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P68433 (H31_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:Hist1h3a
Synonyms:H3a
AND
Name:Hist1h3g
Synonyms:H3.1-221, H3g
AND
Name:Hist1h3h
Synonyms:H3.1-291, H3h
AND
Name:Hist1h3i
Synonyms:H3.1-I, H3i
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.11

Post-translational modification

Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). 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.18 Ref.20 Ref.26 Ref.27

Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.

Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters By similarity.

Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication. Ref.13 Ref.15 Ref.16 Ref.18 Ref.20 Ref.21 Ref.26

Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1 RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin. Ref.12 Ref.14 Ref.17 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28

Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins By similarity. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination. Ref.29

Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression By similarity.

Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. Ref.30

Miscellaneous

This histone is only present in mammals.

Sequence similarities

Belongs to the histone H3 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

A612LO410942EBI-1179609,EBI-1179574From a different organism.
Carm1Q9WVG64EBI-1179609,EBI-4414343From a different organism.
Cbx1P839176EBI-79743,EBI-78119From a different organism.
SETD7Q8WTS62EBI-79743,EBI-1268586From a different organism.
YwhaeP6225911EBI-1179609,EBI-356480From a different organism.
YwhazP6310117EBI-1179609,EBI-354751From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 136135Histone H3.1
PRO_0000221249

Amino acid modifications

Modified residue31Asymmetric dimethylarginine; by PRMT6; alternate By similarity
Modified residue31Citrulline; alternate By similarity
Modified residue31Phosphoarginine; alternate Probable
Modified residue41Phosphothreonine; by GSG2 Ref.22
Modified residue51Allysine; alternate By similarity
Modified residue51N6,N6,N6-trimethyllysine; alternate Ref.13 Ref.26
Modified residue51N6,N6-dimethyllysine; alternate Ref.13 Ref.26
Modified residue51N6-acetyllysine; alternate Ref.26
Modified residue51N6-crotonyl-L-lysine; alternate Ref.30
Modified residue51N6-methyllysine; alternate Ref.13 Ref.26
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.26
Modified residue101N6,N6-dimethyllysine; alternate Ref.18 Ref.26
Modified residue101N6-acetyllysine; alternate Ref.20 Ref.26
Modified residue101N6-crotonyl-L-lysine; alternate Ref.30
Modified residue101N6-methyllysine; alternate Ref.18 Ref.26
Modified residue111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.12 Ref.17 Ref.22 Ref.24 Ref.25
Modified residue121Phosphothreonine; by PKC and CHEK1 By similarity
Modified residue151N6-acetyllysine Ref.15 Ref.18 Ref.26
Modified residue181Asymmetric dimethylarginine; by CARM1; alternate Ref.13 Ref.15 Ref.16 Ref.21
Modified residue181Citrulline; alternate Probable
Modified residue191N6-acetyllysine; alternate Ref.15 Ref.18 Ref.26
Modified residue191N6-crotonyl-L-lysine; alternate Ref.30
Modified residue191N6-methyllysine; alternate Ref.26
Modified residue241N6-acetyllysine; alternate Ref.15 Ref.18 Ref.26
Modified residue241N6-crotonyl-L-lysine; alternate Ref.30
Modified residue241N6-methyllysine; alternate Ref.26
Modified residue271Citrulline By similarity
Modified residue281N6,N6,N6-trimethyllysine; alternate Ref.18 Ref.26
Modified residue281N6,N6-dimethyllysine; alternate Ref.18 Ref.26
Modified residue281N6-acetyllysine; alternate Ref.26
Modified residue281N6-crotonyl-L-lysine; alternate Ref.30
Modified residue281N6-methyllysine; alternate Ref.18 Ref.26
Modified residue291Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.12 Ref.14 Ref.17 Ref.23 Ref.24 Ref.25
Modified residue371N6,N6,N6-trimethyllysine; alternate Probable
Modified residue371N6,N6-dimethyllysine; alternate Ref.18 Ref.26
Modified residue371N6-acetyllysine; alternate Ref.27
Modified residue371N6-methyllysine; alternate Ref.18 Ref.26
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.30
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.26
Modified residue801N6,N6-dimethyllysine; alternate Ref.18 Ref.26
Modified residue801N6-acetyllysine; alternate By similarity
Modified residue801N6-methyllysine; alternate Ref.18 Ref.26
Modified residue811Phosphothreonine By similarity
Modified residue1081Phosphothreonine By similarity
Modified residue1161N6-acetyllysine By similarity
Modified residue1231N6-acetyllysine; alternate By similarity
Modified residue1231N6-methyllysine; alternate Ref.18
Modified residue1291Phosphoarginine Probable
Modified residue1301Phosphoarginine Probable
Modified residue1321Phosphoarginine Potential

Secondary structure

............... 136
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68433 [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]"Structure of a cluster of mouse histone genes."
Sittman D.B., Graves R.A., Marzluff W.F.
Nucleic Acids Res. 11:6679-6697(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequences of four mouse histone H3 genes: implications for evolution of mouse histone genes."
Taylor J.D., Wellman S.E., Marzluff W.F.
J. Mol. Evol. 23:242-249(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3G AND HIST1H3H).
[3]"Nucleotide sequences of mouse histone genes H2A and H3.1."
Kosciessa U., Doenecke D.
Nucleic Acids Res. 17:8861-8861(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CD-1.
Tissue: Testis.
[4]"Characterization of the mouse histone gene cluster on chromosome 13: 45 histone genes in three patches spread over 1Mb."
Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F.
Genome Res. 6:688-701(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3I).
Strain: C57BL/CJ6.
[5]"The human and mouse replication-dependent histone genes."
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3A; HIST1H3G; HIST1H3H AND HIST1H3I).
[6]Franke K., Drabent B., Doenecke D.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[7]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. 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: Testis.
[8]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. 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.
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 58-64, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[11]"Changes in the levels of three different classes of histone mRNA during murine erythroleukemia cell differentiation."
Brown D.T., Wellman S.E., Sittman D.B.
Mol. Cell. Biol. 5:2879-2886(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[12]"Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation."
Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M., Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.
J. Biol. Chem. 274:25543-25549(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
[13]"Hormone-dependent, CARM1-directed, arginine-specific methylation of histone H3 on a steroid-regulated promoter."
Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A., Aswad D.W., Allis C.D., Hager G.L., Stallcup M.R.
Curr. Biol. 11:1981-1985(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5 AND ARG-18.
[14]"Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1."
Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M., Ma W.-Y., Dong Z.
J. Biol. Chem. 276:33213-33219(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-29.
[15]"Crosstalk between CARM1 methylation and CBP acetylation on histone H3."
Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.
Curr. Biol. 12:2090-2097(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT ARG-18.
[16]"Methylation at arginine 17 of histone H3 is linked to gene activation."
Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.
EMBO Rep. 3:39-44(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-18.
[17]"Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation."
Goto H., Yasui Y., Nigg E.A., Inagaki M.
Genes Cells 7:11-17(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
[18]"Identification of methylation and acetylation sites on mouse histone H3 using matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization tandem mass spectrometry."
Cocklin R.R., Wang M.
J. Protein Chem. 22:327-334(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10; LYS-28; LYS-37; LYS-80 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"Histone deimination antagonizes arginine methylation."
Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H., Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P., Bannister A.J., Kouzarides T.
Cell 118:545-553(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION.
[20]"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes."
Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.
Mol. Cell. Biol. 24:9630-9645(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-9, ACETYLATION AT LYS-10.
[21]"Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression."
Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C., Imhof R., Bedford M.T., Natoli G., Hottiger M.O.
EMBO J. 24:85-96(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-18.
[22]"The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment."
Dai J., Sultan S., Taylor S.S., Higgins J.M.G.
Genes Dev. 19:472-488(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-4 AND SER-11.
[23]"Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha."
Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.
J. Biol. Chem. 280:13545-13553(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-29.
[24]"MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2."
Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J., Nightingale K., Iborra F.J., Mahadevan L.C.
J. Cell Sci. 118:2247-2259(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
[25]"Stimulation of the Ras-MAPK pathway leads to independent phosphorylation of histone H3 on serine 10 and 28."
Dunn K.L., Davie J.R.
Oncogene 24:3492-3502(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
[26]"Organismal differences in post-translational modifications in histones H3 and H4."
Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J., Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.
J. Biol. Chem. 282:7641-7655(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 AND LYS-80, IDENTIFICATION BY MASS SPECTROMETRY.
[27]"Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification."
Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.
J. Biol. Chem. 282:7632-7640(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-37.
[28]"Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression."
Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H., Nakanishi M.
Cell 132:221-232(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-12 BY CHEK1.
[29]"The RING domain of RAG1 ubiquitylates histone H3: a novel activity in chromatin-mediated regulation of V(D)J joining."
Grazini U., Zanardi F., Citterio E., Casola S., Goding C.R., McBlane F.
Mol. Cell 37:282-293(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[30]"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: CROTONYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01684 Genomic DNA. Translation: CAA25839.1.
M32460 Genomic DNA. Translation: AAA37811.1.
M32462 Genomic DNA. Translation: AAA37813.1.
X16496 Genomic DNA. Translation: CAA34512.1.
U62670 Genomic DNA. Translation: AAB04763.1.
U62672 Genomic DNA. Translation: AAB04765.1.
AY158944 Genomic DNA. Translation: AAO06254.1.
AY158945 Genomic DNA. Translation: AAO06255.1.
AY158946 Genomic DNA. Translation: AAO06256.1.
AY158952 Genomic DNA. Translation: AAO06262.1.
Y12290 Genomic DNA. Translation: CAA72968.1.
AK006742 mRNA. Translation: BAB24722.1.
AK018952 mRNA. Translation: BAB31493.1.
AK155722 mRNA. Translation: BAE33402.1.
AL590388 Genomic DNA. Translation: CAI25837.1.
AL589651 Genomic DNA. Translation: CAI24113.1.
AL589651 Genomic DNA. Translation: CAI24105.1.
BC107285 mRNA. Translation: AAI07286.1.
BC107287 mRNA. Translation: AAI07288.1.
BC115816 mRNA. Translation: AAI15817.1.
BC116383 mRNA. Translation: AAI16384.1.
BC125355 mRNA. Translation: AAI25356.1.
BC125357 mRNA. Translation: AAI25358.1.
PIRA39525.
S06755.
RefSeqNP_038578.2. NM_013550.5.
NP_659539.1. NM_145073.2.
NP_835513.1. NM_178206.2.
NP_835514.1. NM_178207.2.
UniGeneMm.221301.
Mm.261657.
Mm.377874.
Mm.390558.
Mm.397328.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GUWNMR-B2-17[»]
1U35X-ray3.00A/E1-136[»]
2V83X-ray2.40D/E2-10[»]
2WP1X-ray2.10P/Q15-24[»]
2XL3X-ray2.70D/F2-9[»]
4EZHX-ray2.52C/D25-35[»]
ProteinModelPortalP68433.
SMRP68433. Positions 17-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP68433. 31 interactions.
MINTMINT-191105.

PTM databases

PhosphoSiteP68433.

Proteomic databases

PaxDbP68433.
PRIDEP68433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080859; ENSMUSP00000079670; ENSMUSG00000062417.
ENSMUST00000091701; ENSMUSP00000089293; ENSMUSG00000069265.
ENSMUST00000091754; ENSMUSP00000089348; ENSMUSG00000069312.
ENSMUST00000099704; ENSMUSP00000097295; ENSMUSG00000075032.
GeneID319152.
319153.
360198.
97908.
KEGGmmu:319152.
mmu:319153.
mmu:360198.
mmu:97908.
UCSCuc007prc.1. mouse.

Organism-specific databases

CTD8350.
8354.
8355.
8357.
MGIMGI:2668828. Hist1h3a.
MGI:2145541. Hist1h3g.
MGI:2448349. Hist1h3h.
MGI:2448350. Hist1h3i.

Phylogenomic databases

eggNOGCOG2036.
GeneTreeENSGT00740000114849.
HOVERGENHBG001172.
InParanoidP68433.
KOK11253.
OMARISKMAR.
OrthoDBEOG7HB5C2.
PhylomeDBP68433.
TreeFamTF314241.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_198624. Meiosis.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Gene expression databases

BgeeP68433.
CleanExMM_HIST1H3A.
MM_HIST1H3G.
MM_HIST1H3H.
MM_HIST1H3I.
GenevestigatorP68433.

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

EvolutionaryTraceP68433.
NextBio353176.
SOURCESearch...

Entry information

Entry nameH31_MOUSE
AccessionPrimary (citable) accession number: P68433
Secondary accession number(s): P02295 expand/collapse secondary AC list , P02296, P16106, Q05A97, Q3B7Z8, Q3B7Z9, Q5T009
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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