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 05-OCT-2010, entry version 50. DE RecName: Full=Putative histone H2B type 2-D; GN Name=HIST2H2BD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=22296985; PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3; 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., RA Stein G.S.; RT "Functional characterization of a human histone gene cluster RT 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 RT sterile 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-16; LYS-17; LYS-21 RP AND LYS-24, AND MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026; RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; RT "Substrate and functional diversity of lysine acetylation revealed by RT a proteomics survey."; RL Mol. Cell 23:607-618(2006). CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and CC compact DNA into chromatin, limiting DNA accessibility to the CC cellular machineries which require DNA as a template. Histones CC thereby play a central role in transcription regulation, DNA CC repair, DNA replication and chromosomal stability. DNA CC accessibility is regulated via a complex set of post-translational CC modifications of histones, also called histone code, and CC nucleosome remodeling. CC -!- SUBUNIT: The nucleosome is a histone octamer containing two CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps CC approximately 147 bp of DNA. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- PTM: Phosphorylated on Ser-15 by STK4/MST1 during apoptosis; which CC facilitates apoptotic chromatin condensation. Also phosphorylated CC on Ser-15 in response to DNA double strand breaks (DSBs), and in CC correlation with somatic hypermutation and immunoglobulin class- CC switch recombination. CC -!- MISCELLANEOUS: The mouse orthologous protein seems not to exist. CC -!- SIMILARITY: Belongs to the histone H2B family. CC -!- CAUTION: Could be the product of a pseudogene. In contrast to CC other H2B histones, it does not contain the conserved residue in CC C-terminus that is the target of monoubiquitination. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY131978; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY648853; AAT68256.1; -; Genomic_DNA. DR IPI; IPI00746251; -. DR UniGene; Hs.666643; -. DR ProteinModelPortal; Q6DRA6; -. DR SMR; Q6DRA6; 5-93. DR PRIDE; Q6DRA6; -. DR GeneCards; GC01P149814; -. DR H-InvDB; HIX0029389; -. DR HGNC; HGNC:20517; HIST2H2BD. DR PharmGKB; PA134910805; -. DR HOVERGEN; HBG081588; -. DR PhylomeDB; Q6DRA6; -. DR Genevestigator; Q6DRA6; -. 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:0006334; P:nucleosome assembly; IEA:InterPro. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000558; Histone_H2B. DR Gene3D; G3DSA:1.10.20.10; Histone-fold; 1. DR PANTHER; PTHR23428; Histone_H2B; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR SMART; SM00427; H2B; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00357; HISTONE_H2B; FALSE_NEG. PE 5: Uncertain; KW Acetylation; Chromosome; Complete proteome; DNA-binding; Methylation; KW Nucleosome core; Nucleus; Phosphoprotein. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 164 Putative histone H2B type 2-D. FT /FTId=PRO_0000244825. FT MOD_RES 6 6 N6-acetyllysine. FT MOD_RES 12 12 N6-acetyllysine (By similarity). FT MOD_RES 13 13 N6-acetyllysine. FT MOD_RES 15 15 Phosphoserine; by STK4. FT MOD_RES 16 16 N6-acetyllysine. FT MOD_RES 17 17 N6-acetyllysine. FT MOD_RES 21 21 N6-acetyllysine. FT MOD_RES 24 24 N6-acetyllysine. FT MOD_RES 47 47 N6-methylated lysine (By similarity). FT MOD_RES 58 58 N6-methylated lysine (By similarity). 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 //