H3C_MOUSE
ID H3C_MOUSE Reviewed; 136 AA.
AC P02301;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Histone H3.3C;
DE AltName: Full=Embryonic;
GN Name=H3-5 {ECO:0000250|UniProtKB:Q6NXT2};
GN Synonyms=Gm14384, H3f3c {ECO:0000312|MGI:MGI:3650546};
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=6457299; DOI=10.1073/pnas.78.7.4078;
RA Sittman D.B., Chiu I.-M., Pan C.-J., Cohn R.H., Kedes L.H.,
RA Marzluff W.F. Jr.;
RT "Isolation of two clusters of mouse histone genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4078-4082(1981).
RN [2]
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).
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: 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: 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: 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 (By similarity).
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 and Lys-80 are linked to
CC gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent
CC acetylation of H3 and H4. Methylation at Lys-80 is associated with DNA
CC double-strand break (DSB) responses and is a specific target for
CC TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked
CC to gene repression. Methylation at Lys-10 (H3K9me) is a specific target
CC for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent
CC phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4.
CC Methylation at Lys-5 (H3K4me) and Lys-80 require preliminary
CC monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me)
CC and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin.
CC Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes
CC interaction with PCNA and is required for DNA replication (By
CC 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: 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: 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}.
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DR EMBL; V00754; CAA24131.1; -; Genomic_DNA.
DR EMBL; AL844536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A02633; HSMS34.
DR RefSeq; XP_894986.1; XM_889893.7.
DR AlphaFoldDB; P02301; -.
DR SMR; P02301; -.
DR BioGRID; 551688; 3.
DR IntAct; P02301; 1.
DR MINT; P02301; -.
DR iPTMnet; P02301; -.
DR PhosphoSitePlus; P02301; -.
DR jPOST; P02301; -.
DR MaxQB; P02301; -.
DR PeptideAtlas; P02301; -.
DR PRIDE; P02301; -.
DR ProteomicsDB; 269796; -.
DR MGI; MGI:3650546; H3f3c.
DR InParanoid; P02301; -.
DR OrthoDB; 1564596at2759; -.
DR ChiTaRS; H3f3c; mouse.
DR PRO; PR:P02301; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P02301; protein.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 3: Inferred from homology;
KW Acetylation; ADP-ribosylation; Chromosome; Citrullination; DNA-binding;
KW Hydroxylation; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..136
FT /note="Histone H3.3C"
FT /id="PRO_0000221252"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphothreonine; by HASPIN"
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; by PKC"
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; by PRMT5; alternate"
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; by AURKB, AURKC, RPS6KA3,
FT RPS6KA4 and RPS6KA5"
FT /evidence="ECO:0000250|UniProtKB:P68432"
FT MOD_RES 12
FT /note="Phosphothreonine; by PKC"
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; by CARM1; alternate"
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:P68431"
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:P68432"
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; by AURKB, AURKC and
FT RPS6KA5"
FT /evidence="ECO:0000250|UniProtKB:P68432"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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; 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:Q6NXT2"
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:Q6NXT2"
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"
FT CONFLICT 3
FT /note="L -> H (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="G -> C (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="T -> A (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="P -> S (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="G -> D (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="R -> L (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..57
FT /note="QK -> H (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="R -> H (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="R -> Q (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..101
FT /note="YL -> NR (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="R -> C (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 120..121
FT /note="IM -> VI (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..132
FT /note="RRIR -> HSIL (in Ref. 1; CAA24131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 15315 MW; 6758ED3E62CFF91E CRC64;
MALTKQTARK STGGKAPRKQ LATKATRKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
