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P84228 (H32_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3.2
Gene names
Name:Hist1h3b
Synonyms:H3-53, H3.2, H3b
AND
Name:Hist1h3c
Synonyms:H3-143
AND
Name:Hist1h3d
Synonyms:H3-B
AND
Name:Hist1h3e
Synonyms:H3-F
AND
Name:Hist1h3f
Synonyms:H3.2-221, H3f
AND
Name:Hist2h3b
Synonyms:H3.2-616
AND
Name:Hist2h3c1
Synonyms:H3.2-615, Hist2h3ca1
AND
Name:Hist2h3c2
Synonyms:H3.2-614, Hist2h3ca2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

General annotation (Comments)

Function

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

Subunit structure

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. During nucleosome assembly the chaperone ASF1A interacts with the histone H3-H4 heterodimer By similarity.

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 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.15 Ref.16 Ref.18 Ref.20 Ref.21 Ref.27

Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin. Ref.13 Ref.14 Ref.17 Ref.22 Ref.23 Ref.24 Ref.25

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.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 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.29

Sequence similarities

Belongs to the histone H3 family.

Sequence caution

The sequence AAH94041.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAO06264.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 136135Histone H3.2
PRO_0000221250

Amino acid modifications

Modified residue31Asymmetric dimethylarginine; by PRMT6 By similarity
Modified residue41Phosphothreonine; by GSG2 Ref.22
Modified residue51Allysine; alternate By similarity
Modified residue51N6,N6,N6-trimethyllysine; alternate Ref.27
Modified residue51N6,N6-dimethyllysine; alternate Ref.27
Modified residue51N6-acetyllysine; alternate Ref.27
Modified residue51N6-crotonyl-L-lysine; alternate Ref.29
Modified residue51N6-methyllysine; alternate Ref.27
Modified residue71Phosphothreonine; by PKC By similarity
Modified residue91Citrulline; alternate Probable
Modified residue91Symmetric dimethylarginine; by PRMT5; alternate Ref.20
Modified residue101N6,N6,N6-trimethyllysine; alternate Ref.18 Ref.27
Modified residue101N6,N6-dimethyllysine; alternate Ref.18 Ref.27
Modified residue101N6-acetyllysine; alternate Ref.20 Ref.27
Modified residue101N6-crotonyl-L-lysine; alternate Ref.29
Modified residue101N6-methyllysine; alternate Ref.18 Ref.27
Modified residue111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.13 Ref.17 Ref.22 Ref.24 Ref.25
Modified residue121Phosphothreonine; by PKC By similarity
Modified residue151N6-acetyllysine Ref.15 Ref.18 Ref.27
Modified residue181Asymmetric dimethylarginine; by CARM1; alternate Ref.15 Ref.16 Ref.21
Modified residue181Citrulline; alternate By similarity
Modified residue191N6-acetyllysine; alternate Ref.15 Ref.18 Ref.27
Modified residue191N6-crotonyl-L-lysine; alternate Ref.29
Modified residue191N6-methyllysine; alternate Ref.27
Modified residue241N6-acetyllysine; alternate Ref.15 Ref.18 Ref.27
Modified residue241N6-crotonyl-L-lysine; alternate Ref.29
Modified residue241N6-methyllysine; alternate Ref.27
Modified residue281N6,N6,N6-trimethyllysine; alternate Ref.18 Ref.27
Modified residue281N6,N6-dimethyllysine; alternate Ref.18 Ref.27
Modified residue281N6-acetyllysine; alternate Ref.27
Modified residue281N6-crotonyl-L-lysine; alternate Ref.29
Modified residue281N6-methylated lysine; alternate By similarity
Modified residue281N6-methyllysine; alternate Ref.18 Ref.27
Modified residue291Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.13 Ref.14 Ref.17 Ref.23 Ref.24 Ref.25
Modified residue371N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue371N6,N6-dimethyllysine; alternate Ref.18 Ref.27
Modified residue371N6-acetyllysine; alternate Ref.26
Modified residue371N6-methyllysine; alternate Ref.18 Ref.27
Modified residue381N6-methyllysine By similarity
Modified residue421Phosphotyrosine By similarity
Modified residue571N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue571N6-acetyllysine; alternate By similarity
Modified residue571N6-crotonyl-L-lysine; alternate Ref.29
Modified residue571N6-methyllysine; by EHMT2; alternate By similarity
Modified residue581Phosphoserine By similarity
Modified residue651N6-methyllysine By similarity
Modified residue801N6,N6,N6-trimethyllysine; alternate Ref.18 Ref.27
Modified residue801N6,N6-dimethyllysine; alternate Ref.18 Ref.27
Modified residue801N6-acetyllysine; alternate By similarity
Modified residue801N6-methyllysine; alternate Ref.18 Ref.27
Modified residue811Phosphothreonine By similarity
Modified residue1081Phosphothreonine By similarity
Modified residue1231N6-acetyllysine; alternate By similarity
Modified residue1231N6-methyllysine; alternate Probable

Sequences

Sequence LengthMass (Da)Tools
P84228 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6FD8508EA50A0EEC

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

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

       130 
MPKDIQLARR IRGERA

« Hide

References

« Hide 'large scale' references
[1]"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] (HIST1H3B).
[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] (HIST2H3C2 AND HIST1H3F).
[3]"The mouse histone H2a.2 gene from chromosome 3."
Hurt M.M., Chodchoy N., Marzluff W.F.
Nucleic Acids Res. 17:8876-8876(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
Tissue: Liver.
[4]"Structure of a mouse histone-encoding gene cluster."
Gruber A., Streit A., Reist M., Benninger P., Boehni R., Schuemperli D.
Gene 95:303-304(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3B).
Strain: BALB/c.
[5]"Selection on silent sites in the rodent histone H3 gene family."
DeBry R.W., Marzluff W.F.
Genetics 138:191-202(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3C).
[6]"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] (HIST1H3C).
Strain: C57BL/6J.
[7]"Characterization of the 55-kb mouse histone gene cluster on chromosome 3."
Wang Z.-F., Tisovec R., Debry R.W., Frey M.R., Matera A.G., Marzluff W.F.
Genome Res. 6:702-714(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3D; HIST1H3E; HIST2H3B AND HIST2H3CA1).
[8]"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] (HIST1H3B; HIST1H3C; HIST1H3D; HIST1H3E; HIST1H3F; HIST2H3B; HIST2H3C1 AND HIST2H3C2).
[9]"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. expand/collapse author list , 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: Embryo.
[10]"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. expand/collapse author list , 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.
[11]"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] (HIST2H3C2).
Strain: FVB/N.
Tissue: Kidney.
[12]"An alternative pathway of histone mRNA 3' end formation in mouse round spermatids."
Moss S.B., Ferry R.A., Groudine M.
Nucleic Acids Res. 22:3160-3166(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 79-136.
Strain: CD-1.
Tissue: Testis.
[13]"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.
[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]"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.
[27]"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.
[28]"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.
[29]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X01685 Genomic DNA. Translation: CAA25840.1.
M32459 Genomic DNA. Translation: AAA37810.1.
M32461 Genomic DNA. Translation: AAA37812.1.
X16148 Genomic DNA. Translation: CAA34274.1.
M33989 Genomic DNA. Translation: AAA37764.1.
X80328 Genomic DNA. Translation: CAA56577.1.
U62669 Genomic DNA. Translation: AAB04760.1.
U62671 Genomic DNA. Translation: AAB04764.1.
U62674 Genomic DNA. Translation: AAB04771.1.
U62675 Genomic DNA. Translation: AAB04772.1.
AY158941 Genomic DNA. Translation: AAO06251.1.
AY158947 Genomic DNA. Translation: AAO06257.1.
AY158948 Genomic DNA. Translation: AAO06258.1.
AY158949 Genomic DNA. Translation: AAO06259.1.
AY158950 Genomic DNA. Translation: AAO06260.1.
AY158951 Genomic DNA. Translation: AAO06261.1.
AY158954 Genomic DNA. Translation: AAO06264.1. Different initiation.
AY158955 Genomic DNA. Translation: AAO06265.1.
AK010121 mRNA. Translation: BAB26714.1.
AK020421 mRNA. Translation: BAB32097.1.
AL590388 Genomic DNA. Translation: CAI25840.1.
AL590388 Genomic DNA. Translation: CAI25844.1.
BC015270 mRNA. Translation: AAH15270.1.
BC094041 mRNA. Translation: AAH94041.1. Different initiation.
BC101954 mRNA. Translation: AAI01955.1.
BC101955 mRNA. Translation: AAI01956.1.
BC101956 mRNA. Translation: AAI01957.1.
BC103549 mRNA. Translation: AAI03550.1.
BC120800 mRNA. Translation: AAI20801.1.
BC120802 mRNA. Translation: AAI20803.1.
BC132488 mRNA. Translation: AAI32489.1.
BC132490 mRNA. Translation: AAI32491.1.
Z30939 mRNA. Translation: CAA83209.1.
IPIIPI00230730.
PIRA39525.
JH0304.
S06743.
S45111. S48060.
RefSeqNP_038576.1. NM_013548.3.
NP_473386.1. NM_054045.3.
NP_783584.1. NM_175653.1.
NP_835510.1. NM_178203.1.
NP_835511.1. NM_178204.1.
NP_835512.1. NM_178205.1.
NP_835587.1. NM_178215.1.
NP_835734.2. NM_178216.2.
UniGeneMm.221389.
Mm.261658.
Mm.262517.
Mm.342457.
Mm.347699.
Mm.358797.
Mm.383293.
Mm.422680.
Mm.439791.
Mm.474786.

3D structure databases

ProteinModelPortalP84228.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-49015N.
IntActP84228. 24 interactions.

PTM databases

PhosphoSiteP84228.

Proteomic databases

PaxDbP84228.
PRIDEP84228.

Protocols and materials databases

DNASU319149.
319150.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075558; ENSMUSP00000074994; ENSMUSG00000059309.
ENSMUST00000091703; ENSMUSP00000089295; ENSMUSG00000069267.
ENSMUST00000091752; ENSMUSP00000089346; ENSMUSG00000069310.
ENSMUST00000098843; ENSMUSP00000096442; ENSMUSG00000074403.
ENSMUST00000105105; ENSMUSP00000100737; ENSMUSG00000062808.
ENSMUST00000105107; ENSMUSP00000100739; ENSMUSG00000069273.
ENSMUST00000167403; ENSMUSP00000135215; ENSMUSG00000081058.
ENSMUST00000176059; ENSMUSP00000134751; ENSMUSG00000093769.
ENSMUST00000177796; ENSMUSP00000137496; ENSMUSG00000093769.
GeneID15077.
260423.
319148.
319149.
319150.
319151.
319154.
97114.
KEGGmmu:15077.
mmu:260423.
mmu:319148.
mmu:319149.
mmu:319150.
mmu:319151.
mmu:319154.
mmu:319190.
mmu:97114.

Organism-specific databases

CTD15077.
319154.
8349.
8351.
8352.
8353.
8358.
8968.
97114.
MGIMGI:2448319. Hist1h3b.
MGI:2448320. Hist1h3c.
MGI:2448322. Hist1h3d.
MGI:2448326. Hist1h3e.
MGI:2448329. Hist1h3f.
MGI:2448351. Hist2h3b.
MGI:2448355. Hist2h3c1.
MGI:2448357. Hist2h3c2.

Phylogenomic databases

eggNOGCOG2036.
GeneTreeENSGT00670000097727.
HOVERGENHBG001172.
InParanoidP84228.
KOK11252.
K11253.
OrthoDBEOG412M6S.

Enzyme and pathway databases

ReactomeREACT_118161. Cell Cycle.
REACT_120463. Meiosis.
REACT_27235. Meiotic Recombination (mouse).
REACT_75800. Meiotic Synapsis (mouse).

Gene expression databases

ArrayExpressP84228.
BgeeP84228.
CleanExMM_HIST1H3B.
MM_HIST1H3C.
MM_HIST1H3D.
MM_HIST1H3E.
MM_HIST1H3F.
MM_HIST2H3C1.
MM_HIST2H3C2.
GenevestigatorP84228.
GermOnlineENSMUSG00000059309. Mus musculus.
ENSMUSG00000068853. Mus musculus.
ENSMUSG00000069267. Mus musculus.
ENSMUSG00000069273. Mus musculus.
ENSMUSG00000070392. Mus musculus.
ENSMUSG00000071478. Mus musculus.
ENSMUSG00000074403. Mus musculus.
ENSMUSG00000075032. Mus musculus.

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. Histone-fold. 1 hit.
PROSITEPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio287476.
SOURCESearch...

Entry information

Entry nameH32_MOUSE
AccessionPrimary (citable) accession number: P84228
Secondary accession number(s): A3KMN6 expand/collapse secondary AC list , P02295, P02297, P16105, P17269, P17320, Q60582, Q78E59, Q8CGN9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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