ID H32_CHICK Reviewed; 136 AA. AC P84229; P02295; P02297; P16105; P17269; P17320; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 162. DE RecName: Full=Histone H3.2; DE AltName: Full=Histone H3 class I; GN Name=H3-I; GN and GN Name=H3-II; GN and GN Name=H3-III; GN and GN Name=H3-IV; GN and GN Name=H3-V; GN and GN Name=H3-VI; GN and GN Name=H3-VII; GN and GN Name=H3-VIII; 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=7078654; DOI=10.1038/297434a0; RA Engel J.D., Sugarman B.J., Dodgson J.B.; RT "A chicken histone H3 gene contains intervening sequences."; RL Nature 297:434-436(1982). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3-II AND H3-III). RX PubMed=1874451; DOI=10.1016/0378-1119(91)90092-p; RA Nakayama T.; RT "Nucleotide sequences of two members of the chicken H3 histone-encoding RT gene family."; RL Gene 102:289-290(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3-IV AND H3-V). RC STRAIN=White leghorn; RX PubMed=1956792; DOI=10.1093/nar/19.22.6327; RA Setoguchi Y., Nakayama T.; RT "Nucleotide sequences of new members (H3-IV and H3-V) of the chicken H3 RT histone-encoding gene family."; RL Nucleic Acids Res. 19:6327-6327(1991). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3-VI; H3-VII AND H3-VIII). 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 [6] RP PROTEIN SEQUENCE OF 2-136. RX PubMed=4859525; DOI=10.1111/j.1432-1033.1974.tb03635.x; RA Brandt W.F., von Holt C.; RT "The determination of the primary structure of histone F3 from chicken RT erythrocytes by automatic Edman degradation. 2. Sequence analysis of RT histone F3."; RL Eur. J. Biochem. 46:419-429(1974). RN [7] RP METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-28; LYS-37 AND LYS-80, RP ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=12123664; DOI=10.1006/abio.2002.5719; RA Zhang K., Tang H., Huang L., Blankenship J.W., Jones P.R., Xiang F., RA Yau P.M., Burlingame A.L.; RT "Identification of acetylation and methylation sites of histone H3 from RT chicken erythrocytes by high-accuracy matrix-assisted laser desorption RT ionization-time-of-flight, matrix-assisted laser desorption ionization- RT postsource decay, and nanoelectrospray ionization tandem mass RT spectrometry."; RL Anal. Biochem. 306:259-269(2002). RN [8] RP INTERACTION WITH HMGB1. RX PubMed=19102706; DOI=10.1021/bi8013449; RA Kawase T., Sato K., Ueda T., Yoshida M.; RT "Distinct domains in HMGB1 are involved in specific intramolecular and RT nucleosomal interactions."; RL Biochemistry 47:13991-13996(2008). RN [9] 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 [10] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH H2A; H2B AND H4. 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). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH H2A AND H2B. RX PubMed=12876341; DOI=10.1107/s0907444903011880; RA Chantalat L., Nicholson J.M., Lambert S.J., Reid A.J., Donovan M.J., RA Reynolds C.D., Wood C.M., Baldwin J.P.; RT "Structure of the histone-core octamer in KCl/phosphate crystals at 2.15 A RT resolution."; RL Acta Crystallogr. D 59:1395-1407(2003). 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. Interacts with HMGB1. {ECO:0000269|PubMed:11092917, CC ECO:0000269|PubMed:12876341, ECO:0000269|PubMed:19102706}. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression strongly CC decreases as cell division slows down during the process of CC differentiation. CC -!- PTM: Acetylation is generally linked to gene activation. Acetylation on CC Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 CC (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a CC central role in chromatin structure: localizes at the surface of the CC histone octamer and stimulates transcription, possibly by promoting CC nucleosome instability (By similarity). {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) is linked to gene CC activation. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is CC linked to gene repression and is mutually exclusive with H3 Lys-5 CC methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of CC genes regardless of their transcription state and is enriched on CC inactive promoters, while it is absent on active promoters (By CC similarity). {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 CC (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) CC facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 CC (H3K79me) is associated with DNA double-strand break (DSB) responses CC and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) CC and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys- CC 10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) CC and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and CC acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 CC (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120' CC (By similarity). {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and CC dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) CC by AURKB is crucial for chromosome condensation and cell-cycle CC progression during mitosis and meiosis. In addition phosphorylation at CC Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase CC because it enables the transcription of genes following external CC stimulation, like mitogens, stress, growth factors or UV irradiation CC and result in the activation of genes, such as c-fos and c-jun. CC Phosphorylation at Ser-11 (H3S10ph), which is linked to gene CC activation, prevents methylation at Lys-10 (H3K9me) but facilitates CC acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB CC mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from CC heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an CC essential regulatory mechanism for neoplastic cell transformation. CC Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or CC AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation CC at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic CC transcriptional activation that prevents demethylation of Lys-5 CC (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at CC Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. CC Phosphorylation at Thr-12 (H3T11ph) by PKN1 or isoform M2 of PKM (PKM2) CC is a specific tag for epigenetic transcriptional activation that CC promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. CC Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 CC (HP1 alpha) from chromatin (By similarity). CC {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is CC required for V(D)J recombination. {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine only takes CC place on H3K4me3 and results in gene repression. CC {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Butyrylation of histones marks active promoters and competes with CC histone acetylation. It is present during late spermatogenesis. CC {ECO:0000250|UniProtKB:P68433}. CC -!- PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a CC maximum frequency around the transcription start sites of genes. It CC gives a specific tag for epigenetic transcription activation. CC Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA CC damage promotes chromatin condensation and double-strand breaks (DSBs) CC repair. {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Serine ADP-ribosylation by PARP1 or PARP2 constitutes the primary CC form of ADP-ribosylation of proteins in response to DNA damage. Serine CC ADP-ribosylation at Ser-11 (H3S10ADPr) promotes recruitment of CHD1L. CC H3S10ADPr is mutually exclusive with phosphorylation at Ser-11 CC (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac). CC {ECO:0000250|UniProtKB:P68431}. CC -!- PTM: Serotonylated by TGM2 at Gln-6 (H3Q5ser) during serotonergic CC neuron differentiation (By similarity). H3Q5ser is associated with CC trimethylation of Lys-5 (H3K4me3) and enhances general transcription CC factor IID (TFIID) complex-binding to H3K4me3, thereby facilitating CC transcription (By similarity). {ECO:0000250|UniProtKB:Q71DI3}. CC -!- PTM: Dopaminylated by TGM2 at Gln-6 (H3Q5dop) in ventral tegmental area CC (VTA) neurons (By similarity). H3Q5dop mediates neurotransmission- CC independent role of nuclear dopamine by regulating relapse-related CC transcriptional plasticity in the reward system (By similarity). CC {ECO:0000250|UniProtKB:P84245, ECO:0000250|UniProtKB:Q71DI3}. 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:Q71DI3}. CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X02218; CAA26138.1; -; Genomic_DNA. DR EMBL; J00869; AAA48795.1; ALT_SEQ; Genomic_DNA. DR EMBL; M61154; AAA48796.1; -; Genomic_DNA. DR EMBL; M61155; AAA48797.1; -; Genomic_DNA. DR EMBL; X62291; CAA44180.1; -; Genomic_DNA. DR EMBL; X62292; CAA44181.1; -; Genomic_DNA. DR EMBL; U37577; AAC60003.1; -; Genomic_DNA. DR EMBL; U37578; AAC60004.1; -; Genomic_DNA. DR EMBL; U37579; AAC60005.1; -; Genomic_DNA. DR PIR; S18716; HSCH3. DR RefSeq; NP_001268409.1; NM_001281480.1. DR RefSeq; NP_001268438.1; NM_001281509.2. DR RefSeq; XP_001232833.1; XM_001232832.4. DR RefSeq; XP_001233028.1; XM_001233027.4. DR RefSeq; XP_015144912.1; XM_015289426.1. DR RefSeq; XP_015144926.1; XM_015289440.1. DR RefSeq; XP_416193.2; XM_416193.4. DR PDB; 1EQZ; X-ray; 2.50 A; C/G=1-136. DR PDB; 1HIO; X-ray; 3.10 A; C=44-136. DR PDB; 1HQ3; X-ray; 2.15 A; C/G=1-136. DR PDB; 1TZY; X-ray; 1.90 A; C/G=1-136. DR PDB; 2ARO; X-ray; 2.10 A; C/G=1-136. DR PDB; 2HIO; X-ray; 3.10 A; C=1-136. DR PDB; 3C9K; EM; 20.00 A; C/G=2-136. DR PDB; 7BXT; EM; 4.20 A; A/E=1-64. DR PDB; 7BY0; EM; 4.50 A; A/E=1-64. DR PDBsum; 1EQZ; -. DR PDBsum; 1HIO; -. DR PDBsum; 1HQ3; -. DR PDBsum; 1TZY; -. DR PDBsum; 2ARO; -. DR PDBsum; 2HIO; -. DR PDBsum; 3C9K; -. DR PDBsum; 7BXT; -. DR PDBsum; 7BY0; -. DR AlphaFoldDB; P84229; -. DR EMDB; EMD-1469; -. DR SMR; P84229; -. DR IntAct; P84229; 3. DR STRING; 9031.ENSGALP00000042290; -. DR iPTMnet; P84229; -. DR PaxDb; 9031-ENSGALP00000040958; -. DR Ensembl; ENSGALT00000042655; ENSGALP00000042290; ENSGALG00000027064. DR Ensembl; ENSGALT00000052453; ENSGALP00000044176; ENSGALG00000051325. DR Ensembl; ENSGALT00000056622; ENSGALP00000049375; ENSGALG00000051325. DR Ensembl; ENSGALT00000058115; ENSGALP00000055093; ENSGALG00000038969. DR Ensembl; ENSGALT00000102489; ENSGALP00000069974; ENSGALG00000048231. DR Ensembl; ENSGALT00010029191.1; ENSGALP00010016931.1; ENSGALG00010012169.1. DR Ensembl; ENSGALT00010029379.1; ENSGALP00010017063.1; ENSGALG00010012266.1. DR Ensembl; ENSGALT00010029395.1; ENSGALP00010017073.1; ENSGALG00010012277.1. DR Ensembl; ENSGALT00010029400.1; ENSGALP00010017077.1; ENSGALG00010012277.1. DR Ensembl; ENSGALT00010029534.1; ENSGALP00010017166.1; ENSGALG00010012338.1. DR Ensembl; ENSGALT00010032659.1; ENSGALP00010019354.1; ENSGALG00010013592.1. DR Ensembl; ENSGALT00015023753; ENSGALP00015013889; ENSGALG00015009748. DR Ensembl; ENSGALT00015023810; ENSGALP00015013946; ENSGALG00015009771. DR Ensembl; ENSGALT00015023815; ENSGALP00015013950; ENSGALG00015009771. DR Ensembl; ENSGALT00015023860; ENSGALP00015013996; ENSGALG00015009789. DR Ensembl; ENSGALT00015023862; ENSGALP00015013998; ENSGALG00015009792. DR Ensembl; ENSGALT00015023933; ENSGALP00015014069; ENSGALG00015009818. DR Ensembl; ENSGALT00015023936; ENSGALP00015014071; ENSGALG00015009818. DR GeneID; 100857439; -. DR GeneID; 100858681; -. DR GeneID; 417953; -. DR GeneID; 769852; -. DR GeneID; 770022; -. DR KEGG; gga:100857439; -. DR KEGG; gga:100858681; -. DR KEGG; gga:417953; -. DR KEGG; gga:768333; -. DR KEGG; gga:769809; -. DR KEGG; gga:769852; -. DR KEGG; gga:770022; -. DR CTD; 100857439; -. DR CTD; 100858681; -. DR CTD; 417953; -. DR CTD; 769852; -. DR CTD; 770022; -. DR VEuPathDB; HostDB:geneid_417953; -. DR VEuPathDB; HostDB:geneid_768333; -. DR VEuPathDB; HostDB:geneid_770022; -. DR VEuPathDB; HostDB:LOC100857439; -. DR VEuPathDB; HostDB:LOC121106438; -. DR VEuPathDB; HostDB:LOC121110383; -. DR VEuPathDB; HostDB:LOC769852; -. DR eggNOG; KOG1745; Eukaryota. DR GeneTree; ENSGT01100000263559; -. DR HOGENOM; CLU_078295_4_0_1; -. DR InParanoid; P84229; -. DR OMA; ANDCAIH; -. DR OrthoDB; 4405952at2759; -. DR PhylomeDB; P84229; -. DR TreeFam; TF314241; -. DR Reactome; R-GGA-1266695; Interleukin-7 signaling. DR Reactome; R-GGA-212300; PRC2 methylates histones and DNA. DR Reactome; R-GGA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-GGA-3214847; HATs acetylate histones. DR Reactome; R-GGA-3247509; Chromatin modifying enzymes. 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-68616; Assembly of the ORC complex at the origin of replication. 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 Reactome; R-GGA-983231; Factors involved in megakaryocyte development and platelet production. DR EvolutionaryTrace; P84229; -. DR PRO; PR:P84229; -. DR Proteomes; UP000000539; Chromosome 1. DR Bgee; ENSGALG00000027064; Expressed in liver and 11 other cell types or tissues. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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 Gene3D; 1.10.20.10; Histone, subunit A; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_H2A/H2B/H3. DR InterPro; IPR000164; Histone_H3/CENP-A. DR PANTHER; PTHR11426; HISTONE H3; 1. DR PANTHER; PTHR11426:SF274; HISTONE H3.1T; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00622; HISTONEH3. DR SMART; SM00428; H3; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00322; HISTONE_H3_1; 1. DR PROSITE; PS00959; HISTONE_H3_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Chromosome; Citrullination; KW Direct protein sequencing; DNA-binding; Hydroxylation; Lipoprotein; KW Methylation; Nucleosome core; Nucleus; Palmitate; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:4859525" FT CHAIN 2..136 FT /note="Histone H3.2" FT /id="PRO_0000221260" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 37..38 FT /note="Involved in HMGB1-binding" FT MOD_RES 3 FT /note="Asymmetric dimethylarginine; by PRMT6; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 3 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 4 FT /note="Phosphothreonine; by HASPIN" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 5 FT /note="Allysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 5 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 5 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 5 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 5 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 5 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 5 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 6 FT /note="5-glutamyl dopamine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 6 FT /note="5-glutamyl serotonin; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 7 FT /note="Phosphothreonine; by PKC" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 9 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 9 FT /note="Symmetric dimethylarginine; by PRMT5; alternate" FT /evidence="ECO:0000250" FT MOD_RES 10 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 10 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 10 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 10 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 10 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 10 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 11 FT /note="ADP-ribosylserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 11 FT /note="Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, FT RPS6KA4 and RPS6KA5" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 12 FT /note="Phosphothreonine; by PKC" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 15 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 15 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 15 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 15 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 15 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84228" FT MOD_RES 18 FT /note="Asymmetric dimethylarginine; by CARM1; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 18 FT /note="Citrulline; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 19 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 19 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 19 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 19 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 19 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 19 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 19 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 24 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 24 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 24 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68433" FT MOD_RES 24 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 24 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 24 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 24 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 27 FT /note="Citrulline" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 28 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 28 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000305|PubMed:12123664" FT MOD_RES 29 FT /note="ADP-ribosylserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 29 FT /note="Phosphoserine; alternate; by AURKB, AURKC and FT RPS6KA5" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 37 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 37 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 37 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 37 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 37 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000305|PubMed:12123664" FT MOD_RES 38 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 42 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 57 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84228" FT MOD_RES 57 FT /note="N6-methyllysine; by EHMT2; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 57 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84228" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 65 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 65 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 80 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84228" FT MOD_RES 80 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 80 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 80 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 80 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 80 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 80 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:12123664" FT MOD_RES 80 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P84228" FT MOD_RES 81 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P84243" FT MOD_RES 108 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 116 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 116 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 123 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68431" FT MOD_RES 123 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 123 FT /note="N6-glutaryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 123 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT MOD_RES 123 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT LIPID 111 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q71DI3" FT STRAND 34..37 FT /evidence="ECO:0007829|PDB:1EQZ" FT HELIX 44..57 FT /evidence="ECO:0007829|PDB:1TZY" FT HELIX 65..79 FT /evidence="ECO:0007829|PDB:1TZY" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:1EQZ" FT HELIX 87..114 FT /evidence="ECO:0007829|PDB:1TZY" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:1TZY" FT HELIX 122..131 FT /evidence="ECO:0007829|PDB:1TZY" SQ SEQUENCE 136 AA; 15388 MW; 6FD8508EA50A0EEC CRC64; MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA //