H4_CHICK
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 03-AUG-2022, entry version 156.
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: 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}.
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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 SMR; P62801; -.
DR BioGRID; 679227; 7.
DR IntAct; P62801; 2.
DR STRING; 9031.ENSGALP00000041526; -.
DR PaxDb; P62801; -.
DR Ensembl; ENSGALT00000046737; ENSGALP00000050789; ENSGALG00000047126.
DR Ensembl; ENSGALT00000055350; ENSGALP00000054826; ENSGALG00000050250.
DR Ensembl; ENSGALT00000070686; ENSGALP00000058410; ENSGALG00000037322.
DR Ensembl; ENSGALT00000080967; ENSGALP00000049875; ENSGALG00000042491.
DR Ensembl; ENSGALT00000095438; ENSGALP00000064928; ENSGALG00000048097.
DR Ensembl; ENSGALT00000096775; ENSGALP00000066009; ENSGALG00000053262.
DR Ensembl; ENSGALT00000096855; ENSGALP00000073829; ENSGALG00000053680.
DR GeneID; 100858049; -.
DR GeneID; 100858319; -.
DR GeneID; 417946; -.
DR GeneID; 417950; -.
DR GeneID; 427884; -.
DR GeneID; 770005; -.
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; 64627; -.
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 GeneTree; ENSGT01030000234703; -.
DR GeneTree; ENSGT01050000244867; -.
DR HOGENOM; CLU_109117_2_3_1; -.
DR InParanoid; P62801; -.
DR OMA; QKEHING; -.
DR OrthoDB; 1594208at2759; -.
DR PhylomeDB; P62801; -.
DR Reactome; R-GGA-201722; Formation of the beta-catenin:TCF transactivating complex.
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-3214815; HDACs deacetylate histones.
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-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-GGA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-GGA-5693607; Processing of DNA double-strand break ends.
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 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: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 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-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-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
