H2A2A_MOUSE
ID H2A2A_MOUSE Reviewed; 130 AA.
AC Q6GSS7; P20670; Q811M3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Histone H2A type 2-A;
DE AltName: Full=H2a-614;
DE AltName: Full=H2a-615;
DE AltName: Full=Histone H2A.2;
GN Name=Hist2h2aa1;
GN and
GN Name=Hist2h2aa2;
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].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=2587235; DOI=10.1093/nar/17.21.8876;
RA Hurt M.M., Chodchoy N., Marzluff W.F.;
RT "The mouse histone H2a.2 gene from chromosome 3.";
RL Nucleic Acids Res. 17:8876-8876(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=8858345; DOI=10.1101/gr.6.8.702;
RA Wang Z.-F., Tisovec R., Debry R.W., Frey M.R., Matera A.G., Marzluff W.F.;
RT "Characterization of the 55-kb mouse histone gene cluster on chromosome
RT 3.";
RL Genome Res. 6:702-714(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=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 [6]
RP PHOSPHORYLATION AT SER-2, AND ACETYLATION AT SER-2 AND LYS-6.
RX PubMed=7217105; DOI=10.1016/s0021-9258(19)69487-1;
RA Pantazis P., Bonner W.M.;
RT "Quantitative determination of histone modification. H2A acetylation and
RT phosphorylation.";
RL J. Biol. Chem. 256:4669-4675(1981).
RN [7]
RP UBIQUITINATION AT LYS-120.
RX PubMed=15525528; DOI=10.1016/j.devcel.2004.10.005;
RA de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M., Appanah R.,
RA Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H., Brockdorff N.;
RT "Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to
RT heritable gene silencing and X inactivation.";
RL Dev. Cell 7:663-676(2004).
RN [8]
RP UBIQUITINATION AT LYS-120.
RX PubMed=15509584; DOI=10.1074/jbc.c400493200;
RA Fang J., Chen T., Chadwick B., Li E., Zhang Y.;
RT "Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes
RT and is involved in initiation of X inactivation.";
RL J. Biol. Chem. 279:52812-52815(2004).
RN [9]
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 [10]
RP CROTONYLATION AT LYS-37 AND LYS-119.
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 [11]
RP HYDROXYBUTYRYLATION AT LYS-6; LYS-10; LYS-37; LYS-75; LYS-76; LYS-96 AND
RP LYS-119.
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 [12]
RP METHYLATION AT GLN-105.
RX PubMed=24352239; DOI=10.1038/nature12819;
RA Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J.,
RA Nielsen M.L., Kouzarides T.;
RT "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
RT modification.";
RL Nature 505:564-568(2014).
RN [13]
RP HYDROXYBUTYRYLATION AT LYS-6; LYS-37; LYS-120 AND LYS-126.
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).
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: Deiminated on Arg-4 in granulocytes upon calcium entry.
CC {ECO:0000250|UniProtKB:P0C0S8}.
CC -!- PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and
CC RNF2/RING2 complex gives a specific tag for epigenetic transcriptional
CC repression and participates in X chromosome inactivation of female
CC mammals. It is involved in the initiation of both imprinted and random
CC X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome
CC chromatin. Ubiquitination of H2A functions downstream of methylation of
CC 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be
CC induced by ultraviolet and may be involved in DNA repair. Following DNA
CC double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63'
CC linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases
CC RNF8 and RNF168, leading to the recruitment of repair proteins to sites
CC of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and
CC H2AK15Ub, respectively) in response to DNA damage is initiated by
CC RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-
CC linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to
CC extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and
CC ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and
CC H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8,
CC ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528,
CC ECO:0000269|PubMed:24352239}.
CC -!- PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis.
CC Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses
CC transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by
CC RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is
CC present in the regulatory region of many tumor suppresor genes and
CC down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8}.
CC -!- PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may
CC play a crucial role in the germ-cell lineage.
CC {ECO:0000269|PubMed:16699504}.
CC -!- PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is
CC specifically dedicated to polymerase I. It is present at 35S ribosomal
CC DNA locus and impairs binding of the FACT complex.
CC {ECO:0000269|PubMed:24352239}.
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: Hydroxybutyrylation of histones is induced by starvation.
CC {ECO:0000269|PubMed:27105115}.
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:P0C0S5}.
CC -!- SIMILARITY: Belongs to the histone H2A 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; X16148; CAA34273.1; -; Genomic_DNA.
DR EMBL; U62674; AAB04770.1; -; Genomic_DNA.
DR EMBL; AY158924; AAO06234.1; -; Genomic_DNA.
DR EMBL; AY158925; AAO06235.1; -; Genomic_DNA.
DR EMBL; AY158953; AAO06263.1; -; Genomic_DNA.
DR EMBL; AK002725; BAB22310.1; -; mRNA.
DR EMBL; AK006728; BAB24717.1; -; mRNA.
DR EMBL; BC010564; AAH10564.3; -; mRNA.
DR EMBL; BC062255; AAH62255.1; -; mRNA.
DR EMBL; BC089519; AAH89519.1; -; mRNA.
DR CCDS; CCDS57241.1; -.
DR CCDS; CCDS57242.1; -.
DR PIR; S06742; S06742.
DR RefSeq; NP_038577.1; NM_013549.2.
DR RefSeq; NP_835584.1; NM_178212.3.
DR AlphaFoldDB; Q6GSS7; -.
DR SMR; Q6GSS7; -.
DR BioGRID; 200310; 4.
DR IntAct; Q6GSS7; 1.
DR STRING; 10090.ENSMUSP00000077814; -.
DR iPTMnet; Q6GSS7; -.
DR PhosphoSitePlus; Q6GSS7; -.
DR SwissPalm; Q6GSS7; -.
DR jPOST; Q6GSS7; -.
DR MaxQB; Q6GSS7; -.
DR PaxDb; Q6GSS7; -.
DR PRIDE; Q6GSS7; -.
DR Antibodypedia; 73310; 87 antibodies from 15 providers.
DR DNASU; 15267; -.
DR Ensembl; ENSMUST00000074976; ENSMUSP00000100581; ENSMUSG00000063954.
DR Ensembl; ENSMUST00000078756; ENSMUSP00000077814; ENSMUSG00000064220.
DR GeneID; 15267; -.
DR GeneID; 319192; -.
DR KEGG; mmu:15267; -.
DR KEGG; mmu:319192; -.
DR UCSC; uc008qml.3; mouse.
DR CTD; 723790; -.
DR CTD; 8337; -.
DR MGI; MGI:96097; Hist2h2aa1.
DR MGI; MGI:2448283; Hist2h2aa2.
DR VEuPathDB; HostDB:ENSMUSG00000063954; -.
DR VEuPathDB; HostDB:ENSMUSG00000064220; -.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT00940000156302; -.
DR HOGENOM; CLU_062828_3_1_1; -.
DR InParanoid; Q6GSS7; -.
DR OMA; MPNIHQT; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; Q6GSS7; -.
DR TreeFam; TF300137; -.
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-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-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-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-5689901; Metalloprotease DUBs.
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-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; 15267; 7 hits in 37 CRISPR screens.
DR BioGRID-ORCS; 319192; 9 hits in 33 CRISPR screens.
DR ChiTaRS; Hist2h2aa1; mouse.
DR ChiTaRS; Hist2h2aa2; mouse.
DR PRO; PR:Q6GSS7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6GSS7; protein.
DR Bgee; ENSMUSG00000063954; Expressed in white adipose tissue and 67 other tissues.
DR ExpressionAtlas; Q6GSS7; baseline.
DR Genevisible; Q6GSS7; MM.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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; NAS:UniProtKB.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR032458; Histone_H2A_CS.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 1: Evidence at protein level;
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:0000269|PubMed:7217105"
FT CHAIN 2..130
FT /note="Histone H2A type 2-A"
FT /id="PRO_0000055233"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:7217105"
FT MOD_RES 2
FT /note="Phosphoserine; by RPS6KA5"
FT /evidence="ECO:0000269|PubMed:7217105"
FT MOD_RES 4
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 4
FT /note="Symmetric dimethylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000305|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:0000269|PubMed:7217105"
FT MOD_RES 10
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 10
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 10
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6FI13"
FT MOD_RES 37
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 37
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 37
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 75
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 76
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 96
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 96
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 96
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6FI13"
FT MOD_RES 100
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 105
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:24352239"
FT MOD_RES 119
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 119
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 119
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 120
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 120
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 120
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 121
FT /note="Phosphothreonine; by DCAF1"
FT /evidence="ECO:0000250|UniProtKB:Q6FI13"
FT MOD_RES 126
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 126
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT MOD_RES 126
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q6FI13"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q6FI13"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:15509584,
FT ECO:0000269|PubMed:15525528"
SQ SEQUENCE 130 AA; 14095 MW; 53AEDC6CE3FE8317 CRC64;
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
TESHHKAKGK
