H3C_HUMAN
ID H3C_HUMAN Reviewed; 135 AA.
AC Q6NXT2; E9P281;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Histone H3.3C;
DE AltName: Full=Histone H3.5 {ECO:0000312|HGNC:HGNC:33164};
GN Name=H3-5 {ECO:0000312|HGNC:HGNC:33164};
GN Synonyms=H3F3C {ECO:0000312|HGNC:HGNC:33164};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Seminiferous tubule;
RX PubMed=21274551; DOI=10.1007/s00412-011-0310-4;
RA Schenk R., Jenke A., Zilbauer M., Wirth S., Postberg J.;
RT "H3.5 is a novel hominid-specific histone H3 variant that is specifically
RT expressed in the seminiferous tubules of human testes.";
RL Chromosoma 120:275-285(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [4]
RP PHOSPHORYLATION AT SER-57 AND THR-80.
RX PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
RA Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F.,
RA Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.;
RT "Quantitative interaction proteomics and genome-wide profiling of
RT epigenetic histone marks and their readers.";
RL Cell 142:967-980(2010).
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. Hominid-specific H3.5/H3F3C
CC preferentially colocalizes with euchromatin, and it is associated with
CC actively transcribed genes. {ECO:0000269|PubMed:21274551}.
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 -!- INTERACTION:
CC Q6NXT2; P46379-2: BAG6; NbExp=3; IntAct=EBI-2868501, EBI-10988864;
CC Q6NXT2; P55212: CASP6; NbExp=3; IntAct=EBI-2868501, EBI-718729;
CC Q6NXT2; P06307: CCK; NbExp=3; IntAct=EBI-2868501, EBI-6624398;
CC Q6NXT2; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-2868501, EBI-21553822;
CC Q6NXT2; Q9UER7: DAXX; NbExp=3; IntAct=EBI-2868501, EBI-77321;
CC Q6NXT2; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-2868501, EBI-12593112;
CC Q6NXT2; Q8WXX5: DNAJC9; NbExp=3; IntAct=EBI-2868501, EBI-2349100;
CC Q6NXT2; Q01658: DR1; NbExp=3; IntAct=EBI-2868501, EBI-750300;
CC Q6NXT2; Q8WUP2: FBLIM1; NbExp=3; IntAct=EBI-2868501, EBI-3864120;
CC Q6NXT2; P28799: GRN; NbExp=3; IntAct=EBI-2868501, EBI-747754;
CC Q6NXT2; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-2868501, EBI-1054873;
CC Q6NXT2; P30519: HMOX2; NbExp=3; IntAct=EBI-2868501, EBI-712096;
CC Q6NXT2; P42858: HTT; NbExp=15; IntAct=EBI-2868501, EBI-466029;
CC Q6NXT2; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-2868501, EBI-6398041;
CC Q6NXT2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2868501, EBI-10975473;
CC Q6NXT2; O14901: KLF11; NbExp=3; IntAct=EBI-2868501, EBI-948266;
CC Q6NXT2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2868501, EBI-21591415;
CC Q6NXT2; Q13449: LSAMP; NbExp=3; IntAct=EBI-2868501, EBI-4314821;
CC Q6NXT2; P49321-2: NASP; NbExp=11; IntAct=EBI-2868501, EBI-7038920;
CC Q6NXT2; P62826: RAN; NbExp=3; IntAct=EBI-2868501, EBI-286642;
CC Q6NXT2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2868501, EBI-396669;
CC Q6NXT2; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2868501, EBI-2623095;
CC Q6NXT2; O76024: WFS1; NbExp=3; IntAct=EBI-2868501, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the seminiferous tubules
CC of testis. {ECO:0000269|PubMed:21274551}.
CC -!- PTM: Acetylation is generally linked to gene activation. Acetylation on
CC Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on
CC Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18
CC (H3R17me). Acetylation at Lys-122 (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:P84243}.
CC -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4
CC impairs methylation and represses transcription.
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked
CC to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by
CC PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3
CC (H3R2me2a) by PRMT6 is linked to gene repression and is mutually
CC exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is
CC present at the 3' of genes regardless of their transcription state and
CC is enriched on inactive promoters, while it is absent on active
CC promoters (By similarity). {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Methylation at Lys-5 (H3K4me) is linked to gene activation.
CC Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3
CC and H4. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked
CC to gene repression. Methylation at Lys-10 (H3K9me) is a specific target
CC for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent
CC phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4.
CC Methylation at Lys-5 (H3K4me) requires preliminary monoubiquitination
CC of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28
CC (H3K27me) are enriched in inactive X chromosome chromatin.
CC Monomethylation at Lys-56 (H3K56me1) by EHMT2/G9A in G1 phase promotes
CC interaction with PCNA and is required for DNA replication (By
CC similarity). {ECO:0000250|UniProtKB:P84243}.
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-41 (H3Y41ph) by JAK2 promotes exclusion of CBX5
CC (HP1 alpha) from chromatin (By similarity).
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated
CC by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and
CC results in gene repression (By similarity).
CC {ECO:0000250|UniProtKB:P84243}.
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: Succinylated. Desuccinylation at Lys-122 (H3K122succ) by SIRT7 in
CC response to DNA damage promotes chromatin condensation and double-
CC strand breaks (DSBs) repair. {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Serine ADP-ribosylation constitutes the primary form of ADP-
CC ribosylation of proteins in response to DNA damage. Serine ADP-
CC ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with
CC phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10
CC (H3K9ac). {ECO:0000250|UniProtKB:P68431}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; HQ873957; ADW85800.1; -; mRNA.
DR EMBL; AC023050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066906; AAH66906.1; -; mRNA.
DR CCDS; CCDS31769.1; -.
DR RefSeq; NP_001013721.2; NM_001013699.2.
DR PDB; 2PUY; X-ray; 1.43 A; E=2-11.
DR PDB; 3KV4; X-ray; 2.19 A; B=2-25.
DR PDB; 4Z5T; X-ray; 2.80 A; A/E=1-135.
DR PDB; 5BWN; X-ray; 1.94 A; B=6-14.
DR PDB; 5BWO; X-ray; 2.38 A; B=6-14.
DR PDB; 5F6K; X-ray; 2.41 A; M=2-10.
DR PDB; 5I3L; X-ray; 1.85 A; C=2-21.
DR PDB; 6OI3; X-ray; 1.66 A; B=2-22.
DR PDBsum; 2PUY; -.
DR PDBsum; 3KV4; -.
DR PDBsum; 4Z5T; -.
DR PDBsum; 5BWN; -.
DR PDBsum; 5BWO; -.
DR PDBsum; 5F6K; -.
DR PDBsum; 5I3L; -.
DR PDBsum; 6OI3; -.
DR AlphaFoldDB; Q6NXT2; -.
DR SMR; Q6NXT2; -.
DR BioGRID; 136289; 59.
DR IntAct; Q6NXT2; 46.
DR MINT; Q6NXT2; -.
DR STRING; 9606.ENSP00000339835; -.
DR iPTMnet; Q6NXT2; -.
DR PhosphoSitePlus; Q6NXT2; -.
DR SwissPalm; Q6NXT2; -.
DR BioMuta; H3F3C; -.
DR DMDM; 116248097; -.
DR EPD; Q6NXT2; -.
DR jPOST; Q6NXT2; -.
DR MassIVE; Q6NXT2; -.
DR MaxQB; Q6NXT2; -.
DR PaxDb; Q6NXT2; -.
DR PeptideAtlas; Q6NXT2; -.
DR PRIDE; Q6NXT2; -.
DR ProteomicsDB; 66771; -.
DR TopDownProteomics; Q6NXT2; -.
DR Antibodypedia; 55173; 31 antibodies from 14 providers.
DR DNASU; 440093; -.
DR Ensembl; ENST00000340398.5; ENSP00000339835.3; ENSG00000188375.5.
DR GeneID; 440093; -.
DR KEGG; hsa:440093; -.
DR MANE-Select; ENST00000340398.5; ENSP00000339835.3; NM_001013699.3; NP_001013721.2.
DR UCSC; uc001rkr.3; human.
DR CTD; 440093; -.
DR DisGeNET; 440093; -.
DR GeneCards; H3-5; -.
DR HGNC; HGNC:33164; H3-5.
DR HPA; ENSG00000188375; Tissue enriched (testis).
DR MIM; 616134; gene.
DR neXtProt; NX_Q6NXT2; -.
DR OpenTargets; ENSG00000188375; -.
DR VEuPathDB; HostDB:ENSG00000188375; -.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244918; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q6NXT2; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; Q6NXT2; -.
DR TreeFam; TF314241; -.
DR PathwayCommons; Q6NXT2; -.
DR SignaLink; Q6NXT2; -.
DR SIGNOR; Q6NXT2; -.
DR BioGRID-ORCS; 440093; 51 hits in 1004 CRISPR screens.
DR ChiTaRS; H3F3C; human.
DR EvolutionaryTrace; Q6NXT2; -.
DR GenomeRNAi; 440093; -.
DR Pharos; Q6NXT2; Tbio.
DR PRO; PR:Q6NXT2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6NXT2; protein.
DR Bgee; ENSG00000188375; Expressed in left testis and 78 other tissues.
DR Genevisible; Q6NXT2; HS.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 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 DNA-binding; Hydroxylation; Methylation; Nucleosome core; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..135
FT /note="Histone H3.3C"
FT /id="PRO_0000253960"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Asymmetric dimethylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 3
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 4
FT /note="Phosphothreonine; by HASPIN"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 5
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 5
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 5
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 6
FT /note="5-glutamyl dopamine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 6
FT /note="5-glutamyl serotonin; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 7
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 9
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 9
FT /note="Symmetric dimethylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 10
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68432"
FT MOD_RES 10
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68432"
FT MOD_RES 10
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 10
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 10
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68432"
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:P68432"
FT MOD_RES 12
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 15
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 15
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68432"
FT MOD_RES 15
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 15
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 15
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 18
FT /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 18
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 19
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 19
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 19
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 19
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 24
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 24
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68432"
FT MOD_RES 24
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 24
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 24
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 27
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68432"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68432"
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:P68431"
FT MOD_RES 28
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68432"
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:P68432"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 37
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 41
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 56
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 56
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 56
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 56
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 56
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 56
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 56
FT /note="N6-methyllysine; by EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 56
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20850016"
FT MOD_RES 64
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 64
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 80
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20850016"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q71DI3"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 115
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 122
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 122
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 122
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 122
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 122
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT VARIANT 39
FT /note="H -> R (in dbSNP:rs3759295)"
FT /id="VAR_068164"
FT CONFLICT 88
FT /note="A -> V (in Ref. 1; ADW85800 and 3; AAH66906)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:2PUY"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:4Z5T"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:4Z5T"
FT HELIX 86..113
FT /evidence="ECO:0007829|PDB:4Z5T"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4Z5T"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:4Z5T"
SQ SEQUENCE 135 AA; 15214 MW; F2941F8A9BC61BB5 CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKST PSTCGVKPHR YRPGTVALRE IRRYQKSTEL
LIRKLPFQRL VREIAQDFNT DLRFQSAAVG ALQEASEAYL VGLLEDTNLC AIHAKRVTIM
PKDIQLARRI RGERA
