ID   B2R4S9_HUMAN            Unreviewed;       126 AA.
AC   B2R4S9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Histone H2B {ECO:0000256|RuleBase:RU000451};
GN   Name=HIST1H2BE {ECO:0000313|EMBL:EAW55537.1};
GN   Synonyms=HIST1H2BC {ECO:0000313|EMBL:EAW55530.1}, HIST1H2BF
GN   {ECO:0000313|EMBL:EAW55543.1}, HIST1H2BG
GN   {ECO:0000313|EMBL:EAW55545.1}, HIST1H2BI
GN   {ECO:0000313|EMBL:EAW55554.1};
GN   ORFNames=hCG_1640484 {ECO:0000313|EMBL:EAW55530.1}, hCG_1640985
GN   {ECO:0000313|EMBL:EAW55545.1}, hCG_1641780
GN   {ECO:0000313|EMBL:EAW55554.1}, hCG_1787353
GN   {ECO:0000313|EMBL:EAW55537.1}, hCG_1787365
GN   {ECO:0000313|EMBL:EAW55543.1};
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 {ECO:0000313|EMBL:BAG34876.1};
RN   [1] {ECO:0000313|EMBL:EAW55530.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:EAW55530.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:BAG34876.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA   Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA   Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA   Isogai T.;
RT   "NEDO functional analysis of protein and research application project.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC       DNA into chromatin, limiting DNA accessibility to the cellular
CC       machineries which require DNA as a template. Histones thereby play a
CC       central role in transcription regulation, DNA repair, DNA replication
CC       and chromosomal stability. DNA accessibility is regulated via a complex
CC       set of post-translational modifications of histones, also called
CC       histone code, and nucleosome remodeling.
CC       {ECO:0000256|ARBA:ARBA00002001}.
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. {ECO:0000256|RuleBase:RU000451}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000451}.
CC   -!- SIMILARITY: Belongs to the histone H2B family.
CC       {ECO:0000256|ARBA:ARBA00006846, ECO:0000256|RuleBase:RU000451}.
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DR   EMBL; AK311935; BAG34876.1; -; mRNA.
DR   EMBL; AK312096; BAG35032.1; -; mRNA.
DR   EMBL; CH471087; EAW55530.1; -; Genomic_DNA.
DR   EMBL; CH471087; EAW55537.1; -; Genomic_DNA.
DR   EMBL; CH471087; EAW55543.1; -; Genomic_DNA.
DR   EMBL; CH471087; EAW55545.1; -; Genomic_DNA.
DR   EMBL; CH471087; EAW55554.1; -; Genomic_DNA.
DR   RefSeq; NP_003509.1; NM_003518.3.
DR   RefSeq; NP_003513.1; NM_003522.3.
DR   RefSeq; NP_003514.2; NM_003523.2.
DR   RefSeq; NP_003516.1; NM_003525.2.
DR   RefSeq; NP_003517.2; NM_003526.2.
DR   SMR; B2R4S9; -.
DR   IntAct; B2R4S9; 2.
DR   SwissPalm; B2R4S9; -.
DR   Antibodypedia; 10912; 440 antibodies from 24 providers.
DR   Antibodypedia; 72347; 43 antibodies from 4 providers.
DR   Antibodypedia; 76967; 1 antibodies from 1 providers.
DR   Antibodypedia; 77815; 2 antibodies from 1 providers.
DR   Antibodypedia; 77855; 1 antibodies from 1 providers.
DR   DNASU; 8339; -.
DR   GeneID; 8339; -.
DR   GeneID; 8343; -.
DR   GeneID; 8344; -.
DR   GeneID; 8346; -.
DR   GeneID; 8347; -.
DR   KEGG; hsa:8339; -.
DR   KEGG; hsa:8343; -.
DR   KEGG; hsa:8344; -.
DR   KEGG; hsa:8346; -.
DR   KEGG; hsa:8347; -.
DR   CTD; 8339; -.
DR   CTD; 8343; -.
DR   CTD; 8344; -.
DR   CTD; 8346; -.
DR   CTD; 8347; -.
DR   VEuPathDB; HostDB:ENSG00000180596; -.
DR   VEuPathDB; HostDB:ENSG00000273802; -.
DR   VEuPathDB; HostDB:ENSG00000274290; -.
DR   VEuPathDB; HostDB:ENSG00000277224; -.
DR   VEuPathDB; HostDB:ENSG00000278588; -.
DR   HOGENOM; CLU_075666_2_1_1; -.
DR   OMA; KXSTITS; -.
DR   OrthoDB; 5258202at2759; -.
DR   BioGRID-ORCS; 8339; 255 hits in 1040 CRISPR screens.
DR   BioGRID-ORCS; 8343; 394 hits in 1061 CRISPR screens.
DR   BioGRID-ORCS; 8344; 583 hits in 1069 CRISPR screens.
DR   BioGRID-ORCS; 8346; 79 hits in 1055 CRISPR screens.
DR   BioGRID-ORCS; 8347; 717 hits in 1087 CRISPR screens.
DR   ChiTaRS; HIST1H2BC; human.
DR   ExpressionAtlas; B2R4S9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000558; Histone_H2B.
DR   PANTHER; PTHR23428; HISTONE H2B; 1.
DR   PANTHER; PTHR23428:SF326; HISTONE H2B TYPE 2-E; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00621; HISTONEH2B.
DR   SMART; SM00427; H2B; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00357; HISTONE_H2B; 1.
PE   2: Evidence at transcript level;
KW   Chromosome {ECO:0000256|RuleBase:RU000451};
KW   DNA-binding {ECO:0000256|RuleBase:RU000451};
KW   Nucleosome core {ECO:0000256|RuleBase:RU000451};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000451}.
FT   DOMAIN          11..101
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..35
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   126 AA;  13906 MW;  FAE1479F44BE703D CRC64;
     MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM
     GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
     KYTSSK
//