HINT1_HUMAN - dbPTM
HINT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HINT1_HUMAN
UniProt AC P49773
Protein Name Histidine triad nucleotide-binding protein 1
Gene Name HINT1
Organism Homo sapiens (Human).
Sequence Length 126
Subcellular Localization Cytoplasm. Nucleus. Interaction with CDK7 leads to a more nuclear localization.
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..
Protein Sequence MADEIAKAQVARPGGDTIFGKIIRKEIPAKIIFEDDRCLAFHDISPQAPTHFLVIPKKHISQISVAEDDDESLLGHLMIVGKKCAADLGLNKGYRMVVNEGSDGGQSVYHVHLHVLGGRQMHWPPG
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 Orthologous
Protein Cluster
2Acetylation------MADEIAKAQ
------CHHHHHHHH		24.1222814378
7Acetylation-MADEIAKAQVARPG
-CHHHHHHHHCCCCC		45.0423954790
7Ubiquitination-MADEIAKAQVARPG
-CHHHHHHHHCCCCC		45.0421906983
21MethylationGGDTIFGKIIRKEIP
CCCCEEHHHHHCCCC		24.9868833
21AcetylationGGDTIFGKIIRKEIP
CCCCEEHHHHHCCCC		24.9819608861
21UbiquitinationGGDTIFGKIIRKEIP
CCCCEEHHHHHCCCC		24.9821890473
21MalonylationGGDTIFGKIIRKEIP
CCCCEEHHHHHCCCC		24.9826320211
30AcetylationIRKEIPAKIIFEDDR
HHCCCCCEEEECCCC		30.8619608861
30UbiquitinationIRKEIPAKIIFEDDR
HHCCCCCEEEECCCC		30.8621890473
30MalonylationIRKEIPAKIIFEDDR
HHCCCCCEEEECCCC		30.8626320211
37MethylationKIIFEDDRCLAFHDI
EEEECCCCEEEEEEC		29.66115478497
45PhosphorylationCLAFHDISPQAPTHF
EEEEEECCCCCCCEE		19.6025159151
50PhosphorylationDISPQAPTHFLVIPK
ECCCCCCCEEEEEEH		28.4225850435
64PhosphorylationKKHISQISVAEDDDE
HHHEEEEEEECCCCC		13.9827080861
72PhosphorylationVAEDDDESLLGHLMI
EECCCCCHHHHHHHE		35.5724247654
82AcetylationGHLMIVGKKCAADLG
HHHHEECCHHHHHCC		33.5125953088
82UbiquitinationGHLMIVGKKCAADLG
HHHHEECCHHHHHCC		33.51-
83UbiquitinationHLMIVGKKCAADLGL
HHHEECCHHHHHCCC		24.15-
84GlutathionylationLMIVGKKCAADLGLN
HHEECCHHHHHCCCC		4.2622555962
92AcetylationAADLGLNKGYRMVVN
HHHCCCCCCCEEEEE		63.4626051181
92UbiquitinationAADLGLNKGYRMVVN
HHHCCCCCCCEEEEE		63.46-
94PhosphorylationDLGLNKGYRMVVNEG
HCCCCCCCEEEEECC		9.35-
96SulfoxidationGLNKGYRMVVNEGSD
CCCCCCEEEEECCCC		2.7330846556
102PhosphorylationRMVVNEGSDGGQSVY
EEEEECCCCCCCEEE		27.2328464451
107PhosphorylationEGSDGGQSVYHVHLH
CCCCCCCEEEEEEEE		28.1126356563
109PhosphorylationSDGGQSVYHVHLHVL
CCCCCEEEEEEEEEE		11.9026356563
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 HINT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HINT1_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 HINT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAT5_HUMANKAT5physical
16835243
HINT1_HUMANHINT1physical
16835243
CTNB1_HUMANCTNNB1physical
22647378
MITF_HUMANMITFphysical
22647378
HDAC9_HUMANHDAC9physical
22647378
SIN3A_HUMANSIN3Aphysical
22647378
UB2R1_HUMANCDC34physical
19112177
RBX1_HUMANRBX1physical
19112177
SP1_HUMANSP1physical
19112177
RUVB1_HUMANRUVBL1physical
16014379
RUVB2_HUMANRUVBL2physical
16014379
ALDR_HUMANAKR1B1physical
26344197
AK1BA_HUMANAKR1B10physical
26344197
AK1BF_HUMANAKR1B15physical
26344197
DUT_HUMANDUTphysical
26344197
ENOA_HUMANENO1physical
26344197
ENOG_HUMANENO2physical
26344197
ENOB_HUMANENO3physical
26344197
FABPH_HUMANFABP3physical
26344197
FABP5_HUMANFABP5physical
26344197
FABP7_HUMANFABP7physical
26344197
FKB1A_HUMANFKBP1Aphysical
26344197
FKB1B_HUMANFKBP1Bphysical
26344197
FKBP2_HUMANFKBP2physical
26344197
GPX4_HUMANGPX4physical
26344197
GSTO2_HUMANGSTO2physical
26344197
GSTT1_HUMANGSTT1physical
26344197
CH10_HUMANHSPE1physical
26344197
MIF_HUMANMIFphysical
26344197
NDKB_HUMANNME2physical
26344197
PARK7_HUMANPARK7physical
26344197
MYP2_HUMANPMP2physical
26344197
PPIB_HUMANPPIBphysical
26344197
PRDX2_HUMANPRDX2physical
26344197
PRDX5_HUMANPRDX5physical
26344197
PRDX6_HUMANPRDX6physical
26344197
STIP1_HUMANSTIP1physical
26344197
TAGL_HUMANTAGLNphysical
26344197
TAGL2_HUMANTAGLN2physical
26344197
TAGL3_HUMANTAGLN3physical
26344197
UB2V1_HUMANUBE2V1physical
26344197
UFC1_HUMANUFC1physical
26344197
FBW1A_HUMANBTRCphysical
26520111
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
137200Neuromyotonia and axonal neuropathy, autosomal recessive (NMAN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00131Adenosine monophosphate
Regulatory Network of HINT1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-30, AND MASSSPECTROMETRY.

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