P68433 (H31_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H3.1

Gene names

Name:	Hist1h3a
Synonyms:	H3a
AND
Name:	Hist1h3g
Synonyms:	H3.1-221, H3g
AND
Name:	Hist1h3h
Synonyms:	H3.1-291, H3h
AND
Name:	Hist1h3i
Synonyms:	H3.1-I, H3i

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.
Subcellular location	Nucleus. Chromosome.
Developmental stage	Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation. Ref.11
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 By similarity. 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.13 Ref.15 Ref.16 Ref.18 Ref.20 Ref.21 Ref.26 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 Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin. Ref.12 Ref.14 Ref.17 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28 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 By similarity. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination. Ref.29 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 By similarity. 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
Miscellaneous	This histone is only present in mammals.
Sequence similarities	Belongs to the histone H3 family.

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	nucleosome assembly Inferred from electronic annotation. Source: InterPro regulation of gene silencing Inferred from electronic annotation. Source: Compara
Cellular_component	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
A612L	O41094	2	EBI-1179609,EBI-1179574	From a different organism.
Cbx1	P83917	6	EBI-79743,EBI-78119
SETD7	Q8WTS6	2	EBI-79743,EBI-1268586	From a different organism.

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 H3.1

PRO_0000221249

Amino acid modifications

Modified residue

3

1

Asymmetric dimethylarginine; by PRMT6; alternate By similarity

Modified residue

3

1

Phosphoarginine; alternate Probable

Modified residue

4

1

Phosphothreonine; by GSG2 Ref.22

Modified residue

5

1

Allysine; alternate By similarity

Modified residue

5

1

N6,N6,N6-trimethyllysine; alternate Ref.13 Ref.26

Modified residue

5

1

N6,N6-dimethyllysine; alternate Ref.13 Ref.26

Modified residue

5

1

N6-acetyllysine; alternate Ref.26

Modified residue

5

1

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

Modified residue

5

1

N6-methyllysine; alternate Ref.13 Ref.26

Modified residue

7

1

Phosphothreonine; by PKC By similarity

Modified residue

9

1

Citrulline; alternate Probable

Modified residue

9

1

Symmetric dimethylarginine; by PRMT5; alternate Ref.20

Modified residue

10

1

N6,N6,N6-trimethyllysine; alternate Ref.18 Ref.26

Modified residue

10

1

N6,N6-dimethyllysine; alternate Ref.18 Ref.26

Modified residue

10

1

N6-acetyllysine; alternate Ref.20 Ref.26

Modified residue

10

1

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

Modified residue

10

1

N6-methyllysine; alternate Ref.18 Ref.26

Modified residue

11

1

Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.12 Ref.17 Ref.22 Ref.24 Ref.25

Modified residue

12

1

Phosphothreonine; by PKC and CHEK1 By similarity

Modified residue

15

1

N6-acetyllysine Ref.15 Ref.18 Ref.26

Modified residue

18

1

Asymmetric dimethylarginine; by CARM1; alternate Ref.13 Ref.15 Ref.16 Ref.21

Modified residue

18

1

Citrulline; alternate Probable

Modified residue

19

1

N6-acetyllysine; alternate Ref.15 Ref.18 Ref.26

Modified residue

19

1

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

Modified residue

19

1

N6-methyllysine; alternate Ref.26

Modified residue

24

1

N6-acetyllysine; alternate Ref.15 Ref.18 Ref.26

Modified residue

24

1

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

Modified residue

24

1

N6-methyllysine; alternate Ref.26

Modified residue

28

1

N6,N6,N6-trimethyllysine; alternate Ref.18 Ref.26

Modified residue

28

1

N6,N6-dimethyllysine; alternate Ref.18 Ref.26

Modified residue

28

1

N6-acetyllysine; alternate Ref.26

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.18 Ref.26

Modified residue

29

1

Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.12 Ref.14 Ref.17 Ref.23 Ref.24 Ref.25

Modified residue

37

1

N6,N6,N6-trimethyllysine; alternate Probable

Modified residue

37

1

N6,N6-dimethyllysine; alternate Ref.18 Ref.26

Modified residue

37

1

N6-acetyllysine; alternate Ref.27

Modified residue

37

1

N6-methyllysine; alternate Ref.18 Ref.26

Modified residue

38

1

N6-methyllysine By similarity

Modified residue

42

1

Phosphotyrosine By similarity

Modified residue

57

1

N6,N6,N6-trimethyllysine; alternate By similarity

Modified residue

57

1

N6-acetyllysine; alternate By similarity

Modified residue

57

1

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

Modified residue

57

1

N6-methyllysine; by EHMT2; alternate By similarity

Modified residue

58

1

Phosphoserine By similarity

Modified residue

65

1

N6-methyllysine By similarity

Modified residue

80

1

N6,N6,N6-trimethyllysine; alternate Ref.18 Ref.26

Modified residue

80

1

N6,N6-dimethyllysine; alternate Ref.18 Ref.26

Modified residue

80

1

N6-acetyllysine; alternate By similarity

Modified residue

80

1

N6-methyllysine; alternate Ref.18 Ref.26

Modified residue

81

1

Phosphothreonine By similarity

Modified residue

108

1

Phosphothreonine By similarity

Modified residue

123

1

N6-acetyllysine; alternate By similarity

Modified residue

123

1

N6-methyllysine; alternate Ref.18

Modified residue

129

1

Phosphoarginine Probable

Modified residue

130

1

Phosphoarginine Probable

Modified residue

132

1

Phosphoarginine Potential

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

136

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Helix

46 – 55

10

Helix

65 – 77

13

Beta strand

80 – 82

3

Helix

87 – 114

28

Beta strand

118 – 120

3

Helix

122 – 132

11

Sequences

	Sequence		Length	Mass (Da)
	P68433 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9B89008EA50A0EF6	FASTA	136	15,404
	10 20 30 40 50 60 MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE 70 80 90 100 110 120 LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI 130 MPKDIQLARR IRGERA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of a cluster of mouse histone genes." Sittman D.B., Graves R.A., Marzluff W.F. Nucleic Acids Res. 11:6679-6697(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequences of four mouse histone H3 genes: implications for evolution of mouse histone genes." Taylor J.D., Wellman S.E., Marzluff W.F. J. Mol. Evol. 23:242-249(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3G AND HIST1H3H).
[3]	"Nucleotide sequences of mouse histone genes H2A and H3.1." Kosciessa U., Doenecke D. Nucleic Acids Res. 17:8861-8861(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CD-1. Tissue: Testis.
[4]	"Characterization of the mouse histone gene cluster on chromosome 13: 45 histone genes in three patches spread over 1Mb." Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F. Genome Res. 6:688-701(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3I). Strain: C57BL/CJ6.
[5]	"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] (HIST1H3A; HIST1H3G; HIST1H3H AND HIST1H3I).
[6]	Franke K., Drabent B., Doenecke D. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv.
[7]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.
[8]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[9]	"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].
[10]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 58-64, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[11]	"Changes in the levels of three different classes of histone mRNA during murine erythroleukemia cell differentiation." Brown D.T., Wellman S.E., Sittman D.B. Mol. Cell. Biol. 5:2879-2886(1985) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[12]	"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: PHOSPHORYLATION AT SER-11 AND SER-29.
[13]	"Hormone-dependent, CARM1-directed, arginine-specific methylation of histone H3 on a steroid-regulated promoter." Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A., Aswad D.W., Allis C.D., Hager G.L., Stallcup M.R. Curr. Biol. 11:1981-1985(2001) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-5 AND ARG-18.
[14]	"Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1." Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M., Ma W.-Y., Dong Z. J. Biol. Chem. 276:33213-33219(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-29.
[15]	"Crosstalk between CARM1 methylation and CBP acetylation on histone H3." Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T. Curr. Biol. 12:2090-2097(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT ARG-18.
[16]	"Methylation at arginine 17 of histone H3 is linked to gene activation." Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T. EMBO Rep. 3:39-44(2002) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-18.
[17]	"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.
[18]	"Identification of methylation and acetylation sites on mouse histone H3 using matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization tandem mass spectrometry." Cocklin R.R., Wang M. J. Protein Chem. 22:327-334(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10; LYS-28; LYS-37; LYS-80 AND LYS-123, MASS SPECTROMETRY.
[19]	"Histone deimination antagonizes arginine methylation." Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H., Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P., Bannister A.J., Kouzarides T. Cell 118:545-553(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CITRULLINATION.
[20]	"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes." Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S. Mol. Cell. Biol. 24:9630-9645(2004) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-9, ACETYLATION AT LYS-10.
[21]	"Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression." Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C., Imhof R., Bedford M.T., Natoli G., Hottiger M.O. EMBO J. 24:85-96(2005) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-18.
[22]	"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 AND SER-11.
[23]	"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.
[24]	"MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2." Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J., Nightingale K., Iborra F.J., Mahadevan L.C. J. Cell Sci. 118:2247-2259(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
[25]	"Stimulation of the Ras-MAPK pathway leads to independent phosphorylation of histone H3 on serine 10 and 28." Dunn K.L., Davie J.R. Oncogene 24:3492-3502(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
[26]	"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 AND LYS-28, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 AND LYS-80, MASS SPECTROMETRY.
[27]	"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.
[28]	"Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression." Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H., Nakanishi M. Cell 132:221-232(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-12 BY CHEK1.
[29]	"The RING domain of RAG1 ubiquitylates histone H3: a novel activity in chromatin-mediated regulation of V(D)J joining." Grazini U., Zanardi F., Citterio E., Casola S., Goding C.R., McBlane F. Mol. Cell 37:282-293(2010) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X01684 Genomic DNA. Translation: CAA25839.1.
M32460 Genomic DNA. Translation: AAA37811.1.
M32462 Genomic DNA. Translation: AAA37813.1.
X16496 Genomic DNA. Translation: CAA34512.1.
U62670 Genomic DNA. Translation: AAB04763.1.
U62672 Genomic DNA. Translation: AAB04765.1.
AY158944 Genomic DNA. Translation: AAO06254.1.
AY158945 Genomic DNA. Translation: AAO06255.1.
AY158946 Genomic DNA. Translation: AAO06256.1.
AY158952 Genomic DNA. Translation: AAO06262.1.
Y12290 Genomic DNA. Translation: CAA72968.1.
AK006742 mRNA. Translation: BAB24722.1.
AK018952 mRNA. Translation: BAB31493.1.
AK155722 mRNA. Translation: BAE33402.1.
AL590388 Genomic DNA. Translation: CAI25837.1.
AL589651 Genomic DNA. Translation: CAI24113.1.
AL589651 Genomic DNA. Translation: CAI24105.1.
BC107285 mRNA. Translation: AAI07286.1.
BC107287 mRNA. Translation: AAI07288.1.
BC115816 mRNA. Translation: AAI15817.1.
BC116383 mRNA. Translation: AAI16384.1.
BC125355 mRNA. Translation: AAI25356.1.
BC125357 mRNA. Translation: AAI25358.1.

IPI

IPI00553538.

PIR

A39525.
S06755.

RefSeq

NP_038578.2. NM_013550.4.
NP_659539.1. NM_145073.2.
NP_835513.1. NM_178206.2.
NP_835514.1. NM_178207.2.

UniGene

Mm.221301.
Mm.261657.
Mm.377874.
Mm.390558.
Mm.397328.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GUW	NMR	-	B	2-17	[»]
1U35	X-ray	3.00	A/E	1-136	[»]
2V83	X-ray	2.40	D/E	2-10	[»]
2WP1	X-ray	2.10	P/Q	15-24	[»]
2XL3	X-ray	2.70	D/F	2-9	[»]
4EZH	X-ray	2.52	C/D	25-35	[»]

ProteinModelPortal

P68433.

ModBase

Search...

Protein-protein interaction databases

IntAct

P68433. 27 interactions.

MINT

MINT-191105.

PTM databases

PhosphoSite

P68433.

Proteomic databases

PaxDb

P68433.

PRIDE

P68433.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000080859; ENSMUSP00000079670; ENSMUSG00000062417.
ENSMUST00000091701; ENSMUSP00000089293; ENSMUSG00000069265.
ENSMUST00000091754; ENSMUSP00000089348; ENSMUSG00000069312.
ENSMUST00000099704; ENSMUSP00000097295; ENSMUSG00000075032.

GeneID

319152.
319153.
360198.
97908.

KEGG

mmu:319152.
mmu:319153.
mmu:360198.
mmu:97908.

UCSC

uc007prc.1. mouse.

Organism-specific databases

CTD

8350.
8354.
8355.
8357.

MGI

MGI:2668828. Hist1h3a.
MGI:2145541. Hist1h3g.
MGI:2448349. Hist1h3h.
MGI:2448350. Hist1h3i.

Phylogenomic databases

eggNOG

COG2036.

GeneTree

ENSGT00660000095369.

HOVERGEN

HBG001172.

InParanoid

P68433.

KO

K11253.

OMA

HASMART.

OrthoDB

EOG412M6S.

Enzyme and pathway databases

Reactome

REACT_118161. Cell Cycle.
REACT_120463. Meiosis.
REACT_27235. Meiotic Recombination (mouse).
REACT_75800. Meiotic Synapsis (mouse).

Gene expression databases

ArrayExpress

P68433.

Bgee

P68433.

CleanEx

MM_HIST1H3A.
MM_HIST1H3G.
MM_HIST1H3H.
MM_HIST1H3I.

Genevestigator

P68433.

GermOnline

ENSMUSG00000062417. Mus musculus.
ENSMUSG00000069265. Mus musculus.
ENSMUSG00000069310. Mus musculus.
ENSMUSG00000069312. Mus musculus.

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

P68433.

NextBio

353176.

SOURCE

Search...

Entry information

Entry name

H31_MOUSE

Accession

Primary (citable) accession number: P68433
Secondary accession number(s): P02295 , P02296, P16106, Q05A97, Q3B7Z8, Q3B7Z9, Q5T009

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program