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UniProtKB/Swiss-Prot entry Q16695


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name H31T_HUMAN
Primary accession number Q16695
Secondary accession number Q6FGU4
Integrated into Swiss-Prot on September 26, 2001
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 89)
Name and origin of the protein
Protein name Histone H3.1t
Synonyms H3t
H3/t
H3/g
Gene name
Name: HIST3H3
Synonyms: H3FT
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/s004390050078; PubMed=8834248 [NCBI, ExPASy, EBI, Israel, Japan]
Albig W., Ebentheuer J., Klobeck H., Kunz J., Doenecke D.;
"A solitary human H3 histone gene on chromosome 1.";
Hum. Genet. 97:486-491(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0888-7543(02)96850-3; PubMed=12408966 [NCBI, ExPASy, EBI, Israel, Japan]
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
"The human and mouse replication-dependent histone genes.";
Genomics 80:487-498(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-28, AND MASS SPECTROMETRY.
DOI=10.1038/nmeth715; PubMed=15782174 [NCBI, ExPASy, EBI, Israel, Japan]
Ong S.E., Mittler G., Mann M.;
"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.";
Nat. Methods 1:119-126(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
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: 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.
  • INTERACTION:
    O60341:AOF2; NbExp=1; IntAct=EBI-358900, EBI-710124;
    O75164:JMJD2A; NbExp=3; IntAct=EBI-358900, EBI-936709;
  • SUBCELLULAR LOCATION: Nucleus.
  • TISSUE SPECIFICITY: Expressed in testicular cells.
  • DEVELOPMENTAL STAGE: Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.
  • PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8sme2). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me) (By similarity).
  • PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription (By similarity).
  • PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8sme2) 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).
  • PTM: 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 (By similarity).
  • PTM: Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase. Phosphorylated at Ser-11 during the whole mitosis. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation (By similarity).
  • PTM: Phosphorylation at Ser-11 (H3S10ph) is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) is important during interphase because it enables the transcription of genes following external stimulation, like stress or growth factors. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylation at Ser-11 (H3S10ph) by AURKB/Aurora-B mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin.
  • PTM: Ubiquitinated (By similarity).
  • SIMILARITY: Belongs to the histone H3 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z49861; CAA90020.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF531308; AAN39284.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR542013; CAG46810.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139288; CAI23333.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069079; AAH69079.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101837; AAI01838.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101839; AAI01840.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00216402; -.
PIR S57473; S57473.
RefSeq NP_003484.1; -.
UniGene Hs.248171
3D structure databases
PDB
2V1D; X-ray; 3.10 A; C=2-22.[ExPASy / RCSB / EBI]
PDBsum 2V1D; -.
SMR Q16695; 2-136.
ModBase Q16695.
Protein-protein interaction databases
DIP DIP:922N; -.
IntAct Q16695; 5.
PTM databases
PhosphoSite Q16695; -.
Enzyme and pathway databases
Reactome REACT_7970; Telomere Maintenance.
Organism-specific databases
GeneCards GC01M226679; -.
H-InvDB HIX0028778; -.
HGNC HGNC:4778; HIST3H3.
GenAtlas HIST3H3.
HPA CAB001386; -.
CAB003812; -.
MIM 602820; gene. [NCBI / EBI]
PharmGKB PA29153; -.
Gene expression databases
ArrayExpress Q16695; -.
Bgee Q16695; -.
CleanEx HS_HIST3H3; -.
GermOnline ENSG00000168148; Homo sapiens.
Ontologies
GO
GO:0000786; Cellular component: nucleosome (non-traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003677; Molecular function: DNA binding (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006334; Biological process: nucleosome assembly (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR009072; Histone-fold.
IPR007125; Histone_core_D.
IPR000164; Histone_H3.
Graphical view of domain structure.
Gene3D G3DSA:1.10.20.10; Histone-fold; 1.
PANTHER PTHR11426; Histone_H3; 1.
Pfam PF00125; Histone; 1.
Pfam graphical view of domain structure.
PRINTS PR00622; HISTONEH3.
SMART SM00428; H3; 1.
SMART graphical view of domain structure.
PROSITE PS00322; HISTONE_H3_1; 1.
PS00959; HISTONE_H3_2; FALSE_NEG.
Proteomic databases
PRIDE Q16695; -.
Genome annotation databases
Ensembl ENSG00000168148; Homo sapiens. [Contig view]
GeneID 8290; -.
KEGG hsa:8290; -.
Phylogenomic databases
HOVERGEN Q16695; -.
OMA Q16695; RRSSGMA.
Other
NextBio 31067; -.
SOURCE HIST3H3; Homo sapiens.
ProtoNet Q16695.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Chromosomal protein; Citrullination; DNA-binding; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   136  135     Histone H3.1t. PRO_0000221248
MOD_RES   3     3        Asymmetric dimethylarginine; by PRMT6 (By similarity). 
MOD_RES   4     4        Phosphothreonine (By similarity). 
MOD_RES   5     5        N6-methylated lysine (By similarity). 
MOD_RES   9     9        Citrulline; alternate (By similarity). 
MOD_RES   9     9        Symmetric dimethylarginine; by PRMT5; alternate (By similarity). 
MOD_RES   10    10        N6-acetyllysine; alternate (By similarity). 
MOD_RES   10    10        N6-methylated lysine; alternate (By similarity). 
MOD_RES   11    11        Phosphoserine (By similarity). 
MOD_RES   12    12        Phosphothreonine (By similarity). 
MOD_RES   15    15        N6-acetyllysine (By similarity). 
MOD_RES   18    18        Asymmetric dimethylarginine; by CARM1; alternate (By similarity). 
MOD_RES   18    18        Citrulline; alternate (By similarity). 
MOD_RES   19    19        N6-acetyllysine; alternate (By similarity). 
MOD_RES   19    19        N6-methylated lysine; alternate (By similarity). 
MOD_RES   24    24        N6-acetyllysine (By similarity). 
MOD_RES   28    28        N6-acetyllysine; alternate (By similarity). 
MOD_RES   28    28        N6-methylated lysine; alternate. 
MOD_RES   29    29        Phosphoserine. 
MOD_RES   37    37        N6-acetyllysine; alternate (By similarity). 
MOD_RES   37    37        N6-methylated lysine; alternate (By similarity). 
MOD_RES   65    65        N6-methylated lysine (By similarity). 
MOD_RES   80    80        N6-methylated lysine (By similarity). 
MOD_RES   123   123        N6-methylated lysine (By similarity). 
HELIX   3     5  3      
Sequence information
Length: 136 AA [This is the length of the unprocessed precursor] Molecular weight: 15508 Da [This is the MW of the unprocessed precursor] CRC64: 37375A2C3A377B2B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LATKVARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE 

        70         80         90        100        110        120 
LLIRKLPFQR LMREIAQDFK TDLRFQSSAV MALQEACESY LVGLFEDTNL CVIHAKRVTI 

       130 
MPKDIQLARR IRGERA 

Q16695 in FASTA format

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