H2B1_BOVIN
ID H2B1_BOVIN Reviewed; 126 AA.
AC P62808; A1L599; A5PJG5; P02278; Q32PE8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Histone H2B type 1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus, and Hereford; TISSUE=Liver, and Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-126.
RX PubMed=4644305; DOI=10.1093/oxfordjournals.jbchem.a129911;
RA Iwai K., Hayashi H., Ishikawa K.;
RT "Calf thymus lysine- and serine-rich histone. 3. Complete amino acid
RT sequence and its implication for interactions of histones with DNA.";
RL J. Biochem. 72:357-367(1972).
RN [4]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=6320184; DOI=10.1073/pnas.81.2.371;
RA Urist M.R., Huo Y.K., Brownell A.G., Hohl W.M., Buyske J., Lietze A.,
RA Tempst P., Hunkapiller M., DeLange R.J.;
RT "Purification of bovine bone morphogenetic protein by hydroxyapatite
RT chromatography.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:371-375(1984).
RN [5]
RP PROTEIN SEQUENCE OF 2-20.
RX PubMed=12777396; DOI=10.1074/jbc.m303786200;
RA Tovich P.R., Oko R.J.;
RT "Somatic histones are components of the perinuclear theca in bovine
RT spermatozoa.";
RL J. Biol. Chem. 278:32431-32438(2003).
RN [6]
RP UBIQUITINATION.
RX PubMed=2713375; DOI=10.1021/bi00429a006;
RA Nickel B.E., Allis C.D., Davie J.R.;
RT "Ubiquitinated histone H2B is preferentially located in transcriptionally
RT active chromatin.";
RL Biochemistry 28:958-963(1989).
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 -!- 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 -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is
CC required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me)
CC methylation and transcription activation at specific gene loci, such as
CC HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121
CC (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic
CC transcriptional activation and is also prerequisite for histone H3
CC 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with
CC the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub
CC also acts as a regulator of mRNA splicing: deubiquitination by USP49 is
CC required for efficient cotranscriptional splicing of a large set of
CC exons (By similarity). {ECO:0000250|UniProtKB:P33778}.
CC -!- PTM: Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis;
CC which facilitates apoptotic chromatin condensation. Also phosphorylated
CC on Ser-15 in response to DNA double strand breaks (DSBs), and in
CC correlation with somatic hypermutation and immunoglobulin class-switch
CC recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response
CC to stress promotes transcription (By similarity).
CC {ECO:0000250|UniProtKB:P33778, ECO:0000250|UniProtKB:Q64475}.
CC -!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.
CC It fluctuates in response to extracellular glucose, and associates with
CC transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC marks testis-specific genes in post-meiotic cells, including X-linked
CC genes that escape sex chromosome inactivation in haploid cells.
CC Crotonylation marks active promoters and enhancers and confers
CC resistance to transcriptional repressors. It is also associated with
CC post-meiotically activated genes on autosomes (By similarity).
CC {ECO:0000250|UniProtKB:P33778}.
CC -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC directly derived from endogenous or exogenous lactate, leading to
CC stimulates gene transcription. {ECO:0000250|UniProtKB:P33778}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; BT029886; ABM06136.1; -; mRNA.
DR EMBL; BC108143; AAI08144.1; -; mRNA.
DR EMBL; BC142102; AAI42103.1; -; mRNA.
DR PIR; A02605; HSBO22.
DR RefSeq; NP_001032546.1; NM_001037469.2.
DR RefSeq; XP_002686101.1; XM_002686055.5.
DR RefSeq; XP_002697553.1; XM_002697507.4.
DR RefSeq; XP_002697561.1; XM_002697515.4.
DR RefSeq; XP_002702931.1; XM_002702885.4.
DR RefSeq; XP_003583950.1; XM_003583902.4.
DR RefSeq; XP_003587771.1; XM_003587723.4.
DR RefSeq; XP_010816749.1; XM_010818447.2.
DR RefSeq; XP_010816750.1; XM_010818448.1.
DR RefSeq; XP_010816751.1; XM_010818449.2.
DR RefSeq; XP_010816752.1; XM_010818450.1.
DR RefSeq; XP_010816754.1; XM_010818452.2.
DR RefSeq; XP_010816755.1; XM_010818453.1.
DR RefSeq; XP_010816756.1; XM_010818454.2.
DR RefSeq; XP_010816757.1; XM_010818455.1.
DR RefSeq; XP_010816759.1; XM_010818457.2.
DR RefSeq; XP_010816816.1; XM_010818514.1.
DR RefSeq; XP_010823688.1; XM_010825386.2.
DR RefSeq; XP_010823689.1; XM_010825387.1.
DR RefSeq; XP_010823690.1; XM_010825388.2.
DR RefSeq; XP_010823691.1; XM_010825389.1.
DR RefSeq; XP_010823693.1; XM_010825391.2.
DR RefSeq; XP_010823694.1; XM_010825392.2.
DR RefSeq; XP_010823695.1; XM_010825393.2.
DR RefSeq; XP_010823697.1; XM_010825395.2.
DR RefSeq; XP_010823715.1; XM_010825413.2.
DR RefSeq; XP_010825135.2; XM_010826833.2.
DR RefSeq; XP_015315427.1; XM_015459941.1.
DR RefSeq; XP_015324467.1; XM_015468981.1.
DR RefSeq; XP_581429.3; XM_581429.7.
DR RefSeq; XP_599845.2; XM_599845.8.
DR AlphaFoldDB; P62808; -.
DR SMR; P62808; -.
DR BioGRID; 542671; 1.
DR STRING; 9913.ENSBTAP00000047687; -.
DR iPTMnet; P62808; -.
DR PaxDb; P62808; -.
DR PeptideAtlas; P62808; -.
DR PRIDE; P62808; -.
DR Ensembl; ENSBTAT00000045053; ENSBTAP00000047687; ENSBTAG00000031776.
DR Ensembl; ENSBTAT00000075319; ENSBTAP00000064600; ENSBTAG00000052713.
DR Ensembl; ENSBTAT00000082128; ENSBTAP00000067722; ENSBTAG00000052382.
DR Ensembl; ENSBTAT00000085911; ENSBTAP00000061481; ENSBTAG00000049598.
DR GeneID; 104968456; -.
DR GeneID; 104975676; -.
DR GeneID; 505183; -.
DR GeneID; 615043; -.
DR GeneID; 616776; -.
DR GeneID; 787269; -.
DR GeneID; 787465; -.
DR KEGG; bta:104968456; -.
DR KEGG; bta:104975676; -.
DR KEGG; bta:505183; -.
DR KEGG; bta:615043; -.
DR KEGG; bta:616776; -.
DR KEGG; bta:787269; -.
DR KEGG; bta:787465; -.
DR CTD; 100062934; -.
DR CTD; 483169; -.
DR CTD; 8343; -.
DR CTD; 8344; -.
DR CTD; 8345; -.
DR CTD; 8347; -.
DR CTD; 8348; -.
DR VEuPathDB; HostDB:ENSBTAG00000031776; -.
DR VEuPathDB; HostDB:ENSBTAG00000049598; -.
DR VEuPathDB; HostDB:ENSBTAG00000052382; -.
DR VEuPathDB; HostDB:ENSBTAG00000052713; -.
DR VGNC; VGNC:83581; H2BC13.
DR VGNC; VGNC:83556; H2BC4.
DR VGNC; VGNC:83564; H2BC6.
DR VGNC; VGNC:83566; H2BC7.
DR eggNOG; KOG1744; Eukaryota.
DR GeneTree; ENSGT01050000244832; -.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; P62808; -.
DR OMA; DIFDRMA; -.
DR OrthoDB; 1536672at2759; -.
DR TreeFam; TF300212; -.
DR Reactome; R-BTA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-BTA-110331; Cleavage of the damaged purine.
DR Reactome; R-BTA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-BTA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-BTA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-BTA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-BTA-3214815; HDACs deacetylate histones.
DR Reactome; R-BTA-3214847; HATs acetylate histones.
DR Reactome; R-BTA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-BTA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-BTA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-BTA-5689880; Ub-specific processing proteases.
DR Reactome; R-BTA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-BTA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-BTA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-BTA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-BTA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-BTA-9670095; Inhibition of DNA recombination at telomere.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000031776; Expressed in spiral colon and 59 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 1: Evidence at protein level;
KW Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Glycoprotein; Hydroxylation; Isopeptide bond; Methylation; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23527,
FT ECO:0000269|PubMed:12777396, ECO:0000269|PubMed:4644305,
FT ECO:0000269|PubMed:6320184"
FT CHAIN 2..126
FT /note="Histone H2B type 1"
FT /id="PRO_0000071825"
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"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:P23527"
FT MOD_RES 6
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 6
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64475"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00715"
FT MOD_RES 6
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 6
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 6
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 12
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64475"
FT MOD_RES 12
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 12
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 12
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 13
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 13
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00715"
FT MOD_RES 13
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 15
FT /note="Phosphoserine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 16
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00715"
FT MOD_RES 16
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 16
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 17
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 17
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 17
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 21
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 21
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64475"
FT MOD_RES 21
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00715"
FT MOD_RES 21
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 21
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 21
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 24
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 24
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 24
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 25
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 35
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 35
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64475"
FT MOD_RES 35
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 35
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 35
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 37
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q64475"
FT MOD_RES 44
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 44
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 44
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 47
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 47
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 47
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 58
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 58
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 80
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 86
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 86
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 86
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 86
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 87
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 93
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 109
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 109
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 109
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 109
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00729"
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:Q64475"
FT MOD_RES 117
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 117
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 117
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00729"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 121
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 121
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 121
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 121
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT CARBOHYD 113
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P58876"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5QNW6"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000305|PubMed:2713375"
FT CONFLICT 21
FT /note="K -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 126 AA; 13906 MW; FAE1479F44BE703D CRC64;
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSSK
