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P68431 (H31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3.1
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

Subunit structure

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

Subcellular location

Nucleus. Chromosome.

Developmental stage

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

Post-translational modification

Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Ref.15 Ref.26 Ref.27 Ref.29 Ref.30 Ref.33 Ref.34 Ref.39 Ref.46

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.15 Ref.17 Ref.20 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.32 Ref.33 Ref.35 Ref.37 Ref.44

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.36 Ref.38 Ref.40 Ref.41 Ref.42

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

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.45).

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.43

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 136135Histone H3.1
PRO_0000221245

Amino acid modifications

Modified residue31Asymmetric dimethylarginine; by PRMT6; alternate Ref.32 Ref.35 Ref.37
Modified residue31Citrulline; alternate
Modified residue41Phosphothreonine; by GSG2 Ref.15 Ref.23
Modified residue51Allysine; alternate
Modified residue51N6,N6,N6-trimethyllysine; alternate Ref.26 Ref.27 Ref.33
Modified residue51N6,N6-dimethyllysine; alternate Ref.26 Ref.27 Ref.33
Modified residue51N6-acetyllysine; alternate Ref.33
Modified residue51N6-crotonyl-L-lysine; alternate Ref.43
Modified residue51N6-methyllysine; alternate Ref.26 Ref.27 Ref.33
Modified residue71Phosphothreonine; by PKC Ref.42
Modified residue91Citrulline; alternate
Modified residue91Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residue101N6,N6,N6-trimethyllysine; alternate Ref.15 Ref.17 Ref.26 Ref.27 Ref.33
Modified residue101N6,N6-dimethyllysine; alternate Ref.15 Ref.17 Ref.26 Ref.27 Ref.33
Modified residue101N6-acetyllysine; alternate Ref.15 Ref.26 Ref.27 Ref.29 Ref.30 Ref.33
Modified residue101N6-crotonyl-L-lysine; alternate Ref.43
Modified residue101N6-methyllysine; alternate Ref.15 Ref.17 Ref.26 Ref.27 Ref.33
Modified residue111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.15 Ref.16 Ref.18 Ref.19 Ref.23 Ref.27
Modified residue121Phosphothreonine; by PKC and CHEK1 Ref.19 Ref.36 Ref.38
Modified residue151N6-acetyllysine Ref.15 Ref.26 Ref.27 Ref.29 Ref.30 Ref.33
Modified residue181Asymmetric dimethylarginine; by CARM1; alternate Ref.20 Ref.22 Ref.30
Modified residue181Citrulline; alternate
Modified residue191N6-acetyllysine; alternate Ref.26 Ref.29 Ref.33
Modified residue191N6-crotonyl-L-lysine; alternate Ref.43
Modified residue191N6-methyllysine; alternate Ref.26 Ref.33
Modified residue241N6-acetyllysine; alternate Ref.26 Ref.27 Ref.29 Ref.33
Modified residue241N6-crotonyl-L-lysine; alternate Ref.43
Modified residue241N6-methyllysine; alternate Ref.33
Modified residue271Citrulline
Modified residue281N6,N6,N6-trimethyllysine; alternate Ref.15 Ref.26 Ref.29 Ref.33
Modified residue281N6,N6-dimethyllysine; alternate Ref.15 Ref.26 Ref.29 Ref.33
Modified residue281N6-acetyllysine; alternate Ref.29 Ref.33
Modified residue281N6-crotonyl-L-lysine; alternate Ref.43
Modified residue281N6-methyllysine; alternate Ref.15 Ref.26 Ref.29 Ref.33
Modified residue291Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.15 Ref.16 Ref.18 Ref.23 Ref.24 Ref.27
Modified residue371N6,N6,N6-trimethyllysine; alternate Ref.15 Ref.25 Ref.26 Ref.29 Ref.33
Modified residue371N6,N6-dimethyllysine; alternate Ref.15 Ref.25 Ref.26 Ref.29 Ref.33
Modified residue371N6-acetyllysine; alternate Ref.33 Ref.34
Modified residue371N6-methyllysine; alternate Ref.15 Ref.25 Ref.26 Ref.29 Ref.33
Modified residue381N6-methyllysine Ref.25
Modified residue421Phosphotyrosine Ref.40
Modified residue571N6,N6,N6-trimethyllysine; alternate Ref.33 Ref.44
Modified residue571N6-acetyllysine; alternate Ref.33
Modified residue571N6-crotonyl-L-lysine; alternate Ref.43
Modified residue571N6-methyllysine; by EHMT2; alternate Ref.33 Ref.44
Modified residue581Phosphoserine Ref.41
Modified residue651N6-methyllysine Ref.26 Ref.33
Modified residue801N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue801N6,N6-dimethyllysine; alternate Ref.21 Ref.26 Ref.29 Ref.33
Modified residue801N6-acetyllysine; alternate Ref.33
Modified residue801N6-methyllysine; alternate Ref.21 Ref.26 Ref.29 Ref.33
Modified residue811Phosphothreonine Ref.41
Modified residue1081Phosphothreonine By similarity
Modified residue1161N6-acetyllysine Ref.39
Modified residue1231N6-acetyllysine; alternate Ref.39 Ref.46
Modified residue1231N6-methyllysine; alternate Ref.26 Ref.33

Experimental info

Sequence conflict701R → C in AAH67493. Ref.13
Sequence conflict1001Y → T in CAB02546. Ref.7
Sequence conflict1221P → L in AAH66884. Ref.13
Sequence conflict1351Missing in AAA52651. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P68431 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9B89008EA50A0EF6

FASTA13615,404
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-37 AND LYS-38, IDENTIFICATION BY 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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[29]"Quantitative proteomic analysis of post-translational modifications of human histones."
Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., Grauslund M., Hansen A.M., Jensen O.N.
Mol. Cell. Proteomics 5:1314-1325(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION AT LYS-28; LYS-37 AND LYS-80, IDENTIFICATION BY MASS SPECTROMETRY.
[30]"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.
[31]"Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4."
Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.
Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-3; ARG-9; ARG-18 AND ARG-27.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY.
[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] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-37.
[35]"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.
[36]"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.
[37]"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.
[38]"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.
[39]"Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding."
Manohar M., Mooney A.M., North J.A., Nakkula R.J., Picking J.W., Edon A., Fishel R., Poirier M.G., Ottesen J.J.
J. Biol. Chem. 284:23312-23321(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-116 AND LYS-123.
[40]"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.
[41]"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.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer."
Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M., Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R., Schneider R.
Cell 152:859-872(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-123.
[47]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-15 IN COMPLEX WITH YWHAZ.
[48]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 2-20 IN COMPLEX WITH CHD1.
[49]"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] [Europe PMC] [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.
PIRHSHU3. I37446.
RefSeqNP_003520.1. NM_003529.2.
NP_003521.2. NM_003530.4.
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.
UniGeneHs.132854.
Hs.247813.
Hs.247814.
Hs.248176.
Hs.443021.
Hs.484990.
Hs.532144.
Hs.533292.
Hs.546315.
Hs.586261.
Hs.591778.
Hs.626666.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CS9NMR-A131-136[»]
1CT6NMR-A131-135[»]
1Q3LX-ray1.64P2-16[»]
2B2TX-ray2.45D2-20[»]
2B2UX-ray2.95D4-16[»]
2B2VX-ray2.65D2-16[»]
2B2WX-ray2.40D2-20[»]
2C1JX-ray2.60C/D8-15[»]
2C1NX-ray2.00C/E8-15[»]
2CV5X-ray2.50A/E1-136[»]
2KWJNMR-B2-21[»]
2KWKNMR-B2-21[»]
2L75NMR-B2-14[»]
2LBMNMR-C2-16[»]
2M0ONMR-B32-42[»]
2RI7X-ray1.45P2-10[»]
2UXNX-ray2.72E2-22[»]
2VPGX-ray1.60P/R2-19[»]
3A1BX-ray2.29A2-21[»]
3AFAX-ray2.50A/E1-136[»]
3AVRX-ray1.80B18-39[»]
3AYWX-ray2.90A/E1-136[»]
3AZEX-ray3.00A/E1-136[»]
3AZFX-ray2.70A/E1-136[»]
3AZGX-ray2.40A/E1-136[»]
3AZHX-ray3.49A/E1-136[»]
3AZIX-ray2.70A/E1-136[»]
3AZJX-ray2.89A/E1-136[»]
3AZKX-ray3.20A/E1-136[»]
3AZLX-ray2.70A/E1-136[»]
3AZMX-ray2.89A/E1-136[»]
3AZNX-ray3.00A/E1-136[»]
3B95X-ray2.99P2-16[»]
3KMTX-ray1.78G/H/I26-33[»]
3KQIX-ray1.78B2-13[»]
3LQIX-ray1.92R/S/T2-10[»]
3LQJX-ray1.90Q/T2-10[»]
3O34X-ray1.90B14-33[»]
3O35X-ray1.76D/E24-32[»]
3O37X-ray2.00E/F/G/H2-11[»]
3RIGX-ray2.00C/D5-16[»]
3RIYX-ray1.55C/D5-16[»]
3U4SX-ray2.15C/D8-15[»]
3U5NX-ray1.95C/D2-21[»]
3U5OX-ray2.70I/J/K/L/M/N/O/P2-23[»]
3U5PX-ray2.80I/J/K/L/M/N/O/P2-29[»]
3UEEX-ray2.61B/D2-13[»]
3UEFX-ray2.45B/D2-13[»]
3UIGX-ray2.40P/Q2-16[»]
3UIIX-ray2.60P/Q2-11[»]
3UIKX-ray2.70P/Q2-11[»]
3V43X-ray1.47Q2-19[»]
3W96X-ray3.00A/E1-136[»]
3W97X-ray3.20A/E1-136[»]
3W98X-ray3.42A/E29-136[»]
3W99X-ray3.00A/E1-136[»]
3WA9X-ray3.07A/E1-136[»]
3WAAX-ray3.20A/E1-136[»]
3ZG6X-ray2.20F5-14[»]
3ZVYX-ray1.95C/D2-9[»]
4A0JX-ray2.80C/D2-7[»]
4A0NX-ray2.74C2-7[»]
4A7JX-ray1.90B1-16[»]
4BD3NMR-B32-42[»]
4C1QX-ray2.30C2-10[»]
4F4UX-ray2.00C/D5-16[»]
4F56X-ray1.70C/D5-16[»]
4FWFX-ray2.70E2-21[»]
4HONX-ray1.80F/G7-16[»]
4I51X-ray1.90C/D4-12[»]
4L7XX-ray1.35U2-13[»]
4LK9X-ray1.60B2-22[»]
4LKAX-ray1.61B2-22[»]
4LLBX-ray2.50C/D2-22[»]
4N4HX-ray2.30B22-43[»]
ProteinModelPortalP68431.
SMRP68431. Positions 17-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113946. 163 interactions.
113947. 4 interactions.
113948. 10 interactions.
113949. 31 interactions.
113950. 5 interactions.
113951. 6 interactions.
113952. 4 interactions.
113953. 7 interactions.
113954. 22 interactions.
114458. 6 interactions.
DIPDIP-29371N.
IntActP68431. 54 interactions.
MINTMINT-256465.

PTM databases

PhosphoSiteP68431.

Polymorphism databases

DMDM55977055.

Proteomic databases

PaxDbP68431.
PRIDEP68431.

Protocols and materials databases

DNASU8350.
8352.
8353.
8355.
8356.
8357.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244661; ENSP00000244661; ENSG00000124693.
ENST00000305910; ENSP00000439660; ENSG00000256018.
ENST00000328488; ENSP00000329554; ENSG00000182572.
ENST00000356476; ENSP00000366999; ENSG00000197409.
ENST00000357647; ENSP00000350275; ENSG00000198366.
ENST00000359303; ENSP00000352252; ENSG00000197153.
ENST00000360408; ENSP00000353581; ENSG00000196966.
ENST00000369163; ENSP00000358160; ENSG00000203813.
ENST00000377831; ENSP00000367062; ENSG00000197409.
ENST00000446824; ENSP00000444823; ENSG00000256316.
ENST00000540144; ENSP00000439493; ENSG00000196532.
GeneID8350.
8351.
8352.
8353.
8354.
8355.
8356.
8357.
8358.
8968.
KEGGhsa:8350.
hsa:8351.
hsa:8352.
hsa:8353.
hsa:8354.
hsa:8355.
hsa:8356.
hsa:8357.
hsa:8358.
hsa:8968.
UCSCuc003nfp.1. human.

Organism-specific databases

CTD8350.
8351.
8352.
8353.
8354.
8355.
8356.
8357.
8358.
8968.
GeneCardsGC06M026031.
GC06M026197.
GC06M026250.
GC06M026271.
GC06M027914.
GC06M027920.
GC06P026020.
GC06P026065.
GC06P026225.
GC06P027777.
HGNCHGNC: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.
HPACAB037166.
CAB037178.
CAB037187.
MIM602810. gene.
602811. gene.
602812. gene.
602813. gene.
602814. gene.
602815. gene.
602816. gene.
602817. gene.
602818. gene.
602819. gene.
neXtProtNX_P68431.
PharmGKBPA29148.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2036.
HOVERGENHBG001172.
InParanoidP68431.
KOK11253.
OMAEARSHQE.
OrthoDBEOG7HB5C2.
PhylomeDBP68431.
TreeFamTF314241.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_172623. Chromatin organization.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.

Gene expression databases

BgeeP68431.
CleanExHS_HIST1H3A.
HS_HIST1H3B.
HS_HIST1H3C.
HS_HIST1H3D.
HS_HIST1H3E.
HS_HIST1H3F.
HS_HIST1H3G.
HS_HIST1H3H.
HS_HIST1H3I.
GenevestigatorP68431.

Family and domain databases

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

Other

ChiTaRSHIST1H3F. human.
EvolutionaryTraceP68431.
GeneWikiHIST1H3A.
HIST1H3B.
HIST1H3C.
HIST1H3D.
HIST1H3E.
HIST1H3F.
HIST1H3G.
HIST1H3H.
HIST1H3I.
HIST1H3J.
NextBio31272.
SOURCESearch...

Entry information

Entry nameH31_HUMAN
AccessionPrimary (citable) accession number: P68431
Secondary accession number(s): A0PJT7 expand/collapse secondary AC list , 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: April 16, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM