ID H4_CHICK Reviewed; 103 AA. AC P62801; P02304; P02305; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 164. DE RecName: Full=Histone H4; GN Name=H4-I; GN and GN Name=H4-II; GN and GN Name=H4-III; GN and GN Name=H4-IV; GN and GN Name=H4-V; GN and GN Name=H4-VI; GN and GN Name=H4-VII; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=4000938; DOI=10.1093/nar/13.4.1369; RA Wang S.W., Robins A.J., D'Andrea R., Wells J.R.E.; RT "Inverted duplication of histone genes in chicken and disposition of RT regulatory sequences."; RL Nucleic Acids Res. 13:1369-1387(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6190814; DOI=10.1016/s0021-9258(18)32157-4; RA Sugarman B.J., Dodgson J.B., Engel J.D.; RT "Genomic organization, DNA sequence, and expression of chicken embryonic RT histone genes."; RL J. Biol. Chem. 258:9005-9016(1983). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H4-III AND H4-IV). RX PubMed=1748315; DOI=10.1016/0378-1119(91)90452-h; RA Nakayama T., Takechi S., Ohshige T., Kondo K., Yamamoto K.; RT "Nucleotide sequences of two members of the chicken H4 histone-encoding RT gene family."; RL Gene 108:311-312(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H4-VI AND H4-VII). RC STRAIN=White leghorn; TISSUE=Liver; RX PubMed=8804862; DOI=10.1093/dnares/3.2.95; RA Takami Y., Higashio M., Fukuoka T., Takechi S., Nakayama T.; RT "Organization of the chicken histone genes in a major gene cluster and RT generation of an almost complete set of the core histone protein RT sequences."; RL DNA Res. 3:95-99(1996). RN [5] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). RX PubMed=1946434; DOI=10.1073/pnas.88.22.10148; RA Arents G., Burlingame R.W., Wang B.-C., Love W.E., Moudrianakis E.N.; RT "The nucleosomal core histone octamer at 3.1 A resolution: a tripartite RT protein assembly and a left-handed superhelix."; RL Proc. Natl. Acad. Sci. U.S.A. 88:10148-10152(1991). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=11092917; DOI=10.1107/s0907444900011847; RA Harp J.M., Hanson B.L., Timm D.E., Bunick G.J.; RT "Asymmetries in the nucleosome core particle at 2.5 A resolution."; RL Acta Crystallogr. D 56:1513-1534(2000). 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: 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. Symmetric CC dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a CC crucial role in the germ-cell lineage (By similarity). CC {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: Acetyl-methylated at Lys-6 and Lys-13 (H4K5acme and H4K12acme, CC respectively), acetyl-methylation is an epigenetic mark of active CC chromatin associated with increased transcriptional initiation. Acetyl- CC methylation is formed by acetylation by EP300/p300 of lysine residues CC that are already monomethylated on the same side chain. H4K5acme and CC H4K12acme marks specifically bind BRD2. {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: 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X02218; CAA26137.1; -; Genomic_DNA. DR EMBL; X02218; CAA26140.1; -; Genomic_DNA. DR EMBL; J00866; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M74533; AAA73091.1; -; Genomic_DNA. DR EMBL; M74534; AAA73092.1; -; Genomic_DNA. DR EMBL; U37575; AAC59999.1; -; Genomic_DNA. DR EMBL; U37575; AAC60001.1; -; Genomic_DNA. DR PIR; A02640; HSCH4. DR PIR; JH0507; JH0507. DR RefSeq; NP_001032932.1; NM_001037843.1. DR RefSeq; NP_001032934.1; NM_001037845.1. DR RefSeq; NP_001268414.1; NM_001281485.1. DR RefSeq; XP_001233180.1; XM_001233179.4. DR RefSeq; XP_003640418.1; XM_003640370.3. DR RefSeq; XP_004937726.1; XM_004937669.2. DR RefSeq; XP_425458.2; XM_425458.5. DR PDB; 1EQZ; X-ray; 2.50 A; D/H=1-103. DR PDB; 1HIO; X-ray; 3.10 A; D=28-103. DR PDB; 1HQ3; X-ray; 2.15 A; D/H=1-103. DR PDB; 1TZY; X-ray; 1.90 A; D/H=1-103. DR PDB; 2ARO; X-ray; 2.10 A; D/H=1-103. DR PDB; 2HIO; X-ray; 3.10 A; D=1-103. DR PDB; 3C9K; EM; 20.00 A; D/H=2-103. DR PDBsum; 1EQZ; -. DR PDBsum; 1HIO; -. DR PDBsum; 1HQ3; -. DR PDBsum; 1TZY; -. DR PDBsum; 2ARO; -. DR PDBsum; 2HIO; -. DR PDBsum; 3C9K; -. DR AlphaFoldDB; P62801; -. DR EMDB; EMD-0323; -. DR EMDB; EMD-1469; -. DR SMR; P62801; -. DR BioGRID; 679227; 7. DR IntAct; P62801; 2. DR STRING; 9031.ENSGALP00000049875; -. DR PaxDb; 9031-ENSGALP00000041526; -. DR Ensembl; ENSGALT00015024482; ENSGALP00015014617; ENSGALG00015009999. DR GeneID; 100858049; -. DR GeneID; 100858319; -. DR GeneID; 417946; -. DR GeneID; 417950; -. DR GeneID; 427884; -. DR GeneID; 770142; -. DR KEGG; gga:100858049; -. DR KEGG; gga:100858319; -. DR KEGG; gga:417946; -. DR KEGG; gga:417950; -. DR KEGG; gga:427884; -. DR KEGG; gga:770005; -. DR KEGG; gga:770142; -. DR CTD; 100858049; -. DR CTD; 100858319; -. DR CTD; 417946; -. DR CTD; 417950; -. DR CTD; 427884; -. DR CTD; 770142; -. DR VEuPathDB; HostDB:geneid_100858049; -. DR VEuPathDB; HostDB:geneid_100858319; -. DR VEuPathDB; HostDB:geneid_417946; -. DR VEuPathDB; HostDB:geneid_417950; -. DR VEuPathDB; HostDB:geneid_427884; -. DR VEuPathDB; HostDB:geneid_770005; -. DR VEuPathDB; HostDB:geneid_770142; -. DR VEuPathDB; HostDB:LOC121106538; -. DR eggNOG; KOG3467; Eukaryota. DR HOGENOM; CLU_109117_2_3_1; -. DR InParanoid; P62801; -. DR OMA; RRNRNMS; -. DR OrthoDB; 4405952at2759; -. DR PhylomeDB; P62801; -. DR Reactome; R-GGA-212300; PRC2 methylates histones and DNA. DR Reactome; R-GGA-2299718; Condensation of Prophase Chromosomes. DR Reactome; R-GGA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-GGA-3214841; PKMTs methylate histone lysines. DR Reactome; R-GGA-3214842; HDMs demethylate histones. DR Reactome; R-GGA-3214847; HATs acetylate histones. DR Reactome; R-GGA-3214858; RMTs methylate histone arginines. DR Reactome; R-GGA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-GGA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-GGA-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-GGA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-GGA-5693571; Nonhomologous End-Joining (NHEJ). DR Reactome; R-GGA-5693607; Processing of DNA double-strand break ends. DR Reactome; R-GGA-606279; Deposition of new CENPA-containing nucleosomes at the centromere. DR Reactome; R-GGA-68616; Assembly of the ORC complex at the origin of replication. DR Reactome; R-GGA-69473; G2/M DNA damage checkpoint. DR Reactome; R-GGA-73728; RNA Polymerase I Promoter Opening. DR Reactome; R-GGA-73772; RNA Polymerase I Promoter Escape. DR Reactome; R-GGA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-GGA-9018519; Estrogen-dependent gene expression. DR EvolutionaryTrace; P62801; -. DR PRO; PR:P62801; -. DR Proteomes; UP000000539; Chromosome 1. DR Bgee; ENSGALG00000037322; Expressed in granulocyte and 14 other cell types or tissues. DR ExpressionAtlas; P62801; baseline. 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:0006334; P:nucleosome assembly; IBA:GO_Central. DR CDD; cd00076; H4; 1. DR Gene3D; 1.10.20.10; Histone, subunit A; 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 PANTHER; PTHR10484; HISTONE H4; 1. DR PANTHER; PTHR10484:SF0; HISTONE H4; 1. DR Pfam; PF15511; CENP-T_C; 1. DR PRINTS; PR00623; HISTONEH4. DR SMART; SM00417; H4; 1. DR SMART; SM00803; TAF; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00047; HISTONE_H4; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosome; Citrullination; DNA-binding; KW Hydroxylation; Isopeptide bond; Methylation; Nucleosome core; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..103 FT /note="Histone H4" FT /id="PRO_0000158296" 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:0000250|UniProtKB:P62805" 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|UniProtKB:P62805" 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:P62805" FT MOD_RES 6 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 6 FT /note="N6-acetyl-N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 6 FT /note="N6-acetyllysine" 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-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-acetyllysine" 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-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-acetyl-N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 13 FT /note="N6-acetyllysine" 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-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 17 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 17 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 17 FT /note="N6-butyryllysine; 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:0000250|UniProtKB:P62805" FT MOD_RES 21 FT /note="N6-methylated lysine" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 21 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62805" 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" 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" FT /evidence="ECO:0000250|UniProtKB:P62805" FT MOD_RES 60 FT /note="N6-acetyllysine" 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" 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-acetyllysine" 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 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 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in UFM1); 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 HELIX 26..29 FT /evidence="ECO:0007829|PDB:1TZY" FT HELIX 32..41 FT /evidence="ECO:0007829|PDB:1TZY" FT HELIX 51..76 FT /evidence="ECO:0007829|PDB:1TZY" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:1TZY" FT HELIX 84..93 FT /evidence="ECO:0007829|PDB:1TZY" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:1TZY" SQ SEQUENCE 103 AA; 11367 MW; A9E5DFD3F8B97598 CRC64; MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG //