DHYS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DHYS_HUMAN
• UniProt AC: P49366
• Protein Name: Deoxyhypusine synthase
• Gene Name: DHPS
• Organism: Homo sapiens (Human).
• Sequence Length: 369
• Protein Description: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. This is the first step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function..
• Protein Sequence: MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFGRAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLVQHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFEDWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGSLGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGADYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMDAFMHEKNED

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
1	Acetylation	-------MEGSLERE -------CCCCCCCC	13.69	-
4	Phosphorylation	----MEGSLEREAPA ----CCCCCCCCCCH	17.47	28464451
19	Ubiquitination	GALAAVLKHSSTLPP HHHHHHHHCCCCCCC	34.54	21890473
19 (in isoform 1)	Ubiquitination	-	34.54	21890473
22 (in isoform 3)	Phosphorylation	-	33.41	-
22	Phosphorylation	AAVLKHSSTLPPEST HHHHHCCCCCCCCCC	33.41	-
36 (in isoform 3)	Phosphorylation	-	5.17	25849741
38	Methylation	VRGYDFNRGVNYRAL CCCEECCCCCCHHHH	50.89	-
48	Phosphorylation	NYRALLEAFGTTGFQ CHHHHHHHHCCCCCC	14.24	-
69	Sulfoxidation	AVQQVNAMIEKKLEP HHHHHHHHHHHHCCC	3.24	21406390
72 (in isoform 1)	Ubiquitination	-	52.30	21890473
72	Ubiquitination	QVNAMIEKKLEPLSQ HHHHHHHHHCCCCCC	52.30	21906983
72 (in isoform 2)	Ubiquitination	-	52.30	21890473
73 (in isoform 2)	Ubiquitination	-	45.34	21890473
73 (in isoform 1)	Ubiquitination	-	45.34	21890473
73	Ubiquitination	VNAMIEKKLEPLSQD HHHHHHHHCCCCCCC	45.34	73
78	Phosphorylation	EKKLEPLSQDEDQHA HHHCCCCCCCHHHCC	46.42	17525332
88	Phosphorylation	EDQHADLTQSRRPLT HHHCCCCHHCCCCCC	25.66	17525332
90	Phosphorylation	QHADLTQSRRPLTSC HCCCCHHCCCCCCCC	25.64	23312004
105	Phosphorylation	TIFLGYTSNLISSGI EEEEECHHHHHHHCH	22.58	-
156	Ubiquitination	GEFSLRGKELRENGI EECCCCCHHHHHCCC	47.33	-
196	Phosphorylation	QMVMEQNTEGVKWTP HHHHHCCCCCCCCCH	33.53	23532336
205 (in isoform 1)	Ubiquitination	-	35.21	21890473
205	Ubiquitination	GVKWTPSKMIARLGK CCCCCHHHHHHHHCH	35.21	21906983
205 (in isoform 2)	Ubiquitination	-	35.21	21890473
212 (in isoform 2)	Ubiquitination	-	61.07	21890473
212	Ubiquitination	KMIARLGKEINNPES HHHHHHCHHCCCHHH	61.07	2190698
212 (in isoform 1)	Ubiquitination	-	61.07	21890473
319 (in isoform 2)	Ubiquitination	-	24.63	21890473
329	Ubiquitination	DEAVSWGKIRVDAQP CCCCCCCCEEECCCC	22.53	-
338	Ubiquitination	RVDAQPVKVYADASL EECCCCEEEEECHHH	35.89	-
366	Ubiquitination	MDAFMHEKNED---- HHHHHHHHCCC----	51.46	-
366 (in isoform 1)	Ubiquitination	-	51.46	21890473

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NIF3L_HUMAN	NIF3L1	physical	16189514
NUD18_HUMAN	NUDT18	physical	16189514
IF5A2_HUMAN	EIF5A2	physical	16189514
RL9_HUMAN	RPL9	physical	16189514
ARP2_HUMAN	ACTR2	physical	22863883
ANKY2_HUMAN	ANKMY2	physical	22863883
AN32B_HUMAN	ANP32B	physical	22863883
ARI1_HUMAN	ARIH1	physical	22863883
ARC1B_HUMAN	ARPC1B	physical	22863883
PYRG2_HUMAN	CTPS2	physical	22863883
DPP8_HUMAN	DPP8	physical	22863883
HNRPF_HUMAN	HNRNPF	physical	22863883
HSF1_HUMAN	HSF1	physical	22863883
PLIN3_HUMAN	PLIN3	physical	22863883
2A5D_HUMAN	PPP2R5D	physical	22863883
SRP09_HUMAN	SRP9	physical	22863883
SURF2_HUMAN	SURF2	physical	22863883
DHYS_HUMAN	DHPS	physical	25416956
IF5A1_HUMAN	EIF5A	physical	25416956
RB27B_HUMAN	RAB27B	physical	25416956
REL_HUMAN	REL	physical	25416956
RL9_HUMAN	RPL9	physical	25416956
ZN138_HUMAN	ZNF138	physical	25416956
VASH1_HUMAN	VASH1	physical	25416956
NTAQ1_HUMAN	WDYHV1	physical	25416956
IF5A2_HUMAN	EIF5A2	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND THR-88, AND MASSSPECTROMETRY.
PubMed: 17525332