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 02-SEP-2026, entry version 145. DE RecName: Full=Transcriptional regulator QRICH1 {ECO:0000305}; DE AltName: Full=Glutamine-rich protein 1; GN Name=QRICH1 {ECO:0000303|PubMed:33384352, GN 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 VERBRAS1, AND VARIANT VERBRAS1 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 VERBRAS1, VARIANTS VERBRAS1 RP 511-ARG--HIS-776 DEL AND 536-ARG--HIS-776 DEL, AND CHARACTERIZATION OF RP VARIANT VERBRAS1 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 VERBRAS1. RX PubMed=33738978; DOI=10.1002/ajmg.a.62184; RA Baruch Y., Horn-Saban S., Plotsky Y., Bercovich D., Gershoni-Baruch R.; RT "A case of Ververi-Brady syndrome due to QRICH1 loss of function and the RT literature review."; RL Am. J. Med. Genet. A 185:1913-1917(2021). RN [13] RP INVOLVEMENT IN VERBRAS1, AND VARIANTS VERBRAS1 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). RN [14] RP VARIANTS VERBRAS1 16-ARG--HIS-776 DEL; 181-GLN--HIS-776 DEL; ILE-252; RP 275-GLN--HIS-776 DEL; LEU-284; ASP-394; 420-GLN--HIS-776 DEL; ARG-435; RP 460-GLN--HIS-776 DEL; ARG-527; CYS-550; ASP-574; LEU-603; LEU-628; RP 652-ARG--HIS-776 DEL AND 739-TRP--HIS-776 DEL. RX PubMed=34859529; DOI=10.1002/humu.24308; RG Undiagnosed Diseases Network; RA Kumble S., Levy A.M., Punetha J., Gao H., Ah Mew N., Anyane-Yeboa K., RA Benke P.J., Berger S.M., Bjerglund L., Campos-Xavier B., Ciliberto M., RA Cohen J.S., Comi A.M., Curry C., Damaj L., Denomme-Pichon A.S., Emrick L., RA Faivre L., Fasano M.B., Fievet A., Finkel R.S., Garcia-Minaur S., RA Gerard A., Gomez-Puertas P., Guillen Sacoto M.J., Hoffman T.L., Howard L., RA Iglesias A.D., Izumi K., Larson A., Leiber A., Lozano R., RA Marcos-Alcalde I., Mintz C.S., Mullegama S.V., Moeller R.S., Odent S., RA Oppermann H., Ostergaard E., Pacio-Miguez M., Palomares-Bralo M., RA Parikh S., Paulson A.M., Platzer K., Posey J.E., Potocki L., RA Revah-Politi A., Rio M., Ritter A.L., Robinson S., Rosenfeld J.A., RA Santos-Simarro F., Sousa S.B., Weber M., Xie Y., Chung W.K., Brown N.J., RA Tuemer Z.; RT "The clinical and molecular spectrum of QRICH1 associated RT neurodevelopmental disorder."; RL Hum. Mutat. 43:266-282(2022). RN [15] RP INVOLVEMENT IN VERBRAS1. RX PubMed=37331002; DOI=10.1002/mgg3.2227; RA Wang D., Wu J.; RT "A novel variant in the QRICH1 gene was identified in a patient with severe RT developmental delay."; RL Mol. Genet. Genomic Med. 11:e2227-e2227(2023). RN [16] RP VARIANT VERBRAS1 113-GLN--HIS-776 DEL. RX PubMed=37211757; DOI=10.12659/ajcr.939217; RA Roddate M., Taurina G., Krutovs V., Rots D., Kenina V.; RT "Mother and Daughter with Short Stature, Microcephaly, Mild Dysmorphic RT Features, and Learning Disabilities Due to Ververi-Brady Syndrome RT Associated with a New Variant of the QRICH1 Gene."; RL Am. J. Case Rep. 24:e939217-e939217(2023). RN [17] RP FUNCTION. RX PubMed=40355839; DOI=10.1186/s10020-025-01241-2; RA Zhang L., Chen H., Zou G., Jia W., Dong H., Wang C., Wang H., Liu Y., RA Teng D., Xu B., Zhong L., Gong L., Yang J.; RT "QRICH1 regulates ATF6 transcription to affect pathological cardiac RT hypertrophy progression."; RL Mol. Med. 31:183-183(2025). RN [18] RP STRUCTURE BY ELECTRON MICROSCOPY (3.16 ANGSTROMS) IN COMPLEX WITH SEPHS1 RP AND ZFP91, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=40608935; DOI=10.1126/science.adv2861; RA Bianchi D., Borza R., De Zan E., Huelsz-Prince G., Gregoricchio S., RA Dekker M., Fish A., Mazouzi A., Kroese L.J., Linder S., RA Hernandez-Quiles M., Vermeulen M., Celie P.H.N., Krimpenfort P., Song J.Y., RA Zwart W., Wessels L., Nijman S.M.B., Perrakis A., Brummelkamp T.R.; RT "Zincore, an atypical coregulator, binds zinc finger transcription factors RT to control gene expression."; RL Science 389:eadv2861-eadv2861(2025). 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 PubMed:40355839). Controls the outcome of the unfolded protein response CC (UPR) which is an ER-stress response pathway (PubMed:33384352). ER CC stress induces QRICH1 translation by a ribosome translation re- CC initiation mechanism in response to EIF2S1/eIF-2-alpha phosphorylation, CC and stress-induced QRICH1 regulates a transcriptional program CC associated with protein translation, protein secretion-mediated CC proteotoxicity and cell death during the terminal UPR CC (PubMed:33384352). May cooperate with ATF4 transcription factor CC signaling to regulate ER homeostasis which is critical for cell CC viability (PubMed:33384352). Up-regulates CASP3/caspase-3 activity in CC epithelial cells under ER stress. Central regulator of proteotoxicity CC associated with ER stress-mediated inflammatory diseases in the CC intestines and liver (PubMed:33384352). Core component of the zincore CC complex, a heterotetramer that acts as a molecular 'grip' to stabilize CC transcription factors at DNA-binding sites across the genome, thereby CC controlling gene expression (PubMed:40608935). The zincore complex CC binds specifically to zinc finger transcription factors, such as ZFP91, CC ZNF652, ZNF526 and PRDM15, and stabilizes them onto their cognate DNA CC motif (PubMed:40608935). Involved in chondrocyte hypertrophy, a process CC required for normal longitudinal bone growth (PubMed:30281152). CC {ECO:0000269|PubMed:30281152, ECO:0000269|PubMed:33384352, CC ECO:0000269|PubMed:40355839, ECO:0000269|PubMed:40608935}. CC -!- SUBUNIT: Component of the zincore complex, a heterotetramer composed of CC a dimer of QRICH1 and SEPHS1. {ECO:0000269|PubMed:40608935}. CC -!- INTERACTION: CC Q2TAL8; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-2798044, EBI-11976299; CC Q2TAL8; Q03989: ARID5A; NbExp=3; IntAct=EBI-2798044, EBI-948603; CC Q2TAL8; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-2798044, EBI-1012434; CC Q2TAL8; P40199: CEACAM6; NbExp=3; IntAct=EBI-2798044, EBI-4314501; CC Q2TAL8; A8MTA8-2: CIMIP2B; NbExp=3; IntAct=EBI-2798044, EBI-12160437; 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; Q14192: FHL2; NbExp=5; IntAct=EBI-2798044, EBI-701903; CC Q2TAL8; Q13643: FHL3; NbExp=7; 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=7; 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; H3BRN8: PIERCE2; NbExp=3; IntAct=EBI-2798044, EBI-18394323; 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=9; 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, ECO:0000269|PubMed:40608935}. Chromosome CC {ECO:0000269|PubMed:40608935}. Cytoplasm {ECO:0000269|PubMed:30281152}. CC Cell membrane {ECO:0000269|PubMed:30281152}. Note=The zincore complex CC binds to a highly conserved promoter motif (5'-CTTTAAR-3'). CC {ECO:0000269|PubMed:40608935}. 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 1 (VERBRAS1) [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, CC ECO:0000269|PubMed:33738978, ECO:0000269|PubMed:34859529, CC ECO:0000269|PubMed:37211757, ECO:0000269|PubMed:37331002}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001320580.2. DR RefSeq; NP_001307510.1; NM_001320581.2. DR RefSeq; NP_001307511.1; NM_001320582.2. DR RefSeq; NP_001307512.1; NM_001320583.2. DR RefSeq; NP_001307513.1; NM_001320584.1. DR RefSeq; NP_001307514.1; NM_001320585.1. DR RefSeq; NP_060200.2; NM_017730.4. DR RefSeq; NP_942581.1; NM_198880.3. DR RefSeq; XP_011532165.1; XM_011533863.1. DR RefSeq; XP_047304355.1; XM_047448399.1. DR RefSeq; XP_054202979.1; XM_054347004.1. DR RefSeq; XP_054202980.1; XM_054347005.1. DR PDB; 9HJT; EM; 3.26 A; H/I=1-776. DR PDB; 9HJU; EM; 3.16 A; D/E/H/I=1-776. DR AlphaFoldDB; Q2TAL8; -. DR EMDB; EMD-52226; -. DR EMDB; EMD-52227; -. DR SMR; Q2TAL8; -. DR BioGRID; 120219; 174. DR FunCoup; Q2TAL8; 4205. DR IntAct; Q2TAL8; 114. DR MINT; Q2TAL8; -. DR STRING; 9606.ENSP00000378830; -. DR GlyCosmos; Q2TAL8; 4 sites, 2 glycans. DR GlyGen; Q2TAL8; 6 sites, 2 O-linked glycans (6 sites). DR iPTMnet; Q2TAL8; -. DR MetOSite; Q2TAL8; -. DR PhosphoSitePlus; Q2TAL8; -. DR BioMuta; QRICH1; -. DR DMDM; 121941773; -. DR jPOST; Q2TAL8; -. DR MassIVE; Q2TAL8; -. DR PaxDb; 9606-ENSP00000378830; -. DR PeptideAtlas; Q2TAL8; -. DR ProteomicsDB; 61468; -. DR Pumba; Q2TAL8; -. DR Antibodypedia; 30380; 28 antibodies from 11 providers. DR DNASU; 54870; -. DR Ensembl; ENST00000357496.6; ENSP00000350094.2; ENSG00000198218.13. DR Ensembl; ENST00000395443.7; ENSP00000378830.2; ENSG00000198218.13. DR Ensembl; ENST00000411682.2; ENSP00000412870.2; ENSG00000198218.13. DR Ensembl; ENST00000424300.5; ENSP00000412890.1; ENSG00000198218.13. DR Ensembl; ENST00000703871.1; ENSP00000515516.1; ENSG00000198218.13. DR Ensembl; ENST00000703942.1; ENSP00000515573.1; ENSG00000198218.13. DR Ensembl; ENST00000887075.1; ENSP00000557134.1; ENSG00000198218.13. DR Ensembl; ENST00000887076.1; ENSP00000557135.1; ENSG00000198218.13. DR Ensembl; ENST00000887078.1; ENSP00000557137.1; ENSG00000198218.13. DR Ensembl; ENST00000887079.1; ENSP00000557138.1; ENSG00000198218.13. DR Ensembl; ENST00000887080.1; ENSP00000557139.1; ENSG00000198218.13. DR Ensembl; ENST00000887081.1; ENSP00000557140.1; ENSG00000198218.13. DR Ensembl; ENST00000887083.1; ENSP00000557142.1; ENSG00000198218.13. DR Ensembl; ENST00000887085.1; ENSP00000557144.1; ENSG00000198218.13. DR Ensembl; ENST00000939602.1; ENSP00000609661.1; ENSG00000198218.13. DR Ensembl; ENST00000939607.1; ENSP00000609666.1; ENSG00000198218.13. DR Ensembl; ENST00000939608.1; ENSP00000609667.1; ENSG00000198218.13. DR Ensembl; ENST00000939609.1; ENSP00000609668.1; ENSG00000198218.13. DR Ensembl; ENST00000971842.1; ENSP00000641901.1; ENSG00000198218.13. 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 AGR; HGNC:24713; -. DR ClinPGx; PA142671106; -. 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 OpenTargets; ENSG00000198218; -. DR Orphanet; 580940; QRICH1-related intellectual disability-chondrodysplasia syndrome. DR VEuPathDB; HostDB:ENSG00000198218; -. DR eggNOG; ENOG502QU8W; Eukaryota. DR GeneTree; ENSGT00940000155241; -. DR HOGENOM; CLU_025446_0_0_1; -. DR InParanoid; Q2TAL8; -. DR OMA; QVQIHEA; -. DR OrthoDB; 10025028at2759; -. DR PAN-GO; Q2TAL8; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q2TAL8; -. DR PathwayCommons; Q2TAL8; -. DR SignaLink; Q2TAL8; -. DR SIGNOR; Q2TAL8; -. DR Agora; ENSG00000198218; -. DR BioGRID-ORCS; 54870; 139 hits in 1162 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 211 other cell types or tissues. DR ExpressionAtlas; Q2TAL8; baseline and differential. DR GO; GO:0005694; C:chromosome; EXP:UniProtKB. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. 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 DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB. DR CDD; cd01671; CARD; 1. DR InterPro; IPR057926; QRICH1_dom. DR InterPro; IPR021893; ZMYM2-like_C. DR InterPro; IPR051284; ZnF_MYMT-QRICH1. DR PANTHER; PTHR45736:SF8; TRANSCRIPTIONAL REGULATOR QRICH1; 1. DR PANTHER; PTHR45736; ZINC FINGER MYM-TYPE PROTEIN; 1. DR Pfam; PF12012; DUF3504; 1. DR Pfam; PF25561; QRICH1; 1. DR PDBsum; 9HJT; -. DR PDBsum; 9HJU; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell membrane; Chromosome; Cytoplasm; KW Disease variant; Intellectual disability; Isopeptide bond; Membrane; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation; KW 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 COMPBIAS 419..429 FT /note="Low complexity" 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 16..776 FT /note="Missing (in VERBRAS1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090975" FT VARIANT 113..776 FT /note="Missing (in VERBRAS1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:37211757" FT /id="VAR_090976" FT VARIANT 181..776 FT /note="Missing (in VERBRAS1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090977" FT VARIANT 252 FT /note="M -> I (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090978" FT VARIANT 275..776 FT /note="Missing (in VERBRAS1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090979" FT VARIANT 284 FT /note="P -> L (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090980" FT VARIANT 394 FT /note="H -> D (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090981" FT VARIANT 420..776 FT /note="Missing (in VERBRAS1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090982" FT VARIANT 435 FT /note="Q -> R (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090983" FT VARIANT 460..776 FT /note="Missing (in VERBRAS1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090984" FT VARIANT 511..776 FT /note="Missing (in VERBRAS1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:30281152" FT /id="VAR_084455" FT VARIANT 527 FT /note="G -> R (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090985" FT VARIANT 536..776 FT /note="Missing (in VERBRAS1; likely pathogenic; decreased FT QRICH1 protein expression; decreased growth plate FT chondrocyte hypertrophic differentiation)" FT /evidence="ECO:0000269|PubMed:30281152" FT /id="VAR_084456" FT VARIANT 550 FT /note="Y -> C (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090986" FT VARIANT 574 FT /note="Y -> D (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090987" FT VARIANT 603 FT /note="V -> L (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090988" FT VARIANT 628 FT /note="F -> L (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090989" FT VARIANT 652..776 FT /note="Missing (in VERBRAS1; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:28692176, FT ECO:0000269|PubMed:33009816, ECO:0000269|PubMed:34859529" FT /id="VAR_080962" FT VARIANT 736 FT /note="S -> N (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33009816" FT /id="VAR_084457" FT VARIANT 739..776 FT /note="Missing (in VERBRAS1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34859529" FT /id="VAR_090990" FT CONFLICT 251 FT /note="D -> E (in Ref. 1; BAB85047)" FT /evidence="ECO:0000305" FT HELIX 475..495 FT /evidence="ECO:0007829|PDB:9HJU" FT STRAND 503..506 FT /evidence="ECO:0007829|PDB:9HJU" FT STRAND 514..516 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 521..534 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 542..544 FT /evidence="ECO:0007829|PDB:9HJT" FT HELIX 545..560 FT /evidence="ECO:0007829|PDB:9HJU" FT TURN 561..563 FT /evidence="ECO:0007829|PDB:9HJU" FT TURN 568..570 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 572..574 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 575..586 FT /evidence="ECO:0007829|PDB:9HJU" FT STRAND 594..596 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 599..601 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 605..611 FT /evidence="ECO:0007829|PDB:9HJU" FT STRAND 613..618 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 619..629 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 630..634 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 639..642 FT /evidence="ECO:0007829|PDB:9HJU" FT TURN 647..649 FT /evidence="ECO:0007829|PDB:9HJU" FT STRAND 650..653 FT /evidence="ECO:0007829|PDB:9HJT" FT HELIX 655..657 FT /evidence="ECO:0007829|PDB:9HJT" FT STRAND 668..670 FT /evidence="ECO:0007829|PDB:9HJU" FT TURN 679..682 FT /evidence="ECO:0007829|PDB:9HJU" FT TURN 685..687 FT /evidence="ECO:0007829|PDB:9HJU" FT STRAND 688..690 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 698..700 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 702..712 FT /evidence="ECO:0007829|PDB:9HJU" FT TURN 715..719 FT /evidence="ECO:0007829|PDB:9HJU" FT STRAND 726..728 FT /evidence="ECO:0007829|PDB:9HJU" FT STRAND 740..744 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 747..758 FT /evidence="ECO:0007829|PDB:9HJU" FT HELIX 761..772 FT /evidence="ECO:0007829|PDB:9HJU" 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 //