RMI1_HUMAN
ID RMI1_HUMAN Reviewed; 625 AA.
AC Q9H9A7; Q05BX1; Q05CW3; Q5SQG8; Q5SQG9; Q6P1Q4; Q6PI89; Q7Z6L6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=RecQ-mediated genome instability protein 1;
DE AltName: Full=BLM-associated protein of 75 kDa;
DE Short=BLAP75;
DE AltName: Full=FAAP75;
GN Name=RMI1; Synonyms=C9orf76;
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], AND VARIANT SER-455.
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-100 AND SER-455.
RC TISSUE=Brain, Skin, Testis, 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 [4]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH BLM AND TOP3A, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15775963; DOI=10.1038/sj.emboj.7600622;
RA Yin J., Sobeck A., Xu C., Meetei A.R., Hoatlin M., Li L., Wang W.;
RT "BLAP75, an essential component of Bloom's syndrome protein complexes that
RT maintain genome integrity.";
RL EMBO J. 24:1465-1476(2005).
RN [5]
RP FUNCTION, AND INTERACTION WITH BLM AND TOP3A.
RX PubMed=16595695; DOI=10.1074/jbc.c600051200;
RA Raynard S., Bussen W., Sung P.;
RT "A double Holliday junction dissolvasome comprising BLM, topoisomerase III
RT alpha, and BLAP75.";
RL J. Biol. Chem. 281:13861-13864(2006).
RN [6]
RP FUNCTION, BINDING TO DOUBLE HOLLIDAY JUNCTION, AND INTERACTION WITH TOP3A.
RX PubMed=16537486; DOI=10.1073/pnas.0508295103;
RA Wu L., Bachrati C.Z., Ou J., Xu C., Yin J., Chang M., Wang W., Li L.,
RA Brown G.W., Hickson I.D.;
RT "BLAP75/RMI1 promotes the BLM-dependent dissolution of homologous
RT recombination intermediates.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:4068-4073(2006).
RN [7]
RP IDENTIFICATION IN THE RMI COMPLEX, AND INTERACTION WITH RMI2.
RX PubMed=18923082; DOI=10.1101/gad.1708608;
RA Xu D., Guo R., Sobeck A., Bachrati C.Z., Yang J., Enomoto T., Brown G.W.,
RA Hoatlin M.E., Hickson I.D., Wang W.;
RT "RMI, a new OB-fold complex essential for Bloom syndrome protein to
RT maintain genome stability.";
RL Genes Dev. 22:2843-2855(2008).
RN [8]
RP IDENTIFICATION IN THE RMI COMPLEX, AND INTERACTION WITH RMI2.
RX PubMed=18923083; DOI=10.1101/gad.1725108;
RA Singh T.R., Ali A.M., Busygina V., Raynard S., Fan Q., Du C.-H.,
RA Andreassen P.R., Sung P., Meetei A.R.;
RT "BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component
RT of the Bloom helicase-double Holliday junction dissolvasome.";
RL Genes Dev. 22:2856-2868(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-292, 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 [12]
RP INTERACTION WITH BLM.
RX PubMed=23509288; DOI=10.1073/pnas.1220921110;
RA Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.;
RT "Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase
RT with homologous recombination repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-426, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-334; LYS-387 AND LYS-426, 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).
CC -!- FUNCTION: Essential component of the RMI complex, a complex that plays
CC an important role in the processing of homologous recombination
CC intermediates to limit DNA crossover formation in cells. Promotes TOP3A
CC binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-
CC mediated dissolution. Required for BLM phosphorylation during mitosis.
CC Within the BLM complex, required for BLM and TOP3A stability.
CC {ECO:0000269|PubMed:15775963, ECO:0000269|PubMed:16537486,
CC ECO:0000269|PubMed:16595695}.
CC -!- SUBUNIT: Component of the RMI complex, containing at least TOP3A, RMI1
CC and RMI2. The RMI complex interacts with BLM. Directly interacts with
CC RMI2 and TOP3A. May bind DHJ. Interacts (via N-terminal region) with
CC BLM; the interaction is direct. {ECO:0000269|PubMed:15775963,
CC ECO:0000269|PubMed:16537486, ECO:0000269|PubMed:16595695,
CC ECO:0000269|PubMed:18923082, ECO:0000269|PubMed:18923083,
CC ECO:0000269|PubMed:23509288}.
CC -!- INTERACTION:
CC Q9H9A7; P54132: BLM; NbExp=15; IntAct=EBI-621339, EBI-621372;
CC Q9H9A7; Q96E14: RMI2; NbExp=4; IntAct=EBI-621339, EBI-2555534;
CC Q9H9A7; Q96E14-1: RMI2; NbExp=13; IntAct=EBI-621339, EBI-15876491;
CC Q9H9A7; Q13472: TOP3A; NbExp=10; IntAct=EBI-621339, EBI-621345;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15775963}. Note=Forms
CC foci in response to DNA damage.
CC -!- SIMILARITY: Belongs to the RMI1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20606.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH32494.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH39999.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH53549.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH64937.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK022950; BAB14325.1; -; mRNA.
DR EMBL; AL732446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020606; AAH20606.1; ALT_SEQ; mRNA.
DR EMBL; BC032494; AAH32494.1; ALT_SEQ; mRNA.
DR EMBL; BC039999; AAH39999.1; ALT_FRAME; mRNA.
DR EMBL; BC053549; AAH53549.1; ALT_SEQ; mRNA.
DR EMBL; BC064937; AAH64937.1; ALT_FRAME; mRNA.
DR CCDS; CCDS6669.1; -.
DR RefSeq; NP_079221.2; NM_024945.2.
DR RefSeq; XP_005252268.1; XM_005252211.2.
DR RefSeq; XP_005252270.1; XM_005252213.2.
DR RefSeq; XP_011517336.1; XM_011519034.2.
DR RefSeq; XP_016870629.1; XM_017015140.1.
DR PDB; 3MXN; X-ray; 1.55 A; A=473-625.
DR PDB; 3NBH; X-ray; 2.00 A; A=475-625.
DR PDB; 3NBI; X-ray; 2.00 A; A=2-213.
DR PDB; 4CGY; X-ray; 2.85 A; B=1-219.
DR PDB; 4CHT; X-ray; 3.25 A; B=1-219.
DR PDB; 4DAY; X-ray; 3.30 A; A=473-625.
DR PDBsum; 3MXN; -.
DR PDBsum; 3NBH; -.
DR PDBsum; 3NBI; -.
DR PDBsum; 4CGY; -.
DR PDBsum; 4CHT; -.
DR PDBsum; 4DAY; -.
DR AlphaFoldDB; Q9H9A7; -.
DR SMR; Q9H9A7; -.
DR BioGRID; 123066; 36.
DR ComplexPortal; CPX-3301; BTR double Holliday Junction dissolution complex.
DR CORUM; Q9H9A7; -.
DR DIP; DIP-33324N; -.
DR IntAct; Q9H9A7; 23.
DR MINT; Q9H9A7; -.
DR STRING; 9606.ENSP00000317039; -.
DR iPTMnet; Q9H9A7; -.
DR PhosphoSitePlus; Q9H9A7; -.
DR BioMuta; RMI1; -.
DR DMDM; 322510109; -.
DR EPD; Q9H9A7; -.
DR jPOST; Q9H9A7; -.
DR MassIVE; Q9H9A7; -.
DR MaxQB; Q9H9A7; -.
DR PaxDb; Q9H9A7; -.
DR PeptideAtlas; Q9H9A7; -.
DR PRIDE; Q9H9A7; -.
DR ProteomicsDB; 81306; -.
DR Antibodypedia; 27643; 171 antibodies from 23 providers.
DR DNASU; 80010; -.
DR Ensembl; ENST00000325875.7; ENSP00000317039.3; ENSG00000178966.17.
DR Ensembl; ENST00000445877.6; ENSP00000402433.2; ENSG00000178966.17.
DR GeneID; 80010; -.
DR KEGG; hsa:80010; -.
DR MANE-Select; ENST00000445877.6; ENSP00000402433.2; NM_001358291.2; NP_001345220.1.
DR UCSC; uc004anq.5; human.
DR CTD; 80010; -.
DR DisGeNET; 80010; -.
DR GeneCards; RMI1; -.
DR HGNC; HGNC:25764; RMI1.
DR HPA; ENSG00000178966; Low tissue specificity.
DR MIM; 610404; gene.
DR neXtProt; NX_Q9H9A7; -.
DR OpenTargets; ENSG00000178966; -.
DR PharmGKB; PA134939007; -.
DR VEuPathDB; HostDB:ENSG00000178966; -.
DR eggNOG; KOG3683; Eukaryota.
DR GeneTree; ENSGT00940000161055; -.
DR InParanoid; Q9H9A7; -.
DR OMA; STWHVKV; -.
DR OrthoDB; 531291at2759; -.
DR PhylomeDB; Q9H9A7; -.
DR TreeFam; TF316491; -.
DR PathwayCommons; Q9H9A7; -.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-9701192; Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function.
DR Reactome; R-HSA-9704331; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function.
DR Reactome; R-HSA-9704646; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR Reactome; R-HSA-9709603; Impaired BRCA2 binding to PALB2.
DR SignaLink; Q9H9A7; -.
DR BioGRID-ORCS; 80010; 458 hits in 1082 CRISPR screens.
DR GeneWiki; RMI1; -.
DR GenomeRNAi; 80010; -.
DR Pharos; Q9H9A7; Tbio.
DR PRO; PR:Q9H9A7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9H9A7; protein.
DR Bgee; ENSG00000178966; Expressed in oocyte and 191 other tissues.
DR ExpressionAtlas; Q9H9A7; baseline and differential.
DR Genevisible; Q9H9A7; HS.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; IPI:ComplexPortal.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0002023; P:reduction of food intake in response to dietary excess; IEA:Ensembl.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0071139; P:resolution of recombination intermediates; IDA:ComplexPortal.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR Gene3D; 1.10.8.1020; -; 1.
DR Gene3D; 2.40.50.770; -; 1.
DR IDEAL; IID00421; -.
DR InterPro; IPR033472; DUF1767.
DR InterPro; IPR032199; RMI1_C.
DR InterPro; IPR013894; RMI1_N.
DR InterPro; IPR042470; RMI1_N_C_sf.
DR InterPro; IPR044881; RMI1_N_N_sf.
DR Pfam; PF16099; RMI1_C; 1.
DR Pfam; PF08585; RMI1_N; 1.
DR SMART; SM01161; DUF1767; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA replication; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..625
FT /note="RecQ-mediated genome instability protein 1"
FT /id="PRO_0000227546"
FT REGION 257..282
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 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 387
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 426
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 100
FT /note="Y -> H (in dbSNP:rs17855932)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025556"
FT VARIANT 455
FT /note="N -> S (in dbSNP:rs1982151)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_025557"
FT CONFLICT 11
FT /note="E -> G (in Ref. 1; BAB14325)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="A -> T (in Ref. 1; BAB14325)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="E -> D (in Ref. 3; AAH20606)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="L -> F (in Ref. 3; AAH39999)"
FT /evidence="ECO:0000305"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:3NBI"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:3NBI"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:3NBI"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:3NBI"
FT TURN 71..75
FT /evidence="ECO:0007829|PDB:3NBI"
FT STRAND 77..95
FT /evidence="ECO:0007829|PDB:3NBI"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:3NBI"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4CGY"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:4CHT"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:3NBI"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:3NBI"
FT STRAND 166..176
FT /evidence="ECO:0007829|PDB:3NBI"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:3NBI"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3NBI"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3NBI"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:3NBI"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:4CGY"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:3MXN"
FT HELIX 483..487
FT /evidence="ECO:0007829|PDB:3MXN"
FT HELIX 494..499
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 506..517
FT /evidence="ECO:0007829|PDB:3MXN"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:3MXN"
FT HELIX 547..554
FT /evidence="ECO:0007829|PDB:3MXN"
FT HELIX 558..564
FT /evidence="ECO:0007829|PDB:3MXN"
FT HELIX 568..587
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 589..597
FT /evidence="ECO:0007829|PDB:3MXN"
FT TURN 598..601
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 602..609
FT /evidence="ECO:0007829|PDB:3MXN"
FT HELIX 613..622
FT /evidence="ECO:0007829|PDB:3MXN"
SQ SEQUENCE 625 AA; 70144 MW; 2BB449363DBF76B7 CRC64;
MNVTSIALRA ETWLLAAWHV KVPPMWLEAC INWIQEENNN VNLSQAQMNK QVFEQWLLTD
LRDLEHPLLP DGILEIPKGE LNGFYALQIN SLVDVSQPAY SQIQKLRGKN TTNDLVTAEA
QVTPKPWEAK PSRMLMLQLT DGIVQIQGME YQPIPILHSD LPPGTKILIY GNISFRLGVL
LLKPENVKVL GGEVDALLEE YAQEKVLARL IGEPDLVVSV IPNNSNENIP RVTDVLDPAL
GPSDEELLAS LDENDELTAN NDTSSERCFT TGSSSNTIPT RQSSFEPEFV ISPRPKEEPS
NLSIHVMDGE LDDFSLEEAL LLEETVQKEQ METKELQPLT FNRNADRSIE RFSHNPNTTN
NFSLTCKNGN NNWSEKNVSE QMTNEDKSFG CPSVRDQNRS IFSVHCNVPL AHDFTNKEKN
LETDNKIKQT SSSDSHSLNN KILNREVVNY VQKRNSQISN ENDCNLQSCS LRSSENSINL
SIAMDLYSPP FVYLSVLMAS KPKEVTTVKV KAFIVTLTGN LSSSGGIWSI TAKVSDGTAY
LDVDFVDEIL TSLIGFSVPE MKQSKKDPLQ YQKFLEGLQK CQRDLIDLCC LMTISFNPSL
SKAMVLALQD VNMEHLENLK KRLNK
