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P62804 (H4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histone H4

Cleaved into the following chain:

  1. Osteogenic growth peptide
    Short name=OGP
Gene names
Name:Hist1h4b
Synonyms:Hist4
AND
Name:Hist1h4m
AND
Name:Hist4h4
Synonyms:H4ft
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length103 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.

Osteogenic growth peptide (OGP) stimulates osteogenesis and hematopoiesis.

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. Note: Osteogenic growth peptide is secreted by a mechanism independent from a hydrophobic signal sequence. The mature peptide may be imported into secretory lysosomes by an ABCA1-related protein. Ref.9

Tissue specificity

OGP is found in serum. A potentially OGP-specific transcript is highly expressed in spleen with lower levels in lung, liver, thymus, spinal chord, pituitary gland, adrenal gland, bone marrow and lymph nodes as well as very low levels in kidney, heart and brain. Ref.4

Post-translational modification

Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin By similarity.

Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation By similarity.

Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage By similarity.

Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by SET8. Trimethylation is performed by SUV420H1 and SUV420H2 and induces gene silencing By similarity. Ref.6

Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4 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. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me) By similarity.

Sumoylated, which is associated with transcriptional 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 By similarity.

Sequence similarities

Belongs to the histone H4 family.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Histone H4 (identifier: P62804-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform OGP precursor (identifier: P62804-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 103102Histone H4
PRO_0000158355
Peptide90 – 10314Osteogenic growth peptide Ref.9
PRO_0000225591

Regions

DNA binding17 – 215

Amino acid modifications

Modified residue21N-acetylserine Ref.6
Modified residue21Phosphoserine By similarity
Modified residue41Asymmetric dimethylarginine; by PRMT1; alternate By similarity
Modified residue41Citrulline; alternate By similarity
Modified residue41Omega-N-methylarginine; by PRMT1; alternate By similarity
Modified residue41Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate By similarity
Modified residue61N6-acetyllysine; alternate By similarity
Modified residue61N6-crotonyl-L-lysine; alternate By similarity
Modified residue91N6-acetyllysine; alternate By similarity
Modified residue91N6-crotonyl-L-lysine; alternate By similarity
Modified residue131N6-acetyllysine; alternate By similarity
Modified residue131N6-crotonyl-L-lysine; alternate By similarity
Modified residue171N6-acetyllysine; alternate Ref.6
Modified residue171N6-crotonyl-L-lysine; alternate By similarity
Modified residue211N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue211N6,N6-dimethyllysine; alternate Ref.6
Modified residue211N6-methyllysine; alternate Ref.6
Modified residue321N6-acetyllysine By similarity
Modified residue481Phosphoserine; by PAK2 By similarity
Modified residue521Phosphotyrosine By similarity
Modified residue891Phosphotyrosine By similarity
Modified residue921N6-acetyllysine; alternate By similarity
Cross-link92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Natural variations

Alternative sequence1 – 8484Missing in isoform OGP precursor.
VSP_018804

Sequences

Sequence LengthMass (Da)Tools
Isoform Histone H4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A9E5DFD3F8B97598

FASTA10311,367
        10         20         30         40         50         60 
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK 

        70         80         90        100 
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG 

« Hide

Isoform OGP precursor [UniParc].

Checksum: DA46847BA27B7A8B
Show »

FASTA192,131

References

« Hide 'large scale' references
[1]"A rat histone H4 gene closely associated with the testis-specific H1t gene."
Grimes S., Weisz-Carrington P., Daum H. III, Smith J., Green L., Wright K., Stein G., Stein J.
Exp. Cell Res. 173:534-545(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"Comparison of the structural organization and expression of germinal and somatic rat histone H4 genes."
Wolfe S.A., Anderson J.V., Grimes S.R., Stein G.S., Stein J.S.
Biochim. Biophys. Acta 1007:140-150(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
[3]"Protein-DNA interactions within the rat histone H4t promoter."
Wolfe S.A., Grimes S.R.
J. Biol. Chem. 266:6637-6643(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Correlation between the expression of the histone H4 mRNA variant H4-v.1 and the levels of histone H4-(86-100) and H4-(89-102) (OGP) in various rat tissues and alveolar macrophages."
Poirier R., Lemaire I., Dumont M., Leduc N., Le H.T., Lemaire S.
Peptides 26:1503-1511(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Spleen.
[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].
Tissue: Prostate.
[6]"Primary structure of glycine-rich and arginine-rich histone isolated from chloroleukemic tumor of the rat."
Sautiere P., Tyrou D., Moschetto Y., Biserte G.
Biochimie 53:479-483(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2 AND LYS-17, METHYLATION AT LYS-21.
[7]"Evidence indicating proximity in the nucleosome between the histone H4 N termini and the globular domain of histone H1."
Baneres J.L., Essalouh L., Jariel-Encontre I., Mesnier D., Garrod S., Parello J.
J. Mol. Biol. 243:48-59(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 5-14 AND 19-32.
Tissue: Liver.
[8]Lubec G., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-78, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
[9]"Histone H4-related osteogenic growth peptide (OGP): a novel circulating stimulator of osteoblastic activity."
Bab I., Gazit D., Chorev M., Muhlrad A., Shteyer A., Greenberg Z., Namdar M., Kahn A.
EMBO J. 11:1867-1873(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 90-103, SUBCELLULAR LOCATION.
[10]"Biosynthesis of osteogenic growth peptide via alternative translational initiation at AUG85 of histone H4 mRNA."
Bab I., Smith E., Gavish H., Attar-Namdar M., Chorev M., Chen Y.C., Muhlrad A., Birnbaum M.J., Stein G., Frenkel B.
J. Biol. Chem. 274:14474-14481(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION.
[11]"Mass spectrometry-compatible silver staining of histones resolved on acetic acid-urea-Triton PAGE."
Pramod K.S., Bharat K., Sanjay G.
Proteomics 9:2589-2592(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27433 Genomic DNA. Translation: AAA60735.1.
X13554 Genomic DNA. Translation: CAA31906.1.
M28409 Genomic DNA. Translation: AAA41306.1.
AY936209 mRNA. Translation: AAX28930.1.
BC100619 mRNA. Translation: AAI00620.1.
IPIIPI00561052.
IPI00760138.
PIRHSRT4. A91265.
S53749.
RefSeqNP_001116941.1. NM_001123469.1.
NP_001258150.1. NM_001271221.1.
NP_073177.1. NM_022686.2.
XP_001055174.1. XM_001055174.3.
XP_001055696.1. XM_001055696.2.
XP_001057149.1. XM_001057149.3.
XP_001072344.1. XM_001072344.2.
XP_002725326.2. XM_002725280.2.
XP_002728527.2. XM_002728481.2.
XP_003749898.1. XM_003749850.1.
XP_003749900.1. XM_003749852.1.
XP_003749902.1. XM_003749854.1.
XP_003749904.1. XM_003749856.1.
XP_003753028.1. XM_003752980.1.
XP_003753031.1. XM_003752983.1.
XP_003753043.1. XM_003752995.1.
XP_003754003.1. XM_003753955.1.
XP_575704.1. XM_575704.4.
XP_578415.2. XM_578415.3.
UniGeneRn.10465.
Rn.1659.
Rn.220155.
Rn.44120.

3D structure databases

ProteinModelPortalP62804.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000039949.

PTM databases

PhosphoSiteP62804.

Proteomic databases

PaxDbP62804.
PRIDEP62804.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000040210; ENSRNOP00000039602; ENSRNOG00000032224.
ENSRNOT00000043151; ENSRNOP00000041042; ENSRNOG00000030142.
ENSRNOT00000071512; ENSRNOP00000065233; ENSRNOG00000045840.
ENSRNOT00000071518; ENSRNOP00000066669; ENSRNOG00000046900.
ENSRNOT00000071690; ENSRNOP00000064783; ENSRNOG00000046141.
ENSRNOT00000072147; ENSRNOP00000066653; ENSRNOG00000048735.
ENSRNOT00000072286; ENSRNOP00000067502; ENSRNOG00000050933.
ENSRNOT00000074109; ENSRNOP00000066622; ENSRNOG00000046636.
ENSRNOT00000074198; ENSRNOP00000066695; ENSRNOG00000048642.
ENSRNOT00000074356; ENSRNOP00000067494; ENSRNOG00000049086.
ENSRNOT00000074526; ENSRNOP00000067813; ENSRNOG00000045978.
ENSRNOT00000075028; ENSRNOP00000066550; ENSRNOG00000047826.
ENSRNOT00000075065; ENSRNOP00000067176; ENSRNOG00000048215.
GeneID100360950.
100912290.
100912418.
100912489.
100912564.
291152.
295277.
500351.
502913.
64627.
679983.
680097.
680430.
KEGGrno:100360950.
rno:100912290.
rno:100912418.
rno:100912489.
rno:100912564.
rno:291152.
rno:295277.
rno:500351.
rno:502913.
rno:64627.
rno:679983.
rno:680097.
rno:680430.
UCSCRGD:620814. rat.

Organism-specific databases

CTD100041230.
500351.
8366.
8370.
97122.
RGD620814. Hist1h4b.

Phylogenomic databases

eggNOGCOG2036.
GeneTreeENSGT00690000101710.
ENSGT00690000101714.
HOGENOMHOG000234654.
HOVERGENHBG051878.
InParanoidP62804.
KOK11254.
OrthoDBEOG4KD6NP.

Gene expression databases

GenevestigatorP62804.
GermOnlineENSRNOG00000028928. Rattus norvegicus.
ENSRNOG00000030142. Rattus norvegicus.
ENSRNOG00000031512. Rattus norvegicus.
ENSRNOG00000031838. Rattus norvegicus.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view]
PANTHERPTHR10484. PTHR10484. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00623. HISTONEH4.
SMARTSM00417. H4. 1 hit.
[Graphical view]
SUPFAMSSF47113. Histone-fold. 1 hit.
PROSITEPS00047. HISTONE_H4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio613578.

Entry information

Entry nameH4_RAT
AccessionPrimary (citable) accession number: P62804
Secondary accession number(s): P02304 expand/collapse secondary AC list , P02305, Q5BM23, Q7M0E8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 89 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