OXR1_HUMAN
ID OXR1_HUMAN Reviewed; 874 AA.
AC Q8N573; A6NK11; A8KA34; B3KXL1; B7Z402; B7Z8N5; D3HIS6; Q3LIB5; Q6ZVK9;
AC Q8N8V0; Q9H266; Q9NWC7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Oxidation resistance protein 1;
GN Name=OXR1; ORFNames=Nbla00307;
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 [MRNA] (ISOFORMS 7 AND 8).
RA Yang M., Eide L., Alseth I., Olsen O.E., Johansen R.F., Backe P.H.,
RA Luna L., Holmseth S., Gujord K.M., Ottersen O.P., Danbolt N.C., Bjoras M.;
RT "The human OXR1 is an essential stress response gene expressing five
RT isoforms and sorting to the inner membrane of mitochondria.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 6 AND 7), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-478 (ISOFORM 5).
RC TISSUE=Cerebellum, Embryo, Kidney, Mammary gland, Thalamus, Tongue, and
RC Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-100; PRO-360 AND
RP ARG-516.
RG NIEHS SNPs program;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-874 (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 487-874 (ISOFORM 1), AND FUNCTION.
RX PubMed=11114193; DOI=10.1073/pnas.260495897;
RA Volkert M.R., Elliott N.A., Housman D.E.;
RT "Functional genomics reveals a family of eukaryotic oxidation protection
RT genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14530-14535(2000).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15060142; DOI=10.1128/mcb.24.8.3180-3187.2004;
RA Elliott N.A., Volkert M.R.;
RT "Stress induction and mitochondrial localization of Oxr1 proteins in yeast
RT and humans.";
RL Mol. Cell. Biol. 24:3180-3187(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201; SER-202 AND SER-204, AND
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ALTERNATIVE SPLICING, AND ANTIOXIDANT ACTIVITY DETERMINING REGION.
RX PubMed=22873401; DOI=10.1186/1471-2199-13-26;
RA Murphy K.C., Volkert M.R.;
RT "Structural/functional analysis of the human OXR1 protein: identification
RT of exon 8 as the anti-oxidant encoding function.";
RL BMC Mol. Biol. 13:26-26(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-202, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-294, AND
RP IDENTIFICATION BY 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 [20]
RP VARIANT CHEGDD 368-SER--GLU-874 DEL, AND INVOLVEMENT IN CHEGDD.
RX PubMed=31785787; DOI=10.1016/j.ajhg.2019.11.002;
RA Wang J., Rousseau J., Kim E., Ehresmann S., Cheng Y.T., Duraine L., Zuo Z.,
RA Park Y.J., Li-Kroeger D., Bi W., Wong L.J., Rosenfeld J., Gleeson J.,
RA Faqeih E., Alkuraya F.S., Wierenga K.J., Chen J., Afenjar A., Nava C.,
RA Doummar D., Keren B., Juusola J., Grompe M., Bellen H.J., Campeau P.M.;
RT "Loss of oxidation resistance 1, OXR1, is associated with an autosomal-
RT recessive neurological disease with cerebellar atrophy and lysosomal
RT dysfunction.";
RL Am. J. Hum. Genet. 105:1237-1253(2019).
CC -!- FUNCTION: May be involved in protection from oxidative damage.
CC {ECO:0000269|PubMed:11114193, ECO:0000269|PubMed:15060142}.
CC -!- INTERACTION:
CC Q8N573-5; Q14145: KEAP1; NbExp=3; IntAct=EBI-10265887, EBI-751001;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15060142}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q8N573-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N573-2; Sequence=VSP_039006, VSP_039013;
CC Name=3;
CC IsoId=Q8N573-3; Sequence=VSP_039007, VSP_039009, VSP_039010,
CC VSP_039011;
CC Name=4;
CC IsoId=Q8N573-4; Sequence=VSP_039004, VSP_039012;
CC Name=5;
CC IsoId=Q8N573-5; Sequence=VSP_039008, VSP_039013;
CC Name=6;
CC IsoId=Q8N573-6; Sequence=VSP_039005, VSP_039014;
CC Name=7;
CC IsoId=Q8N573-7; Sequence=VSP_043632, VSP_043633;
CC Name=8;
CC IsoId=Q8N573-8; Sequence=VSP_039008;
CC -!- INDUCTION: By heat shock and oxidative stress.
CC {ECO:0000269|PubMed:15060142}.
CC -!- DISEASE: Cerebellar hypoplasia/atrophy, epilepsy, and global
CC developmental delay (CHEGDD) [MIM:213000]: An autosomal recessive
CC neurodevelopmental disorder characterized by infantile onset of
CC hypotonia, global developmental delay, delayed walking, and severely
CC impaired intellectual development with profound speech delay. Patients
CC manifest cerebellar atrophy and childhood-onset epilepsy.
CC {ECO:0000269|PubMed:31785787}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the OXR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG25715.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH32710.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAY26396.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA91456.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF85588.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAI46186.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/oxr1/";
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DR EMBL; FN650108; CBI84064.1; -; mRNA.
DR EMBL; FN650109; CBI84065.1; -; mRNA.
DR EMBL; AB075503; BAE45753.1; -; mRNA.
DR EMBL; AK000987; BAA91456.1; ALT_INIT; mRNA.
DR EMBL; AK096148; BAC04711.1; -; mRNA.
DR EMBL; AK124441; BAC85852.1; -; mRNA.
DR EMBL; AK127563; BAG54523.1; -; mRNA.
DR EMBL; AK292899; BAF85588.1; ALT_INIT; mRNA.
DR EMBL; AK296561; BAH12388.1; -; mRNA.
DR EMBL; AK303695; BAH14021.1; -; mRNA.
DR EMBL; AK316153; BAH14524.1; -; mRNA.
DR EMBL; DQ020202; AAY26396.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC023344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032710; AAH32710.1; ALT_INIT; mRNA.
DR EMBL; AF309387; AAG25715.1; ALT_INIT; mRNA.
DR EMBL; AL833193; CAI46186.1; ALT_INIT; mRNA.
DR CCDS; CCDS47909.1; -. [Q8N573-5]
DR CCDS; CCDS56547.1; -. [Q8N573-8]
DR CCDS; CCDS56548.1; -. [Q8N573-1]
DR CCDS; CCDS56549.1; -. [Q8N573-4]
DR CCDS; CCDS56550.1; -. [Q8N573-7]
DR CCDS; CCDS6304.2; -. [Q8N573-2]
DR RefSeq; NP_001185461.1; NM_001198532.1. [Q8N573-1]
DR RefSeq; NP_001185462.1; NM_001198533.1. [Q8N573-8]
DR RefSeq; NP_001185463.1; NM_001198534.1. [Q8N573-4]
DR RefSeq; NP_001185464.1; NM_001198535.1. [Q8N573-7]
DR RefSeq; NP_060472.2; NM_018002.3. [Q8N573-5]
DR RefSeq; NP_851999.2; NM_181354.4. [Q8N573-2]
DR RefSeq; XP_016869083.1; XM_017013594.1.
DR AlphaFoldDB; Q8N573; -.
DR SMR; Q8N573; -.
DR BioGRID; 120391; 29.
DR IntAct; Q8N573; 6.
DR MINT; Q8N573; -.
DR STRING; 9606.ENSP00000405424; -.
DR ChEMBL; CHEMBL4295901; -.
DR GlyGen; Q8N573; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N573; -.
DR PhosphoSitePlus; Q8N573; -.
DR BioMuta; OXR1; -.
DR DMDM; 294862456; -.
DR EPD; Q8N573; -.
DR jPOST; Q8N573; -.
DR MassIVE; Q8N573; -.
DR MaxQB; Q8N573; -.
DR PaxDb; Q8N573; -.
DR PeptideAtlas; Q8N573; -.
DR PRIDE; Q8N573; -.
DR ProteomicsDB; 72011; -. [Q8N573-1]
DR ProteomicsDB; 72012; -. [Q8N573-2]
DR ProteomicsDB; 72013; -. [Q8N573-3]
DR ProteomicsDB; 72014; -. [Q8N573-4]
DR ProteomicsDB; 72015; -. [Q8N573-5]
DR ProteomicsDB; 72016; -. [Q8N573-6]
DR ProteomicsDB; 72017; -. [Q8N573-7]
DR ProteomicsDB; 72018; -. [Q8N573-8]
DR Antibodypedia; 26472; 214 antibodies from 28 providers.
DR DNASU; 55074; -.
DR Ensembl; ENST00000297447.10; ENSP00000297447.6; ENSG00000164830.19. [Q8N573-4]
DR Ensembl; ENST00000312046.10; ENSP00000311026.6; ENSG00000164830.19. [Q8N573-2]
DR Ensembl; ENST00000442977.6; ENSP00000405424.2; ENSG00000164830.19. [Q8N573-1]
DR Ensembl; ENST00000449762.6; ENSP00000408659.2; ENSG00000164830.19. [Q8N573-7]
DR Ensembl; ENST00000497705.5; ENSP00000431014.1; ENSG00000164830.19. [Q8N573-3]
DR Ensembl; ENST00000517566.7; ENSP00000429205.2; ENSG00000164830.19. [Q8N573-8]
DR Ensembl; ENST00000531443.6; ENSP00000431966.1; ENSG00000164830.19. [Q8N573-5]
DR GeneID; 55074; -.
DR KEGG; hsa:55074; -.
DR MANE-Select; ENST00000517566.7; ENSP00000429205.2; NM_001198533.2; NP_001185462.1. [Q8N573-8]
DR UCSC; uc003ymf.4; human. [Q8N573-1]
DR CTD; 55074; -.
DR DisGeNET; 55074; -.
DR GeneCards; OXR1; -.
DR HGNC; HGNC:15822; OXR1.
DR HPA; ENSG00000164830; Low tissue specificity.
DR MalaCards; OXR1; -.
DR MIM; 213000; phenotype.
DR MIM; 605609; gene.
DR neXtProt; NX_Q8N573; -.
DR OpenTargets; ENSG00000164830; -.
DR PharmGKB; PA32856; -.
DR VEuPathDB; HostDB:ENSG00000164830; -.
DR eggNOG; KOG2372; Eukaryota.
DR GeneTree; ENSGT00940000155187; -.
DR HOGENOM; CLU_007095_2_0_1; -.
DR InParanoid; Q8N573; -.
DR OMA; SGKDFCH; -.
DR OrthoDB; 767847at2759; -.
DR PhylomeDB; Q8N573; -.
DR TreeFam; TF313530; -.
DR PathwayCommons; Q8N573; -.
DR SignaLink; Q8N573; -.
DR BioGRID-ORCS; 55074; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; OXR1; human.
DR GeneWiki; OXR1; -.
DR GenomeRNAi; 55074; -.
DR Pharos; Q8N573; Tbio.
DR PRO; PR:Q8N573; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8N573; protein.
DR Bgee; ENSG00000164830; Expressed in pons and 209 other tissues.
DR ExpressionAtlas; Q8N573; baseline and differential.
DR Genevisible; Q8N573; HS.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:Ensembl.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0071447; P:cellular response to hydroperoxide; IEA:Ensembl.
DR GO; GO:1900408; P:negative regulation of cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IEA:Ensembl.
DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR006571; TLDc_dom.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF07534; TLD; 1.
DR SMART; SM00257; LysM; 1.
DR SMART; SM00584; TLDc; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51886; TLDC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Epilepsy; Intellectual disability;
KW Mitochondrion; Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..874
FT /note="Oxidation resistance protein 1"
FT /id="PRO_0000231645"
FT DOMAIN 99..142
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 208..275
FT /note="GRAM"
FT DOMAIN 713..874
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..578
FT /note="Mediates oxidative antimutator activity"
FT COMPBIAS 62..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT VAR_SEQ 1..631
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12880961"
FT /id="VSP_039004"
FT VAR_SEQ 1..511
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039005"
FT VAR_SEQ 1..74
FT /note="MTKDKNSPGLKKKSQSVDINAPGFNPLAGAGKQTPQASKPPAPKTPIIEEEQ
FT NNAANTQKHPSRRSELKRFYTI -> MDYLTTFTEKSGRLLRGTANRLLGFGGGGEARQ
FT VRFEDYLREPAQGDLGCGSPPHRPPAPSSPEGP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_039006"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039007"
FT VAR_SEQ 1..22
FT /note="MTKDKNSPGLKKKSQSVDINAP -> MSRLWYGKKGRRHQPINHKYTL (in
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_043632"
FT VAR_SEQ 1..9
FT /note="MTKDKNSPG -> MSVSNLSW (in isoform 5 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_039008"
FT VAR_SEQ 23..680
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_043633"
FT VAR_SEQ 69..74
FT /note="KRFYTI -> MFCQRK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039009"
FT VAR_SEQ 544..571
FT /note="SALLKEKQRHRLHKFLCLRVGKPMRKTF -> KCYRVNEVSSSNCMVSPSFL
FT TDSKAAVP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039010"
FT VAR_SEQ 572..874
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039011"
FT VAR_SEQ 632..653
FT /note="KKIEESETIEDSSNQAAAREWE -> MSRLWYGKKGRRHQPINHKYTL (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:12880961"
FT /id="VSP_039012"
FT VAR_SEQ 654..722
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039014"
FT VAR_SEQ 654..680
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_039013"
FT VARIANT 100
FT /note="E -> G (in dbSNP:rs28921397)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025861"
FT VARIANT 360
FT /note="Q -> P (in dbSNP:rs28921419)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025862"
FT VARIANT 368..874
FT /note="Missing (in CHEGDD)"
FT /evidence="ECO:0000269|PubMed:31785787"
FT /id="VAR_083522"
FT VARIANT 516
FT /note="K -> R (in dbSNP:rs28921420)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025863"
FT CONFLICT 154
FT /note="S -> P (in Ref. 3; BAC04711)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="D -> V (in Ref. 8; AAG25715)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="I -> N (in Ref. 8; AAG25715)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="L -> F (in Ref. 8; AAG25715)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="N -> D (in Ref. 3; BAA91456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 874 AA; 97970 MW; 4231D07369CE2D36 CRC64;
MTKDKNSPGL KKKSQSVDIN APGFNPLAGA GKQTPQASKP PAPKTPIIEE EQNNAANTQK
HPSRRSELKR FYTIDTGQKK TLDKKDGRRM SFQKPKGTIE YTVESRDSLN SIALKFDTTP
NELVQLNKLF SRAVVTGQVL YVPDPEYVSS VESSPSLSPV SPLSPTSSEA EFDKTTNPDV
HPTEATPSST FTGIRPARVV SSTSEEEEAF TEKFLKINCK YITSGKGTVS GVLLVTPNNI
MFDPHKNDPL VQENGCEEYG IMCPMEEVMS AAMYKEILDS KIKESLPIDI DQLSGRDFCH
SKKMTGSNTE EIDSRIRDAG NDSASTAPRS TEESLSEDVF TESELSPIRE ELVSSDELRQ
DKSSGASSES VQTVNQAEVE SLTVKSESTG TPGHLRSDTE HSTNEVGTLC HKTDLNNLEM
AIKEDQIADN FQGISGPKED STSIKGNSDQ DSFLHENSLH QEESQKENMP CGETAEFKQK
QSVNKGKQGK EQNQDSQTEA EELRKLWKTH TMQQTKQQRE NIQQVSQKEA KHKITSADGH
IESSALLKEK QRHRLHKFLC LRVGKPMRKT FVSQASATMQ QYAQRDKKHE YWFAVPQERT
DHLYAFFIQW SPEIYAEDTG EYTREPGFIV VKKIEESETI EDSSNQAAAR EWEVVSVAEY
HRRIDALNTE ELRTLCRRLQ ITTREDINSK QVATVKADLE SESFRPNLSD PSELLLPDQI
EKLTKHLPPR TIGYPWTLVY GTGKHGTSLK TLYRTMTGLD TPVLMVIKDS DGQVFGALAS
EPLKVSDGFY GTGETFVFTF CPEFEVFKWT GDNMFFIKGD MDSLAFGGGG GEFALWLDGD
LYHGRSHSCK TFGNRTLSKK EDFFIQDIEI WAFE
