H4_BOVIN
ID H4_BOVIN Reviewed; 103 AA.
AC P62803; A5PJ80; A5PK53; A8QFF4; P02304; P02305;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Histone H4;
DE AltName: Full=H4.1;
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 [MRNA] (H4-V.1).
RC TISSUE=Adrenal medulla;
RX PubMed=9524213; DOI=10.1016/s0167-4781(97)00173-5;
RA Gendron N., Dumont M., Gagne M.-F., Lemaire S.;
RT "Poly A-containing histone H4 mRNA variant (H4-v.1): isolation and sequence
RT determination from bovine adrenal medulla.";
RL Biochim. Biophys. Acta 1396:32-38(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus, and Hereford;
RC TISSUE=Hypothalamus, Ileum, 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 2-103, ACETYLATION AT SER-2 AND LYS-17, AND METHYLATION
RP AT LYS-21.
RX PubMed=4321977;
RA Wilson R.K., Starbuck W.C., Taylor C.W., Jordan J.J., Busch H.;
RT "Structure of the glycine-rich, arginine-rich histone of the Novikoff
RT hepatoma.";
RL Cancer Res. 30:2942-2951(1970).
RN [4]
RP PROTEIN SEQUENCE OF 2-50.
RC TISSUE=Thymus;
RX PubMed=5817359; DOI=10.1016/s0021-9258(18)94330-9;
RA Ogawa Y., Quagliarotti G., Jordan J.J., Taylor C.W., Starbuck W.C.,
RA Busch H.;
RT "Structural analysis of the glycine-rich, arginine-rich histone. 3.
RT Sequence of the amino-terminal half of the molecule containing the modified
RT lysine residues and the total sequence.";
RL J. Biol. Chem. 244:4387-4392(1969).
RN [5]
RP PROTEIN SEQUENCE OF 51-103.
RC TISSUE=Thymus;
RX PubMed=5780842; DOI=10.1016/s0021-9258(18)91752-7;
RA Quagliarotti G., Ogawa Y., Taylor C.W., Sautiere P., Jordan J.,
RA Starbuck W.C., Busch H.;
RT "Structural analysis of the glycine-rich, arginine-rich histone. II.
RT Sequence of the half of the molecule containing the aromatic amino acids.";
RL J. Biol. Chem. 244:1796-1802(1969).
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 DNA
CC (By similarity). Found in a co-chaperone complex with DNJC9, MCM2 and
CC histone H3.3-H4 dimers (By similarity). Within the complex, interacts
CC with DNJC9 (via C-terminus); the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P62805, ECO:0000250|UniProtKB:P62806}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac)
CC and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in
CC heterochromatin. {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.
CC {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and
CC H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac)
CC and Lys-13 (H4K12ac). Demethylation is performed by JMJD6 (By
CC similarity). Symmetric dimethylation on Arg-4 (H4R3me2s) by the
CC PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage
CC (By similarity). {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1,
CC H4K20me2, H4K20me3). Monomethylation is performed by KMT5A/SET8.
CC Trimethylation is performed by KMT5B and KMT5C and induces gene
CC silencing. Monomethylated at Lys-13 (H4K12me1) by N6AMT1; H4K12me1
CC modification is present at the promoters of numerous genes encoding
CC cell cycle regulators. {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation
CC increases the association of H3.3-H4 with the histone chaperone HIRA,
CC thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome
CC assembly of H3.1-H4 (By similarity). {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to
CC ultraviolet irradiation. This may weaken the interaction between
CC histones and DNA and facilitate DNA accessibility to repair proteins.
CC Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA
CC damage. The exact role of H4K91ub1 in DNA damage response is still
CC unclear but it may function as a licensing signal for additional
CC histone H4 post-translational modifications such as H4 Lys-21
CC methylation (H4K20me) (By similarity). {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Sumoylated, which is associated with transcriptional repression.
CC {ECO:0000250|UniProtKB:P62805}.
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:P62805}.
CC -!- PTM: Butyrylation of histones marks active promoters and competes with
CC histone acetylation. {ECO:0000250|UniProtKB:P62806}.
CC -!- PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by
CC promoting dissociation of the H2A-H2B dimers from nucleosomes.
CC {ECO:0000250|UniProtKB:P62805}.
CC -!- PTM: Ufmylated; monofmylated by UFL1 at Lys-32 (H4K31Ufm1) in response
CC to DNA damage. {ECO:0000250|UniProtKB:P62805}.
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:P62805}.
CC -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
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DR EMBL; AF001288; AAC39176.1; -; mRNA.
DR EMBL; BC114196; AAI14197.1; -; mRNA.
DR EMBL; BC141999; AAI42000.1; -; mRNA.
DR EMBL; BC142359; AAI42360.1; -; mRNA.
DR PIR; A92050; HSBO4.
DR RefSeq; NP_001093194.1; NM_001099724.2.
DR RefSeq; NP_001139343.1; NM_001145871.2.
DR RefSeq; NP_776305.1; NM_173880.2.
DR RefSeq; XP_002684676.1; XM_002684630.3.
DR RefSeq; XP_002697516.1; XM_002697470.4.
DR RefSeq; XP_605163.2; XM_605163.4.
DR RefSeq; XP_874074.1; XM_868981.6.
DR AlphaFoldDB; P62803; -.
DR SMR; P62803; -.
DR BioGRID; 158101; 10.
DR DIP; DIP-44668N; -.
DR IntAct; P62803; 3.
DR MINT; P62803; -.
DR STRING; 9913.ENSBTAP00000047761; -.
DR iPTMnet; P62803; -.
DR PaxDb; P62803; -.
DR PeptideAtlas; P62803; -.
DR PRIDE; P62803; -.
DR Ensembl; ENSBTAT00000052402; ENSBTAP00000047761; ENSBTAG00000040277.
DR Ensembl; ENSBTAT00000054510; ENSBTAP00000052235; ENSBTAG00000052332.
DR Ensembl; ENSBTAT00000056505; ENSBTAP00000053034; ENSBTAG00000052349.
DR Ensembl; ENSBTAT00000068837; ENSBTAP00000062765; ENSBTAG00000052609.
DR Ensembl; ENSBTAT00000072717; ENSBTAP00000067077; ENSBTAG00000053034.
DR GeneID; 280691; -.
DR GeneID; 526789; -.
DR GeneID; 527645; -.
DR GeneID; 530773; -.
DR GeneID; 617875; -.
DR KEGG; bta:526789; -.
DR KEGG; bta:527645; -.
DR KEGG; bta:530773; -.
DR KEGG; bta:617875; -.
DR CTD; 121504; -.
DR CTD; 8360; -.
DR CTD; 8363; -.
DR CTD; 8366; -.
DR VEuPathDB; HostDB:ENSBTAG00000040277; -.
DR VEuPathDB; HostDB:ENSBTAG00000052332; -.
DR VEuPathDB; HostDB:ENSBTAG00000052349; -.
DR VEuPathDB; HostDB:ENSBTAG00000052609; -.
DR VEuPathDB; HostDB:ENSBTAG00000053034; -.
DR VGNC; VGNC:83549; H4C1.
DR VGNC; VGNC:84553; H4C3.
DR VGNC; VGNC:83562; H4C4.
DR eggNOG; KOG3467; Eukaryota.
DR GeneTree; ENSGT01030000234703; -.
DR GeneTree; ENSGT01050000244867; -.
DR HOGENOM; CLU_109117_2_3_1; -.
DR InParanoid; P62803; -.
DR OMA; GFRRCCE; -.
DR OrthoDB; 1564596at2759; -.
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-3214841; PKMTs methylate histone lysines.
DR Reactome; R-BTA-3214842; HDMs demethylate histones.
DR Reactome; R-BTA-3214847; HATs acetylate histones.
DR Reactome; R-BTA-3214858; RMTs methylate histone arginines.
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-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 1.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000040277; Expressed in spiral colon and 103 other tissues.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR CDD; cd00076; H4; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR001951; Histone_H4.
DR InterPro; IPR019809; Histone_H4_CS.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR Pfam; PF15511; CENP-T_C; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00047; HISTONE_H4; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Citrullination; Direct protein sequencing;
KW DNA-binding; Hydroxylation; Isopeptide bond; Methylation; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4321977,
FT ECO:0000269|PubMed:5817359"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158289"
FT DNA_BIND 17..21
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:4321977"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 4
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 4
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 4
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 4
FT /note="Symmetric dimethylarginine; by PRMT5 and PRMT7;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 6
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 9
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 9
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 13
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 17
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:4321977"
FT MOD_RES 17
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 17
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 17
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 17
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 21
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 21
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:4321977"
FT MOD_RES 21
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:4321977"
FT MOD_RES 32
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 45
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 45
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 45
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 48
FT /note="Phosphoserine; by PAK2"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 52
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 60
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 60
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 80
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 80
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 80
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 80
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 89
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 92
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in UFM1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT CONFLICT 55
FT /note="T -> A (in Ref. 2; AAI42000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 11367 MW; A9E5DFD3F8B97598 CRC64;
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG
