ID H37_HUMAN Reviewed; 136 AA. AC Q5TEC6; DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=Histone H3-7 {ECO:0000305}; GN Name=H3-7 {ECO:0000312|HGNC:HGNC:32060}; GN Synonyms=H3-2, HIST2H3PS2 {ECO:0000312|HGNC:HGNC:32060}; 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 {ECO:0000312|EMBL:CAI23568.1}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [2] {ECO:0007744|PDB:4H75} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-9 IN COMPLEX WITH SPIN1. RX PubMed=23077255; DOI=10.1073/pnas.1208517109; RA Yang N., Wang W., Wang Y., Wang M., Zhao Q., Rao Z., Zhu B., Xu R.M.; RT "Distinct mode of methylated lysine-4 of histone H3 recognition by tandem RT tudor-like domains of Spindlin1."; RL Proc. Natl. Acad. Sci. U.S.A. 109:17954-17959(2012). 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 {ECO:0000250|UniProtKB:P68431}. 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. During nucleosome assembly the chaperone ASF1A interacts with the CC histone H3-H4 heterodimer. {ECO:0000250|UniProtKB:P68431}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}. 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 (By similarity). {ECO:0000250|UniProtKB:P84243}. CC -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 CC impairs methylation and represses transcription. CC {ECO:0000250|UniProtKB:P84243}. 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 (By similarity). {ECO:0000250|UniProtKB:P84243}. 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 (By similarity). {ECO:0000250|UniProtKB:P84243}. 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 Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 CC (HP1 alpha) from chromatin (By similarity). CC {ECO:0000250|UniProtKB:P84243}. CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P84243}. 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 (By similarity). CC {ECO:0000250|UniProtKB:P84243}. CC -!- PTM: Butyrylation of histones marks active promoters and competes with CC histone acetylation. It is present during late spermatogenesis. CC {ECO:0000250|UniProtKB:P84243}. 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 constitutes the primary form of ADP- CC ribosylation of proteins in response to DNA damage. Serine ADP- CC ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with CC phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 CC (H3K9ac). {ECO:0000250|UniProtKB:P68431}. CC -!- SIMILARITY: Belongs to the histone H3 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; AC239798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL109948; CAI23568.1; -; Genomic_DNA. DR CCDS; CCDS30842.1; -. DR PDB; 4H75; X-ray; 2.10 A; B=2-9. DR PDBsum; 4H75; -. DR AlphaFoldDB; Q5TEC6; -. DR SMR; Q5TEC6; -. DR IntAct; Q5TEC6; 24. DR STRING; 9606.ENSP00000499501; -. DR BioMuta; HIST2H3PS2; -. DR EPD; Q5TEC6; -. DR MassIVE; Q5TEC6; -. DR MaxQB; Q5TEC6; -. DR PaxDb; 9606-ENSP00000476960; -. DR PeptideAtlas; Q5TEC6; -. DR ProteomicsDB; 65042; -. DR Antibodypedia; 79211; 181 antibodies from 2 providers. DR Ensembl; ENST00000392948.5; ENSP00000476960.1; ENSG00000273213.4. DR Ensembl; ENST00000609879.2; ENSP00000499501.1; ENSG00000273213.4. DR MANE-Select; ENST00000392948.5; ENSP00000476960.1; NM_001372105.2; NP_001359034.1. DR UCSC; uc057jyp.1; human. DR AGR; HGNC:32060; -. DR GeneCards; H3-7; -. DR HGNC; HGNC:32060; H3-7. DR HPA; ENSG00000273213; Low tissue specificity. DR neXtProt; NX_Q5TEC6; -. DR OpenTargets; ENSG00000273213; -. DR VEuPathDB; HostDB:ENSG00000273213; -. DR eggNOG; KOG1745; Eukaryota. DR GeneTree; ENSGT01100000263559; -. DR HOGENOM; CLU_078295_4_0_1; -. DR InParanoid; Q5TEC6; -. DR OrthoDB; 4687963at2759; -. DR PhylomeDB; Q5TEC6; -. DR TreeFam; TF314241; -. DR SignaLink; Q5TEC6; -. DR SIGNOR; Q5TEC6; -. DR PRO; PR:Q5TEC6; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5TEC6; Protein. DR Bgee; ENSG00000273213; Expressed in left ovary and 123 other cell types or tissues. DR ExpressionAtlas; Q5TEC6; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; HDA: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:SF247; HISTONE H3-7; 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 3D-structure; Acetylation; ADP-ribosylation; Chromosome; Citrullination; KW DNA-binding; Hydroxylation; Methylation; Nucleosome core; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q16695" FT CHAIN 2..136 FT /note="Histone H3-7" FT /id="PRO_0000451612" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 3 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 3 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:P84243" 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:P84243" 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-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" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 9 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:P84243" FT MOD_RES 9 FT /note="Symmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 10 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68432" FT MOD_RES 10 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68432" 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-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 10 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68432" FT MOD_RES 11 FT /note="ADP-ribosylserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 11 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68432" FT MOD_RES 12 FT /note="Phosphothreonine" 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:0000250|UniProtKB:P68432" FT MOD_RES 15 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84243" 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" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 18 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:P84243" 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:Q16695" FT MOD_RES 19 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 19 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84243" 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:0000250|UniProtKB:Q16695" FT MOD_RES 24 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 24 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84243" 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|UniProtKB:P84243" FT MOD_RES 28 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68432" FT MOD_RES 28 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68432" 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-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84243" 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:0000250|UniProtKB:P68432" FT MOD_RES 29 FT /note="ADP-ribosylserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 29 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q16695" 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-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84243" FT MOD_RES 57 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 57 FT /note="N6-methyllysine" 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:Q16695" 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:P84243" 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:Q16695" 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:P84243" 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:P84243" 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" SQ SEQUENCE 136 AA; 15430 MW; 6916448FA50B0FEC CRC64; MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQEFK TDLRFQSSAV MALQEAREAY LVGLFEDTNL CAIHAKRVTI MPKDIQLVSR IRGERA //