ID H31_BOVIN Reviewed; 136 AA. AC P68432; P02295; P02296; P16106; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 166. DE RecName: Full=Histone H3.1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP PROTEIN SEQUENCE OF 2-136, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP LYS-15 AND LYS-24, AND METHYLATION AT LYS-10 AND LYS-28. RC TISSUE=Thymus; RX PubMed=4735580; DOI=10.1016/s0021-9258(19)44037-4; RA Delange R.J., Hooper J.A., Smith E.L.; RT "Histone 3. 3. Sequence studies on the cyanogen bromide peptides; complete RT amino acid sequence of calf thymus histone 3."; RL J. Biol. Chem. 248:3261-3274(1973). RN [2] RP PROTEIN SEQUENCE OF 2-136, AND CLEAVAGE OF INITIATOR METHIONINE. RC TISSUE=Thymus; RX PubMed=1167550; DOI=10.1016/s0021-9258(19)41782-1; RA Patthy L., Smith E.L.; RT "Histone III. VI. Two forms of calf thymus histone III."; RL J. Biol. Chem. 250:1919-1920(1975). RN [3] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Thymus; RX PubMed=4735579; DOI=10.1016/s0021-9258(19)44035-0; RA Delange R.J., Smith E.L.; RT "Histone 3. I. Isolation and sequences of the tryptic peptides from the RT maleylated calf thymus protein."; RL J. Biol. Chem. 248:3248-3254(1973). RN [4] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Thymus; RX PubMed=4700459; DOI=10.1016/s0021-9258(19)44036-2; RA Hooper J.A., Smith E.L.; RT "Histone 3. II. Isolation and sequences of chymotryptic peptides from calf RT thymus histone 3."; RL J. Biol. Chem. 248:3255-3260(1973). RN [5] RP PHOSPHORYLATION AT SER-11 AND SER-29. RX PubMed=10464286; DOI=10.1074/jbc.274.36.25543; RA Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M., Okawa K., RA Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.; RT "Identification of a novel phosphorylation site on histone H3 coupled with RT mitotic chromosome condensation."; RL J. Biol. Chem. 274:25543-25549(1999). 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. Interacts with TONSL; CHAF1A; CHAF1B; MCM2 and DNAJC9 (By CC similarity). {ECO:0000250|UniProtKB:P68431}. CC -!- INTERACTION: CC P68432; O43463: SUV39H1; Xeno; NbExp=2; IntAct=EBI-79764, EBI-349968; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression strongly CC decreases as cell division slows down during the process of CC differentiation. CC -!- PTM: Acetylation is generally linked to gene activation. Acetylation on CC Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on CC Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 CC (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a CC central role in chromatin structure: localizes at the surface of the CC histone octamer and stimulates transcription, possibly by promoting CC nucleosome instability. {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 CC impairs methylation and represses transcription. CC {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked CC to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by CC PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 CC (H3R2me2a) by PRMT6 is linked to gene repression and is mutually CC exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is CC present at the 3' of genes regardless of their transcription state and CC is enriched on inactive promoters, while it is absent on active CC promoters. {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 CC (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) CC facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 CC (H3K79me) is associated with DNA double-strand break (DSB) responses CC and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) CC and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys- CC 10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) CC and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and CC acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 CC (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. CC Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in CC inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) CC by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required CC for DNA replication. {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and CC dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) CC by AURKB is crucial for chromosome condensation and cell-cycle CC progression during mitosis and meiosis. In addition phosphorylation at CC Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase CC because it enables the transcription of genes following external CC stimulation, like mitogens, stress, growth factors or UV irradiation CC and result in the activation of genes, such as c-fos and c-jun. CC Phosphorylation at Ser-11 (H3S10ph), which is linked to gene CC activation, prevents methylation at Lys-10 (H3K9me) but facilitates CC acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB CC mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from CC heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an CC essential regulatory mechanism for neoplastic cell transformation. CC Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or CC AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation CC at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic CC transcriptional activation that prevents demethylation of Lys-5 CC (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at CC Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. CC Phosphorylation at Thr-12 (H3T11ph) by PKN1 or isoform M2 of PKM (PKM2) CC is a specific tag for epigenetic transcriptional activation that CC promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. CC Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 CC regulates the transcription of cell cycle regulatory genes by CC modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 CC (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from CC chromatin. {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is CC required for V(D)J recombination (By similarity). Ubiquitinated by the CC CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may CC weaken the interaction between histones and DNA and facilitate DNA CC accessibility to repair proteins (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated CC by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and CC results in gene repression. {ECO:0000250|UniProtKB:P68431}. 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:0000250|UniProtKB:P68431}. CC -!- PTM: Butyrylation of histones marks active promoters and competes with CC histone acetylation. It is present during late spermatogenesis. CC {ECO:0000250|UniProtKB:P68433}. CC -!- PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a CC maximum frequency around the transcription start sites of genes. It CC gives a specific tag for epigenetic transcription activation. CC Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA CC damage promotes chromatin condensation and double-strand breaks (DSBs) CC repair. {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Serine ADP-ribosylation by PARP1 or PARP2 constitutes the primary CC form of ADP-ribosylation of proteins in response to DNA damage. Serine CC ADP-ribosylation at Ser-11 (H3S10ADPr) promotes recruitment of CHD1L. CC H3S10ADPr is mutually exclusive with phosphorylation at Ser-11 CC (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac). CC {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Serotonylated by TGM2 at Gln-6 (H3Q5ser) during serotonergic CC neuron differentiation (By similarity). H3Q5ser is associated with CC trimethylation of Lys-5 (H3K4me3) and enhances general transcription CC factor IID (TFIID) complex-binding to H3K4me3, thereby facilitating CC transcription (By similarity). {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Dopaminylated by TGM2 at Gln-6 (H3Q5dop) in ventral tegmental area CC (VTA) neurons (By similarity). H3Q5dop mediates neurotransmission- CC independent role of nuclear dopamine by regulating relapse-related CC transcriptional plasticity in the reward system (By similarity). CC {ECO:0000250|UniProtKB:P68431, ECO:0000250|UniProtKB:Q6LED0}. 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:P68431}. CC -!- MISCELLANEOUS: This histone is only present in mammals. CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}. CC -!- CAUTION: Disulfide bonds have been reported but this may not be CC physiologically relevant. {ECO:0000305|PubMed:4735580}. 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 PIR; A02624; HSBO3. DR RefSeq; XP_002697506.1; XM_002697460.4. DR RefSeq; XP_002697575.1; XM_002697529.4. DR RefSeq; XP_005196706.1; XM_005196649.3. DR RefSeq; XP_005223855.1; XM_005223798.3. DR RefSeq; XP_010816767.1; XM_010818465.2. DR RefSeq; XP_010823755.1; XM_010825453.2. DR RefSeq; XP_015315463.1; XM_015459977.1. DR RefSeq; XP_015324501.1; XM_015469015.1. DR RefSeq; XP_015324502.1; XM_015469016.1. DR RefSeq; XP_874006.1; XM_868913.4. DR AlphaFoldDB; P68432; -. DR SMR; P68432; -. DR BioGRID; 544398; 4. DR IntAct; P68432; 9. DR STRING; 9913.ENSBTAP00000059273; -. DR iPTMnet; P68432; -. DR PaxDb; 9913-ENSBTAP00000044281; -. DR PeptideAtlas; P68432; -. DR Ensembl; ENSBTAT00000069848.1; ENSBTAP00000074529.1; ENSBTAG00000048478.1. DR Ensembl; ENSBTAT00000071248.1; ENSBTAP00000059273.1; ENSBTAG00000050102.1. DR Ensembl; ENSBTAT00000080858.1; ENSBTAP00000071787.1; ENSBTAG00000054582.1. DR Ensembl; ENSBTAT00000083013.1; ENSBTAP00000061745.1; ENSBTAG00000050209.1. DR Ensembl; ENSBTAT00000085851.1; ENSBTAP00000070745.1; ENSBTAG00000048666.1. DR Ensembl; ENSBTAT00000087179.1; ENSBTAP00000061853.1; ENSBTAG00000050477.1. DR GeneID; 107131750; -. DR GeneID; 616800; -. DR GeneID; 616819; -. DR KEGG; bta:107131750; -. DR KEGG; bta:616800; -. DR KEGG; bta:616819; -. DR CTD; 8356; -. DR CTD; 8357; -. DR CTD; 8358; -. DR VEuPathDB; HostDB:ENSBTAG00000048478; -. DR VEuPathDB; HostDB:ENSBTAG00000048666; -. DR VEuPathDB; HostDB:ENSBTAG00000050102; -. DR VEuPathDB; HostDB:ENSBTAG00000050209; -. DR VEuPathDB; HostDB:ENSBTAG00000050477; -. DR VEuPathDB; HostDB:ENSBTAG00000054582; -. DR VGNC; VGNC:83547; H3C1. DR VGNC; VGNC:83552; H3C2. DR VGNC; VGNC:83553; H3C3. DR VGNC; VGNC:83567; H3C4. DR VGNC; VGNC:84555; H3C6. DR VGNC; VGNC:83572; H3C7. DR eggNOG; KOG1745; Eukaryota. DR GeneTree; ENSGT01100000263514; -. DR HOGENOM; CLU_078295_4_0_1; -. DR InParanoid; P68432; -. DR OMA; NIERETW; -. DR OrthoDB; 5360611at2759; -. DR TreeFam; TF314241; -. DR Reactome; R-BTA-1266695; Interleukin-7 signaling. DR Reactome; R-BTA-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-BTA-212300; PRC2 methylates histones and DNA. DR Reactome; R-BTA-2299718; Condensation of Prophase Chromosomes. DR Reactome; R-BTA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-BTA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-BTA-3214815; HDACs deacetylate histones. DR Reactome; R-BTA-3214841; PKMTs methylate histone lysines. DR Reactome; R-BTA-3214842; HDMs demethylate histones. DR Reactome; R-BTA-3214847; HATs acetylate histones. DR Reactome; R-BTA-3214858; RMTs methylate histone arginines. DR Reactome; R-BTA-3247509; Chromatin modifying enzymes. DR Reactome; R-BTA-427359; SIRT1 negatively regulates rRNA expression. DR Reactome; R-BTA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-BTA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-BTA-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-BTA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3. DR Reactome; R-BTA-68616; Assembly of the ORC complex at the origin of replication. DR Reactome; R-BTA-73728; RNA Polymerase I Promoter Opening. DR Reactome; R-BTA-73772; RNA Polymerase I Promoter Escape. DR Reactome; R-BTA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-BTA-9018519; Estrogen-dependent gene expression. DR Reactome; R-BTA-983231; Factors involved in megakaryocyte development and platelet production. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000048478; Expressed in spiral colon and 77 other cell types or tissues. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. 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; IPR000164; Histone_H3/CENP-A. DR PANTHER; PTHR11426; HISTONE H3; 1. DR PANTHER; PTHR11426:SF242; HISTONE H3.1; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00622; HISTONEH3. DR SMART; SM00428; H3; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00322; HISTONE_H3_1; 1. DR PROSITE; PS00959; HISTONE_H3_2; 1. PE 1: Evidence at protein level; KW Acetylation; ADP-ribosylation; Chromosome; Citrullination; KW Direct protein sequencing; DNA-binding; Hydroxylation; Lipoprotein; KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1167550, FT ECO:0000269|PubMed:4735580" FT CHAIN 2..136 FT /note="Histone H3.1" FT /id="PRO_0000221256" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 3 FT /note="Asymmetric dimethylarginine; by PRMT6; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 3 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 4 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="Allysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 5 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 6 FT /note="5-glutamyl dopamine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 6 FT /note="5-glutamyl serotonin; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 7 FT /note="Phosphothreonine; by PKC" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 9 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 9 FT /note="Symmetric dimethylarginine; by PRMT5; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 10 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:4735580" FT MOD_RES 10 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:4735580" FT MOD_RES 10 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 10 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 10 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 10 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 10 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 10 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:4735580" FT MOD_RES 11 FT /note="ADP-ribosylserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 11 FT /note="Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, FT RPS6KA4 and RPS6KA5" FT /evidence="ECO:0000269|PubMed:10464286" FT MOD_RES 12 FT /note="Phosphothreonine; by PKC and CHEK1" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 15 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 15 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 15 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:4735580" FT MOD_RES 15 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 15 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 15 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 18 FT /note="Asymmetric dimethylarginine; by CARM1; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 18 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250" FT MOD_RES 19 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 19 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 19 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 19 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 19 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 19 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 19 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 19 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 24 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 24 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 24 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:4735580" FT MOD_RES 24 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 24 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 24 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 24 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 24 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 27 FT /note="Citrulline" FT /evidence="ECO:0000250" FT MOD_RES 28 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:4735580" FT MOD_RES 28 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:4735580" FT MOD_RES 28 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 28 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 28 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 28 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 28 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 28 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:4735580" FT MOD_RES 29 FT /note="ADP-ribosylserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 29 FT /note="Phosphoserine; alternate; by AURKB, AURKC and FT RPS6KA5" FT /evidence="ECO:0000269|PubMed:10464286" FT MOD_RES 37 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 37 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 37 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 37 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 37 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 38 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 42 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 57 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250" FT MOD_RES 57 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 57 FT /note="N6-methyllysine; by EHMT2; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 65 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 65 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 80 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 81 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P84243" FT MOD_RES 108 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 116 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 116 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT LIPID 19 FT /note="N6-decanoyllysine" FT /evidence="ECO:0000250|UniProtKB:P68431" SQ SEQUENCE 136 AA; 15404 MW; 9B89008EA50A0EF6 CRC64; MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA //