HINT1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HINT1_MOUSE
• UniProt AC: P70349
• Protein Name: Histidine triad nucleotide-binding protein 1
• Gene Name: Hint1
• Organism: Mus musculus (Mouse).
• Sequence Length: 126
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: Hydrolyzes purine nucleotide phosphoramidates with a single phosphate group, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. Can also convert adenosine 5'-O-phosphorothioate and guanosine 5'-O-phosphorothioate to the corresponding nucleoside 5'-O-phosphates with concomitant release of hydrogen sulfide. In addition, functions as scaffolding protein that modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex and by the complex formed with MITF and CTNNB1. Modulates p53/TP53 levels and p53/TP53-mediated apoptosis. Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (By similarity)..
• Protein Sequence: MADEIAKAQVAQPGGDTIFGKIIRKEIPAKIIFEDDRCLAFHDISPQAPTHFLVIPKKHISQISVADDDDESLLGHLMIVGKKCAADLGLKRGYRMVVNEGADGGQSVYHIHLHVLGGRQMNWPPG

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADEIAKAQ ------CHHHHHHHH	24.12	-
7	Succinylation	-MADEIAKAQVAQPG -CHHHHHHHHHCCCC	45.04	23806337
7	Acetylation	-MADEIAKAQVAQPG -CHHHHHHHHHCCCC	45.04	23806337
21	Succinylation	GGDTIFGKIIRKEIP CCCCEEHHHHHCCCC	24.98	23806337
21	Malonylation	GGDTIFGKIIRKEIP CCCCEEHHHHHCCCC	24.98	26320211
21	Acetylation	GGDTIFGKIIRKEIP CCCCEEHHHHHCCCC	24.98	23806337
21	Ubiquitination	GGDTIFGKIIRKEIP CCCCEEHHHHHCCCC	24.98	27667366
30	Ubiquitination	IRKEIPAKIIFEDDR HHCCCCCEEEECCCC	30.86	27667366
30	Acetylation	IRKEIPAKIIFEDDR HHCCCCCEEEECCCC	30.86	23864654
30	Malonylation	IRKEIPAKIIFEDDR HHCCCCCEEEECCCC	30.86	26320211
38	S-nitrosocysteine	IIFEDDRCLAFHDIS EEECCCCEEEEEECC	4.07	-
38	S-nitrosylation	IIFEDDRCLAFHDIS EEECCCCEEEEEECC	4.07	21278135
45	Phosphorylation	CLAFHDISPQAPTHF EEEEEECCCCCCCEE	19.60	24925903
50	Phosphorylation	DISPQAPTHFLVIPK ECCCCCCCEEEEEEH	28.42	26745281
61	Phosphorylation	VIPKKHISQISVADD EEEHHHEEEEEECCC	22.60	21082442
64	Phosphorylation	KKHISQISVADDDDE HHHEEEEEECCCCCC	12.01	23649490
72	Phosphorylation	VADDDDESLLGHLMI ECCCCCCHHHHHHHE	35.57	26643407
83	Ubiquitination	HLMIVGKKCAADLGL HHHEECCHHHHHHCC	24.15	-
84	S-palmitoylation	LMIVGKKCAADLGLK HHEECCHHHHHHCCC	4.26	26165157
84	S-nitrosylation	LMIVGKKCAADLGLK HHEECCHHHHHHCCC	4.26	21278135
84	S-nitrosocysteine	LMIVGKKCAADLGLK HHEECCHHHHHHCCC	4.26	-
91	Malonylation	CAADLGLKRGYRMVV HHHHHCCCCCCEEEE	41.81	26320211
91	Acetylation	CAADLGLKRGYRMVV HHHHHCCCCCCEEEE	41.81	15614229
109	Phosphorylation	ADGGQSVYHIHLHVL CCCCCEEEEEEEEEE	10.58	25195567

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

Oops, there are no upstream regulatory protein records of HINT1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HINT1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of HINT1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of HINT1_MOUSE !!

Drug and Disease Associations

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