ID H2B1M_MOUSE Reviewed; 126 AA. AC P10854; Q5T008; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 191. DE RecName: Full=Histone H2B type 1-M; DE AltName: Full=H2B 291B; GN Name=H2bc14 {ECO:0000312|MGI:MGI:2448404}; GN Synonyms=Hist1h2bm {ECO:0000312|MGI:MGI:2448404}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3562244; DOI=10.1093/nar/15.7.3023; RA Liu T.-J., Liu L., Marzluff W.F.; RT "Mouse histone H2A and H2B genes: four functional genes and a pseudogene RT undergoing gene conversion with a closely linked functional gene."; RL Nucleic Acids Res. 15:3023-3039(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12408966; DOI=10.1016/s0888-7543(02)96850-3; RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.; RT "The human and mouse replication-dependent histone genes."; RL Genomics 80:487-498(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP PHOSPHORYLATION AT SER-15. RX PubMed=15197225; DOI=10.1084/jem.20032247; RA Fernandez-Capetillo O., Allis C.D., Nussenzweig A.; RT "Phosphorylation of histone H2B at DNA double-strand breaks."; RL J. Exp. Med. 199:1671-1677(2004). RN [5] RP PHOSPHORYLATION AT SER-15. RX PubMed=16039583; DOI=10.1016/j.immuni.2005.05.007; RA Odegard V.H., Kim S.T., Anderson S.M., Shlomchik M.J., Schatz D.G.; RT "Histone modifications associated with somatic hypermutation."; RL Immunity 23:101-110(2005). RN [6] RP PHOSPHORYLATION AT SER-37. RX PubMed=20647423; DOI=10.1126/science.1191241; RA Bungard D., Fuerth B.J., Zeng P.Y., Faubert B., Maas N.L., Viollet B., RA Carling D., Thompson C.B., Jones R.G., Berger S.L.; RT "Signaling kinase AMPK activates stress-promoted transcription via histone RT H2B phosphorylation."; RL Science 329:1201-1205(2010). RN [7] RP CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND RP LYS-35. RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008; RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., RA Ye Y., Khochbin S., Ren B., Zhao Y.; RT "Identification of 67 histone marks and histone lysine crotonylation as a RT new type of histone modification."; RL Cell 146:1016-1028(2011). RN [8] RP SUCCINYLATION AT LYS-121. RX PubMed=22389435; DOI=10.1074/mcp.m111.015875; RA Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.; RT "Lysine succinylation and lysine malonylation in histones."; RL Mol. Cell. Proteomics 11:100-107(2012). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-12, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [10] RP HYDROXYBUTYRYLATION AT LYS-6; LYS-13; LYS-21; LYS-24; LYS-25; LYS-35; RP LYS-44; LYS-47; LYS-58; LYS-86; LYS-109; LYS-117 AND LYS-121. RX PubMed=24681537; DOI=10.1038/nchembio.1497; RA Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., Debernardi A., RA Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., Allis C.D., Ren B., RA Khochbin S., Zhao Y.; RT "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone RT mark."; RL Nat. Chem. Biol. 10:365-370(2014). RN [11] RP HYDROXYBUTYRYLATION AT LYS-6; LYS-12; LYS-21; LYS-35; LYS-109 AND LYS-117. RX PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036; RA Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J., RA Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D., RA Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B., RA White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.; RT "Metabolic regulation of gene expression by histone lysine beta- RT hydroxybutyrylation."; RL Mol. Cell 62:194-206(2016). RN [12] RP LACTYLATION AT LYS-6; LYS-12; LYS-16; LYS-17; LYS-21; LYS-86; LYS-109 AND RP LYS-117. RX PubMed=31645732; DOI=10.1038/s41586-019-1678-1; RA Zhang D., Tang Z., Huang H., Zhou G., Cui C., Weng Y., Liu W., Kim S., RA Lee S., Perez-Neut M., Ding J., Czyz D., Hu R., Ye Z., He M., Zheng Y.G., RA Shuman H.A., Dai L., Ren B., Roeder R.G., Becker L., Zhao Y.; RT "Metabolic regulation of gene expression by histone lactylation."; RL Nature 574:575-580(2019). RN [13] RP ADP-RIBOSYLATION AT GLU-36, AND PHOSPHORYLATION AT SER-37. RX PubMed=32822587; DOI=10.1016/j.molcel.2020.08.002; RA Huang D., Camacho C.V., Setlem R., Ryu K.W., Parameswaran B., Gupta R.K., RA Kraus W.L.; RT "Functional interplay between histone H2B ADP-ribosylation and RT phosphorylation controls adipogenesis."; RL Mol. Cell 79:934-949(2020). CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact CC DNA into chromatin, limiting DNA accessibility to the cellular CC machineries which require DNA as a template. Histones thereby play a CC central role in transcription regulation, DNA repair, DNA replication CC and chromosomal stability. DNA accessibility is regulated via a complex CC set of post-translational modifications of histones, also called CC histone code, and nucleosome remodeling. CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of CC DNA. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is CC required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) CC methylation and transcription activation at specific gene loci, such as CC HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 CC (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic CC transcriptional activation and is also prerequisite for histone H3 CC 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with CC the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub CC also acts as a regulator of mRNA splicing: deubiquitination by USP49 is CC required for efficient cotranscriptional splicing of a large set of CC exons (By similarity). {ECO:0000250|UniProtKB:P33778}. CC -!- PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; CC which facilitates apoptotic chromatin condensation (PubMed:15197225, CC PubMed:16039583). Also phosphorylated on Ser-15 in response to DNA CC double strand breaks (DSBs), and in correlation with somatic CC hypermutation and immunoglobulin class-switch recombination CC (PubMed:15197225). Phosphorylation at Ser-37 (H2BS36ph) by AMPK in CC response to stress promotes transcription (PubMed:20647423, CC PubMed:32822587). {ECO:0000269|PubMed:15197225, CC ECO:0000269|PubMed:16039583, ECO:0000269|PubMed:20647423, CC ECO:0000269|PubMed:32822587}. CC -!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. CC It fluctuates in response to extracellular glucose, and associates with CC transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}. CC -!- PTM: ADP-ribosylated by PARP1 or PARP2 on Ser-7 (H2BS6ADPr) in response CC to DNA damage (By similarity). H2BS6ADPr promotes recruitment of CHD1L CC (By similarity). Mono-ADP-ribosylated on Glu-3 (H2BE2ADPr) by PARP3 in CC response to single-strand breaks (By similarity). Poly ADP-ribosylation CC on Glu-36 (H2BE35ADPr) by PARP1 regulates adipogenesis: it inhibits CC phosphorylation at Ser-37 (H2BS36ph), thereby blocking expression of CC pro-adipogenetic genes (PubMed:32822587). CC {ECO:0000250|UniProtKB:P33778, ECO:0000269|PubMed:32822587}. CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and CC marks testis-specific genes in post-meiotic cells, including X-linked CC genes that escape sex chromosome inactivation in haploid cells. CC Crotonylation marks active promoters and enhancers and confers CC resistance to transcriptional repressors. It is also associated with CC post-meiotically activated genes on autosomes. CC {ECO:0000269|PubMed:21925322}. CC -!- PTM: Hydroxybutyrylation of histones is induced by starvation. CC {ECO:0000269|PubMed:27105115}. CC -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA CC directly derived from endogenous or exogenous lactate, leading to CC stimulates gene transcription. {ECO:0000250|UniProtKB:P33778}. CC -!- SIMILARITY: Belongs to the histone H2B family. {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; X05863; CAA29292.1; -; Genomic_DNA. DR EMBL; AY158928; AAO06238.1; -; Genomic_DNA. DR EMBL; AL589651; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS26290.1; -. DR PIR; S04153; S04153. DR RefSeq; NP_835507.1; NM_178200.2. DR AlphaFoldDB; P10854; -. DR SMR; P10854; -. DR BioGRID; 235105; 8. DR IntAct; P10854; 3. DR STRING; 10090.ENSMUSP00000153457; -. DR GlyCosmos; P10854; 1 site, No reported glycans. DR GlyGen; P10854; 1 site. DR iPTMnet; P10854; -. DR PhosphoSitePlus; P10854; -. DR SwissPalm; P10854; -. DR jPOST; P10854; -. DR MaxQB; P10854; -. DR PaxDb; 10090-ENSMUSP00000106102; -. DR ProteomicsDB; 269668; -. DR Antibodypedia; 53616; 149 antibodies from 19 providers. DR DNASU; 319186; -. DR Ensembl; ENSMUST00000224651.2; ENSMUSP00000153457.2; ENSMUSG00000114279.2. DR GeneID; 319186; -. DR KEGG; mmu:319186; -. DR UCSC; uc007prd.2; mouse. DR AGR; MGI:2448404; -. DR CTD; 8342; -. DR MGI; MGI:2448404; H2bc14. DR VEuPathDB; HostDB:ENSMUSG00000114279; -. DR eggNOG; KOG1744; Eukaryota. DR GeneTree; ENSGT01100000263474; -. DR HOGENOM; CLU_075666_2_1_1; -. DR InParanoid; P10854; -. DR OMA; KSRHESY; -. DR OrthoDB; 4835970at2759; -. DR PhylomeDB; P10854; -. DR TreeFam; TF300212; -. DR Reactome; R-MMU-3214847; HATs acetylate histones. DR BioGRID-ORCS; 319186; 13 hits in 49 CRISPR screens. DR PRO; PR:P10854; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; P10854; Protein. DR Bgee; ENSMUSG00000114279; Expressed in spermatid and 52 other cell types or tissues. DR ExpressionAtlas; P10854; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_H2A/H2B/H3. DR InterPro; IPR000558; Histone_H2B. DR PANTHER; PTHR23428; HISTONE H2B; 1. DR PANTHER; PTHR23428:SF326; HISTONE H2B TYPE 2-E; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR SMART; SM00427; H2B; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00357; HISTONE_H2B; 1. DR Genevisible; P10854; MM. PE 1: Evidence at protein level; KW Acetylation; ADP-ribosylation; Chromosome; DNA-binding; Glycoprotein; KW Hydroxylation; Isopeptide bond; Methylation; Nucleosome core; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P23527" FT CHAIN 2..126 FT /note="Histone H2B type 1-M" FT /id="PRO_0000071840" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 17..35 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylproline" FT /evidence="ECO:0000250|UniProtKB:P23527" FT MOD_RES 3 FT /note="ADP-ribosyl glutamic acid" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 6 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 6 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:27105115" FT MOD_RES 6 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 6 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 6 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 6 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 7 FT /note="ADP-ribosylserine" FT /evidence="ECO:0000250|UniProtKB:Q99879" FT MOD_RES 12 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:27105115" FT MOD_RES 12 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 12 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 12 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 13 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 13 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99879" FT MOD_RES 13 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 15 FT /note="Phosphoserine; by STK4/MST1" FT /evidence="ECO:0000269|PubMed:15197225, FT ECO:0000269|PubMed:16039583" FT MOD_RES 16 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99879" FT MOD_RES 16 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 16 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 17 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99879" FT MOD_RES 17 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 17 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 17 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 21 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 21 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:27105115" FT MOD_RES 21 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99879" FT MOD_RES 21 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 21 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 21 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 24 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 24 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99879" FT MOD_RES 24 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 24 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 25 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 35 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 35 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:27105115" FT MOD_RES 35 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 35 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 35 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99879" FT MOD_RES 36 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000269|PubMed:32822587" FT MOD_RES 37 FT /note="Phosphoserine; by AMPK" FT /evidence="ECO:0000269|PubMed:20647423, FT ECO:0000269|PubMed:32822587" FT MOD_RES 44 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 44 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 44 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 47 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 47 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 47 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62807" FT MOD_RES 58 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62807" FT MOD_RES 58 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 80 FT /note="Dimethylated arginine" FT /evidence="ECO:0000250|UniProtKB:Q96A08" FT MOD_RES 86 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q96A08" FT MOD_RES 86 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 86 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q96A08" FT MOD_RES 86 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 87 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q96A08" FT MOD_RES 93 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q96A08" FT MOD_RES 109 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 109 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:27105115" FT MOD_RES 109 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 109 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 109 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62807" FT MOD_RES 116 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q00729" FT MOD_RES 117 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 117 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:27105115" FT MOD_RES 117 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 117 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 117 FT /note="N6-methylated lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q00729" FT MOD_RES 117 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99879" FT MOD_RES 121 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 121 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 121 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 121 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22389435" FT CARBOHYD 113 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250|UniProtKB:P62807" FT CROSSLNK 6 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q99879" FT CROSSLNK 21 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q5QNW6" FT CROSSLNK 35 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:Q99879" FT CROSSLNK 121 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:Q99879" SQ SEQUENCE 126 AA; 13936 MW; FAE8378A44BE7028 CRC64; MPEPTKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSSK //