LOCUS       NM_021052                517 bp    mRNA    linear   PRI 13-FEB-2025
DEFINITION  Homo sapiens H2A clustered histone 8 (H2AC8), mRNA.
ACCESSION   NM_021052
VERSION     NM_021052.4
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 517)
  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 517)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (bases 1 to 517)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (bases 1 to 517)
  AUTHORS   Kujirai,T. and Kurumizaka,H.
  TITLE     Transcription through the nucleosome
  JOURNAL   Curr Opin Struct Biol 61, 42-49 (2020)
   PUBMED   31790919
  REMARK    Review article
REFERENCE   5  (bases 1 to 517)
  AUTHORS   Matsumoto,S., Cavadini,S., Bunker,R.D., Grand,R.S., Potenza,A.,
            Rabl,J., Yamamoto,J., Schenk,A.D., Schubeler,D., Iwai,S.,
            Sugasawa,K., Kurumizaka,H. and Thoma,N.H.
  TITLE     DNA damage detection in nucleosomes involves DNA register shifting
  JOURNAL   Nature 571 (7763), 79-84 (2019)
   PUBMED   31142837
  REMARK    Erratum:[Nature. 2019 Jul;571(7764):E6. doi:
            10.1038/s41586-019-1343-8.. PMID: 31239520]
REFERENCE   6  (bases 1 to 517)
  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 517)
  AUTHORS   Rodriguez,P., Munroe,D., Prawitt,D., Chu,L.L., Bric,E., Kim,J.,
            Reid,L.H., Davies,C., Nakagama,H., Loebbert,R., Winterpacht,A.,
            Petruzzi,M.J., Higgins,M.J., Nowak,N., Evans,G., Shows,T.,
            Weissman,B.E., Zabel,B., Housman,D.E. and Pelletier,J.
  TITLE     Functional characterization of human nucleosome assembly protein-2
            (NAP1L4) suggests a role as a histone chaperone
  JOURNAL   Genomics 44 (3), 253-265 (1997)
   PUBMED   9325046
REFERENCE   8  (bases 1 to 517)
  AUTHORS   Albig,W., Kioschis,P., Poustka,A., Meergans,K. and Doenecke,D.
  TITLE     Human histone gene organization: nonregular arrangement within a
            large cluster
  JOURNAL   Genomics 40 (2), 314-322 (1997)
   PUBMED   9119399
REFERENCE   9  (bases 1 to 517)
  AUTHORS   Albig,W., Kardalinou,E., Drabent,B., Zimmer,A. and Doenecke,D.
  TITLE     Isolation and characterization of two human H1 histone genes within
            clusters of core histone genes
  JOURNAL   Genomics 10 (4), 940-948 (1991)
   PUBMED   1916825
REFERENCE   10 (bases 1 to 517)
  AUTHORS   Zhong,R., Roeder,R.G. and Heintz,N.
  TITLE     The primary structure and expression of four cloned human histone
            genes
  JOURNAL   Nucleic Acids Res 11 (21), 7409-7425 (1983)
   PUBMED   6647026
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031777.5.
            
            On Jul 7, 2021 this sequence version replaced NM_021052.3.
            
            Summary: Histones are basic nuclear proteins that are responsible
            for the nucleosome structure of the chromosomal fiber in
            eukaryotes. Nucleosomes consist of approximately 146 bp of DNA
            wrapped around a histone 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 is intronless and encodes a
            replication-dependent histone that is a member of the histone H2A
            family. Transcripts from this gene lack polyA tails; instead, they
            contain a palindromic termination element. This gene is found in
            the large 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 :: BP330063.1, DA679005.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match            :: ENST00000303910.5/
                                             ENSP00000303373.2
            RefSeq Select criteria        :: based on single protein-coding
                                             transcript
            replication-dependent histone :: PMID: 12408966
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-517               AL031777.5         22303-22819
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.2"
     gene            1..517
                     /gene="H2AC8"
                     /gene_synonym="H2A.1; H2A.2; H2A/a; H2AC4; H2AFA;
                     HIST1H2AE"
                     /note="H2A clustered histone 8"
                     /db_xref="GeneID:3012"
                     /db_xref="HGNC:HGNC:4724"
                     /db_xref="MIM:602786"
     exon            1..517
                     /gene="H2AC8"
                     /gene_synonym="H2A.1; H2A.2; H2A/a; H2AC4; H2AFA;
                     HIST1H2AE"
                     /inference="alignment:Splign:2.1.0"
     CDS             55..447
                     /gene="H2AC8"
                     /gene_synonym="H2A.1; H2A.2; H2A/a; H2AC4; H2AFA;
                     HIST1H2AE"
                     /note="histone H2AE; H2A histone family, member A; histone
                     1, H2ae; histone cluster 1, H2ae; histone H2A/a; histone
                     cluster 1 H2A family member e"
                     /codon_start=1
                     /product="histone H2A type 1-B/E"
                     /protein_id="NP_066390.1"
                     /db_xref="CCDS:CCDS4595.1"
                     /db_xref="GeneID:3012"
                     /db_xref="HGNC:HGNC:4724"
                     /db_xref="MIM:602786"
                     /translation="MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERV
                     GAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVT
                     IAQGGVLPNIQAVLLPKKTESHHKAKGK"
ORIGIN      
        1 attctttttc tttattcagt ggattgttag ttcttctgct gttaggaagc cactatgtct
       61 ggacgtggaa agcaaggcgg caaagctcgg gcaaaagcta aaacgcgttc ttccagggcc
      121 ggtcttcagt ttccagttgg ccgtgtgcac cgcctcctcc gcaaaggcaa ctactccgaa
      181 cgagtcgggg ccggcgctcc agtgtacctg gcagcggtgc tggaatatct gacggccgag
      241 atcttagagc tagctggcaa cgcggctcgc gacaataaga agacccgcat catcccgcgc
      301 cacctgcagc tagccatccg caacgacgag gagctaaata agcttctagg tcgcgtgacc
      361 atcgcgcagg gcggtgtcct gcccaacatc caggccgtat tgctgcctaa gaagacggag
      421 agccaccata aggccaaggg caagtgaaat gattactagt caaatccgtc agtgatcccg
      481 agtcccagaa accaaaggct cttttcagag ccaccca
//
