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Q16695 (H31T_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 H3.1t

Short name=H3/t
Short name=H3t
Alternative name(s):
H3/g
Gene names
Name:HIST3H3
Synonyms:H3FT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

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.

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 By similarity.

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

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 By similarity.

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 By similarity. Ref.10

Ubiquitinated By similarity.

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.

Sequence similarities

Belongs to the histone H3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 136135Histone H3.1t
PRO_0000221248

Amino acid modifications

Modified residue31Asymmetric dimethylarginine; by PRMT6; alternate By similarity
Modified residue31Citrulline; alternate By similarity
Modified residue41Phosphothreonine; by GSG2 By similarity
Modified residue51Allysine; alternate By similarity
Modified residue51N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue51N6,N6-dimethyllysine; alternate By similarity
Modified residue51N6-acetyllysine; alternate By similarity
Modified residue51N6-methyllysine; alternate By similarity
Modified residue71Phosphothreonine; by PKC By similarity
Modified residue91Citrulline; alternate By similarity
Modified residue91Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residue101N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue101N6,N6-dimethyllysine; alternate By similarity
Modified residue101N6-acetyllysine; alternate By similarity
Modified residue101N6-methyllysine; alternate By similarity
Modified residue111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 By similarity
Modified residue121Phosphothreonine; by PKC By similarity
Modified residue151N6-acetyllysine By similarity
Modified residue181Asymmetric dimethylarginine; by CARM1; alternate By similarity
Modified residue181Citrulline; alternate By similarity
Modified residue191N6-acetyllysine; alternate Ref.9
Modified residue191N6-methyllysine; alternate By similarity
Modified residue241N6-acetyllysine; alternate Ref.9
Modified residue241N6-methyllysine; alternate By similarity
Modified residue271Citrulline By similarity
Modified residue281N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue281N6,N6-dimethyllysine; alternate By similarity
Modified residue281N6-acetyllysine; alternate By similarity
Modified residue281N6-methyllysine; alternate By similarity
Modified residue291Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.8
Modified residue371N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue371N6,N6-dimethyllysine; alternate By similarity
Modified residue371N6-acetyllysine; alternate By similarity
Modified residue371N6-methyllysine; alternate By similarity
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-methyllysine; by EHMT2; alternate By similarity
Modified residue581Phosphoserine Ref.10
Modified residue651N6-methyllysine By similarity
Modified residue801N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue801N6,N6-dimethyllysine; alternate By similarity
Modified residue801N6-acetyllysine; alternate By similarity
Modified residue801N6-methyllysine; alternate By similarity
Modified residue811Phosphothreonine Ref.10
Modified residue1081Phosphothreonine By similarity
Modified residue1161N6-acetyllysine By similarity
Modified residue1231N6-acetyllysine; alternate By similarity
Modified residue1231N6-methyllysine; alternate By similarity

Secondary structure

............... 136
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16695 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 37375A2C3A377B2B

FASTA13615,508
        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 

« Hide

References

« Hide 'large scale' references
[1]"A solitary human H3 histone gene on chromosome 1."
Albig W., Ebentheuer J., Klobeck H., Kunz J., Doenecke D.
Hum. Genet. 97:486-491(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Lung and Placenta.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-58 AND THR-81.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49861 Genomic DNA. Translation: CAA90020.1.
AF531308 Genomic DNA. Translation: AAN39284.1.
CR542013 mRNA. Translation: CAG46810.1.
AK312217 mRNA. Translation: BAG35150.1.
AL139288 Genomic DNA. Translation: CAI23333.1.
CH471098 Genomic DNA. Translation: EAW69877.1.
BC069079 mRNA. Translation: AAH69079.1.
BC101837 mRNA. Translation: AAI01838.1.
BC101839 mRNA. Translation: AAI01840.1.
PIRS57473.
RefSeqNP_003484.1. NM_003493.2.
UniGeneHs.248171.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V1DX-ray3.10C2-22[»]
2YBPX-ray2.02C/D31-42[»]
2YBSX-ray2.32C/D31-42[»]
3A6NX-ray2.70A/E1-136[»]
3T6RX-ray1.95D2-8[»]
ProteinModelPortalQ16695.
SMRQ16695. Positions 17-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113895. 140 interactions.
DIPDIP-922N.
IntActQ16695. 19 interactions.
MINTMINT-1155005.
STRING9606.ENSP00000355657.

PTM databases

PhosphoSiteQ16695.

Polymorphism databases

DMDM18202512.

Proteomic databases

PaxDbQ16695.
PRIDEQ16695.

Protocols and materials databases

DNASU8290.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366696; ENSP00000355657; ENSG00000168148.
GeneID8290.
KEGGhsa:8290.
UCSCuc001hsx.1. human.

Organism-specific databases

CTD8290.
GeneCardsGC01M228612.
HGNCHGNC:4778. HIST3H3.
HPACAB001386.
CAB003812.
MIM602820. gene.
neXtProtNX_Q16695.
PharmGKBPA29153.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2036.
HOGENOMHOG000155290.
HOVERGENHBG001172.
InParanoidQ16695.
KOK11253.
OMAREMARTK.
OrthoDBEOG7HB5C2.
PhylomeDBQ16695.
TreeFamTF314241.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

BgeeQ16695.
CleanExHS_HIST3H3.
GenevestigatorQ16695.

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.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16695.
GeneWikiHIST3H3.
GenomeRNAi8290.
NextBio31067.
PROQ16695.
SOURCESearch...

Entry information

Entry nameH31T_HUMAN
AccessionPrimary (citable) accession number: Q16695
Secondary accession number(s): B2R5K3, Q6FGU4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM