ID H2B1B_HUMAN Reviewed; 126 AA. AC P33778; Q4KN36; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 210. DE RecName: Full=Histone H2B type 1-B; DE AltName: Full=H2B-clustered histone 3 {ECO:0000312|HGNC:HGNC:4751}; DE AltName: Full=Histone H2B.1; DE AltName: Full=Histone H2B.f; DE Short=H2B/f; GN Name=H2BC3 {ECO:0000312|HGNC:HGNC:4751}; GN Synonyms=H2BFF, HIST1H2BB {ECO:0000312|HGNC:HGNC:4751}; 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 [GENOMIC DNA]. RX PubMed=1916825; DOI=10.1016/0888-7543(91)90183-f; RA Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.; RT "Isolation and characterization of two human H1 histone genes within RT clusters of core histone genes."; RL Genomics 10:940-948(1991). 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 MRNA]. 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 IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION, AND PHOSPHORYLATION. RX PubMed=11709551; DOI=10.1074/jbc.m107894200; RA Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.; RT "Global regulation of post-translational modifications on core histones."; RL J. Biol. Chem. 277:2579-2588(2002). RN [5] RP PHOSPHORYLATION AT SER-15. RX PubMed=12757711; DOI=10.1016/s0092-8674(03)00355-6; RA Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A., RA Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.; RT "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile RT twenty kinase."; RL Cell 113:507-517(2003). RN [6] RP UBIQUITINATION AT LYS-121. RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025; RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., RA Reinberg D.; RT "Monoubiquitination of human histone H2B: the factors involved and their RT roles in HOX gene regulation."; RL Mol. Cell 20:601-611(2005). RN [7] RP ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21. RX PubMed=16283522; DOI=10.1007/s11010-005-8285-1; RA Golebiowski F., Kasprzak K.S.; RT "Inhibition of core histones acetylation by carcinogenic nickel(II)."; RL Mol. Cell. Biochem. 279:133-139(2005). RN [8] RP UBIQUITINATION AT LYS-121. RX PubMed=16713563; DOI=10.1016/j.cell.2006.04.029; RA Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D.; RT "Histone H2B monoubiquitination functions cooperatively with FACT to RT regulate elongation by RNA polymerase II."; RL Cell 125:703-717(2006). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-16; LYS-17; LYS-21 AND RP LYS-24, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [10] 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 [11] RP UBIQUITINATION AT LYS-35. RX PubMed=21726816; DOI=10.1016/j.molcel.2011.05.015; RA Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.; RT "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase RT for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation."; RL Mol. Cell 43:132-144(2011). RN [12] RP SUCCINYLATION AT LYS-35; LYS-117 AND LYS-121, AND MALONYLATION AT LYS-117. 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 [13] RP UBIQUITINATION, AND DEUBIQUITINATION BY USP49. RX PubMed=23824326; DOI=10.1101/gad.211037.112; RA Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S., RA Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M., RA Giles K.E., Ma L., Wang H.; RT "USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA RT splicing."; RL Genes Dev. 27:1581-1595(2013). RN [14] 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 [15] RP BUTYRYLATION AT LYS-6 AND LYS-21. RX PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014; RA Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z., RA Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J., RA Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C., Panne D., RA Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.; RT "Dynamic competing histone H4 K5K8 acetylation and butyrylation are RT hallmarks of highly active gene promoters."; RL Mol. Cell 62:169-180(2016). RN [16] RP HYDROXYBUTYRYLATION AT LYS-6; LYS-12; LYS-17; LYS-21; LYS-35; LYS-86; RP LYS-117 AND LYS-121. 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 [17] RP ADP-RIBOSYLATION AT GLU-3. RX PubMed=27530147; DOI=10.1038/ncomms12404; RA Grundy G.J., Polo L.M., Zeng Z., Rulten S.L., Hoch N.C., Paomephan P., RA Xu Y., Sweet S.M., Thorne A.W., Oliver A.W., Matthews S.J., Pearl L.H., RA Caldecott K.W.; RT "PARP3 is a sensor of nicked nucleosomes and monoribosylates histone RT H2B(Glu2)."; RL Nat. Commun. 7:12404-12404(2016). RN [18] RP GLUTARYLATION AT LYS-17; LYS-35; LYS-44; LYS-47; LYS-109; LYS-117 AND RP LYS-121. RX PubMed=31542297; DOI=10.1016/j.molcel.2019.08.018; RA Bao X., Liu Z., Zhang W., Gladysz K., Fung Y.M.E., Tian G., Xiong Y., RA Wong J.W.H., Yuen K.W.Y., Li X.D.; RT "Glutarylation of histone H4 lysine 91 regulates chromatin dynamics."; RL Mol. Cell 0:0-0(2019). RN [19] RP LACTYLATION AT LYS-6; LYS-12; LYS-16; LYS-17; LYS-21; LYS-24; LYS-44; RP LYS-86; LYS-109; LYS-117 AND LYS-121. 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 [20] RP ADP-RIBOSYLATION AT SER-7. RX PubMed=34874266; DOI=10.7554/elife.71502; RA Mohapatra J., Tashiro K., Beckner R.L., Sierra J., Kilgore J.A., RA Williams N.S., Liszczak G.; RT "Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin RT remodeling."; RL Elife 10:0-0(2021). 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 -!- INTERACTION: CC P33778; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-357986, EBI-17589229; 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. {ECO:0000269|PubMed:11709551}. CC -!- PTM: Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress CC promotes transcription (By similarity). Phosphorylated on Ser-15 CC (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic CC chromatin condensation (PubMed:12757711). Also phosphorylated on Ser-15 CC in response to DNA double strand breaks (DSBs), and in correlation with CC somatic hypermutation and immunoglobulin class-switch recombination. CC {ECO:0000250|UniProtKB:Q64475, ECO:0000269|PubMed:12757711}. 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 (PubMed:34874266). H2BS6ADPr promotes recruitment of CC CHD1L (PubMed:34874266). Mono-ADP-ribosylated on Glu-3 (H2BE2ADPr) by CC PARP3 in response to single-strand breaks (PubMed:27530147). Poly ADP- CC ribosylation on Glu-36 (H2BE35ADPr) by PARP1 regulates adipogenesis: it CC inhibits phosphorylation at Ser-37 (H2BS36ph), thereby blocking CC expression of pro-adipogenetic genes (By similarity). CC {ECO:0000250|UniProtKB:Q6ZWY9, ECO:0000269|PubMed:27530147, CC ECO:0000269|PubMed:34874266}. 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: 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:0000269|PubMed:31645732}. 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; X57127; CAA40406.1; -; Genomic_DNA. DR EMBL; AF531285; AAN06685.1; -; Genomic_DNA. DR EMBL; BC096728; AAH96728.1; -; mRNA. DR CCDS; CCDS4575.1; -. DR PIR; I37445; I37445. DR RefSeq; NP_066406.1; NM_021062.2. DR PDB; 3X1S; X-ray; 2.81 A; D/H=2-126. DR PDB; 3X1U; X-ray; 3.25 A; D/H=3-126. DR PDBsum; 3X1S; -. DR PDBsum; 3X1U; -. DR AlphaFoldDB; P33778; -. DR SMR; P33778; -. DR BioGRID; 109271; 372. DR CORUM; P33778; -. DR DIP; DIP-47505N; -. DR IntAct; P33778; 25. DR MINT; P33778; -. DR STRING; 9606.ENSP00000482674; -. DR GlyCosmos; P33778; 4 sites, 2 glycans. DR GlyGen; P33778; 3 sites, 2 O-linked glycans (2 sites). DR iPTMnet; P33778; -. DR MetOSite; P33778; -. DR PhosphoSitePlus; P33778; -. DR SwissPalm; P33778; -. DR BioMuta; HIST1H2BB; -. DR DMDM; 462236; -. DR jPOST; P33778; -. DR MassIVE; P33778; -. DR MaxQB; P33778; -. DR PaxDb; 9606-ENSP00000482674; -. DR PeptideAtlas; P33778; -. DR ProteomicsDB; 54927; -. DR Pumba; P33778; -. DR TopDownProteomics; P33778; -. DR Antibodypedia; 72531; 486 antibodies from 26 providers. DR DNASU; 3018; -. DR Ensembl; ENST00000615966.2; ENSP00000482674.2; ENSG00000276410.4. DR GeneID; 3018; -. DR KEGG; hsa:3018; -. DR MANE-Select; ENST00000615966.2; ENSP00000482674.2; NM_021062.3; NP_066406.1. DR UCSC; uc003nfu.4; human. DR AGR; HGNC:4751; -. DR CTD; 3018; -. DR DisGeNET; 3018; -. DR GeneCards; H2BC3; -. DR HGNC; HGNC:4751; H2BC3. DR HPA; ENSG00000276410; Tissue enhanced (bone marrow, lymphoid tissue, testis). DR MIM; 602803; gene. DR neXtProt; NX_P33778; -. DR OpenTargets; ENSG00000276410; -. DR VEuPathDB; HostDB:ENSG00000276410; -. DR eggNOG; KOG1744; Eukaryota. DR GeneTree; ENSGT01100000263575; -. DR InParanoid; P33778; -. DR OMA; RRMESYN; -. DR OrthoDB; 5258202at2759; -. DR PhylomeDB; P33778; -. DR TreeFam; TF300212; -. DR PathwayCommons; P33778; -. DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine. DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine. DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine. DR Reactome; R-HSA-110331; Cleavage of the damaged purine. DR Reactome; R-HSA-1221632; Meiotic synapsis. DR Reactome; R-HSA-171306; Packaging Of Telomere Ends. DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation. DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA. DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes. DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence. DR Reactome; R-HSA-3214815; HDACs deacetylate histones. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression. DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-5334118; DNA methylation. DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis. DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ). DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends. DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere. DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication. DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint. DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening. DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR Reactome; R-HSA-912446; Meiotic recombination. DR Reactome; R-HSA-9609690; HCMV Early Events. DR Reactome; R-HSA-9610379; HCMV Late Events. DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis. DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere. DR Reactome; R-HSA-9710421; Defective pyroptosis. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR Reactome; R-HSA-9821002; Chromatin modifications during the maternal to zygotic transition (MZT). DR Reactome; R-HSA-9821993; Replacement of protamines by nucleosomes in the male pronucleus. DR SignaLink; P33778; -. DR SIGNOR; P33778; -. DR BioGRID-ORCS; 3018; 530 hits in 1109 CRISPR screens. DR ChiTaRS; HIST1H2BB; human. DR GeneWiki; HIST1H2BB; -. DR GenomeRNAi; 3018; -. DR Pharos; P33778; Tbio. DR PRO; PR:P33778; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P33778; Protein. DR Bgee; ENSG00000276410; Expressed in bone marrow cell and 74 other cell types or tissues. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000786; C:nucleosome; NAS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB. 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:SF384; HISTONE H2B TYPE 2-F; 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; P33778; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Chromosome; DNA-binding; KW Glycoprotein; Hydroxylation; Isopeptide bond; Methylation; Nucleosome core; KW Nucleus; 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-B" FT /id="PRO_0000071832" FT REGION 1..35 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:0000269|PubMed:27530147" 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:0000269|PubMed:16283522" FT MOD_RES 6 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000269|PubMed:27105113" 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:0000269|PubMed:34874266" 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:0000250|UniProtKB:Q64475" 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:0000269|PubMed:16283522, FT ECO:0007744|PubMed:19608861" 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:12757711" FT MOD_RES 16 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16283522, FT ECO:0007744|PubMed:19608861" 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-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:27105115" FT MOD_RES 17 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" 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:0000269|PubMed:31542297" 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:0000269|PubMed:16283522, FT ECO:0007744|PubMed:19608861" FT MOD_RES 21 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000269|PubMed:27105113" 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:0007744|PubMed:19608861" 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:0000269|PubMed:31645732" 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:0000269|PubMed:31542297" FT MOD_RES 35 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22389435" FT MOD_RES 36 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000250|UniProtKB:Q64475" FT MOD_RES 37 FT /note="Phosphoserine; by AMPK" FT /evidence="ECO:0000250|UniProtKB:Q64475" 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:0000269|PubMed:31542297" FT MOD_RES 44 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" 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:0000269|PubMed:31542297" 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-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:27105115" 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-glutaryllysine; alternate" FT /evidence="ECO:0000269|PubMed:31542297" 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:0000269|PubMed:31542297" FT MOD_RES 117 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 117 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22389435" 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:0000269|PubMed:22389435" FT MOD_RES 121 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 121 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:27105115" FT MOD_RES 121 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000269|PubMed:31542297" FT MOD_RES 121 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" 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:P58876" 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:0000269|PubMed:21726816" FT CROSSLNK 121 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000269|PubMed:16307923, FT ECO:0000269|PubMed:16713563" FT HELIX 39..49 FT /evidence="ECO:0007829|PDB:3X1S" FT HELIX 57..84 FT /evidence="ECO:0007829|PDB:3X1S" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:3X1U" FT HELIX 92..102 FT /evidence="ECO:0007829|PDB:3X1S" FT HELIX 105..123 FT /evidence="ECO:0007829|PDB:3X1S" SQ SEQUENCE 126 AA; 13950 MW; D2D6B95A9A344EF7 CRC64; MPEPSKSAPA PKKGSKKAIT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSSK //