P84243 (H33_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H3.3

Gene names

Name:	H3F3A
Synonyms:	H3.3A, H3F3
ORF Names:	PP781
AND
Name:	H3F3B
Synonyms:	H3.3B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Ref.14 Ref.18 Ref.22
Subunit structure	The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Interacts with HIRA, a chaperone required for its incorporation into nucleosomes. Ref.14
Subcellular location	Nucleus. Chromosome.
Developmental stage	Expressed throughout the cell cycle independently of DNA synthesis.
Post-translational modification	Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription. Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters. Specifically enriched in modifications associated with active chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me), which are linked to gene repression, are underrepresented. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication. Ref.8 Ref.9 Ref.11 Ref.15 Ref.16 Ref.17 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.38 Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin. Phosphorylation on Ser-32 (H3S31ph) is specific to regions bordering centromeres in metaphase chromosomes. Ref.9 Ref.10 Ref.12 Ref.13 Ref.19 Ref.20 Ref.21 Ref.31 Ref.32 Ref.35 Ref.36 Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination By similarity. Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (Ref.39). Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. Ref.37
Sequence similarities	Belongs to the histone H3 family.
Sequence caution	The sequence CAH73371.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Citrullination Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome nucleosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 136

135

Histone H3.3

PRO_0000221247

Amino acid modifications

Modified residue

3

1

Asymmetric dimethylarginine; by PRMT6 Ref.26 Ref.29 Ref.30

Modified residue

4

1

Phosphothreonine; by GSG2 Ref.9 Ref.19

Modified residue

5

1

Allysine; alternate

Modified residue

5

1

N6,N6,N6-trimethyllysine; alternate Ref.9 Ref.23 Ref.24 Ref.27

Modified residue

5

1

N6,N6-dimethyllysine; alternate Ref.9 Ref.23 Ref.24 Ref.27

Modified residue

5

1

N6-acetyllysine; alternate Ref.27

Modified residue

5

1

N6-crotonyl-L-lysine; alternate Ref.37

Modified residue

5

1

N6-methyllysine; alternate Ref.9 Ref.23 Ref.24 Ref.27

Modified residue

7

1

Phosphothreonine; by PKC Ref.36

Modified residue

9

1

Citrulline; alternate

Modified residue

9

1

Symmetric dimethylarginine; by PRMT5; alternate By similarity

Modified residue

10

1

N6,N6,N6-trimethyllysine; alternate Ref.8 Ref.9 Ref.11 Ref.23 Ref.24 Ref.27

Modified residue

10

1

N6,N6-dimethyllysine; alternate Ref.8 Ref.9 Ref.11 Ref.23 Ref.24 Ref.27

Modified residue

10

1

N6-acetyllysine; alternate Ref.9 Ref.23 Ref.24 Ref.25 Ref.27

Modified residue

10

1

N6-crotonyl-L-lysine; alternate Ref.37

Modified residue

10

1

N6-methyllysine; alternate Ref.8 Ref.9 Ref.11 Ref.23 Ref.24 Ref.27

Modified residue

11

1

Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.9 Ref.10 Ref.12 Ref.13 Ref.19 Ref.21

Modified residue

12

1

Phosphothreonine; by PKC Ref.13 Ref.31

Modified residue

15

1

N6-acetyllysine Ref.8 Ref.9 Ref.23 Ref.25 Ref.27

Modified residue

18

1

Asymmetric dimethylarginine; by CARM1; alternate Ref.15 Ref.17 Ref.25

Modified residue

18

1

Citrulline; alternate

Modified residue

19

1

N6-acetyllysine; alternate Ref.23 Ref.27

Modified residue

19

1

N6-crotonyl-L-lysine; alternate Ref.37

Modified residue

19

1

N6-methyllysine; alternate Ref.23 Ref.27

Modified residue

24

1

N6-acetyllysine; alternate Ref.8 Ref.23 Ref.27

Modified residue

24

1

N6-crotonyl-L-lysine; alternate Ref.37

Modified residue

24

1

N6-methyllysine; alternate Ref.27

Modified residue

28

1

N6,N6,N6-trimethyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.27

Modified residue

28

1

N6,N6-dimethyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.27

Modified residue

28

1

N6-acetyllysine; alternate Ref.23 Ref.27 Ref.34

Modified residue

28

1

N6-crotonyl-L-lysine; alternate Ref.37

Modified residue

28

1

N6-methylated lysine; alternate By similarity

Modified residue

28

1

N6-methyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.27

Modified residue

29

1

Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.9 Ref.10 Ref.12 Ref.19 Ref.20 Ref.21

Modified residue

32

1

Phosphoserine Ref.9 Ref.21

Modified residue

37

1

N6,N6,N6-trimethyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.27

Modified residue

37

1

N6,N6-dimethyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.27

Modified residue

37

1

N6-acetyllysine; alternate Ref.27 Ref.28 Ref.34

Modified residue

37

1

N6-methyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.27

Modified residue

38

1

N6-methyllysine By similarity

Modified residue

42

1

Phosphotyrosine Ref.32

Modified residue

57

1

N6,N6,N6-trimethyllysine; alternate Ref.27 Ref.38

Modified residue

57

1

N6-acetyllysine; alternate Ref.27

Modified residue

57

1

N6-crotonyl-L-lysine; alternate Ref.37

Modified residue

57

1

N6-methyllysine; by EHMT2; alternate Ref.27 Ref.38

Modified residue

58

1

Phosphoserine Ref.35

Modified residue

65

1

N6-methyllysine Ref.23 Ref.27

Modified residue

80

1

N6,N6,N6-trimethyllysine; alternate By similarity

Modified residue

80

1

N6,N6-dimethyllysine; alternate Ref.16 Ref.23 Ref.27

Modified residue

80

1

N6-acetyllysine; alternate Ref.27

Modified residue

80

1

N6-methyllysine; alternate Ref.16 Ref.23 Ref.27

Modified residue

81

1

Phosphothreonine Ref.35

Modified residue

123

1

N6-acetyllysine; alternate By similarity

Modified residue

123

1

N6-methyllysine; alternate Ref.23 Ref.27

Experimental info

Sequence conflict

9

1

R → L in AAH81561. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

136

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Helix

8 – 10

3

Beta strand

45 – 47

3

Helix

49 – 59

11

Helix

65 – 79

15

Beta strand

80 – 82

3

Beta strand

84 – 86

3

Helix

87 – 110

24

Beta strand

118 – 120

3

Helix

122 – 132

11

Sequences

	Sequence		Length	Mass (Da)
	P84243 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5158ED279E6F9E1C	FASTA	136	15,328
	10 20 30 40 50 60 MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE 70 80 90 100 110 120 LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI 130 MPKDIQLARR IRGERA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of a human histone cDNA: evidence that basally expressed histone genes have intervening sequences and encode polyadenylylated mRNAs." Wells D., Kedes L. Proc. Natl. Acad. Sci. U.S.A. 82:2834-2838(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H3F3A). Tissue: Fibroblast.
[2]	"Unusual structure, evolutionary conservation of non-coding sequences and numerous pseudogenes characterize the human H3.3 histone multigene family." Wells D., Hoffman D., Kedes L. Nucleic Acids Res. 15:2871-2889(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H3F3A).
[3]	"The human replacement histone H3.3B gene (H3F3B)." Albig W., Bramlage B., Gruber K., Klobeck H.-G., Kunz J., Doenecke D. Genomics 30:264-272(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3F3B). Tissue: Testis.
[4]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (H3F3B). Tissue: Retina.
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (H3F3A AND H3F3B). Tissue: Bone marrow, Brain, Colon, Eye, Lung, Muscle, Spinal cord, Testis and Uterus.
[8]	"Human spleen histone H3. Isolation and amino acid sequence." Ohe Y., Iwai K. J. Biochem. 90:1205-1211(1981) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, METHYLATION AT LYS-10; LYS-28 AND LYS-37, ACETYLATION AT LYS-15 AND LYS-24.
[9]	"Modifications of human histone H3 variants during mitosis." Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A., Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F. Biochemistry 44:13202-13213(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-41, METHYLATION AT LYS-5; LYS-10; LYS-28 AND LYS-37, PHOSPHORYLATION AT THR-4; SER-11; SER-29 AND SER-32, ACETYLATION AT LYS-10 AND LYS-15, MASS SPECTROMETRY.
[10]	"Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation." Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M., Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M. J. Biol. Chem. 274:25543-25549(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 58-64; 117-120 AND 124-135, PHOSPHORYLATION AT SER-11 AND SER-29.
[11]	"Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins." Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T. Nature 410:116-120(2001) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-10.
[12]	"Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation." Goto H., Yasui Y., Nigg E.A., Inagaki M. Genes Cells 7:11-17(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
[13]	"Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase." Preuss U., Landsberg G., Scheidtmann K.H. Nucleic Acids Res. 31:878-885(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-11 AND THR-12.
[14]	"Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis." Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y. Cell 116:51-61(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIRA.
[15]	"Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1." Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J. J. Biol. Chem. 279:54348-54357(2004) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-18.
[16]	"Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks." Huyen Y., Zgheib O., Ditullio R.A. Jr., Gorgoulis V.G., Zacharatos P., Petty T.J., Sheston E.A., Mellert H.S., Stavridi E.S., Halazonetis T.D. Nature 432:406-411(2004) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-80.
[17]	"Human PAD4 regulates histone arginine methylation levels via demethylimination." Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L., Sonbuchner L.S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G., Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A. Science 306:279-283(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CITRULLINATION AT ARG-9 AND ARG-18, METHYLATION AT ARG-18.
[18]	"Variant histone H3.3 marks promoters of transcriptionally active genes during mammalian cell division." Chow C.-M., Georgiou A., Szutorisz H., Maia e Silva A., Pombo A., Barahona I., Dargelos E., Canzonetta C., Dillon N. EMBO Rep. 6:354-360(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment." Dai J., Sultan S., Taylor S.S., Higgins J.M.G. Genes Dev. 19:472-488(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-4; SER-11 AND SER-29.
[20]	"Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha." Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z. J. Biol. Chem. 280:13545-13553(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-29.
[21]	"Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes." Hake S.B., Garcia B.A., Kauer M., Baker S.P., Shabanowitz J., Hunt D.F., Allis C.D. Proc. Natl. Acad. Sci. U.S.A. 102:6344-6349(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-11; SER-29 AND SER-32, MASS SPECTROMETRY.
[22]	"Histone H3.3 deposition at E2F-regulated genes is linked to transcription." Daury L., Chailleux C., Bonvallet J., Trouche D. EMBO Rep. 7:66-71(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"Expression patterns and post-translational modifications associated with mammalian histone H3 variants." Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G., Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F. J. Biol. Chem. 281:559-568(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, MASS SPECTROMETRY.
[24]	"Mass spectrometric characterization of human histone H3: a bird's eye view." Thomas C.E., Kelleher N.L., Mizzen C.A. J. Proteome Res. 5:240-247(2006) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10, MASS SPECTROMETRY.
[25]	"Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17." Miao F., Li S., Chavez V., Lanting L., Natarajan R. Mol. Endocrinol. 20:1562-1573(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, CITRULLINATION AT ARG-18.
[26]	"PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation." Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y., Hsieh J., Bauer U.M. Genes Dev. 21:3369-3380(2007) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-3 BY PRMT6.
[27]	"Organismal differences in post-translational modifications in histones H3 and H4." Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J., Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F. J. Biol. Chem. 282:7641-7655(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, MASS SPECTROMETRY.
[28]	"Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification." Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D. J. Biol. Chem. 282:7632-7640(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-37.
[29]	"Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive." Guccione E., Bassi C., Casadio F., Martinato F., Cesaroni M., Schuchlautz H., Luescher B., Amati B. Nature 449:933-937(2007) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-3 BY PRMT6.
[30]	"Arginine methylation of the histone H3 tail impedes effector binding." Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J., Richard S., Bedford M.T. J. Biol. Chem. 283:3006-3010(2008) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-3 BY PRMT6.
[31]	"Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation." Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K., Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H., Buettner R., Schule R. Nat. Cell Biol. 10:53-60(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-12.
[32]	"JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin." Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T., Green A.R., Kouzarides T. Nature 461:819-822(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-42.
[33]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[34]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28 AND LYS-37, MASS SPECTROMETRY.
[35]	"Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers." Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M. Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-58 AND THR-81.
[36]	"Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4." Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Gunther T., Buettner R., Schule R. Nature 464:792-796(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-7.
[37]	"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification." Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y. Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract] Cited for: CROTONYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.
[38]	"Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA." Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A., Carey M.F., Grunstein M. Mol. Cell 46:7-17(2012) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-57.
[39]	"Lysyl oxidase-like 2 deaminates lysine 4 in histone H3." Herranz N., Dave N., Millanes-Romero A., Morey L., Diaz V.M., Lorenz-Fonfria V., Gutierrez-Gallego R., Jeronimo C., Di Croce L., Garcia de Herreros A., Peiro S. Mol. Cell 46:369-376(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ALLYSINE AT LYS-5.
+	Additional computationally mapped references.

Web resources

Wikipedia

Histone H3 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M11354 mRNA. Translation: AAA52653.1.
M11353 mRNA. Translation: AAA52654.1.
Z48950 Genomic DNA. Translation: CAA88778.1.
X05855, X05856, X05857 Genomic DNA. Translation: CAA29288.1. Sequence problems.
AF218029 mRNA. Translation: AAG17271.1.
BX537379 mRNA. Translation: CAD97621.1.
AL512343 Genomic DNA. Translation: CAH73371.1. Sequence problems.
AL512343 Genomic DNA. Translation: CAH73372.1.
BC001124 mRNA. Translation: AAH01124.1.
BC006497 mRNA. Translation: AAH06497.1.
BC012813 mRNA. Translation: AAH12813.1.
BC017558 mRNA. Translation: AAH17558.1.
BC029405 mRNA. Translation: AAH29405.1.
BC038989 mRNA. Translation: AAH38989.1.
BC066901 mRNA. No translation available.
BC067757 mRNA. No translation available.
BC081560 mRNA. Translation: AAH81560.1.
BC081561 mRNA. Translation: AAH81561.1.
BC095447 mRNA. Translation: AAH95447.1.
BC108701 mRNA. Translation: AAI08702.1.

IPI

IPI00219038.

PIR

HSHU33. A27501.

RefSeq

NP_002098.1. NM_002107.4.
NP_005315.1. NM_005324.3.

UniGene

Hs.180877.
Hs.533624.
Hs.726012.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L43	NMR	-	A	2-14	[»]
3ASK	X-ray	2.90	P/Q/R	2-14	[»]
3ASL	X-ray	1.41	B	2-12	[»]
3AV2	X-ray	2.80	A/E	1-136	[»]
3JVK	X-ray	1.80	C	13-20	[»]
3MUK	X-ray	1.75	D	22-29	[»]
3MUL	X-ray	1.65	D	13-20	[»]
3QL9	X-ray	0.93	C	2-16	[»]
3QLA	X-ray	1.60	C/F	2-16	[»]
3QLC	X-ray	2.50	C/D	2-16	[»]
4GNE	X-ray	1.47	B	2-8	[»]
4GNF	X-ray	1.55	C	2-16	[»]
4GNG	X-ray	1.73	B/F	2-16	[»]
4GU0	X-ray	3.10	E/F	2-27	[»]
4GUR	X-ray	2.51	C	2-22	[»]
4GUS	X-ray	2.23	C	2-22	[»]
4GY5	X-ray	2.96	E/F	2-18	[»]
4H9N	X-ray	1.95	A	2-136	[»]
4H9O	X-ray	2.05	A	2-136	[»]
4H9P	X-ray	2.20	A	2-136	[»]
4H9Q	X-ray	1.95	A	2-136	[»]
4H9R	X-ray	2.20	A	2-136	[»]
4H9S	X-ray	2.60	A/B	2-136	[»]
4HGA	X-ray	2.80	B	1-136	[»]

ProteinModelPortal

P84243.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40046N.

IntAct

P84243. 18 interactions.

MINT

MINT-4825076.

STRING

9606.ENSP00000254810.

PTM databases

PhosphoSite

P84243.

Proteomic databases

PaxDb

P84243.

PRIDE

P84243.

Protocols and materials databases

DNASU

3020.
3021.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254810; ENSP00000254810; ENSG00000132475.
ENST00000366813; ENSP00000355778; ENSG00000163041.
ENST00000366815; ENSP00000355780; ENSG00000163041.
ENST00000366816; ENSP00000355781; ENSG00000163041.
ENST00000586607; ENSP00000466020; ENSG00000132475.
ENST00000587560; ENSP00000468714; ENSG00000132475.
ENST00000589599; ENSP00000465813; ENSG00000132475.

GeneID

3020.
3021.

KEGG

hsa:3020.
hsa:3021.

UCSC

uc001hpw.3. human.

Organism-specific databases

CTD

3020.
3021.

H-InvDB

HIX0135637.

HGNC

HGNC:4764. H3F3A.
HGNC:4765. H3F3B.

HPA

CAB011481.
CAB037221.
HPA042570.

MIM

601058. gene.
601128. gene.

neXtProt

NX_P84243.

PharmGKB

PA29140.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2036.

HOVERGEN

HBG001172.

InParanoid

P84243.

KO

K11253.

OMA

CCIRGER.

OrthoDB

EOG4V9TS1.

Enzyme and pathway databases

Reactome

REACT_111183. Meiosis.
REACT_116125. Disease.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P84243.

Bgee

P84243.

CleanEx

HS_H3F3A.
HS_H3F3B.

Genevestigator

P84243.

GermOnline

ENSG00000132475. Homo sapiens.
ENSG00000163041. Homo sapiens.
ENSG00000196285. Homo sapiens.

Family and domain databases

Gene3D

1.10.20.10. 1 hit.

InterPro

IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]

PANTHER

PTHR11426. PTHR11426. 1 hit.

Pfam

PF00125. Histone. 1 hit.
[Graphical view]

PRINTS

PR00622. HISTONEH3.

SMART

SM00428. H3. 1 hit.
[Graphical view]

SUPFAM

SSF47113. Histone-fold. 1 hit.

PROSITE

PS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P84243.

NextBio

11966.

SOURCE

Search...

Entry information

Entry name

H33_HUMAN

Accession

Primary (citable) accession number: P84243
Secondary accession number(s): P06351 , P33155, Q5VV55, Q5VV56, Q66I33, Q9V3W4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.