H31T_HUMAN
ID H31T_HUMAN Reviewed; 136 AA.
AC Q16695; B2R5K3; Q6FGU4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Histone H3.1t;
DE Short=H3/t;
DE Short=H3t;
DE AltName: Full=H3/g;
DE AltName: Full=Histone H3.4 {ECO:0000312|HGNC:HGNC:4778};
GN Name=H3-4 {ECO:0000312|HGNC:HGNC:4778};
GN Synonyms=H3FT, HIST3H3 {ECO:0000312|HGNC:HGNC:4778};
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 [GENOMIC DNA].
RX PubMed=8834248; DOI=10.1007/bf02267072;
RA Albig W., Ebentheuer J., Klobeck H., Kunz J., Doenecke D.;
RT "A solitary human H3 histone gene on chromosome 1.";
RL Hum. Genet. 97:486-491(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-24, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION AT SER-58 AND THR-81.
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).
RN [11]
RP INTERACTION WITH TONSL; CHAF1A AND CHAF1B.
RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041;
RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y.,
RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L.,
RA Patel D.J., Huang H., Groth A.;
RT "DNAJC9 integrates heat shock molecular chaperones into the histone
RT chaperone network.";
RL Mol. Cell 0:0-0(2021).
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 TONSL; CHAF1A and CHAF1B (PubMed:33857403).
CC {ECO:0000269|PubMed:33857403}.
CC -!- INTERACTION:
CC Q16695; Q96GD4: AURKB; NbExp=8; IntAct=EBI-358900, EBI-624291;
CC Q16695; P45973: CBX5; NbExp=2; IntAct=EBI-358900, EBI-78219;
CC Q16695; P04908: H2AC8; NbExp=2; IntAct=EBI-358900, EBI-358971;
CC Q16695; P16104: H2AX; NbExp=12; IntAct=EBI-358900, EBI-494830;
CC Q16695; Q71DI3: H3C15; NbExp=2; IntAct=EBI-358900, EBI-750650;
CC Q16695; P62805: H4C9; NbExp=3; IntAct=EBI-358900, EBI-302023;
CC Q16695; O60341: KDM1A; NbExp=2; IntAct=EBI-358900, EBI-710124;
CC Q16695; O75164: KDM4A; NbExp=6; IntAct=EBI-358900, EBI-936709;
CC Q16695; P49321-2: NASP; NbExp=6; IntAct=EBI-358900, EBI-7038920;
CC Q16695; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-358900, EBI-10226430;
CC Q16695; Q9UHJ3: SFMBT1; NbExp=4; IntAct=EBI-358900, EBI-747398;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- TISSUE SPECIFICITY: Expressed in testicular cells.
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-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-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: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), 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 Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in
CC inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1)
CC by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required
CC for DNA replication (By 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-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5
CC (HP1 alpha) from chromatin (By similarity).
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Ubiquitinated. {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: 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:P68431}.
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; Z49861; CAA90020.1; -; Genomic_DNA.
DR EMBL; AF531308; AAN39284.1; -; Genomic_DNA.
DR EMBL; CR542013; CAG46810.1; -; mRNA.
DR EMBL; AK312217; BAG35150.1; -; mRNA.
DR EMBL; AL139288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW69877.1; -; Genomic_DNA.
DR EMBL; BC069079; AAH69079.1; -; mRNA.
DR EMBL; BC101837; AAI01838.1; -; mRNA.
DR EMBL; BC101839; AAI01840.1; -; mRNA.
DR CCDS; CCDS1572.1; -.
DR PIR; S57473; S57473.
DR RefSeq; NP_003484.1; NM_003493.2.
DR PDB; 2V1D; X-ray; 3.10 A; C=2-22.
DR PDB; 2YBP; X-ray; 2.02 A; C/D=31-42.
DR PDB; 2YBS; X-ray; 2.32 A; C/D=31-42.
DR PDB; 3A6N; X-ray; 2.70 A; A/E=1-136.
DR PDB; 3T6R; X-ray; 1.95 A; D=2-8.
DR PDB; 4V2V; X-ray; 2.00 A; C/D=26-30.
DR PDB; 4V2W; X-ray; 1.81 A; C=17-36.
DR PDB; 6OIE; X-ray; 2.08 A; C/D=2-20.
DR PDB; 6WAT; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/Y/Z/a/b/c/d/e/f/g=22-30.
DR PDB; 6WAU; X-ray; 1.75 A; G/H/I/J/K/L=22-33.
DR PDBsum; 2V1D; -.
DR PDBsum; 2YBP; -.
DR PDBsum; 2YBS; -.
DR PDBsum; 3A6N; -.
DR PDBsum; 3T6R; -.
DR PDBsum; 4V2V; -.
DR PDBsum; 4V2W; -.
DR PDBsum; 6OIE; -.
DR PDBsum; 6WAT; -.
DR PDBsum; 6WAU; -.
DR AlphaFoldDB; Q16695; -.
DR SMR; Q16695; -.
DR BioGRID; 113895; 381.
DR ComplexPortal; CPX-2564; Nucleosome, variant H3.1t-H2A.2-H2B.1.
DR DIP; DIP-922N; -.
DR IntAct; Q16695; 167.
DR MINT; Q16695; -.
DR STRING; 9606.ENSP00000355657; -.
DR GlyGen; Q16695; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16695; -.
DR MetOSite; Q16695; -.
DR PhosphoSitePlus; Q16695; -.
DR SwissPalm; Q16695; -.
DR BioMuta; HIST3H3; -.
DR DMDM; 18202512; -.
DR EPD; Q16695; -.
DR jPOST; Q16695; -.
DR MassIVE; Q16695; -.
DR MaxQB; Q16695; -.
DR PaxDb; Q16695; -.
DR PeptideAtlas; Q16695; -.
DR PRIDE; Q16695; -.
DR ProteomicsDB; 61035; -.
DR TopDownProteomics; Q16695; -.
DR Antibodypedia; 34666; 1979 antibodies from 31 providers.
DR DNASU; 8290; -.
DR Ensembl; ENST00000366696.2; ENSP00000355657.2; ENSG00000168148.4.
DR Ensembl; ENST00000644869.3; ENSP00000494070.1; ENSG00000285435.3.
DR GeneID; 8290; -.
DR KEGG; hsa:8290; -.
DR MANE-Select; ENST00000366696.2; ENSP00000355657.2; NM_003493.3; NP_003484.1.
DR UCSC; uc001hsx.1; human.
DR CTD; 8290; -.
DR DisGeNET; 8290; -.
DR GeneCards; H3-4; -.
DR HGNC; HGNC:4778; H3-4.
DR HPA; ENSG00000168148; Tissue enhanced (brain, testis).
DR MIM; 602820; gene.
DR neXtProt; NX_Q16695; -.
DR OpenTargets; ENSG00000168148; -.
DR VEuPathDB; HostDB:ENSG00000168148; -.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244889; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q16695; -.
DR OMA; ACKAYLV; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; Q16695; -.
DR TreeFam; TF314241; -.
DR PathwayCommons; Q16695; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-HSA-110331; Cleavage of the damaged purine.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-171306; Packaging Of Telomere Ends.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-912446; Meiotic recombination.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR SignaLink; Q16695; -.
DR SIGNOR; Q16695; -.
DR BioGRID-ORCS; 8290; 268 hits in 1067 CRISPR screens.
DR EvolutionaryTrace; Q16695; -.
DR GeneWiki; HIST3H3; -.
DR GenomeRNAi; 8290; -.
DR Pharos; Q16695; Tbio.
DR PRO; PR:Q16695; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q16695; protein.
DR Bgee; ENSG00000168148; Expressed in right testis and 64 other tissues.
DR Genevisible; Q16695; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID00086; -.
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.
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..136
FT /note="Histone H3.1t"
FT /id="PRO_0000221248"
FT REGION 1..43
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:0007744|PubMed:19608861"
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:0007744|PubMed:19608861"
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:0007744|PubMed:18691976"
FT MOD_RES 37
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 37
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
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:P68431"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
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:P68431"
FT MOD_RES 57
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 57
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 57
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 57
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 57
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 57
FT /note="N6-methyllysine; by EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 57
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20850016"
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:P68431"
FT MOD_RES 80
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 80
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
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:P68431"
FT MOD_RES 80
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 80
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 80
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20850016"
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:P68431"
FT MOD_RES 116
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
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:P68431"
FT MOD_RES 123
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 123
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 123
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:6OIE"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:3A6N"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:3A6N"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3A6N"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3A6N"
FT HELIX 87..114
FT /evidence="ECO:0007829|PDB:3A6N"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3A6N"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:3A6N"
SQ SEQUENCE 136 AA; 15508 MW; 37375A2C3A377B2B CRC64;
MARTKQTARK STGGKAPRKQ LATKVARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LMREIAQDFK TDLRFQSSAV MALQEACESY LVGLFEDTNL CVIHAKRVTI
MPKDIQLARR IRGERA
