Q71DI3 (H32_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	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). 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.20 Ref.21 Ref.23 Ref.24 Ref.31 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.25 Ref.26 Ref.28 Ref.29 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.32). 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.30
Sequence similarities	Belongs to the histone H3 family.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Coding sequence diversity	Polymorphism
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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BPTF	Q12830-4	2	EBI-750650,EBI-4288838

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 H3.2

PRO_0000250357

Amino acid modifications

Modified residue

3

1

Asymmetric dimethylarginine; by PRMT6 Ref.20 Ref.23 Ref.24

Modified residue

4

1

Phosphothreonine; by GSG2 Ref.5 Ref.14

Modified residue

5

1

Allysine; alternate

Modified residue

5

1

N6,N6,N6-trimethyllysine; alternate Ref.16 Ref.21

Modified residue

5

1

N6,N6-dimethyllysine; alternate Ref.16 Ref.21

Modified residue

5

1

N6-acetyllysine; alternate Ref.21

Modified residue

5

1

N6-crotonyl-L-lysine; alternate Ref.30

Modified residue

5

1

N6-methyllysine; alternate Ref.16 Ref.21

Modified residue

7

1

Phosphothreonine; by PKC Ref.29

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.5 Ref.8 Ref.16 Ref.21

Modified residue

10

1

N6,N6-dimethyllysine; alternate Ref.5 Ref.8 Ref.16 Ref.21

Modified residue

10

1

N6-acetyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.19 Ref.21

Modified residue

10

1

N6-crotonyl-L-lysine; alternate Ref.30

Modified residue

10

1

N6-methyllysine; alternate Ref.5 Ref.8 Ref.16 Ref.21

Modified residue

11

1

Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.5 Ref.6 Ref.9 Ref.10 Ref.14

Modified residue

12

1

Phosphothreonine; by PKC Ref.10 Ref.25

Modified residue

15

1

N6-acetyllysine Ref.5 Ref.16 Ref.18 Ref.19 Ref.21

Modified residue

18

1

Asymmetric dimethylarginine; by CARM1; alternate Ref.11 Ref.13 Ref.19

Modified residue

18

1

Citrulline; alternate

Modified residue

19

1

N6-acetyllysine; alternate Ref.16 Ref.18 Ref.21

Modified residue

19

1

N6-crotonyl-L-lysine; alternate Ref.30

Modified residue

19

1

N6-methyllysine; alternate Ref.16 Ref.21

Modified residue

24

1

N6-acetyllysine; alternate Ref.16 Ref.18 Ref.21

Modified residue

24

1

N6-crotonyl-L-lysine; alternate Ref.30

Modified residue

24

1

N6-methyllysine; alternate Ref.21

Modified residue

28

1

N6,N6,N6-trimethyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.21

Modified residue

28

1

N6,N6-dimethyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.21

Modified residue

28

1

N6-acetyllysine; alternate Ref.16 Ref.18 Ref.21

Modified residue

28

1

N6-crotonyl-L-lysine; alternate Ref.30

Modified residue

28

1

N6-methylated lysine; alternate By similarity

Modified residue

28

1

N6-methyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.21

Modified residue

29

1

Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.5 Ref.6 Ref.9 Ref.14 Ref.15

Modified residue

37

1

N6,N6,N6-trimethyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.21

Modified residue

37

1

N6,N6-dimethyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.21

Modified residue

37

1

N6-acetyllysine; alternate Ref.21 Ref.22

Modified residue

37

1

N6-methyllysine; alternate Ref.5 Ref.16 Ref.18 Ref.21

Modified residue

38

1

N6-methyllysine By similarity

Modified residue

42

1

Phosphotyrosine Ref.26

Modified residue

57

1

N6,N6,N6-trimethyllysine; alternate Ref.21 Ref.31

Modified residue

57

1

N6-acetyllysine; alternate Ref.21

Modified residue

57

1

N6-crotonyl-L-lysine; alternate Ref.30

Modified residue

57

1

N6-methyllysine; by EHMT2; alternate Ref.21 Ref.31

Modified residue

58

1

Phosphoserine Ref.28

Modified residue

65

1

N6-methyllysine Ref.16 Ref.21

Modified residue

80

1

N6,N6,N6-trimethyllysine; alternate By similarity

Modified residue

80

1

N6,N6-dimethyllysine; alternate Ref.12 Ref.16 Ref.18 Ref.21

Modified residue

80

1

N6-acetyllysine; alternate Ref.21

Modified residue

80

1

N6-methyllysine; alternate Ref.12 Ref.16 Ref.18 Ref.21

Modified residue

81

1

Phosphothreonine Ref.28

Modified residue

108

1

Phosphothreonine Ref.27

Modified residue

123

1

N6-acetyllysine; alternate By similarity

Modified residue

123

1

N6-methyllysine; alternate Ref.16 Ref.21

Natural variations

Natural variant

91

1

M → T.
Corresponds to variant rs2664732 [ dbSNP | Ensembl ].

VAR_059313

Natural variant

128

1

A → V.
Corresponds to variant rs2664731 [ dbSNP | Ensembl ].

VAR_059314

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

136

Helix Strand Turn

Details...

Helix

26 – 29

4

Turn

39 – 41

3

Helix

46 – 57

12

Helix

65 – 77

13

Helix

87 – 114

28

Beta strand

118 – 120

3

Helix

122 – 131

10

Sequences

	Sequence		Length	Mass (Da)
	Q71DI3 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6FD8508EA50A0EEC	FASTA	136	15,388
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, 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, 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]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.

IPI

IPI00171611.

RefSeq

NP_001005464.1. NM_001005464.2.
NP_001116847.1. NM_001123375.2.
NP_066403.2. NM_021059.2.

UniGene

Hs.647745.
Hs.706618.
Hs.712062.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IIJ	NMR	-	B	123-136	[»]
2X4W	X-ray	1.50	B	23-43	[»]
2X4X	X-ray	1.85	B/D/F/H	23-43	[»]
2X4Y	X-ray	1.70	B/D/F/H/J/L/N/P	23-43	[»]
3AV1	X-ray	2.50	A/E	1-136	[»]
3DB3	X-ray	2.40	B	7-12	[»]
3MO8	X-ray	1.69	B	31-42	[»]
3QO2	X-ray	2.49	P/Q/R/S	2-16	[»]
3R93	X-ray	2.06	E/F/G/H	2-16	[»]

ProteinModelPortal

Q71DI3.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48606N.

IntAct

Q71DI3. 7 interactions.

MINT

MINT-4828325.

STRING

9606.ENSP00000333277.

PTM databases

PhosphoSite

Q71DI3.

Proteomic databases

PaxDb

Q71DI3.

PRIDE

Q71DI3.

Protocols and materials databases

DNASU

126961.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000331491; ENSP00000333277; ENSG00000183598.
ENST00000369158; ENSP00000358154; ENSG00000203811.
ENST00000403683; ENSP00000385479; ENSG00000203852.
ENST00000578851; ENSP00000463798; ENSG00000265133.
ENST00000580481; ENSP00000463420; ENSG00000269789.
ENST00000585113; ENSP00000463995; ENSG00000268474.

GeneID

126961.
333932.
653604.

KEGG

hsa:126961.
hsa:333932.
hsa:653604.

UCSC

uc001esv.3. human.

Organism-specific databases

CTD

126961.
333932.
653604.

GeneCards

GC01M149784.
GC01M149812.
GC01P149824.

HGNC

HGNC:20505. HIST2H3A.
HGNC:20503. HIST2H3C.
HGNC:25311. HIST2H3D.

HPA

HPA042570.

MIM

142780. gene.

neXtProt

NX_Q71DI3.

PharmGKB

PA145148728.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2036.

HOGENOM

HOG000155290.

HOVERGEN

HBG001172.

InParanoid

Q71DI3.

KO

K11253.

OMA

RISKMAR.

OrthoDB

EOG4V9TS1.

Enzyme and pathway databases

Reactome

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

Gene expression databases

Bgee

Q71DI3.

CleanEx

HS_HIST2H3A.
HS_HIST2H3C.
HS_HIST2H3D.

Genevestigator

Q71DI3.

GermOnline

ENSG00000183598. 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

ChiTaRS

HIST2H3C. human.

EvolutionaryTrace

Q71DI3.

NextBio

81962.

SOURCE

Search...

Entry information

Entry name

H32_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 112 of the entry and version 3 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.