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P84244 (H33_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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

Names and origin

Protein namesRecommended name:
Histone H3.3
Gene names
Name:H3f3a
Synonyms:H3.3a
AND
Name:H3f3b
Synonyms:H3.3b
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

Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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. Interacts with HIRA, a chaperone required for its incorporation into nucleosomes.

Subcellular location

Nucleus. Chromosome.

Developmental stage

Expressed throughout the cell cycle independently of DNA synthesis. Ref.2

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.9 Ref.12 Ref.14 Ref.20 Ref.21

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.

Specifically enriched in modifications associated with active chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80. 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), which are linked to gene repression, are underrepresented. 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.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.20

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. Phosphorylation on Ser-32 (H3S31ph) is specific to regions bordering centromeres in metaphase chromosomes. metaphase chromosomes. Ref.7 Ref.8 Ref.11 Ref.16 Ref.17 Ref.18 Ref.19

Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination By similarity. Ref.22

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.23

Sequence similarities

Belongs to the histone H3 family.

Sequence caution

The sequence AAH92300.1 differs from that shown. Reason: Frameshift at position 127.

The sequence BAB27616.1 differs from that shown. Reason: Frameshift at position 99.

The sequence BAE35387.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Citrullination
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 136135Histone H3.3
PRO_0000221251

Amino acid modifications

Modified residue31Asymmetric dimethylarginine; by PRMT6; alternate By similarity
Modified residue31Citrulline; alternate By similarity
Modified residue41Phosphothreonine; by GSG2 Ref.16
Modified residue51Allysine; alternate By similarity
Modified residue51N6,N6,N6-trimethyllysine; alternate Ref.20
Modified residue51N6,N6-dimethyllysine; alternate Ref.20
Modified residue51N6-acetyllysine; alternate Ref.20
Modified residue51N6-crotonyl-L-lysine; alternate Ref.23
Modified residue51N6-methyllysine; alternate Ref.20
Modified residue71Phosphothreonine; by PKC By similarity
Modified residue91Citrulline; alternate Probable
Modified residue91Symmetric dimethylarginine; by PRMT5; alternate Ref.14
Modified residue101N6,N6,N6-trimethyllysine; alternate Ref.12 Ref.20
Modified residue101N6,N6-dimethyllysine; alternate Ref.12 Ref.20
Modified residue101N6-acetyllysine; alternate Ref.14 Ref.20
Modified residue101N6-crotonyl-L-lysine; alternate Ref.23
Modified residue101N6-methyllysine; alternate Ref.12 Ref.20
Modified residue111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.7 Ref.11 Ref.16 Ref.18 Ref.19
Modified residue121Phosphothreonine; by PKC By similarity
Modified residue151N6-acetyllysine Ref.9 Ref.12 Ref.20
Modified residue181Asymmetric dimethylarginine; by CARM1; alternate Ref.9 Ref.10 Ref.15
Modified residue181Citrulline; alternate
Modified residue191N6-acetyllysine; alternate Ref.9 Ref.12 Ref.20
Modified residue191N6-crotonyl-L-lysine; alternate Ref.23
Modified residue191N6-methyllysine; alternate Ref.20
Modified residue241N6-acetyllysine; alternate Ref.9 Ref.12 Ref.20
Modified residue241N6-crotonyl-L-lysine; alternate Ref.23
Modified residue241N6-methyllysine; alternate Ref.20
Modified residue271Citrulline By similarity
Modified residue281N6,N6,N6-trimethyllysine; alternate Ref.12 Ref.20
Modified residue281N6,N6-dimethyllysine; alternate Ref.12 Ref.20
Modified residue281N6-acetyllysine; alternate Ref.20
Modified residue281N6-crotonyl-L-lysine; alternate Ref.23
Modified residue281N6-methyllysine; alternate Ref.12 Ref.20
Modified residue291Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.7 Ref.8 Ref.11 Ref.17 Ref.18 Ref.19
Modified residue321Phosphoserine By similarity
Modified residue371N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue371N6,N6-dimethyllysine; alternate Ref.12 Ref.20
Modified residue371N6-acetyllysine; alternate Ref.21
Modified residue371N6-methyllysine; alternate Ref.12 Ref.20
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.23
Modified residue571N6-methyllysine; by EHMT2; alternate By similarity
Modified residue581Phosphoserine By similarity
Modified residue651N6-methyllysine By similarity
Modified residue801N6,N6,N6-trimethyllysine; alternate Ref.12 Ref.20
Modified residue801N6,N6-dimethyllysine; alternate Ref.12 Ref.20
Modified residue801N6-acetyllysine; alternate By similarity
Modified residue801N6-methyllysine; alternate Ref.12 Ref.20
Modified residue811Phosphothreonine By similarity
Modified residue1081Phosphothreonine By similarity
Modified residue1161N6-acetyllysine By similarity
Modified residue1231N6-acetyllysine; alternate By similarity
Modified residue1231N6-methyllysine; alternate Probable

Experimental info

Sequence conflict751I → T in AAH21768. Ref.5
Sequence conflict991A → E in BAE31789. Ref.4
Sequence conflict991A → E in BAE30411. Ref.4
Sequence conflict1291R → C in X91866. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P84244 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5158ED279E6F9E1C

FASTA13615,328
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE 

        70         80         90        100        110        120 
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI 

       130 
MPKDIQLARR IRGERA 

« Hide

References

« Hide 'large scale' references
[1]"Expression of a mouse replacement histone H3.3 gene with a highly conserved 3' noncoding region during SV40- and polyoma-induced Go to S-phase transition."
Hraba-Renevey S., Kress M.
Nucleic Acids Res. 17:2449-2461(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H3F3B).
[2]"Differential expression of the murine histone genes H3.3A and H3.3B."
Bramlage B., Kosciessa U., Doenecke D.
Differentiation 62:13-20(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H3F3A AND H3F3B), DEVELOPMENTAL STAGE.
Tissue: Spermatid.
[3]"H3.3A variant histone mRNA containing an alpha-globin insertion: modulated expression during mouse gametogenesis correlates with meiotic onset."
Lopez-Alanon D.M., Lopez-Fernandez L.A., Castaneda V., Krimer D.B., Del Mazo J.
DNA Cell Biol. 16:639-644(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H3F3A).
Strain: Swiss.
Tissue: Ovary.
[4]"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] (H3F3A AND H3F3B).
Strain: BALB/c, C57BL/6J, DBA/2 and NOD.
Tissue: Bone marrow, Egg, Head, Kidney, Muellerian duct, Stomach and Thymus.
[5]"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] (H3F3A AND H3F3B).
Strain: C57BL/6 and FVB/N.
Tissue: Brain, Colon, Mammary tumor and Retina.
[6]"A new family of 'H3L-like' histone genes."
Mancini P., Pulcrano G., Piscopo M., Aniello F., Branno M., Fucci L.
J. Mol. Evol. 59:458-463(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-122.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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
X13605 mRNA. Translation: CAA31940.1.
Z85979 mRNA. Translation: CAB06625.1.
X91866 mRNA. No translation available.
AK002928 mRNA. Translation: BAB22464.1.
AK011431 mRNA. Translation: BAB27616.1. Frameshift.
AK037900 mRNA. Translation: BAC29895.1.
AK088075 mRNA. Translation: BAC40130.1.
AK135839 mRNA. Translation: BAE22687.1.
AK150467 mRNA. Translation: BAE29584.1.
AK150468 mRNA. Translation: BAE29585.1.
AK150591 mRNA. Translation: BAE29685.1.
AK150928 mRNA. Translation: BAE29966.1.
AK151274 mRNA. Translation: BAE30261.1.
AK151336 mRNA. Translation: BAE30314.1.
AK151451 mRNA. Translation: BAE30411.1.
AK151634 mRNA. Translation: BAE30566.1.
AK151658 mRNA. Translation: BAE30586.1.
AK151661 mRNA. Translation: BAE30589.1.
AK151869 mRNA. Translation: BAE30757.1.
AK152293 mRNA. Translation: BAE31102.1.
AK152453 mRNA. Translation: BAE31231.1.
AK152455 mRNA. Translation: BAE31233.1.
AK152623 mRNA. Translation: BAE31366.1.
AK152911 mRNA. Translation: BAE31590.1.
AK153034 mRNA. Translation: BAE31666.1.
AK153189 mRNA. Translation: BAE31789.1.
AK153239 mRNA. Translation: BAE31831.1.
AK153294 mRNA. Translation: BAE31877.1.
AK153371 mRNA. Translation: BAE31939.1.
AK153530 mRNA. Translation: BAE32069.1.
AK159615 mRNA. Translation: BAE35232.1.
AK159807 mRNA. Translation: BAE35387.1. Frameshift.
AK159850 mRNA. Translation: BAE35427.1.
AK160677 mRNA. Translation: BAE35953.1.
AK161675 mRNA. Translation: BAE36524.1.
AK162040 mRNA. Translation: BAE36694.1.
AK163244 mRNA. Translation: BAE37253.1.
AK167828 mRNA. Translation: BAE39850.1.
AK167879 mRNA. Translation: BAE39892.1.
AK168197 mRNA. Translation: BAE40157.1.
AK168698 mRNA. Translation: BAE40542.1.
AK169042 mRNA. Translation: BAE40831.1.
AK169226 mRNA. Translation: BAE40995.1.
BC002268 mRNA. Translation: AAH02268.1.
BC012687 mRNA. Translation: AAH12687.1.
BC021768 mRNA. Translation: AAH21768.1.
BC037730 mRNA. Translation: AAH37730.1.
BC083353 mRNA. Translation: AAH83353.1.
BC088835 mRNA. Translation: AAH88835.1.
BC092043 mRNA. Translation: AAH92043.1.
BC092300 mRNA. Translation: AAH92300.1. Frameshift.
BC106177 mRNA. Translation: AAI06178.1.
AY383567 Genomic DNA. Translation: AAQ96274.1.
PIRS04186.
RefSeqNP_032236.1. NM_008210.4.
NP_032237.1. NM_008211.3.
XP_006532311.1. XM_006532248.1.
UniGeneMm.138832.
Mm.18516.
Mm.315189.
Mm.316825.
Mm.322735.
Mm.371563.
Mm.389332.
Mm.442502.
Mm.471842.

3D structure databases

ProteinModelPortalP84244.
SMRP84244. Positions 17-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200196. 18 interactions.
200199. 2 interactions.
IntActP84244. 39 interactions.
MINTMINT-4097105.

Proteomic databases

PaxDbP84244.
PRIDEP84244.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016703; ENSMUSP00000016703; ENSMUSG00000016559.
ENSMUST00000106454; ENSMUSP00000102062; ENSMUSG00000016559.
ENSMUST00000161308; ENSMUSP00000124509; ENSMUSG00000060743.
ENSMUST00000162814; ENSMUSP00000125104; ENSMUSG00000060743.
GeneID15078.
15081.
KEGGmmu:15078.
mmu:15081.
UCSCuc007dwr.1. mouse.

Organism-specific databases

CTD3020.
3021.
MGIMGI:1097686. H3f3a.
MGI:1101768. H3f3b.

Phylogenomic databases

eggNOGCOG2036.
GeneTreeENSGT00750000117538.
HOVERGENHBG001172.
InParanoidP84244.
KOK11253.
OMAQEATESY.
OrthoDBEOG7HB5C2.
PhylomeDBP84244.
TreeFamTF314241.

Enzyme and pathway databases

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

Gene expression databases

BgeeP84244.
CleanExMM_H3F3A.
MM_H3F3B.
GenevestigatorP84244.

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

ChiTaRSH3F3B. mouse.
NextBio287482.
PROP84244.
SOURCESearch...

Entry information

Entry nameH33_MOUSE
AccessionPrimary (citable) accession number: P84244
Secondary accession number(s): P06351 expand/collapse secondary AC list , P33155, Q3TW79, Q3U6D6, Q569U8, Q5HZY8, Q6TXQ5, Q8VDJ2, Q9D0H3, Q9V3W4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 101 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

MGD cross-references

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