P68431 (H31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H3.1

Alternative name(s):
Histone H3/a
Histone H3/b
Histone H3/c
Histone H3/d
Histone H3/f
Histone H3/h
Histone H3/i
Histone H3/j
Histone H3/k
Histone H3/l

Gene names

Name:	HIST1H3A
Synonyms:	H3FA
AND
Name:	HIST1H3B
Synonyms:	H3FL
AND
Name:	HIST1H3C
Synonyms:	H3FC
AND
Name:	HIST1H3D
Synonyms:	H3FB
AND
Name:	HIST1H3E
Synonyms:	H3FD
AND
Name:	HIST1H3F
Synonyms:	H3FI
AND
Name:	HIST1H3G
Synonyms:	H3FH
AND
Name:	HIST1H3H
Synonyms:	H3FK
AND
Name:	HIST1H3I
Synonyms:	H3FF
AND
Name:	HIST1H3J
Synonyms:	H3FJ

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
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. 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.15 Ref.16 Ref.18 Ref.19 Ref.23 Ref.24 Ref.27 Ref.35 Ref.37 Ref.38 Ref.40 Ref.41 Ref.42 Ref.43 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.28
Miscellaneous	This histone is only present in mammals and is enriched in acetylation of Lys-15 and dimethylation of Lys-10 (H3K9me2).
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	S phase Non-traceable author statement Ref.26. Source: BHF-UCL blood coagulation Traceable author statement. Source: Reactome nucleosome assembly Inferred from electronic annotation. Source: InterPro regulation of gene silencing Inferred from direct assay Ref.26. Source: BHF-UCL
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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IPL1	P38991	2	EBI-79722,EBI-9319	From a different organism.
MLL	Q03164	10	EBI-79722,EBI-591370
SETD7	Q8WTS6	4	EBI-79722,EBI-1268586

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.15

Chain

2 – 136

135

Histone H3.1

PRO_0000221245

Amino acid modifications

Modified residue

3

1

Asymmetric dimethylarginine; by PRMT6 Ref.32 Ref.36 Ref.39

Modified residue

4

1

Phosphothreonine; by GSG2 Ref.15 Ref.23

Modified residue

5

1

N6-acetyllysine; alternate Ref.33

Modified residue

5

1

N6-methyllysine; alternate Ref.26 Ref.27 Ref.33

Modified residue

7

1

Phosphothreonine; by PKC Ref.43

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.15 Ref.17 Ref.26 Ref.27 Ref.33

Modified residue

10

1

N6,N6-dimethyllysine; alternate Ref.15 Ref.17 Ref.26 Ref.27 Ref.33

Modified residue

10

1

N6-acetyllysine; alternate Ref.15 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.33

Modified residue

10

1

N6-methyllysine; alternate Ref.15 Ref.17 Ref.26 Ref.27 Ref.33

Modified residue

11

1

Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.15 Ref.16 Ref.18 Ref.19 Ref.23 Ref.27

Modified residue

12

1

Phosphothreonine; by PKC and CHEK1 Ref.19 Ref.38 Ref.40

Modified residue

15

1

N6-acetyllysine Ref.15 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.33

Modified residue

18

1

Asymmetric dimethylarginine; by CARM1; alternate Ref.20 Ref.22 Ref.31

Modified residue

18

1

Citrulline; alternate

Modified residue

19

1

N6-acetyllysine; alternate Ref.26 Ref.29 Ref.30 Ref.33

Modified residue

19

1

N6-methyllysine; alternate Ref.26 Ref.33

Modified residue

24

1

N6-acetyllysine; alternate Ref.26 Ref.27 Ref.29 Ref.30 Ref.33

Modified residue

24

1

N6-methyllysine; alternate Ref.33

Modified residue

28

1

N6,N6,N6-trimethyllysine; alternate Ref.15 Ref.26 Ref.30 Ref.33

Modified residue

28

1

N6,N6-dimethyllysine; alternate Ref.15 Ref.26 Ref.30 Ref.33

Modified residue

28

1

N6-acetyllysine; alternate Ref.29 Ref.30 Ref.33

Modified residue

28

1

N6-methyllysine; alternate Ref.15 Ref.26 Ref.30 Ref.33

Modified residue

29

1

Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.15 Ref.16 Ref.18 Ref.23 Ref.24 Ref.27 Ref.35 Ref.37

Modified residue

37

1

N6,N6,N6-trimethyllysine; alternate Ref.15 Ref.25 Ref.26 Ref.30 Ref.33

Modified residue

37

1

N6,N6-dimethyllysine; alternate Ref.15 Ref.25 Ref.26 Ref.30 Ref.33

Modified residue

37

1

N6-acetyllysine; alternate Ref.29 Ref.33 Ref.34

Modified residue

37

1

N6-methyllysine; alternate Ref.15 Ref.25 Ref.26 Ref.30 Ref.33

Modified residue

38

1

N6-methyllysine Ref.25

Modified residue

42

1

Phosphotyrosine Ref.41

Modified residue

57

1

N6,N6,N6-trimethyllysine; alternate Ref.33

Modified residue

57

1

N6-acetyllysine; alternate Ref.33

Modified residue

57

1

N6-methyllysine; alternate Ref.33

Modified residue

58

1

Phosphoserine Ref.42

Modified residue

65

1

N6-methyllysine Ref.26 Ref.33

Modified residue

80

1

N6,N6,N6-trimethyllysine; alternate By similarity

Modified residue

80

1

N6,N6-dimethyllysine; alternate Ref.21 Ref.26 Ref.30 Ref.33

Modified residue

80

1

N6-acetyllysine; alternate Ref.33

Modified residue

80

1

N6-methyllysine; alternate Ref.21 Ref.26 Ref.30 Ref.33

Modified residue

81

1

Phosphothreonine Ref.42

Modified residue

123

1

N6-methyllysine Ref.26 Ref.33

Experimental info

Sequence conflict

70

1

R → C in AAH67493. Ref.13

Sequence conflict

100

1

Y → T in CAB02546. Ref.7

Sequence conflict

122

1

P → L in AAH66884. Ref.13

Sequence conflict

135

1

Missing in AAA52651. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

136

Helix Strand Turn

Details...

Helix

46 – 57

12

Helix

65 – 77

13

Beta strand

80 – 82

3

Helix

87 – 114

28

Beta strand

118 – 120

3

Helix

122 – 131

10

Sequences

	Sequence		Length	Mass (Da)
	P68431 [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]	"The primary structure and expression of four cloned human histone genes." Zhong R., Roeder R.G., Heintz N. Nucleic Acids Res. 11:7409-7425(1983) [PubMed: 6647026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3B).
[2]	"Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5' regulatory sequences." Marashi F., Helms S., Shiels A., Silverstein S., Greenspan D.S., Stein G., Stein J. Biochem. Cell Biol. 64:277-289(1986) [PubMed: 3013246] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Isolation and characterization of two human H1 histone genes within clusters of core histone genes." Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D. Genomics 10:940-948(1991) [PubMed: 1916825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3FD).
[4]	"Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones." Kardalinou E., Eick S., Albig W., Doenecke D. J. Cell. Biochem. 52:375-383(1993) [PubMed: 8227173] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Expression of human histone h1.1 and the nearby core histones." Runge D., Eick S., Doenecke D. Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
[6]	"Characterization of the H1.5 gene completes the set of human H1 subtype genes." Albig W., Meergans T., Doenecke D. Gene 184:141-148(1997) [PubMed: 9031620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3I).
[7]	"Human histone gene organization: nonregular arrangement within a large cluster." Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D. Genomics 40:314-322(1997) [PubMed: 9119399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3D; HIST1H3F AND HIST1H3G).
[8]	"The human histone gene cluster at the D6S105 locus." Albig W., Doenecke D. Hum. Genet. 101:284-294(1997) [PubMed: 9439656] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3H AND HIST1H3J).
[9]	"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: 12408966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3A; HIST1H3B; HIST1H3C; HIST1H3D; HIST1H3E; HIST1H3F; HIST1H3G; HIST1H3H; HIST1H3I; HIST1H3J).
[10]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Caudate nucleus, Stomach and Thymus.
[11]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[12]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[14]	"Human spleen histone H3. Isolation and amino acid sequence." Ohe Y., Iwai K. J. Biochem. 90:1205-1211(1981) [PubMed: 7309716] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Spleen.
[15]	"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: 16185088] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20, 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.
[16]	"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: 10464286] [Abstract] Cited for: PROTEIN SEQUENCE OF 58-64; 117-120 AND 124-135, PHOSPHORYLATION AT SER-11 AND SER-29.
[17]	"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: 11242053] [Abstract] Cited for: METHYLATION AT LYS-10.
[18]	"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: 11856369] [Abstract] Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
[19]	"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: 12560483] [Abstract] Cited for: PHOSPHORYLATION AT SER-11 AND THR-12.
[20]	"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: 15471871] [Abstract] Cited for: METHYLATION AT ARG-18.
[21]	"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: 15525939] [Abstract] Cited for: METHYLATION AT LYS-80.
[22]	"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: 15345777] [Abstract] Cited for: CITRULLINATION AT ARG-9 AND ARG-18, METHYLATION AT ARG-18.
[23]	"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: 15681610] [Abstract] Cited for: PHOSPHORYLATION AT THR-4; SER-11 AND SER-29.
[24]	"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: 15684425] [Abstract] Cited for: PHOSPHORYLATION AT SER-29.
[25]	"Protein identification using sequential ion/ion reactions and tandem mass spectrometry." Coon J.J., Ueberheide B., Syka J.E.P., Dryhurst D.D., Ausio J., Shabanowitz J., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 102:9463-9468(2005) [PubMed: 15983376] [Abstract] Cited for: METHYLATION AT LYS-37 AND LYS-38, MASS SPECTROMETRY.
[26]	"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: 16267050] [Abstract] Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, MASS SPECTROMETRY.
[27]	"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: 16457588] [Abstract] Cited for: METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10; LYS-15 AND LYS-24, PHOSPHORYLATION AT SER-11 AND SER-29, MASS SPECTROMETRY.
[28]	"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: 16678110] [Abstract] Cited for: UBIQUITINATION.
[29]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-15; LYS-19; LYS-24; LYS-28 AND LYS-37, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"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: 16627869] [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.
[31]	"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: 16497732] [Abstract] Cited for: ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, CITRULLINATION AT ARG-18.
[32]	"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: 18079182] [Abstract] Cited for: METHYLATION AT ARG-3 BY PRMT6.
[33]	"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: 17194708] [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.
[34]	"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: 17189264] [Abstract] Cited for: ACETYLATION AT LYS-37.
[35]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[36]	"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: 17898714] [Abstract] Cited for: METHYLATION AT ARG-3 BY PRMT6.
[37]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[38]	"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: 18243098] [Abstract] Cited for: PHOSPHORYLATION AT THR-12 BY CHEK1.
[39]	"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: 18077460] [Abstract] Cited for: METHYLATION AT ARG-3 BY PRMT6.
[40]	"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: 18066052] [Abstract] Cited for: PHOSPHORYLATION AT THR-12.
[41]	"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: 19783980] [Abstract] Cited for: PHOSPHORYLATION AT TYR-42.
[42]	"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: 20850016] [Abstract] Cited for: PHOSPHORYLATION AT SER-58 AND THR-81.
[43]	"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: 20228790] [Abstract] Cited for: PHOSPHORYLATION AT THR-7.
[44]	"Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3." Macdonald N., Welburn J.P.I., Noble M.E.M., Nguyen A., Yaffe M.B., Clynes D., Moggs J.G., Orphanides G., Thomson S., Edmunds J.W., Clayton A.L., Endicott J.A., Mahadevan L.C. Mol. Cell 20:199-211(2005) [PubMed: 16246723] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-15 IN COMPLEX WITH YWHAZ.
[45]	"Double chromodomains cooperate to recognize the methylated histone H3 tail." Flanagan J.F., Mi L.-Z., Chruszcz M., Cymborowski M., Clines K.L., Kim Y., Minor W., Rastinejad F., Khorasanizadeh S. Nature 438:1181-1185(2005) [PubMed: 16372014] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 2-20 IN COMPLEX WITH CHD1.
[46]	"Alteration of the nucleosomal DNA path in the crystal structure of a human nucleosome core particle." Tsunaka Y., Kajimura N., Tate S., Morikawa K. Nucleic Acids Res. 33:3424-3434(2005) [PubMed: 15951514] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00090 Genomic DNA. Translation: CAA24952.1.
M26150 Genomic DNA. Translation: AAA52651.1.
M60746 Genomic DNA. Translation: AAA63185.1.
X57128 Genomic DNA. Translation: CAA40407.1.
Z46261 Genomic DNA. Translation: CAA86403.1.
X83550 Genomic DNA. Translation: CAA58540.1.
Z80784 Genomic DNA. Translation: CAB02546.1.
Z80785 Genomic DNA. Translation: CAB02547.1.
Z80786 Genomic DNA. Translation: CAB02548.1.
Z83735 Genomic DNA. Translation: CAB06030.1.
Z83737 Genomic DNA. Translation: CAB06032.1.
AF531274 Genomic DNA. Translation: AAN10051.1.
AF531275 Genomic DNA. Translation: AAN10052.1.
AF531276 Genomic DNA. Translation: AAN10053.1.
AF531277 Genomic DNA. Translation: AAN10054.1.
AF531278 Genomic DNA. Translation: AAN10055.1.
AF531279 Genomic DNA. Translation: AAN10056.1.
AF531280 Genomic DNA. Translation: AAN10057.1.
AF531281 Genomic DNA. Translation: AAN10058.1.
AF531282 Genomic DNA. Translation: AAN10059.1.
AF531283 Genomic DNA. Translation: AAN10060.1.
AK311991 mRNA. Translation: BAG34929.1.
AK313905 mRNA. Translation: BAG36628.1.
AK314142 mRNA. Translation: BAG36832.1.
AK316611 mRNA. Translation: BAG38198.1.
CR542014 mRNA. Translation: CAG46811.1.
CR542011 mRNA. Translation: CAG46808.1.
CR541983 mRNA. Translation: CAG46780.1.
CR541858 mRNA. Translation: CAG46656.1.
Z98744 Genomic DNA. Translation: CAD24076.1.
Z98744 Genomic DNA. Translation: CAB11424.1.
AL009179 Genomic DNA. Translation: CAA15670.1.
AL031777 Genomic DNA. Translation: CAC03412.1.
AL031777 Genomic DNA. Translation: CAC03413.1.
AL031777 Genomic DNA. Translation: CAC03416.1.
AL031777 Genomic DNA. Translation: CAC03421.1.
BC031333 mRNA. Translation: AAH31333.1.
BC066245 mRNA. Translation: AAH66245.1.
BC066246 mRNA. Translation: AAH66246.1.
BC066247 mRNA. Translation: AAH66247.1.
BC066884 mRNA. Translation: AAH66884.1.
BC067490 mRNA. Translation: AAH67490.1.
BC067491 mRNA. Translation: AAH67491.1.
BC067492 mRNA. Translation: AAH67492.1.
BC067493 mRNA. Translation: AAH67493.1.
BC069133 mRNA. Translation: AAH69133.1.
BC069303 mRNA. Translation: AAH69303.1.
BC069305 mRNA. Translation: AAH69305.2.
BC069818 mRNA. Translation: AAH69818.1.
BC096128 mRNA. Translation: AAH96128.1.
BC096129 mRNA. Translation: AAH96129.1.
BC096130 mRNA. Translation: AAH96130.1.
BC096131 mRNA. Translation: AAH96131.1.
BC096132 mRNA. Translation: AAH96132.1.
BC096133 mRNA. Translation: AAH96133.1.
BC096134 mRNA. Translation: AAH96134.1.
BC099630 mRNA. Translation: AAH99630.1.
BC127610 mRNA. Translation: AAI27611.1.
BC143046 mRNA. Translation: AAI43047.1.
BC148243 mRNA. Translation: AAI48244.1.
BC148250 mRNA. Translation: AAI48251.1.

IPI

IPI00465070.

PIR

HSHU3. I37446.

RefSeq

NP_003520.1. NM_003529.2.
NP_003521.2. NM_003530.3.
NP_003522.1. NM_003531.2.
NP_003523.1. NM_003532.2.
NP_003524.1. NM_003533.2.
NP_003525.1. NM_003534.2.
NP_003526.1. NM_003535.2.
NP_003527.1. NM_003536.2.
NP_003528.1. NM_003537.3.
NP_066298.1. NM_021018.2.

UniGene

Hs.132854.
Hs.247813.
Hs.247814.
Hs.248176.
Hs.443021.
Hs.484990.
Hs.532144.
Hs.533292.
Hs.546315.
Hs.586261.
Hs.591778.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CS9	NMR	-	A	131-136	[»]
1CT6	NMR	-	A	131-135	[»]
1Q3L	X-ray	1.64	P	2-16	[»]
2B2T	X-ray	2.45	D	2-20	[»]
2B2U	X-ray	2.95	D	4-16	[»]
2B2V	X-ray	2.65	D	2-16	[»]
2B2W	X-ray	2.40	D	2-20	[»]
2C1J	X-ray	2.60	C/D	8-15	[»]
2C1N	X-ray	2.00	C/E	8-15	[»]
2CV5	X-ray	2.50	A/E	1-136	[»]
2L75	NMR	-	B	2-14	[»]
2LBM	NMR	-	C	2-16	[»]
2RI7	X-ray	1.45	P	2-10	[»]
2UXN	X-ray	2.72	E	2-22	[»]
3A1B	X-ray	2.29	A	2-21	[»]
3AFA	X-ray	2.50	A/E	1-136	[»]
3AVR	X-ray	1.80	B	18-39	[»]
3AYW	X-ray	2.90	A/E	1-136	[»]
3AZE	X-ray	3.00	A/E	1-136	[»]
3AZF	X-ray	2.70	A/E	1-136	[»]
3AZG	X-ray	2.40	A/E	1-136	[»]
3AZH	X-ray	3.49	A/E	1-136	[»]
3AZI	X-ray	2.70	A/E	1-136	[»]
3AZJ	X-ray	2.89	A/E	1-136	[»]
3AZK	X-ray	3.20	A/E	1-136	[»]
3AZL	X-ray	2.70	A/E	1-136	[»]
3AZM	X-ray	2.89	A/E	1-136	[»]
3AZN	X-ray	3.00	A/E	1-136	[»]
3KMT	X-ray	1.78	G/H/I	26-33	[»]
3O34	X-ray	1.90	B	14-33	[»]
3O35	X-ray	1.76	D/E	24-32	[»]
3O37	X-ray	2.00	E/F/G/H	2-11	[»]
4A0J	X-ray	2.80	C/D	2-7	[»]
4A0N	X-ray	2.74	C	2-7	[»]

ProteinModelPortal

P68431.

SMR

P68431. Positions 2-136.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29371N.

IntAct

P68431. 29 interactions.

MINT

MINT-256465.

STRING

P68431.

PTM databases

PhosphoSite

P68431.

Proteomic databases

PRIDE

P68431.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000230495; ENSP00000230495; ENSG00000112727.
ENST00000244661; ENSP00000244661; ENSG00000124693.
ENST00000328488; ENSP00000329554; ENSG00000182572.
ENST00000356476; ENSP00000366999; ENSG00000197409.
ENST00000357647; ENSP00000350275; ENSG00000198366.
ENST00000359303; ENSP00000352252; ENSG00000197153.
ENST00000360408; ENSP00000353581; ENSG00000196966.
ENST00000360577; ENSP00000353783; ENSG00000196532.
ENST00000369163; ENSP00000358160; ENSG00000203813.
ENST00000377831; ENSP00000367062; ENSG00000197409.

GeneID

8350.
8351.
8352.
8353.
8354.
8355.
8356.
8357.
8358.
8968.

KEGG

hsa:8350.
hsa:8351.
hsa:8352.
hsa:8353.
hsa:8354.
hsa:8355.
hsa:8356.
hsa:8357.
hsa:8358.
hsa:8968.

UCSC

uc003nfp.1. human.

Organism-specific databases

CTD

8350.
8351.
8352.
8353.
8354.
8355.
8356.
8357.
8358.
8968.

GeneCards

GC06M025974.
GC06M026140.
GC06M026193.
GC06M026271.
GC06M027841.
GC06M027862.
GC06P025963.
GC06P026051.
GC06P026225.
GC06P027777.

H-InvDB

HIX0003498.
HIX0005642.
HIX0005644.
HIX0025220.
HIX0032908.
HIX0032917.
HIX0032922.
HIX0032928.

HGNC

HGNC:4766. HIST1H3A.
HGNC:4776. HIST1H3B.
HGNC:4768. HIST1H3C.
HGNC:4767. HIST1H3D.
HGNC:4769. HIST1H3E.
HGNC:4773. HIST1H3F.
HGNC:4772. HIST1H3G.
HGNC:4775. HIST1H3H.
HGNC:4771. HIST1H3I.
HGNC:4774. HIST1H3J.

HPA

CAB037166.
CAB037178.
CAB037187.

MIM

602810. gene.
602811. gene.
602812. gene.
602813. gene.
602814. gene.
602815. gene.
602816. gene.
602817. gene.
602818. gene.
602819. gene.

neXtProt

NX_P68431.

PharmGKB

PA29148.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06375.

GeneTree

ENSGT00560000076869.

HOVERGEN

HBG001172.

InParanoid

P68431.

OMA

DLRFQSQ.

OrthoDB

EOG412M6S.

PhylomeDB

P68431.

Enzyme and pathway databases

Reactome

REACT_111183. Meiosis.
REACT_604. Hemostasis.
REACT_75925. Amyloids.

Gene expression databases

ArrayExpress

P68431.

Bgee

P68431.

CleanEx

HS_HIST1H3A.
HS_HIST1H3B.
HS_HIST1H3C.
HS_HIST1H3D.
HS_HIST1H3E.
HS_HIST1H3F.
HS_HIST1H3G.
HS_HIST1H3H.
HS_HIST1H3I.

Genevestigator

P68431.

GermOnline

ENSG00000112727. Homo sapiens.
ENSG00000124693. Homo sapiens.
ENSG00000178458. Homo sapiens.
ENSG00000182572. Homo sapiens.
ENSG00000196532. Homo sapiens.
ENSG00000196747. Homo sapiens.
ENSG00000196966. Homo sapiens.
ENSG00000197153. Homo sapiens.
ENSG00000197409. Homo sapiens.
ENSG00000198366. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:1.10.20.10. Histone-fold. 1 hit.

KO

K11253.

PANTHER

PTHR11426. Histone_H3. 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

NextBio

31272.

SOURCE

Search...

Entry information

Entry name

H31_HUMAN

Accession

Primary (citable) accession number: P68431
Secondary accession number(s): A0PJT7 , A5PLR1, P02295, P02296, P16106, Q6ISV8, Q6NWP8, Q6NWP9, Q6NXU4, Q71DJ3, Q93081

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

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