LOCUS       NM_001372105             468 bp    mRNA    linear   PRI 07-APR-2024
DEFINITION  Homo sapiens H3.7 histone (putative) (H3-7), transcript variant 1,
            mRNA.
ACCESSION   NM_001372105
VERSION     NM_001372105.2
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 468)
  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 468)
  AUTHORS   Taguchi,H., Xie,Y., Horikoshi,N., Maehara,K., Harada,A., Nogami,J.,
            Sato,K., Arimura,Y., Osakabe,A., Kujirai,T., Iwasaki,T., Semba,Y.,
            Tachibana,T., Kimura,H., Ohkawa,Y. and Kurumizaka,H.
  TITLE     Crystal Structure and Characterization of Novel Human Histone H3
            Variants, H3.6, H3.7, and H3.8
  JOURNAL   Biochemistry 56 (16), 2184-2196 (2017)
   PUBMED   28374988
REFERENCE   3  (bases 1 to 468)
  AUTHORS   Ederveen,T.H., Mandemaker,I.K. and Logie,C.
  TITLE     The human histone H3 complement anno 2011
  JOURNAL   Biochim Biophys Acta 1809 (10), 577-586 (2011)
   PUBMED   21782046
  REMARK    Review article
REFERENCE   4  (bases 1 to 468)
  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   5  (bases 1 to 468)
  AUTHORS   Garcia,B.A., Hake,S.B., Diaz,R.L., Kauer,M., Morris,S.A., Recht,J.,
            Shabanowitz,J., Mishra,N., Strahl,B.D., Allis,C.D. and Hunt,D.F.
  TITLE     Organismal differences in post-translational modifications in
            histones H3 and H4
  JOURNAL   J Biol Chem 282 (10), 7641-7655 (2007)
   PUBMED   17194708
REFERENCE   6  (bases 1 to 468)
  AUTHORS   Morris,S.A., Rao,B., Garcia,B.A., Hake,S.B., Diaz,R.L.,
            Shabanowitz,J., Hunt,D.F., Allis,C.D., Lieb,J.D. and Strahl,B.D.
  TITLE     Identification of histone H3 lysine 36 acetylation as a highly
            conserved histone modification
  JOURNAL   J Biol Chem 282 (10), 7632-7640 (2007)
   PUBMED   17189264
REFERENCE   7  (bases 1 to 468)
  AUTHORS   Goto,H., Yasui,Y., Nigg,E.A. and Inagaki,M.
  TITLE     Aurora-B phosphorylates Histone H3 at serine28 with regard to the
            mitotic chromosome condensation
  JOURNAL   Genes Cells 7 (1), 11-17 (2002)
   PUBMED   11856369
REFERENCE   8  (bases 1 to 468)
  AUTHORS   Lachner,M., O'Carroll,D., Rea,S., Mechtler,K. and Jenuwein,T.
  TITLE     Methylation of histone H3 lysine 9 creates a binding site for HP1
            proteins
  JOURNAL   Nature 410 (6824), 116-120 (2001)
   PUBMED   11242053
REFERENCE   9  (bases 1 to 468)
  AUTHORS   Goto,H., Tomono,Y., Ajiro,K., Kosako,H., Fujita,M., Sakurai,M.,
            Okawa,K., Iwamatsu,A., Okigaki,T., Takahashi,T. and Inagaki,M.
  TITLE     Identification of a novel phosphorylation site on histone H3
            coupled with mitotic chromosome condensation
  JOURNAL   J Biol Chem 274 (36), 25543-25549 (1999)
   PUBMED   10464286
REFERENCE   10 (bases 1 to 468)
  AUTHORS   Ohe,Y. and Iwai,K.
  TITLE     Human spleen histone H3. Isolation and amino acid sequence
  JOURNAL   J Biochem 90 (4), 1205-1211 (1981)
   PUBMED   7309716
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC239798.3.
            
            On Nov 3, 2020 this sequence version replaced NM_001372105.1.
            
            Summary: Histones are basic nuclear proteins responsible for
            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 a member of the H3 family, but is found outside of the histone
            cluster. There is evidence that it is transcribed and has an intact
            CDS, but residue changes in the protein suggest that it may be on
            its way to becoming a psuedogene. [provided by RefSeq, Aug 2019].
            
            Transcript Variant: This variant (1) represents an intronless
            transcript. Variants 1 and 2 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            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.
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392948.5/ ENSP00000476960.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-468               AC239798.3         12992-13459
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.1"
     gene            1..468
                     /gene="H3-7"
                     /gene_synonym="H3-2; H3.7; HIST2H3PS2; p06"
                     /note="H3.7 histone (putative)"
                     /db_xref="GeneID:440686"
                     /db_xref="HGNC:HGNC:32060"
     exon            1..468
                     /gene="H3-7"
                     /gene_synonym="H3-2; H3.7; HIST2H3PS2; p06"
                     /inference="alignment:Splign:2.1.0"
     CDS             12..422
                     /gene="H3-7"
                     /gene_synonym="H3-2; H3.7; HIST2H3PS2; p06"
                     /note="histone 2, H3, pseudogene 2; histone cluster 2 H3
                     pseudogene 2; histone H3.2; histone HIST2H3PS2; H3.2
                     histone (putative)"
                     /codon_start=1
                     /product="histone H3-7"
                     /protein_id="NP_001359034.1"
                     /db_xref="CCDS:CCDS30842.1"
                     /db_xref="GeneID:440686"
                     /db_xref="HGNC:HGNC:32060"
                     /translation="MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRP
                     GTVALREIRRYQKSTELLIRKLPFQRLVREIAQEFKTDLRFQSSAVMALQEAREAYLV
                     GLFEDTNLCAIHAKRVTIMPKDIQLVSRIRGERA"
ORIGIN      
        1 aatgagacag catggcccgt actaagcaga ctgcccgcaa gtcgaccggc ggcaaggccc
       61 cgaggaagca gctggctacc aaagcggccc gcaagagcgc gccggccacg ggcggggtga
      121 agaagccgca ccgctaccgg cccggcaccg tggctctgcg ggagatccgg cgctatcaga
      181 agtctacgga gctgctgatc cgcaagctgc ccttccagcg gctggtacgc gagatcgcgc
      241 aggagtttaa gacggacctg cgcttccaga gctcggccgt gatggcgctg caggaggcca
      301 gagaggccta cctggtgggg ctgttcgaag acacgaacct gtgcgccatc catgccaagc
      361 gcgtgaccat catgcccaag gacatccagt tggtcagccg catccgcggg gagcgggcct
      421 aaggtatatt tttaagtggt cgatctaaag gctcttttca gagccact
//
