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Histone H3.2 (Histone H3 class I)

 H32_CHICK               Reviewed;         136 AA.
P84229; P02295; P02297; P16105; P17269; P17320;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 131.
RecName: Full=Histone H3.2;
AltName: Full=Histone H3 class I;
Name=H3-I;
and
Name=H3-II;
and
Name=H3-III;
and
Name=H3-IV;
and
Name=H3-V;
and
Name=H3-VI;
and
Name=H3-VII;
and
Name=H3-VIII;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=4000938; DOI=10.1093/nar/13.4.1369;
Wang S.W., Robins A.J., D'Andrea R., Wells J.R.E.;
"Inverted duplication of histone genes in chicken and disposition of
regulatory sequences.";
Nucleic Acids Res. 13:1369-1387(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7078654; DOI=10.1038/297434a0;
Engel J.D., Sugarman B.J., Dodgson J.B.;
"A chicken histone H3 gene contains intervening sequences.";
Nature 297:434-436(1982).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3-II AND H3-III).
PubMed=1874451; DOI=10.1016/0378-1119(91)90092-P;
Nakayama T.;
"Nucleotide sequences of two members of the chicken H3 histone-
encoding gene family.";
Gene 102:289-290(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3-IV AND H3-V).
STRAIN=White leghorn;
PubMed=1956792; DOI=10.1093/nar/19.22.6327;
Setoguchi Y., Nakayama T.;
"Nucleotide sequences of new members (H3-IV and H3-V) of the chicken
H3 histone-encoding gene family.";
Nucleic Acids Res. 19:6327-6327(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3-VI; H3-VII AND H3-VIII).
STRAIN=White leghorn; TISSUE=Liver;
PubMed=8804862; DOI=10.1093/dnares/3.2.95;
Takami Y., Higashio M., Fukuoka T., Takechi S., Nakayama T.;
"Organization of the chicken histone genes in a major gene cluster and
generation of an almost complete set of the core histone protein
sequences.";
DNA Res. 3:95-99(1996).
[6]
PROTEIN SEQUENCE OF 2-136.
PubMed=4859525; DOI=10.1111/j.1432-1033.1974.tb03635.x;
Brandt W.F., von Holt C.;
"The determination of the primary structure of histone F3 from chicken
erythrocytes by automatic Edman degradation. 2. Sequence analysis of
histone F3.";
Eur. J. Biochem. 46:419-429(1974).
[7]
METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-28; LYS-37 AND LYS-80,
ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=12123664; DOI=10.1006/abio.2002.5719;
Zhang K., Tang H., Huang L., Blankenship J.W., Jones P.R., Xiang F.,
Yau P.M., Burlingame A.L.;
"Identification of acetylation and methylation sites of histone H3
from chicken erythrocytes by high-accuracy matrix-assisted laser
desorption ionization-time-of-flight, matrix-assisted laser desorption
ionization-postsource decay, and nanoelectrospray ionization tandem
mass spectrometry.";
Anal. Biochem. 306:259-269(2002).
[8]
INTERACTION WITH HMGB1.
PubMed=19102706; DOI=10.1021/bi8013449;
Kawase T., Sato K., Ueda T., Yoshida M.;
"Distinct domains in HMGB1 are involved in specific intramolecular and
nucleosomal interactions.";
Biochemistry 47:13991-13996(2008).
[9]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
PubMed=1946434; DOI=10.1073/pnas.88.22.10148;
Arents G., Burlingame R.W., Wang B.-C., Love W.E., Moudrianakis E.N.;
"The nucleosomal core histone octamer at 3.1 A resolution: a
tripartite protein assembly and a left-handed superhelix.";
Proc. Natl. Acad. Sci. U.S.A. 88:10148-10152(1991).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH H2A; H2B AND H4.
PubMed=11092917; DOI=10.1107/S0907444900011847;
Harp J.M., Hanson B.L., Timm D.E., Bunick G.J.;
"Asymmetries in the nucleosome core particle at 2.5 A resolution.";
Acta Crystallogr. D 56:1513-1534(2000).
[11]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH H2A AND H2B.
PubMed=12876341; DOI=10.1107/S0907444903011880;
Chantalat L., Nicholson J.M., Lambert S.J., Reid A.J., Donovan M.J.,
Reynolds C.D., Wood C.M., Baldwin J.P.;
"Structure of the histone-core octamer in KCl/phosphate crystals at
2.15 A resolution.";
Acta Crystallogr. D 59:1395-1407(2003).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA. Interacts with HMGB1.
{ECO:0000269|PubMed:11092917, ECO:0000269|PubMed:12876341,
ECO:0000269|PubMed:19102706}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression
strongly decreases as cell division slows down during the process
of differentiation.
-!- PTM: Acetylation is generally linked to gene activation.
Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors
methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac)
by EP300/p300 plays a central role in chromatin structure:
localizes at the surface of the histone octamer and stimulates
transcription, possibly by promoting nucleosome instability (By
similarity). {ECO:0000250|UniProtKB:Q71DI3}.
-!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) is linked to
gene activation. Asymmetric dimethylation at Arg-3 (H3R2me2a) by
PRMT6 is linked to gene repression and is mutually exclusive with
H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at
the 3' of genes regardless of their transcription state and is
enriched on inactive promoters, while it is absent on active
promoters (By similarity). {ECO:0000250|UniProtKB:Q71DI3}.
-!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80
(H3K79me) are linked to gene activation. Methylation at Lys-5
(H3K4me) facilitates subsequent acetylation of H3 and H4.
Methylation at Lys-80 (H3K79me) is associated with DNA double-
strand break (DSB) responses and is a specific target for TP53BP1.
Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to
gene repression. Methylation at Lys-10 (H3K9me) is a specific
target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents
subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of
H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me)
require preliminary monoubiquitination of H2B at 'Lys-120' (By
similarity). {ECO:0000250|UniProtKB:Q71DI3}.
-!- PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase
and dephosphorylated during anaphase. Phosphorylation at Ser-11
(H3S10ph) by AURKB is crucial for chromosome condensation and
cell-cycle progression during mitosis and meiosis. In addition
phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is
important during interphase because it enables the transcription
of genes following external stimulation, like mitogens, stress,
growth factors or UV irradiation and result in the activation of
genes, such as c-fos and c-jun. Phosphorylation at Ser-11
(H3S10ph), which is linked to gene activation, prevents
methylation at Lys-10 (H3K9me) but facilitates acetylation of H3
and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the
dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from
heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
essential regulatory mechanism for neoplastic cell transformation.
Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5
or AURKB during mitosis or upon ultraviolet B irradiation.
Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for
epigenetic transcriptional activation that prevents demethylation
of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically
phosphorylated at Thr-12 (H3T11ph) from prophase to early
anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph)
by PKN1 is a specific tag for epigenetic transcriptional
activation that promotes demethylation of Lys-10 (H3K9me) by
KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes
exclusion of CBX5 (HP1 alpha) from chromatin (By similarity).
{ECO:0000250|UniProtKB:Q71DI3}.
-!- PTM: Monoubiquitinated by RAG1 in lymphoid cells,
monoubiquitination is required for V(D)J recombination.
{ECO:0000250|UniProtKB:Q71DI3}.
-!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine only
takes place on H3K4me3 and results in gene repression.
{ECO:0000250|UniProtKB:Q71DI3}.
-!- PTM: Butyrylation of histones marks active promoters and competes
with histone acetylation. It is present during late
spermatogenesis. {ECO:0000250|UniProtKB:P68433}.
-!- PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with
a maximum frequency around the transcription start sites of genes.
It gives a specific tag for epigenetic transcription activation.
{ECO:0000250|UniProtKB:Q71DI3}.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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EMBL; X02218; CAA26138.1; -; Genomic_DNA.
EMBL; J00869; AAA48795.1; ALT_SEQ; Genomic_DNA.
EMBL; M61154; AAA48796.1; -; Genomic_DNA.
EMBL; M61155; AAA48797.1; -; Genomic_DNA.
EMBL; X62291; CAA44180.1; -; Genomic_DNA.
EMBL; X62292; CAA44181.1; -; Genomic_DNA.
EMBL; U37577; AAC60003.1; -; Genomic_DNA.
EMBL; U37578; AAC60004.1; -; Genomic_DNA.
EMBL; U37579; AAC60005.1; -; Genomic_DNA.
PIR; S18716; HSCH3.
RefSeq; NP_001268409.1; NM_001281480.1.
RefSeq; NP_001268438.1; NM_001281509.2.
RefSeq; XP_001232833.1; XM_001232832.4.
RefSeq; XP_001233028.1; XM_001233027.4.
RefSeq; XP_015144912.1; XM_015289426.1.
RefSeq; XP_015144926.1; XM_015289440.1.
RefSeq; XP_416193.2; XM_416193.4.
UniGene; Gga.5274; -.
PDB; 1EQZ; X-ray; 2.50 A; C/G=1-136.
PDB; 1HIO; X-ray; 3.10 A; C=44-136.
PDB; 1HQ3; X-ray; 2.15 A; C/G=1-136.
PDB; 1TZY; X-ray; 1.90 A; C/G=1-136.
PDB; 2ARO; X-ray; 2.10 A; C/G=1-136.
PDB; 2HIO; X-ray; 3.10 A; C=1-136.
PDB; 3C9K; EM; 20.00 A; C/G=2-136.
PDBsum; 1EQZ; -.
PDBsum; 1HIO; -.
PDBsum; 1HQ3; -.
PDBsum; 1TZY; -.
PDBsum; 2ARO; -.
PDBsum; 2HIO; -.
PDBsum; 3C9K; -.
ProteinModelPortal; P84229; -.
SMR; P84229; -.
IntAct; P84229; 3.
STRING; 9031.ENSGALP00000037310; -.
iPTMnet; P84229; -.
PaxDb; P84229; -.
PRIDE; P84229; -.
Ensembl; ENSGALT00000042655; ENSGALP00000042290; ENSGALG00000027064.
Ensembl; ENSGALT00000052021; ENSGALP00000053244; ENSGALG00000040303.
Ensembl; ENSGALT00000052453; ENSGALP00000044176; ENSGALG00000040004.
Ensembl; ENSGALT00000054819; ENSGALP00000058017; ENSGALG00000030424.
Ensembl; ENSGALT00000056622; ENSGALP00000049375; ENSGALG00000035244.
Ensembl; ENSGALT00000058115; ENSGALP00000055093; ENSGALG00000038969.
Ensembl; ENSGALT00000058129; ENSGALP00000055994; ENSGALG00000037930.
Ensembl; ENSGALT00000064088; ENSGALP00000046484; ENSGALG00000043062.
GeneID; 100857439; -.
GeneID; 100858681; -.
GeneID; 417953; -.
GeneID; 768333; -.
GeneID; 769809; -.
GeneID; 769852; -.
GeneID; 770022; -.
KEGG; gga:100857439; -.
KEGG; gga:100858681; -.
KEGG; gga:417953; -.
KEGG; gga:768333; -.
KEGG; gga:769809; -.
KEGG; gga:769852; -.
KEGG; gga:770022; -.
CTD; 417953; -.
CTD; 653604; -.
CTD; 769852; -.
CTD; 8350; -.
CTD; 8355; -.
CTD; 8357; -.
eggNOG; KOG1745; Eukaryota.
eggNOG; COG2036; LUCA.
GeneTree; ENSGT00760000118967; -.
HOGENOM; HOG000155290; -.
HOVERGEN; HBG001172; -.
InParanoid; P84229; -.
KO; K11253; -.
OMA; ANLCTIH; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P84229; -.
TreeFam; TF314241; -.
Reactome; R-GGA-1266695; Interleukin-7 signaling.
Reactome; R-GGA-212300; PRC2 methylates histones and DNA.
Reactome; R-GGA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-GGA-3247509; Chromatin modifying enzymes.
Reactome; R-GGA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-GGA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-GGA-73728; RNA Polymerase I Promoter Opening.
Reactome; R-GGA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-GGA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-GGA-9018519; Estrogen-dependent gene expression.
Reactome; R-GGA-983231; Factors involved in megakaryocyte development and platelet production.
EvolutionaryTrace; P84229; -.
PRO; PR:P84229; -.
Proteomes; UP000000539; Chromosome 1.
Bgee; ENSGALG00000027064; Expressed in 10 organ(s), highest expression level in liver.
GO; GO:0000786; C:nucleosome; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00622; HISTONEH3.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00322; HISTONE_H3_1; 1.
PROSITE; PS00959; HISTONE_H3_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Chromosome;
Citrullination; Complete proteome; Direct protein sequencing;
DNA-binding; Hydroxylation; Methylation; Nucleosome core; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:4859525}.
CHAIN 2 136 Histone H3.2.
/FTId=PRO_0000221260.
SITE 37 38 Involved in HMGB1-binding.
MOD_RES 3 3 Asymmetric dimethylarginine; by PRMT6;
alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 3 3 Citrulline; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 4 4 Phosphothreonine; by HASPIN.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 5 5 Allysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 5 5 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 5 5 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 5 5 N6-methyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 7 7 Phosphothreonine; by PKC.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 9 9 Citrulline; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 9 9 Symmetric dimethylarginine; by PRMT5;
alternate. {ECO:0000250}.
MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 10 10 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 10 10 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 10 10 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 11 11 ADP-ribosylserine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 11 11 Phosphoserine; alternate; by AURKB,
AURKC, RPS6KA3, RPS6KA4 and RPS6KA5.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 12 12 Phosphothreonine; by PKC.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 15 15 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 15 15 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 15 15 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 18 18 Asymmetric dimethylarginine; by CARM1;
alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 18 18 Citrulline; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 19 19 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 19 19 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 19 19 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P68433}.
MOD_RES 19 19 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 19 19 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 24 24 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 24 24 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 24 24 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P68433}.
MOD_RES 24 24 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 24 24 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 27 27 Citrulline.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 28 28 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 28 28 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 28 28 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 28 28 N6-methyllysine; alternate.
{ECO:0000305|PubMed:12123664}.
MOD_RES 29 29 ADP-ribosylserine; alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 29 29 Phosphoserine; alternate; by AURKB, AURKC
and RPS6KA5.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 37 37 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 37 37 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 37 37 N6-methyllysine; alternate.
{ECO:0000305|PubMed:12123664}.
MOD_RES 38 38 N6-methyllysine.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 42 42 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 57 57 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 57 57 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 57 57 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 57 57 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 57 57 N6-methyllysine; by EHMT2; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 57 57 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P84228}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 65 65 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 65 65 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 80 80 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P84228}.
MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 80 80 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 80 80 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 80 80 N6-methyllysine; alternate.
{ECO:0000269|PubMed:12123664}.
MOD_RES 80 80 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P84228}.
MOD_RES 81 81 Phosphothreonine.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P84243}.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 116 116 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 123 123 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P68431}.
MOD_RES 123 123 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
MOD_RES 123 123 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:Q71DI3}.
STRAND 34 37 {ECO:0000244|PDB:1EQZ}.
HELIX 44 57 {ECO:0000244|PDB:1TZY}.
HELIX 65 79 {ECO:0000244|PDB:1TZY}.
STRAND 80 82 {ECO:0000244|PDB:1EQZ}.
HELIX 87 114 {ECO:0000244|PDB:1TZY}.
STRAND 118 120 {ECO:0000244|PDB:1TZY}.
HELIX 122 131 {ECO:0000244|PDB:1TZY}.
SEQUENCE 136 AA; 15388 MW; 6FD8508EA50A0EEC CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA


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