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
//