot
proteins
pubmed
12888522
uniprot
proteins
pubmed
14706070
uniprot
proteins
pubmed
15014970
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15528192
uniprot
proteins
pubmed
15568022
uniprot
proteins
pubmed
16041388
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16198329
uniprot
proteins
pubmed
16470614
uniprot
proteins
pubmed
20956316
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21253564
uniprot
proteins
pubmed
22982292
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
28188285
uniprot
proteins
pubmed
29021242
uniprot
proteins
pubmed
31868295
uniprot
proteins
pubmed
32732889
uniprot
proteins
pubmed
33045062
uniprot
proteins
pubmed
33378678
uniprot
proteins
pubmed
33397958
uniprot
proteins
pubmed
33750804
uniprot
proteins
pubmed
33942715
uniprot
proteins
pubmed
34021134
uniprot
proteins
pubmed
36088389
uniprot
proteins
pubmed
36627242
uniprot
proteins
pubmed
37272356
uniprot
proteins
pubmed
8589716
uniprot
proteins
pubmed
8987822
uniprot
proteins
pubmed
9315629
uniprot
proteins
pubmed
9671495
uniprot
proteins
pubmed
9778149
uniprot
proteins
sequence_length
341
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29021242, ECO:0000269|PubMed:8987822}. Nucleus {ECO:0000269|PubMed:29021242, ECO:0000269|PubMed:31868295, ECO:0000269|PubMed:8987822}.; SUBCELLULAR LOCATION: [Isoform QKI5]: Nucleus {ECO:0000269|PubMed:10506177, ECO:0000269|PubMed:29021242}. Cytoplasm {ECO:0000269|PubMed:10506177}. Note=Localizes predominantly in the nucleus and at lower levels in cytoplasm (PubMed:10506177, PubMed:29021242). It shuttles between the cytoplasm and the nucleus (PubMed:10506177). {ECO:0000269|PubMed:10506177, ECO:0000269|PubMed:29021242}.; SUBCELLULAR LOCATION: [Isoform QKI6]: Cytoplasm, cytosol {ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:20956316, ECO:0000269|PubMed:29021242}. Nucleus {ECO:0000269|PubMed:11297509}. Note=Localizes predominantly in the cytoplasm and at lower levels in nucleus. {ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:29021242}.; SUBCELLULAR LOCATION: [Isoform QKI7]: Cytoplasm, cytosol {ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:29021242}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q96PU8}. Nucleus {ECO:0000269|PubMed:11297509}. Note=Localizes predominantly in the cytoplasm and at much lower levels in nucleus (PubMed:11297509, PubMed:29021242). Shuttles between the cytosol and stress granules in response to stress (By similarity). {ECO:0000250|UniProtKB:Q96PU8, ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:29021242}.
uniprot
proteins