dbPTM

HIS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HIS1_HUMAN
UniProt AC	P15515
Protein Name	Histatin-1
Gene Name	HTN1
Organism	Homo sapiens (Human).
Sequence Length	57
Subcellular Localization	Secreted.
Protein Description	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..
Protein Sequence	MKFFVFALVLALMISMISADSHEKRHHGYRRKFHEKHHSHREFPFYGDYGSNYLYDN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Phosphorylation	ISMISADSHEKRHHG HHHHCCCCHHHHHHC	33.01	22817900
39	Phosphorylation	KFHEKHHSHREFPFY HHHHHCCCCCCCCCC	24.78	21299198
46	Sulfation	SHREFPFYGDYGSNY CCCCCCCCCCCCCCC	14.88	-
46	Sulfation	SHREFPFYGDYGSNY CCCCCCCCCCCCCCC	14.88	17503797
49	Phosphorylation	EFPFYGDYGSNYLYD CCCCCCCCCCCCCCC	20.35	24850871
49	Sulfation	EFPFYGDYGSNYLYD CCCCCCCCCCCCCCC	20.35	-
49	Sulfation	EFPFYGDYGSNYLYD CCCCCCCCCCCCCCC	20.35	17503797
51	Phosphorylation	PFYGDYGSNYLYDN- CCCCCCCCCCCCCC-	18.97	21299198
53	Sulfation	YGDYGSNYLYDN--- CCCCCCCCCCCC---	14.34	-
53	Sulfation	YGDYGSNYLYDN--- CCCCCCCCCCCC---	14.34	17503797
55	Sulfation	DYGSNYLYDN----- CCCCCCCCCC-----	11.77	-
55	Sulfation	DYGSNYLYDN----- CCCCCCCCCC-----	11.77	17503797

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of HIS1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HIS1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of HIS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HIS1_HUMAN !!

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HIS1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The primary structure and functional characterization of the neutralhistidine-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). Cited for: PROTEIN SEQUENCE OF 20-57.	3944083 [Abstract]
"Histatins, a novel family of histidine-rich proteins in human parotidsecretion. Isolation, characterization, primary structure, andfungistatic 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). Cited for: PROTEIN SEQUENCE OF 20-57, AND PHOSPHORYLATION AT SER-21.	3286634 [Abstract]
Sulfation
Reference	PubMed
"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). Cited for: PHOSPHORYLATION, SULFATION AT TYR-46; TYR-49; TYR-53 AND TYR-55,TISSUE SPECIFICITY, AND MASS SPECTROMETRY.	17503797 [Abstract]