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histone H2B type F-M [Homo sapiens]

NCBI Reference Sequence: NP_001157888.2

Identical Proteins FASTA Graphics 

LOCUS       NP_001157888             148 aa            linear   PRI 04-JAN-2024
DEFINITION  histone H2B type F-M [Homo sapiens].
ACCESSION   NP_001157888
VERSION     NP_001157888.2
DBSOURCE    REFSEQ: accession NM_001164416.4
KEYWORDS    RefSeq.
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 148)
  AUTHORS   Molaro A and Drinnenberg IA.
  TITLE     Studying the Evolution of Histone Variants Using Phylogeny
  JOURNAL   Methods Mol Biol 1832, 273-291 (2018)
   PUBMED   30073533
REFERENCE   2  (residues 1 to 148)
  AUTHORS   El Kennani S, Adrait A, Shaytan AK, Khochbin S, Bruley C, Panchenko
            AR, Landsman D, Pflieger D and Govin J.
  TITLE     MS_HistoneDB, a manually curated resource for proteomic analysis of
            human and mouse histones
  JOURNAL   Epigenetics Chromatin 10, 2 (2017)
   PUBMED   28096900
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Talbert PB, Ahmad K, Almouzni G, Ausio J, Berger F, Bhalla PL,
            Bonner WM, Cande WZ, Chadwick BP, Chan SW, Cross GA, Cui L,
            Dimitrov SI, Doenecke D, Eirin-Lopez JM, Gorovsky MA, Hake SB,
            Hamkalo BA, Holec S, Jacobsen SE, Kamieniarz K, Khochbin S,
            Ladurner AG, Landsman D, Latham JA, Loppin B, Malik HS, Marzluff
            WF, Pehrson JR, Postberg J, Schneider R, Singh MB, Smith MM,
            Thompson E, Torres-Padilla ME, Tremethick DJ, Turner BM, Waterborg
            JH, Wollmann H, Yelagandula R, Zhu B and Henikoff S.
  TITLE     A unified phylogeny-based nomenclature for histone variants
  JOURNAL   Epigenetics Chromatin 5, 7 (2012)
   PUBMED   22650316
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D,
            Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL,
            Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles
            ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman
            R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P,
            Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E,
            Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA,
            Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A,
            Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM,
            Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N,
            Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford
            EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J,
            Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E,
            Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke
            G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V,
            Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis
            C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H,
            Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ,
            Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL,
            Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert
            J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock
            R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD,
            Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M,
            Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob
            L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S,
            Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A,
            Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L,
            Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD,
            Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall
            J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G,
            Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N,
            Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R,
            Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM,
            Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S,
            Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C,
            Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC,
            Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor
            PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K,
            Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana
            D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A,
            Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G,
            Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL,
            Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D,
            Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ,
            Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M,
            Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T,
            Gibbs RA, Beck S, Rogers J and Bentley DR.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC234782.5.
            
            On Nov 5, 2020 this sequence version replaced NP_001157888.1.
            
            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 encodes a replication-independent histone
            that is a member of the H2B histone family. [provided by RefSeq,
            Nov 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK093522.1, DB041370.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            replication-independent histone  :: PMID: 22650316
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.2"
     Protein         1..148
                     /product="histone H2B type F-M"
                     /note="histone H2B.s; H2B histone family member M; H2B.M
                     histone"
                     /calculated_mol_wt=16368
     Region          53..137
                     /region_name="HFD_H2B"
                     /note="histone-fold domain found in histone H2B and
                     similar proteins; cd22910"
                     /db_xref="CDD:467035"
     Site            order(54,56..58,60..62,65..72,74..75,78..79,82..83,85..87,
                     89..91,95,105..106,108,111..112,115,118..120,123,126..128,
                     130..131,134..135)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            order(55..57,59..60,63..65,70..72,76,112,116,125..126,
                     128..129,132..133,135..136)
                     /site_type="other"
                     /note="Hif1 binding site [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            order(78,81..82,84..85,88,93,96,99..101,109..110,113,
                     117..118)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467035"
     CDS             1..148
                     /gene="H2BW2"
                     /gene_synonym="H2B/s; H2BFM; H2BM"
                     /coded_by="NM_001164416.4:40..486"
                     /db_xref="CCDS:CCDS55468.2"
                     /db_xref="GeneID:286436"
                     /db_xref="HGNC:HGNC:27867"
ORIGIN      
        1 maeassetts eegqsiqepk eanstkaqkq krrgcrgsrr rhanrrgdsf gdsftpyfpr
       61 vlkqvhqgls lsqeavsvmd smihdildri ateagqlahy tkrvtitsrd iqmavrlllp
      121 gkmgklaeaq gtnaalrtsl caiwqqrk
//
1..148
/gene="H2BW2"
/gene_synonym="H2B/s; H2BFM; H2BM"
/coded_by="NM_001164416.4:40..486"
/db_xref="CCDS:CCDS55468.2"
/db_xref="GeneID:286436"
/db_xref="HGNC:HGNC:27867"
Feature NP_001157888 : 1 segment
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