H3C_XENLA
ID H3C_XENLA Reviewed; 136 AA.
AC P02302;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Histone H3.3C;
GN Name=h3-5; Synonyms=h3f3c;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (GENE CLUSTER X1H1).
RX PubMed=6274702; DOI=10.1016/0014-5793(81)81211-2;
RA Moorman A.F.M., de Boer P.A.J., de Laaf R.T.M., van Dongen W.M.A.M.,
RA Destree O.H.J.;
RT "Primary structure of the histone H3 and H4 genes and their flanking
RT sequences in a minor histone gene cluster of Xenopus laevis.";
RL FEBS Lett. 136:45-52(1981).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF NUCLEOSOME CORE COMPLEX, AND
RP SUBUNIT.
RX PubMed=9305837; DOI=10.1038/38444;
RA Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J.;
RT "Crystal structure of the nucleosome core particle at 2.8 A resolution.";
RL Nature 389:251-260(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF NUCLEOSOME CORE COMPLEX, AND
RP SUBUNIT.
RX PubMed=12559907; DOI=10.1016/s0022-2836(02)01407-9;
RA Suto R.K., Edayathumangalam R.S., White C.L., Melander C., Gottesfeld J.M.,
RA Dervan P.B., Luger K.;
RT "Crystal structures of nucleosome core particles in complex with minor
RT groove DNA-binding ligands.";
RL J. Mol. Biol. 326:371-380(2003).
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. {ECO:0000269|PubMed:12559907, ECO:0000269|PubMed:9305837}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Acetylation is generally linked to gene activation. 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: Asymmetric dimethylation at Arg-18 (H3R17me2a) is linked to gene
CC activation. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is
CC linked to gene repression and is mutually exclusive with H3 Lys-5
CC methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of
CC genes regardless of their transcription state and is enriched on
CC inactive promoters, while it is absent on active promoters (By
CC similarity). {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) are linked to
CC gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent
CC acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated
CC with DNA double-strand break (DSB) responses and is a specific target
CC for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are
CC linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific
CC target 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 (H3K79me) require preliminary
CC monoubiquitination of H2B at 'Lys-120' (By similarity).
CC {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 Phosphorylation at Thr-7 (H3T6ph) by prkcb is a specific tag for
CC epigenetic transcriptional activation that prevents demethylation of
CC Lys-5 (H3K4me) by lsd1/kdm1a. At centromeres, specifically
CC phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by
CC DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 or isoform
CC M2 of PKM (PKM2) is a specific tag for epigenetic transcriptional
CC activation that promotes demethylation of Lys-10 (H3K9me) by
CC kdm4c/jmjd2c. Phosphorylation at Tyr-42 (H3Y41ph) by jak2 promotes
CC exclusion of cbx5 (HP1 alpha) from chromatin (By similarity).
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine only takes
CC place on H3K4me3 and results in gene repression.
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: 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; J00982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J00984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A02634; HSXL32.
DR PDB; 1AOI; X-ray; 2.80 A; A/E=21-136.
DR PDB; 1M18; X-ray; 2.45 A; A/E=2-136.
DR PDB; 1M19; X-ray; 2.30 A; A/E=2-136.
DR PDB; 1M1A; X-ray; 2.65 A; A/E=2-136.
DR PDB; 6FQ8; EM; 4.80 A; A/E=38-135.
DR PDB; 6FTX; EM; 4.50 A; E=30-136.
DR PDB; 6NZO; EM; 3.80 A; A/E=1-136.
DR PDB; 6PX1; EM; 3.30 A; A/E=1-136.
DR PDB; 6PX3; EM; 4.10 A; A/E=1-136.
DR PDBsum; 1AOI; -.
DR PDBsum; 1M18; -.
DR PDBsum; 1M19; -.
DR PDBsum; 1M1A; -.
DR PDBsum; 6FQ8; -.
DR PDBsum; 6FTX; -.
DR PDBsum; 6NZO; -.
DR PDBsum; 6PX1; -.
DR PDBsum; 6PX3; -.
DR AlphaFoldDB; P02302; -.
DR SMR; P02302; -.
DR DIP; DIP-39145N; -.
DR IntAct; P02302; 1.
DR EvolutionaryTrace; P02302; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Chromosome; 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_0000221266"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Asymmetric dimethylarginine; by PRMT6"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 4
FT /note="Phosphothreonine; by HASPIN"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
FT MOD_RES 10
FT /note="N6-(2-hydroxyisobutyryl)lysine; 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-methylated lysine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
FT MOD_RES 12
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 15
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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 18
FT /note="Asymmetric dimethylarginine"
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-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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 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:P84243"
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-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
FT MOD_RES 37
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 42
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-(2-hydroxyisobutyryl)lysine; 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-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 65
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 65
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 80
FT /note="N6-(2-hydroxyisobutyryl)lysine; 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-methylated lysine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 116
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P84243"
FT MOD_RES 123
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 123
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 123
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1AOI"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:1M19"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:1M19"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1M1A"
FT HELIX 87..114
FT /evidence="ECO:0007829|PDB:1M19"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1M19"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:1M19"
SQ SEQUENCE 136 AA; 15487 MW; FE1B7E45DBBC7D95 CRC64;
MARTKQTARK STGGKAPRKQ LVTKAAKKCA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQRSAV MALQEASEAY LVALFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
