H2BWT_HUMAN
ID H2BWT_HUMAN Reviewed; 175 AA.
AC Q7Z2G1; B1AK72; Q147W3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Histone H2B type W-T;
DE AltName: Full=H2B histone family member W testis-specific;
DE AltName: Full=H2B.W histone 1 {ECO:0000312|HGNC:HGNC:27252};
GN Name=H2BW1 {ECO:0000312|HGNC:HGNC:27252};
GN Synonyms=H2BFWT {ECO:0000312|HGNC:HGNC:27252};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND VARIANT HIS-123.
RC TISSUE=Testis;
RX PubMed=15475252; DOI=10.1016/j.ygeno.2004.06.001;
RA Churikov D., Siino J., Svetlova M., Zhang K., Gineitis A., Bradbury E.M.,
RA Zalensky A.;
RT "Novel human testis-specific histone H2B encoded by the interrupted gene on
RT the X chromosome.";
RL Genomics 84:745-756(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-123.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=16449661; DOI=10.1128/mcb.26.4.1518-1526.2006;
RA Boulard M., Gautier T., Mbele G.O., Gerson V., Hamiche A., Angelov D.,
RA Bouvet P., Dimitrov S.;
RT "The NH2 tail of the novel histone variant H2BFWT exhibits properties
RT distinct from conventional H2B with respect to the assembly of mitotic
RT chromosomes.";
RL Mol. Cell. Biol. 26:1518-1526(2006).
CC -!- FUNCTION: Atypical histone H2B. Nucleosomes containing it are
CC structurally and dynamically indistinguishable from those containing
CC conventional H2B. However, unlike conventional H2B, does not recruit
CC chromosome condensation factors and does not participate in the
CC assembly of mitotic chromosomes. May be important for telomere
CC function. {ECO:0000269|PubMed:16449661}.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA.
CC -!- INTERACTION:
CC Q7Z2G1; Q6NXS1: PPP1R2B; NbExp=3; IntAct=EBI-18200422, EBI-10251630;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:15475252}.
CC Chromosome {ECO:0000269|PubMed:15475252}.
CC -!- TISSUE SPECIFICITY: Testis-specific. Present in sperm cells (at protein
CC level). {ECO:0000269|PubMed:15475252}.
CC -!- MISCELLANEOUS: In contrast to other H2B histones, it does not contain
CC the conserved residue in C-terminus that is the target of
CC monoubiquitination.
CC -!- MISCELLANEOUS: Ortholog in primates, but not in rodents.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; AY283369; AAP37489.1; -; Genomic_DNA.
DR EMBL; AY283370; AAP37490.1; -; mRNA.
DR EMBL; AL034485; CAI43100.2; -; Genomic_DNA.
DR EMBL; CH471120; EAX02765.1; -; Genomic_DNA.
DR EMBL; BC038109; AAH38109.1; -; mRNA.
DR EMBL; BC118604; AAI18605.1; -; mRNA.
DR EMBL; BC121816; AAI21817.1; -; mRNA.
DR RefSeq; NP_001002916.3; NM_001002916.4.
DR AlphaFoldDB; Q7Z2G1; -.
DR SMR; Q7Z2G1; -.
DR BioGRID; 127727; 17.
DR IntAct; Q7Z2G1; 1.
DR STRING; 9606.ENSP00000354723; -.
DR iPTMnet; Q7Z2G1; -.
DR PhosphoSitePlus; Q7Z2G1; -.
DR BioMuta; H2BFWT; -.
DR DMDM; 223590216; -.
DR MassIVE; Q7Z2G1; -.
DR PaxDb; Q7Z2G1; -.
DR PeptideAtlas; Q7Z2G1; -.
DR PRIDE; Q7Z2G1; -.
DR Antibodypedia; 65963; 102 antibodies from 17 providers.
DR DNASU; 158983; -.
DR Ensembl; ENST00000217926.7; ENSP00000354723.5; ENSG00000123569.10.
DR GeneID; 158983; -.
DR KEGG; hsa:158983; -.
DR UCSC; uc004elr.4; human.
DR CTD; 158983; -.
DR DisGeNET; 158983; -.
DR GeneCards; H2BW1; -.
DR HGNC; HGNC:27252; H2BW1.
DR HPA; ENSG00000123569; Not detected.
DR MIM; 300507; gene.
DR neXtProt; NX_Q7Z2G1; -.
DR VEuPathDB; HostDB:ENSG00000123569; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_3_0_1; -.
DR InParanoid; Q7Z2G1; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; Q7Z2G1; -.
DR TreeFam; TF300212; -.
DR PathwayCommons; Q7Z2G1; -.
DR SignaLink; Q7Z2G1; -.
DR SIGNOR; Q7Z2G1; -.
DR BioGRID-ORCS; 158983; 13 hits in 687 CRISPR screens.
DR GeneWiki; H2BFWT; -.
DR GenomeRNAi; 158983; -.
DR Pharos; Q7Z2G1; Tbio.
DR PRO; PR:Q7Z2G1; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q7Z2G1; protein.
DR Bgee; ENSG00000123569; Expressed in cortical plate and 8 other tissues.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; PTHR23428; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; Membrane; Nucleosome core; Nucleus;
KW Reference proteome.
FT CHAIN 1..175
FT /note="Histone H2B type W-T"
FT /id="PRO_0000244828"
FT REGION 29..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 87
FT /note="R -> W (in dbSNP:rs17332043)"
FT /id="VAR_049315"
FT VARIANT 123
FT /note="R -> H (in dbSNP:rs553509)"
FT /evidence="ECO:0000269|PubMed:15475252,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_054318"
SQ SEQUENCE 175 AA; 19618 MW; C47C922CBBE96BCC CRC64;
MLRTEVPRLP RSTTAIVWSC HLMATASAMA GPSSETTSEE QLITQEPKEA NSTTSQKQSK
QRKRGRHGPR RCHSNCRGDS FATYFRRVLK QVHQGLSLSR EAVSVMDSLV HDILDRIATE
AGRLARSTKR QTITAWETRM AVRLLLPGQM GKLAESEGTK AVLRTSLYAI QQQRK
