LOCUS       NM_003511                482 bp    mRNA    linear   PRI 03-MAY-2024
DEFINITION  Homo sapiens H2A clustered histone 16 (H2AC16), mRNA.
ACCESSION   NM_003511
VERSION     NM_003511.3
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  (bases 1 to 482)
  AUTHORS   Seal,R.L., Denny,P., Bruford,E.A., Gribkova,A.K., Landsman,D.,
            Marzluff,W.F., McAndrews,M., Panchenko,A.R., Shaytan,A.K. and
            Talbert,P.B.
  TITLE     A standardized nomenclature for mammalian histone genes
  JOURNAL   Epigenetics Chromatin 15 (1), 34 (2022)
   PUBMED   36180920
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (bases 1 to 482)
  AUTHORS   Budziszewski,G.R., Zhao,Y., Spangler,C.J., Kedziora,K.M.,
            Williams,M.R., Azzam,D.N., Skrajna,A., Koyama,Y., Cesmat,A.P.,
            Simmons,H.C., Arteaga,E.C., Strauss,J.D., Kireev,D. and
            McGinty,R.K.
  TITLE     Multivalent DNA and nucleosome acidic patch interactions specify
            VRK1 mitotic localization and activity
  JOURNAL   Nucleic Acids Res 50 (8), 4355-4371 (2022)
   PUBMED   35390161
REFERENCE   3  (bases 1 to 482)
  AUTHORS   Lubula,M.Y., Eckenroth,B.E., Carlson,S., Poplawski,A., Chruszcz,M.
            and Glass,K.C.
  TITLE     Structural insights into recognition of acetylated histone ligands
            by the BRPF1 bromodomain
  JOURNAL   FEBS Lett 588 (21), 3844-3854 (2014)
   PUBMED   25281266
REFERENCE   4  (bases 1 to 482)
  AUTHORS   Kim,W., Chakraborty,G., Kim,S., Shin,J., Park,C.H., Jeong,M.W.,
            Bharatham,N., Yoon,H.S. and Kim,K.T.
  TITLE     Macro histone H2A1.2 (macroH2A1) protein suppresses mitotic kinase
            VRK1 during interphase
  JOURNAL   J Biol Chem 287 (8), 5278-5289 (2012)
   PUBMED   22194607
REFERENCE   5  (bases 1 to 482)
  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   6  (bases 1 to 482)
  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
REFERENCE   7  (bases 1 to 482)
  AUTHORS   El Kharroubi,A., Piras,G., Zensen,R. and Martin,M.A.
  TITLE     Transcriptional activation of the integrated chromatin-associated
            human immunodeficiency virus type 1 promoter
  JOURNAL   Mol Cell Biol 18 (5), 2535-2544 (1998)
   PUBMED   9566873
REFERENCE   8  (bases 1 to 482)
  AUTHORS   Albig,W. and Doenecke,D.
  TITLE     The human histone gene cluster at the D6S105 locus
  JOURNAL   Hum Genet 101 (3), 284-294 (1997)
   PUBMED   9439656
REFERENCE   9  (bases 1 to 482)
  AUTHORS   Albig,W., Meergans,T. and Doenecke,D.
  TITLE     Characterization of the H1.5 gene completes the set of human H1
            subtype genes
  JOURNAL   Gene 184 (2), 141-148 (1997)
   PUBMED   9031620
REFERENCE   10 (bases 1 to 482)
  AUTHORS   Du Clos,T.W., Zlock,L.T. and Marnell,L.
  TITLE     Definition of a C-reactive protein binding determinant on histones
  JOURNAL   J Biol Chem 266 (4), 2167-2171 (1991)
   PUBMED   1989977
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z98744.2.
            
            On Dec 3, 2019 this sequence version replaced NM_003511.2.
            
            Summary: Histones are basic nuclear proteins that are responsible
            for the nucleosome structure of the chromosomal fiber in
            eukaryotes. Two molecules of each of the four core histones (H2A,
            H2B, H3, and H4) form an octamer, around which approximately 146 bp
            of DNA is wrapped in repeating units, called nucleosomes. The
            linker histone, H1, interacts with linker DNA between nucleosomes
            and functions in the compaction of chromatin into higher order
            structures. This gene is intronless and encodes a
            replication-dependent histone that is a member of the histone H2A
            family. Transcripts from this gene lack polyA tails but instead
            contain a palindromic termination element. This gene is found in
            the small histone gene cluster on chromosome 6p22-p21.3. [provided
            by RefSeq, Aug 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC112072.1, SRR1163655.168107.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match            :: ENST00000613174.2/
                                             ENSP00000482538.2
            RefSeq Select criteria        :: based on single protein-coding
                                             transcript
            replication-dependent histone :: PMID: 12408966
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-482               Z98744.2           29058-29539
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     gene            1..482
                     /gene="H2AC16"
                     /gene_synonym="dJ193B12.9; H2A.i; H2A/i; H2AC11; H2AC13;
                     H2AC15; H2AC17; H2AFI; HIST1H2AL"
                     /note="H2A clustered histone 16"
                     /db_xref="GeneID:8332"
                     /db_xref="HGNC:HGNC:4730"
                     /db_xref="MIM:602793"
     exon            1..482
                     /gene="H2AC16"
                     /gene_synonym="dJ193B12.9; H2A.i; H2A/i; H2AC11; H2AC13;
                     H2AC15; H2AC17; H2AFI; HIST1H2AL"
                     /inference="alignment:Splign:2.1.0"
     CDS             39..431
                     /gene="H2AC16"
                     /gene_synonym="dJ193B12.9; H2A.i; H2A/i; H2AC11; H2AC13;
                     H2AC15; H2AC17; H2AFI; HIST1H2AL"
                     /note="H2A histone family, member I; histone 1, H2al;
                     histone cluster 1, H2al; H2A.1; histone H2A/ptl; histone
                     cluster 1 H2A family member l"
                     /codon_start=1
                     /product="histone H2A type 1"
                     /protein_id="NP_003502.1"
                     /db_xref="CCDS:CCDS4634.1"
                     /db_xref="GeneID:8332"
                     /db_xref="HGNC:HGNC:4730"
                     /db_xref="MIM:602793"
                     /translation="MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERV
                     GAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVT
                     IAQGGVLPNIQAVLLPKKTESHHKAKGK"
     regulatory      454..459
                     /regulatory_class="polyA_signal_sequence"
                     /gene="H2AC16"
                     /gene_synonym="dJ193B12.9; H2A.i; H2A/i; H2AC11; H2AC13;
                     H2AC15; H2AC17; H2AFI; HIST1H2AL"
                     /note="hexamer: AATACA"
     polyA_site      482
                     /gene="H2AC16"
                     /gene_synonym="dJ193B12.9; H2A.i; H2A/i; H2AC11; H2AC13;
                     H2AC15; H2AC17; H2AFI; HIST1H2AL"
                     /note="major polyA site"
ORIGIN      
        1 cggctgttct cagttcctcc atttatcgtt tcttcgtcat gtcgggacgc ggcaagcagg
       61 gaggcaaagc tcgcgccaaa gccaagaccc gctcttctcg tgccggtctc cagttccccg
      121 tgggccgagt gcaccgactg ctccgcaagg gcaactatgc tgagcgggtc ggggccggcg
      181 cgccggtgta cctggcggcg gtgctggagt acctgactgc cgagatcctg gagctggcgg
      241 gcaacgccgc ccgcgacaac aagaagaccc gcattatccc gcgccacttg cagctggcca
      301 tccgcaacga cgaggagctc aacaagctgc tgggcaaagt aaccatcgct cagggtggtg
      361 tcctgcccaa catccaggct gtgctactgc ccaagaagac cgagagtcac cacaaggcca
      421 aaggcaaata atgtctccat agaatcactt tccaatacaa cggctctttt cagagccacc
      481 ta
//
