H2BK1_HUMAN
ID H2BK1_HUMAN Reviewed; 122 AA.
AC A0A2R8Y619;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Histone H2B type 2-K1 {ECO:0000312|HGNC:HGNC:53833};
DE AltName: Full=Histone H2B type 2-E1 {ECO:0000305};
GN Name=H2BK1 {ECO:0000312|HGNC:HGNC:53833};
GN Synonyms=H2BE1 {ECO:0000312|HGNC:HGNC:53833};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP IDENTIFICATION.
RX PubMed=31537640; DOI=10.1101/gr.246462.118;
RA Mudge J.M., Jungreis I., Hunt T., Gonzalez J.M., Wright J.C., Kay M.,
RA Davidson C., Fitzgerald S., Seal R., Tweedie S., He L., Waterhouse R.M.,
RA Li Y., Bruford E., Choudhary J.S., Frankish A., Kellis M.;
RT "Discovery of high-confidence human protein-coding genes and exons by
RT whole-genome PhyloCSF helps elucidate 118 GWAS loci.";
RL Genome Res. 29:2073-2087(2019).
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:0000250|UniProtKB:P70696}.
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:0000250|UniProtKB:P70696}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:P70696}.
CC Nucleus {ECO:0000250|UniProtKB:P70696}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; AC021097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R8Y619; -.
DR SMR; A0A2R8Y619; -.
DR GlyGen; A0A2R8Y619; 1 site.
DR MassIVE; A0A2R8Y619; -.
DR PeptideAtlas; A0A2R8Y619; -.
DR Ensembl; ENST00000644661.2; ENSP00000495192.1; ENSG00000285480.2.
DR MANE-Select; ENST00000644661.2; ENSP00000495192.1; NM_001369125.3; NP_001356054.2.
DR GeneCards; H2BE1; -.
DR HGNC; HGNC:53833; H2BK1.
DR HPA; ENSG00000285480; Tissue enhanced (skin).
DR neXtProt; NX_A0A2R8Y619; -.
DR VEuPathDB; HostDB:ENSG00000285480; -.
DR GeneTree; ENSGT01050000244943; -.
DR OMA; GHRKETY; -.
DR SIGNOR; A0A2R8Y619; -.
DR PRO; PR:A0A2R8Y619; -.
DR Proteomes; UP000005640; Chromosome 7.
DR Bgee; ENSG00000285480; Expressed in lower esophagus mucosa and 83 other tissues.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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.
DR PROSITE; PS00357; HISTONE_H2B; 1.
PE 3: Inferred from homology;
KW Chromosome; DNA-binding; Glycoprotein; Hydroxylation; Isopeptide bond;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23527"
FT CHAIN 2..122
FT /note="Histone H2B type 2-K1"
FT /id="PRO_0000450355"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 31
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 31
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 31
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 31
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64475"
FT MOD_RES 40
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 40
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 40
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 43
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 43
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 43
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 43
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 54
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 54
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 54
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 76
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 83
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 89
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 105
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 105
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 105
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 105
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 105
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00729"
FT MOD_RES 113
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 113
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 113
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 113
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 113
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 113
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00729"
FT MOD_RES 113
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 117
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 117
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 117
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT CARBOHYD 109
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
SQ SEQUENCE 122 AA; 13491 MW; 67C3B7CEFCBA432F CRC64;
MSAEYGQRQQ PGGRGGRSSG NKKSKKRCRR KESYSMYIYK VLKQVHPDIG ISAKAMSIMN
SFVNDVFEQL ACEAARLAQY SGRTTLTSRE VQTAVRLLLP GELAKHAVSE GTKAVTKYTS
SK
