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P15515

- HIS1_HUMAN

UniProt

P15515 - HIS1_HUMAN

Protein

Histatin-1

Gene

HTN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. biomineral tissue development Source: UniProtKB-KW
    2. defense response to bacterium Source: UniProtKB
    3. defense response to fungus Source: UniProtKB-KW
    4. killing of cells of other organism Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Fungicide

    Keywords - Biological processi

    Biomineralization

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histatin-1
    Alternative name(s):
    Histidine-rich protein 1
    Post-PB protein
    Short name:
    PPB
    Cleaved into the following chain:
    His1-(31-57)-peptide
    Short name:
    His1 31/57
    Alternative name(s):
    His1-(12-38)-peptide
    Short name:
    His1 12/38
    Histatin-2
    Gene namesi
    Name:HTN1
    Synonyms:HIS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:5283. HTN1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29546.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19193 PublicationsAdd
    BLAST
    Peptidei20 – 5738Histatin-1PRO_0000021416Add
    BLAST
    Peptidei31 – 5727His1-(31-57)-peptidePRO_0000021417Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Phosphoserine3 Publications
    Modified residuei46 – 461Sulfotyrosine; in submandibular gland form1 Publication
    Modified residuei49 – 491Sulfotyrosine; in submandibular gland form1 Publication
    Modified residuei53 – 531Sulfotyrosine; in submandibular gland form1 Publication
    Modified residuei55 – 551Sulfotyrosine; in submandibular gland form1 Publication

    Post-translational modificationi

    Depending on the authors, the form called histatin-2 is alternatively a proteolytic product, or the non-phosphorylated form of histatin-1.2 Publications

    Keywords - PTMi

    Phosphoprotein, Sulfation

    Proteomic databases

    PaxDbiP15515.
    PeptideAtlasiP15515.
    PRIDEiP15515.

    PTM databases

    PhosphoSiteiP15515.

    Expressioni

    Tissue specificityi

    Submandibular and parotid glands.1 Publication

    Gene expression databases

    BgeeiP15515.
    CleanExiHS_HTN1.
    GenevestigatoriP15515.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MUC7Q8TAX72EBI-738638,EBI-738582

    Protein-protein interaction databases

    BioGridi109578. 1 interaction.
    IntActiP15515. 1 interaction.
    STRINGi9606.ENSP00000246896.

    Structurei

    3D structure databases

    ProteinModelPortaliP15515.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histatin/statherin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG249966.
    HOGENOMiHOG000112905.
    HOVERGENiHBG005970.
    InParanoidiP15515.
    KOiK13913.
    OMAiDYGSNYL.
    OrthoDBiEOG7TTQBV.
    PhylomeDBiP15515.
    TreeFamiTF341637.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15515-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFFVFALVL ALMISMISAD SHEKRHHGYR RKFHEKHHSH REFPFYGDYG   50
    SNYLYDN 57
    Length:57
    Mass (Da):6,963
    Last modified:February 1, 1991 - v2
    Checksum:iF3532BD1DCE23D83
    GO

    Mass spectrometryi

    Molecular mass is 4848.2±0.5 Da from positions 20 - 50. Determined by ESI. Not post-translationally modified.1 Publication
    Molecular mass is 4928.2±0.5 Da from positions 20 - 50. Determined by ESI. with 1 phosphate group.1 Publication
    Molecular mass is 5008.6±0.5 Da from positions 20 - 50. Determined by ESI. with 1 phosphate group and 1 sulfate group.1 Publication
    Molecular mass is 5088.4±0.5 Da from positions 20 - 50. Determined by ESI. with 1 phosphate group and 2 sulfate groups.1 Publication
    Molecular mass is 5168.2±0.5 Da from positions 20 - 50. Determined by ESI. with 1 phosphate group and 3 sulfate groups.1 Publication
    Molecular mass is 5247.7±0.5 Da from positions 20 - 50. Determined by ESI. with 1 phosphate group and 4 sulfate groups.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26664 mRNA. Translation: AAA58645.1.
    L04132 Genomic DNA. Translation: AAA02745.1.
    BC017835 mRNA. Translation: AAH17835.1.
    CCDSiCCDS3534.1.
    PIRiI57425. A32541.
    RefSeqiNP_002150.1. NM_002159.2.
    UniGeneiHs.250959.

    Genome annotation databases

    EnsembliENST00000246896; ENSP00000246896; ENSG00000126550.
    ENST00000511674; ENSP00000424501; ENSG00000126550.
    GeneIDi3346.
    KEGGihsa:3346.
    UCSCiuc003hex.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26664 mRNA. Translation: AAA58645.1 .
    L04132 Genomic DNA. Translation: AAA02745.1 .
    BC017835 mRNA. Translation: AAH17835.1 .
    CCDSi CCDS3534.1.
    PIRi I57425. A32541.
    RefSeqi NP_002150.1. NM_002159.2.
    UniGenei Hs.250959.

    3D structure databases

    ProteinModelPortali P15515.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109578. 1 interaction.
    IntActi P15515. 1 interaction.
    STRINGi 9606.ENSP00000246896.

    PTM databases

    PhosphoSitei P15515.

    Proteomic databases

    PaxDbi P15515.
    PeptideAtlasi P15515.
    PRIDEi P15515.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000246896 ; ENSP00000246896 ; ENSG00000126550 .
    ENST00000511674 ; ENSP00000424501 ; ENSG00000126550 .
    GeneIDi 3346.
    KEGGi hsa:3346.
    UCSCi uc003hex.3. human.

    Organism-specific databases

    CTDi 3346.
    GeneCardsi GC04P070916.
    HGNCi HGNC:5283. HTN1.
    MIMi 142701. gene.
    neXtProti NX_P15515.
    PharmGKBi PA29546.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249966.
    HOGENOMi HOG000112905.
    HOVERGENi HBG005970.
    InParanoidi P15515.
    KOi K13913.
    OMAi DYGSNYL.
    OrthoDBi EOG7TTQBV.
    PhylomeDBi P15515.
    TreeFami TF341637.

    Miscellaneous databases

    ChiTaRSi HTN1. human.
    GeneWikii HTN1.
    GenomeRNAii 3346.
    NextBioi 13236.
    PROi P15515.
    SOURCEi Search...

    Gene expression databases

    Bgeei P15515.
    CleanExi HS_HTN1.
    Genevestigatori P15515.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (HIS1 and HIS2)."
      Sabatini L.M., Azen E.A.
      Biochem. Biophys. Res. Commun. 160:495-502(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family."
      Chen Z.W.
      Mol. Biol. Evol. 10:497-511(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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: Skeletal muscle.
    4. "Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans."
      Oppenheim F.G., Xu T., McMillian F.M., Levitz S.M., Diamond R.D., Offner G.D., Troxler R.F.
      J. Biol. Chem. 263:7472-7477(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-57, PHOSPHORYLATION AT SER-21.
      Tissue: Parotid gland.
    5. "The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion."
      Oppenheim F.G., Yang Y.C., Diamond R.D., Hyslop D., Offner G.D., Troxler R.F.
      J. Biol. Chem. 261:1177-1182(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-57.
      Tissue: Parotid gland.
    6. "Rapid purification and characterization of histatins (histidine-rich polypeptides) from human whole saliva."
      Sugiyama K., Ogino T., Ogata K.
      Arch. Oral Biol. 35:415-419(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-57.
      Tissue: Saliva.
    7. "Localization of the genes for histatins to human chromosome 4q13 and tissue distribution of the mRNAs."
      Vanderspek J.C., Wyandt H.E., Skare J.C., Milunsky A., Oppenheim F.G., Troxler R.F.
      Am. J. Hum. Genet. 45:381-387(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-57.
    8. "Tyrosine polysulfation of human salivary histatin 1. A post-translational modification specific of the submandibular gland."
      Cabras T., Fanali C., Monteiro J.A., Amado F., Inzitari R., Desiderio C., Scarano E., Giardina B., Castagnola M., Messana I.
      J. Proteome Res. 6:2472-2480(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, SULFATION AT TYR-46; TYR-49; TYR-53 AND TYR-55, TISSUE SPECIFICITY, MASS SPECTROMETRY.
    9. Cited for: PEPTIDE NOMENCLATURE.

    Entry informationi

    Entry nameiHIS1_HUMAN
    AccessioniPrimary (citable) accession number: P15515
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

    The recommended nomenclature of salivary peptides follows published guidelines (PubMed:20973643). In agreement with the authors, it has been decided to indicate the boundaries of the peptides according to the positions within the precursor, and not in the mature protein, as has formerly been proposed.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3