H4_MOUSE
ID H4_MOUSE Reviewed; 103 AA.
AC P62806; A0AUM5; A4FUP8; A4QMY0; P02304; P02305; Q0VDL9; Q2M2Q5; Q5T006;
AC Q6PDS7; Q811M0; Q9D0C9; Q9D6Q8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Histone H4;
GN Name=H4c1; Synonyms=Hist1h4a;
GN and
GN Name=H4c2; Synonyms=H4-53, Hist1h4b;
GN and
GN Name=H4c3; Synonyms=H4-12, Hist1h4c;
GN and
GN Name=H4c4; Synonyms=Hist1h4d;
GN and
GN Name=H4c6; Synonyms=Hist1h4f;
GN and
GN Name=H4c8; Synonyms=Hist1h4h;
GN and
GN Name=H4c9; Synonyms=Hist1h4i;
GN and
GN Name=H4c11; Synonyms=Hist1h4j;
GN and
GN Name=H4c12; Synonyms=Hist1h4k;
GN and
GN Name=Hist1h4m;
GN and
GN Name=H4c14; Synonyms=Hist2h4, Hist2h4a;
GN and
GN Name=H4f16; Synonyms=Hist4h4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6276563; DOI=10.1016/0022-2836(81)90426-5;
RA Seiler-Tuyns A., Birnstiel M.L.;
RT "Structure and expression in L-cells of a cloned H4 histone gene of the
RT mouse.";
RL J. Mol. Biol. 151:607-625(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H4C2 AND H4C3).
RX PubMed=2915930; DOI=10.1093/nar/17.2.795;
RA Meier V.S., Boehni R., Schuemperli D.;
RT "Nucleotide sequence of two mouse histone H4 genes.";
RL Nucleic Acids Res. 17:795-795(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H4C1).
RC STRAIN=C57BL/6J;
RX PubMed=8858344; DOI=10.1101/gr.6.8.688;
RA Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F.;
RT "Characterization of the mouse histone gene cluster on chromosome 13: 45
RT histone genes in three patches spread over 1Mb.";
RL Genome Res. 6:688-701(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Franke K., Drabent B., Doenecke D.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H4C1; H4C2; H4C3; H4C4; H4C6; H4C8;
RP H4C9; H4C11; H4C12; HIST1H4M; H4C14 AND H4F16).
RX PubMed=12408966; DOI=10.1006/geno.2002.6850;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, Pancreas, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Brain, Embryo, Eye, Heart, Mammary gland, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP METHYLATION AT LYS-21.
RX PubMed=15145825; DOI=10.1101/gad.300704;
RA Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,
RA Reinberg D., Jenuwein T.;
RT "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at
RT constitutive heterochromatin.";
RL Genes Dev. 18:1251-1262(2004).
RN [10]
RP PHOSPHORYLATION AT SER-2.
RX PubMed=16980586; DOI=10.1101/gad.1457006;
RA Krishnamoorthy T., Chen X., Govin J., Cheung W.L., Dorsey J., Schindler K.,
RA Winter E., Allis C.D., Guacci V., Khochbin S., Fuller M.T., Berger S.L.;
RT "Phosphorylation of histone H4 Ser1 regulates sporulation in yeast and is
RT conserved in fly and mouse spermatogenesis.";
RL Genes Dev. 20:2580-2592(2006).
RN [11]
RP METHYLATION AT ARG-4.
RX PubMed=16699504; DOI=10.1038/ncb1413;
RA Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J.,
RA Kouzarides T., Surani M.A.;
RT "Blimp1 associates with Prmt5 and directs histone arginine methylation in
RT mouse germ cells.";
RL Nat. Cell Biol. 8:623-630(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52 AND TYR-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; TYR-52; THR-81 AND
RP TYR-89, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP CROTONYLATION AT LYS-6; LYS-9 AND LYS-17.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J.,
RA Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation as a
RT new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [16]
RP SUCCINYLATION AT LYS-32; LYS-78; LYS-80 AND LYS-92.
RX PubMed=22389435; DOI=10.1074/mcp.m111.015875;
RA Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT "Lysine succinylation and lysine malonylation in histones.";
RL Mol. Cell. Proteomics 11:100-107(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13; LYS-17 AND
RP LYS-32, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13 AND LYS-17, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [19]
RP HYDROXYBUTYRYLATION AT LYS-6; LYS-9; LYS-13; LYS-17; LYS-32; LYS-45;
RP LYS-60; LYS-78; LYS-80 AND LYS-92.
RX PubMed=24681537; DOI=10.1038/nchembio.1497;
RA Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., Debernardi A.,
RA Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., Allis C.D., Ren B.,
RA Khochbin S., Zhao Y.;
RT "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone
RT mark.";
RL Nat. Chem. Biol. 10:365-370(2014).
RN [20]
RP BUTYRYLATION AT LYS-6; LYS-9 AND LYS-13.
RX PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
RA Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
RA Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
RA Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C., Panne D.,
RA Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
RT "Dynamic competing histone H4 K5K8 acetylation and butyrylation are
RT hallmarks of highly active gene promoters.";
RL Mol. Cell 62:169-180(2016).
RN [21]
RP HYDROXYBUTYRYLATION AT LYS-6; LYS-9 AND LYS-13.
RX PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
RA Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
RA Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
RA Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
RA White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lysine beta-
RT hydroxybutyrylation.";
RL Mol. Cell 62:194-206(2016).
RN [22]
RP ACETYLATION AT LYS-17.
RX PubMed=30279482; DOI=10.1038/s41598-018-32927-9;
RA Kelly R.D.W., Chandru A., Watson P.J., Song Y., Blades M., Robertson N.S.,
RA Jamieson A.G., Schwabe J.W.R., Cowley S.M.;
RT "Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone
RT acetylation and crotonylation in vivo.";
RL Sci. Rep. 8:14690-14690(2018).
RN [23]
RP LACTYLATION AT LYS-9; LYS-13; LYS-32 AND LYS-92.
RX PubMed=31645732; DOI=10.1038/s41586-019-1678-1;
RA Zhang D., Tang Z., Huang H., Zhou G., Cui C., Weng Y., Liu W., Kim S.,
RA Lee S., Perez-Neut M., Ding J., Czyz D., Hu R., Ye Z., He M., Zheng Y.G.,
RA Shuman H.A., Dai L., Ren B., Roeder R.G., Becker L., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lactylation.";
RL Nature 574:575-580(2019).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH H2A-Z; H2B AND H3.
RX PubMed=11101893; DOI=10.1038/81971;
RA Suto R.K., Clarkson M.J., Tremethick D.J., Luger K.;
RT "Crystal structure of a nucleosome core particle containing the variant
RT histone H2A.Z.";
RL Nat. Struct. Biol. 7:1121-1124(2000).
RN [25] {ECO:0007744|PDB:4AU7}
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 18-26 IN COMPLEX WITH KMT5C, AND
RP METHYLATION AT LYS-21.
RX PubMed=24049080; DOI=10.1093/nar/gkt776;
RA Southall S.M., Cronin N.B., Wilson J.R.;
RT "A novel route to product specificity in the Suv4-20 family of histone
RT H4K20 methyltransferases.";
RL Nucleic Acids Res. 42:661-671(2014).
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. Found in a co-chaperone complex with DNJC9, MCM2 and histone H3.3-
CC H4 dimers (By similarity). Within the complex, interacts with DNJC9
CC (via C-terminus); the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P62805, ECO:0000269|PubMed:11101893}.
CC -!- INTERACTION:
CC P62806; Q8CDM1: Atad2; NbExp=2; IntAct=EBI-299632, EBI-2944582;
CC P62806; Q9EQQ9: Oga; NbExp=2; IntAct=EBI-299632, EBI-8321615;
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:0000269|PubMed:15145825, ECO:0000269|PubMed:16699504}.
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) (PubMed:24049080). Monomethylation is performed by
CC KMT5A/SET8 (By similarity). Trimethylation is performed by KMT5B and
CC KMT5C and induces gene silencing (PubMed:24049080). Monomethylated at
CC Lys-13 (H4K12me1) by N6AMT1; H4K12me1 modification is present at the
CC promoters of numerous genes encoding cell cycle regulators (By
CC similarity). {ECO:0000250|UniProtKB:P62805,
CC ECO:0000269|PubMed:24049080}.
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. It is present during late spermatogenesis.
CC {ECO:0000269|PubMed:27105113}.
CC -!- PTM: Hydroxybutyrylation of histones is induced by starvation.
CC {ECO:0000269|PubMed:27105115}.
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.
CC {ECO:0000269|PubMed:21925322}.
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; V00753; CAA24130.1; -; Genomic_DNA.
DR EMBL; X13235; CAA31621.1; -; Genomic_DNA.
DR EMBL; X13236; CAA31622.1; -; Genomic_DNA.
DR EMBL; U62672; AAB04766.1; -; Genomic_DNA.
DR EMBL; Y12290; CAA72967.1; -; Genomic_DNA.
DR EMBL; AY158956; AAO06266.1; -; Genomic_DNA.
DR EMBL; AY158957; AAO06267.1; -; Genomic_DNA.
DR EMBL; AY158958; AAO06268.1; -; Genomic_DNA.
DR EMBL; AY158959; AAO06269.1; -; Genomic_DNA.
DR EMBL; AY158960; AAO06270.1; -; Genomic_DNA.
DR EMBL; AY158961; AAO06271.1; -; Genomic_DNA.
DR EMBL; AY158962; AAO06272.1; -; Genomic_DNA.
DR EMBL; AY158963; AAO06273.1; -; Genomic_DNA.
DR EMBL; AY158964; AAO06274.1; -; Genomic_DNA.
DR EMBL; AY158965; AAO06275.1; -; Genomic_DNA.
DR EMBL; AY158966; AAO06276.1; -; Genomic_DNA.
DR EMBL; AY158967; AAO06277.1; -; Genomic_DNA.
DR EMBL; AK007642; BAB25157.1; -; mRNA.
DR EMBL; AK010085; BAB26692.1; -; mRNA.
DR EMBL; AK011560; BAB27698.1; -; mRNA.
DR EMBL; AK139521; BAE24047.1; -; mRNA.
DR EMBL; AL589651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028550; AAH28550.3; -; mRNA.
DR EMBL; BC052219; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC057955; AAH57955.1; -; mRNA.
DR EMBL; BC058529; AAH58529.2; -; mRNA.
DR EMBL; BC087952; AAH87952.1; -; mRNA.
DR EMBL; BC092144; AAH92144.1; -; mRNA.
DR EMBL; BC115446; AAI15447.1; -; mRNA.
DR EMBL; BC115447; AAI15448.1; -; mRNA.
DR EMBL; BC115451; AAI15452.1; -; mRNA.
DR EMBL; BC115448; AAI15449.1; -; mRNA.
DR EMBL; BC115449; AAI15450.1; -; mRNA.
DR EMBL; BC115450; AAI15451.1; -; mRNA.
DR EMBL; BC117010; AAI17011.1; -; mRNA.
DR EMBL; BC117012; AAI17013.1; -; mRNA.
DR EMBL; BC111813; AAI11814.1; -; mRNA.
DR EMBL; BC119241; AAI19242.1; -; mRNA.
DR EMBL; BC119243; AAI19244.1; -; mRNA.
DR EMBL; BC119611; AAI19612.1; -; mRNA.
DR EMBL; BC119612; AAI19613.1; -; mRNA.
DR EMBL; BC125598; AAI25599.1; -; mRNA.
DR EMBL; BC125600; AAI25601.1; -; mRNA.
DR EMBL; BC132186; AAI32187.1; -; mRNA.
DR EMBL; BC132212; AAI32213.1; -; mRNA.
DR EMBL; BC139809; AAI39810.1; -; mRNA.
DR EMBL; BC152397; AAI52398.1; -; mRNA.
DR CCDS; CCDS26291.1; -.
DR CCDS; CCDS26292.1; -.
DR CCDS; CCDS26300.1; -.
DR CCDS; CCDS26306.1; -.
DR CCDS; CCDS26340.1; -.
DR CCDS; CCDS26345.1; -.
DR CCDS; CCDS26353.1; -.
DR CCDS; CCDS26359.1; -.
DR CCDS; CCDS26366.1; -.
DR CCDS; CCDS26367.1; -.
DR CCDS; CCDS39684.1; -.
DR CCDS; CCDS51002.1; -.
DR CCDS; CCDS56872.1; -.
DR PIR; S03426; S03426.
DR PIR; S03427; S03427.
DR RefSeq; NP_001182350.1; NM_001195421.1.
DR RefSeq; NP_291074.1; NM_033596.3.
DR RefSeq; NP_694813.1; NM_153173.4.
DR RefSeq; NP_783583.1; NM_175652.3.
DR RefSeq; NP_783585.1; NM_175654.2.
DR RefSeq; NP_783586.1; NM_175655.2.
DR RefSeq; NP_783587.1; NM_175656.3.
DR RefSeq; NP_783588.1; NM_175657.2.
DR RefSeq; NP_835499.1; NM_178192.2.
DR RefSeq; NP_835500.1; NM_178193.2.
DR RefSeq; NP_835515.1; NM_178208.2.
DR RefSeq; NP_835582.1; NM_178210.2.
DR RefSeq; NP_835583.1; NM_178211.2.
DR PDB; 1F66; X-ray; 2.60 A; B/F=1-103.
DR PDB; 1U35; X-ray; 3.00 A; B/F=1-103.
DR PDB; 2WP2; X-ray; 2.37 A; P/Q=2-21.
DR PDB; 4AU7; X-ray; 2.07 A; C=18-25.
DR PDB; 4DOW; X-ray; 1.95 A; C/D=15-26.
DR PDB; 5B1L; X-ray; 2.35 A; B/F=1-103.
DR PDB; 5B1M; X-ray; 2.34 A; B/F=1-103.
DR PDB; 5XM0; X-ray; 2.87 A; B/F=1-103.
DR PDB; 5XM1; X-ray; 3.45 A; B/F=1-103.
DR PDB; 7DBH; EM; 3.60 A; B/F=1-103.
DR PDB; 7VBM; EM; 3.40 A; B/F=1-103.
DR PDBsum; 1F66; -.
DR PDBsum; 1U35; -.
DR PDBsum; 2WP2; -.
DR PDBsum; 4AU7; -.
DR PDBsum; 4DOW; -.
DR PDBsum; 5B1L; -.
DR PDBsum; 5B1M; -.
DR PDBsum; 5XM0; -.
DR PDBsum; 5XM1; -.
DR PDBsum; 7DBH; -.
DR PDBsum; 7VBM; -.
DR AlphaFoldDB; P62806; -.
DR SMR; P62806; -.
DR BioGRID; 213404; 4.
DR BioGRID; 220610; 7.
DR BioGRID; 235074; 4.
DR BioGRID; 235075; 9.
DR BioGRID; 235076; 3.
DR BioGRID; 235077; 3.
DR BioGRID; 235078; 3.
DR BioGRID; 235079; 4.
DR BioGRID; 235080; 3.
DR BioGRID; 235942; 15.
DR BioGRID; 236472; 12.
DR BioGRID; 236473; 4.
DR BioGRID; 784565; 3.
DR ComplexPortal; CPX-5705; CENP-A nucleosome complex.
DR ComplexPortal; CPX-5712; Nucleosome, variant H3.1-H2A.2-H2B.1.
DR ComplexPortal; CPX-5713; Nucleosome, variant H3.2-H2A.2-H2B.1.
DR ComplexPortal; CPX-5714; Nucleosome, variant H3.g-H2A.2-H2B.1.
DR ComplexPortal; CPX-5715; Nucleosome, variant H3.1-H2A.Z-H2B.1.
DR ComplexPortal; CPX-5716; Nucleosome, variant H3.1-H2A.V-H2B.1.
DR CORUM; P62806; -.
DR DIP; DIP-45837N; -.
DR IntAct; P62806; 19.
DR MINT; P62806; -.
DR STRING; 10090.ENSMUSP00000085006; -.
DR iPTMnet; P62806; -.
DR MetOSite; P62806; -.
DR PhosphoSitePlus; P62806; -.
DR SwissPalm; P62806; -.
DR CPTAC; non-CPTAC-3425; -.
DR EPD; P62806; -.
DR jPOST; P62806; -.
DR MaxQB; P62806; -.
DR PaxDb; P62806; -.
DR PRIDE; P62806; -.
DR ProteomicsDB; 271127; -.
DR TopDownProteomics; P62806; -.
DR ABCD; P62806; 1 sequenced antibody.
DR Antibodypedia; 23657; 2141 antibodies from 39 providers.
DR Antibodypedia; 70431; 12 antibodies from 7 providers.
DR Antibodypedia; 73583; 121 antibodies from 11 providers.
DR Antibodypedia; 75448; 5 antibodies from 3 providers.
DR Antibodypedia; 76313; 19 antibodies from 5 providers.
DR DNASU; 319156; -.
DR Ensembl; ENSMUST00000087714; ENSMUSP00000085006; ENSMUSG00000067455.
DR Ensembl; ENSMUST00000102964; ENSMUSP00000100029; ENSMUSG00000060093.
DR Ensembl; ENSMUST00000102965; ENSMUSP00000100030; ENSMUSG00000069266.
DR Ensembl; ENSMUST00000102967; ENSMUSP00000100032; ENSMUSG00000060678.
DR Ensembl; ENSMUST00000102968; ENSMUSP00000100033; ENSMUSG00000061482.
DR Ensembl; ENSMUST00000102971; ENSMUSP00000100036; ENSMUSG00000069274.
DR Ensembl; ENSMUST00000102972; ENSMUSP00000100037; ENSMUSG00000060981.
DR Ensembl; ENSMUST00000102977; ENSMUSP00000100042; ENSMUSG00000060639.
DR Ensembl; ENSMUST00000102979; ENSMUSP00000100044; ENSMUSG00000069305.
DR Ensembl; ENSMUST00000102983; ENSMUSP00000100048; ENSMUSG00000064288.
DR Ensembl; ENSMUST00000104941; ENSMUSP00000100546; ENSMUSG00000069306.
DR Ensembl; ENSMUST00000171473; ENSMUSP00000129930; ENSMUSG00000091405.
DR Ensembl; ENSMUST00000179285; ENSMUSP00000136357; ENSMUSG00000096010.
DR GeneID; 100041230; -.
DR GeneID; 319155; -.
DR GeneID; 319156; -.
DR GeneID; 319157; -.
DR GeneID; 319158; -.
DR GeneID; 319159; -.
DR GeneID; 319160; -.
DR GeneID; 319161; -.
DR GeneID; 320332; -.
DR GeneID; 326619; -.
DR GeneID; 326620; -.
DR GeneID; 69386; -.
DR GeneID; 97122; -.
DR KEGG; mmu:100041230; -.
DR KEGG; mmu:319155; -.
DR KEGG; mmu:319156; -.
DR KEGG; mmu:319157; -.
DR KEGG; mmu:319158; -.
DR KEGG; mmu:319159; -.
DR KEGG; mmu:319160; -.
DR KEGG; mmu:319161; -.
DR KEGG; mmu:320332; -.
DR KEGG; mmu:326619; -.
DR KEGG; mmu:326620; -.
DR KEGG; mmu:69386; -.
DR KEGG; mmu:97122; -.
DR UCSC; uc007pre.1; mouse.
DR CTD; 100041230; -.
DR CTD; 319161; -.
DR CTD; 320332; -.
DR CTD; 8294; -.
DR CTD; 8359; -.
DR CTD; 8360; -.
DR CTD; 8361; -.
DR CTD; 8362; -.
DR CTD; 8363; -.
DR CTD; 8364; -.
DR CTD; 8365; -.
DR CTD; 8366; -.
DR CTD; 8370; -.
DR MGI; MGI:2448419; H4c1.
DR MGI; MGI:2448436; H4c11.
DR MGI; MGI:2448439; H4c12.
DR MGI; MGI:2140113; H4c14.
DR MGI; MGI:2448420; H4c2.
DR MGI; MGI:2448421; H4c3.
DR MGI; MGI:2448423; H4c4.
DR MGI; MGI:2448425; H4c6.
DR MGI; MGI:2448427; H4c8.
DR MGI; MGI:2448432; H4c9.
DR MGI; MGI:2448443; H4f16.
DR MGI; MGI:2448441; Hist1h4m.
DR VEuPathDB; HostDB:ENSMUSG00000060093; -.
DR VEuPathDB; HostDB:ENSMUSG00000060639; -.
DR VEuPathDB; HostDB:ENSMUSG00000060678; -.
DR VEuPathDB; HostDB:ENSMUSG00000060981; -.
DR VEuPathDB; HostDB:ENSMUSG00000061482; -.
DR VEuPathDB; HostDB:ENSMUSG00000064288; -.
DR VEuPathDB; HostDB:ENSMUSG00000067455; -.
DR VEuPathDB; HostDB:ENSMUSG00000069266; -.
DR VEuPathDB; HostDB:ENSMUSG00000069274; -.
DR VEuPathDB; HostDB:ENSMUSG00000069305; -.
DR VEuPathDB; HostDB:ENSMUSG00000069306; -.
DR VEuPathDB; HostDB:ENSMUSG00000091405; -.
DR VEuPathDB; HostDB:ENSMUSG00000096010; -.
DR eggNOG; KOG3467; Eukaryota.
DR GeneTree; ENSGT01030000234703; -.
DR GeneTree; ENSGT01050000244867; -.
DR HOGENOM; CLU_109117_2_3_1; -.
DR InParanoid; P62806; -.
DR OMA; QKEHING; -.
DR OrthoDB; 1594208at2759; -.
DR PhylomeDB; P62806; -.
DR Reactome; R-MMU-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-MMU-110331; Cleavage of the damaged purine.
DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR Reactome; R-MMU-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR Reactome; R-MMU-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR Reactome; R-MMU-9670095; Inhibition of DNA recombination at telomere.
DR BioGRID-ORCS; 100041230; 11 hits in 36 CRISPR screens.
DR BioGRID-ORCS; 319155; 7 hits in 69 CRISPR screens.
DR BioGRID-ORCS; 319156; 17 hits in 72 CRISPR screens.
DR BioGRID-ORCS; 319157; 8 hits in 50 CRISPR screens.
DR BioGRID-ORCS; 319158; 7 hits in 36 CRISPR screens.
DR BioGRID-ORCS; 319159; 10 hits in 38 CRISPR screens.
DR BioGRID-ORCS; 319160; 9 hits in 37 CRISPR screens.
DR BioGRID-ORCS; 319161; 13 hits in 33 CRISPR screens.
DR BioGRID-ORCS; 320332; 6 hits in 73 CRISPR screens.
DR BioGRID-ORCS; 326619; 12 hits in 68 CRISPR screens.
DR BioGRID-ORCS; 326620; 12 hits in 50 CRISPR screens.
DR BioGRID-ORCS; 69386; 11 hits in 70 CRISPR screens.
DR BioGRID-ORCS; 97122; 10 hits in 71 CRISPR screens.
DR ChiTaRS; Hist1h4b; mouse.
DR ChiTaRS; Hist1h4d; mouse.
DR ChiTaRS; Hist1h4h; mouse.
DR ChiTaRS; Hist1h4i; mouse.
DR EvolutionaryTrace; P62806; -.
DR PRO; PR:P62806; -.
DR Proteomes; UP000000589; Chromosome 13.
DR Proteomes; UP000000589; Chromosome 3.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P62806; protein.
DR Bgee; ENSMUSG00000060093; Expressed in spermatid and 62 other tissues.
DR ExpressionAtlas; P62806; baseline and differential.
DR Genevisible; P62806; MM.
DR GO; GO:0043505; C:CENP-A containing nucleosome; ISO:MGI.
DR GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISO:MGI.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:MGI.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISO:MGI.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0061644; P:protein localization to CENP-A containing chromatin; IC:ComplexPortal.
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|UniProtKB:P62803"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158329"
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:P62803"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16980586"
FT MOD_RES 4
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:16699504"
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:0000269|PubMed:16699504"
FT MOD_RES 6
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 6
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 6
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 6
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
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:0000269|PubMed:24681537"
FT MOD_RES 9
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 9
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 9
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 9
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 9
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
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:0000269|PubMed:24681537"
FT MOD_RES 13
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 13
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 13
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
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:0000269|PubMed:31645732"
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:0000269|PubMed:24681537"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:30279482,
FT ECO:0007744|PubMed:23576753, ECO:0007744|PubMed:23806337"
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:0000269|PubMed:21925322"
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:0000269|PubMed:15145825"
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:0000269|PubMed:24681537"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
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:0000269|PubMed:31645732"
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:0000269|PubMed:22389435"
FT MOD_RES 45
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
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"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:18034455, ECO:0007744|PubMed:21183079"
FT MOD_RES 60
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
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:0000269|PubMed:24681537"
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:0000269|PubMed:22389435"
FT MOD_RES 80
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
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:0000269|PubMed:22389435"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 89
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 92
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
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:0000269|PubMed:31645732"
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:0000269|PubMed:22389435,
FT ECO:0007744|PubMed:23806337"
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 34
FT /note="A -> V (in Ref. 6; BAB26692)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="K -> E (in Ref. 6; BAB27698)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="A -> R (in Ref. 2; CAA31622)"
FT /evidence="ECO:0000305"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:4AU7"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5B1M"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:5B1M"
FT HELIX 51..76
FT /evidence="ECO:0007829|PDB:5B1M"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5B1M"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:5B1M"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5B1M"
SQ SEQUENCE 103 AA; 11367 MW; A9E5DFD3F8B97598 CRC64;
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG
