QRIC1_HUMAN
ID QRIC1_HUMAN Reviewed; 776 AA.
AC Q2TAL8; Q4G0F7; Q7L621; Q8TEA5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Transcriptional regulator QRICH1 {ECO:0000305};
DE AltName: Full=Glutamine-rich protein 1;
GN Name=QRICH1 {ECO:0000312|HGNC:HGNC:24713};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-353 AND LYS-358, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY ER STRESS, AND DOMAIN.
RX PubMed=33384352; DOI=10.1126/science.abb6896;
RA You K., Wang L., Chou C.H., Liu K., Nakata T., Jaiswal A., Yao J.,
RA Lefkovith A., Omar A., Perrigoue J.G., Towne J.E., Regev A., Graham D.B.,
RA Xavier R.J.;
RT "QRICH1 dictates the outcome of ER stress through transcriptional control
RT of proteostasis.";
RL Science 371:0-0(2021).
RN [10]
RP INVOLVEMENT IN VERBRAS, AND VARIANT VERBRAS 652-ARG--HIS-776 DEL.
RX PubMed=28692176; DOI=10.1111/cge.13096;
RA Ververi A., Splitt M., Dean J.C.S., Brady A.F.;
RT "Phenotypic spectrum associated with de novo mutations in QRICH1 gene.";
RL Clin. Genet. 93:286-292(2018).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN VERBRAS, VARIANTS VERBRAS
RP 511-ARG--HIS-776 DEL AND 536-ARG--HIS-776 DEL, AND CHARACTERIZATION OF
RP VARIANT VERBRAS 536-ARG--HIS-776 DEL.
RX PubMed=30281152; DOI=10.1111/cge.13457;
RA Lui J.C., Jee Y.H., Lee A., Yue S., Wagner J., Donnelly D.E., Vogt K.S.,
RA Baron J.;
RT "QRICH1 mutations cause a chondrodysplasia with developmental delay.";
RL Clin. Genet. 95:160-164(2019).
RN [12]
RP INVOLVEMENT IN VERBRAS, AND VARIANTS VERBRAS 652-ARG--HIS-776 DEL AND
RP ASN-736.
RX PubMed=33009816; DOI=10.1111/cge.13853;
RA Foehrenbach M., Jamra R.A., Borkhardt A., Brozou T., Muschke P., Popp B.,
RA Rey L.K., Schaper J., Surowy H., Zenker M., Zweier C., Wieczorek D.,
RA Redler S.;
RT "QRICH1 variants in Ververi-Brady syndrome-delineation of the genotypic and
RT phenotypic spectrum.";
RL Clin. Genet. 99:199-207(2021).
CC -!- FUNCTION: Transcriptional regulator that acts as a mediator of the
CC integrated stress response (ISR) through transcriptional control of
CC protein homeostasis under conditions of ER stress (PubMed:33384352).
CC Controls the outcome of the unfolded protein response (UPR) which is an
CC ER-stress response pathway (PubMed:33384352). ER stress induces QRICH1
CC translation by a ribosome translation re-initiation mechanism in
CC response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced
CC QRICH1 regulates a transcriptional program associated with protein
CC translation, protein secretion-mediated proteotoxicity and cell death
CC during the terminal UPR (PubMed:33384352). May cooperate with ATF4
CC transcription factor signaling to regulate ER homeostasis which is
CC critical for cell viability (PubMed:33384352). Up-regulates
CC CASP3/caspase-3 activity in epithelial cells under ER stress. Central
CC regulator of proteotoxicity associated with ER stress-mediated
CC inflammatory diseases in the intestines and liver (PubMed:33384352).
CC Involved in chondrocyte hypertrophy, a process required for normal
CC longitudinal bone growth (PubMed:30281152).
CC {ECO:0000269|PubMed:30281152, ECO:0000269|PubMed:33384352}.
CC -!- INTERACTION:
CC Q2TAL8; Q03989: ARID5A; NbExp=3; IntAct=EBI-2798044, EBI-948603;
CC Q2TAL8; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-2798044, EBI-1012434;
CC Q2TAL8; H3BRN8: C15orf65; NbExp=3; IntAct=EBI-2798044, EBI-18394323;
CC Q2TAL8; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-2798044, EBI-11976299;
CC Q2TAL8; P40199: CEACAM6; NbExp=3; IntAct=EBI-2798044, EBI-4314501;
CC Q2TAL8; O43186: CRX; NbExp=6; IntAct=EBI-2798044, EBI-748171;
CC Q2TAL8; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2798044, EBI-3867333;
CC Q2TAL8; Q9NQM4: DNAAF6; NbExp=3; IntAct=EBI-2798044, EBI-10239299;
CC Q2TAL8; A8MTA8-2: FAM166B; NbExp=3; IntAct=EBI-2798044, EBI-12160437;
CC Q2TAL8; Q14192: FHL2; NbExp=3; IntAct=EBI-2798044, EBI-701903;
CC Q2TAL8; Q13643: FHL3; NbExp=6; IntAct=EBI-2798044, EBI-741101;
CC Q2TAL8; Q5TD97: FHL5; NbExp=3; IntAct=EBI-2798044, EBI-750641;
CC Q2TAL8; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-2798044, EBI-10172181;
CC Q2TAL8; Q96IK5: GMCL1; NbExp=5; IntAct=EBI-2798044, EBI-2548508;
CC Q2TAL8; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-2798044, EBI-3957665;
CC Q2TAL8; Q9UJY1: HSPB8; NbExp=6; IntAct=EBI-2798044, EBI-739074;
CC Q2TAL8; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-2798044, EBI-9089060;
CC Q2TAL8; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-2798044, EBI-9478422;
CC Q2TAL8; Q14847-2: LASP1; NbExp=3; IntAct=EBI-2798044, EBI-9088686;
CC Q2TAL8; P52954: LBX1; NbExp=3; IntAct=EBI-2798044, EBI-20141748;
CC Q2TAL8; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-2798044, EBI-12039345;
CC Q2TAL8; Q969G2: LHX4; NbExp=3; IntAct=EBI-2798044, EBI-2865388;
CC Q2TAL8; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2798044, EBI-11742507;
CC Q2TAL8; P61968: LMO4; NbExp=3; IntAct=EBI-2798044, EBI-2798728;
CC Q2TAL8; P50221: MEOX1; NbExp=3; IntAct=EBI-2798044, EBI-2864512;
CC Q2TAL8; A7E2Y1-2: MYH7B; NbExp=3; IntAct=EBI-2798044, EBI-12813813;
CC Q2TAL8; Q14938: NFIX; NbExp=3; IntAct=EBI-2798044, EBI-8476987;
CC Q2TAL8; Q14938-5: NFIX; NbExp=3; IntAct=EBI-2798044, EBI-12024662;
CC Q2TAL8; P23511-2: NFYA; NbExp=3; IntAct=EBI-2798044, EBI-11061759;
CC Q2TAL8; Q9UBE8: NLK; NbExp=3; IntAct=EBI-2798044, EBI-366978;
CC Q2TAL8; P26367: PAX6; NbExp=3; IntAct=EBI-2798044, EBI-747278;
CC Q2TAL8; Q7Z3K3: POGZ; NbExp=7; IntAct=EBI-2798044, EBI-1389308;
CC Q2TAL8; P78424: POU6F2; NbExp=3; IntAct=EBI-2798044, EBI-12029004;
CC Q2TAL8; P31321: PRKAR1B; NbExp=3; IntAct=EBI-2798044, EBI-2805516;
CC Q2TAL8; Q9UHX1: PUF60; NbExp=3; IntAct=EBI-2798044, EBI-1053259;
CC Q2TAL8; Q96I25: RBM17; NbExp=4; IntAct=EBI-2798044, EBI-740272;
CC Q2TAL8; P59797: SELENOV; NbExp=3; IntAct=EBI-2798044, EBI-10216195;
CC Q2TAL8; P49903: SEPHS1; NbExp=8; IntAct=EBI-2798044, EBI-714091;
CC Q2TAL8; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-2798044, EBI-747107;
CC Q2TAL8; Q8IYB5-2: SMAP1; NbExp=3; IntAct=EBI-2798044, EBI-12061577;
CC Q2TAL8; Q02086-2: SP2; NbExp=3; IntAct=EBI-2798044, EBI-9088579;
CC Q2TAL8; Q8NEQ6: SRARP; NbExp=3; IntAct=EBI-2798044, EBI-17858294;
CC Q2TAL8; Q96M29: TEKT5; NbExp=3; IntAct=EBI-2798044, EBI-10239812;
CC Q2TAL8; O94842: TOX4; NbExp=5; IntAct=EBI-2798044, EBI-948613;
CC Q2TAL8; Q13077: TRAF1; NbExp=6; IntAct=EBI-2798044, EBI-359224;
CC Q2TAL8; Q12933: TRAF2; NbExp=3; IntAct=EBI-2798044, EBI-355744;
CC Q2TAL8; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-2798044, EBI-11975223;
CC Q2TAL8; Q15942: ZYX; NbExp=3; IntAct=EBI-2798044, EBI-444225;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30281152,
CC ECO:0000269|PubMed:33384352}. Cytoplasm {ECO:0000269|PubMed:30281152}.
CC Cell membrane {ECO:0000269|PubMed:30281152}.
CC -!- INDUCTION: Regulated at the translational level via an alternative
CC ribosome re-initiation mechanism in response to various stress such as
CC endoplasmic reticulum stress or oxidative stress (PubMed:33384352). In
CC the absence of stress, ribosomes re-initiate translation at an
CC inhibitory upstream open reading frames (uORFs) of the QRICH1
CC transcript, which preclude QRICH1 translation. In response to stress
CC and subsequent EIF2S1/eIF-2-alpha phosphorylation, ribosomes bypass the
CC inhibitory uORFs and re-initiate translation at the QRICH1 coding
CC sequence (PubMed:33384352). Positive autoregulation at the
CC transcriptional level (PubMed:33384352). {ECO:0000269|PubMed:33384352}.
CC -!- DOMAIN: The CARD domain may be involved in the regulation of caspase
CC activity in the context of programmed cell death.
CC {ECO:0000303|PubMed:33384352}.
CC -!- DISEASE: Ververi-Brady syndrome (VERBRAS) [MIM:617982]: An autosomal
CC dominant disorder characterized by mild developmental delay and
CC intellectual disability, speech delay, learning difficulties, autistic
CC features, and mild facial dysmorphism. {ECO:0000269|PubMed:28692176,
CC ECO:0000269|PubMed:30281152, ECO:0000269|PubMed:33009816}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
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DR EMBL; AK074313; BAB85047.1; -; mRNA.
DR EMBL; BC000978; AAH00978.2; -; mRNA.
DR EMBL; BC098375; AAH98375.1; -; mRNA.
DR EMBL; BC110855; AAI10856.1; -; mRNA.
DR CCDS; CCDS2787.1; -.
DR RefSeq; NP_001307509.1; NM_001320580.1.
DR RefSeq; NP_001307510.1; NM_001320581.1.
DR RefSeq; NP_001307511.1; NM_001320582.1.
DR RefSeq; NP_001307512.1; NM_001320583.1.
DR RefSeq; NP_001307513.1; NM_001320584.1.
DR RefSeq; NP_001307514.1; NM_001320585.1.
DR RefSeq; NP_060200.2; NM_017730.3.
DR RefSeq; NP_942581.1; NM_198880.2.
DR RefSeq; XP_011532165.1; XM_011533863.1.
DR AlphaFoldDB; Q2TAL8; -.
DR SMR; Q2TAL8; -.
DR BioGRID; 120219; 141.
DR IntAct; Q2TAL8; 70.
DR MINT; Q2TAL8; -.
DR STRING; 9606.ENSP00000378830; -.
DR GlyGen; Q2TAL8; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; Q2TAL8; -.
DR MetOSite; Q2TAL8; -.
DR PhosphoSitePlus; Q2TAL8; -.
DR BioMuta; QRICH1; -.
DR DMDM; 121941773; -.
DR EPD; Q2TAL8; -.
DR jPOST; Q2TAL8; -.
DR MassIVE; Q2TAL8; -.
DR MaxQB; Q2TAL8; -.
DR PaxDb; Q2TAL8; -.
DR PeptideAtlas; Q2TAL8; -.
DR PRIDE; Q2TAL8; -.
DR ProteomicsDB; 61468; -.
DR Antibodypedia; 30380; 31 antibodies from 11 providers.
DR DNASU; 54870; -.
DR Ensembl; ENST00000357496.6; ENSP00000350094.2; ENSG00000198218.11.
DR Ensembl; ENST00000395443.7; ENSP00000378830.2; ENSG00000198218.11.
DR Ensembl; ENST00000424300.5; ENSP00000412890.1; ENSG00000198218.11.
DR GeneID; 54870; -.
DR KEGG; hsa:54870; -.
DR MANE-Select; ENST00000395443.7; ENSP00000378830.2; NM_198880.3; NP_942581.1.
DR UCSC; uc003cvu.4; human.
DR CTD; 54870; -.
DR DisGeNET; 54870; -.
DR GeneCards; QRICH1; -.
DR HGNC; HGNC:24713; QRICH1.
DR HPA; ENSG00000198218; Low tissue specificity.
DR MalaCards; QRICH1; -.
DR MIM; 617387; gene.
DR MIM; 617982; phenotype.
DR neXtProt; NX_Q2TAL8; -.
DR OpenTargets; ENSG00000198218; -.
DR Orphanet; 580940; QRICH1-related intellectual disability-chondrodysplasia syndrome.
DR PharmGKB; PA142671106; -.
DR VEuPathDB; HostDB:ENSG00000198218; -.
DR eggNOG; ENOG502QU8W; Eukaryota.
DR GeneTree; ENSGT00940000155241; -.
DR HOGENOM; CLU_025446_0_0_1; -.
DR InParanoid; Q2TAL8; -.
DR OMA; DKMVGTT; -.
DR OrthoDB; 587724at2759; -.
DR PhylomeDB; Q2TAL8; -.
DR TreeFam; TF336988; -.
DR PathwayCommons; Q2TAL8; -.
DR SignaLink; Q2TAL8; -.
DR BioGRID-ORCS; 54870; 120 hits in 1082 CRISPR screens.
DR ChiTaRS; QRICH1; human.
DR GeneWiki; QRICH1; -.
DR GenomeRNAi; 54870; -.
DR Pharos; Q2TAL8; Tdark.
DR PRO; PR:Q2TAL8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q2TAL8; protein.
DR Bgee; ENSG00000198218; Expressed in granulocyte and 209 other tissues.
DR ExpressionAtlas; Q2TAL8; baseline and differential.
DR Genevisible; Q2TAL8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
DR GO; GO:0140467; P:integrated stress response signaling; IMP:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0036499; P:PERK-mediated unfolded protein response; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR InterPro; IPR021893; DUF3504.
DR Pfam; PF12012; DUF3504; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Disease variant;
KW Intellectual disability; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Unfolded protein response.
FT CHAIN 1..776
FT /note="Transcriptional regulator QRICH1"
FT /id="PRO_0000269853"
FT DOMAIN 6..48
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 139..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 511..776
FT /note="Missing (in VERBRAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30281152"
FT /id="VAR_084455"
FT VARIANT 536..776
FT /note="Missing (in VERBRAS; decreased QRICH1 protein
FT expression; decreased growth plate chondrocyte hypertrophic
FT differentiation; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:30281152"
FT /id="VAR_084456"
FT VARIANT 652..776
FT /note="Missing (in VERBRAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28692176,
FT ECO:0000269|PubMed:33009816"
FT /id="VAR_080962"
FT VARIANT 736
FT /note="S -> N (in VERBRAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33009816"
FT /id="VAR_084457"
FT CONFLICT 251
FT /note="D -> E (in Ref. 1; BAB85047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 776 AA; 86436 MW; D98CBAA9315B4D6B CRC64;
MNNSLENTIS FEEYIRVKAR SVPQHRMKEF LDSLASKGPE ALQEFQQTAT TTMVYQQGGN
CIYTDSTEVA GSLLELACPV TTSVQPQTQQ EQQIQVQQPQ QVQVQVQVQQ SPQQVSAQLS
PQLTVHQPTE QPIQVQVQIQ GQAPQSAAPS IQTPSLQSPS PSQLQAAQIQ VQHVQAAQQI
QAAEIPEEHI PHQQIQAQLV AGQSLAGGQQ IQIQTVGALS PPPSQQGSPR EGERRVGTAS
VLQPVKKRKV DMPITVSYAI SGQPVATVLA IPQGQQQSYV SLRPDLLTVD SAHLYSATGT
ITSPTGETWT IPVYSAQPRG DPQQQSITHI AIPQEAYNAV HVSGSPTALA AVKLEDDKEK
MVGTTSVVKN SHEEVVQTLA NSLFPAQFMN GNIHIPVAVQ AVAGTYQNTA QTVHIWDPQQ
QPQQQTPQEQ TPPPQQQQQQ LQVTCSAQTV QVAEVEPQSQ PQPSPELLLP NSLKPEEGLE
VWKNWAQTKN AELEKDAQNR LAPIGRRQLL RFQEDLISSA VAELNYGLCL MTREARNGEG
EPYDPDVLYY IFLCIQKYLF ENGRVDDIFS DLYYVRFTEW LHEVLKDVQP RVTPLGYVLP
SHVTEEMLWE CKQLGAHSPS TLLTTLMFFN TKYFLLKTVD QHMKLAFSKV LRQTKKNPSN
PKDKSTSIRY LKALGIHQTG QKVTDDMYAE QTENPENPLR CPIKLYDFYL FKCPQSVKGR
NDTFYLTPEP VVAPNSPIWY SVQPISREQM GQMLTRILVI REIQEAIAVA NASTMH
