H2B2D_HUMAN
ID H2B2D_HUMAN Reviewed; 164 AA.
AC Q6DRA6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Putative histone H2B type 2-D;
DE AltName: Full=H2B-clustered histone 19 pseudogene {ECO:0000312|HGNC:HGNC:20517};
GN Name=H2BC19P {ECO:0000312|HGNC:HGNC:20517};
GN Synonyms=HIST2H2BD {ECO:0000312|HGNC:HGNC:20517};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12408966; DOI=10.1006/geno.2002.6850;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15527963; DOI=10.1016/j.gene.2004.07.036;
RA Braastad C.D., Hovhannisyan H., van Wijnen A.J., Stein J.L., Stein G.S.;
RT "Functional characterization of a human histone gene cluster duplication.";
RL Gene 342:35-40(2004).
RN [3]
RP PHOSPHORYLATION AT SER-15.
RX PubMed=12757711; DOI=10.1016/s0092-8674(03)00355-6;
RA Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A.,
RA Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.;
RT "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile
RT twenty kinase.";
RL Cell 113:507-517(2003).
RN [4]
RP ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
RX PubMed=16283522; DOI=10.1007/s11010-005-8285-1;
RA Golebiowski F., Kasprzak K.S.;
RT "Inhibition of core histones acetylation by carcinogenic nickel(II).";
RL Mol. Cell. Biochem. 279:133-139(2005).
RN [5]
RP CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND
RP LYS-35.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J.,
RA Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation as a
RT new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [6]
RP SUCCINYLATION AT LYS-35.
RX PubMed=22389435; DOI=10.1074/mcp.m111.015875;
RA Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT "Lysine succinylation and lysine malonylation in histones.";
RL Mol. Cell. Proteomics 11:100-107(2012).
RN [7]
RP HYDROXYBUTYRYLATION AT LYS-6; LYS-13; LYS-21; LYS-24; LYS-25; LYS-35;
RP LYS-44; LYS-47; LYS-58 AND LYS-86.
RX PubMed=24681537; DOI=10.1038/nchembio.1497;
RA Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., Debernardi A.,
RA Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., Allis C.D., Ren B.,
RA Khochbin S., Zhao Y.;
RT "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone
RT mark.";
RL Nat. Chem. Biol. 10:365-370(2014).
RN [8]
RP BUTYRYLATION AT LYS-6 AND LYS-21.
RX PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
RA Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
RA Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
RA Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C., Panne D.,
RA Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
RT "Dynamic competing histone H4 K5K8 acetylation and butyrylation are
RT hallmarks of highly active gene promoters.";
RL Mol. Cell 62:169-180(2016).
RN [9]
RP HYDROXYBUTYRYLATION AT LYS-6; LYS-12; LYS-17; LYS-21; LYS-35 AND LYS-86.
RX PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
RA Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
RA Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
RA Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
RA White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lysine beta-
RT hydroxybutyrylation.";
RL Mol. Cell 62:194-206(2016).
RN [10]
RP GLUTARYLATION AT LYS-17; LYS-35; LYS-44 AND LYS-47.
RX PubMed=31542297; DOI=10.1016/j.molcel.2019.08.018;
RA Bao X., Liu Z., Zhang W., Gladysz K., Fung Y.M.E., Tian G., Xiong Y.,
RA Wong J.W.H., Yuen K.W.Y., Li X.D.;
RT "Glutarylation of histone H4 lysine 91 regulates chromatin dynamics.";
RL Mol. Cell 0:0-0(2019).
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: Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress
CC promotes transcription (By similarity). Phosphorylated on Ser-15
CC (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic
CC chromatin condensation. Also phosphorylated on Ser-15 in response to
CC DNA double strand breaks (DSBs), and in correlation with somatic
CC hypermutation and immunoglobulin class-switch recombination.
CC {ECO:0000250|UniProtKB:Q64475, ECO:0000269|PubMed:12757711}.
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:0000269|PubMed:21925322}.
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:P33778}.
CC -!- MISCELLANEOUS: The mouse orthologous protein seems not to exist.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. In contrast to other H2B
CC histones, it does not contain the conserved residue in C-terminus that
CC is the target of monoubiquitination. {ECO:0000305}.
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DR EMBL; AY131978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY648853; AAT68256.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6DRA6; -.
DR SMR; Q6DRA6; -.
DR IntAct; Q6DRA6; 1.
DR iPTMnet; Q6DRA6; -.
DR PhosphoSitePlus; Q6DRA6; -.
DR SwissPalm; Q6DRA6; -.
DR BioMuta; HGNC:20517; -.
DR DMDM; 74709219; -.
DR EPD; Q6DRA6; -.
DR jPOST; Q6DRA6; -.
DR MassIVE; Q6DRA6; -.
DR MaxQB; Q6DRA6; -.
DR PRIDE; Q6DRA6; -.
DR ProteomicsDB; 66254; -.
DR GeneCards; H2BC19P; -.
DR HGNC; HGNC:20517; H2BC19P.
DR neXtProt; NX_Q6DRA6; -.
DR InParanoid; Q6DRA6; -.
DR PathwayCommons; Q6DRA6; -.
DR SignaLink; Q6DRA6; -.
DR Pharos; Q6DRA6; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q6DRA6; protein.
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; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; PTHR23428; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 5: Uncertain;
KW Acetylation; Chromosome; DNA-binding; Hydroxylation; Isopeptide bond;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23527"
FT CHAIN 2..164
FT /note="Putative histone H2B type 2-D"
FT /id="PRO_0000244825"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..33
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:P23527"
FT MOD_RES 6
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 6
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522"
FT MOD_RES 6
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 6
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 6
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 12
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 12
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 12
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 12
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 13
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 13
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522"
FT MOD_RES 13
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 15
FT /note="Phosphoserine; by STK4/MST1"
FT /evidence="ECO:0000269|PubMed:12757711"
FT MOD_RES 16
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522"
FT MOD_RES 16
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 16
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 17
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 17
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 17
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 17
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 21
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 21
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 21
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522"
FT MOD_RES 21
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 21
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 21
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 24
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 24
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 24
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 25
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 35
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 35
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 35
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 35
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 35
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 37
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q64475"
FT MOD_RES 44
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 44
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 44
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 47
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 47
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 47
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 58
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 58
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 80
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 86
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 86
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 86
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 86
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 86
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 87
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 93
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P58876"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5QNW6"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
SQ SEQUENCE 164 AA; 18018 MW; 1361A7840661B6A7 CRC64;
MPEPAKFAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKRVH PDTGIWCKAM
GIMNSFLNDI FERIAGEASR LAHYNKRSTI TSRRSRRPCA CCCPASWPST PCPRAPRRSP
STPAPSESLP GPGARSLPPS LPPRVAGCFV SKGSFQGHLT PLVK
