LOCUS       NM_001123375             469 bp    mRNA    linear   PRI 21-SEP-2024
DEFINITION  Homo sapiens H3 clustered histone 13 (H3C13), mRNA.
ACCESSION   NM_001123375 XM_497711
VERSION     NM_001123375.3
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 469)
  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 469)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (bases 1 to 469)
  AUTHORS   Hammond,C.M., Bao,H., Hendriks,I.A., Carraro,M., Garcia-Nieto,A.,
            Liu,Y., Reveron-Gomez,N., Spanos,C., Chen,L., Rappsilber,J.,
            Nielsen,M.L., Patel,D.J., Huang,H. and Groth,A.
  TITLE     DNAJC9 integrates heat shock molecular chaperones into the histone
            chaperone network
  JOURNAL   Mol Cell 81 (12), 2533-2548 (2021)
   PUBMED   33857403
REFERENCE   4  (bases 1 to 469)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (bases 1 to 469)
  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   6  (bases 1 to 469)
  AUTHORS   Ruthenburg,A.J., Li,H., Milne,T.A., Dewell,S., McGinty,R.K.,
            Yuen,M., Ueberheide,B., Dou,Y., Muir,T.W., Patel,D.J. and
            Allis,C.D.
  TITLE     Recognition of a mononucleosomal histone modification pattern by
            BPTF via multivalent interactions
  JOURNAL   Cell 145 (5), 692-706 (2011)
   PUBMED   21596426
REFERENCE   7  (bases 1 to 469)
  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   8  (bases 1 to 469)
  AUTHORS   Bruston,F., Delbarre,E., Ostlund,C., Worman,H.J., Buendia,B. and
            Duband-Goulet,I.
  TITLE     Loss of a DNA binding site within the tail of prelamin A
            contributes to altered heterochromatin anchorage by progerin
  JOURNAL   FEBS Lett 584 (14), 2999-3004 (2010)
   PUBMED   20580717
REFERENCE   9  (bases 1 to 469)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   10 (bases 1 to 469)
  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.
            
            On Dec 3, 2019 this sequence version replaced NM_001123375.2.
            
            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 H3
            family. [provided by RefSeq, Aug 2015].
            
            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            :: ENST00000331491.2/
                                             ENSP00000333277.2
            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
            1-469               AC239868.2         97795-98263         c
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     gene            1..469
                     /gene="H3C13"
                     /gene_synonym="H3C14; H3C15; HIST2H3D"
                     /note="H3 clustered histone 13"
                     /db_xref="GeneID:653604"
                     /db_xref="HGNC:HGNC:25311"
     exon            1..469
                     /gene="H3C13"
                     /gene_synonym="H3C14; H3C15; HIST2H3D"
                     /inference="alignment:Splign:2.1.0"
     CDS             13..423
                     /gene="H3C13"
                     /gene_synonym="H3C14; H3C15; HIST2H3D"
                     /note="histone 2, H3d; histone cluster 2, H3d; histone
                     cluster 2 H3 family member d; H3-clustered histone 14;
                     H3-clustered histone 15"
                     /codon_start=1
                     /product="histone H3.2"
                     /protein_id="NP_001116847.1"
                     /db_xref="CCDS:CCDS41388.1"
                     /db_xref="GeneID:653604"
                     /db_xref="HGNC:HGNC:25311"
                     /translation="MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRP
                     GTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLV
                     GLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA"
ORIGIN      
        1 caatgagaca gcatggcccg tactaagcag actgcccgca agtcgaccgg cggcaaggcc
       61 ccgaggaagc agctggctac caaagcggcc cgcaagagcg cgccggccac gggcggggtg
      121 aagaagccgc accgctaccg gcccggcacc gtggctctgc gggagatccg gcgctaccag
      181 aagtctacgg agctgctgat ccgcaagctg cccttccagc ggctggtacg cgagatcgcg
      241 caggacttta agacggacct gcgcttccag agctcggccg tgatggcgct gcaggaggcc
      301 agcgaggcct acctggtggg gctgttcgaa gacacgaacc tgtgcgccat ccatgccaag
      361 cgcgtgacca tcatgcccaa ggacatccag ttggcccgcc gcatccgcgg ggagcgggcc
      421 taaggcatat ttttaagtgg tcgatctaaa ggctcttttc agagccact
//
