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Q71DI3 (H32_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3.2
Alternative name(s):
Histone H3/m
Histone H3/o
Gene names
Name:HIST2H3A
AND
Name:HIST2H3C
Synonyms:H3F2, H3FM
AND
Name:HIST2H3D
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

Core component of nucleosome. 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.

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. During nucleosome assembly the chaperone ASF1A interacts with the histone H3-H4 heterodimer.

Subcellular location

Nucleus. Chromosome.

Developmental stage

Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.

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.5 Ref.16 Ref.18 Ref.19 Ref.22 Ref.23 Ref.27 Ref.35

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.

Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. 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) are linked to gene repression. 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.5 Ref.8 Ref.11 Ref.12 Ref.13 Ref.16 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.33

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. Ref.5 Ref.6 Ref.9 Ref.10 Ref.14 Ref.15 Ref.26 Ref.28 Ref.30 Ref.31

Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination By similarity. Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins. Ref.17

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.34).

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.32

Sequence similarities

Belongs to the histone H3 family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 136135Histone H3.2
PRO_0000250357

Amino acid modifications

Modified residue31Asymmetric dimethylarginine; by PRMT6; alternate Ref.21 Ref.24 Ref.25
Modified residue31Citrulline; alternate
Modified residue41Phosphothreonine; by GSG2 Ref.5 Ref.14
Modified residue51Allysine; alternate
Modified residue51N6,N6,N6-trimethyllysine; alternate Ref.16 Ref.22
Modified residue51N6,N6-dimethyllysine; alternate Ref.16 Ref.22
Modified residue51N6-acetyllysine; alternate Ref.22
Modified residue51N6-crotonyllysine; alternate Ref.32
Modified residue51N6-methyllysine; alternate Ref.16 Ref.22
Modified residue71Phosphothreonine; by PKC Ref.31
Modified residue91Citrulline; alternate
Modified residue91Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residue101N6,N6,N6-trimethyllysine; alternate Ref.5 Ref.8 Ref.16 Ref.22
Modified residue101N6,N6-dimethyllysine; alternate Ref.5 Ref.8 Ref.16 Ref.22
Modified residue101N6-acetyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.19 Ref.22
Modified residue101N6-crotonyllysine; alternate Ref.32
Modified residue101N6-methyllysine; alternate Ref.5 Ref.8 Ref.16 Ref.22
Modified residue111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.5 Ref.6 Ref.9 Ref.10 Ref.14
Modified residue121Phosphothreonine; by PKC Ref.10 Ref.26
Modified residue151N6-acetyllysine Ref.5 Ref.16 Ref.18 Ref.19 Ref.22
Modified residue181Asymmetric dimethylarginine; by CARM1; alternate Ref.11 Ref.13 Ref.19
Modified residue181Citrulline; alternate
Modified residue191N6-acetyllysine; alternate Ref.16 Ref.18 Ref.22
Modified residue191N6-crotonyllysine; alternate Ref.32
Modified residue191N6-methyllysine; alternate Ref.16 Ref.22
Modified residue241N6-acetyllysine; alternate Ref.16 Ref.18 Ref.22
Modified residue241N6-crotonyllysine; alternate Ref.32
Modified residue241N6-methyllysine; alternate Ref.22
Modified residue271Citrulline
Modified residue281N6,N6,N6-trimethyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.22
Modified residue281N6,N6-dimethyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.22
Modified residue281N6-acetyllysine; alternate Ref.16 Ref.18 Ref.22
Modified residue281N6-crotonyllysine; alternate Ref.32
Modified residue281N6-methyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.22
Modified residue291Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.5 Ref.6 Ref.9 Ref.14 Ref.15
Modified residue371N6,N6,N6-trimethyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.22
Modified residue371N6,N6-dimethyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.22
Modified residue371N6-acetyllysine; alternate Ref.22 Ref.23
Modified residue371N6-methyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.22
Modified residue381N6-methyllysine By similarity
Modified residue421Phosphotyrosine Ref.28
Modified residue571N6,N6,N6-trimethyllysine; alternate Ref.22 Ref.33
Modified residue571N6-acetyllysine; alternate Ref.22
Modified residue571N6-crotonyllysine; alternate Ref.32
Modified residue571N6-methyllysine; by EHMT2; alternate Ref.22 Ref.33
Modified residue581Phosphoserine Ref.30
Modified residue651N6-methyllysine Ref.16 Ref.22
Modified residue801N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue801N6,N6-dimethyllysine; alternate Ref.12 Ref.16 Ref.18 Ref.22
Modified residue801N6-acetyllysine; alternate Ref.22
Modified residue801N6-methyllysine; alternate Ref.12 Ref.16 Ref.18 Ref.22
Modified residue811Phosphothreonine Ref.30
Modified residue1081Phosphothreonine Ref.29
Modified residue1161N6-acetyllysine Ref.27
Modified residue1231N6-acetyllysine; alternate Ref.27 Ref.35
Modified residue1231N6-methyllysine; alternate Ref.16 Ref.22

Natural variations

Natural variant911M → T.
Corresponds to variant rs2664732 [ dbSNP | Ensembl ].
VAR_059313
Natural variant1281A → V.
Corresponds to variant rs2664731 [ dbSNP | Ensembl ].
VAR_059314

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q71DI3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6FD8508EA50A0EEC

FASTA13615,388
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE 

        70         80         90        100        110        120 
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI 

       130 
MPKDIQLARR IRGERA 

« Hide

References

« Hide 'large scale' references
[1]"The human and mouse replication-dependent histone genes."
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Functional characterization of a human histone gene cluster duplication."
Braastad C.D., Hovhannisyan H., van Wijnen A.J., Stein J.L., Stein G.S.
Gene 342:35-40(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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].
[4]"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].
[5]"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-10; LYS-28 AND LYS-37, PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 AND LYS-15, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"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.
[7]"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.
Tissue: Spleen.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage."
Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., Zhang Y.
Mol. Cell 22:383-394(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[18]"Quantitative proteomic analysis of post-translational modifications of human histones."
Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., Grauslund M., Hansen A.M., Jensen O.N.
Mol. Cell. Proteomics 5:1314-1325(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION AT LYS-28; LYS-37 AND LYS-80, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights."
Agez M., Chen J., Guerois R., van Heijenoort C., Thuret J.-Y., Mann C., Ochsenbein F.
Structure 15:191-199(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 121-136 IN COMPLEX WITH ASF1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF531305 Genomic DNA. No translation available.
AF531307 Genomic DNA. Translation: AAN39283.1.
AY648851 Genomic DNA. Translation: AAT68254.1.
AL591493 Genomic DNA. Translation: CAI12559.1.
AL591493 Genomic DNA. Translation: CAI12561.1.
AL591493 Genomic DNA. Translation: CAI12566.1.
BC074969 mRNA. Translation: AAH74969.2.
BC130635 mRNA. Translation: AAI30636.1.
BC130637 mRNA. Translation: AAI30638.1.
CCDSCCDS30848.1.
CCDS30850.1.
CCDS41388.1.
RefSeqNP_001005464.1. NM_001005464.2.
NP_001116847.1. NM_001123375.2.
NP_066403.2. NM_021059.2.
UniGeneHs.647745.
Hs.706618.
Hs.712062.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IIJNMR-B121-136[»]
2X4WX-ray1.50B23-43[»]
2X4XX-ray1.85B/D/F/H23-43[»]
2X4YX-ray1.70B/D/F/H/J/L/N/P23-43[»]
3AV1X-ray2.50A/E1-136[»]
3DB3X-ray2.40B7-12[»]
3MO8X-ray1.69B31-42[»]
3QO2X-ray2.49P/Q/R/S2-16[»]
3R93X-ray2.06E/F/G/H2-16[»]
4MZFX-ray2.10A2-8[»]
4MZGX-ray1.70A/C2-21[»]
4MZHX-ray2.20B2-10[»]
4OUCX-ray1.90B2-12[»]
ProteinModelPortalQ71DI3.
SMRQ71DI3. Positions 17-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126025. 91 interactions.
130616. 20 interactions.
575920. 3 interactions.
DIPDIP-48606N.
IntActQ71DI3. 8 interactions.
MINTMINT-4828325.
STRING9606.ENSP00000333277.

PTM databases

PhosphoSiteQ71DI3.

Polymorphism databases

DMDM74758899.

Proteomic databases

MaxQBQ71DI3.
PaxDbQ71DI3.
PRIDEQ71DI3.

Protocols and materials databases

DNASU126961.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331491; ENSP00000333277; ENSG00000183598.
ENST00000369158; ENSP00000358154; ENSG00000203811.
ENST00000403683; ENSP00000385479; ENSG00000203852.
ENST00000578851; ENSP00000463798; ENSG00000265133.
ENST00000580481; ENSP00000463420; ENSG00000270263.
ENST00000585113; ENSP00000463995; ENSG00000270827.
GeneID126961.
333932.
653604.
KEGGhsa:126961.
hsa:333932.
hsa:653604.
UCSCuc001esv.3. human.

Organism-specific databases

CTD126961.
333932.
653604.
GeneCardsGC01M149784.
GC01M149812.
GC01P149824.
HGNCHGNC:20505. HIST2H3A.
HGNC:20503. HIST2H3C.
HGNC:25311. HIST2H3D.
HPAHPA042570.
MIM142780. gene.
neXtProtNX_Q71DI3.
PharmGKBPA145148728.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2036.
HOGENOMHOG000155290.
HOVERGENHBG001172.
InParanoidQ71DI3.
KOK11253.
OMAQEASKAY.
OrthoDBEOG7HB5C2.
PhylomeDBQ71DI3.
TreeFamTF314241.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_172623. Chromatin organization.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_71. Gene Expression.

Gene expression databases

BgeeQ71DI3.
CleanExHS_HIST2H3A.
HS_HIST2H3C.
HS_HIST2H3D.
GenevestigatorQ71DI3.

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

ChiTaRSHIST2H3C. human.
EvolutionaryTraceQ71DI3.
GeneWikiHIST2H3C.
NextBio81962.
SOURCESearch...

Entry information

Entry nameH32_HUMAN
AccessionPrimary (citable) accession number: Q71DI3
Secondary accession number(s): A2BDF6, A6NFS4, Q6B053
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 122 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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