LOCUS       NP_001019770             126 aa            linear   PRI 07-APR-2024
DEFINITION  histone H2B type 2-F isoform a [Homo sapiens].
ACCESSION   NP_001019770 XP_496411
VERSION     NP_001019770.1
DBSOURCE    REFSEQ: accession NM_001024599.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Kim,S.C., Sprung,R., Chen,Y., Xu,Y., Ball,H., Pei,J., Cheng,T.,
            Kho,Y., Xiao,H., Xiao,L., Grishin,N.V., White,M., Yang,X.J. and
            Zhao,Y.
  TITLE     Substrate and functional diversity of lysine acetylation revealed
            by a proteomics survey
  JOURNAL   Mol Cell 23 (4), 607-618 (2006)
   PUBMED   16916647
REFERENCE   5  (residues 1 to 126)
  AUTHORS   Pavri,R., Zhu,B., Li,G., Trojer,P., Mandal,S., Shilatifard,A. and
            Reinberg,D.
  TITLE     Histone H2B monoubiquitination functions cooperatively with FACT to
            regulate elongation by RNA polymerase II
  JOURNAL   Cell 125 (4), 703-717 (2006)
   PUBMED   16713563
REFERENCE   6  (residues 1 to 126)
  AUTHORS   Bonenfant,D., Coulot,M., Towbin,H., Schindler,P. and van Oostrum,J.
  TITLE     Characterization of histone H2A and H2B variants and their
            post-translational modifications by mass spectrometry
  JOURNAL   Mol Cell Proteomics 5 (3), 541-552 (2006)
   PUBMED   16319397
REFERENCE   7  (residues 1 to 126)
  AUTHORS   Zhu,B., Zheng,Y., Pham,A.D., Mandal,S.S., Erdjument-Bromage,H.,
            Tempst,P. and Reinberg,D.
  TITLE     Monoubiquitination of human histone H2B: the factors involved and
            their roles in HOX gene regulation
  JOURNAL   Mol Cell 20 (4), 601-611 (2005)
   PUBMED   16307923
REFERENCE   8  (residues 1 to 126)
  AUTHORS   Golebiowski,F. and Kasprzak,K.S.
  TITLE     Inhibition of core histones acetylation by carcinogenic nickel(II)
  JOURNAL   Mol Cell Biochem 279 (1-2), 133-139 (2005)
   PUBMED   16283522
REFERENCE   9  (residues 1 to 126)
  AUTHORS   Cheung,W.L., Ajiro,K., Samejima,K., Kloc,M., Cheung,P.,
            Mizzen,C.A., Beeser,A., Etkin,L.D., Chernoff,J., Earnshaw,W.C. and
            Allis,C.D.
  TITLE     Apoptotic phosphorylation of histone H2B is mediated by mammalian
            sterile twenty kinase
  JOURNAL   Cell 113 (4), 507-517 (2003)
   PUBMED   12757711
REFERENCE   10 (residues 1 to 126)
  AUTHORS   Marzluff,W.F., Gongidi,P., Woods,K.R., Jin,J. and Maltais,L.J.
  TITLE     The human and mouse replication-dependent histone genes
  JOURNAL   Genomics 80 (5), 487-498 (2002)
   PUBMED   12408966
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC239868.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 4, 2005 this sequence version replaced XP_496411.1.
            
            Summary: Histones are basic nuclear proteins that are responsible
            for the nucleosome structure of the chromosomal fiber in
            eukaryotes. This structure consists of approximately 146 bp of DNA
            wrapped around a nucleosome, an octamer composed of pairs of each
            of the four core histones (H2A, H2B, H3, and H4). The chromatin
            fiber is further compacted through the interaction of a linker
            histone, H1, with the DNA between the nucleosomes to form higher
            order chromatin structures. This gene encodes a
            replication-dependent histone that is a member of the histone H2B
            family and is found in a histone cluster on chromosome 1. [provided
            by RefSeq, Aug 2015].
            
            Transcript Variant: This variant (1) differs in the 3' coding
            region and 3' UTR, compared to variant 2. The encoded isoform (a)
            has a shorter C-terminus compared to isoform b.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK289664.1, DB229053.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match            :: ENST00000369167.3/
                                             ENSP00000358164.1
            RefSeq Select criteria        :: based on manual assertion,
                                             conservation
            replication-dependent histone :: PMID: 12408966
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..126
                     /product="histone H2B type 2-F isoform a"
                     /note="histone H2B type 2-F; histone cluster 2, H2bf;
                     histone cluster 2 H2B family member f"
                     /calculated_mol_wt=13789
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylproline.
                     /evidence=ECO:0000250|UniProtKB:P23527; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16283522; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            12
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            13
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16283522; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by STK4/MST1.
                     /evidence=ECO:0000269|PubMed:12757711; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            16
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16283522,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            17
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16283522,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            24
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P33778; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Region          30..123
                     /region_name="HFD_H2B"
                     /note="histone-fold domain found in histone H2B and
                     similar proteins; cd22910"
                     /db_xref="CDD:467035"
     Site            order(31,33,36,38,40..42,44..46,49..56,58..59,62..63,
                     66..67,69..71,73..75,79,89..90,92,95..96,99,102..104,107,
                     110..112,114..115,118..119,122..123)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            order(31..37,40..41,43,54..56,89)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:467035"
     Site            order(35,39..41,43..44,47..49,54..56,60,96,100,109..110,
                     112..113,116..117,119..120,123)
                     /site_type="other"
                     /note="Hif1 binding site [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:Q64475; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            47
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            58
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            order(62,65..66,68..69,72,77,80,83..85,93..94,97,101..102)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            80
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            86
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            86
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            87
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            93
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            109
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            113
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q00729; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     Site            117
                     /site_type="methylation"
                     /note="N6-methylated lysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00729; propagated from
                     UniProtKB/Swiss-Prot (Q5QNW6.3)"
     CDS             1..126
                     /gene="H2BC18"
                     /gene_synonym="HIST2H2BF"
                     /coded_by="NM_001024599.5:48..428"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30846.1"
                     /db_xref="GeneID:440689"
                     /db_xref="HGNC:HGNC:24700"
ORIGIN      
        1 mpdpaksapa pkkgskkavt kvqkkdgkkr krsrkesysv yvykvlkqvh pdtgisskam
       61 gimnsfvndi feriageasr lahynkrsti tsreiqtavr lllpgelakh avsegtkavt
      121 kytssk
//
