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H4_MACFA
ID   H4_MACFA                Reviewed;         103 AA.
AC   Q4R362;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Histone H4;
GN   ORFNames=QtsA-19327;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 {ECO:0000250}. Chromosome {ECO:0000250}.
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: 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; AB179406; BAE02457.1; -; mRNA.
DR   RefSeq; XP_005553865.1; XM_005553808.2.
DR   RefSeq; XP_005553874.1; XM_005553817.2.
DR   RefSeq; XP_005553915.1; XM_005553858.2.
DR   RefSeq; XP_005595820.1; XM_005595763.2.
DR   RefSeq; XP_015285901.1; XM_015430415.1.
DR   RefSeq; XP_015300301.1; XM_015444815.1.
DR   RefSeq; XP_015305257.1; XM_015449771.1.
DR   RefSeq; XP_015305258.1; XM_015449772.1.
DR   RefSeq; XP_015305274.1; XM_015449788.1.
DR   RefSeq; XP_015305275.1; XM_015449789.1.
DR   RefSeq; XP_015305282.1; XM_015449796.1.
DR   AlphaFoldDB; Q4R362; -.
DR   SMR; Q4R362; -.
DR   STRING; 9541.XP_005553801.1; -.
DR   PRIDE; Q4R362; -.
DR   Ensembl; ENSMFAT00000073932; ENSMFAP00000060160; ENSMFAG00000047801.
DR   Ensembl; ENSMFAT00000076138; ENSMFAP00000050616; ENSMFAG00000059817.
DR   Ensembl; ENSMFAT00000084708; ENSMFAP00000054204; ENSMFAG00000049183.
DR   Ensembl; ENSMFAT00000087807; ENSMFAP00000061761; ENSMFAG00000059848.
DR   Ensembl; ENSMFAT00000088574; ENSMFAP00000062404; ENSMFAG00000055044.
DR   Ensembl; ENSMFAT00000092399; ENSMFAP00000059355; ENSMFAG00000051323.
DR   Ensembl; ENSMFAT00000100177; ENSMFAP00000063504; ENSMFAG00000060595.
DR   Ensembl; ENSMFAT00000101353; ENSMFAP00000046291; ENSMFAG00000064237.
DR   GeneID; 102117606; -.
DR   GeneID; 102119092; -.
DR   GeneID; 102121500; -.
DR   GeneID; 102121517; -.
DR   GeneID; 102132001; -.
DR   GeneID; 102136865; -.
DR   GeneID; 102137230; -.
DR   GeneID; 102138137; -.
DR   GeneID; 102138275; -.
DR   GeneID; 107129595; -.
DR   GeneID; 107129596; -.
DR   KEGG; mcf:102121500; -.
DR   KEGG; mcf:102121517; -.
DR   KEGG; mcf:102132001; -.
DR   KEGG; mcf:102138137; -.
DR   KEGG; mcf:107129595; -.
DR   VEuPathDB; HostDB:ENSMFAG00000004793; -.
DR   VEuPathDB; HostDB:ENSMFAG00000007792; -.
DR   VEuPathDB; HostDB:ENSMFAG00000009138; -.
DR   VEuPathDB; HostDB:ENSMFAG00000010779; -.
DR   VEuPathDB; HostDB:ENSMFAG00000010981; -.
DR   VEuPathDB; HostDB:ENSMFAG00000011190; -.
DR   VEuPathDB; HostDB:ENSMFAG00000013334; -.
DR   VEuPathDB; HostDB:ENSMFAG00000029079; -.
DR   VEuPathDB; HostDB:ENSMFAG00000030750; -.
DR   VEuPathDB; HostDB:ENSMFAG00000030781; -.
DR   VEuPathDB; HostDB:ENSMFAG00000030786; -.
DR   VEuPathDB; HostDB:ENSMFAG00000030821; -.
DR   VEuPathDB; HostDB:ENSMFAG00000033838; -.
DR   VEuPathDB; HostDB:ENSMFAG00000037475; -.
DR   eggNOG; KOG3467; Eukaryota.
DR   GeneTree; ENSGT01030000234703; -.
DR   GeneTree; ENSGT01050000244867; -.
DR   OrthoDB; 1594208at2759; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Proteomes; UP000233100; Chromosome 4.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   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   3: Inferred from homology;
KW   Acetylation; Chromosome; Citrullination; DNA-binding; Hydroxylation;
KW   Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62803"
FT   CHAIN           2..103
FT                   /note="Histone H4"
FT                   /id="PRO_0000307386"
FT   DNA_BIND        17..21
FT                   /evidence="ECO:0000250"
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:P62803"
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"
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"
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"
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:0000250|UniProtKB:P62803"
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"
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:P62803"
FT   MOD_RES         21
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62803"
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"
SQ   SEQUENCE   103 AA;  11367 MW;  A9E5DFD3F8B97598 CRC64;
     MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
     VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG
 
 
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