HTN1

Histatin 1

Identifiers

HTN1 ; HIS1

External IDs

OMIM: 142701 HomoloGene: 88658 GeneCards: HTN1 Gene

Gene ontology
Molecular function	• protein binding
Cellular component	• extracellular region
Biological process	• biomineral tissue development • killing of cells of other organism • defense response to bacterium • defense response to fungus
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

n/a

n/a

RefSeq (mRNA)

NM_002159

n/a

RefSeq (protein)

NP_002150

n/a

Location (UCSC)

Chr 4:
70.92 – 70.92 Mb

n/a

PubMed search

n/a

Histatin-1 is a protein that in humans is encoded by the HTN1 gene.^[1]

References

↑ "Entrez Gene: HTN1 histatin 1".

Sugiyama K, Ogino T, Ogata K (1990). "Rapid purification and characterization of histatins (histidine-rich polypeptides) from human whole saliva.". Arch. Oral Biol. 35 (6): 415–9. doi:10.1016/0003-9969(90)90202-L. PMID 2372245.
Sabatini LM, Azen EA (1989). "Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (HIS1 and HIS2).". Biochem. Biophys. Res. Commun. 160 (2): 495–502. doi:10.1016/0006-291X(89)92460-1. PMID 2719677.
vanderSpek JC, Wyandt HE, Skare JC et al. (1989). "Localization of the genes for histatins to human chromosome 4q13 and tissue distribution of the mRNAs.". Am. J. Hum. Genet. 45 (3): 381–7. PMC 1683406. PMID 2773933.
Oppenheim FG, Xu T, McMillian FM et al. (1988). "Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans.". J. Biol. Chem. 263 (16): 7472–7. PMID 3286634.
Oppenheim FG, Yang YC, Diamond RD et al. (1986). "The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion.". J. Biol. Chem. 261 (3): 1177–82. PMID 3944083.
Sabatini LM, Ota T, Azen EA (1993). "Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family.". Mol. Biol. Evol. 10 (3): 497–511. PMID 8336540.
Driscoll J, Zuo Y, Xu T et al. (1996). "Functional comparison of native and recombinant human salivary histatin 1.". J. Dent. Res. 74 (12): 1837–44. doi:10.1177/00220345950740120601. PMID 8600179.
Iontcheva I, Oppenheim FG, Offner GD, Troxler RF (2000). "Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system.". J. Dent. Res. 79 (2): 732–9. doi:10.1177/00220345000790020601. PMID 10728974.
Flora B, Gusman H, Helmerhorst EJ et al. (2002). "A new method for the isolation of histatins 1, 3, and 5 from parotid secretion using zinc precipitation.". Protein Expr. Purif. 23 (1): 198–206. doi:10.1006/prep.2001.1493. PMID 11570863.
Tamaki N, Tada T, Morita M, Watanabe T (2003). "Comparison of inhibitory activity on calcium phosphate precipitation by acidic proline-rich proteins, statherin, and histatin-1.". Calcif. Tissue Int. 71 (1): 59–62. doi:10.1007/s00223-001-1084-0. PMID 12060866.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Yin A, Margolis HC, Grogan J et al. (2003). "Physical parameters of hydroxyapatite adsorption and effect on candidacidal activity of histatins.". Arch. Oral Biol. 48 (5): 361–8. doi:10.1016/S0003-9969(03)00012-8. PMID 12711380.
Michels AA, Nguyen VT, Fraldi A et al. (2003). "MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner.". Mol. Cell. Biol. 23 (14): 4859–69. doi:10.1128/MCB.23.14.4859-4869.2003. PMC 162212. PMID 12832472.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Bruno LS, Li X, Wang L et al. (2005). "Two-hybrid analysis of human salivary mucin MUC7 interactions.". Biochim. Biophys. Acta 1746 (1): 65–72. doi:10.1016/j.bbamcr.2005.08.007. PMID 16203048.
Cabras T, Fanali C, Monteiro JA et al. (2007). "Tyrosine polysulfation of human salivary histatin 1. A post-translational modification specific of the submandibular gland.". J. Proteome Res. 6 (7): 2472–80. doi:10.1021/pr0700706. PMID 17503797.

Pore-forming toxins (TC 1C)

Antimicrobial cationic peptides

Other, human

Perforin

Other, nonhuman

Index of cells

Description	Structure nucleus chromosome genetics Organelles peroxisome cytoskeleton centrosome epithelia cilia mitochondria Membranes proteins cell adhesions Membrane transport ion channels vesicular transport solute carrier ABC transporters ATPase oxidoreduction-driven

Disease	Structural peroxisome cytoskeleton cilia mitochondria nucleus scleroprotein Membrane channelopathy solute carrier ATPase ABC transporters other extracellular ligands cell surface receptors intracellular signalling Vesicular transport Pore-forming toxins

HTN1

References

Further reading