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 27-MAR-2024, entry version 168. 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}; 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; 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 PDB; 7XUV; X-ray; 1.60 A; B=243-262. DR PDBsum; 3MXN; -. DR PDBsum; 3NBH; -. DR PDBsum; 3NBI; -. DR PDBsum; 4CGY; -. DR PDBsum; 4CHT; -. DR PDBsum; 4DAY; -. DR PDBsum; 7XUV; -. DR AlphaFoldDB; Q9H9A7; -. DR SMR; Q9H9A7; -. DR BioGRID; 123066; 39. 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; 9606-ENSP00000317039; -. DR PeptideAtlas; Q9H9A7; -. DR ProteomicsDB; 81306; -. DR Pumba; Q9H9A7; -. DR Antibodypedia; 27643; 184 antibodies from 24 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 AGR; HGNC:25764; -. 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; SATWHVK; -. DR OrthoDB; 68841at2759; -. 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 homologous recombination repair (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; 481 hits in 1162 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 192 other cell types or tissues. DR ExpressionAtlas; Q9H9A7; baseline and differential. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS: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:0071139; P:resolution of DNA recombination intermediates; IDA:ComplexPortal. DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central. DR GO; GO:0009749; P:response to glucose; IEA:Ensembl. DR Gene3D; 2.40.50.510; -; 2. DR Gene3D; 1.10.8.1020; RecQ-mediated genome instability protein 1, N-terminal domain; 1. DR Gene3D; 2.40.50.770; RecQ-mediated genome instability protein Rmi1, C-terminal domain; 1. DR IDEAL; IID00421; -. DR InterPro; IPR032199; RMI1_C. DR InterPro; IPR049363; RMI1_N. DR InterPro; IPR042470; RMI1_N_C_sf. DR InterPro; IPR044881; RMI1_N_N_sf. DR InterPro; IPR013894; RMI1_OB. DR PANTHER; PTHR14790:SF15; RECQ-MEDIATED GENOME INSTABILITY PROTEIN 1; 1. DR PANTHER; PTHR14790; RECQ-MEDIATED GENOME INSTABILITY PROTEIN 1 RMI1; 1. DR Pfam; PF16099; RMI1_C; 1. DR Pfam; PF08585; RMI1_N_C; 1. DR Pfam; PF21000; RMI1_N_N; 1. DR SMART; SM01161; DUF1767; 1. DR Genevisible; Q9H9A7; HS. 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 244..250 FT /evidence="ECO:0007829|PDB:7XUV" FT HELIX 253..258 FT /evidence="ECO:0007829|PDB:7XUV" 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 //