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P84243 (H33_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3.3
Gene names
Name:H3F3A
Synonyms:H3.3A, H3F3
ORF Names:PP781
AND
Name:H3F3B
Synonyms:H3.3B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Ref.8 Ref.9 Ref.23 Ref.24 Ref.25 Ref.28 Ref.29 Ref.33 Ref.42

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.28 Ref.30 Ref.31 Ref.40

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.32 Ref.34 Ref.37 Ref.38

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.41).

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.39

Sequence similarities

Belongs to the histone H3 family.

Sequence caution

The sequence CAH73371.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 136135Histone H3.3
PRO_0000221247

Amino acid modifications

Modified residue31Asymmetric dimethylarginine; by PRMT6; alternate Ref.26 Ref.30 Ref.31
Modified residue31Citrulline; alternate
Modified residue41Phosphothreonine; by GSG2 Ref.9 Ref.19
Modified residue51Allysine; alternate
Modified residue51N6,N6,N6-trimethyllysine; alternate Ref.9 Ref.23 Ref.24 Ref.28
Modified residue51N6,N6-dimethyllysine; alternate Ref.9 Ref.23 Ref.24 Ref.28
Modified residue51N6-acetyllysine; alternate Ref.28
Modified residue51N6-crotonyl-L-lysine; alternate Ref.39
Modified residue51N6-methyllysine; alternate Ref.9 Ref.23 Ref.24 Ref.28
Modified residue71Phosphothreonine; by PKC Ref.38
Modified residue91Citrulline; alternate
Modified residue91Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residue101N6,N6,N6-trimethyllysine; alternate Ref.8 Ref.9 Ref.11 Ref.23 Ref.24 Ref.28
Modified residue101N6,N6-dimethyllysine; alternate Ref.8 Ref.9 Ref.11 Ref.23 Ref.24 Ref.28
Modified residue101N6-acetyllysine; alternate Ref.9 Ref.23 Ref.24 Ref.25 Ref.28
Modified residue101N6-crotonyl-L-lysine; alternate Ref.39
Modified residue101N6-methyllysine; alternate Ref.8 Ref.9 Ref.11 Ref.23 Ref.24 Ref.28
Modified residue111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.9 Ref.10 Ref.12 Ref.13 Ref.19 Ref.21
Modified residue121Phosphothreonine; by PKC Ref.13 Ref.32
Modified residue151N6-acetyllysine Ref.8 Ref.9 Ref.23 Ref.25 Ref.28
Modified residue181Asymmetric dimethylarginine; by CARM1; alternate Ref.15 Ref.17 Ref.25
Modified residue181Citrulline; alternate
Modified residue191N6-acetyllysine; alternate Ref.23 Ref.28
Modified residue191N6-crotonyl-L-lysine; alternate Ref.39
Modified residue191N6-methyllysine; alternate Ref.23 Ref.28
Modified residue241N6-acetyllysine; alternate Ref.8 Ref.23 Ref.28
Modified residue241N6-crotonyl-L-lysine; alternate Ref.39
Modified residue241N6-methyllysine; alternate Ref.28
Modified residue271Citrulline
Modified residue281N6,N6,N6-trimethyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.28
Modified residue281N6,N6-dimethyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.28
Modified residue281N6-acetyllysine; alternate Ref.23 Ref.28 Ref.36
Modified residue281N6-crotonyl-L-lysine; alternate Ref.39
Modified residue281N6-methyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.28
Modified residue291Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.9 Ref.10 Ref.12 Ref.19 Ref.20 Ref.21
Modified residue321Phosphoserine Ref.9 Ref.21
Modified residue371N6,N6,N6-trimethyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.28
Modified residue371N6,N6-dimethyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.28
Modified residue371N6-acetyllysine; alternate Ref.28 Ref.29 Ref.36
Modified residue371N6-methyllysine; alternate Ref.8 Ref.9 Ref.23 Ref.28
Modified residue381N6-methyllysine By similarity
Modified residue421Phosphotyrosine Ref.34
Modified residue571N6,N6,N6-trimethyllysine; alternate Ref.28 Ref.40
Modified residue571N6-acetyllysine; alternate Ref.28
Modified residue571N6-crotonyl-L-lysine; alternate Ref.39
Modified residue571N6-methyllysine; by EHMT2; alternate Ref.28 Ref.40
Modified residue581Phosphoserine Ref.37
Modified residue651N6-methyllysine Ref.23 Ref.28
Modified residue801N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue801N6,N6-dimethyllysine; alternate Ref.16 Ref.23 Ref.28
Modified residue801N6-acetyllysine; alternate Ref.28
Modified residue801N6-methyllysine; alternate Ref.16 Ref.23 Ref.28
Modified residue811Phosphothreonine Ref.37
Modified residue1081Phosphothreonine By similarity
Modified residue1161N6-acetyllysine Ref.33
Modified residue1231N6-acetyllysine; alternate Ref.33 Ref.42
Modified residue1231N6-methyllysine; alternate Ref.23 Ref.28

Experimental info

Sequence conflict91R → L in AAH81561. Ref.7

Secondary structure

................... 136
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P84243 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5158ED279E6F9E1C

FASTA13615,328
        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 

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References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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]"Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4."
Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.
Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-3; ARG-9; ARG-18 AND ARG-27.
[28]"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, IDENTIFICATION BY MASS SPECTROMETRY.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding."
Manohar M., Mooney A.M., North J.A., Nakkula R.J., Picking J.W., Edon A., Fishel R., Poirier M.G., Ottesen J.J.
J. Biol. Chem. 284:23312-23321(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-116 AND LYS-123.
[34]"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.
[35]"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.
[36]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"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.
[38]"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.
[39]"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.
[40]"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.
[41]"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.
[42]"Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer."
Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M., Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R., Schneider R.
Cell 152:859-872(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-123.
+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.
PIRHSHU33. A27501.
RefSeqNP_002098.1. NM_002107.4.
NP_005315.1. NM_005324.3.
UniGeneHs.180877.
Hs.533624.
Hs.726012.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L43NMR-A2-14[»]
3ASKX-ray2.90P/Q/R2-14[»]
3ASLX-ray1.41B2-12[»]
3AV2X-ray2.80A/E1-136[»]
3JVKX-ray1.80C13-20[»]
3MUKX-ray1.75D22-29[»]
3MULX-ray1.65D13-20[»]
3QL9X-ray0.93C2-16[»]
3QLAX-ray1.60C/F2-16[»]
3QLCX-ray2.50C/D2-16[»]
4GNEX-ray1.47B2-8[»]
4GNFX-ray1.55C2-16[»]
4GNGX-ray1.73B/F2-16[»]
4GU0X-ray3.10E/F2-27[»]
4GURX-ray2.51C2-22[»]
4GUSX-ray2.23C2-22[»]
4GY5X-ray2.96E/F2-18[»]
4H9NX-ray1.95A2-136[»]
4H9OX-ray2.05A2-136[»]
4H9PX-ray2.20A2-136[»]
4H9QX-ray1.95A2-136[»]
4H9RX-ray2.20A2-136[»]
4H9SX-ray2.60A/B2-136[»]
4HGAX-ray2.80B1-136[»]
4L58X-ray1.48B2-13[»]
4N4IX-ray2.00B20-43[»]
ProteinModelPortalP84243.
SMRP84243. Positions 17-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109272. 73 interactions.
109273. 9 interactions.
DIPDIP-40046N.
IntActP84243. 33 interactions.
MINTMINT-4825076.
STRING9606.ENSP00000254810.

PTM databases

PhosphoSiteP84243.

Polymorphism databases

DMDM55977062.

Proteomic databases

PaxDbP84243.
PRIDEP84243.

Protocols and materials databases

DNASU3020.
3021.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254810; ENSP00000254810; ENSG00000132475.
ENST00000366813; ENSP00000355778; ENSG00000163041.
ENST00000366815; ENSP00000355780; ENSG00000163041.
ENST00000366816; ENSP00000355781; ENSG00000163041.
ENST00000586607; ENSP00000466020; ENSG00000132475.
ENST00000587560; ENSP00000468714; ENSG00000132475.
ENST00000589599; ENSP00000465813; ENSG00000132475.
GeneID3020.
3021.
KEGGhsa:3020.
hsa:3021.
UCSCuc001hpw.3. human.

Organism-specific databases

CTD3020.
3021.
H-InvDBHIX0135637.
HGNCHGNC:4764. H3F3A.
HGNC:4765. H3F3B.
HPACAB011481.
CAB037221.
HPA042570.
MIM601058. gene.
601128. gene.
neXtProtNX_P84243.
PharmGKBPA29140.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2036.
HOVERGENHBG001172.
InParanoidP84243.
KOK11253.
OMAQEATESY.
PhylomeDBP84243.
TreeFamTF314241.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP84243.
BgeeP84243.
CleanExHS_H3F3A.
HS_H3F3B.
GenevestigatorP84243.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]
PANTHERPTHR11426. PTHR11426. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00622. HISTONEH3.
SMARTSM00428. H3. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP84243.
GeneWikiH3F3A.
NextBio11966.
PROP84243.
SOURCESearch...

Entry information

Entry nameH33_HUMAN
AccessionPrimary (citable) accession number: P84243
Secondary accession number(s): P06351 expand/collapse secondary AC list , P33155, Q5VV55, Q5VV56, Q66I33, Q9V3W4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM