dbPTM

IF5A1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF5A1_HUMAN
UniProt AC	P63241
Protein Name	Eukaryotic translation initiation factor 5A-1
Gene Name	EIF5A
Organism	Homo sapiens (Human).
Sequence Length	154
Subcellular Localization	Cytoplasm. Nucleus. Endoplasmic reticulum membrane Peripheral membrane protein Cytoplasmic side. Nucleus, nuclear pore complex. Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the loca
Protein Description	mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF-alpha-mediated apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation. Also described as a cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts..
Protein Sequence	MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVREDLRLPEGDLGKEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADDLDFET ------CCCCCCCCC	21.01	-
9	Phosphorylation	ADDLDFETGDAGASA CCCCCCCCCCCCCCC	40.11	28355574
15	Phosphorylation	ETGDAGASATFPMQC CCCCCCCCCCCCCCC	27.24	25159151
17	Phosphorylation	GDAGASATFPMQCSA CCCCCCCCCCCCCHH	26.27	24275569
22	S-palmitoylation	SATFPMQCSALRKNG CCCCCCCCHHHHHCC	1.77	26865113
23	Phosphorylation	ATFPMQCSALRKNGF CCCCCCCHHHHHCCE	17.28	29507054
27	Acetylation	MQCSALRKNGFVVLK CCCHHHHHCCEEEEC	63.37	19608861
27	Sumoylation	MQCSALRKNGFVVLK CCCHHHHHCCEEEEC	63.37	-
27	Ubiquitination	MQCSALRKNGFVVLK CCCHHHHHCCEEEEC	63.37	22817900
27	Sumoylation	MQCSALRKNGFVVLK CCCHHHHHCCEEEEC	63.37	-
27 (in isoform 1)	Ubiquitination	-	63.37	21890473
34	Acetylation	KNGFVVLKGRPCKIV HCCEEEECCCEEEEE	41.06	25953088
34	Sumoylation	KNGFVVLKGRPCKIV HCCEEEECCCEEEEE	41.06	-
34	Ubiquitination	KNGFVVLKGRPCKIV HCCEEEECCCEEEEE	41.06	27667366
34	Sumoylation	KNGFVVLKGRPCKIV HCCEEEECCCEEEEE	41.06	-
34	Neddylation	KNGFVVLKGRPCKIV HCCEEEECCCEEEEE	41.06	32015554
34	Succinylation	KNGFVVLKGRPCKIV HCCEEEECCCEEEEE	41.06	23954790
34 (in isoform 1)	Ubiquitination	-	41.06	21890473
38	S-palmitoylation	VVLKGRPCKIVEMST EEECCCEEEEEEEEC	4.53	21044946
39	Acetylation	VLKGRPCKIVEMSTS EECCCEEEEEEEECC	53.09	23954790
39	Sumoylation	VLKGRPCKIVEMSTS EECCCEEEEEEEECC	53.09	-
39	Ubiquitination	VLKGRPCKIVEMSTS EECCCEEEEEEEECC	53.09	21906983
39	Sumoylation	VLKGRPCKIVEMSTS EECCCEEEEEEEECC	53.09	-
39	2-Hydroxyisobutyrylation	VLKGRPCKIVEMSTS EECCCEEEEEEEECC	53.09	-
39 (in isoform 1)	Ubiquitination	-	53.09	21890473
43	Sulfoxidation	RPCKIVEMSTSKTGK CEEEEEEEECCCCCC	3.52	30846556
44	Phosphorylation	PCKIVEMSTSKTGKH EEEEEEEECCCCCCC	18.94	29255136
45	Phosphorylation	CKIVEMSTSKTGKHG EEEEEEECCCCCCCC	32.69	29255136
46	Phosphorylation	KIVEMSTSKTGKHGH EEEEEECCCCCCCCC	22.40	29255136
47	Acetylation	IVEMSTSKTGKHGHA EEEEECCCCCCCCCE	62.48	19379712
47	Ubiquitination	IVEMSTSKTGKHGHA EEEEECCCCCCCCCE	62.48	19379712
50	Hypusine	MSTSKTGKHGHAKVH EECCCCCCCCCEEEE	52.20	-
50	Ubiquitination	MSTSKTGKHGHAKVH EECCCCCCCCCEEEE	52.20	22817900
50	Other	MSTSKTGKHGHAKVH EECCCCCCCCCEEEE	52.20	3095320
50	Acetylation	MSTSKTGKHGHAKVH EECCCCCCCCCEEEE	52.20	25953088
55	Acetylation	TGKHGHAKVHLVGID CCCCCCEEEEEEEEE	25.23	30582461
55	Ubiquitination	TGKHGHAKVHLVGID CCCCCCEEEEEEEEE	25.23	22817900
57 (in isoform 2)	Ubiquitination	-	17.68	21890473
57	Ubiquitination	KHGHAKVHLVGIDIF CCCCEEEEEEEEECC	17.68	22817900
57	Acetylation	KHGHAKVHLVGIDIF CCCCEEEEEEEEECC	17.68	19608861
64	Ubiquitination	HLVGIDIFTGKKYED EEEEEECCCCCCHHH	6.99	27667366
64	Neddylation	HLVGIDIFTGKKYED EEEEEECCCCCCHHH	6.99	32015554
64 (in isoform 2)	Ubiquitination	-	6.99	21890473
65	Phosphorylation	LVGIDIFTGKKYEDI EEEEECCCCCCHHHC	48.72	21712546
67	Acetylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	23749302
67	Sumoylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	-
67	Ubiquitination	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	23000965
67	Sumoylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	-
67	Neddylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	32015554
67	2-Hydroxyisobutyrylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	-
67	Succinylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	23954790
67 (in isoform 1)	Ubiquitination	-	49.47	21890473
68	Methylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
68	Acetylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	16916647
68	Sumoylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
68	Ubiquitination	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	23000965
68	Sumoylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
68	2-Hydroxyisobutyrylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
68	Malonylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	26320211
68 (in isoform 1)	Ubiquitination	-	56.04	21890473
68	Ubiquitination	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	22053931
69	Phosphorylation	DIFTGKKYEDICPST ECCCCCCHHHCCCCC	23.48	28796482
69	Ubiquitination	DIFTGKKYEDICPST ECCCCCCHHHCCCCC	23.48	21963094
69 (in isoform 2)	Ubiquitination	-	23.48	21890473
73	Glutathionylation	GKKYEDICPSTHNMD CCCHHHCCCCCCCCC	3.17	22555962
74 (in isoform 2)	Phosphorylation	-	42.47	27251275
75	Phosphorylation	KYEDICPSTHNMDVP CHHHCCCCCCCCCCC	37.58	25849741
76	Phosphorylation	YEDICPSTHNMDVPN HHHCCCCCCCCCCCC	11.47	25849741
77	Ubiquitination	EDICPSTHNMDVPNI HHCCCCCCCCCCCCC	31.77	29967540
77	Acetylation	EDICPSTHNMDVPNI HHCCCCCCCCCCCCC	31.77	19608861
79	Sulfoxidation	ICPSTHNMDVPNIKR CCCCCCCCCCCCCCC	4.22	21406390
80	Ubiquitination	CPSTHNMDVPNIKRN CCCCCCCCCCCCCCC	59.02	22817900
85	Sumoylation	NMDVPNIKRNDFQLI CCCCCCCCCCCEEEE	52.36	-
85	Ubiquitination	NMDVPNIKRNDFQLI CCCCCCCCCCCEEEE	52.36	23000965
85	Sumoylation	NMDVPNIKRNDFQLI CCCCCCCCCCCEEEE	52.36	-
85	2-Hydroxyisobutyrylation	NMDVPNIKRNDFQLI CCCCCCCCCCCEEEE	52.36	-
85	Acetylation	NMDVPNIKRNDFQLI CCCCCCCCCCCEEEE	52.36	25953088
85	Malonylation	NMDVPNIKRNDFQLI CCCCCCCCCCCEEEE	52.36	26320211
85 (in isoform 1)	Ubiquitination	-	52.36	21890473
97 (in isoform 2)	Ubiquitination	-	14.65	21890473
97	Ubiquitination	QLIGIQDGYLSLLQD EEEEEECCCCHHHCC	14.65	23000965
97	Neddylation	QLIGIQDGYLSLLQD EEEEEECCCCHHHCC	14.65	32015554
98	Phosphorylation	LIGIQDGYLSLLQDS EEEEECCCCHHHCCC	11.04	28796482
98 (in isoform 2)	Ubiquitination	-	11.04	21890473
98	Ubiquitination	LIGIQDGYLSLLQDS EEEEECCCCHHHCCC	11.04	23000965
100	Phosphorylation	GIQDGYLSLLQDSGE EEECCCCHHHCCCCC	20.67	28796482
105	O-linked_Glycosylation	YLSLLQDSGEVREDL CCHHHCCCCCCHHHH	24.72	23301498
106 (in isoform 2)	Phosphorylation	-	45.79	27251275
113	Methylation	GEVREDLRLPEGDLG CCCHHHHCCCCCCHH	61.59	-
115 (in isoform 2)	Ubiquitination	-	36.77	21890473
115	Ubiquitination	VREDLRLPEGDLGKE CHHHHCCCCCCHHHH	36.77	23000965
121	Acetylation	LPEGDLGKEIEQKYD CCCCCHHHHHHHHHC	63.92	23954790
121	Ubiquitination	LPEGDLGKEIEQKYD CCCCCHHHHHHHHHC	63.92	27667366
121	Neddylation	LPEGDLGKEIEQKYD CCCCCHHHHHHHHHC	63.92	32015554
121	2-Hydroxyisobutyrylation	LPEGDLGKEIEQKYD CCCCCHHHHHHHHHC	63.92	-
121	Succinylation	LPEGDLGKEIEQKYD CCCCCHHHHHHHHHC	63.92	23954790
121 (in isoform 1)	Ubiquitination	-	63.92	21890473
121	Ubiquitination	LPEGDLGKEIEQKYD CCCCCHHHHHHHHHC	63.92	22053931
126	Sumoylation	LGKEIEQKYDCGEEI HHHHHHHHHCCCCHH	30.21	-
126	Ubiquitination	LGKEIEQKYDCGEEI HHHHHHHHHCCCCHH	30.21	22817900
126	Sumoylation	LGKEIEQKYDCGEEI HHHHHHHHHCCCCHH	30.21	-
127	Phosphorylation	GKEIEQKYDCGEEIL HHHHHHHHCCCCHHH	19.03	-
129	Glutathionylation	EIEQKYDCGEEILIT HHHHHHCCCCHHHHH	7.20	22555962
130 (in isoform 2)	Phosphorylation	-	32.45	27251275
141	Sulfoxidation	LITVLSAMTEEAAVA HHHHHHHCCHHHHHH	4.32	30846556
150	Ubiquitination	EEAAVAIKAMAK--- HHHHHHHHHHHC---	23.52	33845483
151 (in isoform 2)	Ubiquitination	-	9.32	21890473
151	Ubiquitination	EAAVAIKAMAK---- HHHHHHHHHHC----	9.32	27667366
151	Neddylation	EAAVAIKAMAK---- HHHHHHHHHHC----	9.32	32015554
156	Ubiquitination	IKAMAK--------- HHHHHC---------		33845483
180	Ubiquitination	--------------------------------- ---------------------------------		33845483

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
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:24509416

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF5A1_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 IF5A1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL5_HUMAN	RPL5	physical	9465063
XPO1_HUMAN	XPO1	physical	10381392
XPO1_HUMAN	XPO1	physical	22939629
MACF1_HUMAN	MACF1	physical	22939629
VAPA_HUMAN	VAPA	physical	22939629
GLSK_HUMAN	GLS	physical	22863883
CH60_HUMAN	HSPD1	physical	22863883
MEOX2_HUMAN	MEOX2	physical	25416956
REL_HUMAN	REL	physical	25416956

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 IF5A1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-46, AND MASS SPECTROMETRY.	19413330 [Abstract]
"The effect of hypusine modification on the intracellular localizationof eIF5A."; Lee S.B., Park J.-H., Kaevel J., Sramkova M., Weigert R., Park M.H.; Biochem. Biophys. Res. Commun. 383:497-502(2009). Cited for: ACETYLATION AT LYS-47, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-47AND LYS-50.	19379712 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-46, AND MASS SPECTROMETRY.	19413330 [Abstract]